CRISPRimmunity

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Overview of predicted results

Overview of the results

Contig_ID	Contig_def	CRISPR array number	Contig Signature genes	Self targeting spacer number	Target MGE spacer number	Prophage number	Anti-CRISPR protein number
NZ_CP053660	Nocardioides sp. zg-579 chromosome, complete genome	10 crisprs	cas3,DEDDh,csa3,cas4,WYL,RT	1	1	0	0

Cas Category Instructions

Results visualization

1. NZ_CP053660

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CRISPR-Cas detection and classification

Crispr_ID: NZ_CP053660_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP053660_1

54857-54941

Orphan

Consensus_repeat	Method
GGTTTTGTCGGCCGGCCGATGAA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP053660_1

>merge|NZ_CP053660|1|54857-54941|CRISPRCasFinder
GGTTTTGTCGGCCGGCCGATGAACCTGGCGGCTGGCCGACGGAACTTCAGCGTCCCACCGGGAGTTTTGTCGGCCGGCCGATGAA

>NZ_CP053660|1|1|54857-54941|CRISPRCasFinder
GGTTTTGTCGGCCGGCCGATGAA	CCTGGCGGCTGGCCGACGGAACTTCAGCGTCCCACCGGG
AGTTTTGTCGGCCGGCCGATGAA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP053660.1\|WP_154615999.1\|48195_48954_-\|ROK-family-protein	unknown	unknown	gnl\|CDD\|224851
NZ_CP053660.1\|WP_154615989.1\|56495_56711_+\|ferredoxin	unknown	unknown	gnl\|CDD\|224064
NZ_CP053660.1\|WP_154616001.1\|47540_48131_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP053660.1\|WP_171895921.1\|51851_52775_+\|glycosyltransferase-family-2-protein	unknown	unknown	gnl\|CDD\|366154
NZ_CP053660.1\|WP_154616003.1\|46007_47348_+\|NAD-dependent-malic-enzyme	unknown	unknown	gnl\|CDD\|223358
NZ_CP053660.1\|WP_171895920.1\|51048_51855_+\|CDP-alcohol-phosphatidyltransferase-family-protein	unknown	unknown	gnl\|CDD\|376450
NZ_CP053660.1\|WP_154615985.1\|60108_61440_+\|protein-kinase	unknown	unknown	gnl\|CDD\|270916
NZ_CP053660.1\|WP_154615983.1\|61445_63488_-\|VWA-domain-containing-protein	unknown	unknown	gnl\|CDD\|238733
NZ_CP053660.1\|WP_154615993.1\|54046_54802_+\|ABC-transporter-permease	unknown	unknown	gnl\|CDD\|130314
NZ_CP053660.1\|WP_154615995.1\|52982_54050_+\|ATP-binding-cassette-domain-containing-protein	unknown	unknown	gnl\|CDD\|130256
NZ_CP053660.1\|WP_154612315.1\|45262_45856_-\|TetR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|188483
NZ_CP053660.1\|WP_171895919.1\|49031_50855_-\|aminotransferase-class-I/II-fold-pyridoxal-phosphate-dependent-enzyme	unknown	unknown	gnl\|CDD\|133014
NZ_CP053660.1\|WP_154615979.1\|64239_65205_+\|zinc-binding-dehydrogenase	unknown	unknown	gnl\|CDD\|176203
NZ_CP053660.1\|WP_154612648.1\|58899_60087_+\|M15-family-metallopeptidase	unknown	unknown	gnl\|CDD\|379247
NZ_CP053660.1\|WP_154616007.1\|42854_45197_-\|MMPL-family-transporter	unknown	unknown	gnl\|CDD\|225272
NZ_CP053660.1\|WP_171895922.1\|57375_58767_+\|MFS-transporter	unknown	unknown	gnl\|CDD\|129794
NZ_CP053660.1\|WP_154615981.1\|63564_64230_+\|MOSC-N-terminal-beta-barrel-domain-containing-protein	unknown	unknown	gnl\|CDD\|225758
NZ_CP053660.1\|WP_154615991.1\|55047_56496_+\|fatty-acid-desaturase	unknown	unknown	gnl\|CDD\|239589
NZ_CP053660.1\|WP_154612306.1\|56794_57379_+\|TetR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|375982
NZ_CP053660.1\|WP_171897154.1\|65866_66364_+\|2-phosphosulfolactate-phosphatase	unknown	unknown	gnl\|CDD\|377205

Protein	Function_ID	Function_description	E-value
NZ_CP053660.1\|WP_154615999.1\|48195_48954_-\|ROK-family-protein	gnl\|CDD\|224851	COG1940, NagC, Transcriptional regulator/sugar kinase [Transcription / Carbohydrate transport and metabolism].	2.30553e-29
NZ_CP053660.1\|WP_154615989.1\|56495_56711_+\|ferredoxin	gnl\|CDD\|224064	COG1141, Fer, Ferredoxin [Energy production and conversion].	1.52388e-06
NZ_CP053660.1\|WP_171897154.1\|65866_66364_+\|2-phosphosulfolactate-phosphatase	gnl\|CDD\|377205	pfam04029, 2-ph_phosp, 2-phosphosulpholactate phosphatase. Thought to catalyze 2-phosphosulpholactate = sulpholactate + phosphate. Probable magnesium cofactor. Involved in the second step of coenzyme M biosynthesis. Inhibited by vanadate in Methanococcus jannaschii. Also known as the ComB family.	2.27968e-12
NZ_CP053660.1\|WP_171895921.1\|51851_52775_+\|glycosyltransferase-family-2-protein	gnl\|CDD\|366154	pfam00535, Glycos_transf_2, Glycosyl transferase family 2. Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.	2.04014e-23
NZ_CP053660.1\|WP_154616003.1\|46007_47348_+\|NAD-dependent-malic-enzyme	gnl\|CDD\|223358	COG0281, SfcA, Malic enzyme [Energy production and conversion].	6.66579e-171
NZ_CP053660.1\|WP_171895920.1\|51048_51855_+\|CDP-alcohol-phosphatidyltransferase-family-protein	gnl\|CDD\|376450	pfam01066, CDP-OH_P_transf, CDP-alcohol phosphatidyltransferase. All of these members have the ability to catalyze the displacement of CMP from a CDP-alcohol by a second alcohol with formation of a phosphodiester bond and concomitant breaking of a phosphoride anhydride bond.	1.61453e-08
NZ_CP053660.1\|WP_154615985.1\|60108_61440_+\|protein-kinase	gnl\|CDD\|270916	cd14014, STKc_PknB_like, Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.	2.22692e-65
NZ_CP053660.1\|WP_154615983.1\|61445_63488_-\|VWA-domain-containing-protein	gnl\|CDD\|238733	cd01456, vWA_ywmD_type, VWA ywmD type:Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Not much is known about the function of the members of this subgroup. All members of this subgroup however have a conserved MIDAS motif. .	9.26679e-28
NZ_CP053660.1\|WP_154615993.1\|54046_54802_+\|ABC-transporter-permease	gnl\|CDD\|130314	TIGR01247, drrB, daunorubicin resistance ABC transporter membrane protein. This model describes daunorubicin resistance ABC transporter, membrane associated protein in bacteria and archaea. The protein associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other].	7.56898e-18
NZ_CP053660.1\|WP_154615995.1\|52982_54050_+\|ATP-binding-cassette-domain-containing-protein	gnl\|CDD\|130256	TIGR01188, drrA, daunorubicin resistance ABC transporter ATP-binding subunit. This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other].	2.32464e-97
NZ_CP053660.1\|WP_154612315.1\|45262_45856_-\|TetR-family-transcriptional-regulator	gnl\|CDD\|188483	TIGR03968, transcriptional_regulator_TetR_family, mycofactocin system transcriptional regulator. Members of this family are TetR family putative transcriptional regulators that occur in genome contexts near proteins of the mycofactocin system. These include the precursor peptide (TIGR03969), a radical SAM peptide maturase (TIGR03962), and a putative carrier protein (TIGR03967). [Regulatory functions, DNA interactions].	8.0376e-16
NZ_CP053660.1\|WP_171895919.1\|49031_50855_-\|aminotransferase-class-I/II-fold-pyridoxal-phosphate-dependent-enzyme	gnl\|CDD\|133014	cd02523, PC_cytidylyltransferase, Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline. This family contains proteins similar to prokaryotic phosphocholine (P-cho) cytidylyltransferases. Phosphocholine (PC) cytidylyltransferases catalyze the transfer of a cytidine monophosphate from CTP to phosphocholine to form CDP-choline. PC is the most abundant phospholipid in eukaryotic membranes and it is also important in prokaryotic membranes. For pathogenic prokaryotes, the cell surface PC facilitates the interaction with host surface and induces attachment and invasion. In addition cell wall PC serves as scaffold for a group of choline-binding proteins that are secreted from the cells. Phosphocholine (PC) cytidylyltransferase is a key enzyme in the prokaryotic choline metabolism pathway. It has been hypothesized to consist of a choline transport system, a choline kinase, CTP:phosphocholine cytidylyltransferase, and a choline phosphotransferase that transfers P-Cho from CDP-Cho to either lipoteichoic acid or lipopolysaccharide.	6.35767e-66
NZ_CP053660.1\|WP_154615979.1\|64239_65205_+\|zinc-binding-dehydrogenase	gnl\|CDD\|176203	cd08241, QOR1, Quinone oxidoreductase (QOR). QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR acts in the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.	2.28471e-133
NZ_CP053660.1\|WP_154612648.1\|58899_60087_+\|M15-family-metallopeptidase	gnl\|CDD\|379247	pfam13539, Peptidase_M15_4, D-alanyl-D-alanine carboxypeptidase. This family resembles VanY, pfam02557, which is part of the peptidase M15 family.	1.58433e-17
NZ_CP053660.1\|WP_154616007.1\|42854_45197_-\|MMPL-family-transporter	gnl\|CDD\|225272	COG2409, COG2409, Predicted drug exporters of the RND superfamily [General function prediction only].	2.32645e-114
NZ_CP053660.1\|WP_171895922.1\|57375_58767_+\|MFS-transporter	gnl\|CDD\|129794	TIGR00711, Uncharacterized_MFS-type_transporter_YhcA, drug resistance transporter, EmrB/QacA subfamily. This subfamily of drug efflux proteins, a part of the major faciliator family, is predicted to have 14 potential membrane-spanning regions. Members with known activities include EmrB (multiple drug resistance efflux pump) in E. coli, FarB (antibacterial fatty acid resistance) in Neisseria gonorrhoeae, TcmA (tetracenomycin C resistance) in Streptomyces glaucescens, etc. In most cases, the efflux pump is described as having a second component encoded in the same operon, such as EmrA of E. coli. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Other].	2.38536e-69
NZ_CP053660.1\|WP_154615981.1\|63564_64230_+\|MOSC-N-terminal-beta-barrel-domain-containing-protein	gnl\|CDD\|225758	COG3217, COG3217, Uncharacterized Fe-S protein [General function prediction only].	8.56041e-19
NZ_CP053660.1\|WP_154615991.1\|55047_56496_+\|fatty-acid-desaturase	gnl\|CDD\|239589	cd03512, Alkane-hydroxylase, Alkane hydroxylase is a bacterial, integral-membrane di-iron enzyme that shares a requirement for iron and oxygen for activity similar to that of the non-heme integral-membrane acyl coenzyme A (CoA) desaturases and acyl lipid desaturases. The alk genes in Pseudomonas oleovorans encode conversion of alkanes to acyl CoA. The alkane omega-hydroxylase (AlkB) system is responsible for the initial oxidation of inactivated alkanes. It is a three-component system comprising a soluble NADH-rubredoxin reductase (AlkT), a soluble rubredoxin (AlkG), and the integral membrane oxygenase (AlkB). AlkB utilizes the oxygen rebound mechanism to hydroxylate alkanes. This mechanism involves homolytic cleavage of the C-H bond by an electrophilic metal-oxo intermediate to generate a substrate-based radical. As with other members of this superfamily, this domain family has extensive hydrophobic regions that would be capable of spanning the membrane bilayer at least twice. The active site structure of AlkB is not known, however, spectroscopic and genetic evidence points to a nitrogen-rich coordination environment located in the cytoplasm with as many as eight histidines coordinating the two iron ions and a carboxylate residue bridging the two metals. Like all other members of this superfamily, there are eight conserved histidines seen in the histidine cluster motifs: HXXXH, HXXXHH, and HXXHH. These histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within the homolog, stearoyl CoA desaturase. Also included in this CD are terminal alkane hydroxylases (AlkM), xylene monooxygenase hydroxylases (XylM), p-cymene monooxygenase hydroxylases (CymAa), and other related proteins.	9.67762e-154
NZ_CP053660.1\|WP_154612306.1\|56794_57379_+\|TetR-family-transcriptional-regulator	gnl\|CDD\|375982	pfam18556, TetR_C_35, Bacterial Tetracyclin repressor, C-terminal domain. This is the C-terminal tetracyclin repressor domain found in bacteria. Family members include TetR family transcriptional regulators Rv3249c and Rv1816 found in Mycobacterium tuberculosis. Palmitic acid (a fatty acid) and isopropyl laurate (a fatty acid ester), were identified as binding ligands to Rv3249c and Rv1816 respectively. Similar to other TetR family regulators, these proteins are alpha-helical dimeric proteins consisting of a smaller N-terminal DNA-binding domain and a larger C-terminal regulatory domain.	1.01045e-32

>NZ_CP053660.1|WP_154615993.1|54046_54802_+|ABC-transporter-permease
MRTFLRETSIVFSRQLRMNLRNPAWVIIGMLQPVLYLLLFAPLLKPVIGQLGVNQYTWFVPGMLVQLGIFGAFFAGFSLIGEWREGVIEAERVTPASRSALLLGRLGRDLLQLLVQALILVGLGLVMGMEWNPGGILLGIVLTILLGGACAAASDAFALTVKSEDVLAPVINLVMMPVLLLSGILLPMSFGAAWLDTLADLMPIRHVVDAVRGAFFGEFDASTMGWGVGWTVLLFGLAMWWGAAVFRRENA
>NZ_CP053660.1|WP_154615995.1|52982_54050_+|ATP-binding-cassette-domain-containing-protein
MIHARGLVQTFHTGRGKEKKAVQAVDGVDIDVAEGEVVGFLGPNGAGKTTTLRILTTLLRPTAGTATVAGYDVATQPVQVRRSIGYCSQVGSTFSGAYAGDEVVDHGMLYGMSRKDAVAKGQELFDRLQLDGLWRRMPKNMSGGQKRRLDIVMGLIHSPSLVFLDEPTTGLDPQARANLWEHIADLRTEQGATVFLTTHYLDEADALADRIVVIDRGRIVASDTSDNLKAQVAGDLVVLEVSADEHVAVARDRLGSLAPDVTVEGRHVRGRVARAGRVVPGLLRDLDAAGVALDSIEVARPTLDDVFLTLTGRSLRDAEAPAAGPDGDGPPADVPLPAEPSPTPGATSPTTGAAR
>NZ_CP053660.1|WP_171895921.1|51851_52775_+|glycosyltransferase-family-2-protein
MNPPVNPPDRPTVDVVIATRNRPELLRRAIAAVLAQTADCDLTCLVVFDQCEPDESLAEEGPDRRVRVLANTRRPGLAGGRNTGILAGTGDLVAFCDDDDAWLPEKLEVQLALLAESGADTSVTGITVEYDGRSVDRVPTADQLRLENLARRRVMAAHPSSVVVRREALLGRIGLVDEEIPGSYGEDFDWLLRAAVYPIAVVPRPLVRVRWGGSQFSQQWQTIVDAIDYSLGKHAVFHRDPRALGRLYGRRAFALAALGRPEARRAVLRTVRVAPLEPRAYLAAAVALHVVSAERLLHLAHQRGHGI
>NZ_CP053660.1|WP_171895920.1|51048_51855_+|CDP-alcohol-phosphatidyltransferase-family-protein
MPTVRPEPGRQLTELWTFFAVDPVGVPLSRRLARVRGVTPNRLTALALALGLAAAALMGTGRLRAAGALFVLRYFVDCLDGTVARMQDACSTRGAFADLGSDIVGVTAAYAALGWYLVGHGQLAGAWPVALLGALGLYNWLLGHRKRLAAEAGLGSGGSAHHWNRSRGPVGWWVGFCDRRGVSAVPWAVEVEIATLGLAPLLLPTSALPAAFLAALAFYLLADALNARRVWRVAGHLDAARRAEATTPAPGVAAERATDPLLPQGARP
>NZ_CP053660.1|WP_171895919.1|49031_50855_-|aminotransferase-class-I/II-fold-pyridoxal-phosphate-dependent-enzyme
MQALILAAGVGRRLGRLTRDRTKCMVEVHGRTLLERSLDALVDNGIERVVIVVGHRGQGVRDAIGSAYRGVPVTYVENADHATTNNIHSLYLAAGELAADDTLLLESDLIFEPRIIERLLAHPAPDVAAVAAYRSWMDGTMVTLGRDEVIEAFVPKHLVDGSAMGQYFKTVNIYKLSQEFIKNRYLPFLEAYVRSVGPNDYYEQVLRVIAGLDHHGLVGMPLEGEAWYEIDDVQDHQIAETLFAPAEERYDHYLRRHGGFWRFPGLLDFCYLVNPYFPTPALRQELARSFDTLLTEYPSCSAVQNHLAAKMFGGEPDCFLVGNGAAELIAALGEEVGARTVGVTVPTFEEYVKRFPHAEVVAVRGPGGGLETDLEHYLRLLERVDLLVLVNPDNPSGRCLRTEEVLTLLDRAERSGKRVLLDESFVDFADPAHATSLLRQDVLDAHPAAVVVKSISKSYGVPGARLGVLATRDADLLGRVARRLSVWNVNSVGEYFLQVIGHHQAAYVEACARLRAERDHLTAELAATDGLRVLPSQANYLLCEVTTGASGADIVSRLLGEHRVLVKDCAGKPGFEGLGPHLRIAVRDRADNEVLVHALRSVLAAAG
>NZ_CP053660.1|WP_154615999.1|48195_48954_-|ROK-family-protein
MAATPAPQTPIGIDFGGTGIKGAPVDLEVGDFAAERVRVRTPHPSTPAVVAEVFRELLSAFPDLTGPVGVTVPGIVRHGVVGSAANIDPAWVGTDADALFTEATGREVHVVNDADAAGLAEVRYGAARGRGGLVIVTTLGTGIGSALVHDGRLVPNSELGHLELDGHVAEKHAANSAREREDLSMKEWAGRLTAYYRHLERLFSPDLFVVGGGISKRADEFLPLLGLDTEIVPATLLNKAGVVGAALHAVGG
>NZ_CP053660.1|WP_154616001.1|47540_48131_-|hypothetical-protein
MSRTAVVVVPLLVLLVGTGGLGARMLLADPDEADASAGPARCWDGSTSDDGVEGCSHPRGLDGLAWVFPSVDLDDRACTGMEEGRAARWTCRARAGGEPVTLTYAAVPDARKAVRRLDRTYADGDRAPARAEDGSVNRWVWRLSEPDESGRWLLTSAYREHPYSVRVAAPSARARDLALRELVEHRDPAEVRGVPE
>NZ_CP053660.1|WP_154616003.1|46007_47348_+|NAD-dependent-malic-enzyme
MRLHTAPDHGVVGAVATTISQAGGIVTAMDVSESSHERLVVDVTCSASDADHAAVLEQEVDALEGVTVHKTSDRTFLLHLGGKIEVASKVPMRNRDDLSMAYTPGVGRVSSAIAEHPEDVWRLTTKGNTVAVVTDGSAVLGLGNIGPGAALPVMEGKAALFKRFAGIDAWPICLDTQDTDEIVRAVELIAPGFGGINLEDIAAPRCFEIERRLRASLDIPVFHDDQHGTAIVVLAALTNALRVVHKDLDSVRVVVSGGGAAGTAIVTLLLAAGVTDVVVVDRQGALSADDESLTGAHRQLAEVTNPRRATGDLHTVLTGADVFIGVSAPRILQPEWIKDMATDPVVFALANPDPEVDPVEADKYAAVVASGRSDYPNQINNVLAFPGVFRGLLDARASEITIEMLLRAAKAIAHVVQDDELNPSFIIPTVFHPDVPKAVAAAVRGA
>NZ_CP053660.1|WP_154612315.1|45262_45856_-|TetR-family-transcriptional-regulator
MSGSAIELSRRDAKRRETEDRISDCAQRLVAEHGLDGFTMEDLAAAADVSRRTLFNYFPSKVDAVLGNLPTIPADVRETFVRGGPHGALVEDLAVLARVVLADTDLQREQVDRLQHILTTTPRLAMSVHCRFEEVSADIAALVAQRDPGLTGMPARLLVRLLVTVFDSAMAAYVAGDDRPLADLFDEHLAAARRLLA
>NZ_CP053660.1|WP_154616007.1|42854_45197_-|MMPL-family-transporter
MATLLHRLGLTAYRRWPIVIATWVVLFVALGASVAAFAKPMSDSFSIPGIPSEKASDMQAELFPGAPDPSERATVNVVVAAPEGERLADPEWTKATQALIADLTELPQMPETPLADPVTAAEQQRQQLLDAAKKAGSDPKVAEANAAALSPLSEDGRVGTITWDFAVESVADVDPATIEALEDTMAEARDSGLTVEANGSGSQGMLHIGGTSELIGIAVALVVLVLTFGSLVAAGLPIVTAAVGVGFGVTGISLMTAFTDIGSTTPMLATMIGLAVGIDYCLFILARFRAEMEHTSDRQDATGLAVGTAGSAVVFAGLTVLIALAALALVRIPFLTSMGIAAAGTVLVAVLVALTLLPALLGMLGSKVFAGRVRRYRPARDHDGSILNNGVRWARLVGRAPVAVVVLVVVALGSLAIPMKGLHLAFPTDSTAAADSTQRKASDLVADAFGPGRDAPLLVVVDSRDVAADERPAAYGSVVEWAAGQDDVRNAQIIGQNEDGTGAQVLITPESGPEDTATEDLLSNLRDGQADLEESTGAELGVTGTTAIFTDVSERLSDALPIYLLVVIGLAFILLMIVFRSILVPLTATLGFLLSVLATLGITVAVFQEGVFGLVEGQPIVSFMPIFLIGLVFGLAMDYQVFLVTRMRESHVHGMSTRDAVVDGFRNSARVVAAAAVIMISVFAAFILIDEPIIKSMGFALAVAVFLDAFIVRMALVPALLYLMGEKAWWLPAWLDKLLPNVDVEGEQLERGRGGELVPGEAGAGTTGTTGADEGERQPV
>NZ_CP053660.1|WP_154615991.1|55047_56496_+|fatty-acid-desaturase
MNAIPNTTVPEGSTEQWTDKKRYLWLIGLVVPSLAFLAYAGWKLTGFGGFFWLGPIVILVIVPAIDLVAGLDRSNPPDDVIEALEQDRYYRWITYLFLPVQYAGFLGAMYLIAAGDPLSGIGRGSGDLAVWEAVGLAISIGCIGGIGINTAHELGHKKESHERWLSKIALAQSFYGHFYIEHNRGHHVRVATPEDPASSRVGESFYRFWPRTVLGSLRSAWSLEKRRYARKGQHPFRLGNDVLNAWLMSAVLFAAVVAWLGPGVLPYLALQAVIGFSLLEVVNYMEHYGMLRQKVGAGTRQRYERVDPSHSWNSNNIATNVLLYHLQRHSDHHANPTRRYQTLRDFEESPVLPTGYAGMIVLALVPPLWRRVMDPRVHGHFGGDMSRANIQPGKRDRILAAYPTPVVAPTAAERDDLTPGAVEEVLAARCPSCSYVYDVEVGDEHEGFAAGTAWADIPADWCCPDCGVREKVDFVPLARMDA
>NZ_CP053660.1|WP_154615989.1|56495_56711_+|ferredoxin
MGAPAGPVRIAVDRDLCEGLGMCEAMASDYFELDDDEVMHVLDETPAEADRGRVHAAVEACPVLALRLAPA
>NZ_CP053660.1|WP_154612306.1|56794_57379_+|TetR-family-transcriptional-regulator
MTPPGATPPTTRDRVVDAAVRMTVELGWSRVTMVRLADEVGVSRQTVYNEMGSKAGLAEAIIARELDRFLGVVTLAFDEHADDLVGAIRAATRAVLELAQDNPLLHAVVSATHGADTELLPLLTTQAESLLSAAQAVVTERVAPYDVGLEPEHLAAAIDMVVRVVLSHVMQPSDPPARTADRIAWLAGRVLRVG
>NZ_CP053660.1|WP_171895922.1|57375_58767_+|MFS-transporter
MTGPAAVRLGTPTGRAVIAAATLGSGLTLLDGTVVNVALVRIGEDLDASLAQLQWVTNGYLLSLASLILLGGSLGDRFGRRRVFVVGTVWFALASLACGLAPTAETLIAARVLQGVGGALLTPGSLAMIQGAFAAEDRPRAIGAWSGLGGVATAIGPFVGGALVDHASWRWIFGVNLPLAVLTVAVAVRAVPETRDPHAAGRVDLPGAALATLGLAGTTYALIEWGDALALPAGVLAVAALVAFVVVERRRPDPMLDPALFADRTFSAANAMTLLVYAALGAVMFFLVIELQTVGGYSALAAGTATLPITACMLLLAARGGALGARIGPRVPMTLGPLVMAVGVALLLGVGADVDYLTDVLPGVTVFGLGLALLVAPLTATVLAAAPQEQAGVASGVNNAVARAGSLLAVAALPVAVGLGGEQYADPVALGEAYRSAMLACAALLVLGGLVSWFAIRRDVLAE
>NZ_CP053660.1|WP_154612648.1|58899_60087_+|M15-family-metallopeptidase
MPLVAAAVLLLGACGGGSAPAPAPAPGTSSGTSSAAPQPGGGTASPAGDYAVEPPGPLRGSTLEGPDMLVYSQDPLSEEMVEQIAGLRGVDAVEPLAMAQVPVEDKVINLAAVDPATYRRFVPAPSARLLEAWRRVAGGEIAVLPEMKRKIPMDDQGFLSLGNVRDAPKAHVGAYVAQVPQVDAVVNEKWGAVLGMKPGNALLVSTDITAPQALRKPIQQIAGEDASVQILGPDLDTSVQQTAFLVGSVADAVGTFNYTVLGGGRIAPDPAWVTEHIRTEPVPILGAVTCNKAIFPQLRAALTEVVQRGLTAEIKPDEYAGCYYPRFIAGSTKLSNHSFGLALDFNVPGNLRGTVGEMDRTVVAIFKKWGFGWGGDWRYTDPMHFEMVAIVEPRT
>NZ_CP053660.1|WP_154615985.1|60108_61440_+|protein-kinase
MQPAPTTVFAGRYRLLDHLGEGGMGTVWRVLDEREQRVVAAKVLGRTDAVSLLRFLREQATRVVHPHVLTPIGWAGEDDLVLFTMPVVEGGSLEDLVRRRGGPPPVSAPVSAPALPPVLPPLLAAELLRQLLAGLAAIHAAGVVHRDVKPANLLLHPTGSGRPHLVVSDFGVAVDLAGPRLTETGAVVGTPGYLAPEVAGGAAAAPAADLYAAGQVALFLLLGAPASVPGALPARPDRVPDALWDLLADLVAADPAARPSAEEALDRLGHPSLAWHPDAVGHVRVDAVTAPLPGAAGVAGRRTLPEPTRVRAPREPRRPSALRAGLATVLLAGAAVALVLALWRPWAGPAAEPDPAPAPSPSAPVNPSPTPSSTSSSTGPSGGATPSGPAPSAPGSVEVGRVVTRVGQPCEAAELGLRETTLGGVDVVCRAAGAGGPAWRRAG
>NZ_CP053660.1|WP_154615983.1|61445_63488_-|VWA-domain-containing-protein
MGTTARSLPALLALVAVLLTPAPATTAAAAPATAPAAAPAPANALGAAEEDPGQLLLMLDASGSMKEPDPSGTTKMVAAKRALTSVVDTLPEDSTVGLRVYGDRSDSCRDSRLVAPLATLDRDALRAAINQTQPTGETPIAHSLREAVKDLGPEGRRTIVLVSDGEETCAPNPCQAVRALVGSGIDLRIDTVGFGVGAPARDQLQCIADAGGGTYYDAADAEALTASLAKLSQRATRPFTVTGEPVEATIRPEEGPLLEPGQYTDRFVVGSPLRYYRLARTPGSTVRFSVTARPLATAGTLDVEDLDVTVTTPAGETCESERESRFDPLGLGQVLVLHLRVDGATPEELAAASAAADPSPTESASESASGSASDPASTPTEEPVEPAEPCATSEELVVAVSRTQGEKRPAPVEVVYVEEPVVTDLADLPAQLDGAPGEPTPAPAQGDGTPVVGGGGFSDAPVLEDGTYRETLLPGEQVFYRVPVDWGQSATVTVDLPAPGEVVRLSSTSYINVQADLFTPDRLRFTNLKSIASLSDSTMSSQATRVIPEVRYRNREAVPTNDPGWSWADLQASTFAGDHYLALSREQAEPGTDEAQPVTVRFRVAVTGEPAGAPTYDGTDPTAEESADAEDAAGDGSADGAGDTEAAAATGGSALPWVLGAGVLVLVLGAVVTVVVRRRA
>NZ_CP053660.1|WP_154615981.1|63564_64230_+|MOSC-N-terminal-beta-barrel-domain-containing-protein
MRVVEVRRYPVKSLRGESLERADVEARGVVGDRWWALREPDGKLGSGKSTRRFRKMAGLLELAATYDGDVPVVTLPDGSTWRAPDPALDEALTAYVGRPVALRQESDVEHHDEGPLHLVTTATLDRLGADGALLRANLVVDVPGIQPFAEDLWAGRELRFEDGPVLVVREPMPRCVMVGSAVLHEATRLNDGSAGVVVDVVSGGPVAIGQHVVLGDRAPAR
>NZ_CP053660.1|WP_154615979.1|64239_65205_+|zinc-binding-dehydrogenase
MRAARVLDTTGPADVRVEEVAEPTPGAGDVLVEVHSVGVSFPDLLLSRGEYQMKPEVPFTLGVDFAGTVVSGPGFEPGQRVAGVGGWGGAAELVANPAGFVFALPDELSYDEGAALPMNYLTADFTLHDRAGLREGETVLVHGAAGGVGTATIQVAKGMGARTIAVVSTEEKAKVARDAGADEAVLIDGFKDAAKELTGGVGVDVVVDVVGGDLFTDSLRALAPQGRLMVVGFAAGQSIPQVKVNRLLLNNIDVRGVGWGAYAMLRDGFMAQQWERLVPMMTSGVVKPPIGTTYPLEDFAQALLDMEARRTLGKSVVRVRG
>NZ_CP053660.1|WP_171897154.1|65866_66364_+|2-phosphosulfolactate-phosphatase
MAGVGVSGAGGSGDSGVGGGAQVAGAGGGPAVVAASLRNAAAVADWLAPRVAAGATVALVPAGERWPDGSLRPAAEDLWGAGAVLAGLPATLLADPVATSPEARVAVAAWRSVADRLPAELAACAGGRELADLGFADDVAVAAQVGASGVVPLLVDGEFRPAPVM

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Crispr_ID: NZ_CP053660_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP053660_2

278466-278577

Orphan

Consensus_repeat	Method
GGCCTGAGCGTGTCGAAACCCGGTGAGGTG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP053660_2

>merge|NZ_CP053660|2|278466-278577|CRISPRCasFinder
GGCCTGAGCGTGTCGAAACCCGGTGAGGTGCGCAGGGCGGTGGGGACGGCCGCCCCCGCTGGTTGAGCAGCGAAGGCCGCCAGGCCTGAGTGTGTCGAAACCCGGTGAGGTG

>NZ_CP053660|2|2|278466-278577|CRISPRCasFinder
GGCCTGAGCGTGTCGAAACCCGGTGAGGTG	CGCAGGGCGGTGGGGACGGCCGCCCCCGCTGGTTGAGCAGCGAAGGCCGCCA
GGCCTGAGTGTGTCGAAACCCGGTGAGGTG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP053660.1\|WP_154613403.1\|278720_279020_+\|GIY-YIG-nuclease-family-protein	unknown	unknown	gnl\|CDD\|198403
NZ_CP053660.1\|WP_154612810.1\|285384_286491_+\|ring-opening-amidohydrolase	unknown	unknown	gnl\|CDD\|274266
NZ_CP053660.1\|WP_154613402.1\|276312_276987_+\|SRPBCC-family-protein	unknown	unknown	gnl\|CDD\|176853
NZ_CP053660.1\|WP_154613387.1\|267146_268622_-\|FdrA-family-protein	unknown	unknown	gnl\|CDD\|180395
NZ_CP053660.1\|WP_154613401.1\|273913_276316_+\|molybdopterin-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|376913
NZ_CP053660.1\|WP_154613653.1\|277049_278405_+\|amidase	unknown	unknown	gnl\|CDD\|236028
NZ_CP053660.1\|WP_154613654.1\|287843_289514_+\|long-chain-fatty-acid--CoA-ligase	unknown	unknown	gnl\|CDD\|181381
NZ_CP053660.1\|WP_154613405.1\|281559_283542_+\|hydantoinase-B/oxoprolinase-family-protein	unknown	unknown	gnl\|CDD\|376810
NZ_CP053660.1\|WP_171895976.1\|269556_270819_+\|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|379258
NZ_CP053660.1\|WP_154613655.1\|289663_290776_+\|YihY/virulence-factor-BrkB-family-protein	unknown	unknown	gnl\|CDD\|377085
NZ_CP053660.1\|WP_171895977.1\|272424_273285_+\|xanthine-dehydrogenase-family-protein-subunit-M	unknown	unknown	gnl\|CDD\|224238
NZ_CP053660.1\|WP_171895978.1\|273281_273917_+\|(2Fe-2S)-binding-protein	unknown	unknown	gnl\|CDD\|224991
NZ_CP053660.1\|WP_154613404.1\|279490_281563_+\|hydantoinase/oxoprolinase-family-protein	unknown	unknown	gnl\|CDD\|223223
NZ_CP053660.1\|WP_154613407.1\|290934_291726_-\|SRPBCC-domain-containing-protein	unknown	unknown	gnl\|CDD\|176856
NZ_CP053660.1\|WP_154613406.1\|284433_285381_+\|carbamate-kinase	unknown	unknown	gnl\|CDD\|237071
NZ_CP053660.1\|WP_154612811.1\|286600_287767_-\|CoA-transferase	unknown	unknown	gnl\|CDD\|367110
NZ_CP053660.1\|WP_154613014.1\|265734_267093_-\|DUF1116-domain-containing-protein	unknown	unknown	gnl\|CDD\|377673
NZ_CP053660.1\|WP_154612808.1\|283562_284363_+\|NmrA-family-NAD(P)-binding-protein	unknown	unknown	gnl\|CDD\|187578
NZ_CP053660.1\|WP_171895975.1\|268686_269454_-\|DUF2877-domain-containing-protein	unknown	unknown	gnl\|CDD\|378658
NZ_CP053660.1\|WP_154612802.1\|270966_272331_+\|nitrate-reductase	unknown	unknown	gnl\|CDD\|132655

Protein	Function_ID	Function_description	E-value
NZ_CP053660.1\|WP_154613403.1\|278720_279020_+\|GIY-YIG-nuclease-family-protein	gnl\|CDD\|198403	cd10456, GIY-YIG_UPF0213, The GIY-YIG domain of uncharacterized protein family UPF0213 related to structure-specific endonuclease SLX1. This family contains a group of uncharacterized proteins found mainly in bacteria and several in dsDNA viruses. Although their function roles have not been recognized, these proteins show significant sequence similarities with the N-terminal GIY-YIG endonuclease domain of structure-specific endonuclease subunit SLX1, which binds another structure-specific endonuclease subunit SLX4 to form an active heterodimeric SLX1-SLX4 complex. This complex functions as a 5' flap endonuclease in yeast, and has also been identified as a Holliday junction resolvase in human.	1.08431e-28
NZ_CP053660.1\|WP_154612810.1\|285384_286491_+\|ring-opening-amidohydrolase	gnl\|CDD\|274266	TIGR02714, Cyanuric_acid_amidohydrolase, ring-opening amidohydrolases. Members of this family are are ring-opening amidohydrolases, including cyanuric acid amidohydrolase (EC 3.5.2.15) (AtzD and TrzD) and barbiturase. Note that barbiturase does not act as defined for EC 3.5.2.1 (barbiturate + water = malonate + urea) but rather catalyzes the ring-opening of barbituric acid to ureidomalonic acid (see Soong, et al., ).	1.28282e-179
NZ_CP053660.1\|WP_154613402.1\|276312_276987_+\|SRPBCC-family-protein	gnl\|CDD\|176853	cd05018, CoxG, Carbon monoxide dehydrogenase subunit G (CoxG). CoxG has been shown, in Oligotropha carboxidovorans, to anchor the carbon monoxide (CO) dehydrogenase to the cytoplasmic membrane. The gene encoding CoxG is part of the Cox cluster (coxBCMSLDEFGHIK) located on a low-copy-number, circular, megaplasmid pHCG3. This cluster includes genes encoding subunits of CO dehydrogenase and several accessory components involved in the utilization of CO. This family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands.	3.95682e-50
NZ_CP053660.1\|WP_154613387.1\|267146_268622_-\|FdrA-family-protein	gnl\|CDD\|180395	PRK06091, PRK06091, membrane protein FdrA; Validated.	3.18279e-127
NZ_CP053660.1\|WP_154613401.1\|273913_276316_+\|molybdopterin-dependent-oxidoreductase	gnl\|CDD\|376913	pfam02738, Ald_Xan_dh_C2, Molybdopterin-binding domain of aldehyde dehydrogenase.	0
NZ_CP053660.1\|WP_154613653.1\|277049_278405_+\|amidase	gnl\|CDD\|236028	PRK07486, PRK07486, amidase; Provisional.	6.12066e-155
NZ_CP053660.1\|WP_154613654.1\|287843_289514_+\|long-chain-fatty-acid--CoA-ligase	gnl\|CDD\|181381	PRK08316, PRK08316, acyl-CoA synthetase; Validated.	0
NZ_CP053660.1\|WP_154613405.1\|281559_283542_+\|hydantoinase-B/oxoprolinase-family-protein	gnl\|CDD\|376810	pfam02538, Hydantoinase_B, Hydantoinase B/oxoprolinase. This family includes N-methylhydaintoinase B which converts hydantoin to N-carbamyl-amino acids, and 5-oxoprolinase EC:3.5.2.9 which catalyzes the formation of L-glutamate from 5-oxo-L-proline. These enzymes are part of the oxoprolinase family and are related to pfam01968.	8.11151e-159
NZ_CP053660.1\|WP_171895976.1\|269556_270819_+\|helix-turn-helix-domain-containing-protein	gnl\|CDD\|379258	pfam13556, HTH_30, PucR C-terminal helix-turn-helix domain. This helix-turn-helix domain is often found at the C-terminus of PucR-like transcriptional regulators such as Bacillus subtilis pucR and is likely to be DNA-binding.	4.05059e-14
NZ_CP053660.1\|WP_154613655.1\|289663_290776_+\|YihY/virulence-factor-BrkB-family-protein	gnl\|CDD\|377085	pfam03631, Virul_fac_BrkB, Virulence factor BrkB. This family acts as a virulence factor. In Bordetella pertussis, BrkB is essential for resistance to complement-dependent killing by serum. This family was originally predicted to be ribonuclease BN, but this prediction has since been shown to be incorrect.	4.11969e-25
NZ_CP053660.1\|WP_171895977.1\|272424_273285_+\|xanthine-dehydrogenase-family-protein-subunit-M	gnl\|CDD\|224238	COG1319, CoxM, Aerobic-type carbon monoxide dehydrogenase, middle subunit CoxM/CutM homologs [Energy production and conversion].	5.43382e-67
NZ_CP053660.1\|WP_171895978.1\|273281_273917_+\|(2Fe-2S)-binding-protein	gnl\|CDD\|224991	COG2080, CoxS, Aerobic-type carbon monoxide dehydrogenase, small subunit CoxS/CutS homologs [Energy production and conversion].	1.43968e-70
NZ_CP053660.1\|WP_154613404.1\|279490_281563_+\|hydantoinase/oxoprolinase-family-protein	gnl\|CDD\|223223	COG0145, HyuA, N-methylhydantoinase A/acetone carboxylase, beta subunit [Amino acid transport and metabolism / Secondary metabolites biosynthesis, transport, and catabolism].	0
NZ_CP053660.1\|WP_154613407.1\|290934_291726_-\|SRPBCC-domain-containing-protein	gnl\|CDD\|176856	cd07814, SRPBCC_CalC_Aha1-like, Putative hydrophobic ligand-binding SRPBCC domain of Micromonospora echinospora CalC, human Aha1, and related proteins. This family includes the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of Micromonospora echinospora CalC, human Aha1, and related proteins. Proteins in this group belong to the SRPBCC domain superfamily of proteins, which bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. MeCalC confers resistance to the enediyne, calicheamicin gamma 1 (CLM), by a self sacrificing mechanism which results in inactivation of both CalC and the highly reactive diradical enediyne species. MeCalC can also inactivate two other enediynes, shishijimicin and namenamicin. A crucial Gly of the MeCalC CLM resistance mechanism is not conserved in this subgroup. This family also includes the C-terminal, Bet v1-like domain of Aha1, one of several co-chaperones, which regulate the dimeric chaperone Hsp90. Aha1 promotes dimerization of the N-terminal domains of Hsp90, and stimulates its low intrinsic ATPase activity, and may regulate the dwell time of Hsp90 with client proteins. Aha1 can act as either a positive or negative regulator of chaperone-dependent activation, depending on the client protein, but the mechanisms by which these opposing functions are achieved are unclear. Aha1 is upregulated in a number of tumor lines co-incident with the activation of several signaling kinases.	6.71896e-23
NZ_CP053660.1\|WP_154613406.1\|284433_285381_+\|carbamate-kinase	gnl\|CDD\|237071	PRK12353, PRK12353, putative amino acid kinase; Reviewed.	9.19364e-145
NZ_CP053660.1\|WP_154612811.1\|286600_287767_-\|CoA-transferase	gnl\|CDD\|367110	pfam02515, CoA_transf_3, CoA-transferase family III. CoA-transferases are found in organisms from all lines of descent. Most of these enzymes belong to two well-known enzyme families, but recent work on unusual biochemical pathways of anaerobic bacteria has revealed the existence of a third family of CoA-transferases. The members of this enzyme family differ in sequence and reaction mechanism from CoA-transferases of the other families. Currently known enzymes of the new family are a formyl-CoA: oxalate CoA-transferase, a succinyl-CoA: (R)-benzylsuccinate CoA-transferase, an (E)-cinnamoyl-CoA: (R)-phenyllactate CoA-transferase, and a butyrobetainyl-CoA: (R)-carnitine CoA-transferase. In addition, a large number of proteins of unknown or differently annotated function from Bacteria, Archaea and Eukarya apparently belong to this enzyme family. Properties and reaction mechanisms of the CoA-transferases of family III are described and compared to those of the previously known CoA-transferases.	2.85951e-132
NZ_CP053660.1\|WP_154613014.1\|265734_267093_-\|DUF1116-domain-containing-protein	gnl\|CDD\|377673	pfam06545, DUF1116, Protein of unknown function (DUF1116). This family contains hypothetical bacterial proteins of unknown function.	1.09333e-122
NZ_CP053660.1\|WP_154612808.1\|283562_284363_+\|NmrA-family-NAD(P)-binding-protein	gnl\|CDD\|187578	cd05269, TMR_SDR_a, triphenylmethane reductase (TMR)-like proteins, NMRa-like, atypical (a) SDRs. TMR is an atypical NADP-binding protein of the SDR family. It lacks the active site residues of the SDRs but has a glycine rich NAD(P)-binding motif that matches the extended SDRs. Proteins in this subgroup however, are more similar in length to the classical SDRs. TMR was identified as a reducer of triphenylmethane dyes, important environmental pollutants. This subgroup also includes Escherichia coli NADPH-dependent quinine oxidoreductase (QOR2), which catalyzes two-electron reduction of quinone; but is unlikely to play a major role in protecting against quinone cytotoxicity. Atypical SDRs are distinct from classical SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.	1.9473e-30
NZ_CP053660.1\|WP_171895975.1\|268686_269454_-\|DUF2877-domain-containing-protein	gnl\|CDD\|378658	pfam11392, DUF2877, Protein of unknown function (DUF2877). This bacterial family of proteins are putative carboxylase proteins however this cannot be confirmed.	7.14227e-22
NZ_CP053660.1\|WP_154612802.1\|270966_272331_+\|nitrate-reductase	gnl\|CDD\|132655	TIGR03616, Putative_pyrimidine_permease_RutG, pyrimidine utilization transport protein G. This protein is observed in operons extremely similar to that characterized in E. coli K-12 responsible for the import and catabolism of pyrimidines, primarily uracil. This protein is a member of the uracil-xanthine permease family defined by TIGR00801. As well as the The Nucleobase:Cation Symporter-2 (NCS2) Family (TC 2.A.40).	9.96822e-103

>NZ_CP053660.1|WP_154613653.1|277049_278405_+|amidase
MAAAVRRRDVSARELLDLHLARIAERNPQLNAVVSLDEERARAGAAAADEALARGEEVGPLHGLPFAFKDTHAVGGWRTTYGSTLRAEHVPDRDELLVERVRGAGAVTIGKTNVPEFAAGSHTFNKVFGTTLNPVDASRSAGGSSGGAACALAAGMVPLADGSDMGGSLRNPASFCGVVGMRPSLGRVPEWPLYNQWETTSVGGPMARNVADLALLLSVMAGPDARAPQALGDAGSTFADPRPAALGGLRVALSTDLGGAFEVDHEVAGVVEATGRALASAGAAVSGAHPDLGLAEDTFRTLRAWHFQAKFGALLAEHPDAFKASLADNIRAGESLTGADVARAYTQRTALSETMREFFGSYDVLVLPVSQVPPFPADQEFPSAINGKPMETYLDWMRSAYFITVTGCPAISVPAGTTRDGLPVGVQIVAPHGADLRLLEVARAVEGLVSP
>NZ_CP053660.1|WP_154613402.1|276312_276987_+|SRPBCC-family-protein
MKIAGQNTIAAPVDKVWEALLDPRVLVATIPGCEQLQTTGENAYAMTVSAGVAAIKGTYNGACTLSDLQQHESLTMGLKGAGAPGTIDATVAVRFEPQGEETVLSYDADAVVGGMIGGVGQRMLTSVSRRMAAEFFGNVEKVIANGLPAEAAAAPAAPASSDGAAPAGAAAPAAVAADATVFAAAAAAPRASVGGDQSFLTGVVVGGALVLAGVVVGGLLGRRR
>NZ_CP053660.1|WP_154613401.1|273913_276316_+|molybdopterin-dependent-oxidoreductase
MTTKLMGEAVQRVEDDRLLRGGGQYVDDIDLGALHVAVLRSPHAHARILSVDVDAVLDVEGVHAVWTYDDLEGAMAEPLPLLIPHPTLTHGRTQYALARDEVNYVGEAIAIVVAEDRYVAEDAVAQIVVDYELLPAVVGIEAARAAEHLVHDDVPGNIAARSEQSNGDAEAAIAAAPHTLSLDFDIERSACMPMEGRGVTARWDTANGRLQVWTSTQTSTGVRAAVAAKLGLDLLQVDVITPDVGGGFGVKINHPWPEELLVSLAAQRLGRPVKFTEDRREHFISSAHERAQLHHVEVGFDDEGRLLGLDVRFWHDHGAYTPYGLIVPINASTQLVGPYKTGPYRVVFDSLYTNTVIVTPYRGAGRPQGCFVMERTMDAIAAYLGKDRADVREVNLIQPDEFPYDHGLVFQDGRETIYDSGDFPAMLEKIKTLVGWEGFPAYRAEMAAQGRRVGIGLAAYVEGTGAGPYEGAHVNIESSGKVKVATGLTSQGQGHQTAFAQIVADELGVPFEDVEITTGDTRRMAYAVGTFASRAAVMSGSAIHLAAKRAKEKVLRLASDALEADPEDLQIVDGVVSVKGSPGTSISLGTVAVLSNPLRYAFDEASKAATQFSVGDPTKPPVAEDDEPGLEGKDFYSPTRSTFASGMHAVIVETDPDTAEITILKYAVVHDCGTVINPMIVEGQIHGGVAQGVGGALYEKMAYDESGQLLNASFMDFLMPYVTEVPDSIDIDHLETPSPLNPLGIKGAGEAGVIPGSAAIAAAIEDAEGLPITAMPISPSELFELRAQHAVATTTPEENR
>NZ_CP053660.1|WP_171895978.1|273281_273917_+|(2Fe-2S)-binding-protein
MTVAENPAGNPAGKTAEKTHDVRLEVNGVTHDVAVPARRLLSDALRQECGLTGTHVGCEHGVCGACTVLVDGRPVRSCLMFAVSAVGTEITTVEGLAEPDGSLNPVQQAFRECHGLQCGFCTPGFLTTVTAGLKENPCPTHEEAKEMVAGNLCRCTGYQNIVKAVERAAEIARGDAPAAPPPDGPDGGLEAASGEAEVARDDDASTTGLGA
>NZ_CP053660.1|WP_171895977.1|272424_273285_+|xanthine-dehydrogenase-family-protein-subunit-M
MKPTAFDYARPETLEEAVQALGSHPDSKVLAGGQSLVPLMSMRLAAPALLVDINGLPDLDHVTADASGVRIGALARHADVLASPDVRRVQPLVSLALANVAHPTIRNRGTTVGSIVHADAAAEMPMVLQLLDGSVDVVGPAGRRTIAAADLYVGPLESSLAHDEVAVEAFFPALPAGSGVAFEEISRRHGDYAMCGVAAVVAVEDGRVVSARAGYLSVSDVPVVVDLTEALAGAVDEPALARAAEAALAQLEPETDIHASAAYRAHLVTVLTARVLTAAHDHAREE
>NZ_CP053660.1|WP_154612802.1|270966_272331_+|nitrate-reductase
MSMFKWTQVDPAPGEAVGPMERLSWGKTIGLGAQHVVAMFGATFVFPLIMGLDANLAILFSGICTILFLLVVNNKVPSYLGTSGSFVSGVAAIRAQGGDSADVTGAILIAGVILLLVGVLVHYIGTNAIKRILPPAVTGAVVMLIGFNLAPVVANTYWPQDQWIALATAAFVVVAAVRFPGFWSRISIFLALIFGYALSFLTDVVFGQITSPDGTGTVTTRDRVNLSGLGDAPWFGLPTGDLADGVSKVHAPDFSLTFALLVIPAVIALIAENTGHVRAVAEMTGDDLDPYMGRALGADGAATALASAFGASPTTTYAENIGVMSATKVYSTAAYYVAAAVAIILGLCPKFGVVINAIPGGVLGGITVVLYGMIGLIGAKIWVDNRIDFGSPINMVPLAAGLIAGIGNVTLVMGDFELSGIALGTIMVIAFYHLVNIGRPRDHKTGAEDVTRAM
>NZ_CP053660.1|WP_171895976.1|269556_270819_+|helix-turn-helix-domain-containing-protein
MSSPTPSPEPSVEPLDVDELAEGLAQQVLANADLGAIVDAIGASLRVDVAVTTTDGRERVTRLRDAVRGALEAGDLVDPTGRLRVERLDAEDTVLAGGSRVHRLQVATPAQPLGHLVVVADRALTDLERVALRRAVTAVALSISRQQAVSAVENKYRGDFLRDVLLGRAGSEEFVREHVAGFGWDLGGPSIVLVAQLDPPPAGEPSGTVEEQRLWQERFADAWRQVLGGVSRAVPVADFGSEVVTVLPAEGSVPGSDPVLRLVRTVAGDKGGGRRPFSVGVGRLARDVRSLPESYAQAYRAVAVGRRVRGGGTTTWFDELGLHRLIAMVPDDMELRAFATDVLGELAGQTEEAAALRETLQVLLSTNFNVAEAARLQFFHYNTIRYRVTKLERLLGPITSDHNLRLDVAVALKVLEVVGG
>NZ_CP053660.1|WP_171895975.1|268686_269454_-|DUF2877-domain-containing-protein
MPPPRSTRTRVAGAGTAALRRRLQEEPGTGEVVHSGASAIYVLLRHEAGDRVVGVAAHGAVHVPATIATALASLPDVPVGTPATVVDGVLHVGHLAVAVDRLVPTDLPALPPEAADRLAAATPDLTPVRDQLPAAALDALAAGDGDAVEALLGRGDGLTPVGDDVVAGWLVAARAADRPRGAVAAGVRRWAHRTTTLSATLLVDAIEGGCIPEFRSLLLALATGRDVDGAVARLTAVGHTSGAGMLLGAGLALRP
>NZ_CP053660.1|WP_154613387.1|267146_268622_-|FdrA-family-protein
MTVEHVEIRAGAYADSVALLQVSRDVAATPGVVAAQVAMATELNLEVLAGMGFTLPPASPNDMVVALRVEDDGVVPAALAAVDAALAAARKGAAGGGDTTLAAPRTTGSALRRAGGGLALVSVPGASALVEAMDALDAGSDVMVFSDNVPVEQELALKRIARDRGLLVMGPDCGTAVVGGVGLGFANTTAPGRVGIVAASGTGCQQVLALLDHAGVGVSAALGVGGRDLSAAIGGISTMTALDRLDADPTIEQVIVVSKPPAAEVAAAVEEYAAGLGTPVRFALLGAGQPDITTQVESLLADLGVAVPEWPTWGSPAQAVGGSALRGLFVGGTLCDEAMLIAAESLGGIRSNIPLSPELALGPDLTAPGHLMIDFGDDGLTRGRAHPMIDPTLRLDQLTKVAQDPDTAVVLLDVVLGHGAQDDPAADLAPAIAAARAVRDVPVVVACVGTSADPQGLQRQAEALAAAGAEVHLSNAAATRRALALVPGGTL
>NZ_CP053660.1|WP_154613014.1|265734_267093_-|DUF1116-domain-containing-protein
MFAAAVEAQAVPVERVDWKPPMDGTVDDLATVAADPLRRDANARAVKQMLDVQAMLVGVAPASELLGLEKGQFLHAGPPIEWARTAGPLRGALMGAAAFEGLVEDPEDAVALFEAGTEVALEPCHHRGAVGPMAGVVSPSMWMFVLEDPATGRRTYCSLNEGLGKVLRYGAYSPEVLQRLRWMRDSLGPLLAEAVTAAGPIDATAILGQMLQMGDEAHNRNRAGTLMLLRDLAPHLVRSSRPAEEVAEALAFVGGNDHFFLNVAMPACKLALDAARDIEGSTMVVAMARNGTDFGIQVSGTGDQWFTGPAQLADGLFLGDYGPEDANPDIGDSAITETAGIGGFAMAAAPAIVRFVGGTVPDALATSRRMREITIGENDRWPIPVLDFAGAATGIDVSAVCRTGILPQINTGMAGRVAGVGQVGAGLVTPPASIFPAALAALAERTRARAEA
>NZ_CP053660.1|WP_154613403.1|278720_279020_+|GIY-YIG-nuclease-family-protein
MAWTYLLECADGSYYVGSTTDLERRVSEHDLGLGAAYTRPGRRRPVRLVWSAEFNRIDDAYYFEKQLQGWSRAKRQALIDGRLDDLPALARGRWRDAGG
>NZ_CP053660.1|WP_154613404.1|279490_281563_+|hydantoinase/oxoprolinase-family-protein
MTRRMRIGIDTGGTFTDVVAFDEDSGTVVTTKTPSTPGNPADGFLAGIDKVLDLAGASFDDVVAVSHGTTVATNQLLEGKVDALGFITTEGYEAMLEIARQSVPDGYGNSYFWVKPDRIVPRDLVKGVGGRLDHTGAEIRPFDEQGARTVARWFKNQGIDTLGVCFLHAYANPAHEERMREILLEEHPDAVVSISSEVLREYREYERSMTTLVDAAVKPKLSRYVTNIKDRLASQSGRTIPFYVMKSNGGVLSADEVVHQPITTVLSGPAAGALGAALIAKVAGFDKVLTSDGGGTSTDVSVVIDGEPTLTTEGSVGVYPSKIPMIDVVTVGAGGGSIAWLSPEGTLKVGPHSAGADPGPICYRKGGTEVTITDAHVFLGRIPPHLLGGEIPLDVDSASAAIRELAAKLEITPEACATGILEISAWNQANALRQVTVKRGLDVRDFTLTTFGGSGSLLLCRLMDVLGVPTVLVPPNPGNVSAFGLLTVDVKNDYVQTHVALHEDLEPAALQREYDVLTERAAAALATEGFAPEEHVFVRTADVRYFGQAFEVRVAVPDGPISEESLRTVADRFHAEHHTLYGYDFAQDPTQQVEVVNLRVSGVGPIRRPEIPKAISDQATPQQTSTRPVCFDAEAGYVDTPVYWRPDLPAGQELVGPVIIEEFGSTVPIHPGFTARVDDYANIVVTRSDA
>NZ_CP053660.1|WP_154613405.1|281559_283542_+|hydantoinase-B/oxoprolinase-family-protein
MTTDTHSGTSTFAGAPDLGSRRAPTQFPFGPLTEDSGRSADPVLVEIVQGSLAAVEHEVETAIARTSRSPMIRDAHDFRAGIHDRRLRKLTGRSYSALVHPVARDFPIEEMREGDVFFHNDVYLSEGGIGHLPDLCVTVPVFAGPEGERRVVAFVQAFGHHDDIGGAVPGSMPSHATSVYEEGLAVPPIKLWDAGVPNRSALTIMTRNSRMPESLAADLDAECSACLMGARRLGELFDRYGIETVEACFDAIIDRSTETYRREILSKIPVGTWTWEDYAEHDGVDDPQLHTQRITLTRTAADDPDGERLVLDFAGTSPQAKGPINHCGDYSDGVFLKKWLAPILRNLADTPERMAELDVNEGVVPLIEMRFPEKGTLLTPIFPAPTNARTFVILRLLGVLAGVIAKAVDGKMPADQETIRYTGVYGEDLEGRPYLMREVLGGGSGGRYYADGEDTIHVVPDSRNLPTEFTESRFPFIVESLSLAVDSGGAGQFRGGLGYEKHIRMLKDAHFMSIADRSILACWGVKGGKAGTPFQVVIDAGGPNEREVDALADAEEVKAGEVIRIRTTGGGGWGNPLDRDPELVVRDVRWRKVSTEAALADYGVVLTGSVDDDTLSYDAEATATERAGRPAPAVEDAFFDRGPGYGTLAGGAASAEVDHL
>NZ_CP053660.1|WP_154612808.1|283562_284363_+|NmrA-family-NAD(P)-binding-protein
MNVAVLGGTGKTGRAVVAALAQVGVSARPLGRSAFEDLPAALAGADAVHVIAPNLHPDEPAYVASVLAAAAEANVDRLTYHSVASPYAPSMPHHLGKAVAEDLVRRSGLRWTVLQPCAYVQNFLPALADLPAEGGELAVPYAVDTPFGLVDLDDVAAATAVVLTTPGHEGATYELGGPALVTVAGVAGAAAEVLERPVRARRTDPDAWRGEGLDERERAWLRSMFAYYDDHGLPTGPLPLAALLAMVGRAPSPVADVLARVLAGTS
>NZ_CP053660.1|WP_154613406.1|284433_285381_+|carbamate-kinase
MRILLALGGNAMTSPDGKARPEDQIAAAEKAMEAVAALVAEGIDVIVTHGNGPQVGNLLVKNEIAAGVVPLVPLDWCGAQTQGTIGNILVNALDRALALRGIERPAAALVTRTRVDADDPAFAKPSKPIGRYLPEPEARRMIEHGETWEDRGERGWRRVVASPEPLEVLDAPAVVALVDAGFVVVANGGGGIPTVRRDDGSLAGVEAVIDKDLGAALLARDIEVDMLVIATDVAHAVLGFGTPEAEDVGEVTLTQMREHAAAGHFAGGSMGPKVDAVCRFVEHSGRPGVITDLGTIVAAANRTAGTIVVPDRKEA
>NZ_CP053660.1|WP_154612810.1|285384_286491_+|ring-opening-amidohydrolase
MPEAIEVRKVPIHSVADASELAKLIDEGVFAADRVIAIIGKTEGNGGVNDYTRIIADRAFREVLIEKGAPADQVKQVPIVWSGGTDGVISPHATIFATVDVPEDDPSRQEQRLTVGFAMSEPILPEEIGYVAMIKKVADGVKVAMERAGITDVKDVHYVQTKTPLLTIHTIRDAHSRGKEVWTEHTHESMDLSNGVTGLGIAVALGEIEMPSDEDVMKNRDLFSSVASCSSGVELDQAQIVVVGNATGVGGRYRIGHSVMKDALDQDGIWEAIKSAGLDLPERPHHTDLDGRLVNVFLKCEVSGDGQVRGRRNAMLDDSDVHWHRQIKSCVGGVTAAVTGDPAVFVSVSAAHQGPDGGGPVAAIVDLG
>NZ_CP053660.1|WP_154612811.1|286600_287767_-|CoA-transferase
MPAPLDDVLVLDLTRALAGPHAAMMLGDLGARVIKVESPTGDDTRGWGPPFVDPAEEGASRESTYFLSTNRNKESITLDLKDPADQEVLAKLVQRADVLMENFRVGVLDRLGFPVSRLHELNPRLVVLQITGFGHDGPEASRSGFDQIAQGEGGLMSLTGLTEPTKVGVPIADLLAGMNGAYGVVSALYERERTGKGRVVHTSLLAGMVGVHAFQGTKWTVAKEVPGLAGGHHPSIAPYGMFRSATAPVQIACGSEKLWQAFAKEFGIDPAGEGFATNAERVANRDALIETIEGLLADVDAETALARLDAAGVPAGKVRSLDDVYSWEQTLSQGLLLDVEHSTLGPIQLPGSPLRFDDNAFSGAREQHVAPPTLGQHNDAIRAWLDED
>NZ_CP053660.1|WP_154613654.1|287843_289514_+|long-chain-fatty-acid--CoA-ligase
MARALAWAAPHHPCPTAPPRGAPVPETPTSAPATDRTADHATDVRTARGNGLGDVLRRSAARHPGKPAIVDGATTLTYRELDAMVDAVAWSLERDGIGVGDRVALLSRNSWQFAALAWGAARRGAVLVPVNFMLTAPEVAFLLGDAEVSLAFAQDAFAGVMGEALETAGLADAAPLVTIGEGAGEARSFDRWLEDAPAGWEAPYVDDDAPVRIMYTSGTESRPKGAMLSSRSLVAEYTSCIVDGGMSADDVDLHTLPLYHCAQLDCFLGPDLMLGATSIILPAPDPAAVLAAIAEHGVTKYFAPPTVWISLLRSPDLDRTDTSSLRKGYYGASPMPVEVLRELLERLPGVDLWNFYGQTEIAPVATILPPHEQLEAAGSAGRPVLNVETRVVDDEGRPVPVGEVGEIVHRTPQATLGYWRNPEKTAEAFRGGWFHSGDLGILDEHGRLSVVDRKKDMIKSGGENVASREVEEALYLHPDVSEVAVFGIADPKWIEAVVAAVVLKDGSTATAADLVEHCRARLAAYKCPKRIELREALPKNPSGKILKRVLREEITG
>NZ_CP053660.1|WP_154613655.1|289663_290776_+|YihY/virulence-factor-BrkB-family-protein
MRDGDREETGPKTGPADPASPADQPLGGVDAWQRRHPVVAFPLAVVYKFFDDQGVYLAVLITYYAFVAVVPLLLLATSVLGFVLQADAELQARILDSAIANFPVVGDQLGRPEGLQGSVAAIVIGGLAAVYGSLGLGTALQNAVNITWAVPRNSRPNPFLVRLRSLVLLATGGLALVALTVLAALNQVLASRLGGSALVQWGLTLALIGLVAAILTVLLWVSGGRRQPVHTAVPGAVLTAVLWHALQMVSASVAQQAANQASSMNQTFGLVLGLLAVTYLAATSAVLGMEVNVVVHRRLWPRALLTPFTDAVALTDADRRAYAGYARAQRHKGFEVVEVRFKDLLEEDPDAPEDGSDDAPEDRADGGSVR
>NZ_CP053660.1|WP_154613407.1|290934_291726_-|SRPBCC-domain-containing-protein
MSTTPNVPYRLEFSVEVPGTPEQVWQAIATAQGMSAWFTPTEMEEREGGSLHFSMGPEMGSDGQVTAWEPPRRLVYEEDWAALMGKEPDALSPLTSEFLVEAQSGGTCVVRVTSSGFGTGAAWEPEFWDTMAPGWMPFFDNLRLYLAHFPGQEATHLEATASHDGAADALWSALHDALDLGAKGATVEVRGATGTVERVGDRQMLVRLTAPVPGMLSLYTWDDADGRATAGVRAYLFSADAADYVRREEPAWRAWLEGLSVPA

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Crispr_ID: NZ_CP053660_3

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP053660_3

848435-848589

Orphan

Consensus_repeat	Method
CGCCAGGGCTCGCTGCTCGACCAGCGGGTGGCCGCCAGGGCTCGCTGCTCGACCA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP053660_3

>merge|NZ_CP053660|3|848435-848589|CRISPRCasFinder
CGCCAGGGCTCGCTGCTCGACCAGCGGGTGGCCGCCAGGGCTCGCTGCTCGACCAGCGGGGGTGGCCGCCAGGGCTCGCTGCTCGACCAGCGGGGGTGGCCGCCAGGGCTCGCTGCTCGACCAGCGGGTGGCCGCCAGGGCTCGCTGGTCGACCA

>NZ_CP053660|3|3|848435-848589|CRISPRCasFinder
CGCCAGGGCTCGCTGCTCGACCAGCGGGTGGCCGCCAGGGCTCGCTGCTCGACCA	GCGGGGGTGGCCGCCAGGGCTCGCTGCTCGACCAGCGGGGGTGGC
CGCCAGGGCTCGCTGCTCGACCAGCGGGTGGCCGCCAGGGCTCGCTGGTCGACCA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP053660.1\|WP_154613814.1\|853369_854626_+\|glucose-1-phosphate-adenylyltransferase	unknown	unknown	gnl\|CDD\|234846
NZ_CP053660.1\|WP_154613813.1\|851612_852038_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP053660.1\|WP_154613812.1\|850184_850910_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP053660.1\|WP_171896128.1\|845549_846173_+\|dienelactone-hydrolase-family-protein	unknown	unknown	gnl\|CDD\|366166
NZ_CP053660.1\|WP_154613811.1\|849660_850188_+\|YfcE-family-phosphodiesterase	unknown	unknown	gnl\|CDD\|223695
NZ_CP053660.1\|WP_154613803.1\|842818_843178_+\|rhodanese-like-domain-containing-protein	unknown	unknown	gnl\|CDD\|238089
NZ_CP053660.1\|WP_154613806.1\|845369_845513_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP053660.1\|WP_171896133.1\|852145_853333_-\|glycogen-synthase	unknown	unknown	gnl\|CDD\|273997
NZ_CP053660.1\|WP_154613999.1\|849325_849574_+\|TraR/DksA-C4-type-zinc-finger-protein	unknown	unknown	gnl\|CDD\|274340
NZ_CP053660.1\|WP_154613816.1\|855282_855765_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP053660.1\|WP_154613805.1\|844895_845285_-\|DUF2237-family-protein	unknown	unknown	gnl\|CDD\|378344
NZ_CP053660.1\|WP_171896132.1\|850831_851593_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP053660.1\|WP_171896130.1\|847686_848052_+\|HNH-endonuclease	unknown	unknown	gnl\|CDD\|238038
NZ_CP053660.1\|WP_171896135.1\|854633_855224_-\|mismatch-specific-DNA-glycosylase	unknown	unknown	gnl\|CDD\|381679
NZ_CP053660.1\|WP_154613802.1\|841832_842822_+\|aldo/keto-reductase	unknown	unknown	gnl\|CDD\|381312
NZ_CP053660.1\|WP_154613810.1\|848717_849209_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP053660.1\|WP_154613807.1\|846178_846703_+\|gluconokinase	unknown	unknown	gnl\|CDD\|225804
NZ_CP053660.1\|WP_154613804.1\|843222_844371_+\|23S-rRNA-(uracil(747)-C(5))-methyltransferase-RlmC	unknown	unknown	gnl\|CDD\|235128
NZ_CP053660.1\|WP_154613808.1\|846782_847781_+\|DUF222-domain-containing-protein	unknown	unknown	gnl\|CDD\|367155
NZ_CP053660.1\|WP_171896127.1\|844445_844856_+\|hypothetical-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_CP053660.1\|WP_154613814.1\|853369_854626_+\|glucose-1-phosphate-adenylyltransferase	gnl\|CDD\|234846	PRK00844, glgC, glucose-1-phosphate adenylyltransferase; Provisional.	0
NZ_CP053660.1\|WP_171896128.1\|845549_846173_+\|dienelactone-hydrolase-family-protein	gnl\|CDD\|366166	pfam00561, Abhydrolase_1, alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes.	5.34505e-07
NZ_CP053660.1\|WP_154613811.1\|849660_850188_+\|YfcE-family-phosphodiesterase	gnl\|CDD\|223695	COG0622, COG0622, Predicted phosphoesterase [General function prediction only].	4.6491e-37
NZ_CP053660.1\|WP_154613803.1\|842818_843178_+\|rhodanese-like-domain-containing-protein	gnl\|CDD\|238089	cd00158, RHOD, Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. The cysteine containing enzymatically active version of the domain is also found in the Cdc25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and certain stress proteins such as senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions (no active site cysteine) are also seen in dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases, where they are believed to play a regulatory role in multidomain proteins.	3.00047e-26
NZ_CP053660.1\|WP_171896133.1\|852145_853333_-\|glycogen-synthase	gnl\|CDD\|273997	TIGR02149, glgA_Coryne, glycogen synthase, Corynebacterium family. This model describes Corynebacterium glutamicum GlgA and closely related proteins in several other species. This enzyme is required for glycogen biosynthesis and appears to replace the distantly related TIGR02095 family of ADP-glucose type glycogen synthase in Corynebacterium glutamicum, Mycobacterium tuberculosis, Bifidobacterium longum, and Streptomyces coelicolor. [Energy metabolism, Biosynthesis and degradation of polysaccharides].	0
NZ_CP053660.1\|WP_154613999.1\|849325_849574_+\|TraR/DksA-C4-type-zinc-finger-protein	gnl\|CDD\|274340	TIGR02890, conserved_hypothetical_protein, regulatory protein, yteA family. Members of this predicted regulatory protein are found only in endospore-forming members of the Firmicutes group of bacteria, and in nearly every such species; Clostridium perfringens seems to be an exception. The member from Bacillus subtilis, the model system for the study of the sporulation program, has been designated both yteA and yzwB. Some (but not all) members of this family show a strong sequence match to Pfam family pfam01258 the C4-type zinc finger protein, DksA/TraR family, but only one of the four key Cys residues is conserved. All members of this protein family share an additional C-terminal domain. Smaller proteins from the proteobacteria with just the N-terminal domain, including DksA and DksA2 are RNA polymerase-binding regulatory proteins even if the Zn-binding site is not conserved. [Unknown function, General].	4.51626e-20
NZ_CP053660.1\|WP_154613805.1\|844895_845285_-\|DUF2237-family-protein	gnl\|CDD\|378344	pfam09996, DUF2237, Uncharacterized protein conserved in bacteria (DUF2237). This domain, found in various hypothetical bacterial proteins, has no known function.	6.41184e-67
NZ_CP053660.1\|WP_171896130.1\|847686_848052_+\|HNH-endonuclease	gnl\|CDD\|238038	cd00085, HNHc, HNH nucleases; HNH endonuclease signature which is found in viral, prokaryotic, and eukaryotic proteins. The alignment includes members of the large group of homing endonucleases, yeast intron 1 protein, MutS, as well as bacterial colicins, pyocins, and anaredoxins.	9.13463e-07
NZ_CP053660.1\|WP_171896135.1\|854633_855224_-\|mismatch-specific-DNA-glycosylase	gnl\|CDD\|381679	cd10028, UDG-F2_TDG_MUG, Uracil DNA glycosylase family 2, includes thymine DNA glycosylase, mismatch-specific uracil DNA glycosylase and similar proteins. Uracil DNA glycosylase family 2 consists of thymine DNA glycosylase (TDG), which removes uracil and thymine from G:U and G:T mismatches in double-stranded DNA. It includes mismatch-specific uracil DNA glycosylase (MUG), the prokaryotic homolog of TDG. Escherichia coli MUG is highly specific to G:U mismatches but also repairs G:T mismatches at high enzyme concentration. Uracil-DNA glycosylases (UDGs) initiate repair of uracils in DNA. Uracil in DNA can arise as a result of misincorporation of dUMP residues by DNA polymerase or via deamination of cytosine. Uracil in DNA mispaired with guanine is one of the major pro-mutagenic events, causing G:C->A:T mutations. Thus, UDG is an essential enzyme for maintaining the integrity of genetic information. UDGs have been classified into various families on the basis of their substrate specificity, conserved motifs, and structural similarities. Although these families demonstrate different substrate specificities, often the function of one enzyme can be complemented by the other..	8.50892e-63
NZ_CP053660.1\|WP_154613802.1\|841832_842822_+\|aldo/keto-reductase	gnl\|CDD\|381312	cd19086, AKR_AKR11C1, AKR11C family of aldo-keto reductase (AKR). Bacillus subtilis uncharacterized oxidoreductase YqkF is a founding member of aldo-keto reductase family 11 member C1 (AKR11C1). It may function as oxidoreductase. This family also includes Bacillus halodurans AKR11C1, an NADPH-dependent 4-hydroxy-2,3-trans-nonenal reductase.	3.94263e-90
NZ_CP053660.1\|WP_154613804.1\|843222_844371_+\|23S-rRNA-(uracil(747)-C(5))-methyltransferase-RlmC	gnl\|CDD\|235128	PRK03522, rumB, 23S rRNA (uracil(747)-C(5))-methyltransferase RlmC.	0
NZ_CP053660.1\|WP_154613807.1\|846178_846703_+\|gluconokinase	gnl\|CDD\|225804	COG3265, GntK, Gluconate kinase [Carbohydrate transport and metabolism].	6.91874e-74
NZ_CP053660.1\|WP_154613808.1\|846782_847781_+\|DUF222-domain-containing-protein	gnl\|CDD\|367155	pfam02720, DUF222, Domain of unknown function (DUF222). This family is often found associated to the N-terminus of the HNH endonuclease domain pfam01844. The function of this domain is uncertain. This family has been called the 13E12 repeat family.	2.68549e-13

>NZ_CP053660.1|WP_171896130.1|847686_848052_+|HNH-endonuclease
MLDDGGVISAATARRLACEAGLIPAVLGTRSELLDLGRKTRLFSGAQRRGLNLTQPTCTAEGCDWPAHLCHAHHDQPWSSGGTTDLANARNLCPRHHARIHDPAFETSHLPDGKVAFHRRT
>NZ_CP053660.1|WP_154613808.1|846782_847781_+|DUF222-domain-containing-protein
MAKDARHHAHTVCRAVAKSRKKTRAAATADLWSMSDEDVEATLLEAEKLRAQADALALRLVAEADRRHAGERAGATDTASWWAHRTRQERRVAKGRARLAESLNRHEPTSAALVEGAISIDHARVITSCVDRLPEDLEDPTVPARAEQHLLDEAAHLDPKTLAVLAKHVLTVVAPEVGEARDARALEREEREARANAWLTMCPDGKGSVRGKFSIPELHAAMLHKTLLAYAAPKHQAATRTEDPDAAEEIERRPSPERMGDAFCELLERLPTDTLPRLGGLNATVVVTLDHESLGGGLAPGGARRRRRHLCRHRQTPRMRSRTHPGRPWHQV
>NZ_CP053660.1|WP_154613807.1|846178_846703_+|gluconokinase
MGHLLVVMGVSGSGKSTVGAALARRLGVPFADADDLHPAANIAKMSRGEPLDDGDRRPWLEEVGRWLARHLDGGVMSCSALKRAYRDQLRHHAPATTFVLLDGDPDVIARRQSVRAGHFMPASLLTSQLATLEPLEPDEGGIVLDVDQGVDAIVQAYLDAVEARGRGRRGGARS
>NZ_CP053660.1|WP_171896128.1|845549_846173_+|dienelactone-hydrolase-family-protein
MSQPRLVATRTPPRAEAVVLVLHGGDQRPEDPLVSPWQLSVLRMVPVAARIARAGRGRLAVHRVLNARRGWGTGRTPVDDARWAMDRVGERYGDLPVGLVGHSLGGRAALLAGQDPRVAAVVALNPWLHRADDADLAGRRVLLVHGTEDRVAAPERARAVADRLRRRADVEWREVPGAGHAMLRHRPVFERAAADFLTETLLPPGVR
>NZ_CP053660.1|WP_154613806.1|845369_845513_+|hypothetical-protein
MYAATRPRPRGSWRALSREQKQARLQRLRERQRREVELEIRRLGPLD
>NZ_CP053660.1|WP_154613805.1|844895_845285_-|DUF2237-family-protein
MGERNVLGGELVPCGTDPLTGFYRDGSCSCGSDDVGLHAVCAVMTADFLEHQRSVGNDLTTPRPEWHFPGLHPGDPWCVVAGRWLQSYQAGAAAPVVLAATNERALEVVRIELLEEHAVDVPPDLSSLG
>NZ_CP053660.1|WP_171896127.1|844445_844856_+|hypothetical-protein
MAEDYCELCDLPLSQCVHGRPEPVPVPAEKAAPVRTRTPARVPGTPVKKAPPRKWTSPDELKAPIVALLQEHGGELPADEVFPALDELLGEALRPGDRDPSPTGEPRWQLAARKARRALQDEGVIEPGTPGVWRLR
>NZ_CP053660.1|WP_154613804.1|843222_844371_+|23S-rRNA-(uracil(747)-C(5))-methyltransferase-RlmC
MELTRSVAVRCDYFDTGRCRSCTLLDQPYPTQLAEKQREVAALLPTPAAGWSEPVASAPAGFRNKAKMVVGGTAAAPTLGILDRDLAGVDLRECRLHTPGLHDALPVLADFIARADLAPYDVAQRRGELKHLLVTESPAGELMVRFVCRSQEPVARLRKHLPWLLERLPVAVATVNLQPDHKAVLEGERELVLTPSSTLAMPLGAVTLHLRPRSFFQTNTAMAVALYAEASAWVAELAPASVWDLYCGVGGFALHLAAPGRAVTGVEISAEAVRSAEHSAAAAGLSDARFVAGDATAYALDAAGDTRPDLVVVNPPRRGIGDQLAGWLEGSGVPHVLYSSCNARTLAADLAAMPSYAPVRGRLLDMFPNTRHYEVLVLLRRR
>NZ_CP053660.1|WP_154613803.1|842818_843178_+|rhodanese-like-domain-containing-protein
MRILLLPFLLVGLLGLGACAEDTSEIERLIDRGATVLDVRTPEEYAAGHIDGAANLDLGAEDFRDRVDELPRDTYYVVYCASGARATRAIEVMRGLGFGSVVNGGGYDALADLGLPTTE
>NZ_CP053660.1|WP_154613802.1|841832_842822_+|aldo/keto-reductase
MDARTLGRTGRDVSVVGLGTWQLGADWGEVSEADARAVLEASVASGVTFLDTADVYGDGRSEQVIGAFLRDHDGLTVATKMGRRVDQVPENYRLDAFREWTDRSRRNLGVDTLDLVQLHCPPSATIADDATYDALDTLVADGAVAAYGVSVETADQALAAIARPHVASVQIILNAFRLKPLDRVLPAAQEAGVGIIARVPLASGLLSGRYDEQTTFAADDHRTYNRDGSAFDKGETFSGVDFATGVAAAREFSRLAAEHGPEGATPAQVALAWVWQQPGVTTVIPGARNPEQARANAAAGSLPPLSAELLSGVRGLYDSYFREAVHGQW
>NZ_CP053660.1|WP_154613810.1|848717_849209_+|hypothetical-protein
MSILTLATRTASVIRPLSVPVRGRLYRRGLDQPVGHAYFDRAGTDDVVVTESREASLLGPQAPVRGLTVHVERGAGEADLTFVLAATTWSRVSRRVRPEVPGLEWTMTGVLADPEAADGADGGEPLLVAARMVGGHTAELAVARQGQPWQEFGCLLISAQATA
>NZ_CP053660.1|WP_154613999.1|849325_849574_+|TraR/DksA-C4-type-zinc-finger-protein
MVEASRDTNADDEHDPEGATIAFERSQLDTLVQQAVRRLAEIEAALDRLAAGTYGVCERCGRPIPAERLEVRPEARRCVACG
>NZ_CP053660.1|WP_154613811.1|849660_850188_+|YfcE-family-phosphodiesterase
MDLVIMADTHLPKRAKDLPAALWAAVEAADVVVHAGDWVDEATLDRLEERSRRLVACWGNNDGPGLRARLPEVARVELDGVRLGVVHETGGRQGREARADAAYPDLDVLVFGHSHIPWDTTTPRGLRLLNPGSPTDRRQQPHCTYLTARVADGVLGDVALHRLPPRTATAPRRTS
>NZ_CP053660.1|WP_154613812.1|850184_850910_+|hypothetical-protein
MRSTNTLSALPARVGGAVIATAVRGLAAARPAEKPMHPVGRVLRGRLERRGVEPGTGVRFLDEPGIDEVVARESKGIGLPEGLPDIHGLAIKVPLGGASPAEAAEESVEHGRRHADVLLSTNGWGPVSRFLVVPSAGMTTRPLTTLFPYRGPQGAVLLGARYVAEHHVELAVAGLRSGWRVFADLHLESVDPDSAAEDDPALEFDAILNELPGLPNYPWVRRVRAPSYAIARRSRRSSDQQ
>NZ_CP053660.1|WP_171896132.1|850831_851593_-|hypothetical-protein
MTTLVYLLLGGSGPLRDALLAGGLRDRLAALGAGRLQVNLDDDPVADAMRIASPDGPVRAVVSVWTGDTATGAVIGAVTDALAGAVAGSGARLAGYEVEQRRPLEPPAVPDGVRADALANVAVLRRPAELDEAEWRHRWLVDHTPVAIATQGTFGYLQNVVVAPVTADAPYVSAIVEELFPMAATTDLHAFYGTGGDDAELRSRMEQMMASVSRFGADRGLDLAPTSRYCWSLERRERRAIAYDGARTRRTQG
>NZ_CP053660.1|WP_154613813.1|851612_852038_-|hypothetical-protein
MTFAPVIETQTDVERAWRALMRPLGWTRASTWLMFVGPDGRPFAHLTEIDDCEGPPPADVAAQLGRLLGHLRDGPLPAGVRVAFLRSRPGVHGIEDDDRAWAATLYAAARTAGMPAEVVHLATDEDVVAVPMEEATLPATT
>NZ_CP053660.1|WP_171896133.1|852145_853333_-|glycogen-synthase
MRVDVLTKEYPPEIYGGAGVHVAELVRALRRREDLTTRVRAFGAPREEPGTSSYAEPAELTGANPALRTLGVDLAMADACAGADLVHSHTWYANLAGHLAGLLHGVPHVVTAHSLEPLRPWKAEQLGGGYAVSGWAERTAYEAAAAVVAVSHAMRDDVLAAYPAVDPARVHVVHNGIDTDLWSPVTDPDRVRGHGLDPDRPSVVFVGRITRQKGLPWFLRAVAALPPEVQVVLCAGAPDTPEIEAEVVALVAELQATRTGVVWIRDMLPRADVVALLSAATVFACPSVYEPLGIVNLEAMACETAVVATATGGIPEVVVDGETGLLVPIEQATDGTGTPVDPDRYVADLAAALTELATDPARAAEMGRAGRVRARSAFDWDTIAERTVEVYRSVI
>NZ_CP053660.1|WP_154613814.1|853369_854626_+|glucose-1-phosphate-adenylyltransferase
MRATSRKKVLAIVLAGGEGKRLMPLTADRAKPAVPFAGIYRLIDFALSNVVNSGYLKVVVLTQYKSHSLDRHISQTWRMSTMLGNYVTPVPAQQRLGKHWYLGSGDAIFQSLNLIRDERPDTVVVVGADHVYRMDFAQMVAQHCESGAACTVAAIRQPIGIADQFGVIDVHPEDPTRIRDFLEKPADPVGLPDSPHEVLASMGNYVFEADALVEAVTRDATTTGSKHDMGADIVPAFVRRSQAAVYDYRDNVVPGATDRDRGYWRDVGTIGTFYAAHMDVVSPLPVFNLYNFDWPIYTSYGPQPPAKVVQGADGAPARVDEAVLSPGSVVSGGTVLRSVISPAVGVAAGAVVEGSVLMQGVRIGPGAVVHNAILDKNVVVPAGARVGVDHEEDRARGFHVEDGLVVLGKDQPFPDPQG
>NZ_CP053660.1|WP_171896135.1|854633_855224_-|mismatch-specific-DNA-glycosylase
MPSSFTRAELESFRDREVPDLLPGPEGPELRLLFVGINPGLWTAATQTHFAHPGNRFYPALLAAGIVERRIDPAAGMTDEDREHLRSRGIGITNVVRRATAKASELSAEEYRAGGLALVETVRRTRPHVVAVAGITAYRAAFSLPKAVPGRQPEPLAGAELWVVPNPSGLNAHETVASLAEAYAAPARAAGILPER
>NZ_CP053660.1|WP_154613816.1|855282_855765_+|hypothetical-protein
MRRHLGTLALSAVLALAVGSTAACGEADGDPSESAVAGIPSPTQETVDPLDADGVESVEIKLVRGTDVGGIVTAEAVPVTEEADLEAFLEQFDPAFAEQVRTRVGQVVLGEEQGILAQVVAVGCESPTSATLRGNAIQTDVPKSSEECRAPVTTVALAVA

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Crispr_ID: NZ_CP053660_4

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP053660_4

1910475-1910573

Orphan

Consensus_repeat	Method
CCGGTTGGCCGCTGAAACTTCATCGGCCCGGCGACAG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP053660_4

>merge|NZ_CP053660|4|1910475-1910573|CRISPRCasFinder
CCGGTTGGCCGCTGAAACTTCATCGGCCCGGCGACAGCTTCAGCGGCCGGCCGACAAAGCTGCCGGTTGGCCGCTGAAGCTTCATCGGCCCGGCGACAG

>NZ_CP053660|4|4|1910475-1910573|CRISPRCasFinder
CCGGTTGGCCGCTGAAACTTCATCGGCCCGGCGACAG	CTTCAGCGGCCGGCCGACAAAGCTG
CCGGTTGGCCGCTGAAGCTTCATCGGCCCGGCGACAG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP053660.1\|WP_154614510.1\|1921811_1922720_+\|NAD-dependent-epimerase/dehydratase-family-protein	unknown	unknown	gnl\|CDD\|223528
NZ_CP053660.1\|WP_171896599.1\|1912690_1913449_+\|class-I-SAM-dependent-methyltransferase	unknown	unknown	gnl\|CDD\|181382
NZ_CP053660.1\|WP_154614515.1\|1909124_1909904_+\|glucose-1-dehydrogenase	unknown	unknown	gnl\|CDD\|187600
NZ_CP053660.1\|WP_154614511.1\|1917417_1918557_+\|CDP-glycerol-glycerophosphotransferase-family-protein	unknown	unknown	gnl\|CDD\|224799
NZ_CP053660.1\|WP_154611811.1\|1904348_1905581_+\|MCE-family-protein	unknown	unknown	gnl\|CDD\|224380
NZ_CP053660.1\|WP_154614519.1\|1901957_1903127_+\|MCE-family-protein	unknown	unknown	gnl\|CDD\|273384
NZ_CP053660.1\|WP_154614512.1\|1915272_1917354_+\|acyl-CoA-dehydrogenase-family-protein	unknown	unknown	gnl\|CDD\|173841
NZ_CP053660.1\|WP_154611808.1\|1908005_1908200_+\|ferredoxin	unknown	unknown	gnl\|CDD\|224064
NZ_CP053660.1\|WP_154614603.1\|1907037_1908009_+\|FAD-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|223566
NZ_CP053660.1\|WP_154611800.1\|1918972_1920217_-\|alpha/beta-hydrolase-fold-domain-containing-protein	unknown	unknown	gnl\|CDD\|223730
NZ_CP053660.1\|WP_154614516.1\|1906122_1906878_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|313734
NZ_CP053660.1\|WP_154612157.1\|1914497_1915106_-\|class-I-SAM-dependent-methyltransferase	unknown	unknown	gnl\|CDD\|379276
NZ_CP053660.1\|WP_154614518.1\|1903123_1904335_+\|MCE-family-protein	unknown	unknown	gnl\|CDD\|273384
NZ_CP053660.1\|WP_171896598.1\|1911420_1912704_+\|glycosyltransferase-family-4-protein	unknown	unknown	gnl\|CDD\|340831
NZ_CP053660.1\|WP_154614513.1\|1913441_1914539_+\|prenyltransferase	unknown	unknown	gnl\|CDD\|273702
NZ_CP053660.1\|WP_154611807.1\|1908204_1909113_+\|3-oxoacyl-ACP-reductase	unknown	unknown	gnl\|CDD\|181120
NZ_CP053660.1\|WP_154614517.1\|1905577_1906126_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP053660.1\|WP_154611799.1\|1920327_1921755_+\|wax-ester/triacylglycerol-synthase-family-O-acyltransferase	unknown	unknown	gnl\|CDD\|274360
NZ_CP053660.1\|WP_154614514.1\|1909914_1910418_+\|TIGR03618-family-F420-dependent-PPOX-class-oxidoreductase	unknown	unknown	gnl\|CDD\|274679
NZ_CP053660.1\|WP_154611804.1\|1910600_1911203_-\|TetR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|380056

Protein	Function_ID	Function_description	E-value
NZ_CP053660.1\|WP_154614510.1\|1921811_1922720_+\|NAD-dependent-epimerase/dehydratase-family-protein	gnl\|CDD\|223528	COG0451, WcaG, Nucleoside-diphosphate-sugar epimerases [Cell envelope biogenesis, outer membrane / Carbohydrate transport and metabolism].	2.91032e-26
NZ_CP053660.1\|WP_171896599.1\|1912690_1913449_+\|class-I-SAM-dependent-methyltransferase	gnl\|CDD\|181382	PRK08317, PRK08317, hypothetical protein; Provisional.	1.55989e-23
NZ_CP053660.1\|WP_154614515.1\|1909124_1909904_+\|glucose-1-dehydrogenase	gnl\|CDD\|187600	cd05341, 3beta-17beta-HSD_like_SDR_c, 3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs. This subgroup includes members identified as 3beta17beta hydroxysteroid dehydrogenase, 20beta hydroxysteroid dehydrogenase, and R-alcohol dehydrogenase. These proteins exhibit the canonical active site tetrad and glycine rich NAD(P)-binding motif of the classical SDRs. 17beta-dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the SDR family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.	8.1098e-83
NZ_CP053660.1\|WP_154614511.1\|1917417_1918557_+\|CDP-glycerol-glycerophosphotransferase-family-protein	gnl\|CDD\|224799	COG1887, TagB, Putative glycosyl/glycerophosphate transferases involved in teichoic acid biosynthesis TagF/TagB/EpsJ/RodC [Cell envelope biogenesis, outer membrane].	6.15742e-09
NZ_CP053660.1\|WP_154611811.1\|1904348_1905581_+\|MCE-family-protein	gnl\|CDD\|224380	COG1463, Ttg2C, ABC-type transport system involved in resistance to organic solvents, periplasmic component [Secondary metabolites biosynthesis, transport, and catabolism].	1.22372e-47
NZ_CP053660.1\|WP_154614519.1\|1901957_1903127_+\|MCE-family-protein	gnl\|CDD\|273384	TIGR00996, Mtu_fam_mce, virulence factor Mce family protein. Members of this paralogous family are found as six tandem homologous proteins in the same orientation per cassette, in four separate cassettes in Mycobacterium tuberculosis. The six members of each cassette represent six subfamilies. One subfamily includes the protein mce (mycobacterial cell entry), a virulence protein required for invasion of non-phagocytic cells. [Cellular processes, Pathogenesis].	2.58651e-53
NZ_CP053660.1\|WP_154614512.1\|1915272_1917354_+\|acyl-CoA-dehydrogenase-family-protein	gnl\|CDD\|173841	cd01152, ACAD_fadE6_17_26, Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26. Putative acyl-CoA dehydrogenases (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position.	2.94006e-104
NZ_CP053660.1\|WP_154611808.1\|1908005_1908200_+\|ferredoxin	gnl\|CDD\|224064	COG1141, Fer, Ferredoxin [Energy production and conversion].	2.16211e-09
NZ_CP053660.1\|WP_154614603.1\|1907037_1908009_+\|FAD-dependent-oxidoreductase	gnl\|CDD\|223566	COG0492, TrxB, Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones].	3.12682e-61
NZ_CP053660.1\|WP_154611800.1\|1918972_1920217_-\|alpha/beta-hydrolase-fold-domain-containing-protein	gnl\|CDD\|223730	COG0657, Aes, Esterase/lipase [Lipid metabolism].	6.665e-35
NZ_CP053660.1\|WP_171896598.1\|1911420_1912704_+\|glycosyltransferase-family-4-protein	gnl\|CDD\|340831	cd03801, GT4_PimA-like, phosphatidyl-myo-inositol mannosyltransferase. This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.	1.4834e-58
NZ_CP053660.1\|WP_154612157.1\|1914497_1915106_-\|class-I-SAM-dependent-methyltransferase	gnl\|CDD\|379276	pfam13578, Methyltransf_24, Methyltransferase domain. This family appears to be a methyltransferase domain.	2.63808e-17
NZ_CP053660.1\|WP_154614518.1\|1903123_1904335_+\|MCE-family-protein	gnl\|CDD\|273384	TIGR00996, Mtu_fam_mce, virulence factor Mce family protein. Members of this paralogous family are found as six tandem homologous proteins in the same orientation per cassette, in four separate cassettes in Mycobacterium tuberculosis. The six members of each cassette represent six subfamilies. One subfamily includes the protein mce (mycobacterial cell entry), a virulence protein required for invasion of non-phagocytic cells. [Cellular processes, Pathogenesis].	2.93956e-53
NZ_CP053660.1\|WP_154614516.1\|1906122_1906878_+\|hypothetical-protein	gnl\|CDD\|313734	pfam10571, UPF0547, Uncharacterized protein family UPF0547. This domain contains a zinc-ribbon motif.	0.00216111
NZ_CP053660.1\|WP_154614513.1\|1913441_1914539_+\|prenyltransferase	gnl\|CDD\|273702	TIGR01577, Uncharacterized_glycosyl_hydrolase_MJ1610, oligosaccharide amylase. The name of this type of amylase is based on the characterization of an glucoamylase family enzyme from Thermoactinomyces vulgaris. The T. vulgaris enzyme was expressed in E. coli and, like other glucoamylases, it releases beta-D-glucose from starch. However, unlike previously characterized glucoamylases, this T. vulgaris amylase hydrolyzes maltooligosaccharides (maltotetraose, maltose) more efficiently than starch (1), indicating this enzyme belongs to a class of glucoamylase-type enzymes with oligosaccharide-metabolizing activity.	0.000329439
NZ_CP053660.1\|WP_154611807.1\|1908204_1909113_+\|3-oxoacyl-ACP-reductase	gnl\|CDD\|181120	PRK07792, fabG, 3-ketoacyl-(acyl-carrier-protein) reductase; Provisional.	3.18799e-144
NZ_CP053660.1\|WP_154611799.1\|1920327_1921755_+\|wax-ester/triacylglycerol-synthase-family-O-acyltransferase	gnl\|CDD\|274360	TIGR02946, Putative_diacyglycerol_O-acyltransferase_Mb3115, acyltransferase, WS/DGAT/MGAT. This bacteria-specific protein family includes a characterized, homodimeric, broad specificity acyltransferase from Acinetobacter sp. strain ADP1, active as wax ester synthase, as acyl coenzyme A:diacylglycerol acyltransferase, and as acyl-CoA:monoacylglycerol acyltransferase. [Unknown function, Enzymes of unknown specificity].	9.34733e-153
NZ_CP053660.1\|WP_154614514.1\|1909914_1910418_+\|TIGR03618-family-F420-dependent-PPOX-class-oxidoreductase	gnl\|CDD\|274679	TIGR03618, Rv1155_F420, PPOX class probable F420-dependent enzyme. A Genome Properties metabolic reconstruction for F420 biosynthesis shows that slightly over 10 percent of all prokaryotes with fully sequenced genomes, including about two thirds of the Actinomyces, make F420. The Partial Phylogenetic Profiling algorithm identifies this members of this protein family as high-scoring proteins to the F420 biosynthesis profile. A member of this family, Rv1155, was crytallized after expression in Escherichia coli, which does not synthesize F420; the crystal structure shown to resemble FMN-binding proteins, but with a recognizable empty cleft corresponding to, yet differing profounding from, the FMN site of pyridoxine 5'-phosphate oxidase. We propose that this protein family consists of F420-binding enzymes. [Unknown function, Enzymes of unknown specificity].	3.21357e-21
NZ_CP053660.1\|WP_154611804.1\|1910600_1911203_-\|TetR-family-transcriptional-regulator	gnl\|CDD\|380056	pfam17925, TetR_C_20, Tetracyclin repressor-like, C-terminal domain. TetR family regulators are involved in the transcriptional control of multidrug efflux pumps, pathways for the biosynthesis of antibiotics, response to osmotic stress and toxic chemicals, control of catabolic pathways, differentiation processes, and pathogenicity. The TetR proteins identified in overm ultiple genera of bacteria and archaea share a common helix-turn-helix (HTH) structure in their DNA-binding domain. However, TetR proteins can work in different ways: they can bind a target operator directly to exert their effect (e.g. TetR binds Tet(A) gene to repress it in the absence of tetracycline), or they can be involved in complex regulatory cascades in which the TetR protein can either be modulated by another regulator or TetR can trigger the cellular response. TetR regulates the expression of the membrane-associated tetracycline resistance protein, TetA, which exports the tetracycline antibiotic out of the cell before it can attach to the ribosomes and inhibit protein synthesis. TetR blocks transcription from the genes encoding both TetA and TetR in the absence of antibiotic. The C-terminal domain is multi-helical and is interlocked in the homodimer with the helix-turn-helix (HTH) DNA-binding domain. This entry represents the C-terminal domain present the transcriptional regulator KstR that regulates a large set of genes responsible for cholesterol catabolism. This is important for Mycobacterium tuberculosis during infection, both at an early stage in the macrophage phagosome and later within the necrotic granuloma.	3.89459e-30

>NZ_CP053660.1|WP_154614514.1|1909914_1910418_+|TIGR03618-family-F420-dependent-PPOX-class-oxidoreductase
MGMANQRSQVVMSPDEVDTFLTQQRSSTVATMGPNGQVHLVAMWYAWLDGHVWLETKAKSQKVVNLRRDPRMSFLVETGHTYDQLRGVSLEGNGVVVDDEKTVWDVCVNVFERYNAPYTEELRPFVELMAKNRVVVRLDVDRVRSWDHRKLGLDPLELGGSTAAFLD
>NZ_CP053660.1|WP_154614515.1|1909124_1909904_+|glucose-1-dehydrogenase
MGRLAGKVAIVTGAAMGQGAAISRAFVAEGAAVVLADIAKDAGQELADQLAGQVAGESGGRAHFAHHDVGDAASWASVVEDANARFGPVSVLANNAGLLRFGEIATMPQDEVELLFRVNQLGCFLGMQAVTATMRANGGGSIINASSVEGLAGMAGCAAYAATKWAIRGMTKCAAMELGPHGIRVNSVHPGMIDTPMTRVHGGDAAMEYGASKVPLRRVGTPADIAPLYVYLASEESAYVNGAEIAIDGGVTSTHAFGG
>NZ_CP053660.1|WP_154611807.1|1908204_1909113_+|3-oxoacyl-ACP-reductase
MTSSEDLSLDGRVAVVTGAGAGLGRAEALALAAAGAKVVLNDLPGAADEAVEEIRARGGEATVVEGDVAERSTADAMVAAAVDGFGSLDIVVNNAGMTRDRMLFNMSDEEWDAVIRVHLRGHFLLSRNAAAYWRGRSKEIDGPVYGRVVNTASEAFLGGSPGQPNYAAAKAGIAALTLSTARGLGRIGVRANAICPRARTAMTAGVFGEDTSGQEVDPYSPDHVAPLVAYLASPAAEAITGQVFVVYGGMVALVAAPVVEQRFDASGSVWDLEDLAKQVGGYFDGRDPAVGFAADSIMQLTV
>NZ_CP053660.1|WP_154611808.1|1908005_1908200_+|ferredoxin
MSTIKVDFDLCESNALCEAMAPEVFELDDDDYLLVKADETTPETEGDVRRAVAACPRAAISLEG
>NZ_CP053660.1|WP_154614603.1|1907037_1908009_+|FAD-dependent-oxidoreductase
MVEVDLVVVGAGPTGLFATYYAGFRGHRVAVVDSLPELGGQVTAMYPEKMILDVAGFPAVKGRDLVAGLVEQAATADPTYLLARTATTLEHHDDGVVVHLDDGTRVSAGAVLVTAGIGKFSPRALPAGEGWLGRGLEFFVPSFAPYAGKDVVIVGGGDSAFDWALHLEPVAGSVRLVHRRDAFRAHERTVQQVRDSSVEILTRAEVTALHGAGALESVEITVDGEPTTYPAQAVVAALGFLADLGPLQEWGIEVRKRHVVVDSAMRTNLPRVFAAGDITEYPGKVRLIAVGFGEAATAVNNATVAIDPTAHVFPGHSSEGNQS
>NZ_CP053660.1|WP_154614516.1|1906122_1906878_+|hypothetical-protein
MREPTVTQPDTQPDAHPDTKTCAYCAETIKAAAIRCRYCGSDLDPEPPVEQAVAEPPVEAARAEDVAAPPAIATSSTPGPRRWPAGVLAVVVVALAVVFVRMLTVDEPEGDVPAGTTPLAGGVVFASEGAKSAGLSAASEAAEKVLSYSAATLDEDMAAALPLLAPKMQTEYRETLEAIREDTVRNEAKVEASVVAASAISASEHDVKALLFVNQSTTGKNAEQPRADLNRVVVTLHRDAGDWVVTDLDAL
>NZ_CP053660.1|WP_154614517.1|1905577_1906126_+|hypothetical-protein
MRATVRSRWTLFTAVLAVLAVGLAAAIAVTALRSEDGRDALDRAVTGSAGRGDAELTAAHREVAEAARDLTLAFLEVDHADMEPLTEDVLALATGEFADQYAANVEQLIEAAKRNKSVSTGEVVALGVGDLDADSALVYVAADSEVQNVTTDGTSQPRYYRLQIDMVREDGQWLASNVQFVG
>NZ_CP053660.1|WP_154611811.1|1904348_1905581_+|MCE-family-protein
MTRGVKVRLALFVALAAVGIVYITGTYLGLVDRVLGRGLTISATLPDSGGLFVGSEVTYRGVKIGKVASMEVTREGLEAELALEEGTRIPLDARVEVHNLSAVGEQYLDIVPEDGRGPYAEDGDVLVGDDASLPIGEDELLVDLDALVASVDKGNLSTVIEELGLAFQDTAGPLEEMVDSGSRFVEAALANEEATFRLLDNGRTVLQTQQRHREDIRTFARSLADLTGTLRGKDPELRTVLEGGASAVREVERLMAGLEPTMPVFIGNLVTLNQIVTTRLPAVEQLLVTFPKIVANGFTGTPGDGYGHINLQLAQNPGPCREGFMPSDQWRPASDLADNETYPATCRSGAPYNQRGPKYAPRFGGSTSRVAPGATLADEPAVTVGSRGGLQEVFGDDAWRWMLIGPQEGM
>NZ_CP053660.1|WP_154614518.1|1903123_1904335_+|MCE-family-protein
MTRPRPRSRPRQRRALVGLASLAAAVPLLAACDFDGAYDLPLPGSPVSGEETFTVTAEFHDVLNVVPRSPVMVSDVVVGEVDEVDRDGWNAVVRLKIRSDIELPDNAVAEIRQTSLLGEKYVALEEPTGRARGRLEDGDRLELADTGRNPEVEEVLGALSFLLSGGGVGQIKQISDEVNDMLSGRTDDVRSLFGQLEELVGGLDEQKDDIVSAMESLNRLAATLNRESRTITDAIEATGPALEVLNQQHEQLVAMLGQLDELGEVGTRVINGTKENLLADLDHLRPILKRLNETGDSLPRGLSLLISFPFPEQASEIVKGDYANAKFALDVSLEGLTQLIEQPGDGPSIPLPDIPGLPDLPDIPLPDIPGLPTLPGLGRTATDGYTHDASVGTGGGLLAGGLG
>NZ_CP053660.1|WP_154614519.1|1901957_1903127_+|MCE-family-protein
MPRLTLRAAGALVAALLLVGTVLVLVGGDGGGQKKVTAHFARAVSIYPGTEVRILGVPVGEVTAVVPEGTSVRVDMVYDASYDVPADARAVIVTPTLVADRFVQLTPVHTEGPVLADGADIPLAETASPVELDRIYESLSTLANALGPNGANRNGSLDTLLASGAEALDGQGRTANQLIRDLSAAATTFGDNSGDLFGTVRQLDAFTRTLARNDGLVDEFMGDLARATNQLSGERQELGQALEALAGAVGTVEAFVKDNRKALVGEVEDLTDVLDVLVAEQESLTMAIEKGPLGLGNLALGFDTKTGSQNARIQVGPNVEDLDGFLCAIVTNAGVPAARTVCRLLESLLEPLGLGLPTGPARAAAPDTRVPGEAVPAQDLRELLGGGPR
>NZ_CP053660.1|WP_154611804.1|1910600_1911203_-|TetR-family-transcriptional-regulator
MSTINSLNVEDLGSAAQRDRRKRILDATIDLATKGGFDAVQMRAVADQAEVALGTLYRYFPSKIHLLVSALGREFERTEAARRDVEVPGDTASERVINVLKGTTRGLQSSPHLTEALTRAFMFADASVQAEIHQVGMLLTSMLTRAMHPEQPEPTDDDIAIARVIGDVWLSALVGWVTGRMTAAETGAQIERAVHLILRD
>NZ_CP053660.1|WP_171896598.1|1911420_1912704_+|glycosyltransferase-family-4-protein
MRIAMLSYRSAPHTGGQGIYLRHLTRELANLGHDVEVFSGQPYPELDHPDVRLTKVPSLDLYRQPDPFRVPKLHEFRDRIDVEEFLTMCAAGFPEPKTFSSRVARVLRDRVEDFDIVHDNQVLGYGMLDIEKMGLPLITTLHHPITFDRRIDIAQTRNPWRKFTLWRWYGFLRMQAKVARAARKILTPSEASKRDIAKDFGVDPARMQVILLGVEDGFKPPTKPRVPGRILAMASADAPMKGIATLLEAFAKLRTERDVELVLITKPRPGGTTEKLIDKYAIGDSVRFVSGVSDAELVDLMGSAEVACVPSLYEGFSLPTAELMACATPLVVSRAGAIPEVTGPDGEAADLVTPGDVGELTHALGALLDDPERRARMGAAGRRRVEEMFSWRAVAVKVAAAYEEVIEDYRRERAAGPSDERNHRAHR
>NZ_CP053660.1|WP_171896599.1|1912690_1913449_+|class-I-SAM-dependent-methyltransferase
MLTVDFDRLGLRPGDRVLDMGCGAGRHAFEMYRRGGDVIAFDMDADELANVRDLFVAMKEAGEVPEGAEADVKEGDALQLPFADGEFDRIVAAEVLEHIWADVDAIKEMVRVLRPGGTLAISVPRWLPEVVNWKLSSDYHNAEGGHIRIYTDHELIDKVTKAGRPNDGTPGDAMVFLGKDYAHGLHTPYWWIKCAVGVTNDEHPLAKAYHKLLVWEIMKQPTALKVAGKVLDPLIGKSMVLYFQKPAAGADV
>NZ_CP053660.1|WP_154614513.1|1913441_1914539_+|prenyltransferase
MSELLPYVEGVLSASQVAETAASIAAMQEASGAVPWTTGEHVDIWNHVEAAMAMLVGGQVEAAERAYAWVPTMQRADGSWPMKIVAGEVDDERGEVNMSAYFAVGLWHHWLVRRDLAFVERFWPSVRAGLDWVVGQQLPFGGIRWTPTEEGALLAGSSSIYQSLRAGVALADLLDDPQPEWELAGGRLGHAVREHRDLFLDKATYSMDWYYPVLGGAVRGDAAFALLETRWDDFVVPGLGIRCVDTNPWVTGAETCELVMALDAIGDHRRAMGLLADMQHLRAEDGKYWTGWVFGDDVNWPHEWTTYTAAAVVLAVDALGEVAGHASAGSGIMRGTSLAPHFSELALECGCASADELARSAGRPS
>NZ_CP053660.1|WP_154612157.1|1914497_1915106_-|class-I-SAM-dependent-methyltransferase
MPEDEGMLLHRVALERLAHGPALEVGTYCGKSAIYLGAAAREVGGPQAVVFTVDHHRGSEENQAGWEHHDASLVDPELGVMDTLPTFRRTLRLAGLEDQVVAVIGRSTTVSAHWRTPLSMLFIDGGHAEEHAQNDYAGWARWLEVGGLLVIHDVFQHPADGGQAPYHVFLRALASGAFEEVEALGSMRVLRRTAGAPGELVG
>NZ_CP053660.1|WP_154614512.1|1915272_1917354_+|acyl-CoA-dehydrogenase-family-protein
MSIGISDEHVELADSLRKWAASLDGPALVRAAEGEAAEPFAATWQAVTEMGVATIGLPEAAGGGGGSELDQAVALEACARELVPGPLLGPVVAQALLGETEVAAAIGGGAVVAIGLSDLVWDVPSATHVLAEVADGWRVLPVEAVTVTPGTGLDLSRRYGAVTVEDPAAGVAVPGLSRELLHRTAVTYAAAEAAGLARWCLDTAVEYAKVREQFGQKIGAFQAVKHLCAQMLETVEAITGAAWDVASAARPGTAGADDDQWAFAADVAAVTCFDGAVEVAKSCIQVLGGIGFTFEHDAHLYLRRAVALRSLLGSTDEAARRLTARAVGGTRRRLEVDLEGRDEAVRADVRARVEAIAARPEDERRAALVDAGYLMPHWPAPYGIGADAVTQLVIDTELARAGVTRPDIVIAGWALPTILEHGTDAQRERFVAPSLRGELVWCQLFSEPGSGSDLASLRTRAEKVEGGWRLTGQKVWTSVADRADWGICLARTDPDAPQHRGISYFLVDMRSAGIDVRPLREITGEALFNEVFLDEVFVPDDMLVAEPGDGWRLARTTLANERVAMAGSRLAKSTERAVELAAVGLTAAQEVRVGQAVALSTVCSLLGVRSTLRSLAGQGPGPESSVAKLLGVRNRQDASELVVSLHGDRALTDAEDVRADVWEMLNTRCLSIAGGTTQVLRNVAGERILGLPR
>NZ_CP053660.1|WP_154614511.1|1917417_1918557_+|CDP-glycerol-glycerophosphotransferase-family-protein
MHDAAILAYFADDTTRTYQLVQWLPVLELLQEQHPVAVVARDPAAAELLAAHTSLPVELAVSFPELTELYAAVDPKVVLYCNNSMLNFQSLLHGRALHVHINHGESDKQSMASNNAKAYDRVFVAGEAAVQRHVAGLLELDTSRLVRTGRPQLDLRLEPLLEPTDRRTVLYAPTWEGDAEYNDYTSVDTIGPDVVRAILAVPDVRLVYKPHPKVVTSTTPGVRDGHRAILALLDEAVRREPDAGHVAILLGDILAVMPDCDAMVTDVSSVGLDWLYLRTERPIFITDRHHDAERLRQEVPVSRCADVLDDVDVSALTELLTARLAHDEHHLARVAMRHHYFDDLAVGDSTVRFLDAVAELVARRDALLGESAPGAAITA
>NZ_CP053660.1|WP_154611800.1|1918972_1920217_-|alpha/beta-hydrolase-fold-domain-containing-protein
MSFLRRQIVTAALTANAIRPLPGFRPGIPAFMAGWLVGELAPHALALTVADAAAHARGPRRDVRGLALAAASTAGLSYLVWQARKVQHQAEDSLVEALGADYVEQLDAEPTPADLAVPWRRLVNPFRMRDARVRVEKNIAYDPAIGKRGLLDVYSPADGVPDGGAPVLIQVHGGGWTIGNKDQQGIPLMQHLAGKGWVCVAINYRLSPRAEWPAHVIDVKKAIAWVKANIAEHGGDPDYIAITGGSAGGHLVALAALTPGDAAYQPGFEDADTSVQVAVPHYGVYDFAGSTGTRAAEQLRDLFLAPRVLKTTFAADPQAFEDASPILRITPEAPDFFVLHGAYDTLVPVAQARAFVEKLRRISKRSVVYAELPGAQHAFDIFPSIRSSHVVRAIDRYLHWHWNQYRRERGRVAG
>NZ_CP053660.1|WP_154611799.1|1920327_1921755_+|wax-ester/triacylglycerol-synthase-family-O-acyltransferase
MFDRLSGLDASFLYLETPSQLMHVCGFILLDPSTMPEEYSFARLQATIDERVRDTPAFTRKLRRVPLGLDHPIWVRDKQFDIERHVHRLALPRPGGLAELTELAGHLAGLPLDRSRPLWEMWVIEGYDAGLGHDLVAVFMKMHHATVDGVSGANLVSHLCSLEPEAPPLGTADDQRYGRDADHLELLGRAVLSNVTKPLHAARLLTPSVRSVASTIGRARAGTAMAAPLTAPRTSFNGTITSHRTIALVDMELEQVREVKAATGTTVNDVVLTVAGGALRSYLADRGELPEDSLLATVPVSVHGTSQRSAGVNKVSALFAKLGTDEEDPLVRLEEMATRNKHAKEHHNAISADALQDWAEFAAPRTFGLAMRTYAGLRLAERHPVVHNLVISNVPGPPVPLYFCGAEVLGLYPLGPVFHGAGLNITVMSNHGHLHVGVIACRESVPHPEDLVQRFPVELDALRAAVARSGTSSVG
>NZ_CP053660.1|WP_154614510.1|1921811_1922720_+|NAD-dependent-epimerase/dehydratase-family-protein
MSEQAADAPVVVVTGANGFVGAATCAALVERGARVRGVVRRAGTAPSGVEERVGEFSDPGFAASVVDGASAVVTTVHPMAADRETQHRVGVEGTTTIARAARDAGVRRLVHVSTAAVYDRSPGADDVDESSALVGEDAGDYGVTKRDTDASLAAVEAITRVLVRPPAILGPGATSVWNTLRPGAIRENPAARRTAPDRSFAWVHVTDLATFLADVATGAVPDAEDPARGPVAGECTPVNLAAEPARARDYFGTVAEAVGVEPEWVEEPVWTGRIVADRARGWGWSPAVTLDAALTELAEGLR

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Crispr_ID: NZ_CP053660_5

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP053660_5

1987108-1987194

Orphan

Consensus_repeat	Method
TTCATCAAGGTATGCAGGCGAACCG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP053660_5

>merge|NZ_CP053660|5|1987108-1987194|CRISPRCasFinder
TTCATCAAGGTATGCAGGCGAACCGTCACATCCCTCGGTGAACTCACCCCGGGGAGTGATGGTTCATCAAGGTATGCAGGCGAACCG

>NZ_CP053660|5|5|1987108-1987194|CRISPRCasFinder
TTCATCAAGGTATGCAGGCGAACCG	TCACATCCCTCGGTGAACTCACCCCGGGGAGTGATGG
TTCATCAAGGTATGCAGGCGAACCG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP053660.1\|WP_154614445.1\|1993239_1994403_-\|thiolase-domain-containing-protein	unknown	unknown	gnl\|CDD\|181378
NZ_CP053660.1\|WP_154614593.1\|1989799_1990996_+\|cytochrome-P450	unknown	unknown	gnl\|CDD\|225035
NZ_CP053660.1\|WP_154614450.1\|1984587_1985346_-\|enoyl-CoA-hydratase-family-protein	unknown	unknown	gnl\|CDD\|181174
NZ_CP053660.1\|WP_171896617.1\|1987309_1988251_+\|type-IV-toxin-antitoxin-system-AbiEi-family-antitoxin-domain-containing-protein	unknown	unknown	gnl\|CDD\|379128
NZ_CP053660.1\|WP_154614442.1\|1996603_1997647_+\|LLM-class-F420-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|274647
NZ_CP053660.1\|WP_154614446.1\|1988447_1989611_-\|steroid-3-ketoacyl-CoA-thiolase	unknown	unknown	gnl\|CDD\|181145
NZ_CP053660.1\|WP_171896618.1\|1992314_1993124_-\|type-I-methionyl-aminopeptidase	unknown	unknown	gnl\|CDD\|238519
NZ_CP053660.1\|WP_154611749.1\|1981154_1981619_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP053660.1\|WP_154614454.1\|1978855_1979455_+\|TetR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|366102
NZ_CP053660.1\|WP_154614448.1\|1986202_1987084_+\|SDR-family-NAD(P)-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|236099
NZ_CP053660.1\|WP_154614449.1\|1985384_1986206_+\|SDR-family-oxidoreductase	unknown	unknown	gnl\|CDD\|236116
NZ_CP053660.1\|WP_154614441.1\|1997643_1999308_+\|AMP-binding-protein	unknown	unknown	gnl\|CDD\|235731
NZ_CP053660.1\|WP_154614452.1\|1980777_1981158_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP053660.1\|WP_171896616.1\|1982864_1983701_-\|CoA-transferase	unknown	unknown	gnl\|CDD\|224968
NZ_CP053660.1\|WP_154614592.1\|1991129_1992281_+\|cytochrome-P450	unknown	unknown	gnl\|CDD\|225035
NZ_CP053660.1\|WP_154614453.1\|1979447_1980611_+\|acetyl-CoA-C-acetyltransferase	unknown	unknown	gnl\|CDD\|181123
NZ_CP053660.1\|WP_171896615.1\|1981785_1982868_-\|nitronate-monooxygenase	unknown	unknown	gnl\|CDD\|367316
NZ_CP053660.1\|WP_154614443.1\|1995525_1996545_-\|OB-fold-domain-containing-protein	unknown	unknown	gnl\|CDD\|224462
NZ_CP053660.1\|WP_154614451.1\|1983697_1984591_-\|acyl-CoA--acetate/3-ketoacid-CoA-transferase-subunit-alpha	unknown	unknown	gnl\|CDD\|224702
NZ_CP053660.1\|WP_154614444.1\|1994402_1995455_-\|lipid-transfer-protein	unknown	unknown	gnl\|CDD\|181173

Protein	Function_ID	Function_description	E-value
NZ_CP053660.1\|WP_154614445.1\|1993239_1994403_-\|thiolase-domain-containing-protein	gnl\|CDD\|181378	PRK08313, PRK08313, thiolase domain-containing protein.	0
NZ_CP053660.1\|WP_154614593.1\|1989799_1990996_+\|cytochrome-P450	gnl\|CDD\|225035	COG2124, CypX, Cytochrome P450 [Secondary metabolites biosynthesis, transport, and catabolism].	6.2598e-89
NZ_CP053660.1\|WP_154614450.1\|1984587_1985346_-\|enoyl-CoA-hydratase-family-protein	gnl\|CDD\|181174	PRK07938, PRK07938, enoyl-CoA hydratase family protein.	3.59727e-156
NZ_CP053660.1\|WP_171896617.1\|1987309_1988251_+\|type-IV-toxin-antitoxin-system-AbiEi-family-antitoxin-domain-containing-protein	gnl\|CDD\|379128	pfam13338, AbiEi_4, Transcriptional regulator, AbiEi antitoxin. AbiEi_4 is the cognate antitoxin of the type IV toxin-antitoxin 'innate immunity' bacterial abortive infection (Abi) system that protects bacteria from the spread of a phage infection. The Abi system is activated upon infection with phage to abort the cell thus preventing the spread of phage through viral replication. There are some 20 or more Abis, and they are predominantly plasmid-encoded lactococcal systems. TA, toxin-antitoxin, systems on plasmids function by killing cells that lose the plasmid upon division. AbiE phage resistance systems function as novel Type IV TAs and are widespread in bacteria and archaea. The cognate antitoxin is pfam13338.	2.20471e-07
NZ_CP053660.1\|WP_154614442.1\|1996603_1997647_+\|LLM-class-F420-dependent-oxidoreductase	gnl\|CDD\|274647	TIGR03559, F420_Rv3520c, probable F420-dependent oxidoreductase, Rv3520c family. Members of this protein family are predicted to be oxidoreductases dependent on coenzyme F420. The family includes a single member in Mycobacterium tuberculosis (Rv3520c/MT3621) but four in Mycobacterium smegmatis. Prediction that this family is F420-dependent is based primarily on Partial Phylogenetic Profiling vs. F420 biosynthesis. [Unknown function, Enzymes of unknown specificity].	1.53982e-173
NZ_CP053660.1\|WP_154614451.1\|1983697_1984591_-\|acyl-CoA--acetate/3-ketoacid-CoA-transferase-subunit-alpha	gnl\|CDD\|224702	COG1788, AtoD, Acyl CoA:acetate/3-ketoacid CoA transferase, alpha subunit [Lipid metabolism].	6.10886e-62
NZ_CP053660.1\|WP_154614453.1\|1979447_1980611_+\|acetyl-CoA-C-acetyltransferase	gnl\|CDD\|181123	PRK07801, PRK07801, acetyl-CoA C-acetyltransferase.	0
NZ_CP053660.1\|WP_154614454.1\|1978855_1979455_+\|TetR-family-transcriptional-regulator	gnl\|CDD\|366102	pfam00440, TetR_N, Bacterial regulatory proteins, tetR family.	3.11972e-14
NZ_CP053660.1\|WP_154614448.1\|1986202_1987084_+\|SDR-family-NAD(P)-dependent-oxidoreductase	gnl\|CDD\|236099	PRK07791, PRK07791, short chain dehydrogenase; Provisional.	6.87394e-141
NZ_CP053660.1\|WP_154614449.1\|1985384_1986206_+\|SDR-family-oxidoreductase	gnl\|CDD\|236116	PRK07856, PRK07856, SDR family oxidoreductase.	1.1184e-134
NZ_CP053660.1\|WP_154614441.1\|1997643_1999308_+\|AMP-binding-protein	gnl\|CDD\|235731	PRK06188, PRK06188, acyl-CoA synthetase; Validated.	0
NZ_CP053660.1\|WP_171896616.1\|1982864_1983701_-\|CoA-transferase	gnl\|CDD\|224968	COG2057, AtoA, Acyl CoA:acetate/3-ketoacid CoA transferase, beta subunit [Lipid metabolism].	2.23308e-25
NZ_CP053660.1\|WP_154614592.1\|1991129_1992281_+\|cytochrome-P450	gnl\|CDD\|225035	COG2124, CypX, Cytochrome P450 [Secondary metabolites biosynthesis, transport, and catabolism].	7.04253e-89
NZ_CP053660.1\|WP_171896618.1\|1992314_1993124_-\|type-I-methionyl-aminopeptidase	gnl\|CDD\|238519	cd01086, MetAP1, Methionine Aminopeptidase 1. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and Peptidase M. Catalyzes release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.	3.39626e-110
NZ_CP053660.1\|WP_171896615.1\|1981785_1982868_-\|nitronate-monooxygenase	gnl\|CDD\|367316	pfam03060, NMO, Nitronate monooxygenase. Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane dioxygenase (NPD) (EC:1.13.11.32), is an FMN-dependent enzyme that uses molecular oxygen to oxidize (anionic) alkyl nitronates and, in the case of the enzyme from Neurospora crassa, (neutral) nitroalkanes to the corresponding carbonyl compounds and nitrite. Previously classified as 2-nitropropane dioxygenase, but it is now recognized that this was the result of the slow ionization of nitroalkanes to their nitronate (anionic) forms. The enzymes from the fungus Neurospora crassa and the yeast Williopsis saturnus var. mrakii (formerly classified as Hansenula mrakii) contain non-covalently bound FMN as the cofactor. Active towards linear alkyl nitronates of lengths between 2 and 6 carbon atoms and, with lower activity, towards propyl-2-nitronate. The enzyme from N. crassa can also utilize neutral nitroalkanes, but with lower activity. One atom of oxygen is incorporated into the carbonyl group of the aldehyde product. The reaction appears to involve the formation of an enzyme-bound nitronate radical and an a-peroxynitroethane species, which then decomposes, either in the active site of the enzyme or after release, to acetaldehyde and nitrite.	9.34476e-79
NZ_CP053660.1\|WP_154614443.1\|1995525_1996545_-\|OB-fold-domain-containing-protein	gnl\|CDD\|224462	COG1545, COG1545, Predicted nucleic-acid-binding protein containing a Zn-ribbon [General function prediction only].	3.22766e-40
NZ_CP053660.1\|WP_154614446.1\|1988447_1989611_-\|steroid-3-ketoacyl-CoA-thiolase	gnl\|CDD\|181145	PRK07850, PRK07850, steroid 3-ketoacyl-CoA thiolase.	0
NZ_CP053660.1\|WP_154614444.1\|1994402_1995455_-\|lipid-transfer-protein	gnl\|CDD\|181173	PRK07937, PRK07937, lipid-transfer protein; Provisional.	0

>NZ_CP053660.1|WP_154614448.1|1986202_1987084_+|SDR-family-NAD(P)-dependent-oxidoreductase
MSTLLDGRVAIVTGAGRGIGRAHALELARHGASVVVNDYGVSLSGEGTGETPAESVVAEIEAMGGQAVANAADVADFAAAEAMVHQAVEVFGGLDILVNNAGFVRDRMLVNTSEEEWDAVIRVHLKGHFAPLRHAGAYWRAEAKAGRTRAARVVNTSSGAGLQGSIGQATYSAAKAGIAGLTLVAAAELGRYGVTVNAIAPVARTRMTEGAFDTSAMPEPEDNSPLVAWLASEDAGDVTGRVIEIEGGTITLENAWAHGPSRDNGTRWSATDLGPVVRDLIASAPAPEPVYGA
>NZ_CP053660.1|WP_154614449.1|1985384_1986206_+|SDR-family-oxidoreductase
MSLALDLSGRVALVTGGTQGIGLGITRSFLAAGATVVTCSRSAVEPLAGTTHHVCDVRDAEAVTGLVDAVVAAHGRLDVLVNNAGGAPYALASEASPRFHDKVVGLNLMAPLVAAQAANRVMQGQPGGGAIVNVSSVSATRPSPGTAAYGAAKAGLDSLTRSLAVEWAPRVRVNSIDVGLCRTEHTDDHYGGDAGVAAIERTIPLGRMARPEEVGHVAVFLASDLASYVSGARLECHGGGEPPVFLSALTSPAPSTPSTPSTPSTPSTQEQNR
>NZ_CP053660.1|WP_154614450.1|1984587_1985346_-|enoyl-CoA-hydratase-family-protein
MPITSELRADGIRVVTMDHPPVNALTVQGWFDVAAALDEAGRDQATHVVVLRAEGRGFNAGVDIKEMQHSSGFGALIGANKGCYAAFKAVYECAVPVVAAVNGFCLGGGVGLVGNADCVIASDDAYFGVPEVNQGALGAATHMARLVPQHMMRTLYFTARTIPAKDLVQFGSVLEVVPRAELDDAAMALAAEIAAKDTRVVRAAKEALNGIDPIDVNKSYRFEQGFTFELNLAGVSDELRDDFAGTEKAATR
>NZ_CP053660.1|WP_154614451.1|1983697_1984591_-|acyl-CoA--acetate/3-ketoacid-CoA-transferase-subunit-alpha
MTKGPRDKRMSIDEVVGELRDGMTIGIGGWGPRRKPMALVRAILRSDLKDLTIVSWGGADVGLLARAGKIRKLVFAFVSLDSVPLEPNFQRARQDGTIPELVELDEGMFQTGLSAAAQRLPFLPMRAGLGSDVLVNQPWISTVTSPYAAADGTHEELVAVPALHLDVALVHLNRADKHGNATYLGPDPYFDDLFCMAADRAFVSCEQVVDTAGLTVDTPVQRLLLSRMLVDGVVETPNGAHFTTCTPDYERDERFQRAYAAAAGGSAEDWTAFEQRFLSGDEDAYQAAVAAFTEEGK
>NZ_CP053660.1|WP_171896616.1|1982864_1983701_-|CoA-transferase
MSSTGSTGSTGSTGSTGTTRADLCAAAIADAFRDDGEIFASPMGLLPMLGVRLAKLTSNPDLVISDGESLFLAGVPPLFAKADVVEGWIPFRKVFDVVAHGPRHVMMGATQVDRHGNQNISAIGDWARPKRQLLGSRGAPGNTVNNRTSYWVPKHSPRVFVEAVDIVTGVGPKRAMEAGPAAARYNDIHRIVTNLAVLDVKGAGDTVRLLSVHPGVDVEAVREATGFELEVPAEVPTTREPTAEELVIIREVLDPKGLRFKEVPQEAPQERSQKVAGR
>NZ_CP053660.1|WP_171896615.1|1981785_1982868_-|nitronate-monooxygenase
MIEQLLRTPLTDLTGVRHPVVQTGMGWVSGPRLVSGTANAGGLGILASATMTFAELEAAIVEVKGRTDQPFGVNLRADAADAPDRCRLLVEHGVKVASFALAPKPELIAMLKENGVVVMPSIGAAKHAVKVASWGADAVMVQGGEGGGHTGPVPTTLLLPSVLDALRGAGSEIPVVAAGGFFDGRGLAAALSYGAAGVGMGTRFLLTSDSAVPDAVKRLYLERGLTDTVVTAKVDGMPHRMLRTDLVAELEETGTLRRLAPTARRTLEFKRDSGMGWLALARDGRSMRRAQGRTLGQMALAANTPTMLKAGLVEGDTSAGVLASGQVVGLIDDLPSCEDLIDRIVTGAAAELRRAASYVG
>NZ_CP053660.1|WP_154611749.1|1981154_1981619_-|hypothetical-protein
MDRAVLLWMVPVNLLLVAWVWIGRMLFGVGGWMVLVYLISIVPVLLLALLVTSVLALTQRPGPDGRRALTRPQTQAQLFVWAAMLVFGAFSFDFGDVEDSDTALLVKVLGDHEAVWAATMTIMVVAALTTVVAWIALVATLTGARRRAAVPSEA
>NZ_CP053660.1|WP_154614452.1|1980777_1981158_-|hypothetical-protein
MSAPTPPPRRARHLLDPDNPSAPRPTRARARSRSTQKSMSIDTVQRYVLSVLAATTILHMSVGLVLAGLIIDDEHRVSQVGLCVLGGAFGVLAVAAALAIHRKNALSPWLLLGTIPGIVGVWLVLT
>NZ_CP053660.1|WP_154614453.1|1979447_1980611_+|acetyl-CoA-C-acetyltransferase
MPEAFIVDAVRTPTGKRGGALAAMHSADLAAHSITALVDRTGVDPGAVDDVILGCCDTIGSQAGDVARTAWLAAGLPDHVPGVTIDRQCGSSQQAVHFAAQAVMSGTQDLVVAGGVQNMSAIPISAAMLVGQQYGFSTPFAESPGWQKRFGDQEVSQFRSAEMIAEKWGHTREQLEAYALASHERALTAIAEGRFDREVVPVPLADGSVFATDQCPRQTSLEKMASLQPLAPGGRITAAVASQICDASSAVLIASEQAVADHGLTPRARVHHLSVRGDDPVWMLTGPIRATRHALERSGLSVDDIDLFECNEAFAPVVLAWMEEIGVPHEKVNVNGGGIALGHPIGATGTRLMTTLLHELERTGGRYGLQTMCEGGGQANVTIIERL
>NZ_CP053660.1|WP_154614454.1|1978855_1979455_+|TetR-family-transcriptional-regulator
MSAQTRTEGTDRRRELLSIAAELFADKGFKNTTVRDIADAAGILSGSLYHHFDSKESMVDEILSSFQAELFAAYDEVLRSDDDARTKIERAVRLSFEAIDRRRHEVAIFQNEADFLGQQERFAYLAERNAESRAVWITLLDDGVRSGALRADLDIELTYRFIRDTVWVAVRWYRPGGKLSHTAVADQYLTILLDGIAHA
>NZ_CP053660.1|WP_171896617.1|1987309_1988251_+|type-IV-toxin-antitoxin-system-AbiEi-family-antitoxin-domain-containing-protein
MDPLRVLAEEIGFFTRAQARDAGYADRDVTRAVRQGLWRRIRRGYYTFGDLWRIADPVDQHRIRSRAVIDSLGDRVALSHVSGVIEHGVDVWGLDLSRVHVTRLDGGPGRIEGDVVHHEGFCGAGEVVERDGRRVLPPERCVVEAGSRTDNERALVMMDSLLHRGLVEHGELFAQFELMARWPFVQHLHLAVRMADGRAESVGESRGRYLFWSHGLPVPQLQYAVRDSKGAVVATSDWGWPEHGLLGEFDGQLKYGRLLRPGQDAGSVVFAEKQREDLAREVSGMGMVRLVWSDYDRPALTVARVRRALRLSG
>NZ_CP053660.1|WP_154614446.1|1988447_1989611_-|steroid-3-ketoacyl-CoA-thiolase
MGTPVIIDAVRTPLGKRKGWLAGVHPAVLLGFAQREVLARAGLDPELVEQVVGGCVTQAGEQSNDMVRRAWLHAGLPQHTGATAIDAQCGSGQQSAHLVHDMVAAGTIDVGIACGVESMSRIPLGSNVPPGLGDPRPDDWTIDMPNQFEAADRIARNRGLSRSDLDAFGLASQQKARVAVDEGRFKREIAPIEAPVLDEDGSPTGETRLVERDQGLRDTTSEGLASLRTVLPDGLHTAGTSSQISDGASAVLIMDEDKARSLGLTPRARIVTHCLVGSDPYYHLDGPIEATSRALSRAGMSISDLDLFEINEAFASVALSWAGQHSVDMDRVNVNGGAIALGHPVGSTGTRLITTALHELERRDAATALVSMCAGGAMATGTILERV
>NZ_CP053660.1|WP_154614593.1|1989799_1990996_+|cytochrome-P450
MAERLPHEELLALRRTSPVSWIAQDEAARAGFPDHEGYWALSRHADVAAVSKDQVNFSTRENGVIIRFAPEMTREEVEQTGFLLINHDAPDHTKLRQIVSRAFTPRAINALHDGLKARAEQIVDDAVAKGEGNFVEDVAAELPLQAIAELLGVPQADRGKLFEWSNQMLSYDDPEVEGDQMTAFMEILAYSMALADERRTNPQDDILTRLVTADVKVGTEEGRGLTDDEFGFFMILLAVAGNETTRNAITWGMHAFLQNPDQWELYKRERPATAVDEIIRWATPVTVFQRTAINDVEIGGQAIAKGDRVGLLYASANFDEDVFEDPFRFDIMRDHNPHQAFGGHGAHYCIGANLARLEVDLIFRALADRGVDLTQLSEPRKLRSSWINGVKELRVAYR
>NZ_CP053660.1|WP_154614592.1|1991129_1992281_+|cytochrome-P450
MRQAGPLTWVEQAPGTYDGMAPESGNGYWAVTRHADVSTVSKNSKDWSNAENGAIIRFSEGMLREQVEMQRVIMLNQDAPEHPTTRQIVSRAFTPRSINELEDLMRQRAETIVRGAVERGTGDFVEEVAAELPLQAIADLIGVPQEDRFKLFDWSNQMLASDDPDYPGDPDVAAAEILGYAMTMAAERQANPRDDLITRLLNAHKGERGLTDDEFGYFVILLAVAGNETTRNAISHGMNAFLDNPDQWELWKAERPATMIDEVVRWGTPVTVFQRTAVRDVEIGGVTVTRGQRVGLFYASANFDEDVFADPFRFDITRDPNPQLGFGGHGAHYCLGANLARQEIRVIFDALADHAPDIAKEREPRRLRHSWINGLKDLPVRYA
>NZ_CP053660.1|WP_171896618.1|1992314_1993124_-|type-I-methionyl-aminopeptidase
MIELRTPAQIEEMRAAGRFVADVVTALAEAADVGVNLLELDALAHQMIRERGAESCYIDYHPSFGASPFGKVLCTSVNDAVLHGLPRDYVLQDGDLLSVDFAASVDGWVSDSAYSLVVGTARPEDLALINTTQRALEAGISAAQPGAKVGDISHAIASVAREAGLRINTQFGGHGVGRTMHGDPHIPNDGRPGRGFTLKPGLVIAIEPWFLHTTDEIFTDADGWTIRSLDGSRGAHMEHTIAITADGPLVLTAREREPVLKGGLAPAQA
>NZ_CP053660.1|WP_154614445.1|1993239_1994403_-|thiolase-domain-containing-protein
MAKQPAAIVGVGQTHHRAKREDVSMAGLCREAIDRALEDANLSLDDIDAIVVGKAPDLFEGVMMPELFLAESLGAAGKPLLRVHTAGSVGGSTAIVAASLVQAGVHQRVLTVAYEKQSESNAMWALSVPVPFNMPVHAGAGGYFAPHVRSYIRRSNAPTHVGAVVAAKDRQNALKNPYAHLRNPDTTVESVLASQMLWDPIRYDETCPSSDGACAMVIVDEDTAAASPNPAWIHGTVMRSEATTAAERDQVNPQAGRDAAAYLWKQAGITDPLREIDAAEIYVPFSWFEPMWLENLGFTAEGEGWKLTESGGTAMDGTLPVNCSGGVLSSNPIGASGMLRFGEAALQVRGAAGEHQVDGARRALGHAYGGGSQFFAMWVVGADKPTS
>NZ_CP053660.1|WP_154614444.1|1994402_1995455_-|lipid-transfer-protein
MREVAVVGFAQRQMEEFDGSPTCVELLVPLFAECYEQTGWTRRDIGFWCSGSSDYLAGRSFSFVQAVDAIGVIPPVNESHVEMDAAWALYEAWLKIQTGEVDTALVYGFGKSSAGVLRRTLALQLDPYTMTPLWPDTVSLAGLQARAGIDAGLWDERAMAEVVNRSLTDAEKNEYAVRKGGSSVEELLARPVYADPLRKHDCAPVTDGAAAIVLAADDRAREVCDRPAWITGLSHYVDPISMGTRDLTRSPSAARAGAGVDLGGVEVAELHAPFSHQELVLRRELGLPADVAVNPSGGALAGNPMFTGGLIRFGEAARKVWQGEATKVLGHATSGPALQQNIVCTMEGRN
>NZ_CP053660.1|WP_154614443.1|1995525_1996545_-|OB-fold-domain-containing-protein
MSRTLSAPVTVAFDYTRSTGPVLGRFLTGLRDQRVVGGRTSEGRVVVPPPEFDPVTHRQLDDFVEVADTGTVTSWTWVPEPVAGQPLDRPFAFVLVTLDGADAPLVHALDVTSPDQVRTGMRVRIRWAPERVGAITDIACFEPVVELDEVEIGAGGPDRARPQPRDEAATEQSRSGDGPAAVTTVITPVELDYLYAASPEESAFYRALAEGRIIGQRCPTCGKVYVPPRSACPADGTPTTDEVELSQTGTVTTFCVVNVPFLGQRIKPPYVSAYVLLDGADIAFLHLILDIPAEEVRMGMRVEAVWKPREEWGTTIENISHFRPTGEPDADFDTYKQHL
>NZ_CP053660.1|WP_154614442.1|1996603_1997647_+|LLM-class-F420-dependent-oxidoreductase
MKLGLQLGYWGAQPPTGVAELVAAAEDAGFDAVFTAEAWGSDAFTPLAWWGRETTRLRLGTSIVQMSGRTPTSIAMHALTLDHLSGGRVVLGMGVSGPQVVEGWYGQPFAKPLARTREVVDIIRQVLAREAPVTNDGPHHPMPYAGPGATGLGKPLKPIVHPLRADIPIWLGAEGPKNVAQTAEIADGWIPIFYTPRSAGMYQPWLDEGFARPGARRTRADFEIAATCHLEIVEDAAGKQAVIDAMKPFVALYMGGMGAKDQNFHKQVFERMGHAALADEVQELYLAGEKDRATALIPDDLVDDMHIIGTAGEVRERVAQWEETGVTTLLLSCRSADEVRRVAEVLA
>NZ_CP053660.1|WP_154614441.1|1997643_1999308_+|AMP-binding-protein
MSAPTIDAPATEDLLRLGTHNGHLMVAALKKHRTKPVMMLSPSSGEGFAETLVGGQVADRISQYVQAFEALGAGRGTAGALLALNRPEVLFVLGAGQTQGYRRTSLHPLGSLEDHAYVINDAEITTLVIDPNPMFVERALGLLERCPELTTVLTLGPVPEALASTRAEVADLTAKAAEFDPRPLEAVPLPHDHVVSITYTGGTTGKPKGVIGTARQMNTMTQIQMSEWEWPESPRFLMCTPLSHAGAAFFVPTVLKGGCLYVLAKFDPAEVLRTIEEQRITATMLVPSMLYALMDHPDSRTRDLSSLETVYYGASAINPVRLREAIDRFGPIFAQYYGQSEAPMVISYLGKEDHVSGGDRRLSSCGRPSAFLRAALLGEDGQPVPPGEPGEICVAGPLLAGGYWKLPEPTAETFRDGWMHTGDVAREDEDGFWYIVDRTKDMIVTGGFNVFPREVEDVVAEHPAVAQVGVIGTPHEKFGEAVTAIVVLREDAPRDEESVARMTAEIQEMVKERKGSVQSPKQVVVADALPLTALGKPDKKALRAQYWTGDRAVG

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Crispr_ID: NZ_CP053660_6

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP053660_6

2065305-2065390

Orphan

Consensus_repeat	Method
AACTTCATCGTCCCGGCGCCAGTT	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP053660_6

>merge|NZ_CP053660|6|2065305-2065390|CRISPRCasFinder
AACTTCATCGTCCCGGCGCCAGTTTCATCGGCCGGCCGATGAACCTCCCGGTTGGCCGATAAAACTTCAGCGTCCCGGCGCCAGTT

>NZ_CP053660|6|6|2065305-2065390|CRISPRCasFinder
AACTTCATCGTCCCGGCGCCAGTT	TCATCGGCCGGCCGATGAACCTCCCGGTTGGCCGATAA
AACTTCAGCGTCCCGGCGCCAGTT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP053660.1\|WP_171896641.1\|2063546_2064185_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|376278
NZ_CP053660.1\|WP_171896643.1\|2072514_2073510_+\|GTP-3',8-cyclase-MoaA	unknown	unknown	gnl\|CDD\|234672
NZ_CP053660.1\|WP_154614412.1\|2068160_2068964_+\|enoyl-CoA-hydratase/isomerase-family-protein	unknown	unknown	gnl\|CDD\|119339
NZ_CP053660.1\|WP_171896640.1\|2062989_2063550_+\|ASCH-domain-containing-protein	unknown	unknown	gnl\|CDD\|119345
NZ_CP053660.1\|WP_154614410.1\|2070862_2071621_+\|SDR-family-oxidoreductase	unknown	unknown	gnl\|CDD\|187602
NZ_CP053660.1\|WP_154611705.1\|2057101_2058520_+\|Fe-S-cluster-assembly-protein-SufB	unknown	unknown	gnl\|CDD\|131035
NZ_CP053660.1\|WP_154611692.1\|2074181_2074394_+\|dodecin-domain-containing-protein	unknown	unknown	gnl\|CDD\|377810
NZ_CP053660.1\|WP_154611694.1\|2073513_2073726_-\|acetone-carboxylase	unknown	unknown	unknown
NZ_CP053660.1\|WP_154611702.1\|2062152_2062602_+\|SUF-system-NifU-family-Fe-S-cluster-assembly-protein	unknown	unknown	gnl\|CDD\|273918
NZ_CP053660.1\|WP_154611698.1\|2066459_2068058_+\|ATP-binding-cassette-domain-containing-protein	unknown	unknown	gnl\|CDD\|223562
NZ_CP053660.1\|WP_154614411.1\|2068974_2070849_+\|ATP-binding-cassette-domain-containing-protein	unknown	unknown	gnl\|CDD\|224055
NZ_CP053660.1\|WP_154611703.1\|2060124_2060886_+\|Fe-S-cluster-assembly-ATPase-SufC	unknown	unknown	gnl\|CDD\|223473
NZ_CP053660.1\|WP_154614414.1\|2064338_2065244_+\|phosphotransferase	unknown	unknown	gnl\|CDD\|366736
NZ_CP053660.1\|WP_154611701.1\|2062598_2062982_+\|DUF59-domain-containing-protein	unknown	unknown	gnl\|CDD\|225062
NZ_CP053660.1\|WP_154611693.1\|2073780_2074122_-\|DUF3099-domain-containing-protein	unknown	unknown	gnl\|CDD\|378630
NZ_CP053660.1\|WP_154614415.1\|2060882_2062148_+\|SufS-family-cysteine-desulfurase	unknown	unknown	gnl\|CDD\|131034
NZ_CP053660.1\|WP_171896642.1\|2071506_2072427_-\|SURF1-family-protein	unknown	unknown	gnl\|CDD\|119401
NZ_CP053660.1\|WP_154614413.1\|2065436_2066393_-\|neutral-zinc-metallopeptidase	unknown	unknown	gnl\|CDD\|225203
NZ_CP053660.1\|WP_171896638.1\|2058569_2059784_+\|Fe-S-cluster-assembly-protein-SufD	unknown	unknown	gnl\|CDD\|376550
NZ_CP053660.1\|WP_171896639.1\|2059780_2060128_+\|non-heme-iron-oxygenase-ferredoxin-subunit	unknown	unknown	gnl\|CDD\|239604

Protein	Function_ID	Function_description	E-value
NZ_CP053660.1\|WP_171896641.1\|2063546_2064185_+\|hypothetical-protein	gnl\|CDD\|376278	pfam18859, acVLRF1, Actinobacteria/chloroflexi VLRF1 release factor. Archaeo-eukaryotic release factor domain family belonging to the VLRF1 clade, observed primarily in the actinbacteria and chloroflexi bacterial lineages. Contains a conserved glutamine residue in the release factor catalytic loop, suggesting it functions as an active peptidyl-tRNA hydrolase at the ribosome.	1.26356e-40
NZ_CP053660.1\|WP_171896643.1\|2072514_2073510_+\|GTP-3',8-cyclase-MoaA	gnl\|CDD\|234672	PRK00164, moaA, GTP 3',8-cyclase MoaA.	0
NZ_CP053660.1\|WP_154614412.1\|2068160_2068964_+\|enoyl-CoA-hydratase/isomerase-family-protein	gnl\|CDD\|119339	cd06558, crotonase-like, Crotonase/Enoyl-Coenzyme A (CoA) hydratase superfamily. This superfamily contains a diverse set of enzymes including enoyl-CoA hydratase, napthoate synthase, methylmalonyl-CoA decarboxylase, 3-hydoxybutyryl-CoA dehydratase, and dienoyl-CoA isomerase. Many of these play important roles in fatty acid metabolism. In addition to a conserved structural core and the formation of trimers (or dimers of trimers), a common feature in this superfamily is the stabilization of an enolate anion intermediate derived from an acyl-CoA substrate. This is accomplished by two conserved backbone NH groups in active sites that form an oxyanion hole.	6.05881e-51
NZ_CP053660.1\|WP_171896640.1\|2062989_2063550_+\|ASCH-domain-containing-protein	gnl\|CDD\|119345	cd06553, ASCH_Ef3133_like, ASC-1 homology domain, subfamily similar to Enterococcus faecalis Ef3133. The ASCH domain, a small beta-barrel domain found in all three kingdoms of life, resembles the RNA-binding PUA domain and may also interact with RNA. ASCH has been proposed to function as an RNA-binding domain during coactivation, RNA-processing and the regulation of prokaryotic translation.	3.11693e-58
NZ_CP053660.1\|WP_154614410.1\|2070862_2071621_+\|SDR-family-oxidoreductase	gnl\|CDD\|187602	cd05344, BKR_like_SDR_like, putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR. This subgroup resembles the SDR family, but does not have a perfect match to the NAD-binding motif or the catalytic tetrad characteristic of the SDRs. It includes the SDRs, Q9HYA2 from Pseudomonas aeruginosa PAO1 and APE0912 from Aeropyrum pernix K1. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.	1.63495e-66
NZ_CP053660.1\|WP_154611705.1\|2057101_2058520_+\|Fe-S-cluster-assembly-protein-SufB	gnl\|CDD\|131035	TIGR01980, UPF0051_protein_slr0074, FeS assembly protein SufB. This protein, SufB, forms a cytosolic complex SufBCD. This complex enhances the cysteine desulfurase of SufSE. The system, together with SufA, is believed to act in iron-sulfur cluster formation during oxidative stress. Note that SufC belongs to the family of ABC transporter ATP binding proteins, so this protein, encoded by an adjacent gene, has often been annotated as a transporter component. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other].	0
NZ_CP053660.1\|WP_154611692.1\|2074181_2074394_+\|dodecin-domain-containing-protein	gnl\|CDD\|377810	pfam07311, Dodecin, Dodecin. Dodecin is a flavin-binding protein,found in several bacteria and few archaea and represents a stand-alone version of the SHS2 domain. It most closely resembles the SHS2 domains of FtsA and Rpb7p, and represents a single domain small-molecule binding form.	1.12973e-29
NZ_CP053660.1\|WP_154611702.1\|2062152_2062602_+\|SUF-system-NifU-family-Fe-S-cluster-assembly-protein	gnl\|CDD\|273918	TIGR01994, Iron-sulfur_cluster_assembly_scaffold_protein_IscU, SUF system FeS assembly protein, NifU family. Three iron-sulfur cluster assembly systems are known so far. ISC is broadly distributed while NIF tends to be associated with nitrogenase in nitrogen-fixing bacteria. The most recently described is SUF, believed to be important to maintain the function during aerobic stress of enzymes with labile Fe-S clusters. It is fairly widely distributed. This family represents one of two different proteins proposed to act as a scaffold on which the Fe-S cluster is built and from which it is transferred. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other].	6.18917e-63
NZ_CP053660.1\|WP_154611698.1\|2066459_2068058_+\|ATP-binding-cassette-domain-containing-protein	gnl\|CDD\|223562	COG0488, Uup, ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only].	8.50931e-177
NZ_CP053660.1\|WP_154614411.1\|2068974_2070849_+\|ATP-binding-cassette-domain-containing-protein	gnl\|CDD\|224055	COG1132, MdlB, ABC-type multidrug transport system, ATPase and permease components [Defense mechanisms].	1.25844e-162
NZ_CP053660.1\|WP_154611703.1\|2060124_2060886_+\|Fe-S-cluster-assembly-ATPase-SufC	gnl\|CDD\|223473	COG0396, sufC, Cysteine desulfurase activator ATPase [Posttranslational modification, protein turnover, chaperones].	3.6908e-137
NZ_CP053660.1\|WP_154614414.1\|2064338_2065244_+\|phosphotransferase	gnl\|CDD\|366736	pfam01636, APH, Phosphotransferase enzyme family. This family consists of bacterial antibiotic resistance proteins, which confer resistance to various aminoglycosides they include: aminoglycoside 3'-phosphotransferase or kanamycin kinase / neomycin-kanamycin phosphotransferase and streptomycin 3''-kinase or streptomycin 3''-phosphotransferase. The aminoglycoside phosphotransferases inactivate aminoglycoside antibiotics via phosphorylation. This family also includes homoserine kinase. This family is related to fructosamine kinase pfam03881.	0.00347119
NZ_CP053660.1\|WP_154611701.1\|2062598_2062982_+\|DUF59-domain-containing-protein	gnl\|CDD\|225062	COG2151, PaaD, Predicted metal-sulfur cluster biosynthetic enzyme [General function prediction only].	6.15412e-33
NZ_CP053660.1\|WP_154611693.1\|2073780_2074122_-\|DUF3099-domain-containing-protein	gnl\|CDD\|378630	pfam11298, DUF3099, Protein of unknown function (DUF3099). Some members in this family of proteins are annotated as membrane proteins however this cannot be confirmed. Currently no function is known.	4.21888e-20
NZ_CP053660.1\|WP_154614415.1\|2060882_2062148_+\|SufS-family-cysteine-desulfurase	gnl\|CDD\|131034	TIGR01979, Probable_cysteine_desulfurase, cysteine desulfurases, SufSfamily. This model represents a subfamily of NifS-related cysteine desulfurases involved in FeS cluster formation needed for nitrogen fixation among other vital functions. Many cysteine desulfurases are also active as selenocysteine lyase and/or cysteine sulfinate desulfinase. This subfamily is associated with the six-gene SUF system described in E. coli and Erwinia as an FeS cluster formation system during oxidative stress. The active site Cys is this subfamily resembles GHHC with one or both His conserved. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other].	0
NZ_CP053660.1\|WP_171896642.1\|2071506_2072427_-\|SURF1-family-protein	gnl\|CDD\|119401	cd06662, SURF1, SURF1 superfamily. Surf1/Shy1 has been implicated in the posttranslational steps of the biogenesis of the mitochondrially-encoded Cox1 subunit of cytochrome c oxidase (complex IV). Cytochrome c oxidase (complex IV), the terminal electron-transferring complex of the respiratory chain, is an assemblage of nuclear and mitochondrially-encoded subunits. Its assembly is mediated by nuclear encoded assembly factors, one of which is Surf1/Shy1. Mutations in human Surf1 are a major cause of Leigh syndrome, a severe neurodegenerative disorder.	1.27858e-39
NZ_CP053660.1\|WP_154614413.1\|2065436_2066393_-\|neutral-zinc-metallopeptidase	gnl\|CDD\|225203	COG2321, COG2321, Predicted metalloprotease [General function prediction only].	5.56138e-83
NZ_CP053660.1\|WP_171896638.1\|2058569_2059784_+\|Fe-S-cluster-assembly-protein-SufD	gnl\|CDD\|376550	pfam01458, UPF0051, Uncharacterized protein family (UPF0051).	2.47723e-79
NZ_CP053660.1\|WP_171896639.1\|2059780_2060128_+\|non-heme-iron-oxygenase-ferredoxin-subunit	gnl\|CDD\|239604	cd03528, Rieske_RO_ferredoxin, Rieske non-heme iron oxygenase (RO) family, Rieske ferredoxin component; composed of the Rieske ferredoxin component of some three-component RO systems including biphenyl dioxygenase (BPDO) and carbazole 1,9a-dioxygenase (CARDO). The RO family comprise a large class of aromatic ring-hydroxylating dioxygenases found predominantly in microorganisms. These enzymes enable microorganisms to tolerate and even exclusively utilize aromatic compounds for growth. ROs consist of two or three components: reductase, oxygenase, and ferredoxin (in some cases) components. The ferredoxin component contains either a plant-type or Rieske-type [2Fe-2S] cluster. The Rieske ferredoxin component in this family carries an electron from the RO reductase component to the terminal RO oxygenase component. BPDO degrades biphenyls and polychlorinated biphenyls. BPDO ferredoxin (BphF) has structural features consistent with a minimal and perhaps archetypical Rieske protein in that the insertions that give other Rieske proteins unique structural features are missing. CARDO catalyzes dihydroxylation at the C1 and C9a positions of carbazole. Rieske ferredoxins are found as subunits of membrane oxidase complexes, cis-dihydrodiol-forming aromatic dioxygenases, bacterial assimilatory nitrite reductases, and arsenite oxidase. Rieske ferredoxins are also found as soluble electron carriers in bacterial dioxygenase and monooxygenase complexes.	6.5438e-42

>NZ_CP053660.1|WP_154614414.1|2064338_2065244_+|phosphotransferase
MWQPEPGWLAVPGGRGASTVGVWRTVLGDQPVVVKRLARPLPGDPVELSDPHHPAYWRRAADVLVERLVVATPGLRAEPQAAAEEDTEGITLTQAWVEDAANSGLFVARCLGRFAGAALAAPALARDQLRSRMLRVEHRGGWPTLARTTVADVADHLWRRRTTLLAELDALPQVAQHGDPTPANLPGREGDDVLAIDWGTLGHGPVGADLGYYSLLAREELDPLVDAYLLGLPDGLATADQVRHAARVTAVLTALNGAEWALARAAGGEGALAGKFRHPAVAPHLRALQRQAPHVEALLGR
>NZ_CP053660.1|WP_171896641.1|2063546_2064185_+|hypothetical-protein
MSPGAAGSRPSVVLVPAQRWPRWVLNFQGRHGATALEVTSGDLFGAAADGSTFAASLPFAERYAGLPDAEAFAAACAAPEDWGVLLVRKGGFAMARVAGRTVVDSKVGQRHVQGRTKAGGQSQQRFARRRDNQARAAYEAAAGHAARILHGLSGPLVTGGDRAAVEEVLAGPPLDRLTVVGPWLAVPDPRRAVLDAAVLDACAVQVAVHNAS
>NZ_CP053660.1|WP_171896640.1|2062989_2063550_+|ASCH-domain-containing-protein
MTDTASDPASDPANVLASDLASDPEVETFWVLARRQAKLERLPAYFGPSGLVSLPPPAWSFGATPEQADELAGLVLDGVKTATASAAEDYALEGEPLPEPGTLGIVLDGGGHPRALVATTEVRVVAFEEVDEAHAHAEGEGDRTLATWRARHEAFFRDVDPHGRGFRPDMPVVLERFKVLHPKPGR
>NZ_CP053660.1|WP_154611701.1|2062598_2062982_+|DUF59-domain-containing-protein
MTELDHSDLPEVPEATGAPAPAGSSTVSPEEVTEAMKDVVDPELGINVVDLGLVYDVHVDEGSNVVLDMTLTSAACPLTDVIQDQTNAALEGLVNDVAINWVWMPPWGPDKITEDGREQLRALGFNV
>NZ_CP053660.1|WP_154611702.1|2062152_2062602_+|SUF-system-NifU-family-Fe-S-cluster-assembly-protein
MNAELDSLYQEIILDHYKNPHHAGLREPYEAEVHHVNPTCGDEVTLRVHIADGTVADVSYDAVGCSISQASASVMTDLVIGKPVDEAMSVHEEFLTLMQGKGTVEPDEDVLEDGIAFAGVAKFPARVKCALLSWMAWKDATARSLEETR
>NZ_CP053660.1|WP_154614415.1|2060882_2062148_+|SufS-family-cysteine-desulfurase
MIVLPGLLPELEVIRKDFPILERTLAGGVPLVYLDSANTSQKPQCVIDAMVDHLERHNANVARAMHQLGAESSEAFENARDVVARFIGAPSRDEVVFTKNASEALNLVANTLAWATGDLAIGAGDEVVITEMEHHSNIVPWQMLTERKGATLRWFGLTETGELDLSEIDSLITERTKVVSLTWVSNMLGTINPVAEIARRAHEVGAIVVVDASQAAPQLPVDVTEVDADVLVFTGHKVVGPTGIGVLWGKRSLLEQLPPFLGGGEMIETVRMERSTYAGIPHKFEAGTPPIVEAVGLGAALDYLAAVGMENIHRHEQAITGYALEGLATIPGLRVLGPLDATRRGGAIAFEMDGVHPHDIAQVLDSRGIAVRAGHHCAKPAHARFGVQSTTRMSSYLYTTPAEIDALVEGLEHTRAYFKVG
>NZ_CP053660.1|WP_154611703.1|2060124_2060886_+|Fe-S-cluster-assembly-ATPase-SufC
MSELVIKDLQVSVDTEDGPKEILKGVTLTIGSGETHAIMGPNGSGKSTLAYSIAGHPKYTITGGSVTLDGEDVLTMSVDERARAGLFLAMQYPVEVPGVSVSNFLRTAKTAIDGEAPKLRTWVKDVNGALQRLNLDPTFGTRSVNEGFSGGEKKRHEIAQLELLNPKVAILDETDSGLDIDALKVVSEGVNRFREQEGKGVLLITHYTRILRYIKPDFVHVFVAGKVAASGGPELADELEAEGYDKYLKAAAV
>NZ_CP053660.1|WP_171896639.1|2059780_2060128_+|non-heme-iron-oxygenase-ferredoxin-subunit
MTFERACWLSDVPDDEALGVTVGAYDVAIARNGDEVFALQDLCSHAAVSLSEGEVADCAVECWLHGSRFDLRTGKPTGLPATEPVATFPVEVRESPDGPSVYVDTTTTLNGVTPS
>NZ_CP053660.1|WP_171896638.1|2058569_2059784_+|Fe-S-cluster-assembly-protein-SufD
MTVTDTDPAIARDSVASALEQDRVESHLNPPPSYDLADHPLPTGREEVWRFTPLKRLRGILDGEASATKLRREVSLPEGVTLTEITAEQARELGELAPNDRPSALAVANAGGAVLLDVPADLELETTDPVVVTLTGENADDLVWGHVVVRLGRHSKATIVLRHTGSARYAATTTVVVGDGAELNMVSLQDWDDDAVHLGRDAIRVGRDASVKHTSVSFGGDVVRMHANVEYDGPGGHAELLGLYFADAGQHLEHRLFADHNQPRTKSNVAYKGALQGKGARTVWIGNVLIRKVAEGIETYEENRNLVLTDGCQADSVPNLEIETGEIEGAGHASATARFDDEQLFYLRSRGVSDAEARRLVLHGFFNDLIRKVGIPSLEEQLTATVEAELAKNVLDGLPPVGSS
>NZ_CP053660.1|WP_154611705.1|2057101_2058520_+|Fe-S-cluster-assembly-protein-SufB
MTSIEELNPELKGIGRYEFGWADPDTAGATAKRGLNEDVVRDISSKKSEPQWMLDLRLKGLKLFGRKPMPTWGSDLGGIDFDNIKYFVRSSEKQAATWDDLPEDIKNTYDKLGIPEAEKQRLVSGVAAQYESEVVYHSIREDLEAQGVLFLDTDTALKEQPELFKEYFGTVIPVGDNKFSALNTAVWSGGSFIYVPKGVHVDIPLQAYFRINTENMGQFERTLIIADEDSYVHYVEGCTAPIYSSDSLHSAVVEIIVKKGARVRYTTIQNWSNNVYNLVTKRATCEAGATMEWVDGNIGSKVTMKYPAVYLMGEHAKGETLSIAFAGEGQHQDAGAKMVHAAPNTSSSILSKSVARGGGRTSYRGLIQVNEGAHGSKSNVLCDALLVDQISRSDTYPYVDIREDDVSMGHEASVSKVSDDQLFYLMSRGMEEDEAMAMIVRGFVEPIAKELPMEYALELNRLIELQMEGAVG
>NZ_CP053660.1|WP_154614413.1|2065436_2066393_-|neutral-zinc-metallopeptidase
MRFNPKARLDTGRVRDRGRGSGGGFGRGGRGGGLGGARMPVPGGMRTGGGIGGVIVLVLLFVLVQCVGGGVPGLGGGGGAAYDTGRFADTDRYENCRTGEDANDDVDCARVAVENSLHDFWSDELGNRFRPVEQLATFSGSTQTGCGGASSAVGPFYCPPDSSIYLDTTFFEEVLDRQLGGPSGGFVEPYVLAHEYGHHIQNLLGTMGRVRTQQGPTSDAVRLELQADCYAGMWARAATSTEDADGNVLISELTRQDVEEAVAAAEAVGDDRIQQKTQGQVTEESWTHGSAAMRVRWFETGYDTGSLEACDTFAADRL
>NZ_CP053660.1|WP_154611698.1|2066459_2068058_+|ATP-binding-cassette-domain-containing-protein
MITATQLEVRAGARLLMENVSFRVAPGDKIGLVGRNGAGKTTLTKILAGEGQPAAGTVTTTSEVGYLPQDPRTGDPEVLARDRILSARGLDDVVRRLRDAETGMGSDDPNVRDKAMRRYERADAELHAGGGYAAESEAAVIAHSLGIEDRILAQPLKTLSGGQRRRVELARILFSGAEILILDEPTNHLDADSIVWLRDFLKAHRGGFIVISHDNGLLEETVNKVLHLDANRGEIDVYNMGWKDYLVQRETDERRRKRERANAETKAKTLTDQANRMRAKASKASAAQSMLKRAEKMMAGLEGERQADKVARIVFPKPAACGKTPLTATGLSKSYGSLEVFTDVDLAIDKGSRVVILGLNGAGKTTMLRILAGVDQADTGEVVPGHGLKVGYYAQEHETLDTDRTVLENMQSAAPQLTDTEARSVLGSFLFSGEDAHKPAKVLSGGEKTRLALASLVVSSANVLLLDEPTNNLDPASREEVLAAIRSYEGAIVLVTHDEGAVRALEPDRVLLLPDGDEDLWNEGYADLVSLA
>NZ_CP053660.1|WP_154614412.1|2068160_2068964_+|enoyl-CoA-hydratase/isomerase-family-protein
MTTPSPETLAAAGLQLDLTGPVATITLDRPDVRNAQTPAMWRALADLGEALPGDVRVVVVRGNGAAFSAGLDRRLLDPSSVGGEEESVAGLVMLSDEELSATIDAYQRGFTFLRDPRFVSVAAVHGYAIGAGFQLALACDLRVLSTDAQLSMKEAALGLVPDLTGTKPLVDSVGYARALEICATARMVGADEAVRIGLALAAVPTEELDSTVADLVQALVAPLPGAVREIKELLQGAQERDLETQRRLEREAQVRRFREMAALAGGR
>NZ_CP053660.1|WP_154614411.1|2068974_2070849_+|ATP-binding-cassette-domain-containing-protein
MSGMYGAGAAWRHLRSDRSVVDNRITGATLRRVLGFARPHRRTIAVFLVLTVIDAAMVVVTPLLVQRVVDDGILKNDARLVTVLALAMAGVAVLNALLAVLGGWLSSKIGEGLIYDLRTQVFGHVQRQSLAFFTRTQTGALVSRLNNDVIGAQRAFTSTLSSTVSNTIAVLVVGIAMFALSWQVTLLCLAMFPILFGVSRFVSSKLAGLTRRQMDGNADLGNVMTERFNVGGAMLLKLFGRRGEEDALFADKAANVRDLGVRISLITRIFGAAMMLVPALATALVYGVGGHLAIDGTLTVGTLLALATLLLRLLGPLQGLSNVRIDVMTALVSFERVFEVLDLPSLVREKPGAVALPPTASRLEFDHVSFSYPRADDVSLASLETVARTESRDNGPVLHDISFVADAGQMIALVGPSGAGKTTVTHLVARLYDVNGGAVRVGGHDVRDVTLQSLEDTVGYVTQDAHMFHDTIRANLLYARPGASDEEIWQALEAAQVSTLVRALPDGLDTVVGDRGYRLSGGERQRLAIARLLLKAPSIVVLDEATAHLDSGSEVAVQRALDAAHAGRTSLVIAHRLSTVRNADQILVVQDGRIVQSGTHTQLLAQGGLYADLYRTQLVEDVPA
>NZ_CP053660.1|WP_154614410.1|2070862_2071621_+|SDR-family-oxidoreductase
MDLQLTDRVLLVTGGARGLGRATAEVLVAEGARVVLSGRSEDSLAAARAELGPDRVATVVADNADPATPGRLLAAAHDAFGRLDGALVSVGGPPAGTVLEASDEQWRDAFDSVFLGAVRICRTVVEALPAGGSLALVLSSSVRSPLAGLAVSNGLRPGLAMVAKTLADEVGPRGVRVNGLLPGRVATDRVAELDALADDPAAERARAEAAIPLRRYGRPEEFGRAAAFLLSPAASFVSGVMLPVDGGALRAL
>NZ_CP053660.1|WP_171896642.1|2071506_2072427_-|SURF1-family-protein
MRRFRILLSRRWAFFALAIVGVAWATWWLGNWQFDRLEDRRSSNAVVERNENLEPAPVAEVLSPGGDVAEDDEWRVVTATGEYAVEDTVIVRYRTRDGEAGIEVVVPLITADGTALVVDRGWMPTDNRGGDAEGVPDPPSGEVTITGYVRADGTGDSTRVVDGSTRAVSSEEIGEAIGRPTYGGFVDLRSEDPEPAETLTPRDLPEQNDGPHFFYGLQWWFFGVLAIFGFLYLAYDELKRGPHGQRGSRRPPRPKADPRTGKRPPREPAQSARSAPPSTGSITPETNDAAGESRNAAARPNSSGRP
>NZ_CP053660.1|WP_171896643.1|2072514_2073510_+|GTP-3',8-cyclase-MoaA
MTRPLQDRYGRVATDLRVSLTDRCNLRCNYCMPAEGLDWLPDDSVLSDDEVVRLIGIGVSHLGVREVRFTGGEPLVRRGLVGIVERTRALGPDLELSITTNALGLARTADKLAAAGLDRVNVSLDSVRAETFHAITRRDRLPDVVAGLEAAQAAGLGPVKVNAVLLRGTNDDQAGELLAWCLERGYELRFIEQMPLDAQHGWSRTGMITAEEIFERLSRDFELSPAVEPRGSAPAELFRVDGGPGTVGVIASVTRPFCGDCDRVRLTADGQVRNCLFAREESDLRAALRGGATDEEIADRWVVAMLGKRAGHGIDDPTFLQPDRPMSAIGG
>NZ_CP053660.1|WP_154611694.1|2073513_2073726_-|acetone-carboxylase
MDPDTCSAKGCTAPAAWQLQWNNPKLHTPDRRKVWLACGDHRSSLSDFLTARGFLKDVVPHEAGASQGRE
>NZ_CP053660.1|WP_154611693.1|2073780_2074122_-|DUF3099-domain-containing-protein
MARDQRRDRDDAVRITTAASSHNADIAARQRRYLLSMSIRSICFVGAVVAALAGIQWLWPFLIAGAILLPYVAVVLANVQATRKEGFALQDAAYGAPELPAAPSDPEVGHSAR
>NZ_CP053660.1|WP_154611692.1|2074181_2074394_+|dodecin-domain-containing-protein
MTNRTYRVTEIVGTSPDGIDEAIRNGVERAARTLRHLDWFEVTQVRGQVKDGTVEHFQVGIKVGFRLEDD

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Crispr_ID: NZ_CP053660_7

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP053660_7

3663274-3663350

Orphan

Consensus_repeat	Method
GGGCGCCTCCTGCTCGACCAGCAG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP053660_7

>merge|NZ_CP053660|7|3663274-3663350|CRISPRCasFinder
GGGCGCCTCCTGCTCGACCAGCAGCGGGCCCGCAGGCCGAAGATCGCCTCACGGGGCGCCTCCTGCGCGACCAGCAG

>NZ_CP053660|7|7|3663274-3663350|CRISPRCasFinder
GGGCGCCTCCTGCTCGACCAGCAG	CGGGCCCGCAGGCCGAAGATCGCCTCACG
GGGCGCCTCCTGCGCGACCAGCAG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP053660.1\|WP_171896984.1\|3666321_3667200_+\|branched-chain-amino-acid-ABC-transporter-permease	unknown	unknown	gnl\|CDD\|119324
NZ_CP053660.1\|WP_154615554.1\|3668367_3669714_+\|ABC-transporter-substrate-binding-protein	unknown	unknown	gnl\|CDD\|380566
NZ_CP053660.1\|WP_154615564.1\|3660984_3661437_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP053660.1\|WP_154615560.1\|3663379_3664609_-\|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|225306
NZ_CP053660.1\|WP_154615575.1\|3652372_3653677_+\|trypsin-like-peptidase-domain-containing-protein	unknown	unknown	gnl\|CDD\|273938
NZ_CP053660.1\|WP_154615552.1\|3670026_3670632_-\|methyltransferase	unknown	unknown	gnl\|CDD\|368316
NZ_CP053660.1\|WP_171896981.1\|3657910_3658792_+\|inositol-phosphorylceramide-synthase	unknown	unknown	gnl\|CDD\|239481
NZ_CP053660.1\|WP_171896979.1\|3654787_3656485_-\|ABC-F-family-ATP-binding-cassette-domain-containing-protein	unknown	unknown	gnl\|CDD\|223562
NZ_CP053660.1\|WP_171896982.1\|3660026_3660983_+\|alpha/beta-hydrolase	unknown	unknown	gnl\|CDD\|369561
NZ_CP053660.1\|WP_154615550.1\|3670628_3671510_-\|tRNA-pseudouridine(38-40)-synthase-TruA	unknown	unknown	gnl\|CDD\|234577
NZ_CP053660.1\|WP_154615558.1\|3665604_3666309_+\|ATP-binding-cassette-domain-containing-protein	unknown	unknown	gnl\|CDD\|223487
NZ_CP053660.1\|WP_171896985.1\|3671487_3673143_+\|FAD-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|273540
NZ_CP053660.1\|WP_154615573.1\|3653744_3654791_-\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|366181
NZ_CP053660.1\|WP_171896983.1\|3664783_3665605_+\|ABC-transporter-ATP-binding-protein	unknown	unknown	gnl\|CDD\|213186
NZ_CP053660.1\|WP_154615546.1\|3673172_3674102_-\|carbohydrate-kinase	unknown	unknown	gnl\|CDD\|238572
NZ_CP053660.1\|WP_171896980.1\|3656569_3657739_+\|dienelactone-hydrolase-family-protein	unknown	unknown	gnl\|CDD\|335313
NZ_CP053660.1\|WP_154615562.1\|3661738_3663061_-\|HNH-endonuclease	unknown	unknown	gnl\|CDD\|238038
NZ_CP053660.1\|WP_154615556.1\|3667201_3668371_+\|branched-chain-amino-acid-ABC-transporter-permease	unknown	unknown	gnl\|CDD\|119323
NZ_CP053660.1\|WP_154615566.1\|3658841_3659993_+\|acyl-CoA-dehydrogenase-family-protein	unknown	unknown	gnl\|CDD\|173847
NZ_CP053660.1\|WP_154615578.1\|3650654_3652268_-\|long-chain-fatty-acid--CoA-ligase	unknown	unknown	gnl\|CDD\|235730

Protein	Function_ID	Function_description	E-value
NZ_CP053660.1\|WP_171896984.1\|3666321_3667200_+\|branched-chain-amino-acid-ABC-transporter-permease	gnl\|CDD\|119324	cd06582, TM_PBP1_LivH_like, Transmembrane subunit (TM) of Escherichia coli LivH and related proteins. LivH is one of two TMs of the E. coli LIV-1/LS transporter, a Periplasmic Binding Protein (PBP)-dependent ATP-Binding Cassette (ABC) transporter involved in the uptake of branched-chain amino acids (AAs). These types of transporters generally bind type 1 PBPs. PBP-dependent ABC transporters consist of a PBP, two TMs, and two cytoplasmic ABCs, and are mainly involved in importing solutes from the environment. The solute is captured by the PBP, which delivers it to a gated translocation pathway formed by the two TMs. The two ABCs bind and hydrolyze ATP and drive the transport reaction. E. coli LivH forms a heterodimer with another TM, LivM, to generate the transmembrane pore. LivM is not included in this subgroup. The LIV-1/LS transporter is comprised of two TMs (LivM and LivH), two ABCs (LivG and LivF), and one of two alternative PBPs, LivJ (LIV-BP) or LivK (LS-BP). In addition to transporting branched-chain AAs including leucine, isoleucine and valine, the E. coli LIV-1/LS transporter is involved in the uptake of the aromatic AA, phenylalanine.	2.39791e-52
NZ_CP053660.1\|WP_154615554.1\|3668367_3669714_+\|ABC-transporter-substrate-binding-protein	gnl\|CDD\|380566	cd06343, PBP1_ABC_ligand_binding-like, type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems predicted to be involved in uptake of amino acids, peptides, or inorganic ions. This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems that are predicted to be involved in uptake of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however its ligand specificity has not been determined experimentally.	3.65602e-122
NZ_CP053660.1\|WP_154615560.1\|3663379_3664609_-\|helix-turn-helix-domain-containing-protein	gnl\|CDD\|225306	COG2508, COG2508, Regulator of polyketide synthase expression [Signal transduction mechanisms / Secondary metabolites biosynthesis, transport, and catabolism].	1.86685e-20
NZ_CP053660.1\|WP_154615575.1\|3652372_3653677_+\|trypsin-like-peptidase-domain-containing-protein	gnl\|CDD\|273938	TIGR02037, Probable_periplasmic_serine_protease_do/HhoA-like, periplasmic serine protease, Do/DeqQ family. This family consists of a set proteins various designated DegP, heat shock protein HtrA, and protease DO. The ortholog in Pseudomonas aeruginosa is designated MucD and is found in an operon that controls mucoid phenotype. This family also includes the DegQ (HhoA) paralog in E. coli which can rescue a DegP mutant, but not the smaller DegS paralog, which cannot. Members of this family are located in the periplasm and have separable functions as both protease and chaperone. Members have a trypsin domain and two copies of a PDZ domain. This protein protects bacteria from thermal and other stresses and may be important for the survival of bacterial pathogens.// The chaperone function is dominant at low temperatures, whereas the proteolytic activity is turned on at elevated temperatures. [Protein fate, Protein folding and stabilization, Protein fate, Degradation of proteins, peptides, and glycopeptides].	7.84089e-88
NZ_CP053660.1\|WP_154615552.1\|3670026_3670632_-\|methyltransferase	gnl\|CDD\|368316	pfam05175, MTS, Methyltransferase small domain. This domain is found in ribosomal RNA small subunit methyltransferase C as well as other methyltransferases.	9.5101e-37
NZ_CP053660.1\|WP_171896981.1\|3657910_3658792_+\|inositol-phosphorylceramide-synthase	gnl\|CDD\|239481	cd03386, PAP2_Aur1_like, PAP2_like proteins, Aur1_like subfamily. Yeast Aur1p or Ipc1p is necessary for the addition of inositol phosphate to ceramide, an essential step in yeast sphingolipid synthesis, and is the target of several antifungal compounds such as aureobasidin.	1.91727e-24
NZ_CP053660.1\|WP_171896979.1\|3654787_3656485_-\|ABC-F-family-ATP-binding-cassette-domain-containing-protein	gnl\|CDD\|223562	COG0488, Uup, ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only].	2.3168e-95
NZ_CP053660.1\|WP_171896982.1\|3660026_3660983_+\|alpha/beta-hydrolase	gnl\|CDD\|369561	pfam07859, Abhydrolase_3, alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes.	3.59489e-86
NZ_CP053660.1\|WP_154615550.1\|3670628_3671510_-\|tRNA-pseudouridine(38-40)-synthase-TruA	gnl\|CDD\|234577	PRK00021, truA, tRNA pseudouridine(38-40) synthase TruA.	9.18042e-106
NZ_CP053660.1\|WP_154615558.1\|3665604_3666309_+\|ATP-binding-cassette-domain-containing-protein	gnl\|CDD\|223487	COG0410, LivF, ABC-type branched-chain amino acid transport systems, ATPase component [Amino acid transport and metabolism].	9.57756e-106
NZ_CP053660.1\|WP_171896985.1\|3671487_3673143_+\|FAD-dependent-oxidoreductase	gnl\|CDD\|273540	TIGR01292, Thioredoxin_reductase, thioredoxin-disulfide reductase. This model describes thioredoxin-disulfide reductase, a member of the pyridine nucleotide-disulphide oxidoreductases (pfam00070). [Energy metabolism, Electron transport].	1.17408e-63
NZ_CP053660.1\|WP_154615573.1\|3653744_3654791_-\|GNAT-family-N-acetyltransferase	gnl\|CDD\|366181	pfam00583, Acetyltransf_1, Acetyltransferase (GNAT) family. This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.	0.000430494
NZ_CP053660.1\|WP_171896983.1\|3664783_3665605_+\|ABC-transporter-ATP-binding-protein	gnl\|CDD\|213186	cd03219, ABC_Mj1267_LivG_branched, ATP-binding cassette component of branched chain amino acids transport system. The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).	7.14951e-98
NZ_CP053660.1\|WP_154615546.1\|3673172_3674102_-\|carbohydrate-kinase	gnl\|CDD\|238572	cd01167, bac_FRK, Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for fructose, as are all FRKs, but they catalyzes the conversion of fructose to fructose-6-phosphate, which is an entry point into glycolysis via conversion into glucose-6-phosphate. This is in contrast to FRKs [or ketohexokinases (KHKs)] from mammalia and halophilic archaebacteria, which phosphorylate fructose to fructose-1-phosphate.	1.06568e-59
NZ_CP053660.1\|WP_171896980.1\|3656569_3657739_+\|dienelactone-hydrolase-family-protein	gnl\|CDD\|335313	pfam03403, PAF-AH_p_II, Platelet-activating factor acetylhydrolase, isoform II. Platelet-activating factor acetylhydrolase (PAF-AH) is a subfamily of phospholipases A2, responsible for inactivation of platelet-activating factor through cleavage of an acetyl group. Three known PAF-AHs are the brain heterotrimeric PAF-AH Ib, whose catalytic beta and gamma subunits are aligned in pfam02266, the extracellular, plasma PAF-AH (pPAF-AH), and the intracellular PAF-AH isoform II (PAF-AH II). This family aligns pPAF-AH and PAF-AH II, whose similarity was previously noted.	1.8606e-11
NZ_CP053660.1\|WP_154615562.1\|3661738_3663061_-\|HNH-endonuclease	gnl\|CDD\|238038	cd00085, HNHc, HNH nucleases; HNH endonuclease signature which is found in viral, prokaryotic, and eukaryotic proteins. The alignment includes members of the large group of homing endonucleases, yeast intron 1 protein, MutS, as well as bacterial colicins, pyocins, and anaredoxins.	2.32808e-09
NZ_CP053660.1\|WP_154615556.1\|3667201_3668371_+\|branched-chain-amino-acid-ABC-transporter-permease	gnl\|CDD\|119323	cd06581, TM_PBP1_LivM_like, Transmembrane subunit (TM) of Escherichia coli LivM and related proteins. LivM is one of two TMs of the E. coli LIV-1/LS transporter, a Periplasmic Binding Protein (PBP)-dependent ATP-Binding Cassette (ABC) transporter involved in the uptake of branched-chain amino acids (AAs). These types of transporters generally bind type 1 PBPs. PBP-dependent ABC transporters consist of a PBP, two TMs, and two cytoplasmic ABCs, and are mainly involved in importing solutes from the environment. The solute is captured by the PBP, which delivers it to a gated translocation pathway formed by the two TMs. The two ABCs bind and hydrolyze ATP and drive the transport reaction. E. coli LivM forms a heterodimer with another TM, LivH, to generate the transmembrane pore. LivH is not included in this subgroup. The LIV-1/LS transporter is comprised of two TMs (LivM and LivH), two ABCs (LivG and LivF), and one of two alternative PBPs, LivJ (LIV-BP) or LivK (LS-BP). In addition to transporting branched-chain AAs including leucine, isoleucine and valine, the E. coli LIV-1/LS transporter is involved in the uptake of the aromatic AA, phenylalanine.	4.14925e-61
NZ_CP053660.1\|WP_154615566.1\|3658841_3659993_+\|acyl-CoA-dehydrogenase-family-protein	gnl\|CDD\|173847	cd01158, SCAD_SBCAD, Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA dehydrogenases. Short chain acyl-CoA dehydrogenase (SCAD). SCAD is a mitochondrial beta-oxidation enzyme. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of SCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. This subgroup also contains the eukaryotic short/branched chain acyl-CoA dehydrogenase(SBCAD), the bacterial butyryl-CoA dehydorgenase(BCAD) and 2-methylbutyryl-CoA dehydrogenase, which is involved in isoleucine catabolism. These enzymes are homotetramers.	2.6191e-156
NZ_CP053660.1\|WP_154615578.1\|3650654_3652268_-\|long-chain-fatty-acid--CoA-ligase	gnl\|CDD\|235730	PRK06187, PRK06187, long-chain-fatty-acid--CoA ligase; Validated.	0

>NZ_CP053660.1|WP_154615562.1|3661738_3663061_-|HNH-endonuclease
MALIATLEHPLDTPADVLASARAEQKAVNAAEARLLEAAVQWCVLHPAESLDDAATWSVFRGFGDKPVCLAGEGAPFVTEFAVVEFAAGLGKSEDAGRAYLAEALELRYRLPKLWAKVTSLDLPAWKARSLARRTLHLPKKGAAFVDTHLAPVASTIGPAALERLLEEALVRFDPDEAQRVATERAEARHVTVQSRQVSFGGHVDVWATLDLADALDLDDALAKGAARLERLGCTDTLDARRSVALGDMARRQMQLEFDTDPKPLVVHVHQSPDGTLDDITRVENVRGFVLTTQLADWCTRAARGQASITVKPVIDLAERIHVEAYEVPDRLSQQTRLRDLHCVFPWCTRPAHATSRVDDDHVVPHARGGPTATENIAPLCRRHHRAKTHAGWDQQTPAPGTYLWRGPTGLTYRVDHHGTHDLGPEPPPPESPAAEPSPT
>NZ_CP053660.1|WP_154615564.1|3660984_3661437_+|hypothetical-protein
MAGLLTTRDVALAVAPGLLSLADPSALSGRGLAAYRLGVAATTVASTVVELDDPDLHAPPAVRWAGGVAVGALLWRTMPRWERADVALHSWLTAHGVPRSRLVVATLSTAAVLALAALERRRPTDDGQPDPGPDHEPDSEQVRDPDPVVG
>NZ_CP053660.1|WP_171896982.1|3660026_3660983_+|alpha/beta-hydrolase
MAIDPQIDGLLQLMAGSGHPPMWQQSPEDARRGFRVLTVDLRDPAFVPEVAAVEDVTVPGAAGPLAARIYRPSAGSAGSAPLPTVAFFHGGGFVIGDLDTHDLTCRTIATLCEAVVVSVDYRLAPEHPFPAAPDDALAAAHWVADSLADLGGSDRMGVAGDSAGGNLSAVVAQAFRDEGRPLAGQLLVYPVTDMGGSYPSHTENAEGFFLDTQTMAWFGAQYVGDPSALGDPRLSPLHGRLDGLAPAVVVTAELDPLRDDGNAYARALAEAGVRVEHRVFPGMIHGFVDMGRHSAAAQAAIEETCALFRTVLHDEAGR
>NZ_CP053660.1|WP_154615566.1|3658841_3659993_+|acyl-CoA-dehydrogenase-family-protein
MDLSLSDEQEGFRALARDFLEREAVPHRVEWDRREAVDLAIIPAMGEIGFFGLTIPEEYGGIGGDYLTYALAMEELGRADSALRGIVSVSNGLVGKSILAAGTEEQKQEWLPRIASGEVLGCFGLTEPDIGSDAGNLTSRAVRDGDDYVINGRKLFITNGTWAQVALILARTGGPGARGVTAFLVPTDTPGFEAREIKGKLGLRGQATAELFLDDVRVPASARLGEEGQGFKIAMASLDKGRVSVAAGCVGIIQGCLESSVSYATTRTQFGKPIAAFQLVQDMIADISLDADAARLLVWRCADLIDRGLPFRMPAAKAKLFASEAAVRAANNAIQVHGGSGYVDEYPAQKYLRDARVMTLYEGTSQVQKLLIGRAETGISAFV
>NZ_CP053660.1|WP_171896981.1|3657910_3658792_+|inositol-phosphorylceramide-synthase
MTAYAVVLALWSQLLGVPNDTVQVFLWLWLATIAWNVQEPRRHHLQFLRDWWPPVLGLVIYFYSRGVTDELGLPVHITMPIRVDEWLGGGTTPTEHLQAAWCGDPCLRDSAPRWYDVALTTVYASHFVTGLTLAAVLWMRSRPEWVRWMRRYLAINFGALVVYILYPMAPPWMASGDGYMGEVTRITSRGWADLGLGRFDLVLQGVGNPVAAMPSLHAGIAFLVAGYGIVRLRSPWRWVLVAYPLAMSLALVYFAEHYVIDVVAGALLAALVLAGCTWWERRQDRGPALRAGQ
>NZ_CP053660.1|WP_171896980.1|3656569_3657739_+|dienelactone-hydrolase-family-protein
MTRLTRASRILATTASASALALGLLAAPAPAAPSVPAAPAADEAAPGPTAYAGDGPYGVGQRSMRLPSGALVEVWYPTRPADVAGQPEGTYDVVDWLPPVLEGFLPDGAAVTHPSGGVRRAPIARRGFPLVVFSHGFAGFRQQSSFLTSAIASWGYVVAAPDHRSRTMTTVLGGTPGTTTDVQDLRDTITLVGSKSRTRKNWLHKRVDMTRVAAVGHSAGGRAVENLAVADPRVDTWVGMAGAATGALDEGATAVPTQPGVLLVGGADQIVTRERMEAAYAAMSAPKRWVELGGAGHLAFSDLCEVGEGEAGLLSVADLLGVPIPANLIRLASDGCIDPELASVDAWPAIRHVVVAQLRAVLGPDQATPAAFDGLVEAWPGVVTDSRSE
>NZ_CP053660.1|WP_171896979.1|3654787_3656485_-|ABC-F-family-ATP-binding-cassette-domain-containing-protein
MGHVDVAGVRYELPDGRVLLDEVSFRVGEGQKVALVGANGAGKTTLLRIITGDLQPHAGVVTRSGGLGIMRQQVAHGSTTVADLLLSVSPPRVRAAAAEVDRLEVALMETDDEPTQLAYATALGEYADAGGYDVEVTWDVCTTAALGLPYDRVKYRELSTLSGGEQKRLVLEFLLRGPDQVLLLDEPDNYLDVPGKIWLEGRIRESDKTVLMISHDRELLDNTATRVVTVELGAGGPGTGNTVWTHPGGFASYHQARTDRFARFEEMRKRWDEEHAKLKALVLRLKVKSEYNDGMSSQYRAAQTRLRKFEEAGPPTEQPREQQVSMRLTGGRTGKRAVVCEQLELTGLMRPFDLEVWYGERVAVLGSNGSGKSHFLRLLAAGGTDPDVEHRPVGEVEIRPVAHTGKARLGARVRPGWFVQTHEHPELVGRTLLEVLHRGDGHPDGRKGMGREQAARVLDRYELAHAGEQTFESLSGGQQARFQILLLELSGATLLLLDEPTDNLDVQSAEALEEGLAAFEGTVLAVTHDRWFARGFDRFLVYGADGEVYESEGPVWDEGRVARAR
>NZ_CP053660.1|WP_154615573.1|3653744_3654791_-|GNAT-family-N-acetyltransferase
MSTSGTDLRIVAVDPFDDAALEAWHATYAVAEAHGYEDTATVWQLEEVRALMQAPASGYRIDAWNGLLGTEPDAFVVAAGWMRTPRHDNLDRADLSVHVLPAHRRRGHGTRVLAHLEQVARERGRSILLAEAHYAYAAGPAGAGECGPEFARARGYALGLGDVQRRLRLPVAAGLLDRLAAEAAPHHAAYTLRSWAGPVPDELLDGWAEVTASLTTEAPVGELALEPERPDPVAVREHEAVLARQGRRKYNTVALAPDGTVAAYTDLVTTVHEPGRAYQWGTLVRRAHRGHRLGLAVKVANLRLLQAGRPDLTHLLTYNAEVNDHMVAVNDLLGFEPVARLGEFQKRL
>NZ_CP053660.1|WP_154615575.1|3652372_3653677_+|trypsin-like-peptidase-domain-containing-protein
MTENYPNPQTGGHTPDPHATAPLHGQPAGPPPAAPPAAGLATPPAPPRRGRKGFAAAVLAGALVVGGGAGLGGAAVWSAFDDEGTSTSAGSDRTSSQVVSASDEEAPKGSVEQVAAKVLPSVVQIEVSGAQGAGSGSGIVLSSDGVILTNNHVIEAAADGGEMTVAFSDGSRAEAEILGRDPLTDTAVIKAKGVDDLTPATIGDSESLDVGEQVVAIGSPFGLESTVTSGIVSALDRPVNVGQDDQNNSTTYPAIQTDAAINPGNSGGPLVNMNGEVVGINSSIRTASSTGGEAGSIGLGFAIPVDPVLPIVDQMSEGERPTHARLGISVSDPGARAAAEGPSGLLGQQQPQAEQEDDAPAVIGAEVVELGEDSTAGEAGIKAGDVITAIDDTRINSADSLVATIRSYRPGDEVSVTFLRDGQEQTVTLELASD
>NZ_CP053660.1|WP_154615578.1|3650654_3652268_-|long-chain-fatty-acid--CoA-ligase
MTATAPDSDLATAAPDPVFVDDRLAHWARTTPDAEAMTYLGRTWTWAEWDERVRRAAGALQQLGVGRGDVVAFLDKNHPACVELSLAAGSLGAANAIVNWRSAGDEVEYAVNDSGAKVLVVGRELMPTLDAVRDRLPAVEHVVEVTPDGADGDAWEALLAAATPVGRAPEVEPDDVCLVMYSSGTTGRPKGVMLSHRNMVSHTVNAHDGWGFEPGDKSMVAMPLFHVGGSSYVLFGIHDGIPSVMTRDPDGMSLAGAILAGANRTFLVPAVLAQVLQSGEDAVKLFGALKTYTYGAAPMPPPLLRAAMAAWPDTDFMQVYGLTEVAGVATHLMPEDHRTAEASGHPERLVSAGKAVPGVEIRIVDPGTLEDLPVGTHGEIWLRTPQLMKGFLNKPEATAEVVVEDGWFRTGDMGKLDEDGYLFVEDRLKDMIISGGENIYSPEVERVLAEHPAVMEVAIIGIPDDTWGESVKAVVALKPDTSATEEELIAYCREHLAHFKCPRSVDVIEALPRNPTGKILKRDLRAPYWEGRSRGVN
>NZ_CP053660.1|WP_154615560.1|3663379_3664609_-|helix-turn-helix-domain-containing-protein
MRPAQSAAAAPAGTSAGAAPARAWALLLDQADTIADSITLALFERDASLYERMGPELRVDVRESTRVHIRRGLEVLSGRRTQGSPTAIDIWRETGRRRARQGVPLELVLNAYMLGARVLWEALIARSATAPDGVVDDQVLLAAGGTVWSNLDVQNAVLIEAYRREAARLQRHDLQRQQSFLDALLEGRGADPDFADEARTVLDVGPDDTVACVVALYDDPPDSLGPAEDRLDKLGVVSRWHVRSGIYFGLLAGPLPDEPGIAELFAPYAAGRMGVATAPDGIAGFATAFQLATRAAETLPRAGRGVVPVSERLPEVLLAGSPQVAPLLLARTLGPILALPEAQSRTLLDTLAALLRHGGSPTHAAEDLYCHRNTVIYRLKQIEQLTGRSLADPRDKLLLDLALMACGSA
>NZ_CP053660.1|WP_171896983.1|3664783_3665605_+|ABC-transporter-ATP-binding-protein
MPSSTSAAPPATKPAVPPPTALELSGITVTFGGITALSEVDLAVVPGTVHGVIGPNGAGKTTLFNVACGFVVPDAGTISRAGDRLERLHPHDLAGLGMARTLQGLGLFDRVTVLENVVVGADRHARTGFLGSLLGLPGAAREERALRERAMEVLDRLGIGAYAARYPGSLPYPVRKRVALARALAAEPDLLLLDEPASGLGAADMDELGDLVRGLAAERAISVMLVEHHMDLVMRVCDEITVLDFGRRIAHGPPDLVRNDPAVLAAYLGEEVD
>NZ_CP053660.1|WP_154615558.1|3665604_3666309_+|ATP-binding-cassette-domain-containing-protein
MLTVTDLCAGYGPVRALEGVSFTADRGRVTAVLGANGAGKTTLLRTVSGLHRADRGSVELDGKPLDRVAAERMPALGLAHVPEGRGVITELTVEENLRLGGLGRAGSVDAADLDRVYTLFPVLADRRAAVAHVLSGGERQMLVIARALMARPTMLLLDEPSLGLAPRIVAQIFELLRGLVESESLSVLLVEQNARSALSIAHRGVVLNLGRVVADDAAEVLAADDQLRHAYLGF
>NZ_CP053660.1|WP_171896984.1|3666321_3667200_+|branched-chain-amino-acid-ABC-transporter-permease
MQQLLNTALGGLTLGMVYAAFALALVLIWRSTRIVNFAQAPMAMVTTFVALVVVDAGHSYWLAFAAALASGLLLGAVVERLIVRRVEGGPEINAVILTLGLFIVLHALAAVVFGNRYRSFPAPFGVRGIEVGGTTIALTGFGVFTILAVLVTMGLLLALFRYTDLGLRMRASAYNPEVARLLGVRVGRMLTLGWALASLVGSLAGLLIAGGSLVHPGYMDSVVVYGFVAAVLGGLDSPIGAVVGGLLLGLALSFVSGYVGSQLVALAALVILMLVLTLRPGGLFAQTAARRV
>NZ_CP053660.1|WP_154615556.1|3667201_3668371_+|branched-chain-amino-acid-ABC-transporter-permease
MTALRTWWAGSLLGRHLLLALVGLVVVVVVLESSSDFRNLQLASMAYLGIAAGGLTVLTGLNGQISLGHGALMAIGAYTAALLLDDRDAGTPLPLVVLAAIAVTLLVGVVVGAAAARLHGPYLAGATLALAVAVPGIALYFKEELGGEQGLRVVLPDIPAWVLDLAFFVTGQDLTRSRYVAYLAWLTLIVTFVLLANLSRGRVGRRWRAVRDDEVAAELAGIRLGRARVSAFVVSAAAAGAAGAMMAVTVRLAAPSGFTITLSLTLLTAVVLGGLGSLTGALLGAALLTFLPQVVTDLGVDAGLSDIQAAELSPLVYGLVMVAVILLAPAGLVGTARTALLRRRLRRTGPASDKPGPASDVPGPDAPPAVPTTPTAATTTSTTSKGTTT
>NZ_CP053660.1|WP_154615554.1|3668367_3669714_+|ABC-transporter-substrate-binding-protein
MRRRLRRSAPLAGVLAGALLLSACGAGGRDDDGDGGSGGDAAVDTPGVTEDSIKIGAHFPLTGVAAPGYNEIPTGAKAYFDYVNAQGGVNGRQIEYVVRDDGYNPTNTSSVTNELVLEEEIFAMVGGLGTPTHSAVVDFLNDEGVPDFFVSSGSLQWGDDPENAPYTFGWQPDYEIEGKIIGQYVAENMPDAKVGLFLQDDDFGDDAEKGVRQFVDDQIVAAERYTSGNTDVGPQVAGLQAAGADLVLAFNTPSYTALSQLVALKLGYQPQWFYSNVGSDADLVGSLLSRFSEGAVEGGSGSLDGVMTTEYIPGVDQPDDPWVQLWEKVWDEHGEKGELTNYRVYGMSHAYAFVQALMAAGEDLTRDGLVEAMEEVGAGLDGPQLAPFRYSADSHLGISGLRVVEIRDGAGEDLTPVLVTDIGDAEIVEDDSGQDADAPPESGVPEAS
>NZ_CP053660.1|WP_154615552.1|3670026_3670632_-|methyltransferase
MSEQEEHYFSADPSVPFKRAPVTAEVWGRTLSLVSGSGVFAQGRVDIGTSVLFRETEPPAGGRVLDLGCGYGVIGLAVAVCVPGATVTAVDVNERAVLLANENAAALGVADRYRAATPDAVEPHATYDEIWSNPPIRIGKQALHELLLTWLPRLAPGGRAVMVVGKNLGADSLQRWLGEQGFPTTRLASAKGFRVLESRRR
>NZ_CP053660.1|WP_154615550.1|3670628_3671510_-|tRNA-pseudouridine(38-40)-synthase-TruA
MIAGAALTPSSVRKDEGVRIRIDLAYDGSGFHGWAAQPGLRTVQGELSAAAATALRMPSVELVCAGRTDAGVHARGQVVHLDVEPDALARSAGRAPDPPLEALVRRLNGILPADVRVRRAVEAAPGFDARFSALWRRYAYRVADTPAAVDPLVRGHVLAWPRPVDVEAMNEAAVLLLGQHDFASFCKQREGATTIRVLQELSWRRLPSGVAEATVRADAFCHSMVRSLVGCLLAVGEGRRPVAWAGEILAAERRDASVPVVHAHGLTLEEVAYPPDAELGARVELTRARRERA
>NZ_CP053660.1|WP_171896985.1|3671487_3673143_+|FAD-dependent-oxidoreductase
MSAAPAIILVSEHHLDDLEGAFGRYEREYDVRSARSGVAAEALAREVVATGGTVALFVAESVLPDCHVLEGFHRWRAVAPNARRMVAAHWDRFLTDAPVLRAGLAKGKYDAYLLMPRGIRDEEFHHAVTDLLSDWGATVAEPEVVSAKIISPVRDARVLAIRDFLDRMGMASRVYHPDDPVARHLLGDHVDDAAYPLVWAPERPAVEDATVRTVAMSLYGAPSDLDVEGTVDVCVVGGGPAGLATAVYAASEGLSCVVLEAEAIGGQAGTSSMIRNYLGFPRGISGMRLAQRARNQALRFGTRFVTGWEVQGLVPGAGGAPHLVRTDGGDVAARAVVVASGVAYRKLRVEPLEELVGSGVFYGAAMTAAREMEDQDVVVVGGGNSAGQAAVHLARFARSVTVLVRRPDVAATMSQYLVGEIAYHPRITVTTCGEVVDGGGDSRLEWIDVRDTRDGSVHRREVGGLFLLLGAEPRADWLPTEVARDERGFVLTGRDVPRARWVDGLPPANLATTVPGVFAAGDIRAGSMKRVAAASGEGASVVPLVHQWLAP
>NZ_CP053660.1|WP_154615546.1|3673172_3674102_-|carbohydrate-kinase
MVAEAGPEARDVLVVGEALVDVVRAPDGTTREHAGGSAANVAVALARLGRPVRLATAYAADDRGALLARHLDAAGVALATDPAVLARTSAALATIGAGGAATYEFDLSWELGPVADEPAPLHVHACSLGAVVAPGAEDVAALLRRLRDRATVSYDVNARPAVTGTGADVVARVERVAALADLVKASDEDLAALWPDLDEASAVAHLLALGPGVVVVTRGADGATWTGAGRTVEVASLPVEVADTIGAGDTFGAALVDALWERGLLGAERRERLRGIGEVEVAEVLAHAARAAAVTVSRPGADPPYRHEL

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Crispr_ID: NZ_CP053660_8

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP053660_8

4028088-4028179

Orphan

Consensus_repeat	Method
CGGTTCATCAAGGTATGCAGCCGAACCGAC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP053660_8

>merge|NZ_CP053660|8|4028088-4028179|CRISPRCasFinder
CGGTTCATCAAGGTATGCAGCCGAACCGACACTCCCCTCGGTGAGCTCACCGTGGGAAGTGACGGTTCATCAAGGTATGCAGGCGAACCGAC

>NZ_CP053660|8|8|4028088-4028179|CRISPRCasFinder
CGGTTCATCAAGGTATGCAGCCGAACCGAC	ACTCCCCTCGGTGAGCTCACCGTGGGAAGTGA
CGGTTCATCAAGGTATGCAGGCGAACCGAC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP053660.1\|WP_154612607.1\|4025152_4026073_+\|LysR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|176112
NZ_CP053660.1\|WP_154612738.1\|4032725_4033313_-\|VTT-domain-containing-protein	unknown	unknown	gnl\|CDD\|223659
NZ_CP053660.1\|WP_171897361.1\|4020026_4020923_+\|diacylglycerol-kinase	unknown	unknown	gnl\|CDD\|224513
NZ_CP053660.1\|WP_154616634.1\|4026466_4028020_+\|DHA2-family-efflux-MFS-transporter-permease-subunit	unknown	unknown	gnl\|CDD\|129794
NZ_CP053660.1\|WP_154612603.1\|4029393_4029888_+\|DUF2867-domain-containing-protein	unknown	unknown	unknown
NZ_CP053660.1\|WP_154612612.1\|4018532_4019816_-\|adenylosuccinate-synthase	unknown	unknown	gnl\|CDD\|234904
NZ_CP053660.1\|WP_154612606.1\|4026045_4026468_-\|DUF3151-family-protein	unknown	unknown	gnl\|CDD\|378646
NZ_CP053660.1\|WP_154616632.1\|4035258_4036050_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|185594
NZ_CP053660.1\|WP_171897066.1\|4015783_4017202_-\|adenylosuccinate-lyase	unknown	unknown	gnl\|CDD\|176471
NZ_CP053660.1\|WP_154612740.1\|4031059_4031707_-\|rRNA-methyltransferase	unknown	unknown	gnl\|CDD\|349969
NZ_CP053660.1\|WP_154616636.1\|4022031_4023984_+\|lysine--tRNA-ligase	unknown	unknown	gnl\|CDD\|234829
NZ_CP053660.1\|WP_171897363.1\|4034038_4035238_+\|pyridoxal-phosphate-dependent-aminotransferase	unknown	unknown	gnl\|CDD\|236095
NZ_CP053660.1\|WP_154612739.1\|4031839_4032562_+\|VTT-domain-containing-protein	unknown	unknown	gnl\|CDD\|182775
NZ_CP053660.1\|WP_154612602.1\|4030411_4030990_-\|dienelactone-hydrolase-family-protein	unknown	unknown	gnl\|CDD\|223489
NZ_CP053660.1\|WP_154612610.1\|4020968_4021961_-\|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|99777
NZ_CP053660.1\|WP_154616635.1\|4024058_4025051_-\|putative-sulfate-exporter-family-transporter	unknown	unknown	gnl\|CDD\|225411
NZ_CP053660.1\|WP_171897359.1\|4017240_4018506_-\|phosphoribosylamine--glycine-ligase	unknown	unknown	gnl\|CDD\|234856
NZ_CP053660.1\|WP_154612741.1\|4029911_4030388_+\|LOG-family-protein	unknown	unknown	gnl\|CDD\|375733
NZ_CP053660.1\|WP_154616633.1\|4033408_4033990_-\|orotate-phosphoribosyltransferase	unknown	unknown	gnl\|CDD\|234771
NZ_CP053660.1\|WP_171897067.1\|4028278_4029310_-\|class-II-fructose-bisphosphate-aldolase	unknown	unknown	gnl\|CDD\|236406

Protein	Function_ID	Function_description	E-value
NZ_CP053660.1\|WP_154612607.1\|4025152_4026073_+\|LysR-family-transcriptional-regulator	gnl\|CDD\|176112	cd08420, PBP2_CysL_like, C-terminal substrate binding domain of LysR-type transcriptional regulator CysL, which activates the transcription of the cysJI operon encoding sulfite reductase, contains the type 2 periplasmic binding fold. CysL, also known as YwfK, is a regular of sulfur metabolism in Bacillus subtilis. Sulfur is required for the synthesis of proteins and essential cofactors in all living organism. Sulfur can be assimilated either from inorganic sources (sulfate and thiosulfate), or from organic sources (sulfate esters, sulfamates, and sulfonates). CysL activates the transcription of the cysJI operon encoding sulfite reductase, which reduces sulfite to sulfide. Both cysL mutant and cysJI mutant are unable to grow using sulfate or sulfite as the sulfur source. Like other LysR-type regulators, CysL also negatively regulates its own transcription. In Escherichia coli, three LysR-type activators are involved in the regulation of sulfur metabolism: CysB, Cbl and MetR. The topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.	3.69722e-61
NZ_CP053660.1\|WP_171897361.1\|4020026_4020923_+\|diacylglycerol-kinase	gnl\|CDD\|224513	COG1597, LCB5, Sphingosine kinase and enzymes related to eukaryotic diacylglycerol kinase [Lipid metabolism / General function prediction only].	3.95503e-45
NZ_CP053660.1\|WP_154616634.1\|4026466_4028020_+\|DHA2-family-efflux-MFS-transporter-permease-subunit	gnl\|CDD\|129794	TIGR00711, Uncharacterized_MFS-type_transporter_YhcA, drug resistance transporter, EmrB/QacA subfamily. This subfamily of drug efflux proteins, a part of the major faciliator family, is predicted to have 14 potential membrane-spanning regions. Members with known activities include EmrB (multiple drug resistance efflux pump) in E. coli, FarB (antibacterial fatty acid resistance) in Neisseria gonorrhoeae, TcmA (tetracenomycin C resistance) in Streptomyces glaucescens, etc. In most cases, the efflux pump is described as having a second component encoded in the same operon, such as EmrA of E. coli. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Other].	3.3234e-83
NZ_CP053660.1\|WP_154612602.1\|4030411_4030990_-\|dienelactone-hydrolase-family-protein	gnl\|CDD\|223489	COG0412, COG0412, Dienelactone hydrolase and related enzymes [Secondary metabolites biosynthesis, transport, and catabolism].	3.53341e-13
NZ_CP053660.1\|WP_154612612.1\|4018532_4019816_-\|adenylosuccinate-synthase	gnl\|CDD\|234904	PRK01117, PRK01117, adenylosuccinate synthetase; Provisional.	0
NZ_CP053660.1\|WP_154612606.1\|4026045_4026468_-\|DUF3151-family-protein	gnl\|CDD\|378646	pfam11349, DUF3151, Protein of unknown function (DUF3151). This family of proteins with unknown function appears to be restricted to Actinobacteria.	1.85177e-65
NZ_CP053660.1\|WP_154616632.1\|4035258_4036050_-\|hypothetical-protein	gnl\|CDD\|185594	PTZ00395, PTZ00395, Sec24-related protein; Provisional.	3.64511e-05
NZ_CP053660.1\|WP_171897066.1\|4015783_4017202_-\|adenylosuccinate-lyase	gnl\|CDD\|176471	cd03302, Adenylsuccinate_lyase_2, Adenylsuccinate lyase (ASL)_subgroup 2. This subgroup contains mainly eukaryotic proteins similar to ASL, a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and, the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP). ASL deficiency has been linked to several pathologies including psychomotor retardation with autistic features, epilepsy and muscle wasting.	7.39358e-170
NZ_CP053660.1\|WP_154612740.1\|4031059_4031707_-\|rRNA-methyltransferase	gnl\|CDD\|349969	cd18096, SpoU-like, SAM-dependent rRNA or tRNA methylase related to SpoU. RNA 2'-O ribose methyltransferase catalyzes the methyltransfer from S-adenosyl-L-methionine (AdoMet) to the 2'-OH group of ribose in tRNA or rRNA. It is part of the SpoU family of MTases, a subfamily of the SPOUT methyltransferase superfamily. The SPOUT methyltransferase superfamily is a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot.	3.62283e-58
NZ_CP053660.1\|WP_154616636.1\|4022031_4023984_+\|lysine--tRNA-ligase	gnl\|CDD\|234829	PRK00750, lysK, lysyl-tRNA synthetase; Reviewed.	6.31193e-166
NZ_CP053660.1\|WP_171897363.1\|4034038_4035238_+\|pyridoxal-phosphate-dependent-aminotransferase	gnl\|CDD\|236095	PRK07777, PRK07777, putative succinyldiaminopimelate transaminase DapC.	0
NZ_CP053660.1\|WP_154612739.1\|4031839_4032562_+\|VTT-domain-containing-protein	gnl\|CDD\|182775	PRK10847, PRK10847, DedA family protein.	9.63975e-42
NZ_CP053660.1\|WP_154612738.1\|4032725_4033313_-\|VTT-domain-containing-protein	gnl\|CDD\|223659	COG0586, DedA, Uncharacterized membrane-associated protein [Function unknown].	1.35971e-38
NZ_CP053660.1\|WP_154612610.1\|4020968_4021961_-\|helix-turn-helix-domain-containing-protein	gnl\|CDD\|99777	cd06170, LuxR_C_like, C-terminal DNA-binding domain of LuxR-like proteins. This domain contains a helix-turn-helix motif and binds DNA. Proteins belonging to this group are response regulators; some act as transcriptional activators, others as transcriptional repressors. Many are active as homodimers. Many are two domain proteins in which the DNA binding property of the C-terminal DNA binding domain is modulated by modifications of the N-terminal domain. For example in the case of Lux R which participates in the regulation of gene expression in response to fluctuations in cell-population density (quorum-sensing), a signaling molecule, the pheromone Acyl HSL (N-acyl derivatives of homoserine lactone), binds to the N-terminal domain and leads to LuxR dimerization. For others phophorylation of the N-terminal domain leads to multimerization, for example Escherichia coli NarL and Sinorhizobium melilot FixJ. NarL controls gene expression of many respiratory-related operons when environmental nitrate or nitrite is present under anerobic conditions. FixJ is involved in the transcriptional activation of nitrogen fixation genes. The group also includes small proteins which lack an N-terminal signaling domain, such as Bacillus subtilis GerE. GerE is dimeric and acts in conjunction with sigmaK as an activator or a repressor modulating the expression of various genes in particular those encoding the spore-coat. These LuxR family regulators may share a similar organization of their target binding sites. For example the LuxR dimer binds the lux box, a 20bp inverted repeat, GerE dimers bind two 12bp consensus sequences in inverted orientation having the central four bases overlap, and the NarL dimer binds two 7bp inverted repeats separated by 2 bp.	1.72086e-07
NZ_CP053660.1\|WP_154616635.1\|4024058_4025051_-\|putative-sulfate-exporter-family-transporter	gnl\|CDD\|225411	COG2855, COG2855, Predicted membrane protein [Function unknown].	4.46014e-61
NZ_CP053660.1\|WP_171897359.1\|4017240_4018506_-\|phosphoribosylamine--glycine-ligase	gnl\|CDD\|234856	PRK00885, PRK00885, phosphoribosylamine--glycine ligase; Provisional.	0
NZ_CP053660.1\|WP_154612741.1\|4029911_4030388_+\|LOG-family-protein	gnl\|CDD\|375733	pfam18306, LDcluster4, SLOG cluster4 family. Family in the SLOG superfamily, observed as a standalone domain with little informative genome context, although related families in the SLOG superfamily are predicted to function in diverse conflict contexts.	7.35606e-40
NZ_CP053660.1\|WP_154616633.1\|4033408_4033990_-\|orotate-phosphoribosyltransferase	gnl\|CDD\|234771	PRK00455, pyrE, orotate phosphoribosyltransferase; Validated.	2.22231e-42
NZ_CP053660.1\|WP_171897067.1\|4028278_4029310_-\|class-II-fructose-bisphosphate-aldolase	gnl\|CDD\|236406	PRK09197, PRK09197, fructose-bisphosphate aldolase; Provisional.	0

>NZ_CP053660.1|WP_154616634.1|4026466_4028020_+|DHA2-family-efflux-MFS-transporter-permease-subunit
MGSIVHGAVFTELVTSTASTTAAPDAPEKDPWPALFALCLGFFMILVDSTIVSVATPAIIEDLQADVNAVVWVTSAYLLAYAVPVLITGRLGDRFGPRRMYLIGLTVFTLASLWCGLTGSIEGLVAARVVQGLGAAMITPQTMAIITRIFPAERRGKAMGLWGATAGVATLVGPILGGVLVDALGWEWIFFINVPVGIVGFVLALRLVPVLQTNSHRFDWLGVALSGVGMFLLVFGVQEGHQLEWSALVWSMIVGGIVFLALFVGWQARNRAEPLVPLSLFRDRNFSLANVAISAMGFAITAMAIPLMLWAQVVRGLSPTRAALLLVPMAVMSIALARPVGGMTDRVHPRLLTGSGLAAIIVSLVWLALLLGPDGSVLWLVPPMLLLGIGNAFVWAPNSATATRNLPLQRAGAGAGVYNATRQVGAVLGAAAIGVLIDARLAAEGLPPYGGGEAGASAAGALPAPVAAAFSDAMGTSLLLPPAVLVVGLLAALCFERPGHAGFGGGSVAPVPAAAAD
>NZ_CP053660.1|WP_154612606.1|4026045_4026468_-|DUF3151-family-protein
MTIGRDLMAGPPPTHLPADPATDALAAGETPVDVVRRSPASPVAWAALAGEAVAADADPVTVYAYARVGYHRSLDLLRRNGWKGHGPVPWEHEPNRGFLTCLALLAKAARAIGETDEWERCRDFLRDSSPTAYAELLGDA
>NZ_CP053660.1|WP_154612607.1|4025152_4026073_+|LysR-family-transcriptional-regulator
MSTPLDLTGLDLLVRVAETGSVGAAARQVGMAQPNASRVLAKLERQLGLTLLVRTTAGSRLTTEGEVVVAWAREALTAVDRVVLGARSLAAQRQAHLTVASSLTVAEHLAPRWLARFRRDHPDLHVSLDVGNSHHVLERVVSGRVPLGFVESPTVPRTVASTAVARDRLLVVVGPTHPWARRRTPVTAAELVASDLVVREAGSGTRETLVRALDLAGHALGEQRLELASTAAVKAAAAEGGAPAVLSELAVAAELATGQLVDVPVADLDLSRALRAVWLPSRRPEGPAAALLRLARSGQASPRSSA
>NZ_CP053660.1|WP_154616635.1|4024058_4025051_-|putative-sulfate-exporter-family-transporter
MVDRRVPGLALAAAAGGAALAVHALVPGLGSTLVAVLLGFAAAASGRLPEAVRPGLATASRTVLRVGVALLGLQLVLADVLGLGWPVVAVVVGVVALGIAGTLLAARLLGVPPEQGLLVACGFSICGAAAVAALDGVRRGRAEDVARVVALVVVCGSAAMLAVPLLGSALGLSPVAAGAWAGASVHEVGQVVVAGGLLGSAALQVAVAVKLGRVLLLAPVLAVVAVRARRETEADTDTAAEGVRRPPLVPGFVLAFVGLVALRTLVPLPDVALDAAAQVQSAALATAMFALGCSLDPAALRRTGRRLVALAAVATAVVALLGLPAAYLVG
>NZ_CP053660.1|WP_154616636.1|4022031_4023984_+|lysine--tRNA-ligase
MLGAYVDRAGRRTRGRRRPARPASGDAEAGRRAGGCRDRRRGRFRRPPPPAVAWVLVPGRPSSRGGPHPTYVQERTVARGNRSDQGADPTDWVTRAADDAIRHAGIGEGEDRLITCASGASPSGPIHLGNLREFLTPHLVAEEIRRRGLRVRHLHSWDDFDRFRKVPAGVPASWAEHIGRPLSAVPDPWECHESWAEHFKAPLRAALAEMGVEMEEVSQTERYRAGAYTEQVLHAIRHRDTIEEVLAKHRTKKAEPVAENDQEAAALADSVAEADEPAGSGSLARFPYKPYCRECGRDTVDVTAYDDETTDLAYTCASCGFTGVTNVATQHEGKLVWKVDWPMRWSVEGVDFEPGGLDHSTPGSSYTVGKELVKRVFDFRAPSYVAYAFVGFAGMQKMSSSAGGVPTAADALKVLEAPILRWLYARRQPKQAFNIDFGAEVVRLYDEWDSLGRKAADPAKRDAQVLAFERASATAAAGTLPTPPVVVPFRLLSSVADVTAGSAELISGIVDRAGYAHDSVEDLQPRLGRAMTWTAEFVPAEDRTTVREEADAERLANLSEDEQRWLAQLLDRLPAELDVDDTTALVYGVPKLARGLALDDAPTDEVKADQKAFFRLLYELLVGAERGPRLPTLFLALGSDRIRRLLTPPA
>NZ_CP053660.1|WP_154612610.1|4020968_4021961_-|helix-turn-helix-domain-containing-protein
MAGPRVPATLLEALGLGDDDDHFYERVRAQSGREVVSVAAALMRTPAELLRDLQPFMEHGIVRVEDDRVFVDSPTEAVVRVLAETAATAERAHARLTDLAAAVPLMTRRGRPLGGGPEGVRPLDGEVSGGGSPVELLRSLVERSTGEVRWLRPDPFRGPAEPAYAEVVAKAVAQGRRCRGIYPVRTLADARDGLAHRVAIGEEVRVLPQVPTRMLIVGSTHAVVPEPLGTADDPRSLVRERGLVQALTLWFDSMWQRALPVPELERADARPDLRRFLLQQLAAGAQDEQIARRLGVSLRTVRRRVADLLAELGADTRFQAGVEAARRGWL
>NZ_CP053660.1|WP_171897361.1|4020026_4020923_+|diacylglycerol-kinase
MITNSDAGTDDELQLERALAILRERTSVEVCATSDPGELDGVLHRAGSRRIVVAGGDGSMHAVVAALHRRRELSEAVLGLLPLGTGNDFARGNDIPLDVEEAARVVLHGRPRQMDLILDEVGEIVVNSVHAGAGAQASRRADRWKDRLHRVGVGGVNLGKLGYPIGALIASVKPPYVRLRVEVDGEVVVDYDEPILMIAVGNGSSVGGGTELVPEADARDGLMDVMIARTVGPLQRVGYLAALVRGTHHERDDVLYLRGRQVTIDGEEFYCSADGEVYGPERRRTWRVEPAAYCLVLP
>NZ_CP053660.1|WP_154612612.1|4018532_4019816_-|adenylosuccinate-synthase
MPAIVVLGAQWGDEGKGKATDLLATTDPIDYVVRTSGGHNAGHTIVINGEKYATHLLPSGILTPGATSVIANGVVVSPEALFRELDGLLERGVEIGGLVVSANAHVIASYHSTIDKVTERFLGKNQIGTTGRGIGPAYSDKVNRYGVRIADLFDEKILRQKIEAALDVRNHLLTKIYNRRAIEVDAVVEELTAYVDRLRPMVADTSLLLNQALDRGQTVLFEGAQATMLDVDHGTYPFVTSSSPVAGGVCTGAGIGPTRIDRVIGVIKAYTTRVGAGPFPTELFDEDGVQLQKLGGEIGVSTGRTRRCGWYDAVVARYSSRVNGLTDYFLTKLDILGAWERIPVCVAYEIDGVRHEEMPMTQTEFHHATPIYEYFDGWGTDISGCRSFEELPVNAQRYVQALEELSGTKIWAVGVGPGREQTVVVNP
>NZ_CP053660.1|WP_171897359.1|4017240_4018506_-|phosphoribosylamine--glycine-ligase
MLVVGTGGREHALALALSRDPAVSEVHAAPGNPGIGAVATLHDVDPGDPAAVAALASGLGVDLVVVGPEAPLVAGVADAVTEAGIACFGPSRAAARLEGSKAFAKEVMAAAGVPTARSRVCSTPAEVAEALDAFGAPYVVKDDALAAGKGVVVTTDRAEALAHAATCGTVVVEEFLDGPEVSLFAVCDGATTRALQPAQDFKRIHDGGRGPNTGGMGSYSPLPWAPPDLAALVVATVVQPTLDEMARRGAPFRGCLYVGLALTAAGPRVIEFNVRFGDPDVQPVLALLDSPLGELLLAAAEGRLDEVAPPRFRTGAAVSVVLASAGYPESSSKGDVITGADRAAARADVDVIHAGTALDGDALVTAGGRVLAVRATGADVAAARAAAYSAAEEISFPGMQRRSDIAAEPLGVVEGAAVLAD
>NZ_CP053660.1|WP_171897066.1|4015783_4017202_-|adenylosuccinate-lyase
MSVPNVLATRYAAPDLAGIWSPEHKVVLERQLWIAVLKAQRDLGIEVPDGVVEAYEAVVDQVDLASIAARERVTRHDVKARIEEFCALAGHEHVHKGMTSRDLTENVEQLQVRQSLRIIRDRAVATLARLARLAAEHELTVMAGRSHNVAAQATTLGKRFATVADEMLVALDRVEDLLGRYPLRGIKGPMGTAQDMLDLLDGDEARLAELEQRVADHLGFDRVLTSVGQVYPRSLDFDVLSALVQLVAGPSNLATTIRLMAGNELVTEGFKEGQVGSSAMPHKMNSRSCERVNGLAVVTRGYLSMIGELAGDQWNEGDVSDSVVRRVALPDAFFAVDGLFQTFLTVLDEFGAFPAVIQRELDRYLPFLATTKVLMAAVRNGVGREAAHEAIKEAAVGTALDMRRGQAENDVFARLAADPRLGLSADQLASLVAEPITFTGAAVAQVQEVVRRVAAVTERHPEAAAYAPGAIL
>NZ_CP053660.1|WP_171897067.1|4028278_4029310_-|class-II-fructose-bisphosphate-aldolase
MPIATPEKYAEMLDAAKQNAYAFPAINVSSSQTLNAALKGFADAGSDGIIQVSTGGAEYLSGPSVKNMVSGSVAFAQYAAEVAKNYPVNIALHTDHCPKDKLDGFVRPLLEISRERVQRGEAPLFQSHMWDGSAVPLEENLTIATELLEKCIEAKIILEIEVGVVGGEEDGVAHEINDKLYSTPADAIATAKALGYGERGYYMTALTFGNVHGVYKPGNVKLRPEVLKEAQEAVVSEFGLEAGAKPFHLVFHGGSGSSAEDIAAAVDYGVVKMNIDTDTQYAFTRPVAAHMFTNYDGVLKVDGEVGNKKTYDPRAWGKAAEAGMAARIVEACEHLRSAGATLG
>NZ_CP053660.1|WP_154612603.1|4029393_4029888_+|DUF2867-domain-containing-protein
MLRRTSLRTTRRASTVPLPAQHAWAVVACGLAGPRWYVDAGPLVVRGLIDRLAGGGGRRWPVPDRPELLRGDTAGFWRVWEVQDDPGAGPRRLVLVADVRSPGRVTLTTTVTPTGAVTCRIEQQVRLDPDGLLGAAYLLVDLPARETVAELVHRRLLHDVLRDR
>NZ_CP053660.1|WP_154612741.1|4029911_4030388_+|LOG-family-protein
MDAAGHGRYVAVVGPADSATAGQLAAATEVGRLLAEAGAVVLTGGLHGVMRAAATGARDAGGTAIGLLPGRDRAAGSPEHTFLLPTGLGELRNGLLVRAADAVVAVGGSWGTLSEIALARRTGVPLVLLDPWDLPDDVGTVVGSPAEALTALGRALGA
>NZ_CP053660.1|WP_154612602.1|4030411_4030990_-|dienelactone-hydrolase-family-protein
MADLVLFHHALGLTDGVRAFADRIRAAGHTVETPDLFDGARFETIEAGVAHAQEVGFATVLDRARAAVDGLPEGLVYAGFSLGVLPAQQLAQTRPGARGAVLMESFVPPSEFGSWPAGVPAQVHGMDADPFFAQEGDLDAAREFAGSGVAEVELFTYPGDVHLFADSGLPGYDQDAAGLVADRVLEFLDRLH
>NZ_CP053660.1|WP_154612740.1|4031059_4031707_-|rRNA-methyltransferase
MPHGPVEVGVGPWEGPWPTGEQYDAALLAEGDRRNVVDRYRYWTVEAIVADLDTRRHDFHVAIENWQHDFNIGTIVRSANAFLAAEVHIVGNRRWNRRGAMVTDRYQHVRHHPTVADLAAYLRDLPGGPVPLLGIDNLPGSAHLETMEVPRRVCFLFGQEGPGLSEGARAACDGTFSIAQFGSTRSINASAAAAIAMHSWVRAHADLSDESAWRG
>NZ_CP053660.1|WP_154612739.1|4031839_4032562_+|VTT-domain-containing-protein
MMLGLDFLDPQWLLSQFGAELFWISLIIVFVECGLFFPFLPGDSLLFALGIFIATGQIDLFPGTRLVELGIAMVLMVLAAWLGNVTGYEIGRRIGPSLRDRDGRVLKQKYFDQTEVFFDRHGNKALVIGRFVAFVRTYITVVAGITGMPRRRFYTWSLVGGICWVIGVTCLGYFLGHTVPWLESNIDLIFLVILAFTAVPIAYEWWRHRRTDSPLADDNDHDGRPDRDITGASVPPRHGS
>NZ_CP053660.1|WP_154612738.1|4032725_4033313_-|VTT-domain-containing-protein
MERLGAPGAGLAIALENLFPPLPSELILPLAGFTASRGSFTLAEAIGWTTAGSVVGAMLLYVLGVLIGRRRIYWVWERLPLVKVEDLEKTEAWFGRHGRKAVFFGRMIPIFRSLISVPAGLERMPFGQFLLLTLAGSAIWNTVFVLAGYWLGEQWHRVEEYVGVFQWIVIGTVLAAVCWWLVVRVRAIRHERRST
>NZ_CP053660.1|WP_154616633.1|4033408_4033990_-|orotate-phosphoribosyltransferase
MAAVTTTDDSLAADIDACCRLTGTFTLRSGQVAPEYFDKYLFEADPILLQRVAREMVQLLPHDTELVGGLELGGVPLATSVSGMTGTPALFVRKKAKEYGTCKLAEGPAVAGRRVTLIEDVITTGGAVRDATLALREAGALVEVVVCAIDRSPAGEQPLADLGLEIRAVLTKADLDAARAAATATATDAAGTA
>NZ_CP053660.1|WP_171897363.1|4034038_4035238_+|pyridoxal-phosphate-dependent-aminotransferase
MTPRTAARTAARTAARTAARLHGIPPTIFTEMSALALRTGSVNLGQGFPDADGPASVREAAVAALREGHNQYAPGPGVPALRQAVARHQQRHYGLELDPDTEVVVTTGATEGIAAALLGLVDPGDEVVVLEPYYDSYTAMIQMAGGVRRPVTLRAPDFRLDPDELRAAVGPRTKLILLNSPHNPTGTVLTRAELAAVAEVAVEHDLVVVTDEVYEHLTFGHEHVPLATLPGMRERTLTLSSVGKSWSLTGWKVGWATGPRELVGALLGAKQWLTFTSGAPLQPAVARALDEEAEWPLELARDLRERRDLLCAGLAEVGMDVRVPEGTYFAIADVAAYGWEDGRAFCLALPERAGVVAIPAVAFHDDVEAGRHLVRWAFCKDASVIEDGLARLREADLGA
>NZ_CP053660.1|WP_154616632.1|4035258_4036050_-|hypothetical-protein
MSSPYGSPPPDEDPYGQRPADQSDPAQQPSAPDQAPNPYGPNSSGQNPYGQDSYGQSPAGQQPAPGQAPYGQAPYGQPPAGQQPYGQPYGAAYGTAPRDPDERPGTVTAAAVITLITAGLSALLYGLVAVALIVARDSLADDLRRTIEDDPAFDGTNMPTGDELTGFLIVIMIVLCLWSVIACVLAVLAMRRSNVARILLVISAAITALFSLVGIVSVVSAVPLIASIAVIVLLFVGGAGDWFARRGQQQQEQLPPGTSQPWG

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Click the colored protein region to show detailed information

Crispr_ID: NZ_CP053660_9

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP053660_9

4062612-4062696

Orphan

Consensus_repeat	Method
CATCAAGGTATGCAGCCGAACCG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP053660_9

>merge|NZ_CP053660|9|4062612-4062696|CRISPRCasFinder
CATCAAGGTATGCAGCCGAACCGCCACTCCCCCGTGTGAGCTCACCGTGGGGAGTGTGGCTCCATCAAGGTATGCAGCCGAACCG

>NZ_CP053660|9|9|4062612-4062696|CRISPRCasFinder
CATCAAGGTATGCAGCCGAACCG	CCACTCCCCCGTGTGAGCTCACCGTGGGGAGTGTGGCTC
CATCAAGGTATGCAGCCGAACCG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP053660.1\|WP_154616612.1\|4071749_4072913_-\|cupin	unknown	unknown	gnl\|CDD\|369647
NZ_CP053660.1\|WP_154612586.1\|4054686_4055292_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP053660.1\|WP_154616615.1\|4065756_4067145_-\|NAD(P)-binding-domain-containing-protein	unknown	unknown	gnl\|CDD\|109787
NZ_CP053660.1\|WP_154616616.1\|4065151_4065760_-\|TetR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224228
NZ_CP053660.1\|WP_171897069.1\|4055873_4056296_-\|nuclear-transport-factor-2-family-protein	unknown	unknown	gnl\|CDD\|379275
NZ_CP053660.1\|WP_154616621.1\|4055350_4055842_-\|nitroreductase-family-deazaflavin-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|281995
NZ_CP053660.1\|WP_154616677.1\|4058481_4059255_+\|SDR-family-oxidoreductase	unknown	unknown	gnl\|CDD\|181159
NZ_CP053660.1\|WP_154612578.1\|4064219_4065155_-\|alpha/beta-fold-hydrolase	unknown	unknown	gnl\|CDD\|366166
NZ_CP053660.1\|WP_154616617.1\|4061484_4062606_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|215598
NZ_CP053660.1\|WP_154616614.1\|4067235_4068429_-\|DUF2236-domain-containing-protein	unknown	unknown	gnl\|CDD\|378343
NZ_CP053660.1\|WP_171897072.1\|4070826_4071753_-\|sucrase-ferredoxin	unknown	unknown	gnl\|CDD\|227101
NZ_CP053660.1\|WP_154612582.1\|4060533_4060989_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP053660.1\|WP_154616676.1\|4059293_4060436_+\|sulfotransferase	unknown	unknown	gnl\|CDD\|379204
NZ_CP053660.1\|WP_154616618.1\|4061020_4061473_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP053660.1\|WP_171897070.1\|4057246_4058407_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP053660.1\|WP_154616613.1\|4069771_4070830_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|223515
NZ_CP053660.1\|WP_154616619.1\|4056342_4057242_+\|TIGR03619-family-F420-dependent-LLM-class-oxidoreductase	unknown	unknown	gnl\|CDD\|274680
NZ_CP053660.1\|WP_154612579.1\|4062788_4064090_-\|MFS-transporter	unknown	unknown	gnl\|CDD\|340863
NZ_CP053660.1\|WP_154616611.1\|4072909_4073104_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP053660.1\|WP_171897071.1\|4068473_4069775_-\|glycosyltransferase	unknown	unknown	gnl\|CDD\|133042

Protein	Function_ID	Function_description	E-value
NZ_CP053660.1\|WP_154616612.1\|4071749_4072913_-\|cupin	gnl\|CDD\|369647	pfam08007, Cupin_4, Cupin superfamily protein. This family contains many hypothetical proteins that belong to the cupin superfamily.	2.41574e-18
NZ_CP053660.1\|WP_154616615.1\|4065756_4067145_-\|NAD(P)-binding-domain-containing-protein	gnl\|CDD\|109787	pfam00743, FMO-like, Flavin-binding monooxygenase-like. This family includes FMO proteins, cyclohexanone mono-oxygenase and a number of different mono-oxygenases.	2.25327e-80
NZ_CP053660.1\|WP_154616616.1\|4065151_4065760_-\|TetR-family-transcriptional-regulator	gnl\|CDD\|224228	COG1309, AcrR, Transcriptional regulator [Transcription].	0.000914839
NZ_CP053660.1\|WP_171897069.1\|4055873_4056296_-\|nuclear-transport-factor-2-family-protein	gnl\|CDD\|379275	pfam13577, SnoaL_4, SnoaL-like domain. This family contains a large number of proteins that share the SnoaL fold.	1.50286e-25
NZ_CP053660.1\|WP_154616619.1\|4056342_4057242_+\|TIGR03619-family-F420-dependent-LLM-class-oxidoreductase	gnl\|CDD\|274680	TIGR03619, F420_Rv2161c, probable F420-dependent oxidoreductase, Rv2161c family. Coenzyme F420 has a limited phylogenetic distribution, including methanogenic archaea, Mycobacterium tuberculosis and related species, Colwellia psychrerythraea 34H, Rhodopseudomonas palustris HaA2, and others. Partial phylogenetic profiling identifies protein subfamilies, within the larger family called luciferase-like monooxygenanases (pfam00296), that appear only in F420-positive genomes and are likely to be F420-dependent. This model describes a domain found in a distinctive subset of bacterial luciferase homologs, found only in F420-biosynthesizing members of the Actinobacteria. [Unknown function, Enzymes of unknown specificity].	7.34361e-56
NZ_CP053660.1\|WP_154616677.1\|4058481_4059255_+\|SDR-family-oxidoreductase	gnl\|CDD\|181159	PRK07890, PRK07890, short chain dehydrogenase; Provisional.	6.31962e-127
NZ_CP053660.1\|WP_154612579.1\|4062788_4064090_-\|MFS-transporter	gnl\|CDD\|340863	cd06173, MFS_MefA_like, Macrolide efflux protein A and similar proteins of the Major Facilitator Superfamily of transporters. This family is composed of Streptococcus pyogenes macrolide efflux protein A (MefA) and similar transporters, many of which remain uncharacterized. Some members may be multidrug resistance (MDR) transporters, which are drug/H+ antiporters (DHAs) that mediate the efflux of a variety of drugs and toxic compounds, conferring resistance to these compounds. MefA confers resistance to 14-membered macrolides including erythromycin and to 15-membered macrolides. It functions as an efflux pump to regulate intracellular macrolide levels. The MefA-like family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	1.21386e-63
NZ_CP053660.1\|WP_154616613.1\|4069771_4070830_-\|hypothetical-protein	gnl\|CDD\|223515	COG0438, RfaG, Glycosyltransferase [Cell envelope biogenesis, outer membrane].	1.92844e-09
NZ_CP053660.1\|WP_154616614.1\|4067235_4068429_-\|DUF2236-domain-containing-protein	gnl\|CDD\|378343	pfam09995, DUF2236, Uncharacterized protein conserved in bacteria (DUF2236). This domain, found in various hypothetical bacterial proteins, has no known function. This family contains a highly conserved arginine and histidine that may be active site residues for an as yet unknown catalytic activity.	3.25482e-19
NZ_CP053660.1\|WP_171897072.1\|4070826_4071753_-\|sucrase-ferredoxin	gnl\|CDD\|227101	COG4759, COG4759, Uncharacterized protein conserved in bacteria containing thioredoxin-like domain [Posttranslational modification, protein turnover, chaperones].	8.81077e-32
NZ_CP053660.1\|WP_154616676.1\|4059293_4060436_+\|sulfotransferase	gnl\|CDD\|379204	pfam13469, Sulfotransfer_3, Sulfotransferase family.	1.00769e-58
NZ_CP053660.1\|WP_154616617.1\|4061484_4062606_+\|hypothetical-protein	gnl\|CDD\|215598	PLN03138, PLN03138, Protein TOC75; Provisional.	1.3889e-05
NZ_CP053660.1\|WP_154616621.1\|4055350_4055842_-\|nitroreductase-family-deazaflavin-dependent-oxidoreductase	gnl\|CDD\|281995	pfam04075, F420H2_quin_red, F420H(2)-dependent quinone reductase. This family of proteins is found in the genera Mycobacterium and Streptomyces. Member protein Rv3547 has been characterized as a deazaflavin-dependent nitroreductase. Rv1558 is an F420H(2)-dependent quinone reductase involved in oxidative stress protection.	2.64557e-33
NZ_CP053660.1\|WP_154612578.1\|4064219_4065155_-\|alpha/beta-fold-hydrolase	gnl\|CDD\|366166	pfam00561, Abhydrolase_1, alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes.	2.20394e-10
NZ_CP053660.1\|WP_171897071.1\|4068473_4069775_-\|glycosyltransferase	gnl\|CDD\|133042	cd06420, GT2_Chondriotin_Pol_N, N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase. Chondroitin polymerase is a two domain, bi-functional protein. The N-terminal domain functions as a GalNAc transferase. The bacterial chondroitin polymerase catalyzes elongation of the chondroitin chain by alternatively transferring the GlcUA and GalNAc moiety from UDP-GlcUA and UDP-GalNAc to the non-reducing ends of the chondroitin chain. The enzyme consists of N-terminal and C-terminal domains in which the two active sites catalyze the addition of GalNAc and GlcUA, respectively. Chondroitin chains range from 40 to over 100 repeating units of the disaccharide. Sulfated chondroitins are involved in the regulation of various biological functions such as central nervous system development, wound repair, infection, growth factor signaling, and morphogenesis, in addition to its conventional structural roles. In Caenorhabditis elegans, chondroitin is an essential factor for the worm to undergo cytokinesis and cell division. Chondroitin is synthesized as proteoglycans, sulfated and secreted to the cell surface or extracellular matrix.	7.89445e-25

>NZ_CP053660.1|WP_154616617.1|4061484_4062606_+|hypothetical-protein
MSTVVAADPASCRDTADDLRKVRRRADRAEDHGRERSRHFASAAASGEIALALSSACEVVSGAGRRLSDDADTAETALRRFADGIEEVEQAMEQAWQTALARGLQSSLYRDIVLPADPTEGQVLAWNDAVGTVNRLRERELTLSQALIDALSTITPEQLRRPPGLDPAQPLPVPGTGGSGGGSGSGSGGGASGGGGSAHGGGGKSWEPAGAGPSGPGSGGGKSWEPAGAGVGSAHAELVGTPQATLHETPDVRGELLLGQQVRDAEARLEQLQAQLSQATDPAAQEALAAELAAGEQQLVETREQLAQLQQRNDEIEAANQAAQSAAQHGQHGQHGAQLVGQLGPTFEAAPLSAGPEFEPVPDAYAWPIPGPR
>NZ_CP053660.1|WP_154616618.1|4061020_4061473_+|hypothetical-protein
MGEMRLEANDLTRTAATLYERGERLSSTTVALPTTGVDSGAALQLLETRARDLGEQLTTLADVVVEVRDEVDTVDRFQVTRYHLENAQPGGAADAPQLPTLPPRSDDAPSHVLNLPFHDVLNLPENLTPDHDAAGHDAGAGGSGPGQKDR
>NZ_CP053660.1|WP_154612582.1|4060533_4060989_+|hypothetical-protein
MTSTPLLTLPPGWHHHPDPAPDVLVAARGGPALGSGVAPELVLRRAELPDRLRGDLAGWRAAAVADLARLLDSFALEDTEQLDLEGREVLYQRFAHRGVGVELLTEQWSWQVGAWGLTLTGTVALEDYADLCEVLEDAAASVEPGALMSAV
>NZ_CP053660.1|WP_154616676.1|4059293_4060436_+|sulfotransferase
MTRERPDVGSYDDILAAAVRTTGLSDLGGTAHEEGLRVLVDDLASPEAGLTPRGNYFQRSEVKSALVGRLLTQAQFTARPEHAAVPIERPVFVLGLPRTGTTALHRLLHADPAAQGLEMWLTQYPQPRPPRETWEADPIFGAMQQAFAAHHVESPEYRGIHYMDATTVEECWRLLRQTGKSSSYESLANLPRYSAWLAEQDWTDAYARHRQNLQLVGLNDPDKRWVLKNPSHLTALDALMAVYPDALVVYTHRDPVVCIASSCSLSAETTAGHSTTYVGETIGRTQLDLWARAFHAFHDARPRYDQAQFVDVAFAGLLADPLGTARSVYERFGLDFTPEAQAAMAEIDRESKQGAAKPSHRYAIEDYGLTEADVRAAFDR
>NZ_CP053660.1|WP_154616677.1|4058481_4059255_+|SDR-family-oxidoreductase
MLEGKVLVLSGVGPGLGRALGAEAARMGADLVLASRTERRLEKMAETVRAHGRRALVVPTDITDEASRVALVEQALAEFGRVDCLVNNAFAIPPMDPLTTLDLDGLRAANETNVFAPLRLTALFADALAATRGSVLMVNSCVLYQSQEEFAGYKLSKGALEHLSSSLATELGPRGIRLNSVAPSYIYEDVNKGYFDWIASESGRTHDEVYAEKAAPTDLKRLASPAEVARAALVLATDLCSAVTGQVLNVDCGEFHR
>NZ_CP053660.1|WP_171897070.1|4057246_4058407_+|hypothetical-protein
MSSSLDLTKPLRDAIAEAEELIANAPFIRTEQDRLEGYEYLAGRIRMAMQTAFDYDLERPLFVNPTHQFSRQGLDNPDALYFNAFLREGVEYVVRGRRGTTADLSFQVMAGTYGPGQAPRSCAAFDDRELDIADDGTFEFRYTAEPGATTLIVREVFNDWDTEERGVLWIERPDTMGRPAAPLTEARLAKRYEVAARSLVGSIQTWFAFPHFFQYQQPVNTLTPPQTTPGGLASQRSSIGHYELGEDQALVITVPECTDCAYQAVQIGSDWYVSTDYETHQTSLTKAQAVTDPDGMMRFVVSERPPSVPGGSIANWLETTGHRTGSMMLRWQRLERDLGPEDGPSVEVVPFDSVRDLLPHHSPVTPEEYAARIAARQRSVARRMLS
>NZ_CP053660.1|WP_154616619.1|4056342_4057242_+|TIGR03619-family-F420-dependent-LLM-class-oxidoreductase
MRFTYAEAMTRADYYAPLAQAAEAAGYTSMTVADSLIYPEESDSTYPYTDTGDREFLDGKEFIEAMVLCAHLFAVTSTLRLTPFVLKLPVRPPVLVAKQASSLAALSGNRLGLGVGISPWPEDFAALGVPWERRGKRMDECIDIVRGLTRPQDPDGGQEYFSYSGEFYEVASLKQTPAPTARLPLLVGGHADAALRRAVRKGDGWMHAGGDGEELDRLLARLAEIRREEGDTREDFEVHVISYDAYDPDGIKRLADKGVTDCIVGFRVPYVVGPDTEPLEKKIAHLEQYAENVIAKVEG
>NZ_CP053660.1|WP_171897069.1|4055873_4056296_-|nuclear-transport-factor-2-family-protein
MDLQELSDRTEIAAVLTRYTRAIDTGEFDRLETVFTPDAQIDYTESGGIAGGYAEVAPWLAEVLPAFFPRRMHTLGQVAIELAGDEAEVAAYFHNPMPVTGEDGAERVVEFGGIYHHRMVRTPDGWRSRELREEIVWKRT
>NZ_CP053660.1|WP_154616621.1|4055350_4055842_-|nitroreductase-family-deazaflavin-dependent-oxidoreductase
MGLPDEKPAGLDSPVVPKVLKRVAKVQVAAFRATNGRVGSTWRIGAGWRKPVPTLLLDHVGRKSGTRFTTPLLYLEDGADLVIVASQGGLPKHPQWYRNLLAHPDTQVALKGERVRPVRARVADPEERAALWPRLVELYADFDRYQRWTDREIPVVVLEPRRG
>NZ_CP053660.1|WP_154612586.1|4054686_4055292_-|hypothetical-protein
MPPDQPSGPPTDKLGDQRPDRPVLSGLIALVGVGLVVGLVLGGVALGAVSVLGLGGDDGGSGRSSDQQAFYLPKPQPTDEPDGPLITLAPEPGGDGSASAEPSESATTEAAEDEISLSAGQASVTPMQQIDLTGVYTGGEGAILQVQRFADGTWVDFPVTASVSNEMFSTYIQTGQLGENKFRVVDTSTGLESNEVTVTIG
>NZ_CP053660.1|WP_154612579.1|4062788_4064090_-|MFS-transporter
MTWTARLRATLLGLRMDTTPLRESRDFRLLFWAGSVFYLGGMITYVAVPFQVYSLTGSNFAVGAIGLVELAPLVVFGLYGGALADHVDRRKLLIWTGVAQAFFTGVLAVNAFRDEPDVWVVFVVAVFLVSCSALQRPSREALLPRTVRHDQLMAANALGSFGIQIGVLLGPAIGGVLIATVGIGWCFLIDVVGLAIATLLYVRMRSYAHRAETTPPSLEGIRQGVRYALSRRDLLGTYLVDIAAMLLALPVVLFPALVEEVFENPELLGGLYIAQTLGAMLATATSGWTSRVHHHGRAIVVAAAAYGACVALAGLMPSFWLVLLFLGLSGCADMISGIFRATVWSQTIPEAMRGRLAGIEMLSYSLGPLGGQVRAGVTADLWSVRGAITSGGVACVAGVALTATWLRDFWSYDDRTDEYAVAERAARAATGDA
>NZ_CP053660.1|WP_154612578.1|4064219_4065155_-|alpha/beta-fold-hydrolase
MTSQQPPATAPEATPGTRRDVAFASAGVELSAWHFPAATDDLAGPAGRPVVVMAHGLAGTKDSGLEPYARGLAAAGLDVLAFDYRGFGTSGGAPRQTVSMAGQVADYRAAAMAAKRLDGVDPDRLVLWGVSLAGGHVLSVGAGREDVAAVVALAPLVDGLAAGRLAMRHHKPSAMLRSTVEGVRSRVAGPRTMPVVARPGELGALTLDGCYEDYLAIAGPSWRNEIDAAVGLELGGHRPAKHAADLRCPLLVQIADHDRSAPPHAALKAAFAGRGEVRHYPCDHFDVYAGRDWFEPALAHQVHFLRRHLAP
>NZ_CP053660.1|WP_154616616.1|4065151_4065760_-|TetR-family-transcriptional-regulator
MSPAATRGDQRRAALLEALDQALRKAGPHARLEDINVADLSRRAGVTRSAFYFYFDNKAAAVAALMDEMEDDAWDAAGLLGGDGAMSERIATAIRSVVEGWRRRTHVHRAMLEARATSPAVRERWEQRIAAFVEVVAALVESERAAGRAPAGPPATALATALLDLNDRTLERLVRAADTTGEDHIDAVVHLWTSAIYGRTTP
>NZ_CP053660.1|WP_154616615.1|4065756_4067145_-|NAD(P)-binding-domain-containing-protein
MRAPTTAVIGAGISGLTVTKMLADYGVPGTTFESSDRVGGNWAFGNPNGHSSAYRSLHIDTSKYQLSFKDFPMPEHYPDFPHHTDIKAYLDSYADAFGLRERIEFENGVVHADRLPDGGWELQTQRGETRRFDLLVVANGHHWDPRTADFPGEFTGESIHSHHYVDPWTPLHLMDKRILVVGLGNSAADITVELSQRVLRNQVTLSTRSSAWIVPKLMYGKPADMNYRTYPQLPLSWQRKVAQWGQRFTGSDPRNYGLPAPNHKFFEAHPTQSTELPLRLKSGDVTARGNVARLDGSTVHFEDGASAEFDVIVYATGYNLTFPFFDPAFISAPGNRIDLYKRILKPGLDDLLFAGFAQATPTLFPFVESQARLIAAYAVGEYAPPPVEQMQEVIRADDALYMGHMLDRPRHTHQLDYFVYEHQMRTKELPEGRERARRAGAPALAGRSAAVPEPTAPEPTVL
>NZ_CP053660.1|WP_154616614.1|4067235_4068429_-|DUF2236-domain-containing-protein
MVVSAAPSRFAADRAWSARAAAPLRWTAGPGARPGPAEVDALRRGLLRRDEVAAALVRAVREDRTVSMREVHAALAAGGAGPDAPAPLRDFFAAVAQRPDWVDDDLLARGAEACRTFGHDAGLVLTHGSLLGGYRTAAALEPLARTGRLTGEETLRRIGETTAWWRAVTAPAGLEPGAEGHRLALHVRVMHGFVNHHLEQDPTWEWDLRGVPINQYDQASTLGVFSTSFLLHLRLLGVRVPRRDAAAVMHLWSYVGWLMGVDEEWLPRTERRGRRLLYHFLSHDPPPDENSRTLAAALIDMVDLAPYGPLRRRWERERALSVSTWLLGPAAMRDLGLPVRAPWYGVWRVAANLGWTQVVGRLPGGRLRLLVRADRHHRRQERAWHGEAAPGIGAIPA
>NZ_CP053660.1|WP_171897071.1|4068473_4069775_-|glycosyltransferase
MSRPPSGATVPGNRWDLAGPRTGPPPTVTVVVTHYEQPRELARTLHALGRQTHPADRLEVVVADDGSATAPTVPDGVRLVRQADEGFRAAAARNLGAAAGTGEVLVFLDADTTPEPGYVAAISRLPHLLPEALVVGRRRHADLVAVPVDAPVEDAGPAHELSSPAWLVEGYRRTRDLVEADDTSYRFVLSAVAACSRWLHTHIGGFDETFAAYGGEDWEWAARAWRHGALLAHEPAAVAWHDGPDFAARDSAADRARALAETLAIARRVPAPGAAPRGLLVGPRDPLVTIADGLDPTGLLVALDSLLAALPTAHVQAPAYVAGLLAGDPRVAAGPPPGTPAWHLHLERPVRGSAEAWRAVVARLAGPDAPGLLRLTGADGAPLVTARTLRGVRRQERWGRTDLFAERAEPAAGLGLAAVRPGTTLEAHLGGWG
>NZ_CP053660.1|WP_154616613.1|4069771_4070830_-|hypothetical-protein
MSTLQEPPLQVVAGPRTHGVVEYAAQLARALGAPSLVGPAEVLDGPVPDGPAHLHFTERLLGPTPAVAVRRAVGLCTRVPTTVTLHDVPQPWAGEERARAYAEVVRACAGWAVSSHHEADLVLRALARVGADRDVPPGVVVHLPVVPVQPRPTRGEGPDRDGPATLAALGFVYPDKGHRELLQAATELRARGHEVDVACLGSPVEGHADLLAELHRRARAGGVGLTVTGWLPDDELVAAMARADVPVSGHRHLSASASVNRWLAVGRRPLLLDGPYAREVDALRPGAHVLHDDAGLVPAIERALADPASTWLPEGAVPGPDLDASARQYAAWWASVHRAVPDPVPPVFVPFP
>NZ_CP053660.1|WP_171897072.1|4070826_4071753_-|sucrase-ferredoxin
MTTAPFRCSAASVERGEAPAGTASTVRAFLLIEHPGPWGVEALRDARLPDGLGPRIAAAAAAARVRPLLVRRPARTRGEGSAAGLRVIAASCLPGGTRLESGVLDDPHQVLDLDLVSLRAGGSSGLDPHDGTVLAVCTHGRHDACCAELGRPVAAALAAAHPEETWEVSHIGGDRYAGNLLLLPDGLYYGRLDPDAAIAVAAATARGHVELDHLRGRTAYPMAVQAAEVALRRALGETRRDAVRWTGRSVEGPATNPVTTAVFAVAGESWSVRVRTLAGPPARLTCRASRDDPTPRHEVEAVAREDAG
>NZ_CP053660.1|WP_154616612.1|4071749_4072913_-|cupin
MTLDDRTPVGGPHPALDLLSGDARTFLEKVWASRVHLHRTAPADLVGLLSLDDADHLLTSTAIRTPSVRLAQDGAVLAESSYTRSATLAGKQLTGLVDGRRALAAFADGATVVLQGLHRYHPPLTRLVAELELELGHPCQANAYLTPPGSQGFAVHADRHDVFVFQTAGTKQWEVHGPDGPEEVLLEPGLSMYLPTGTPHAARAQDTVSLHVTIGINQLTWRGLVRRTLEPLLAEVPDDHLPAGWLDDRGPVATGLADRLEALAARVREADAEAAAEREVRRFLSTRPPRLPGGLHDVLRVGSLTDETPLRRRAGHPCVLVPGAEGRVEVLLGDRVLDVPARVAPAIEEVRARGELRPADLAEHLDPQSRLVLCRRLVREGLLEVLP
>NZ_CP053660.1|WP_154616611.1|4072909_4073104_-|hypothetical-protein
MTTVPAGDPTMGLAESGDADGDATDSTDGDAGDADGTDSDGTDSDGTDSDGTDSDGTDSDGTDA

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Click the colored protein region to show detailed information

Crispr_ID: NZ_CP053660_10

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP053660_10

4209012-4209074

Orphan

Consensus_repeat	Method
CCGCTGGTTGAGCAGCCAAGGCC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP053660_10

>merge|NZ_CP053660|10|4209012-4209074|CRISPRCasFinder
CCGCTGGTTGAGCAGCCAAGGCCCGCACCGCCTGCTCGCACCGCTGGTTGAGCAGCGAAGGCC

>NZ_CP053660|10|10|4209012-4209074|CRISPRCasFinder
CCGCTGGTTGAGCAGCCAAGGCC	CGCACCGCCTGCTCGCA
CCGCTGGTTGAGCAGCGAAGGCC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP053660.1\|WP_154616570.1\|4202227_4202821_+\|DUF3558-family-protein	unknown	unknown	gnl\|CDD\|378803
NZ_CP053660.1\|WP_154616564.1\|4221441_4222209_+\|anti-sigma-factor	unknown	unknown	gnl\|CDD\|378389
NZ_CP053660.1\|WP_154616569.1\|4202868_4203714_+\|thioesterase-family-protein	unknown	unknown	gnl\|CDD\|379298
NZ_CP053660.1\|WP_171897101.1\|4200132_4200831_+\|response-regulator-transcription-factor	unknown	unknown	gnl\|CDD\|223816
NZ_CP053660.1\|WP_154612479.1\|4213899_4215165_+\|DUF222-domain-containing-protein	unknown	unknown	gnl\|CDD\|367155
NZ_CP053660.1\|WP_154612483.1\|4207041_4208967_-\|chorismate-binding-protein	unknown	unknown	gnl\|CDD\|223225
NZ_CP053660.1\|WP_154616565.1\|4220132_4220801_+\|fasciclin-domain-containing-protein	unknown	unknown	gnl\|CDD\|367095
NZ_CP053660.1\|WP_154612481.1\|4211628_4212636_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP053660.1\|WP_154616661.1\|4205208_4206378_-\|chorismate-binding-protein	unknown	unknown	gnl\|CDD\|223225
NZ_CP053660.1\|WP_171897100.1\|4197636_4199937_-\|PQQ-dependent-sugar-dehydrogenase	unknown	unknown	gnl\|CDD\|369642
NZ_CP053660.1\|WP_154616568.1\|4215881_4217555_-\|molybdopterin-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|239028
NZ_CP053660.1\|WP_154612480.1\|4212894_4213644_-\|enoyl-CoA-hydratase/isomerase-family-protein	unknown	unknown	gnl\|CDD\|236109
NZ_CP053660.1\|WP_154616571.1\|4200827_4202231_+\|HAMP-domain-containing-protein	unknown	unknown	gnl\|CDD\|223715
NZ_CP053660.1\|WP_154612482.1\|4209233_4211459_-\|AAA-family-ATPase	unknown	unknown	gnl\|CDD\|226482
NZ_CP053660.1\|WP_171897103.1\|4220840_4221440_+\|ECF-RNA-polymerase-sigma-factor-SigK	unknown	unknown	gnl\|CDD\|182015
NZ_CP053660.1\|WP_154612489.1\|4196760_4197633_+\|fructosamine-kinase-family-protein	unknown	unknown	gnl\|CDD\|225547
NZ_CP053660.1\|WP_154616566.1\|4218985_4220005_+\|DUF21-domain-containing-protein	unknown	unknown	gnl\|CDD\|224173
NZ_CP053660.1\|WP_171897102.1\|4206467_4207037_-\|aminodeoxychorismate/anthranilate-synthase-component-II	unknown	unknown	gnl\|CDD\|153214
NZ_CP053660.1\|WP_154612484.1\|4203742_4205266_-\|glucose-6-phosphate-dehydrogenase	unknown	unknown	gnl\|CDD\|237234
NZ_CP053660.1\|WP_154616567.1\|4217627_4218986_+\|DUF21-domain-containing-protein	unknown	unknown	gnl\|CDD\|224173

Protein	Function_ID	Function_description	E-value
NZ_CP053660.1\|WP_154616570.1\|4202227_4202821_+\|DUF3558-family-protein	gnl\|CDD\|378803	pfam12079, DUF3558, Protein of unknown function (DUF3558). This family of proteins is functionally uncharacterized. This protein is found in bacteria. Proteins in this family are typically between 177 to 195 amino acids in length.	2.50895e-06
NZ_CP053660.1\|WP_154616564.1\|4221441_4222209_+\|anti-sigma-factor	gnl\|CDD\|378389	pfam10099, RskA, Anti-sigma-K factor rskA. This domain, formerly known as DUF2337, is the anti-sigma-K factor, RskA. In Mycobacterium tuberculosis the protein positively regulates expression of the antigenic proteins MPB70 and MPB83.	1.96857e-25
NZ_CP053660.1\|WP_154616569.1\|4202868_4203714_+\|thioesterase-family-protein	gnl\|CDD\|379298	pfam13622, 4HBT_3, Thioesterase-like superfamily. This family contains a wide variety of enzymes, principally thioesterases. These enzymes are part of the Hotdog fold superfamily.	2.69841e-17
NZ_CP053660.1\|WP_171897101.1\|4200132_4200831_+\|response-regulator-transcription-factor	gnl\|CDD\|223816	COG0745, OmpR, Response regulators consisting of a CheY-like receiver domain and a winged-helix DNA-binding domain [Signal transduction mechanisms / Transcription].	2.98288e-84
NZ_CP053660.1\|WP_154612479.1\|4213899_4215165_+\|DUF222-domain-containing-protein	gnl\|CDD\|367155	pfam02720, DUF222, Domain of unknown function (DUF222). This family is often found associated to the N-terminus of the HNH endonuclease domain pfam01844. The function of this domain is uncertain. This family has been called the 13E12 repeat family.	1.34564e-23
NZ_CP053660.1\|WP_154612483.1\|4207041_4208967_-\|chorismate-binding-protein	gnl\|CDD\|223225	COG0147, TrpE, Anthranilate/para-aminobenzoate synthases component I [Amino acid transport and metabolism / Coenzyme metabolism].	6.49678e-49
NZ_CP053660.1\|WP_154616565.1\|4220132_4220801_+\|fasciclin-domain-containing-protein	gnl\|CDD\|367095	pfam02469, Fasciclin, Fasciclin domain. This extracellular domain is found repeated four times in grasshopper fasciclin I as well as in proteins from mammals, sea urchins, plants, yeast and bacteria.	3.59509e-32
NZ_CP053660.1\|WP_154616566.1\|4218985_4220005_+\|DUF21-domain-containing-protein	gnl\|CDD\|224173	COG1253, TlyC, Hemolysins and related proteins containing CBS domains [General function prediction only].	1.86937e-71
NZ_CP053660.1\|WP_154616661.1\|4205208_4206378_-\|chorismate-binding-protein	gnl\|CDD\|223225	COG0147, TrpE, Anthranilate/para-aminobenzoate synthases component I [Amino acid transport and metabolism / Coenzyme metabolism].	4.11655e-106
NZ_CP053660.1\|WP_171897100.1\|4197636_4199937_-\|PQQ-dependent-sugar-dehydrogenase	gnl\|CDD\|369642	pfam07995, GSDH, Glucose / Sorbosone dehydrogenase. Members of this family are glucose/sorbosone dehydrogenases that possess a beta-propeller fold.	7.3848e-21
NZ_CP053660.1\|WP_154616568.1\|4215881_4217555_-\|molybdopterin-dependent-oxidoreductase	gnl\|CDD\|239028	cd02110, SO_family_Moco_dimer, Subgroup of sulfite oxidase (SO) family molybdopterin binding domains that contains conserved dimerization domain. This molybdopterin cofactor (Moco) binding domain is found in a variety of oxidoreductases, main members of this family are nitrate reductase (NR) and sulfite oxidase (SO). .	3.0735e-61
NZ_CP053660.1\|WP_154612480.1\|4212894_4213644_-\|enoyl-CoA-hydratase/isomerase-family-protein	gnl\|CDD\|236109	PRK07827, PRK07827, enoyl-CoA hydratase family protein.	9.97049e-85
NZ_CP053660.1\|WP_154616571.1\|4200827_4202231_+\|HAMP-domain-containing-protein	gnl\|CDD\|223715	COG0642, BaeS, Signal transduction histidine kinase [Signal transduction mechanisms].	1.08823e-56
NZ_CP053660.1\|WP_154612482.1\|4209233_4211459_-\|AAA-family-ATPase	gnl\|CDD\|226482	COG3973, COG3973, Superfamily I DNA and RNA helicases [General function prediction only].	8.3432e-59
NZ_CP053660.1\|WP_154612489.1\|4196760_4197633_+\|fructosamine-kinase-family-protein	gnl\|CDD\|225547	COG3001, COG3001, Uncharacterized protein conserved in bacteria [Function unknown].	1.40435e-59
NZ_CP053660.1\|WP_171897103.1\|4220840_4221440_+\|ECF-RNA-polymerase-sigma-factor-SigK	gnl\|CDD\|182015	PRK09646, PRK09646, ECF RNA polymerase sigma factor SigK.	3.1915e-89
NZ_CP053660.1\|WP_171897102.1\|4206467_4207037_-\|aminodeoxychorismate/anthranilate-synthase-component-II	gnl\|CDD\|153214	cd01743, GATase1_Anthranilate_Synthase, Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase. Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase (ASase). This group contains proteins similar to para-aminobenzoate (PABA) synthase and ASase. These enzymes catalyze similar reactions and produce similar products, PABA and ortho-aminobenzoate (anthranilate). Each enzyme is composed of non-identical subunits: a glutamine amidotransferase subunit (component II) and a subunit that produces an aminobenzoate products (component I). ASase catalyses the synthesis of anthranilate from chorismate and glutamine and is a tetrameric protein comprising two copies each of components I and II. Component II of ASase belongs to the family of triad GTases which hydrolyze glutamine and transfer nascent ammonia between the active sites. In some bacteria, such as Escherichia coli, component II can be much larger than in other organisms, due to the presence of phosphoribosyl-anthranilate transferase (PRTase) activity. PRTase catalyses the second step in tryptophan biosynthesis and results in the addition of 5-phosphoribosyl-1-pyrophosphate to anthranilate to create N-5'-phosphoribosyl-anthranilate. In E.coli, the first step in the conversion of chorismate to PABA involves two proteins: PabA and PabB which co-operate to transfer the amide nitrogen of glutamine to chorismate forming 4-amino-4 deoxychorismate (ADC). PabA acts as a glutamine amidotransferase, supplying an amino group to PabB, which carries out the amination reaction. A third protein PabC then mediates elimination of pyruvate and aromatization to give PABA. Several organisms have bipartite proteins containing fused domains homologous to PabA and PabB commonly called PABA synthases. These hybrid PABA synthases may produce ADC and not PABA.	1.47156e-78
NZ_CP053660.1\|WP_154612484.1\|4203742_4205266_-\|glucose-6-phosphate-dehydrogenase	gnl\|CDD\|237234	PRK12854, PRK12854, glucose-6-phosphate 1-dehydrogenase; Provisional.	0
NZ_CP053660.1\|WP_154616567.1\|4217627_4218986_+\|DUF21-domain-containing-protein	gnl\|CDD\|224173	COG1253, TlyC, Hemolysins and related proteins containing CBS domains [General function prediction only].	1.56493e-97

>NZ_CP053660.1|WP_154612483.1|4207041_4208967_-|chorismate-binding-protein
MTSTPNARDAIAALQGHEAWAIIRRSTRAGDRDSVGLVGGKRSVVESLLDVPLEEGVPEAGHIADRLLAVPFRQVAERGFEAHDDGTPLVVVDVETELEFSVAEVVEAIDEVEVTFADRGGFETDDEEYGRLVEAIIRDEIGQGEGANLVVGRHYRAKVDAWGAEAALAVFRRLLERERGAYWTFLFFTGDRYLIGASPERHVSIHGGDVRMNPISGTFRIPREPDADVKGGLLEFLRDEKEIYELFMVVDEELKMMCDICNQGGQVLGPFLKPMSRLVHTEYLLAGRTDRDPREVLRDTMYAATVTGSPVENACRLIKAYETEGRGYYGAALAVLGRDPEGGPVVDSPIVIRTADVDLDGNLKVTAGATLVRDSDAAYEVAETHAKAGGILSAFGLVPAAPTPDVNVAELVNDEDVLLALNARNRRLSSFWLTDQGGSAPDPRLAGRSAVILDGEDDFVNMLRHVLGVLGMTSTVVRHEEYVAGCLDGFDLVIVGPGPGDPRDDADPKMANLRAAVAELLAKERPFLAVCLGHQALCHELGIPLAYKDIVFQGTQSPVTLEGRTERVGFYNTFVGRVGDGDALPEGVRVDTDPATGDVHHLAGPHYRGIQFHAESILTERGYDLLHDYVVALLLDRPGDA
>NZ_CP053660.1|WP_171897102.1|4206467_4207037_-|aminodeoxychorismate/anthranilate-synthase-component-II
MAPDVVVVDHHDSYTWNLVDLLAQVTGALPRVVQHDEVTAAEVLAHERVVLSPGPGRPDDPADFGVGREVLRAATRPVLGVCLGMQGLVAAYGGRVERVEPAHGVVAHVTHDGRGVLAGLPQGFAAVRYHSLAATVVPDCLEVTARCEDGTVMGVRHRTLPLEGVQFHPESVLSEHGLRIVASFLAGPT
>NZ_CP053660.1|WP_154616661.1|4205208_4206378_-|chorismate-binding-protein
MLGWLTDDDVSLSYAAATRTVTRHAGGRSEVVAEGADVFAVLEAELAAGSPEDQWFGYLGYACRPDLPARPAQGVPDAVWMRPSHVRRVAPAGSAPAAARTVPPAAAPAPGWYVEAFEKVQEALRGGHSYEVNLTHRERVADAVDPVTAYLRLRALNPAPYAGFLQHDVPGARAWLLSSSPERYAAVTADPGGGRTLETRPIKGTTPRGTTPAEDAAAAERLRTEQRYRAENLMVVDLLRNDVASVCAPGSVEVPALMEVESYATVHQLVSTVRGRLRPEVSTVGALRALFPAGSMTGAPKRRTMEVIDAVEATPRGVYAGAFGRVAADGTADLGVVIRSLVTAGDGSWELGTGGGVTVHSDVGSEHAEARWKAERLLAVFADRGGNPP
>NZ_CP053660.1|WP_154612484.1|4203742_4205266_-|glucose-6-phosphate-dehydrogenase
MEGGAAPRRLRGPRRQPPVSTVESLAKPHVIVLFGATGDLSRRKLLPGLLHLFEAGLLADTRIVGTSLEEVDTAHFESFAREACEEFGDGTIDDARWAPFGNLLSYLPQSAGPQALADEVARAEETLPGPEERKRRLHYLSVPPKAALDVVHQLDKAGLVERSRIVMEKPFGTDLASAVNLNAELHEVFDEQQIFRIDHFLGKEAAQNILAFRFANGLFEPIWNRNFIDHVQIDVPETLGLEGRTKFYESTGAYRDMVVTHLMQVLAFMAMEPPTSLEPDPISDEKNKVFRSMKAIDPHDVVRGQYAGYRGKEEVADDSDTETFIALKVEIDNWRWAGVPIYLRTGKKLAESARIISIAFKEPPLSMFPAGSQAGMQGPDHLTFDLADQSRMSLSFYGKRPGPGMKLEKLSMQFATHETSSSTAVLAAYERLIHDAMRGDHTLFTTAEGIETLWEKSTALLETPPPVRTYQPGTWGPNAIHQLVAPNAWRLPFERGWRTPAPDGTDA
>NZ_CP053660.1|WP_154616569.1|4202868_4203714_+|thioesterase-family-protein
MELAFFTSDDGENLVATDLAVSSWGSDHLHGVAVSGAMARALEQRIEAEGRTDLHPARYTADLFRPAGRAPMTFTTDVVRVGPRLALIDVVAHQEGRAVARASALFLKPTGSTEGEVWSPGGHPSPPPEDVAPPTTEPHVPFLHSDAGWSQDFREHQNASRKTSWNSAVPVVAGEPATAFQAAAAIADGASLVTNWGTRGVEHINTDITLTLVRRPAGTEIGLQAVDRLEQDGIAVGTASVFDREGPLGTIVLTSLANARRTVDLGKEQWEDDGRRTTSGA
>NZ_CP053660.1|WP_154616570.1|4202227_4202821_+|DUF3558-family-protein
MRRALLAAPLVPLLLLAGCGSGDADSGNGGGSGEAGASSPHGGSDPGTGASTPVASWNPCDDLTAAEVGRLLGEEVREEVGEPGAMRCTFVPVAEGGATIDVNYLWFDGSFAEAWDSIGADVAGKVRDVDVPTAEAARTVEQVTDDAAVVTGFVQTGGLIESVNAIVLDPDERDRLVRATRGMLRLLSERAPERAAD
>NZ_CP053660.1|WP_154616571.1|4200827_4202231_+|HAMP-domain-containing-protein
MSRLLRSLAGRVTLLTTIAVGLAVAFVAVGAFMTVRVQLQSTLDNSLLERAHAAAKYPLLSELTNDYQLPSWALGAADVRIAFVYSDGSYRTYDQLPPMQLDAERDVATGDRDWTARTIYAGGRDYRVVAVPAGKGGALVVAQSLEPQQQVLARLGVVMLVFGLLGVVAAGVAGWAVARNGLRPVRRLTSEVEAIARTEDLDPIEVEGDDEVARLATAFNEMLTALAASRDRQRRLVADAGHELRTPLTSLRTNIELLTQADAETAGVLPEGARAELLADVHAQIEELTTLIGDLVELSRDDEAAHVVAPVDLAEVVDQALARVRRRAPGLEFDVAVEPFEVVGDSAALERAVTNLLDNAAKWSPPGGTVTVRLAGGVLTVDDEGPGISEEDRPHVFDRFWRAEESRGMPGSGLGLSIVARVADRHAGTVEVDRSPAGGARFVLTLPAPAPAAPPPSGAHLWTGGRG
>NZ_CP053660.1|WP_171897101.1|4200132_4200831_+|response-regulator-transcription-factor
MPPTAKPRVLVVDDDKAVRESLRRSLEFNGYEVATANDGAEALAAIGRVSPDVVVMDVMMPRLDGIEATRALRAAGNDVPVLVLTARDAVGDRVEGLDAGADDYLTKPFALAELLARLRALLRRVVPAEDDPDEVLSFADLSMDVATREVRRGDRLIELTRTEFTLLEMFLRRPRRVLERSFILEEVWGYDFPTTANSLEVYVGYLRRKTEAEGEPRLIHTVRGVGYVLKEA
>NZ_CP053660.1|WP_171897100.1|4197636_4199937_-|PQQ-dependent-sugar-dehydrogenase
MTTPAPAAPAPGETAADQQRVVVPARAADPVLPDRFQEEVVLGGLDQPTAVDFGPAGEIFVADKAGVVRVWESPEAQPVQVVDLSTEVHNLYDRGLLGLAVDPGFPERPYLYVLYAYDHVLGSAEPAPRWGVPGVSYDDCPDPEDGGPGAEDMGCVASGRLSRLTLAKVPGGWRASGEKRVMLEGWCMQYPSHATGSLHVGPDGHLWASGGEGAHYLEVDRGQLGAPYWPGGNPCGDPAREGGSLRAQDVRTTGDPTGLSGAVVRIDLETGEGVPGNPFAGRAEENARRIVAYGMRNPFRFAFRPGTGGTDPEVYVGDVGQGGWEEINRLRPGGPAENFGWPCFEGPDRNAGFDPLDLPLCESLYRDGSAAQPFYAYPRTGAIAGESCPTGSASISGLQFGASATYPSAYRGALFFSDYSRQCIWVMGKRADGSPDPRSVRPFLEGAASPVELLTGPEGDLYYLSLGVDAQGYPAAGAGSLRRVRYVAGNRPPEARIESRTPVWGPSPLDVVLDASVSTDAEDDILGYRWDLDGDGEFDDADSPEVYTTVTGAEDVTVRVRVTDGNGGEDIGAIVLHPGDAGPPVLTIASPARDLRWAVGDRIPLAATATDPDGTEPTVTWSVALAHCPNDVCHTHPLQTAVPGDTLVRAPDHEHPSYLLVSATATDGRGLSTTESFRLDPRTVRLRFRTKPGGLPLSIAGVRRAKTWTGTFIVGSRVTVTAPKRHRRDRARFVFKRWSDGGRRTHTYVAPARPATLTAVYRRQKK
>NZ_CP053660.1|WP_154612489.1|4196760_4197633_+|fructosamine-kinase-family-protein
MARQPLVARRAEGLLGAAVVATAPVAGGDTATATKLRLSNGTTALMKTMPHAPADFFEAEARGLRWLGEVEGGARVPEVLGVDSECLVMRWIEPGKQTADAAADLGRALAATHAAGAAAYGAGPGGEHRDTYIARLPLPNRPAPTWAEFYAVRRVLPYLKLARDRGAMTDEQAATVESVVGKLPALLPEEGPARLHGDLWNGNVVWGVDGVHLVDPAAYGGHREMDLAMLSLFGLPHLPKMIEAYAEVTPLTEGWEDRLALHQLFPLLVHACLFGGGYGPRAAAAAARYR
>NZ_CP053660.1|WP_154612482.1|4209233_4211459_-|AAA-family-ATPase
MSEAAAASQHDQQDQHVAEREVAAEQAFVDRVYRQLSESADAARQLAQEGHQRGRLGHEGGLVERDAMVFQAAKRIAQLDAAHEGLVFGRLDLEPEVDTAPRYVGRIGLRDADRDSLLIDWRAPAAAVFYQATAAEPHHVIRRRVLRCTGPQVVGVEDELLDADALERSGLDLPIVGEGALMAQLSRARDRSMHSIVATIQAEQDKAIRAPSKGVVTISGGPGTGKTVVALHRAAFLLYTERRRYETGGVLVVGPSGVFMRYIERVLPSLGETAVALRSLGEVVDGVRATRHDEPAVADVKGAARMAELMRRTARQQAPGSPTEFRIFYRDDTIVLDRGLLGRLRRQLMSQGRRNKQLPRVAPTLLDAMWRQVRGERGRDRGRESFQEEMLSDQRFVDFAVAWWPPLDAPTVLGWLRDPDILARVGEGVVSAEEQRLLLKSWSGASDLSVADVALLDELRYALGDVPAKPEDDRDDPLAVIEGAVDLQELTTAADREYAPSGRAWAPPQHRIEDDGFAHVLVDEAQDLTPMQWRMVGRRGRAASWTIVGDPAQSSWPVREEAEAARAEALEGKRIHSFHLSTNYRNSAEIYAYAEAYARRVGLDADLPTAVRSTGVEPVEVTGVADLEAATREAVVDVAGRVGGTVGIVVPVARRSEVNSWLASWPELADAAPSARAAVDSSVTPSGEDRVVVLTGLDTKGLEFDGIVVVRPQEIEDESLTGRATLYVVLTRATQLLTTIS
>NZ_CP053660.1|WP_154612481.1|4211628_4212636_+|hypothetical-protein
MTAGAGDGADGPGGARWLRRARVAGAVAVVAALAVAVPLAPRWVEASRPEAPLAAPGTVEVSTECRTRADGGLDHPDFLLGDASWARFCVVGGSYPRPIGSALVPDTVLSDGAAALVGGWQRSEGPVGPCRPTPSATKFAVQVGFDDGTVAEVYGETSECAAYTRPGPGTRVVPGGRVFRELMTALALEESGGSGGAGGSVAPAPSPTCPAAPPALPSAITRRPATGLAATGVAEAVVCRYDRPGADPVGTPLRPTEAERVRLLALGAFDPTPPACTPDPGAASYVVLLAGHDGATYDLGLAGGDCDAVRLDDQRLGTSPALATALAGLAAGTGS
>NZ_CP053660.1|WP_154612480.1|4212894_4213644_-|enoyl-CoA-hydratase/isomerase-family-protein
MSDELVHYAVADDVATITLDSPHNRNALSGQLVRELGERLEQAESDPAAKVVLVRAEGTVFCSGADLSEASAAGSEDAPRGIVRLQRLMVGSTKPVVLRLQGAVRAGGIGLVAAADVVVANEDATFALTEVKLGLAPAVISLTVLPRLTSRAAAYTFLTGETFTGTEAERMGLVTRAVPAAELDAEVARVCASLATGAVQGLRETKALLAHDLLERIDRLGDDVAAQSARLFGSAEAREAMTAFLSRKK
>NZ_CP053660.1|WP_154612479.1|4213899_4215165_+|DUF222-domain-containing-protein
MAKDSRHHAHTVCRAVAKSRRKTRQAATADLWSMSDEDVEATILEAEKLRAQADALALRLVAEADRRHAGERAGATDTAAWWAHRTRQERRVAKGRARLAESLDRHAPTSAALVEGAISVDHARVITSCVDRLPDDLEDPTVPARAEQHLLDEAAHLDPKTLAVLAKHVLTVVAPEIGEARDARALEREEREARANAWLTMCPDGKGSVRGKFSIPELHAAMLHKTLLAYAAPKHQTATRTEDPEAEQVERRPSPERMGDAFCEFLERLPTDGLPKLGGLNATVVVTMDLESLVGGLAPGVLDDGGVISAATARRLACEAGLIPAVLGSRSELLDLGRRTRLFSGAQRRGLNLTQPTCTADGCDWPAHLCHAHHDQPWSHGGTTDLANARNLCPRHHARIHDPAFETTHLPDGKVAFHRRT
>NZ_CP053660.1|WP_154616568.1|4215881_4217555_-|molybdopterin-dependent-oxidoreductase
MVLGQRPVRGPSSWPPRGRAWAASQSGHSVRGEVRSERLPVNRLLAALSGVLATLAGVAAGHLAAALLDPATSPVLAVGSQVIDLTPTPVKEWAISQFGTRDKPILIGSVLVGVVLLAAVAGLLARRRFAYGAAVFVLLVAVPAVIAVTRPTAGVSAVAPSLVALVVGLAALAWLVRAAAPAAVGGRVGAPAEDRVEDRPGEAGGPSRRGLLVAMGVVAGAAAVLGGAGRWVASYRTRAVAIDLPAAAKPLPPLPEGLEERFAGITPLQVANSDFYRVDTRLDVPIVDVEEWTLTIDGDVEEEVTFTLDDILAMDLVEKDITLTCVSNSVGGEFVGGARWLGVPLNELLDRAGVGTRADQILSTDVDGMTISTPLALATDGRDALLAVGMNGEQLPREHGFPARMVIPGLYGFISATKWVTRMTLTTYDAETAYWTDRDWATEAPIKPSSRIDTPRALAPLDVGEVVVGGVAWAQQNGGVGTVQVRIDGGPWQDAELGPDVGNDYWRQWFYRWDAASGQHRIASRVVDGDGGPQSPARANPFPEGSSGIQELIVTVG
>NZ_CP053660.1|WP_154616567.1|4217627_4218986_+|DUF21-domain-containing-protein
MTPLLSLLLGLLVVLAITAVTGYFVAQEFAYMAVDRSRLKARAAAGDATARRALKVTRRTSFMLSGAQLGITVTGLLVGYVAEPLIGDSLGTMLGGVGVPTAVGVGVGTVLALVFSTFVQMLFGELFPKNLAIARPGPVADRLAFSTLAYLKATGPLIWVFDQSSNLLLRALRIEPVHDVEHSATARDLEHIVADSREAGDLPEELSVLLDRILDFPTRDVEHAMVPRPRVGTVPEGTPVADVRRLMATGHSRYPVLDAAGGVLGVVHLADVLDAPAGAQLADLTRPALVVPTRMALPDALEELVHSRNELAAVIDEHGGFVGALTVEDLAEELVGELTDEHDEQVRVVLDDAGGSWLVAGDQPLDEVERTLDQDLPTGDYQTLAGLVIAEHGRLPEVGTVVDIRLPDDPADLVHEGEPHARHARMEVVEVEQHVPALLRITLVPAGTGEES
>NZ_CP053660.1|WP_154616566.1|4218985_4220005_+|DUF21-domain-containing-protein
MENPIVVAVATVLIIAASAFFVAVEFALMAAKKHRLEDAAASSRSARAALRSSSELTVLLAGSQLGITISVLALGAITKPAVHHWLTPVFEGWGAALWLADVAGFVLALVVVTFLHLVVGEMAPKSWAIAHPERSATMLAIPMRAFMWATRPMLRLLNDAANWCLRRVGVDPVDEMAAGQDPAALRQLVEHSANVGALDASYSAQLSGALDLETLTIGELVRPAPPTAVPATARVADVQAASRRSGHLRILVADGDDAIGLVHVRDTLEEPEDAPLGPLTRPLLRLPADTTVYAALARMRETSNQLAVVTDLGGPPRLPGVVTVADLLRRLLPMADQRA
>NZ_CP053660.1|WP_154616565.1|4220132_4220801_+|fasciclin-domain-containing-protein
MKLQTLRRTGVAAAAISLSLGLAACSSEDDSDSASDGSSSSAAESPSETMSSPSEEETMAAEGAAAQTFGDACSAVPADGPGSFDGMVQDPVATAASNNPLLETLVTAVGAVDGLGDTLNSAEALTVFAPTNDAFAAIPEKQLQALLKDQKKLGAILSHHVVAGQLDPEAVVGKQDTLNKDTITVEGDTSGMTVDGATVLCGNIPTANATVYVIDQVLMPQG
>NZ_CP053660.1|WP_171897103.1|4220840_4221440_+|ECF-RNA-polymerase-sigma-factor-SigK
MEHLRPVAPGGPAEGSPVAPDLADLLRAAGRGDQQAFAQLYDATCSRVVGMAVRVVRDPAQAEEVAQEAFLEIWRTASRYDPDRGSPLSWLLTITHRKAVDRVRSAEASTRRDQNYHHQNQPVPHDATAEAAHASLEARRVRTALGSLTPVQREALELAYFGGYTHTEVATMLELPVGTAKTRIRDGLIRLRDTMGVGS
>NZ_CP053660.1|WP_154616564.1|4221441_4222209_+|anti-sigma-factor
MSDDIHALSGAYAVDALDDIERAQFERHLAGCEACREEVDGLRETAALLAETTMTTPSAELRDRVLAGIATVRPLPPVVPPHAPTGEGLPASPAPTTPSTRGPRRRWLTMVAAAAAVMAVGVGGTVVAQQPWSEDSSEAPRLSAVDRIKAADDVQTFRHRFPDGAEAVLYRSPSLNEAVVVTHDMGPAPDGKVYQAWLQHDDTMVSAGLMPEGPDNVVPLQGDPATADGFGITVEPAGGSVVPSKEKPVLLVEFT

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Self-targeting detection

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_ID	Protospacer_location	Mismatch	Identity
NZ_CP053660_8	8.1\|4028118\|32\|NZ_CP053660\|CRISPRCasFinder	4028118-4028149	32	NZ_CP053660.1	3809223-3809254	2	0.938

1. spacer 8.1|4028118|32|NZ_CP053660|CRISPRCasFinder matches to position: 3809223-3809254, mismatch: 2, identity: 0.938

actcccctcggtgagctcaccgtgggaagtga	CRISPR spacer
actcccctcggtgagctcaccctggggagtga	Protospacer
********************* ****.*****

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity
NZ_CP053660_8	8.1\|4028118\|32\|NZ_CP053660\|CRISPRCasFinder	4028118-4028149	32	NZ_AP017656	Sphingobium cloacae strain JCM 10874 plasmid pSCLO_2, complete sequence	238970-239001	8	0.75
NZ_CP053660_8	8.1\|4028118\|32\|NZ_CP053660\|CRISPRCasFinder	4028118-4028149	32	NZ_CP018821	Sphingomonas koreensis strain ABOJV plasmid tig00000001, complete sequence	110508-110539	8	0.75

1. spacer 8.1|4028118|32|NZ_CP053660|CRISPRCasFinder matches to NZ_AP017656 (Sphingobium cloacae strain JCM 10874 plasmid pSCLO_2, complete sequence) position: , mismatch: 8, identity: 0.75

actcccctcggtgagctcaccgtgggaagtga	CRISPR spacer
gtgccccgcggtgagctcagcgtgggagagga	Protospacer
.. **** *********** *******.. **

2. spacer 8.1|4028118|32|NZ_CP053660|CRISPRCasFinder matches to NZ_CP018821 (Sphingomonas koreensis strain ABOJV plasmid tig00000001, complete sequence) position: , mismatch: 8, identity: 0.75

actcccctcggtgagctcaccgtgggaagtga	CRISPR spacer
gtgccccgcggtgagctcagcgtgggagagga	Protospacer
.. **** *********** *******.. **

Prophage detection

Region	Region Position	Protein_number	Hit_taxonomy	Key_proteins	Att_site	Prophage annotation

Anti-CRISPR protein detection

Acr ID	Acr position	Acr size	Homology with known anti	Neighbor HTH/AcRanker	Neighbor Aca	In prophage	Protospacer in prophage