CRISPRimmunity

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_CP012897	Brevundimonas sp. DS20, complete genome	3 crisprs	DinG,csa3,DEDDh,WYL	0	2	2	0

1. NZ_CP012897

CRISPR-Cas detection and classification

Crispr_ID: NZ_CP012897_1

• CRISPR_ID: NZ_CP012897_1
• CRISPR_location: 963863-963954
• CRISPR_type: Orphan
• Repeat_type: NA
• Spacer_info: 1 spacers
• Cas_protein_info: csa3

Consensus repeat of NZ_CP012897_1

Consensus_repeat	Method
GGCTCGCTGCTTGAGCGCGGAAGGG	CRISPRCasFinder

spacers of NZ_CP012897_1

>1.1|963888|42|NZ_CP012897|CRISPRCasFinder
CGCTACGCTCGCGATGCGTTCCCGCCTTCGCGGGAATGACGA

CRISPR arrays and Neighbor proteins around NZ_CP012897_1

CRISPR arrays

The CRISPR arrays of NZ_CP012897_1

>merge|NZ_CP012897|1|963863-963954|CRISPRCasFinder
GGCTCGCTGCTTGAGCGCGGAAGGGCGCTACGCTCGCGATGCGTTCCCGCCTTCGCGGGAATGACGAGGCTCGCTGCTTGAGCGCGAAGGGG

>NZ_CP012897|1|1|963863-963954|CRISPRCasFinder
GGCTCGCTGCTTGAGCGCGGAAGGG	CGCTACGCTCGCGATGCGTTCCCGCCTTCGCGGGAATGACGA
GGCTCGCTGCTTGAGCGCGAAGGGG

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP012897.1|WP_054764617.1|960418_961291_-|isoaspartyl-peptidase/L-asparaginase	unknown	unknown	gnl|CDD|271337
NZ_CP012897.1|WP_054764619.1|962593_962992_-|DUF1232-domain-containing-protein	unknown	unknown	gnl|CDD|225876
NZ_CP012897.1|WP_054764615.1|956078_956519_+|DUF350-domain-containing-protein	unknown	unknown	gnl|CDD|226289
NZ_CP012897.1|WP_054764620.1|963047_963830_+|SDR-family-oxidoreductase	unknown	unknown	gnl|CDD|187629
NZ_CP012897.1|WP_054764616.1|956538_957369_+|trypsin-like-peptidase-domain-containing-protein	unknown	unknown	gnl|CDD|379142
NZ_CP012897.1|WP_054764623.1|965212_966751_+|deoxyribodipyrimidine-photo-lyase	unknown	unknown	gnl|CDD|225588
NZ_CP012897.1|WP_054764628.1|968710_969430_-|heme-ABC-transporter-permease	unknown	unknown	gnl|CDD|273492
NZ_CP012897.1|WP_054764618.1|961432_962434_+|NADPH:quinone-oxidoreductase-family-protein	unknown	unknown	gnl|CDD|176203
NZ_CP012897.1|WP_054764612.1|954216_954678_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP012897.1|WP_054764625.1|967603_967858_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP012897.1|WP_054764621.1|964243_964705_-|DUF3429-family-protein	unknown	unknown	gnl|CDD|378761
NZ_CP012897.1|WP_054764629.1|970191_970815_-|heme-ABC-exporter-ATP-binding-protein-CcmA	unknown	unknown	gnl|CDD|226617
NZ_CP012897.1|WP_054764627.1|968490_968709_-|heme-exporter-protein-CcmD	unknown	unknown	gnl|CDD|377440
NZ_CP012897.1|WP_054764622.1|964852_965209_+|DUF393-domain-containing-protein	unknown	unknown	gnl|CDD|367833
NZ_CP012897.1|WP_082382595.1|957473_960341_-|insulinase-family-protein	unknown	unknown	gnl|CDD|223685
NZ_CP012897.1|WP_082382596.1|969487_970195_-|heme-exporter-protein-CcmB	unknown	unknown	gnl|CDD|200083
NZ_CP012897.1|WP_054764613.1|954674_955586_-|acyl-CoA-desaturase	unknown	unknown	gnl|CDD|239582
NZ_CP012897.1|WP_054764626.1|967927_968494_-|DsbE-family-thiol:disulfide-interchange-protein	unknown	unknown	gnl|CDD|239308
NZ_CP012897.1|WP_054764614.1|955676_956009_+|winged-helix-turn-helix-transcriptional-regulator	csa3	COG0640_csa3_CAS-I-A	gnl|CDD|238042
NZ_CP012897.1|WP_054764624.1|966832_967603_+|M48-family-metallopeptidase	unknown	unknown	gnl|CDD|320690

HMMScan for Signature genes

Protein	Cas_name	Cas_description	E-value	Identity	Coverage
NZ_CP012897.1|WP_054764614.1|955676_956009_+|winged-helix-turn-helix-transcriptional-regulator	csa3	COG0640_csa3_CAS-I-A	1.2e-19	65.6	0.0

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
NZ_CP012897.1|WP_054764617.1|960418_961291_-|isoaspartyl-peptidase/L-asparaginase	gnl|CDD|271337	cd04701, Asparaginase_2, Bacterial/fungal L-Asparaginase type 2. L-Asparaginase hydrolyzes L-asparagine to L-aspartate and ammonia. The proenzyme undergoes an autoproteolytic cleavage into alpha and beta subunits to expose a threonine residue which becomes the N-terminal residue of the beta subunit. The threonine residue plays a central role in hydrolase activity. Some asparaginases can also hydrolyze L-glutamine and are termed glutaminase-asparaginase. This is a member of the Ntn-hydrolase superfamily, and this subfamily covers mostly bacterial and fungal enzymes.	7.74575e-102
NZ_CP012897.1|WP_054764619.1|962593_962992_-|DUF1232-domain-containing-protein	gnl|CDD|225876	COG3339, COG3339, Uncharacterized conserved protein [Function unknown].	6.37178e-29
NZ_CP012897.1|WP_054764615.1|956078_956519_+|DUF350-domain-containing-protein	gnl|CDD|226289	COG3766, COG3766, Predicted membrane protein [Function unknown].	1.60571e-32
NZ_CP012897.1|WP_054764620.1|963047_963830_+|SDR-family-oxidoreductase	gnl|CDD|187629	cd05371, HSD10-like_SDR_c, 17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs. HSD10, also known as amyloid-peptide-binding alcohol dehydrogenase (ABAD), was previously identified as a L-3-hydroxyacyl-CoA dehydrogenase, HADH2. In fatty acid metabolism, HADH2 catalyzes the third step of beta-oxidation, the conversion of a hydroxyl to a keto group in the NAD-dependent oxidation of L-3-hydroxyacyl CoA. In addition to alcohol dehydrogenase and HADH2 activites, HSD10 has steroid dehydrogenase activity. Although the mechanism is unclear, HSD10 is implicated in the formation of amyloid beta-petide in the brain (which is linked to the development of Alzheimer's disease). Although HSD10 is normally concentrated in the mitochondria, in the presence of amyloid beta-peptide it translocates into the plasma membrane, where it's action may generate cytotoxic aldehydes and may lower estrogen levels through its use of 17-beta-estradiol as a substrate. HSD10 is a member of the SRD family, but differs from other SDRs by the presence of two insertions of unknown function. 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 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 (15-PGDH) numbering). 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) 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. Extended SDRs have additional elements in the C-terminal region, 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. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.	4.58617e-113
NZ_CP012897.1|WP_054764616.1|956538_957369_+|trypsin-like-peptidase-domain-containing-protein	gnl|CDD|379142	pfam13365, Trypsin_2, Trypsin-like peptidase domain. This family includes trypsin-like peptidase domains.	4.79772e-15
NZ_CP012897.1|WP_054764623.1|965212_966751_+|deoxyribodipyrimidine-photo-lyase	gnl|CDD|225588	COG3046, COG3046, Uncharacterized protein related to deoxyribodipyrimidine photolyase [General function prediction only].	0
NZ_CP012897.1|WP_054764628.1|968710_969430_-|heme-ABC-transporter-permease	gnl|CDD|273492	TIGR01191, Heme_exporter_protein_C, heme exporter protein CcmC. This model describes the cyt c biogenesis protein encoded by ccmC in bacteria. It must be noted an arabidopsis, a tritcum and a piscum plant proteins were recognizable in the clade. Quite likely they are of organellar origin. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes, ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in the heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other].	3.78156e-78
NZ_CP012897.1|WP_054764618.1|961432_962434_+|NADPH:quinone-oxidoreductase-family-protein	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.	8.20861e-152
NZ_CP012897.1|WP_082382596.1|969487_970195_-|heme-exporter-protein-CcmB	gnl|CDD|200083	TIGR01190, Heme_exporter_protein_B, heme exporter protein CcmB. This model describes the cyt c biogenesis protein encoded by ccmB in bacteria. Bacterial c-type cytochromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome C. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other].	5.67999e-45
NZ_CP012897.1|WP_054764627.1|968490_968709_-|heme-exporter-protein-CcmD	gnl|CDD|377440	pfam04995, CcmD, Heme exporter protein D (CcmD). The CcmD protein is part of a C-type cytochrome biogenesis operon. The exact function of this protein is uncertain. It has been proposed that CcmC, CcmD and CcmE interact directly with each other, establishing a cytoplasm to periplasm haem delivery pathway for cytochrome c maturation. These proteins contain a predicted transmembrane helix.	1.67253e-08
NZ_CP012897.1|WP_054764621.1|964243_964705_-|DUF3429-family-protein	gnl|CDD|378761	pfam11911, DUF3429, Protein of unknown function (DUF3429). This family of proteins are functionally uncharacterized. This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 147 to 245 amino acids in length.	2.58782e-10
NZ_CP012897.1|WP_054764629.1|970191_970815_-|heme-ABC-exporter-ATP-binding-protein-CcmA	gnl|CDD|226617	COG4133, CcmA, ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones].	4.43427e-66
NZ_CP012897.1|WP_054764622.1|964852_965209_+|DUF393-domain-containing-protein	gnl|CDD|367833	pfam04134, DUF393, Protein of unknown function, DUF393. Members of this family have two highly conserved cysteine residues near their N-terminus. The function of these proteins is unknown.	6.57909e-18
NZ_CP012897.1|WP_082382595.1|957473_960341_-|insulinase-family-protein	gnl|CDD|223685	COG0612, PqqL, Predicted Zn-dependent peptidases [General function prediction only].	6.73197e-96
NZ_CP012897.1|WP_054764613.1|954674_955586_-|acyl-CoA-desaturase	gnl|CDD|239582	cd03505, Delta9-FADS-like, The Delta9 Fatty Acid Desaturase (Delta9-FADS)-like CD includes the delta-9 and delta-11 acyl CoA desaturases found in various eukaryotes including vertebrates, insects, higher plants, and fungi. The delta-9 acyl-lipid desaturases are found in a wide range of bacteria. These enzymes play essential roles in fatty acid metabolism and the regulation of cell membrane fluidity. Acyl-CoA desaturases are the enzymes involved in the CoA-bound desaturation of fatty acids. Mammalian stearoyl-CoA delta-9 desaturase is a key enzyme in the biosynthesis of monounsaturated fatty acids, and in yeast, the delta-9 acyl-CoA desaturase (OLE1) reaction accounts for all de nova unsaturated fatty acid production in Saccharomyces cerevisiae. These non-heme, iron-containing, ER membrane-bound enzymes are part of a three-component enzyme system involving cytochrome b5, cytochrome b5 reductase, and the delta-9 fatty acid desaturase. This complex catalyzes the NADH- and oxygen-dependent insertion of a cis double bond between carbons 9 and 10 of the saturated fatty acyl substrates, palmitoyl (16:0)-CoA or stearoyl (18:0)-CoA, yielding the monoenoic products palmitoleic (16:l) or oleic (18:l) acids, respectively. In cyanobacteria, the biosynthesis of unsaturated fatty acids is initiated by delta 9 acyl-lipid desaturase (DesC) which introduces the first double bond at the delta-9 position of a saturated fatty acid that has been esterified to a glycerolipid. This domain family has extensive hydrophobic regions that would be capable of spanning the membrane bilayer at least twice. Comparison of sequences also reveals the existence of three regions of conserved histidine cluster motifs that contain the residues: HXXXXH, HXXHH, and H/QXXHH. These histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within the rat stearoyl CoA delta-9 desaturase. Some eukaryotic (Fungi, Euglenozoa, Mycetozoa, Rhodophyta) desaturase domains have an adjacent C-terminal cytochrome b5-like domain.	1.4267e-43
NZ_CP012897.1|WP_054764626.1|967927_968494_-|DsbE-family-thiol:disulfide-interchange-protein	gnl|CDD|239308	cd03010, TlpA_like_DsbE, TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, periplasmic TRX-like reductase containing a CXXC motif that specifically donates reducing equivalents to apocytochrome c via CcmH, another cytochrome c maturation (Ccm) factor with a redox active CXXC motif. Assembly of cytochrome c requires the ligation of heme to reduced thiols of the apocytochrome. In bacteria, this assembly occurs in the periplasm. The reductase activity of DsbE in the oxidizing environment of the periplasm is crucial in the maturation of cytochrome c.	3.55311e-51
NZ_CP012897.1|WP_054764614.1|955676_956009_+|winged-helix-turn-helix-transcriptional-regulator	gnl|CDD|238042	cd00090, HTH_ARSR, Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric repressors. ARSR subfamily of helix-turn-helix bacterial transcription regulatory proteins (winged helix topology). Includes several proteins that appear to dissociate from DNA in the presence of metal ions.	1.29895e-20
NZ_CP012897.1|WP_054764624.1|966832_967603_+|M48-family-metallopeptidase	gnl|CDD|320690	cd07331, M48C_Oma1_like, Peptidase M48C, integral membrane endopeptidase. This subfamily contains peptidase M48C Oma1 (also called mitochondrial metalloendopeptidase OMA1) protease homologs that are mostly uncharacterized. Oma1 is part of the quality control system in the inner membrane of mitochondria, with its catalytic site facing the matrix space. It cleaves and thereby promotes the turnover of mistranslated or misfolded membrane proteins. Oma1 can cleave the misfolded multi-pass membrane protein Oxa1, thus exerting a function similar to the ATP-dependent m-AAA protease for quality control of inner membrane proteins; it cleaves a misfolded polytopic membrane protein at multiple sites. It has been proposed that in the absence of m-AAA protease, proteolysis of Oxa1 is mediated by Oma1 in an ATP-independent manner. Oma1 is part of highly conserved mitochondrial metallopeptidases, with homologs present in higher eukaryotes, eubacteria and archaebacteria, all containing the zinc binding motif (HEXXH). It forms a high molecular mass complex in the inner membrane, possibly a homo-hexamer.	4.26353e-69

Protein sequences

>NZ_CP012897.1|WP_054764620.1|963047_963830_+|SDR-family-oxidoreductase
MKLDSSIAAVVTGGASGLGEGTARAIAATGAKVALFDLNAEKGEAIAAEIGGVFCQVDVTDDASVAAAFEKARAAHGQERLTVNCAGIATGMKTVSRKKDTGEIKAHDMAQFERTVRVNLFGTFRVLSQSAAGMVTLEPMADGERGLIVNTASVAAQDGQIGQAAYSASKGGVYAMTLPIARDLAQEGVRCNTILPGIMWTPMMAGMDQKIQDALAAAIPFPSRLGTPADYASLVLELARNVYINGECIRLDGAIRLAPR
>NZ_CP012897.1|WP_054764619.1|962593_962992_-|DUF1232-domain-containing-protein
MTAKAKPVSPEDALDPKKALVPTVVKVNEARVTRGFWPKIQRTAARIPFADQALAAWYAARDPQTPLPAKGMIFAALAYFVMPVDAIPDLFAGIGYTDDAAVIAALIATLGANIKRRHRDQAEEAVERLRGG
>NZ_CP012897.1|WP_054764618.1|961432_962434_+|NADPH:quinone-oxidoreductase-family-protein
MRAVLSKAAGGPETLVVEDVLDPTPKAGEVVIEVKAVGINYPDTLIIEDKYQFRPERPFSPGAEVAGVVEAVGEGVKGVAKGDRVIAVPGWGGLVERLAVRAETVIPMPEAMSFEEAAALIMTYGTSYYALKDRAQLKPGETLLVLGAAGGVGAAAVELGKAMGARVVAAASTNDKVEFALALGADNGLIYPTGPMDKAAQKELSGEFKLATGRDGADVVYDAVGGDYAEPALRAMDWNGRYLVVGFPAGIPALPLNLTLLKSVSVIGVFWGAAVARDPKGHAANMAELMQMYAEGKIKPRVSKTFPLEKAGAAIKALGDRQALGKIVVVVGD
>NZ_CP012897.1|WP_054764617.1|960418_961291_-|isoaspartyl-peptidase/L-asparaginase
MTALILHGGAGARRERNYDAEVAHMRQVVEAMKPRLDAGESALDVATAAVVMLEDSGLYVAGKGASPNLAGAYELDASLMDGSTKRAGSVAALQGFRNPVVAARAVMERTPHVMLVGEGAALFAQDQGLEPIADEAAWYTGAGQGEDNHPPGTLSHGTVGACVLDSQGRLAAATSTAGVFGKMPGRAGDTPIPAAGTWADGHAATSCTGQGEYFIRVAAAAQVAWRVAAGQSLADATQAVIDEIGQMGGDGGLIALDAAGNIAAPFNSQGMKHAWLTPDGEIGVEVFERR
>NZ_CP012897.1|WP_082382595.1|957473_960341_-|insulinase-family-protein
MKFRLTATVAASALLLGLAAPAFAAPAAALAPAPVTAQAQQGVVVPPLGFTKRVLPNGLEVYTARDADTSNVTVQVWYKVGSKDDPAGRSGFAHLFEHLMFKATKNLPPETFDRLTEDVGGSNNAFTADDTTAYFETVPANHLQRMLFAEAERMGSLVVDEPTFVAERDVVKEEYRQRILANPYGRLFGLFVPETLYQESPYRRPGIGSIEELNASSLDDVLRFHATYYRPDNAYLIVAGNFDQAQLDRWIDQYFTPLKNPATPLPTNNVAEPEPTGPRDVTYYAPNVPLPAVVIGWPTVKYADADRAALTVLDGILSTGESSRLYRSLVYDQQIAAQIGSTPDFAQQAGNLTALAIMAQGHTAEEGIAALNAEIAKLRDAPVTAAELTEAKNEIVADALRNRETVDDRASALGFALINTGDAAAADREIAQIQAVTVADVQRVARKYLTPQRQSTIRYLPADEQNPPSVQKMNVDAPVKVADLAPAGTPAVLLPEAQRTPLPQPGAEVAPATPAVADFRLDNGLRVLVAPTDGVPLVSARLSFDAGSSDDPAGKAGIAAMTAALLTQGTKTKSAPEIATEIEQLGASIGAGAGVDFTNVYANAPANAFPQTVALMADLVKNPTFAAEELERQQAQTLDNLRVALSQPGSIAGQAVGRVVYGDAPYGAPGSGTVQSVPAITPADVAAFHAARYRPSDATLVFSGDITPAAARALAQQAFGDWRPAGQAAAPVAAPAGQALAPRIVVVNQPGAGQAAVVAAIRGVSRTDADYFPLTLGNTLLGGGFSSRLNQEIRIKRGLSYGAGSSLGARADAGLFTASTQTKNETADEVADLILAEIAKLGAETPTQADLAPRRATLIGGFGRSLETVDGLGALVANLALYDLPMSDLADYAGRVRAVTPEQVQAAFAEHLPVNRASLVIVGDGSLFLDALRAKHPNLEVIEASELNLNSGSLK
>NZ_CP012897.1|WP_054764616.1|956538_957369_+|trypsin-like-peptidase-domain-containing-protein
MQFPRLPDWAIYGAVAGVLLAVSLGRRENADAPPAPPPPDEIEGALLGPITPFDTAVTLDAPDTPFTPKSGTAFSIAGRGRWVTARHVVEGCRRPALVVGGGRAVAADVRLAPRADVALLLTEGGPPALPVAAEAPLRKGQRAFHPGFPQGRAGEVTSRLLGRETLKVFGRGAHDEPVLAWAEVGRTDGLEGTLSGLSGAPVMDGRGRVLGVTIAEAPRRGRIYTTAPESFAPAIRGEQRADEAALGEPVTIDNYGRVADALRRDLRVAQVVCLSV
>NZ_CP012897.1|WP_054764615.1|956078_956519_+|DUF350-domain-containing-protein
MDPSLTNVLSSAEVQAFASGFPVMVTHLIVTLLLLAAGATVYALLTPWKEIALIREGNPAAAVAFAGILVGLAIPLAVSLSVSTSVRDVAIWGVATLVLQLLAFRVVDLMLHGLPQRIKDGEVAASVVLVGAKLATALILSAALTG
>NZ_CP012897.1|WP_054764614.1|955676_956009_+|winged-helix-turn-helix-transcriptional-regulator
MQRVFEALSSPVRRKILAYLAHADLTAGEIAAKFEISKPAVSQHLSVLEVAGLVTSEKKGQYVHYSLAPDQLTNTLNGYVQEVCPVAKPLKRESAALAKARANKPDDAGL
>NZ_CP012897.1|WP_054764613.1|954674_955586_-|acyl-CoA-desaturase
MDHADPCAVNSLVETPGCSPIEGRVVWDPRHSLWNGAMLAAALIFGAKTFSLAAVAVFVVVTGTTLLLGHSVGFHRRLIHGSFDCPLWLERVLAWFGTLVGMSGPFWMIRTHDIRDWAQRQTDCHDYLAHRRPMAVDAWWQMHCRLVLERPPQFELGRIGRDPFYRFLERTWMLQQLPVAAALWLMGGWGFVVWGVCARVSASVIGHWFVGHLAHRRGPQTWLVREAGVQAHDVPWAAIPTMGEAWHNNHHAYPGSAKIGLYPGQSDWGFRFIQLLERLGLAWDVRTPESMGPRPLNRVVAKI
>NZ_CP012897.1|WP_054764612.1|954216_954678_-|hypothetical-protein
MIKSMSDRLGTLIIANVLAASTTAGMSAIGMWISIIVSPGETGLGNALGGGLLFGLLAALYGFIISFPVYLVGLIVVGIPTWWILHNSGRTSVGAFSITAAIESVIAGAIVFRLLAPGTELAAPLLAIPGGLAGWIIWRRSYRPLTPPPAPPS
>NZ_CP012897.1|WP_054764621.1|964243_964705_-|DUF3429-family-protein
MDTNAPARLPSLARQLGFSGLLPQAAAVALLVGGGAELRPLALGLAFGYAALIFSFLGGVWWGLAAAARGKAPAWVWGVAVLPSLLALAAAWPLAAGESDLRLSLGLLGGFIALSVLVDLRLKALGLTPEGWLGLRLPLSLGLGALTLAAALL
>NZ_CP012897.1|WP_054764622.1|964852_965209_+|DUF393-domain-containing-protein
MSRLVVWHDGACPLCRREIVLMRRLDRRGVIEFVDVAGDGDVACPLDRETLLARFHAREDGRILSGAAAFAAMWRAIPLLRPLGLAARSPIVLAGLEAAYRLFLKVRPRLQALARRAG
>NZ_CP012897.1|WP_054764623.1|965212_966751_+|deoxyribodipyrimidine-photo-lyase
MAVLRLVLGDQLSDRLTALEGLDPAADTVLMAEVRDEATYVRHHKQKIALVFAAMRNHAERLRARGVRVRYVAIDDPDNSGSITGELARALDAGVYDRAVLTECGEWRLAEHLAAFAEGAGLPVEIREDRRFLCSHDRFRRWASGKSQLRMEFFYREMRRATGLLMDGDQPEGGRWNYDAENRKKLPRGVRPPKRLRITPNAITQSAMADVACLFPDHFGALHDFGWPTTAEEAETVLEDFLANILSGFGDWQDAMAEDQPWMWHGLISTSLNLGLLDPMDVCRRAEAVYRAGRAPLNAAEGFIRQILGWREFVRGIYWLKAPEYRARNFLDADRNLPWFYWSGETDMACVADVVRTTRENAYAHHIQRLMVTGNLALLLGVHPDAVDDWYMAVYADAYEWVEMPNTRGMALFADGGIVGSKPYAASGAYIDRMSDYCGGCRYDVKSKSGDAACPFNRLYWGFLERNRGRLRDNPRLAMPYRTLDGFGEARRAALAAEAEACRTLLGATPRD
>NZ_CP012897.1|WP_054764624.1|966832_967603_+|M48-family-metallopeptidase
MIALRRPASRLPVRLLAAAVAASALSACAYNEALGRNQLLLVDNAALAQQSNAAWREAISKPGVQTSGAQVDRIRRVGNRLVQAAGLGDRTWDYAVFSEKSPNAFVLPSGQIGVTDSLLALVQNDDQLATVIGHEIGHVVANHAAERASSQAATSIGLAAVGGAAGRYGDAVNAYGGLAAQYGLLLPYSRRDELEADRLGVDYMQAAGFRPSQAVALWRLMAAQRQASIPQFASTHPSDATRIDLLQQYIAGKGWS
>NZ_CP012897.1|WP_054764625.1|967603_967858_-|hypothetical-protein
MSAIRPGLPQTLPPSGGETSSARNAQAAFFRAALNQVQTNPIQAAPIQPQTPAASPTRPTPPSPSTDGQPPRIMRPGTYLDIKV
>NZ_CP012897.1|WP_054764626.1|967927_968494_-|DsbE-family-thiol:disulfide-interchange-protein
MNRWLALLPLVVAVALFALFAGWSLKRDPAFKPDAMVGQPIPETVLPMLEGDTAGPGNLDLKTAGVGRPMLVNVFASWCAPCRIEHPKLLALKARGIAVVGVAYKDEPVATRAFLDELGDPYSMVLVDREGRAGLDLGISGVPETFAVDAMGRITAKQSGPLLNDADIERLVASMQAPARAPPSKSSR
>NZ_CP012897.1|WP_054764627.1|968490_968709_-|heme-exporter-protein-CcmD
MLDLDMAPYAAFVWPAWGVSALVLAALTARAVVASRKWKRELERLEKDQSATSDAAVSPRPQAAQSAIGPLK
>NZ_CP012897.1|WP_054764628.1|968710_969430_-|heme-ABC-transporter-permease
MFGLSNPQRFMRFTGPLTPVLWTAAAVLLAVGTWLSFTVPADYQQGDTVRIMFVHVPAASLGLGAYAALGVSSFFALVFRHALADAAARAAALPGAAFTALALFTGSLWGQPMWGTWWVWDARLTSVLVLFLFYLGYMALRASIDDEQKGARAAAVLGLVGLINLPIVKFSVDWWNTLHQPASFLTPGASGLDPVYLPPFLTMLAAYGVLFAALWLTAIRTEIRRRRVLSLRARKALEA
>NZ_CP012897.1|WP_082382596.1|969487_970195_-|heme-exporter-protein-CcmB
MRRPVDAEPRPPGLRGATRVLLERELDLAWSGGGGPLLACGFFACLTAVLPLAAGGDPRTLSPVAGGIAWLALALASLLSLERLFERDLEDGALDLLAIGHLPLESVVLIKALAQWIAVGLPLALTAPVAALALGLPVSLAPLAALSALIGGAGFALTGALGAALALGAKRGGLLIAVVVLPLFIPPVVFGAGALERAASGQSPAPALAFLTAYVLFAGVIAAFAGAAAVRNAQG
>NZ_CP012897.1|WP_054764629.1|970191_970815_-|heme-ABC-exporter-ATP-binding-protein-CcmA
MIHTLSISDLTVSRGERRLFSGLSLDLRAGEAVALTGANGAGKTSLLRTVAGLLRPDAGEIAFHDGDGNRLDDHLARGREVHFLGHQDGLKTGRTARRELGFQCDWLGHTQTGFDHAVEAFGLEPLLDLEVRRLSAGQRRRLAMGRLVGSPRALWLLDEPMAPLDARWRAVFADQMRRHLDADGLILAAVHDPLPIPARTLDLGGLA

Crispr_ID: NZ_CP012897_2

• CRISPR_ID: NZ_CP012897_2
• CRISPR_location: 2027455-2027572
• CRISPR_type: Orphan
• Repeat_type: NA
• Spacer_info: 1 spacers

Consensus repeat of NZ_CP012897_2

Consensus_repeat	Method
CGGACACATCGGACACATCGGACACTGTTTTTC	CRISPRCasFinder

spacers of NZ_CP012897_2

>2.1|2027488|52|NZ_CP012897|CRISPRCasFinder
TGTGTCCGGCAGGGGCCGAACGGTTCTTCCGCTCCGCCGAGGGCTTCACCTC

CRISPR arrays and Neighbor proteins around NZ_CP012897_2

CRISPR arrays

The CRISPR arrays of NZ_CP012897_2

>merge|NZ_CP012897|2|2027455-2027572|CRISPRCasFinder
CGGACACATCGGACACATCGGACACTGTTTTTCTGTGTCCGGCAGGGGCCGAACGGTTCTTCCGCTCCGCCGAGGGCTTCACCTCCGGACAGATCGGACACATCGGACACTGTTTTTC

>NZ_CP012897|2|2|2027455-2027572|CRISPRCasFinder
CGGACACATCGGACACATCGGACACTGTTTTTC	TGTGTCCGGCAGGGGCCGAACGGTTCTTCCGCTCCGCCGAGGGCTTCACCTC
CGGACAGATCGGACACATCGGACACTGTTTTTC

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP012897.1|WP_054765521.1|2024758_2025079_+|hypothetical-protein	unknown	unknown	unknown
NZ_CP012897.1|WP_054765520.1|2024037_2024685_+|ATP-dependent-Clp-protease-proteolytic-subunit	unknown	unknown	gnl|CDD|178955
NZ_CP012897.1|WP_082382673.1|2022533_2023877_+|trigger-factor	unknown	unknown	gnl|CDD|234956
NZ_CP012897.1|WP_054765524.1|2027799_2030196_+|endopeptidase-La	unknown	unknown	gnl|CDD|223542
NZ_CP012897.1|WP_054765517.1|2021221_2021638_+|hypothetical-protein	unknown	unknown	gnl|CDD|377576
NZ_CP012897.1|WP_054765518.1|2021639_2022341_-|MBL-fold-metallo-hydrolase	unknown	unknown	gnl|CDD|293823
NZ_CP012897.1|WP_152951105.1|2039638_2040817_+|NADH-quinone-oxidoreductase-subunit-D	unknown	unknown	gnl|CDD|180385
NZ_CP012897.1|WP_054765523.1|2025930_2027199_+|ATP-dependent-Clp-protease-ATP-binding-subunit-ClpX	unknown	unknown	gnl|CDD|235422
NZ_CP012897.1|WP_054765514.1|2016998_2018225_+|acyl-CoA-dehydrogenase	unknown	unknown	gnl|CDD|173844
NZ_CP012897.1|WP_054765525.1|2030747_2034047_-|autotransporter-outer-membrane-beta-barrel-domain-containing-protein	unknown	unknown	gnl|CDD|214872
NZ_CP012897.1|WP_082382674.1|2034373_2035624_+|glycosyltransferase	unknown	unknown	gnl|CDD|340842
NZ_CP012897.1|WP_054765516.1|2020719_2020941_-|general-stress-protein	unknown	unknown	gnl|CDD|226252
NZ_CP012897.1|WP_152950061.1|2038284_2038896_+|NADH-quinone-oxidoreductase-subunit-B	unknown	unknown	gnl|CDD|235797
NZ_CP012897.1|WP_054765526.1|2036101_2037733_-|AbgT-family-transporter	unknown	unknown	gnl|CDD|225525
NZ_CP012897.1|WP_054765529.1|2038892_2039537_+|NADH-quinone-oxidoreductase-subunit-C	unknown	unknown	gnl|CDD|235691
NZ_CP012897.1|WP_054765527.1|2037937_2038315_+|NADH-quinone-oxidoreductase-subunit-A	unknown	unknown	gnl|CDD|180638
NZ_CP012897.1|WP_054765530.1|2040813_2041491_+|NADH-quinone-oxidoreductase-subunit-NuoE	unknown	unknown	gnl|CDD|237082
NZ_CP012897.1|WP_082382791.1|2025085_2025727_-|HAD-IB-family-hydrolase	unknown	unknown	gnl|CDD|273654
NZ_CP012897.1|WP_054766918.1|2030304_2030580_+|HU-family-DNA-binding-protein	unknown	unknown	gnl|CDD|197709
NZ_CP012897.1|WP_054765515.1|2018339_2020499_+|L-histidine-N(alpha)-methyltransferase	unknown	unknown	gnl|CDD|274581

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
NZ_CP012897.1|WP_054765520.1|2024037_2024685_+|ATP-dependent-Clp-protease-proteolytic-subunit	gnl|CDD|178955	PRK00277, clpP, ATP-dependent Clp protease proteolytic subunit; Reviewed.	2.16314e-138
NZ_CP012897.1|WP_054765526.1|2036101_2037733_-|AbgT-family-transporter	gnl|CDD|225525	COG2978, AbgT, Putative p-aminobenzoyl-glutamate transporter [Coenzyme metabolism].	0
NZ_CP012897.1|WP_082382673.1|2022533_2023877_+|trigger-factor	gnl|CDD|234956	PRK01490, tig, trigger factor; Provisional.	4.08799e-161
NZ_CP012897.1|WP_054765524.1|2027799_2030196_+|endopeptidase-La	gnl|CDD|223542	COG0466, Lon, ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones].	0
NZ_CP012897.1|WP_054765517.1|2021221_2021638_+|hypothetical-protein	gnl|CDD|377576	pfam05957, DUF883, Bacterial protein of unknown function (DUF883). This family consists of several hypothetical bacterial proteins of unknown function.	0.00613377
NZ_CP012897.1|WP_054765518.1|2021639_2022341_-|MBL-fold-metallo-hydrolase	gnl|CDD|293823	cd07737, YcbL-like_MBL-fold, Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase domain. This subgroup includes Salmonella enterica serovar typhimurium YcbL which has type II hydroxyacylglutathione hydrolase (EC 3.1.2.6, also known as glyoxalase II) activity, and has a single metal ion binding site, and Thermus thermophilus TTHA1623 which does not have GLX2 activity and has two metal ion binding sites with a glyoxalase II-type metal coordination. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.	8.52054e-112
NZ_CP012897.1|WP_152951105.1|2039638_2040817_+|NADH-quinone-oxidoreductase-subunit-D	gnl|CDD|180385	PRK06075, PRK06075, NADH-quinone oxidoreductase subunit D.	0
NZ_CP012897.1|WP_054765523.1|2025930_2027199_+|ATP-dependent-Clp-protease-ATP-binding-subunit-ClpX	gnl|CDD|235422	PRK05342, clpX, ATP-dependent Clp protease ATP-binding subunit ClpX.	0
NZ_CP012897.1|WP_054765514.1|2016998_2018225_+|acyl-CoA-dehydrogenase	gnl|CDD|173844	cd01155, ACAD_FadE2, Acyl-CoA dehydrogenases similar to fadE2. FadE2-like Acyl-CoA dehydrogenase (ACAD). 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 ACAD 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. ACAD's are generally homotetramers and have an active site glutamate at a conserved position.	0
NZ_CP012897.1|WP_054765525.1|2030747_2034047_-|autotransporter-outer-membrane-beta-barrel-domain-containing-protein	gnl|CDD|214872	smart00869, Autotransporter, Autotransporter beta-domain. Secretion of protein products occurs by a number of different pathways in bacteria. One of these pathways known as the type IV pathway was first described for the IgA1 protease. The protein component that mediates secretion through the outer membrane is contained within the secreted protein itself, hence the proteins secreted in this way are called autotransporters. This family corresponds to the presumed integral membrane beta-barrel domain that transports the protein. This domain is found at the C-terminus of the proteins it occurs in. The N-terminus contains the variable passenger domain that is translocated across the membrane. Once the passenger domain is exported it is cleaved auto-catalytically in some proteins, in others a different peptidase is used and in some cases no cleavage occurs.	2.01557e-13
NZ_CP012897.1|WP_082382674.1|2034373_2035624_+|glycosyltransferase	gnl|CDD|340842	cd03814, GT4-like, glycosyltransferase family 4 proteins. This family is most closely related to the GT4 family of glycosyltransferases and includes a sequence annotated as alpha-D-mannose-alpha(1-6)phosphatidyl myo-inositol monomannoside transferase from Bacillus halodurans. 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 bacteria and eukaryotes.	7.98929e-79
NZ_CP012897.1|WP_054765516.1|2020719_2020941_-|general-stress-protein	gnl|CDD|226252	COG3729, GsiB, General stress protein [General function prediction only].	0.00117134
NZ_CP012897.1|WP_152950061.1|2038284_2038896_+|NADH-quinone-oxidoreductase-subunit-B	gnl|CDD|235797	PRK06411, PRK06411, NADH-quinone oxidoreductase subunit NuoB.	9.14087e-105
NZ_CP012897.1|WP_054765529.1|2038892_2039537_+|NADH-quinone-oxidoreductase-subunit-C	gnl|CDD|235691	PRK06074, PRK06074, NADH dehydrogenase subunit C; Provisional.	1.17323e-99
NZ_CP012897.1|WP_054765527.1|2037937_2038315_+|NADH-quinone-oxidoreductase-subunit-A	gnl|CDD|180638	PRK06602, PRK06602, NADH:ubiquinone oxidoreductase subunit A; Validated.	1.37926e-54
NZ_CP012897.1|WP_054765530.1|2040813_2041491_+|NADH-quinone-oxidoreductase-subunit-NuoE	gnl|CDD|237082	PRK12373, PRK12373, NADH-quinone oxidoreductase subunit E.	5.61985e-102
NZ_CP012897.1|WP_082382791.1|2025085_2025727_-|HAD-IB-family-hydrolase	gnl|CDD|273654	TIGR01490, Uncharacterized_protein_Rv3661/MT3761, HAD-superfamily subfamily IB hydrolase, TIGR01490. This hypothetical equivalog is a member of the IB subfamily (TIGR01488) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The sequences modelled here are all bacterial. The IB subfamily includes the enzyme phosphoserine phosphatase (TIGR00338). Due to this relationship, several of these sequences have been annotated as "phosphoserine phosphatase related proteins," or "Phosphoserine phosphatase-family enzymes." There is presently no evidence that any of the enzymes in this model possess PSPase activity. OMNI|NTL01ML1250 is annotated as a "possible transferase," however this is due to the C-terminal domain found on this sequence which is homologous to a group of glycerol-phosphate acyltransferases (between trusted and noise to TIGR00530). A subset of these sequences including OMNI|CC1962, the Caulobacter crescentus CicA protein cluster together and may represent a separate equivalog. [Unknown function, Enzymes of unknown specificity].	1.07319e-42
NZ_CP012897.1|WP_054766918.1|2030304_2030580_+|HU-family-DNA-binding-protein	gnl|CDD|197709	smart00411, BHL, bacterial (prokaryotic) histone like domain.	6.59951e-29
NZ_CP012897.1|WP_054765515.1|2018339_2020499_+|L-histidine-N(alpha)-methyltransferase	gnl|CDD|274581	TIGR03440, egtB_TIGR03440, ergothioneine biosynthesis protein EgtB. Members of this family include EgtB, and enzyme of the ergothioneine biosynthesis, as found in numerous Actinobacteria. Characterized homologs to this family include a formylglycine-generating enzyme that serves as a maturase for an aerobic sulfatase (cf. the radical SAM enzymes that serve as anaerobic sulfatase maturases). [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs].	0

Protein sequences

>NZ_CP012897.1|WP_054765523.1|2025930_2027199_+|ATP-dependent-Clp-protease-ATP-binding-subunit-ClpX
MTKAAGSDAKSTLYCSFCGKSQHEVRKLIAGPTVFICDECVELCMDIIREEHKIGFKKTSDGVPTPKEIRDVLDDYVIGQSHAKKVLSVAVHNHYKRLNHATKNNDVELAKSNIMLIGPTGSGKTLLAQTLARIIDVPFTMADATTLTEAGYVGEDVENIILKLLQASDYNVERAQRGIVYIDEIDKISRKSDNPSITRDVSGEGVQQALLKIMEGTVASVPPQGGRKHPQQEFLQVDTANILFIVGGAFAGLEKVISARGEGASIGFGAKVKEIDERRTGDILKGVEPDDLMRFGLIPEFIGRLPVLATLEDLDETALVTILTEPKNALVKQYKRLFEMENVELTFTDDALIAVAKKAITRKTGARGLRSILEGILLETMFELPTFEGVEEVVVNAEVIDGKAQPLLIYSEASKKKADGAA
>NZ_CP012897.1|WP_082382791.1|2025085_2025727_-|HAD-IB-family-hydrolase
MGSLQELRQSRINSEQPLVAFDFDGTLTIRDSFTQFLRWKAGPGGWALGLVKLAPALAAYGRDRDRGRIKAASVKEFLAGMDRESLEAEAERFADLVWDRFMRPDALKVWNDWGERGAHRVIVTASPETTVEPFARRLGAEALLGTPLTFDAEGRVTGAFDGANCRGEEKVRRLKAAYGEDLVLTAAYGDTSGDAEMLAIAQSPGFRVFTQRP
>NZ_CP012897.1|WP_054765521.1|2024758_2025079_+|hypothetical-protein
MQFTRDPSGTIEVEGETYAWEIRRQPRPVGGAVWEGMAVSLRHVDFKREAIIQFPPPLRPNGRPDVEKQRVNVDAVRNAVTAAIEAGWDPTSRGKAMVFDVDADGR
>NZ_CP012897.1|WP_054765520.1|2024037_2024685_+|ATP-dependent-Clp-protease-proteolytic-subunit
MRDPIELMNMNLVPMVVEQSSRGERSFDIFSRLLRERIIFLTGPFEDGMASLICAQLLFLESENPKKEISMYINSPGGQVTSALAIYDTMQYIKSPVSTVVMGMAASAGSLILTAGEAGQRIALPNARVMVHQPSGGFRGQASDIERHAEDIRYTKKRLNEIYVHHTGRTYEEVERTLDRDHFMSAEEAKAWGIVDHVYDRREQADADGIKTPGA
>NZ_CP012897.1|WP_082382673.1|2022533_2023877_+|trigger-factor
MQVVEKSNEGLSRVIAVTIPVAELNEKLEARVKEVAPQMKLKGFRPGKVPVAHVKKTFGRDFMGEIINAQLNETSQKALDEAKIRPAAPAEMKLTSDMDKVIAGQEDLAYEMSLEIMPDFTPVDPKTLKLERPTYEASDADLDEALTELAGQAKSYEDKKGKTVKAAEGDQLTIDFLGKLDGEPFDGGAAEDADLVIGSGRFIPGFEEQLKGAKVGEEKTIEVTFPENYQAAHLAGKLATFDIKVKAIKAEVEAKVDDEFAKRIGLESLDRLKELLSQNLNQQYAGAARFKLKRALLDQLDAAHDFPLPPKMVEAEFDGIWQQVEADKAAGRLPEEDAAKSEEDLKAEYKKIAERRVRLGLVLAEIGRAHNVQVTDQELNAALLQEARNYPGQEQAVLNFYRQNPNAAAQMRAPIYEEKVVDLIVGLAEVTDKPISKEELLKEDEEG
>NZ_CP012897.1|WP_054765518.1|2021639_2022341_-|MBL-fold-metallo-hydrolase
MTQPASPIGVFVTPVTPLQQNCTTVWCTATNKAAVIDPGGSVDAILAEVARRGLTLDQIWITHGHLDHAGGAAEMQEKTGVRITGPQKADQFWIDRIVETGRMYGLPEARPFTPDRWLEDGDTVSLGETTWEVRHCPGHTPGHVIFFNPAARFAQVGDVLFKGSVGRTDFPMSDPPALIRSVVEKLWPLGDDVTFVPGHGPISTFGEERRTNPFVSDAALQRAPMQREPVGPA
>NZ_CP012897.1|WP_054765517.1|2021221_2021638_+|hypothetical-protein
MVFSSEWRTRPAPQCSPPALGADMGNWIRSGRFSVRTPEIPMTQTPIAPSSPDDIVTEDDGPTQRLDRQADAILAEGEARSFEDTTSLRQALREDAAMIRSKVAGRVETARDGIRDEPMRTTLYALGIGVIIGMLMRR
>NZ_CP012897.1|WP_054765516.1|2020719_2020941_-|general-stress-protein
MDGQTSRPSGVSKRGFASMDPERQREIARKGGASVPSEKRSFSQDRSLAAQAGRKGGEASHGPKKDAASNGAE
>NZ_CP012897.1|WP_054765515.1|2018339_2020499_+|L-histidine-N(alpha)-methyltransferase
MNARLESDTRAASDVTRFRAIRGAMPALAEGLSPEDLAAQSMPDCSPGKWHLAHTSWFFEAMILSADPAYAPVDPRFQQLFNSYYEALGERVPRPQRGLMTRPSVNEVLSYRREIDRRMAAWLASGPFSGHQRYLFELGLHHDQQHQELFLMDLLNLMACSPLDPAAYAVEPRQAPPEAPRGGAVVFDGGLVSIGHGGAGFAFDNEGPSHRVWLEPFALAADLVTNGDWLGFIADGGYARPELWLSDGWATVKAEAWTAPLYWRRDGDDWTVLSLIGRAPVDPTAPVRHVSFYEADAYARWAGKRLPSEAEWEHAATTAPDAFSNLSGEVWQWTSSAYAPYPGFQPTPGTAAEYNGKFMANQMVLRGGAFATPPGHARVTYRNFFYPQQRWAFMGLRLAEDAPRGRTSFIEDAQTAAFRRDLVQGLSRDQKAVPPKWFYDAEGSRLFEEITALPEYYPTRQETALLRDRAAALTADFGPEAVLVEFGSGASEKTRILLDAAPDLGAYVPLDISETALLDAVARLSADYPALRVQPVLGDFEHLSPLPDDLPQGRRIGFFPGSTIGNLEPEEAVRFLASARRMLGEGALFILGVDLVKDPATLVAAYDDGRGVTAAFNLNLLVRANAELDADFDLDAFAHRAVWNPDHSRMEMHLQALRQTAARVGDRAFTFMAGETLHTESSRKFTPDSVEALAKESGWSMAGFEVSPEPRVALALLRG
>NZ_CP012897.1|WP_054765514.1|2016998_2018225_+|acyl-CoA-dehydrogenase
MDFRHSDRALDWHARVRRFLDEQVIPREADYFAQVRENPNRQAPVMEAMKAAAREAGLWNMFLPGGHDGENGGAGLTNLEYAPLAEMMGRHLWTAEVFNCNAPDTGNMEVLHMYGNAAQQDRWLKPLMAGDIRSAFLMTEPEVASSDATNIQTRIERDGDHYVINGRKWWSTNMAHPNVAVTIVMGKTDPDAAAHAQQSQIIVPVDTPGFRVERMLSVFGYDEKPIGHAEVVLENVRVPVENLIAGEGRGFEIAQGRLGPGRIHHCMRVIGAAERALELMVTRLLNRTAFRKQLAEHSVWEQRVAEARTNIEMCRLLVLKAAWMMDEAGAKNARSEIAQIKVAAPRMALQVIDDAIQAFGGAGVSADTPLAELYATVRTLRIADGPDEVHNRAIARLEYAKHGGRPSA
>NZ_CP012897.1|WP_054765524.1|2027799_2030196_+|endopeptidase-La
MTDTKILPVLPLRDIVVFPHMVVPLFVGREKSVKALDEIMKGEKQILLATQKNSVDDDPSPDAIYPIGVLASVLQLLKLPDGTVKVLVEGKGRARLTRFTDRTDYFEAEAVEIEDEPGETSQAEAMLRAVVEQFENYVKLNKKVPPEALSSIPQITDASKLADSVAAHLSVKIIDKQGLLETIDVPKRLEKVYGLMEGEISVLQVEKKIRSRVKRQMEKTQREYYLNEQMKAIQRELGETDDARDEIMDLEKRIRKTRLSKEARTKAEAEVKKLRNMSPMSAESTVVRNYLDWLLSVPWGKAKQKPIDLVRAEEILEEDHFGLEKVKERIIEYLAVQARTGSLKGPILCLVGPPGVGKTSLAKSIAKATGREYVRMSLGGVRDESEIRGHRRTYIGSMPGKIIQSMKKAKTTNAFVLLDEIDKLGADWRGDPSSALLEVLDPAQNSTFGDHYLEVDYDLSQVMFVTTANSLNMPQPLMDRMEIIRVSGYTEDEKVEIAKRHVLPKQMKDHGLKDGELVVPEETIRDLIRYYTREAGVRSLERALGGLARKAVREMAKTGAASITVDAEKLAEYAGVKKFRYGETDEEDQVGIVTGLAWTEFGGDILTIEAIKMPGRGRMTVTGNLKDVMKESISAAASYVRSRALDFGVKPPVFEKTDIHVHVPDGATPKDGPSAGVAMTVAMVSVLTGVPIRKDIAMTGEITLRGRVTAIGGLKEKLLAALRSGVKTVLIPQENEKDLADVPDNVKSALEIVPISTADEALKWALVGALTPVEWDETAEPLPTPVPPAEGATAAVSH
>NZ_CP012897.1|WP_054766918.1|2030304_2030580_+|HU-family-DNA-binding-protein
MTKAELIGRMATAANISRDQAKAALEAFTDGVVEALSHGHDVKLIGFGSFTTIERKAGVARNPQTGQAIARAASRTARFRAGEGLKSALNA
>NZ_CP012897.1|WP_054765525.1|2030747_2034047_-|autotransporter-outer-membrane-beta-barrel-domain-containing-protein
MRILLATAVAIAPLMAVSGAQAEVVVSTARTTPIRTANATGTAADNVRLASGGSVAVNSGAAVTLDSSNTVDLDSGSSITMDKAADGATGILVNGGNTGSVTVGGAINITDSQETADIKDTDGDGDLDGPFATGTGRYGVRVTGASPFTGNVLVESSGSITVEGNNSYGLGVESAVNGKVQSLGTIRVVGDNTAGVRTTAPVSGNVDLAGSISATGAGATGVSVEGAVGGALKIHSTIATTGYRYTTPPPARPSTGTFDNATTLFLDELDADDLLQGGPAVRVGANVAGGVLLDKALAYSAAGIDGDDDKDGVKNGDEDDDGDGVKNRDDLDRDGDGVPDASETTAALTSLGAAPALLIGSTANTVTLGAVGTGDAAYGLINRGAITGSGVYSGVQGRGLQLGVDGGQAVTIAGGVRNEGSIAASAVDANATAIQVGAGVSAPALVNTGTIQAVVAGKGTEAATGVLIGVGANVGSLTNTGTMIASYGGDDGSATVIRDQSGSLTQLNNAGVIAGSLTASSSSLADVSGTVTAIDLSANTSGVTLRQYGVPAAADSTATDTDKDGVPDASEPQIVGAIKLGSGADTFNVENGTVVGDIAFGAGADRLAISGGAVVQGAITDSDGALDINVSKGTLNATQTTATNISSLNVGADGVLITTLDPKADRAGGFNVSGAATLATGAQLGVRFSSLLEGPERFDIIKAGTLNVGQIDKQLLAENSPYLYVVEAGVDQGANSLYIDARRRTAQEAGLIPVEASAYDAVYAALGANETVRNLFLSQTGRDGFIDAYEQMLPDHSGGPLMSLSAGVDAVTRALTGRNASAAPGETSAWLQEINFYADKDKTDSYGFRSEGFGVAGGVEKGSSLGAFGVTAAFTSSDIKDPEAEAEEVLSANLLELGLYWRAQGQYWTTWARAAGGYASFSADRSLVAGGVYLNNTSDWHGWTAAAAGGASYERNYGRLNVRPEIYAEYFRLSEDARSEKGGGDGFDLDIDSRDSHIFSAVAAMNVGYGFGRDGWIRPELRIGYRQNLSVDAGETIARFASGGPDFILSPDAVEGGGLLLGFRMNLGNELGMLSLTGDAELLEDYVRYSLLLRASFRF
>NZ_CP012897.1|WP_082382674.1|2034373_2035624_+|glycosyltransferase
MTLTDLDVHESELRLIPGLDVEVADTLRALKQASQDERPRLLDTTMLYAPRSGGVKRYLLSKKAWIEANRPGVSHSLIVPGARHRARADGIVQLRATRLPFGDGYRWPSSVKRWSAWVAAMKPSIIEAGDPYTPGQGALEAGQRVGCPVVGFCHSDPAGLAALHFGEWAKKPVEKRWARLFSQFDRVVSPSRFIARRLEEAGVDNIVIRPLGVEVDTFRPDRRDRSWLLKELGLGPDARLLCFAGRPAKEKNVDVLIEAVQKLGAPYYLVLVGAGSGMPAEDRVISLPYEKDPRAVAKIIASCDAFVHANDKEPFGLIVLEAMACGRPVVGVNAGGVAETVDSTVGQLAASAEADDYAQAIEALFARDIEAIGRAAREKAVSRFAWNRVFEDLCMVYGELTGEAAFVQPEAAFAVH
>NZ_CP012897.1|WP_054765526.1|2036101_2037733_-|AbgT-family-transporter
MNPAARLLNTVERIGNRLPDPVFLFLWLVGGLILLSMIGAALGWSAVNPVTGDRLAAQSLLSPENLERLIIGMPRTLADFPPLGIVVTIIYGASVAERAGLFATAIRGALLNAPRAILTPIVVVTGMVSHHASDASYVVVIPLAAVIFAAAGRHPLAGLAAGFAAVSGGYAGNLFPGASDALILGITEPAAHLIDPSYSVNIAGNWFFIIGVVLVFTPIVWFLTDRVIEPRLGPWAPSADAAAPAASEKQPLTADEKRGLAWAGLALMGMIALWALITLLPGSPFVDPTAEPEQRFNPLYRSLVAFFAVTFFLTGAAYGAGSRSIQSHRDLVRMMRDGIAQLAPYIVLAFFAAHFVAMFNWSGLGPILAVNAAAELKSLALPAPLLLICVVFVSCFFDLFIGSASAKWSALAPIVVPMFMLLGISPEMTTAAYRMGDSVTNIATPLMSYFPLILTFAQRWDPRFGLGSLMATMLPYAGAFLVAGLIMVAAWVTLDLPLGPGVGVYYEPPAPAVAAQEPAAGGLAGPHTPPQPAAVPSPTAPSR
>NZ_CP012897.1|WP_054765527.1|2037937_2038315_+|NADH-quinone-oxidoreductase-subunit-A
MNAFLLEYLPVLIFAGVAAFIGVLFIALPLLLAPKNPDAEKLSAYECGFNAFDDARMKFDVRFYLVSILFIIFDLEVAFLFPWAVSMFDLSQAGMIFAFWSMMVFLGVLTIGFIYEWKKGALEWE
>NZ_CP012897.1|WP_152950061.1|2038284_2038896_+|NADH-quinone-oxidoreductase-subunit-B
MEEGSPGMGVIAPSSPLPGAMVPANSAARSTVEGYDPKVHDKFFEAVNTELGERGFLTASLDDVITWARTGSLMWMTFGLACCAVEMIQMSMPRFDVERFGMAPRGSPRHSDLMIVAGTLTNKMAPAIRKVYDQMPDPRYVVSMGSCANGGGYYHYSYSVVRGCDRVVPVDVYVPGCPPTAEALLYGLLQLQKKIRRTGTIDR
>NZ_CP012897.1|WP_054765529.1|2038892_2039537_+|NADH-quinone-oxidoreductase-subunit-C
MSSLAVQAQFEAALTPMGAELVGALAGDGWGVEAQVAFGELTLVAPREHIVEVMTALRDRFGFQQLLDVCGADYPDREERFEVVYHLLSLTRNARIRVKVATDEVQPVPTVCHVYPSAGWFEREAYDMYGVIFAGHPDMRRLLTDYGFEGHPLRKDFPMTGYVEVRYDEEQKRVVYEPVKLTQEFRTFDFLSPWEGADYPAPVLPGDEKAGVKG
>NZ_CP012897.1|WP_152951105.1|2039638_2040817_+|NADH-quinone-oxidoreductase-subunit-D
MDDRKFTINFGPQHPAAHGVLRLVLELDGEIVERVDPHIGLLHRGTEKLMEARTYLQNVPYLDRLDYVAPMNQEHAFCLAIEKLLGIEVPYRAQLIRVLYSEIGRIGNHLLNATMQAMDVGALTPPLWGHEEREKLMVFYERASGARLHANYFRPGGVHQDLPMDLIDDIGRWCLEFPKALADIESLVTENRIFKQRNVDIGVVSKEQALAWGFSGVMLRGSDIAWDLRKSQPYECYAEMEFDIPVGKNGDCWDRYLCRIEEMKQSVRIMEQCIHKLRNCPGEPVMVEDNKIVPPRRGEMKRSMESLIHHFKLYTEGFKTPEGEVYAAVEAPKGEFGIYLVSDGTNKPYRVKISAPGFRHLQAMDWMNRGHQLADVSAILGSLDIVFGEVDR
>NZ_CP012897.1|WP_054765530.1|2040813_2041491_+|NADH-quinone-oxidoreductase-subunit-NuoE
MSVRRLAKEQPASFAFSKDTQAKAEWWIKKYPENRRQSAVIPILWLVQKQEGWVSEPAIRAVGELLGMPFIRVMEVATFYTMFMLEPVGKTALIQVCGTTPCMLRGANELMKVCKEKIGPKDHLSADGRFTWQEVECLGACSNAPMAQINDYYYEDLTPETMAQVIDDFAAGKAPKPGSYIGRHNAAPAGGAKTLLDPKLYDGSAAKPIKKLPNSDPAPVEKAPA

Crispr_ID: NZ_CP012897_3

• CRISPR_ID: NZ_CP012897_3
• CRISPR_location: 2848092-2848162
• CRISPR_type: Orphan
• Repeat_type: NA
• Spacer_info: 1 spacers

Consensus repeat of NZ_CP012897_3

Consensus_repeat	Method
TTCCTCGACCTCGGCCTCTACGG	CRISPRCasFinder

spacers of NZ_CP012897_3

>3.1|2848115|25|NZ_CP012897|CRISPRCasFinder
CGCCGGTCGCGACAGGGCGAACCCA

CRISPR arrays and Neighbor proteins around NZ_CP012897_3

CRISPR arrays

The CRISPR arrays of NZ_CP012897_3

>merge|NZ_CP012897|3|2848092-2848162|CRISPRCasFinder
TTCCTCGACCTCGGCCTCTACGGCGCCGGTCGCGACAGGGCGAACCCATTCCACGACCTCGGCCTCTACGG

>NZ_CP012897|3|3|2848092-2848162|CRISPRCasFinder
TTCCTCGACCTCGGCCTCTACGG	CGCCGGTCGCGACAGGGCGAACCCA
TTCCACGACCTCGGCCTCTACGG

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP012897.1|WP_054766186.1|2857152_2857938_+|thioredoxin-domain-containing-protein	unknown	unknown	gnl|CDD|239321
NZ_CP012897.1|WP_054766172.1|2836804_2837263_+|RidA-family-protein	unknown	unknown	gnl|CDD|100006
NZ_CP012897.1|WP_054766182.1|2850598_2851276_-|SDR-family-oxidoreductase	unknown	unknown	gnl|CDD|187662
NZ_CP012897.1|WP_054766173.1|2837259_2838408_+|N-acetyltransferase	unknown	unknown	gnl|CDD|377314
NZ_CP012897.1|WP_156314248.1|2855771_2857124_+|M48-family-metalloprotease	unknown	unknown	gnl|CDD|227122
NZ_CP012897.1|WP_054766175.1|2840334_2842638_-|ATP-dependent-Clp-protease-ATP-binding-subunit-ClpA	unknown	unknown	gnl|CDD|274241
NZ_CP012897.1|WP_054766179.1|2845871_2847560_-|cisplatin-damage-response-ATP-dependent-DNA-ligase	unknown	unknown	gnl|CDD|236428
NZ_CP012897.1|WP_156314247.1|2853010_2855665_+|Rne/Rng-family-ribonuclease	unknown	unknown	gnl|CDD|224447
NZ_CP012897.1|WP_054766177.1|2843148_2843637_+|nuclear-transport-factor-2-family-protein	unknown	unknown	gnl|CDD|379639
NZ_CP012897.1|WP_054766995.1|2843696_2844176_-|TIGR01841-family-phasin	unknown	unknown	gnl|CDD|227777
NZ_CP012897.1|WP_054766176.1|2842651_2842981_-|ATP-dependent-Clp-protease-adapter-ClpS	unknown	unknown	gnl|CDD|178809
NZ_CP012897.1|WP_156314202.1|2851316_2852489_-|N-acetylmuramoyl-L-alanine-amidase	unknown	unknown	gnl|CDD|119407
NZ_CP012897.1|WP_054766996.1|2849566_2849872_-|BolA-family-transcriptional-regulator	unknown	unknown	gnl|CDD|376601
NZ_CP012897.1|WP_054766994.1|2835795_2836701_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP012897.1|WP_054766181.1|2849917_2850586_+|J-domain-containing-protein	unknown	unknown	gnl|CDD|99751
NZ_CP012897.1|WP_054766178.1|2844419_2845850_+|D-alanyl-D-alanine-carboxypeptidase	unknown	unknown	gnl|CDD|224600
NZ_CP012897.1|WP_054765980.1|2858585_2859776_-|elongation-factor-Tu	unknown	unknown	gnl|CDD|234596
NZ_CP012897.1|WP_054766174.1|2838566_2840243_-|class-I-SAM-dependent-methyltransferase	unknown	unknown	gnl|CDD|379312
NZ_CP012897.1|WP_082382719.1|2860212_2861097_+|23S-rRNA-(guanosine(2251)-2'-O)-methyltransferase-RlmB	unknown	unknown	gnl|CDD|223640
NZ_CP012897.1|WP_054766187.1|2857949_2858507_+|CDP-alcohol-phosphatidyltransferase	unknown	unknown	gnl|CDD|223632

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
NZ_CP012897.1|WP_054766186.1|2857152_2857938_+|thioredoxin-domain-containing-protein	gnl|CDD|239321	cd03023, DsbA_Com1_like, DsbA family, Com1-like subfamily; composed of proteins similar to Com1, a 27-kDa outer membrane-associated immunoreactive protein originally found in both acute and chronic disease strains of the pathogenic bacteria Coxiella burnetti. It contains a CXXC motif, assumed to be imbedded in a DsbA-like structure. Its homology to DsbA suggests that the protein is a protein disulfide oxidoreductase. The role of such a protein in pathogenesis is unknown.	1.20819e-42
NZ_CP012897.1|WP_054766172.1|2836804_2837263_+|RidA-family-protein	gnl|CDD|100006	cd02199, YjgF_YER057c_UK114_like_1, This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site.	1.3631e-65
NZ_CP012897.1|WP_054766182.1|2850598_2851276_-|SDR-family-oxidoreductase	gnl|CDD|187662	cd09761, A3DFK9-like_SDR_c, Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, classical (c) SDRs. This subgroup includes a putative carbohydrate or polyalcohol metabolizing SDR (A3DFK9) from Clostridium thermocellum. Its members have a TGXXXGXG classical-SDR glycine-rich NAD-binding motif, and some have a canonical SDR active site tetrad (A3DFK9 lacks the upstream Asn). 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 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 (15-PGDH) numbering). 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) 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. Extended SDRs have additional elements in the C-terminal region, 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. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.	1.70687e-67
NZ_CP012897.1|WP_054766173.1|2837259_2838408_+|N-acetyltransferase	gnl|CDD|377314	pfam04339, FemAB_like, Peptidogalycan biosysnthesis/recognition. FemAB_like is a family of both baterial and Viridiplantae proteins with responsibility for building interpeptide bridges in peptidoglycan. Such a function is feasible for bacteria but less likely for the plant members of this family. Perhaps the plant-members are using homologous proteins to recognize bacterial peptidoglcans as part of their innate immune system.	0
NZ_CP012897.1|WP_156314248.1|2855771_2857124_+|M48-family-metalloprotease	gnl|CDD|227122	COG4783, COG4783, Putative Zn-dependent protease, contains TPR repeats [General function prediction only].	3.18637e-108
NZ_CP012897.1|WP_054766175.1|2840334_2842638_-|ATP-dependent-Clp-protease-ATP-binding-subunit-ClpA	gnl|CDD|274241	TIGR02639, ATP-dependent_Clp_protease_subunit, ATP-dependent Clp protease ATP-binding subunit clpA. [Protein fate, Degradation of proteins, peptides, and glycopeptides].	0
NZ_CP012897.1|WP_054766179.1|2845871_2847560_-|cisplatin-damage-response-ATP-dependent-DNA-ligase	gnl|CDD|236428	PRK09247, PRK09247, ATP-dependent DNA ligase; Validated.	0
NZ_CP012897.1|WP_156314247.1|2853010_2855665_+|Rne/Rng-family-ribonuclease	gnl|CDD|224447	COG1530, CafA, Ribonucleases G and E [Translation, ribosomal structure and biogenesis].	1.43727e-165
NZ_CP012897.1|WP_054766177.1|2843148_2843637_+|nuclear-transport-factor-2-family-protein	gnl|CDD|379639	pfam14534, DUF4440, Domain of unknown function (DUF4440).	8.54806e-10
NZ_CP012897.1|WP_054766995.1|2843696_2844176_-|TIGR01841-family-phasin	gnl|CDD|227777	COG5490, COG5490, Uncharacterized conserved protein [Function unknown].	9.9218e-16
NZ_CP012897.1|WP_054766176.1|2842651_2842981_-|ATP-dependent-Clp-protease-adapter-ClpS	gnl|CDD|178809	PRK00033, clpS, ATP-dependent Clp protease adaptor protein ClpS; Reviewed.	4.61709e-49
NZ_CP012897.1|WP_156314202.1|2851316_2852489_-|N-acetylmuramoyl-L-alanine-amidase	gnl|CDD|119407	cd02696, MurNAc-LAA, N-acetylmuramoyl-L-alanine amidase or MurNAc-LAA (also known as peptidoglycan aminohydrolase, NAMLA amidase, NAMLAA, Amidase 3, and peptidoglycan amidase; EC 3.5.1.28) is an autolysin that hydrolyzes the amide bond between N-acetylmuramoyl and L-amino acids in certain cell wall glycopeptides. These proteins are Zn-dependent peptidases with highly conserved residues involved in cation co-ordination. MurNAc-LAA in this family is one of several peptidoglycan hydrolases (PGHs) found in bacterial and bacteriophage or prophage genomes that are involved in the degradation of the peptidoglycan. In Escherichia coli, there are five MurNAc-LAAs present: AmiA, AmiB, AmiC and AmiD that are periplasmic, and AmpD that is cytoplasmic. Three of these (AmiA, AmiB and AmiC) belong to this family, the other two (AmiD and AmpD) do not. E. coli AmiA, AmiB and AmiC play an important role in cleaving the septum to release daughter cells after cell division. In general, bacterial MurNAc-LAAs are members of the bacterial autolytic system and carry a signal peptide in their N-termini that allows their transport across the cytoplasmic membrane. However, the bacteriophage MurNAc-LAAs are endolysins since these phage-encoded enzymes break down bacterial peptidoglycan at the terminal stage of the phage reproduction cycle. As opposed to autolysins, almost all endolysins have no signal peptides and their translocation through the cytoplasmic membrane is thought to proceed with the help of phage-encoded holin proteins. The amidase catalytic module is fused to another functional module (cell wall binding module or CWBM) either at the N- or C-terminus, which is responsible for high affinity binding of the protein to the cell wall.	2.1573e-55
NZ_CP012897.1|WP_054766996.1|2849566_2849872_-|BolA-family-transcriptional-regulator	gnl|CDD|376601	pfam01722, BolA, BolA-like protein. This family consist of the morphoprotein BolA from E. coli and its various homologs. In E. coli over expression of this protein causes round morphology and may be involved in switching the cell between elongation and septation systems during cell division. The expression of BolA is growth rate regulated and is induced during the transition into the the stationary phase. BolA is also induced by stress during early stages of growth and may have a general role in stress response. It has also been suggested that BolA can induce the transcription of penicillin binding proteins 6 and 5.	1.65177e-32
NZ_CP012897.1|WP_054766181.1|2849917_2850586_+|J-domain-containing-protein	gnl|CDD|99751	cd06257, DnaJ, DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonine family. Hsp40 proteins are characterized by the presence of a J domain, which mediates the interaction with Hsp70. They may contain other domains as well, and the architectures provide a means of classification.	2.51395e-10
NZ_CP012897.1|WP_054766178.1|2844419_2845850_+|D-alanyl-D-alanine-carboxypeptidase	gnl|CDD|224600	COG1686, DacC, D-alanyl-D-alanine carboxypeptidase [Cell envelope biogenesis, outer membrane].	1.74669e-103
NZ_CP012897.1|WP_054765980.1|2858585_2859776_-|elongation-factor-Tu	gnl|CDD|234596	PRK00049, PRK00049, elongation factor Tu; Reviewed.	0
NZ_CP012897.1|WP_054766174.1|2838566_2840243_-|class-I-SAM-dependent-methyltransferase	gnl|CDD|379312	pfam13649, Methyltransf_25, Methyltransferase domain. This family appears to be a methyltransferase domain.	6.25914e-18
NZ_CP012897.1|WP_082382719.1|2860212_2861097_+|23S-rRNA-(guanosine(2251)-2'-O)-methyltransferase-RlmB	gnl|CDD|223640	COG0566, SpoU, rRNA methylases [Translation, ribosomal structure and biogenesis].	2.26155e-72
NZ_CP012897.1|WP_054766187.1|2857949_2858507_+|CDP-alcohol-phosphatidyltransferase	gnl|CDD|223632	COG0558, PgsA, Phosphatidylglycerophosphate synthase [Lipid metabolism].	0.000141128

Protein sequences

>NZ_CP012897.1|WP_054766179.1|2845871_2847560_-|cisplatin-damage-response-ATP-dependent-DNA-ligase
MRAFAELLDRLSLTASRNAKLVLVRDYLKATPDPDRGWALAALTGDLTFDAAKPAMIRKAVEGRVDATLFGWSYDYVGDLAETVALIWPGQSDHRPNREPELGEVVDALRAAGRTEVRALLETWLDALEPKGRWALLKLMTGGLRVGLSARLAKTAAAMMRPAEAVAPPKAEGGEARAVLEPVDVSAVEEVWHAVDPPYADLFAWLEGRAERPSPDAPGRFRPVMLAVAVDETADLPRLDPADYAAEWKWDGIRVQAVVEGGVRKLWSRTGDEISAAFPDVMETLAFAGALDGELVVWRDGAVAPFGDLQQRLNRKTVDAKAMAAFPAAVIAYDLLADETGDLRALPLRDRRARLEALVGAHPEARLHLSPLVDYADWTELARLRADPPVGAAAEGLMLKRWDSPYVAGRPKGPWFKWKRDPHVIDAVLMYAQRGHGKRSSFYSDYTFGVWTEAGALTPVGKAYFGFTDEELKQLDKFVRDHTVERFGPVRSVRAERDFGLVLEIAFEGLQRSSRHKSGVAMRFPRISRIRWDKPAREADTLDGVMDLLDALESGGGRVARS
>NZ_CP012897.1|WP_054766178.1|2844419_2845850_+|D-alanyl-D-alanine-carboxypeptidase
MLSLFRRGLFAVLALSLVFSANVRPIEAQAQSQENSRYAAIVIDAASGEVLFSRHADARRYPASLTKMMTLYLTFEALSQGRVKADDVLTVSPHAASQPPSKLGLAAGQTITLDDAMRATAVRSANDMAVAIAEHVGGSESRFTSLMTQKAQQLGMTQTRYFTANGLPDARQVTSARDQAILARAIMRDFPQYYSYFGLHDWAYNGRSYRNTNGLLPTGNGYDGMKTGYTNASGYNLAASAVRDGRRLITVVLGGRSSASRNAHVAELMDTGFEVERRRAQGESIQIAQSFFEQRGFGVGSEALSPSAPVAYAALSDDEDAIGGETSAVAYTAAPAPAALPTRITPAPSERRAAADTAGRAPANLTASLNGGSGAAAPARRTTPPPAREAARAAPSRASGRWAVQVGAFKDEKVASDWLTEVNRRFRTQFANAERNVQTAGEWYRSRFTGLTEDAAKAACEALSERRVTCMVVRPD
>NZ_CP012897.1|WP_054766995.1|2843696_2844176_-|TIGR01841-family-phasin
MADTAETIKKTADSAAKAQNQAQAHAAEFQAAGAKALREGIDKSVASLTELNAHGKKNLDAVVESATVAQKGAEALSQQALGFAKTSWEDGVAAAKELSTARSVQEFFELQTTWAKKSMERYMSELAKTNEIVTTTVKDSLKPINERVTASVETFQAAR
>NZ_CP012897.1|WP_054766177.1|2843148_2843637_+|nuclear-transport-factor-2-family-protein
MSVALAAAPLAALALLAAPSPGQTLRESVMAADARLFSVFFEACDPATLRTLVTDDFEFFDDRGGRVATDADGFVAQYADRCQDRLAPDAWRSRREALADAVAVYPIENYGAVETGEHVFYERRGDGPETRVGRARFTQMWKREGETWKLARVFSYDHTPLP
>NZ_CP012897.1|WP_054766176.1|2842651_2842981_-|ATP-dependent-Clp-protease-adapter-ClpS
MPIQRPGETGGGQGTAVVTETKPKLQKPSLYRVLILNDDYSPMEFVVYVLERFFQKSREEATRIMLHVHQHGVGVCGVYTYEVAETKVAQVIETARRHQHPLQCTMEKD
>NZ_CP012897.1|WP_054766175.1|2840334_2842638_-|ATP-dependent-Clp-protease-ATP-binding-subunit-ClpA
MPSFSRPLEETLHRAVGYANARRHEYATLEHLLLALIDDPDAANVMRACNVDLSALKAALNLYVDNDLAALATADGEDAKPTAGFQRVIQRAVIHVQSSGREEVSGANVLVAIFSERESHAAYFLQEQDMTRYDAVNFIAHGIAKKAGAGEARPAKGASPEEAEDQSAVKQGGEALEAYCVDLNEKSRQGKVDPLIGRQAEVERSIQILCRRTKNNPLLVGDPGVGKTAIAEGLARKIVNGEVPDVLKDATIYSLDMGALLAGTRYRGDFEERLKQVVKELENHDNAVLFIDEIHTVIGAGATSGGAMDASNLLKPALASGSLRCMGSTTYKEYRQHFEKDRALVRRFQKIDVNEPTVEDTVKILKGLKTYYEQHHKVRYTDSAVRTAVELSARYMTDRKLPDKAIDVIDEAGASQMLLTESKRKKVIGQKEVEAVIAKMARIPAKSVSKSDTESLRELEVDLKRVVFGQEQAIEQVSAAMKLARAGLRDPNKPIGSFLFSGPTGVGKTEVARQLASTLGIEMQRFDMSEYMERHTVSRLIGAPPGYVGHDQGGLLTDAVDQHPHSVVLLDEIEKAHPDVYNILLQVMDNGLLTDAVGKKVDFRNVILIMTTNAGAADNARASIGFGRGKVEGEDEKAIQRLFAPEFRNRLDAIVAFKPLQADTIRSVVTKFILQLEAQLADRNITIELTDEAADWLAKNGFDELYGARPLARVIQDSIKKPLADDILFGRLTRGGHVKVQLKDGKIDFDIKSAGGVPAKSEEEETA
>NZ_CP012897.1|WP_054766174.1|2838566_2840243_-|class-I-SAM-dependent-methyltransferase
MGQVEQIEEAAALLAQAERRQADGDLHGAFAAYKACLKAAPDFAPALSGLGLFLAEHGDPGTAAQLLSRATAVGDDVLRRRTEPTFARLLAGLTPNAWNAVLDRDLQTCLASPTVDPQTLARVTAETLLLKQARFDGSASMLSDMGRDPLWLAFLSRCVNVSPAMEARLDAVREALAEMSVEGGRPDATIGVLIAALGVNGFASEYVASARQAEGVAAILYRPPTPADVSALGEGEIQAQLIRRAVDEPARERNLARTVPAFTPDCEDAVSEAVKDQYEANPYPRWSAPPSPRPRPLREAVSVLPGLDRKAFGDRVETVLIAGCGTGFEPIDLARMDPSLAITAMDLSRASLAHGMRVAEDLGLTQIRFVQGDILKLDQVQARFDVITSTGVIHHMARPEDGLARLAGVLRPGGAVRLGLYSERARAVVRAAHDLIRERAWTPVETDIRAFRAHVLALPEGEPLAALRESADFYSLSGCRDLVFHVQEHRYTPPLLGELIAGAGLRLVGFEASAEAKAAFATAFGRADPLDLQLWDQLETRQPRLFAGMYHLWAQRPA
>NZ_CP012897.1|WP_054766173.1|2837259_2838408_+|N-acetyltransferase
MTFTLTVHDGIADIGREAWDACACPTGDPFVSYDFLHACEASGSAAPHQGWAPRHLALRDEDDAVLGVMPLYLKGHSQGEYVFDHSWADAYERAGGRYYPKLLGAVPFTPATGPRFLNHPDTDAATVRQALLQGALTLVERLGVSSLHVNFPTETEWTDMAQAGLLLRQDIQFIWRNDGYQTFDDFLAALSANRRKTIRRERRDAQAGLDIRILTGADIAEAHWDAFFAFYMDTGDRKWGRPYLTRDFFSRVGATMADRIALVMAFRDERPIAGALNFIGRDALYGRQWGALEDVPFLHFELCYYQAIEFAVARGLSRVEAGAQGEHKIARGYLPSPVYSAHFIADPALRGPVADYLRREGPAVEAQRREMTEELSPFKKEN
>NZ_CP012897.1|WP_054766172.1|2836804_2837263_+|RidA-family-protein
MTIESRIAELGITLPEPAKAVANYVPFVQSGAVVHISGQLSNDASGGIKGTVGVDVTPEQAAAAARLCGINLLAQIKAACDGDLGRVVRIVKLGGFVQAGPEFEAIPAVINGCSDLMVEVFGDAGRHARSAVGVYKLPLGFAVEVDAVVEIR
>NZ_CP012897.1|WP_054766994.1|2835795_2836701_-|hypothetical-protein
MDLHLTSDVAAFQAVLARLSPSDWAHVDAAMEPAGAKAAEAAPHWDFEMPARAVDAVLGASASDAVRRGLIASWALRLPDRVATLALPPEVLSLYPYWIEQLAAFLTQAEGDYDFDHWAKDVRFSLALSVPAAKSQVIDLSSPVGPGQIIKHVRDGWGFGPLFRYLKAGAKREPWLEVHTESRWLRGFNEEGWNDAWATAAEICRTRPELAGMIGSSWFYDPPLTEISPRLAHLRLNPLKGGAFMVHQGPGEIHTQRAATASASRKALIDSGEYTARSWLMVWPRKELIAWADRRKAVALV
>NZ_CP012897.1|WP_054766996.1|2849566_2849872_-|BolA-family-transcriptional-regulator
MSDGPVATIIREKLTAALSPQRLEIEDDSWRHAGHHHEGGMDAQPGGESHFNLVIVSSAFEGVSRVLRQRRINDLLRAELAGPVHALSIKALTPAEAVHSV
>NZ_CP012897.1|WP_054766181.1|2849917_2850586_+|J-domain-containing-protein
MSASFQYKPRFTDIRVKPPKAEEEAAQADVLHLKPGEKPCQWPDCRRAATAKAPKSRERLNDFYEFCQAHAGEYNKGWNFYAGMTEGEIRAAQENEAMTGGRPTWEMKAGRFTREAAAFSAKMGTSNTTGAGSWRDSFGLFGRRGDQAPQSPTEDRRVGKLERGALADLDLEPGADKAAVKARYHEMLKRFHPDTNGGDRGAEAKLQRVIKAWKTLKKAGLA
>NZ_CP012897.1|WP_054766182.1|2850598_2851276_-|SDR-family-oxidoreductase
MKRAIVTGGAGLIGAGICQALASEGWQVVSFDKKAAAPGTRQILCDVSDEASVAAAFEDLGWSELDLLVNNAGIADPANGPLAELSLEAWRRTLDSHLTGAFLMSRAVIPRLKEGASVVNMASTRAFMSEPETEAYAASKGALVALTHAMAISLGPKVRVNAIAPGWVADPDDVTAADHEQHPVGRVGRAKDVAQAVLYLAAAEFVTGQVLTLDGGMTRKMIYAD
>NZ_CP012897.1|WP_156314202.1|2851316_2852489_-|N-acetylmuramoyl-L-alanine-amidase
MTALAFVVICACVLFATRGFAWGAQGDVLAVRFGADRDRTRVVIDLDKSTQGRVINAGDGGRITLALAGVAPGRGLNGGGSGLVRAYQVTAVGGASRVELELARDSQIERRFLLPPGDGVAHYRYVVDLKANGGAVGPAAQRVSPTPAPRRAEKPLVVIDAGHGGRDPGASGAKVSESEVTLAAALTLKAELERTGRYRVLLTRETNTYVDLYRRVAIARRADADLFISLHADAGTDPAVRGASVYTLSEQGAGRAVREFTRSDNWHRELHLPGRDPSVDRILLDMTQRATQNRSAQFARVLLTHLEASDHPLLRRSHRDAGLAVLLAPDVPAVLLEMGFITNPEDERLLTDERARRRLMRSVADGIDRYFREPAAALMTASNDGPAGQP
>NZ_CP012897.1|WP_156314247.1|2853010_2855665_+|Rne/Rng-family-ribonuclease
MLIDAAHPEETRVAIVDGRQIEEFDFESRAKRQLRGNIYLAKVTRVEPSLQAAFVEYGGNRHGFLAFNEIHPDYYQIPVADREAIMAEAHDDEDEDDLDRESTGDDVDPEAALADEERLKRRLMRRYKIQDVIKRRQILLVQVVKDERGAKGAALTTWLSLAGRYCVLMPNTGKGGGISRKITNTSDRRRLKSAVAALDVPKGMGLIIRTAGAKRTKAEIKRDYQYLLRLWETIRETTLASHAPSLIYEEENLVRRAVRDMFDKDFDGIQVEGVEGFKEARDFMRVLMPAQAKKVHLYRGSRPLFAANGIEELLTQIHQPVVPLKSGGYLVVNQTEALVAIDVNSGRATKERNVEQTAFKTNLEAAEEAARQLRLRDLAGLVVIDFIDMDEGKNNRTVERVLKEALSTDRARIQMGRISPFGLMEISRQRRRLGVIEGATEACPHCQGTGRIRSAESAALMTLRAVDIEAGKNGAGVVVLKVCTAVGLYILNHKRAYLQSLLERRGLNVIVQIDDSLGQGEHNIERTETNEDFVAPEIEMPILDDDFDASLYEDEDEEDDEEIIADDEDDDLDALDREDSDDDEPRERAERHDGGGRGRNRRRRRGGRRDEEGGETDTADTMDVADASDDEDDENGRRRRRGRRGGRRVREDGERDVYSWVRGRTPSLDNPYVWFDPLNPGRPEPRSDRAERGDRPAAAEAEVEGLNVVAAASGGEEGGRSRRRRRRGRGRGGDAQDLKADAAVAETADETPEAAVLTETVAAEAQPEAQAEPQSAVQPEPQRRRVRRKTAAAPTVATPAEAEVEVEVESETPAAAVTPEPEPVQPEATPTAVEADQPVLTAATAELETFEAPKPEVDIEAIIAEDPNQIVAPPEKPKRGWWRR
>NZ_CP012897.1|WP_156314248.1|2855771_2857124_+|M48-family-metalloprotease
MAFAALVAAGQASAQSLIRDTEIEGIIREWVDPVFVSMGLNPSDVEVLLVNDNELNAFATRGRIMGVNTGLILRTKNPNELLGVMAHEAGHIKNRHTQRDGAQNAAKQPMFMTMALGALAIAAGAPDAGVALLGSSQYFGTIGALQYMQSQEGEADLTGARALEAAGESGAGLVSFFENFRAQEVFSDARRYPYFRSHPLSSQRIESLRRFVQDQPHYDHRDSPERMAQHALILAKIHAFMDPPNTTLRAYPSSDVSLPGRYARAIAWYRDGQTDKALTAVDALIAEDPQNPYFAELKGQIYFEEGRPAEAVAAHREAVRLKPDAPLLRINLAHALIGTEDPKNLDEAIDQLKHATVAERENTMAWRLLGQAYAAQGKEGEARLATAEYYFAAGQEQQATQFALRARSMLDPNSIEWRRAVDIVLASGATPDDLLDLDRREAGRRPATLN
>NZ_CP012897.1|WP_054766186.1|2857152_2857938_+|thioredoxin-domain-containing-protein
MTHDAPAPETPAAPPAPARRMNGAVAGYVALGVSVVALGLAAAPYLGGGSSDVRAYLLEHPEVLQEASLALQAKEGQARVDETNQAAAANAALLAPDRRDPAFGPADAKVTVIEFFDFRCPGCKAVAPQYRALMAAHPDVRFVFKDWPILDRGEDITSQYAARAALAAHQQGKYLEVYDALMTERALTPETIDRILVEHGVDLARAKATLAAPDTTRHIADIHTTAAALKLQGTPTFFVNGMAAASIDPAEIARMIEAAKR
>NZ_CP012897.1|WP_054766187.1|2857949_2858507_+|CDP-alcohol-phosphatidyltransferase
MRRLPWALVIFRLVAAPALLGLALIGPSAAITAAVLLSLAVLSDILDGVIARRLDCVTPNLRHWDSRADVVFWLGAAIALLLMHPALVATLLPPALALVALETANHALSIAKFRREASPHHWMSKVFCLALWALFAQLFVTGQPTALLWAAFGLGVISQIEAAAITLRLKTWRCDVPSVFSLNSR
>NZ_CP012897.1|WP_054765980.1|2858585_2859776_-|elongation-factor-Tu
MAKEKFERTKPHCNIGTIGHVDHGKTTLTAAITMTLAKAGGAKAMNYADIDAAPEEKARGITINTAHVEYETANRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPALVVFMNKVDLVDDEELLELVEMEVRELLSSYQFPGDEIPITKGSAKAATDGVNPEIGEQRILALMETVDSYIPQPERPVDLPFLMPVEDVFSISGRGTVVTGRVEKGIIKVGEEVEIVGIRPVQKTTCTGVEMFRKLLDQGQAGDNVGVLLRGTKREDVERGQVLCKPGSITPHTKFLAEAYILTKEEGGRHTPFFTNYRPQFYFRTTDVTGIVKLKEGVEMIMPGDNAELNVELITPIAMDQGLRFAIREGGRTVGAGVVAKIVE
>NZ_CP012897.1|WP_082382719.1|2860212_2861097_+|23S-rRNA-(guanosine(2251)-2'-O)-methyltransferase-RlmB
MSSKSERNDRRSGKKPIPANPSSGPRERGQKPVAKGFSGREDASRTPRSPDRGKADADNFLWGRHPVLAALANPARRGMGRLLATPERAAEIEEGRLAHGHKIEVVEGQILTRMLPPGAVHQGLAFKVQPLEGVSLDDLADPAQGVIVMLDQLTDPQNVGAIFRSALAFGARGIVVQDRHAPALAGALAKAAVGATERLPHARVTNLSRALERLADLGWRAVGLDGSAEQTLEEALDAQPTVLVMGSEGDGIRRLVAEHCDVLAKIPMPGGFESLNVSNAAAVALYEAARAQRG

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity
NZ_CP012897_3	3.1|2848115|25|NZ_CP012897|CRISPRCasFinder	2848115-2848139	25	MN703405	Mycobacterium phage Aneem, complete genome	14923-14947	5	0.8
NZ_CP012897_3	3.1|2848115|25|NZ_CP012897|CRISPRCasFinder	2848115-2848139	25	MH338237	Mycobacterium phage Joselito, complete genome	14923-14947	5	0.8
NZ_CP012897_3	3.1|2848115|25|NZ_CP012897|CRISPRCasFinder	2848115-2848139	25	MK524507	Mycobacterium phage Orange, complete genome	14923-14947	5	0.8
NZ_CP012897_3	3.1|2848115|25|NZ_CP012897|CRISPRCasFinder	2848115-2848139	25	MK524514	Mycobacterium phage Bud, complete genome	14929-14953	5	0.8
NZ_CP012897_3	3.1|2848115|25|NZ_CP012897|CRISPRCasFinder	2848115-2848139	25	MN310547	Mycobacterium phage Hutc2, complete genome	14926-14950	5	0.8
NZ_CP012897_3	3.1|2848115|25|NZ_CP012897|CRISPRCasFinder	2848115-2848139	25	NC_031257	Mycobacterium phage Mulciber, complete genome	14923-14947	5	0.8
NZ_CP012897_3	3.1|2848115|25|NZ_CP012897|CRISPRCasFinder	2848115-2848139	25	MH338236	Mycobacterium phage Ebony, complete genome	14972-14996	5	0.8
NZ_CP012897_3	3.1|2848115|25|NZ_CP012897|CRISPRCasFinder	2848115-2848139	25	MK494130	Mycobacterium phage Fibonacci, complete genome	14926-14950	5	0.8
NZ_CP012897_3	3.1|2848115|25|NZ_CP012897|CRISPRCasFinder	2848115-2848139	25	MK524511	Mycobacterium phage Bowtie, complete genome	14923-14947	5	0.8
NZ_CP012897_3	3.1|2848115|25|NZ_CP012897|CRISPRCasFinder	2848115-2848139	25	MK524519	Mycobacterium phage Salz, complete genome	14920-14944	5	0.8
NZ_CP012897_3	3.1|2848115|25|NZ_CP012897|CRISPRCasFinder	2848115-2848139	25	MN586006	Mycobacterium phage Bachome, complete genome	14920-14944	5	0.8
NZ_CP012897_3	3.1|2848115|25|NZ_CP012897|CRISPRCasFinder	2848115-2848139	25	MK524513	Mycobacterium phage Munch, complete genome	14923-14947	5	0.8
NZ_CP012897_3	3.1|2848115|25|NZ_CP012897|CRISPRCasFinder	2848115-2848139	25	MF140410	Mycobacterium phage Et2Brutus, complete genome	14926-14950	5	0.8
NZ_CP012897_3	3.1|2848115|25|NZ_CP012897|CRISPRCasFinder	2848115-2848139	25	MH536828	Mycobacterium phage Snape, complete genome	14926-14950	5	0.8
NZ_CP012897_3	3.1|2848115|25|NZ_CP012897|CRISPRCasFinder	2848115-2848139	25	KY471460	Mycobacterium phage Jabith, complete genome	14975-14999	5	0.8
NZ_CP012897_3	3.1|2848115|25|NZ_CP012897|CRISPRCasFinder	2848115-2848139	25	MN892487	Mycobacterium phage Mabel, complete genome	14987-15011	5	0.8
NZ_CP012897_1	1.1|963888|42|NZ_CP012897|CRISPRCasFinder	963888-963929	42	NZ_CP017076	Novosphingobium resinovorum strain SA1 plasmid pSA1, complete sequence	715155-715196	7	0.833
NZ_CP012897_1	1.1|963888|42|NZ_CP012897|CRISPRCasFinder	963888-963929	42	NZ_CP017076	Novosphingobium resinovorum strain SA1 plasmid pSA1, complete sequence	1624671-1624712	9	0.786
NZ_CP012897_1	1.1|963888|42|NZ_CP012897|CRISPRCasFinder	963888-963929	42	NZ_CP017076	Novosphingobium resinovorum strain SA1 plasmid pSA1, complete sequence	1396039-1396080	9	0.786

1. spacer 3.1|2848115|25|NZ_CP012897|CRISPRCasFinder matches to MN703405 (Mycobacterium phage Aneem, complete genome) position: , mismatch: 5, identity: 0.8

cgccggtcgcgacagggcgaaccca	CRISPR spacer
gtccggtcgcgccagggcgaacctg	Protospacer
  ********* ***********..

2. spacer 3.1|2848115|25|NZ_CP012897|CRISPRCasFinder matches to MH338237 (Mycobacterium phage Joselito, complete genome) position: , mismatch: 5, identity: 0.8

cgccggtcgcgacagggcgaaccca	CRISPR spacer
gtccggtcgcgccagggcgaacctg	Protospacer
  ********* ***********..

3. spacer 3.1|2848115|25|NZ_CP012897|CRISPRCasFinder matches to MK524507 (Mycobacterium phage Orange, complete genome) position: , mismatch: 5, identity: 0.8

cgccggtcgcgacagggcgaaccca	CRISPR spacer
gtccggtcgcgccagggcgaacctg	Protospacer
  ********* ***********..

4. spacer 3.1|2848115|25|NZ_CP012897|CRISPRCasFinder matches to MK524514 (Mycobacterium phage Bud, complete genome) position: , mismatch: 5, identity: 0.8

cgccggtcgcgacagggcgaaccca	CRISPR spacer
gtccggtcgcgccagggcgaacctg	Protospacer
  ********* ***********..

5. spacer 3.1|2848115|25|NZ_CP012897|CRISPRCasFinder matches to MN310547 (Mycobacterium phage Hutc2, complete genome) position: , mismatch: 5, identity: 0.8

cgccggtcgcgacagggcgaaccca	CRISPR spacer
gtccggtcgcgccagggcgaacctg	Protospacer
  ********* ***********..

6. spacer 3.1|2848115|25|NZ_CP012897|CRISPRCasFinder matches to NC_031257 (Mycobacterium phage Mulciber, complete genome) position: , mismatch: 5, identity: 0.8

cgccggtcgcgacagggcgaaccca	CRISPR spacer
gtccggtcgcgccagggcgaacctg	Protospacer
  ********* ***********..

7. spacer 3.1|2848115|25|NZ_CP012897|CRISPRCasFinder matches to MH338236 (Mycobacterium phage Ebony, complete genome) position: , mismatch: 5, identity: 0.8

cgccggtcgcgacagggcgaaccca	CRISPR spacer
gtccggtcgcgccagggcgaacctg	Protospacer
  ********* ***********..

8. spacer 3.1|2848115|25|NZ_CP012897|CRISPRCasFinder matches to MK494130 (Mycobacterium phage Fibonacci, complete genome) position: , mismatch: 5, identity: 0.8

cgccggtcgcgacagggcgaaccca	CRISPR spacer
gtccggtcgcgccagggcgaacctg	Protospacer
  ********* ***********..

9. spacer 3.1|2848115|25|NZ_CP012897|CRISPRCasFinder matches to MK524511 (Mycobacterium phage Bowtie, complete genome) position: , mismatch: 5, identity: 0.8

cgccggtcgcgacagggcgaaccca	CRISPR spacer
gtccggtcgcgccagggcgaacctg	Protospacer
  ********* ***********..

10. spacer 3.1|2848115|25|NZ_CP012897|CRISPRCasFinder matches to MK524519 (Mycobacterium phage Salz, complete genome) position: , mismatch: 5, identity: 0.8

cgccggtcgcgacagggcgaaccca	CRISPR spacer
gtccggtcgcgccagggcgaacctg	Protospacer
  ********* ***********..

11. spacer 3.1|2848115|25|NZ_CP012897|CRISPRCasFinder matches to MN586006 (Mycobacterium phage Bachome, complete genome) position: , mismatch: 5, identity: 0.8

cgccggtcgcgacagggcgaaccca	CRISPR spacer
gtccggtcgcgccagggcgaacctg	Protospacer
  ********* ***********..

12. spacer 3.1|2848115|25|NZ_CP012897|CRISPRCasFinder matches to MK524513 (Mycobacterium phage Munch, complete genome) position: , mismatch: 5, identity: 0.8

cgccggtcgcgacagggcgaaccca	CRISPR spacer
gtccggtcgcgccagggcgaacctg	Protospacer
  ********* ***********..

13. spacer 3.1|2848115|25|NZ_CP012897|CRISPRCasFinder matches to MF140410 (Mycobacterium phage Et2Brutus, complete genome) position: , mismatch: 5, identity: 0.8

cgccggtcgcgacagggcgaaccca	CRISPR spacer
gtccggtcgcgccagggcgaacctg	Protospacer
  ********* ***********..

14. spacer 3.1|2848115|25|NZ_CP012897|CRISPRCasFinder matches to MH536828 (Mycobacterium phage Snape, complete genome) position: , mismatch: 5, identity: 0.8

cgccggtcgcgacagggcgaaccca	CRISPR spacer
gtccggtcgcgccagggcgaacctg	Protospacer
  ********* ***********..

15. spacer 3.1|2848115|25|NZ_CP012897|CRISPRCasFinder matches to KY471460 (Mycobacterium phage Jabith, complete genome) position: , mismatch: 5, identity: 0.8

cgccggtcgcgacagggcgaaccca	CRISPR spacer
gtccggtcgcgccagggcgaacctg	Protospacer
  ********* ***********..

16. spacer 3.1|2848115|25|NZ_CP012897|CRISPRCasFinder matches to MN892487 (Mycobacterium phage Mabel, complete genome) position: , mismatch: 5, identity: 0.8

cgccggtcgcgacagggcgaaccca	CRISPR spacer
gtccggtcgcgccagggcgaacctg	Protospacer
  ********* ***********..

17. spacer 1.1|963888|42|NZ_CP012897|CRISPRCasFinder matches to NZ_CP017076 (Novosphingobium resinovorum strain SA1 plasmid pSA1, complete sequence) position: , mismatch: 7, identity: 0.833

cgctacgct-cgcgatgcgttcccgccttcgcgggaatgacga	CRISPR spacer
-gctacttcacgagatgggttcccgccttcgcgggaatgacgg	Protospacer
 ***** .. ** **** ************************.

18. spacer 1.1|963888|42|NZ_CP012897|CRISPRCasFinder matches to NZ_CP017076 (Novosphingobium resinovorum strain SA1 plasmid pSA1, complete sequence) position: , mismatch: 9, identity: 0.786

----cgctacgctcgcgatgcgttcccgccttcgcgggaatgacga	CRISPR spacer
gaaccgtca----ggagatgggttcccgccttcgcgggaatgacga	Protospacer
    **..*     * **** *************************

19. spacer 1.1|963888|42|NZ_CP012897|CRISPRCasFinder matches to NZ_CP017076 (Novosphingobium resinovorum strain SA1 plasmid pSA1, complete sequence) position: , mismatch: 9, identity: 0.786

cgctacgct-cgcgatgcgttcccgccttcgcgggaatgacga	CRISPR spacer
-gcggcgtcaggagatgggttcccgctttcgcgggaatgacga	Protospacer
 ** .**..  * **** ********.****************

Prophage detection

Region	Region Position	Protein_number	Hit_taxonomy	Key_proteins	Att_site
DBSCAN-SWA_1	1280512 : 1286075	9	Rhodobacter_phage(40.0%)	capsid,protease,head,portal,tail	NA
DBSCAN-SWA_2	1613330 : 1620529	10	Paracoccus_phage(50.0%)	capsid,protease,head,terminase,portal,tail	NA

Sequences of DBSCAN-SWA_1

Nucleotide sequences of DBSCAN-SWA_1

>NZ_CP012897|1280512:1286075|DBSCAN-SWA
GATGGGTGGGATGCGGTGGCCGTTCGGCCGGGGCGGGCGTGCGCCCGATCCGGGCGCGCCGGAGGCGAAGACCAGTCGGACGGCGGTGCTGCTGTCGGGCGTCGGGCGGGCGCGGTGGACGGGCAATGACTACGCCGGCCTGGCGCGCGAAGGCTATCAGAAGAACGCCGTGGCCTATCGCTGCATCCGCATGATCGCGGAGGCGGCGGCCTCGGCGCCCTTTGCGGTCTTTGTGGACGGGGTGCGCGACGAGACCCATCCGCTGGCGCGGCTGATCCGCCGGCCCAATCCCGAACAGTCGGGGGCGGAGCTGATGGAGGCGGTTTACGGATCGCTTCAGGTCTCGGGCAACGCCTGGGTGGAAGCGGTGGGGGACGCGGTTCCCGAGGAGCTGTGGGCGCTCAGGTCGGACCGGGTCAAGGTGGTTCCCGGCCGGTCGGGCTGGCCCGAGGCGTGGGATTATTCCGTAGACGGACGGTCGATCCGGATCGGGCGGGCGGCTGACGGCTGGGCGCCGGTGATGCAGCTGAAGCTGTGGCATCCGCTGGACGACTGGTACGGCCTGTCGCCGCTGGAGGCGGCGGCGCAAGGGGTGGATGCGCACAATGCGGCCGGGGCCTGGAACAAGGCCCTGCTGGACAATGGGGCGCGGCCGTCCGGCGCCCTGATCTATGGGGCCAAGGGCGGCGAGCGGCTGACCGACGGACAGTTCGAGGCGCTGAAGGCCCAACTGTCCAGCGCCTACGCCGGGGTGGAGAACGCCGGGCGGCCGATCCTGCTGGAAGGCGGGATGGACTGGAAGCCCCTGAGCCTGACCCCCGCCGAGATGGACTTCACCGCCGGGCGACATGCGGCGGCGCGCGAGATCGCCCTGGCCTTCGGGGTTCCGCCGCAGCTGCTGGGGATACCGGGGGACGCCACCTATTCCAACTATCGCGAGGCCAACACCGCCTTCTGGCGACAGACGGTCATCCCCCTGGTGCGCAAGGCGGCGGGCGCGATGACCGGCTGGCTGGGCGGACGGTTCCCCGGCTGCGAGGTGCGGGCCGATCTGGAGGCCGTGCCGGCCTTGCAGCCCGAACGCGACGCCCTGTGGGCGCGGCTGGAGGCGGCCAGCTTCCTGACGGACGCGGAGCGGCGACGGATGGCGGGGGTGGAGGGATGAGGAAGGCGTGGCGAGTGTCGAGTGGCGAGTGGCGAGGGAGACGTGACGCATGAGCGACGACTCTCAGGTCCGGCGCGTGCCGACCGCCCTGGTGATCGCGGTGGTGGTGCAGACCATCGGCGGACTGGTCTGGGCGGGCGGGGCGGCGGCGCGGATCGCGACCCTGGAGCAGAGGGTCGGGGAACAGAGGCTGGTGGCCGAACGGCTGGCGCGGCTGGAGACCCAAGGCGAGGCGACGGCGGCGGCTGTCGAGCGGATCGAACGGCGGCTGGAGGGGGGCGGGTGAGTGGTTAGTGGCGAGTGGCGAGTGGCGAGTGGTGAGGCGAACCAGGCGATTGGACGAAGGCAGGCGCGACTTCGCTCGCCCCTCGCCCCTCGCCACTCGCCACTCCTGATCCAGGGCTACGCCTCCCTGTGGGGCGTGGCGGATCTGAACGGGGACGTGGTCCAGGCGGGGGCGTTCGCCGACAGTCTGGCGAAGACGGGCGCCGAAGGGGTGCGGATGCTGAACCAGCACGACGGCCGGGCGCCGGTCGGGGTCTGGGACGAGGTGCGCGAGGACGAACGCGGCCTGTTCGTGCGCGGCCGGATCGAGGACTGGTCGCCCGAGGCCCGCTTCGCCGCCGCCCTGAGCCGGGCGGGGGCGATGGACGGGCTGTCCATCGGATACCGCACGGCGCGGGCGCGGCGTCAGGGACGTTTGAGGGTGCTGAGCGGGGTCGAGCTGTGGGAGGTGTCGCTGGTGACGTTTCCCATGCTGCCGGGGGCGCGGTTTAGGGTGTCGGGGGTGTGACGGGGCCGGGCCGATCGTGAATGATACTCTAAGACCGTCATCCTCGGGCTTGACCCGAGGATCGAGCGATCCGCCGCTTGAGCAAAGACGCGGGCGCAGAGCCTGGCCAGGGGCCGATCCTCGGGTCAAGCCCGAGGATGACGGGTCTGGCTGAGCGGTCTGGGCCGTGGGCGGATCGCGCCAGATGACCGCGATCCCGATTCTAGCGGCTTCAGCTTTTGGGCGTGGCGGCTTCGATATTGGCCTGGAGGGCCTGCATTTCGGCGGTGATCGCTTCCATTTCCGCCGTGCATTCGTCGGAGGAGATGGTGGCGGCGCGCGGGGACGCCTTGCCCTTTTCATAGGCCGCCAGGAGGAACTCGGAGGCCGCCTTCTTTTCCGGATCGGTCTCATTGGCCAGGGCGGCGCGGACCTCTTGCGCGACGTCGGGCGGGAACTGGCGTTCGCACGTGCCCAGGGTTTCGAACATGCGCGTCATGCCGGCGAAGACCTGATTGACCTGTTTCGCCTGTTCGGGCGGCAGGCCGGAGGTGTCGGGCGGCGTCTGAAGCGCCAGGGCGCCGGCGAAGGCGAGAACGAGACTGAACATGGGTGAAGCTCCTCCGTCACGCGGAGTAGCACGATTTTCGAGGGACGGCTGCCGTCCATCACAGGTTTCGGGCCACGCCCGGATCACGCGGCGCCGAAGACGGGCGCCTTCACACCGGAGACATCATGAAAGAGACCAAACAGGCTTCGGGCCATCCCGAGGCGCACGGCGCCGTGCGCGAGATGATGGCGGCGTTCGAGGCGTTCAAAGGGGCGAATGACGCCCGGCTGGGCGAGATCGAGAAGAAGGCGGCGGCCGATGTGCTGCTGGAGGAGAAGGTCGCCCGGATCGACCAGGCGGTGGCGGCGGCCCAGGCGCGGCTGGACCGGGTGATGAGCCAGAACCGGCGTCCGGCGATCGGCGGCGAGCCGGTGGAGCCTGTGTCGGCGCCCGAGGCGAAGGCGGCGTGGGACGGCTATCTGAAGACGGGCCACTCGCCTCAACTGGCCGGCGCCCTGGAGGTCAAGGCGGGACTTTCGACGGGGGCGACCTCGGGCGGCTATGTCGCGCCCTATGAGACCGAGCGGGCCATCGAGCGGCGGCTGATGGCGGCCTCGCCGATGCGCGAGATCGCGACGGTCAGGACGGTGGCGGCGGGCGTGTTCCGAAAGCCGGTCTCGACGGCGGGCGTGGCCTGCGGCTGGGTGGCGGAGACGGCGGCGCGGCCCGAGACCGATCCGGCGACCCTGGCCCTGCTGGAATTCCCCTCGGCGGATCTGTACGCCAATCCGGCGGCGACCCAGGCCCTGCTGGACGACGCCATGGTCGATCTGGACGAATGGCTGGCGGCCGAGGTCGAGGACGCCTTTGCGGCCCAGGAGACCCAGGCCTTTGTGGCCGGCGACGGGGTGAACAAGCCCAAGGGCTTTCTGGCCTATCCGACGGCGGCGGACGCGGGTCAGGTCTGGGGCCAGATCGGTTATGTGGCCTCGGGCGCCGCAGGCGGGTTCGCGGCCGACAGTCCGACCGACCGGCTGATCGACCTGATCTATGCGCCCAAGGCCCAGTATAGGCCGAACGGCCGGTTCGTGATGAACCGGAAGACGGTCTCGGCCGTGCGCAAGTTCAAGGACGCGGACGGCAACTATATTTGGCAGCCGGCGACGCGGCTGGGCGAGACGGCCAGCCTGCTGGGCTATCCGGTCACCGAGATCGAGACCATGCCGGATGTGGCGGCCAACAGTCTGTCGATCGCCTTCGGGGACTTCCAGCGGGGCTATCTGATCGTGGATCGGGCGGGGGTGCGGGTGTTGCGCGACCCTTATTCGGCCAAGCCCTATGTCCTGTTCTACACGACCAAGCGGGTCGGCGGCGGGGTGCAGAACTTCGACGCCGTGAAGGTCATGAAGTTCTCCGCGAGCTGATCGGGTCGTCTCCTCCCTGTCGCGCAGCGACGGGGAGGTGGCGCGGCGCGTCTTCGCGCCGTGACGGAGGGGCTCTGCGGGCGTTGAAGAGCCCCTCCACCACTTCGTGGTCCCCCTCCCCATTGCATGGGGAGGAGACTGATTTCTGACGACGGAGATTTTCGATGGCGCAACCGGTGACGGCGGCGGAGGCGAAGCTGTTTTTGAGGGTCGAGCATGAGGCCGAGGACGGCCTGATCCAGACCCTGATTGAGGCGGCCCAGGCGCGGGTGGAGGCGGAGGTGGGGCTGAGCCTGACCTCGACCGCGCCGGCGGGGCTGAGGCTGGCGATCCTGATGCTGGTGCTGCGGGCCTATGAGCGGGGCGAGGCGGCGGCGGACCTGTCGATCGACGAATGGACCGCCCCCTATCGCACGGTGCGGCTGTGAGGGTTCTGGCGAGCCTGTTCCGGCCGGTGGAGGCCGAGACCCCCTATGGCGGGCGCAGCGTGAGCTTCGAACCCGTCGGCTCGGCCTGGCTGACCTGCGGGACGCGGCGGCGGGTCGAACGGGGCGAGGGCGATCAGAGGCGGACGGTCGAGCGGCTGAGCGCCGAGGCGCGGGCCGACGCGCGGCTGGCGGTCGGGCGGGTGCTGCGGTTCGGCGGCGCCGACTGGGACATCGTCGGCCTTGATCCTCTGCGGCCGGGGCGGCTGCGGCTGGAGCTGGAGCGGGTACGATGAAGGATCATGAGAGCGCCCTGCAAAAGGCGGTGGTCGCGGCCCTGAAGGCGGATGCGGCGGTGTCGGCCCTGATCGGCGGGCGGGTGTTCGACCGGCCGCCGGAGGGCGCGGCCTGCCCCTATCTGGCGCTGGGCCGATGCGAGAGCCGGCCGCTGGCGGCGGACGGGGGCGGGGTGGAGCAGAGGCTGACCCTGACCGGGGTGTCGCGCTTCCTCGGCGCGGAAGAGGCCAAGGCGATGGCGGCGGCGGTGCGGGCCTGTCTGCACGAGGCGGTGCTGGAGGCGGACGGGGTGCGGACCGCGACCCTGAGGGCGACCTTCGCCGACGTGTTCGGGGCGAGCGACGGACGGCGGACCTATGCGGTGGTGCGGCTGAGGGCGGTGACCGAGGAAGTGGCGAGTGGTTAGTGGCGAGTGGCGAGTTGGGTCGGGAAGGCGGAAGCAGCGGGGGGAGCCGTTGCGACGACCTTCCTCGCCACTCGTCACTCGCCACCCGCCACTCAGGAGCAAAGCGAGGACAAGATGACCGCACAGGCGGGCAAGGACATGCTGCTGAAGATCGAGGGCGCGCCGGGCGTCTTCACGACGGTGGCGGGGTTGAGGGCGCGGACGATTTCGCTGAACGCGCGCACGGTGGACGCCACCGACGGCGACAGCGCCGGACGGTGGCGCGAACTGCTGGCCGGCGCCGGGGTCAAGTCGGCGGCGGTGTCGGGCCAGGGGATCTTCCGCGATGCGGCCTCGGACGCCCTGGTGCGGGAAGCCTTCTTCGATCAGGCGGCCAAGCGGTGGCGGCTGGTGGTGCCGGACTTCGGCGTGCTGGAGGGGCCGTTCCTGGTAGCGGCCCTGGAATACGCCGGAACGCATGAGGGGGAGGCGACCTTCGCCCTGAGCCTGGCCAGCGCTGGGGCGGTCGGGTTTTCGGCGGCGTGA

Protein sequences of DBSCAN-SWA_1

>NZ_CP012897|1280512:1286075|1282680_1283058_-|WP_054764894.1|DBSCAN-SWA
MFSLVLAFAGALALQTPPDTSGLPPEQAKQVNQVFAGMTRMFETLGTCERQFPPDVAQEVRAALANETDPEKKAASEFLLAAYEKGKASPRAATISSDECTAEMEAITAEMQALQANIEAATPKS
>NZ_CP012897|1280512:1286075|1282067_1282469_+|WP_082382771.1|head,protease|DBSCAN-SWA
MIQGYASLWGVADLNGDVVQAGAFADSLAKTGAEGVRMLNQHDGRAPVGVWDEVREDERGLFVRGRIEDWSPEARFAAALSRAGAMDGLSIGYRTARARRQGRLRVLSGVELWEVSLVTFPMLPGARFRVSGV
>NZ_CP012897|1280512:1286075|1280512_1281676_+|WP_082382618.1|portal|DBSCAN-SWA
MGGMRWPFGRGGRAPDPGAPEAKTSRTAVLLSGVGRARWTGNDYAGLAREGYQKNAVAYRCIRMIAEAAASAPFAVFVDGVRDETHPLARLIRRPNPEQSGAELMEAVYGSLQVSGNAWVEAVGDAVPEELWALRSDRVKVVPGRSGWPEAWDYSVDGRSIRIGRAADGWAPVMQLKLWHPLDDWYGLSPLEAAAQGVDAHNAAGAWNKALLDNGARPSGALIYGAKGGERLTDGQFEALKAQLSSAYAGVENAGRPILLEGGMDWKPLSLTPAEMDFTAGRHAAAREIALAFGVPPQLLGIPGDATYSNYREANTAFWRQTVIPLVRKAAGAMTGWLGGRFPGCEVRADLEAVPALQPERDALWARLEAASFLTDAERRRMAGVEG
>NZ_CP012897|1280512:1286075|1283183_1284422_+|WP_054764895.1|capsid|DBSCAN-SWA
MKETKQASGHPEAHGAVREMMAAFEAFKGANDARLGEIEKKAAADVLLEEKVARIDQAVAAAQARLDRVMSQNRRPAIGGEPVEPVSAPEAKAAWDGYLKTGHSPQLAGALEVKAGLSTGATSGGYVAPYETERAIERRLMAASPMREIATVRTVAAGVFRKPVSTAGVACGWVAETAARPETDPATLALLEFPSADLYANPAATQALLDDAMVDLDEWLAAEVEDAFAAQETQAFVAGDGVNKPKGFLAYPTAADAGQVWGQIGYVASGAAGGFAADSPTDRLIDLIYAPKAQYRPNGRFVMNRKTVSAVRKFKDADGNYIWQPATRLGETASLLGYPVTEIETMPDVAANSLSIAFGDFQRGYLIVDRAGVRVLRDPYSAKPYVLFYTTKRVGGGVQNFDAVKVMKFSAS
>NZ_CP012897|1280512:1286075|1284586_1284850_+|WP_054764896.1|head,tail|DBSCAN-SWA
MAQPVTAAEAKLFLRVEHEAEDGLIQTLIEAAQARVEAEVGLSLTSTAPAGLRLAILMLVLRAYERGEAAADLSIDEWTAPYRTVRL
>NZ_CP012897|1280512:1286075|1285664_1286075_+|WP_054764899.1|tail|DBSCAN-SWA
MTAQAGKDMLLKIEGAPGVFTTVAGLRARTISLNARTVDATDGDSAGRWRELLAGAGVKSAAVSGQGIFRDAASDALVREAFFDQAAKRWRLVVPDFGVLEGPFLVAALEYAGTHEGEATFALSLASAGAVGFSAA
>NZ_CP012897|1280512:1286075|1281725_1281962_+|WP_054764893.1|DBSCAN-SWA
MSDDSQVRRVPTALVIAVVVQTIGGLVWAGGAAARIATLEQRVGEQRLVAERLARLETQGEATAAAVERIERRLEGGG
>NZ_CP012897|1280512:1286075|1285139_1285550_+|WP_054764898.1|DBSCAN-SWA
MKDHESALQKAVVAALKADAAVSALIGGRVFDRPPEGAACPYLALGRCESRPLAADGGGVEQRLTLTGVSRFLGAEEAKAMAAAVRACLHEAVLEADGVRTATLRATFADVFGASDGRRTYAVVRLRAVTEEVASG
>NZ_CP012897|1280512:1286075|1284855_1285143_+|WP_082382772.1|head,tail|DBSCAN-SWA
MASLFRPVEAETPYGGRSVSFEPVGSAWLTCGTRRRVERGEGDQRRTVERLSAEARADARLAVGRVLRFGGADWDIVGLDPLRPGRLRLELERVR

Homologous phage analysis in the prophage region

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_082382618.1|1280512_1281676_+|portal	phage portal protein	W8ECU7	Geobacillus_phage	2.2e-65	40.1
WP_054764893.1|1281725_1281962_+	hypothetical protein	NA	NA	NA	NA
WP_082382771.1|1282067_1282469_+|head,protease	HK97 family phage prohead protease	A0A0U2BX10	Paracoccus_phage	9.3e-24	49.2
WP_054764894.1|1282680_1283058_-	hypothetical protein	NA	NA	NA	NA
WP_054764895.1|1283183_1284422_+|capsid	phage major capsid protein	Q3HQT0	Burkholderia_phage	1.3e-84	44.9
WP_054764896.1|1284586_1284850_+|head,tail	phage gp6-like head-tail connector protein	NA	NA	NA	NA
WP_082382772.1|1284855_1285143_+|head,tail	phage head-tail adapter protein	NA	NA	NA	NA
WP_054764898.1|1285139_1285550_+	DUF3168 domain-containing protein	I3UM06	Rhodobacter_phage	4.8e-07	36.3
WP_054764899.1|1285664_1286075_+|tail	phage major tail protein, TP901-1 family	I3UM07	Rhodobacter_phage	2.4e-14	36.6

Sequences of DBSCAN-SWA_2

Nucleotide sequences of DBSCAN-SWA_2

>NZ_CP012897|1613330:1620529|DBSCAN-SWA
CTTAGCCATCAGCGCCACCGCTCGTCGCCTGGATCAGCAGCCACGTCCGGTCGCCGTCCATGTCGCCGATGAAGCCGATGTTGAAGGTGCGGCTTGTGTCGCGCGCATCGACCATCCGGTCCCCTGTCTGGAGCGAGCGCGTCCCGCTGTCCGAGCGAACCCAGCAGTCCCACTGCACCCGGCCCGACAAGCGGTCGGACTGAACCGTTTCGCTGCCTCGGGTTGGGAGCAGGCTGGCGGCCCGGCTGATGCCGAGAGGCGCCCAATCTTCGACCGGATTTCCGTAGATGTCCCCGCCCTCCTTCCTTCGGGAGAAGGAAACACGATGCTTTAAGTCGCCTGCACCCTTAGGCTTCGGCATCGTCCGACTTCCGGGCCGGGGCCTTCACCTCGACCGCCTTGCCAGCCGCGACCGCAGCCTCGCCGGCCTCGCGCTTCACGGTCAGCTCATGACCCTTGCGGTACTCGATCAGGACGCGGTGATTATCGGCGGGGGTGTAGGGGAAGTCGTCGGTGAAGCGGACGCGCATGGCGATCTCCTCAAATCCTGATGGTGCGGAAAGGGCGCAGCAGGTTCTCGGCGGTGGGGTTCACGTCATAGGACTGTCCGGCCGTTACAGACTCGCGGCTGGCGTAGAGGTCGCCCAGGTTCAACAACGCAGCCGCCTTAAATGACGGTTCGGCGCCGACCGGCACCAACTTCAAATCGCAGTATGTCAGACAGGCTTGAACCGCTGCGTCCGTGTAAAGCTGGATCAGCTCGTCCTCATCGTCGATGTCGACGCGAAGGTGTTGCTTGGCCTCGTCAAGGCTGAGGAGCGGTCCAGTGGTCAGAACGACGACGTTGAGCGCCACGGTCAGCCCGCCTTGTTCTTGAGCTTGGGCTCGGCTTTGTTTTTCGGCGCGGCGTCCGCCTTAGCCCGGATCGGCTTCAAGACCCCATTGGCGACGAGATGCGAGACCTCTGCGGCGTTGCCTTCGTAGGTCTCGCCCGCGTGGTAGAGGCGGTCGAAAAGCACCTGACGGGTGACTTCGTACTTCTGGATCATGATGGCCTCCTTGTGAGGGGGTCGATCTTCTCGGCCGCCACAAAAAGAGGCCCGGCAGGCGCGAACCCGCCGGGCTGTTTCAGTTCAGGAGGATCAGGTGACCCGGCCGAAGTCGCCGTAGATGAAGGCTTCAGGACGGTAGACCGCCAGAGCCAGACGCTCTTCAGCCAGGATGGTCACGAGGTTCTTGGTGAAGTCGTCATTGACGTAGCCGGTTTCGACCCGCGCATCCCAGCGGTCGAAGACCTGGGCGCCCATGCGGAAGGCGCCGGTCAGGAACTTATCGACCGCAATGGCCTGCGTCGCGACCACGGGCAGACCCCACAGTGTGGGCGAAATCGTGCCCTGCGGATTGCCGATGATGTAGCGACCTTCGCCGTCCTTCAGCGTCTCGATCCAGGCCCAATCGATCGGGTTCATGACGTGACCCGTCGCCGGGTACTCCGCCAGAGCCGCTTGCAGCATGGCGAGGCGCATCAGGTCGATGCTGGTCGGCGAGGACAGGGTGATCGGCGCCGAATAGGCGGTGGCCTGCGGGATGATGCCGTGCAGGTTCTGACCCGACCCGCTGCCGTTCAGCAGTTGCTGCTCCTCGACATAGGCCAGGCCGTAAAGGAGGCGCTGGTCGATGGTCGAACGGAGTTGCGACACGTCGCTCAGGATCTGCTTCGAAGCCTTCATCCAGTGAGCGATGACCTTGGCGGAGGTCGTCACCAGATCAAACTTCAGGTCCGATTCCGGCTTTGCGGCGCCTTCGGCAACCGGGGCGGCGCTGTTCGTGAAGCCGGTCTCCTTGACGTACTCCAGAGTGGAGCCATCCATGCGGCCCTGCGAAAGCAGGTCACGCACCGTCAGCCGGCGCTGGGGAAGGGGCAGGATGCCGGGGAGGCGGGTGGTCTGAACCGCGTCGCCGACGGAGCCGGCCGCATCGGTCGTAGCGGAGGTCAGGGTGGCCTTGATCTGCAAATCGCCGCCGCGCGCCGACTTGGAGAAGCCCGTCGCTTCGAAGTTCTTGAAGCCTTCCGACTCCACGAACTGTTCGCCGATGGACTTCTGACGGTCATCGGCGTTTCCGCCGCCGCGCGCCATCTTCTGCTCCAGATCGTCCAGACGGGCCTTGGCCTCATTCATGGCGGTCAGGGCGCCGTCGATGGTTTCCTTCTGCGACGCCGACGCATCGACGCCCTTCTGGGCTTCGGCGACGGCCTTTTCGGCGAGGCCCTTCACCTCGTCGAACTTCTTCTCGAAGTCGCCCTTGATCTCGGCAGCGAGGTCCGCCGCCGACTTCTGGCCGCGATCATCGTCGGGGCCGTAGGCGACTTGAAGGCCGCGTAGCATCAGGGGCGCGCCGACAACCTGAAAAGCCATGGCGCGGGTTGCGGCAAGCGCGAGCGCGCCCACCGCCAGGGAATGACGGTTCGTCATAGTGGTTCTCCGATAAGGGGTGTTGATGAGCCTGCCGCGCGAGACGGTCAGGCGAGGGTGGTCAGCCGCGCAGGCGCTCCAGGAACTCCAGCACGTCATCCGCCTTCGCCTCGGGCTCCCCCCGAAGGTGTGGCGTCGCCTTGGCGGCGATGGCCGTCGCCAGGGCTTTCGAGAACCCGCCTTCATCCCGAAGGAAGGCCTCAAACTCACGGACGGTCGGCAGATTGCCGCCGGCCAGGATGCTCTTCACGTCGGTCACGCGGGCGGCGCGACCCAACGCGCCGAAGGTCACGAGCGAAACCTCGCGAAGGTCCAACTTGATCAGGCGCAGCACTCCAGCGCGATCGTCGTCGGGCGCGGTCTGAACCGTGCGATAGCCGATCGACAACTCGTCCAACGCGCCGCCCTTTAGCAGCCCGTACGCCTCAGCGGCCTGCGTCGAGGCGTCCTTCAGGATGCGGCCTTTGACGTACAGGCCCTTGGCGTCTTCAGCGATGTCTTCCCAGACACCGATCGGGTGGGCGGGGTCATGCTGCCACAGCATCTTGACCGACCGCCCCTTGCGCCTGCCATCGACCAAGGACGCCGTGAACGCGCCGGGCTCCACCACCTCGTTATAGCTGTCCACAACGCCGAATGCAGAGGCGTAGCCCTCGATCACGCCGTCATCGCCTACCGCTTTCACGTCGAGTGGCAGGCCGGCGTCTTTGAACTGCAAGGTCATCATTCGCCTCCTGCGACGAGCGCTGGCGGGTTCGCCATGTTGATCGGAATGTTCTGCGACTGCATCCGGGGAACATCGCCGCCCGGAACCGGCGGCAGGTTTTCGAGGGCGCGAACCTCATTGATCGTCATCGCGCCGATCTGGGTCATCTTCTGGTAGAACTCTGACCGGCCCTTGCTGTCGGCGCGAAGCAGGCCCTCAAGGTTGAACTCGACCACGATCCCAGCCGCGCGATCCGCTGGGCTCAGAAGCTGCTTCATGATCGCTTGTTCGATCCGCTTCAGGCGGCGGCGCAGGGTGAACTTCTGGAAACGCAGGGTCTGCTCTTCCAGGCCAGTACCCCAGCTGGTGGACTTCTCCGTGTGCCCGATCATGTGCGGGGGAACTTCGAAGAAGCGGCAAATCTCTTCGACGCTGAACGACCGGCTTTCCAGCATCTGGGCGTCTTCAGGCGTGAACGAGATCTGATGGGGAACGATGCCGCCCTCAAGCAACATCGGGCGCCCCGCGTTCATGGCGCCCGCGTGTTTCTCCTGAAGAGCCTTCTCCAGCGGAACCCGGATGCTTTCGCCCAATGTCTTTTCGGCGGGCGTGGTCAAGATCAGAGACGGGCGAACCCCATTAGCGAACGTCGTCTGTGCGGCGGCGTTGACTGCAAGCGACAGGCCGAAGACCTGACGGCCATAGCTCAGCGTCGAAAGGCCGCCCAAGGGGGAGCCGCCAAAGCCCCGGACGTGGAAGACGTTTTCCTGCGGCTCATCATAGGCCGTGCCGTTGTCGGTCCAGCGGTAGCGCAGCGACCCGTCAGCCTGCCGCGTAATCGACGGGCTGTAGATCGGATGAAGGGCGACGACACGGCCGCCGATCCTCTCGATCCGGGCGTGCATGTTGCCGCGAAGCTCAAGCGCAGCCTGTCCACCCTCCCAGAAATCGAGCGCGGTTTGGTCGTAGTTGGGGCTGTCGTGCAGAACCCGGTAGAGCGGATGGTCTCTCGCAGCGACCCGATTGCCCGCCGCATCCGTCCGATAAACCATCAAGGGCAGGGAGGCGATCGTACCGGCAAGGAGGTTGACACAGGCCCAAGCCGCCGAGAGGCCAAGAATGCCGACCTCCGTCACCGGCACCCCGGCGTTCACGGGGTCAAGCCATCCATCCGTGTTTGTCAGGGACAGTTGGCGAGACGGCGGGTCCCAGGACTTCAATCCAAGGGCTGAAAGAGCCTTGGCGATCAAGCCGCGACCCCCAGGCTCGCGAGATATTCCTTCCATCCCGCCCCCTTCGCCATAGGCTTCCGCGACATCAGCATCATTGCGTTGAAGGCCGCGACCAATGGGTCGATCTTGGCCCGGCCGGCCGATTGTTTCGTGATGATCACGGCGCCGCCGCGAACCTCGACCTTCGCGTTCCCGACGCACCAGGCCATCATCCGTTGACCGCCGTGCTTCAGAGACCCGTTCTTGAGCTTGATCTCAGAACCCCAGGATGCCGGGGAGAGGGCGAAGCCTTGGCGTATGGCGACTTGCTGGCCTGGAGCTATCCCACGCGCCTCAAGTTCGTCCACAAGGGCCGCAACACCAATAGGGTCGATCCCGACGCCTTCCGCTTCAGGAAGCAGACCGGCCTCTTTGACCCGCTCGATATAGGCGGCGGCCTCCATGATCGGGGCCATCGGATCTTCGGAGATCGTCAAGTCGCCGTCAGTCTCGAAATCCTTCAGTCGGCTGGCGATGTCCTGGCGCCGCTTCAGCACGTCGTCATGAGCCCAGGCGTGGGTCCAGAGAAGCCACTTCTGGGTTTCACTGCACCGACCCAAGACGGCGAGACCAAACAAGTCATCCAAGCCGCCGCCGTCGATCCCGACCGTGCAGACTTCCGAACGCCTCAGAACCTCGTCCAGCGTCAGGCTCTTGTCGGCCGCGCCTTCCCAATAGTCGGCCCCGGCCCAGCGGTTATTCGCCAGCTTCAGCCCGATTTCGACGTTCAGATGTTTGGCGAGGAAGACCTGACGGGTTCCGTCGTTGGCGTCGCGGACCTTCTCAAGTTCCCGCTCCAGATAGGCCACATCGACGGAACGACCGATGTTCGGGTTCGTGATGTAGAAGTTCTTCGGATCGAGGTACGCCTCGGTCTCCGCCATGTCCTCGGGAAACTCGTAGATGACCGGCAGACTCTCCCGGTCCTTGATCTTCCCGTCGCGCACACCCCGGAAATAGTCCAGCTTAGCCTTGAACACCCCGGCCGGCTCTTCGTCCGACTGAGTGCTGGCCCAGATGACGAAACCCTCGGGCCGAGACACCAGACCGCCCGTCGCCTCGCGCAACATGGCGTCCGCCTTGGCGCGCTTTCCGAAGACCCAAAGCTCATCGACAAATATGTAACCGGCCTTCTTGCCGGACACCGTGTCGGAATCCGCCGCGACCACCTTCAGCGCCGCGCCCGTCCCCCGGTGGGTGATCGTTCGGACGTGGCTTTGGACCTGAAGCAGTTCTCCAAGCTCATCATCCGCCTTGATCATGTCCCAGGCGGGCTGAAAGGCGTTGTTCGCGACTTCGATCGTCGGCGCCAGGATCAGCAGCTCAGCCGAATGCCGCCAGTTGCGGATCAGCGCCGTAACCATGATCCCGGCGGCGATGGTGGACTTAGAATTCTTTTTTGAGATCAAAAGGAAGAATTCTCTGATCAGTTGCCGACCGGCGTCCCGATCAAAGGCCCCAAAGATCGCCCGGACGAAATCGAAGACCCAATCCTCGCAAGCCTCGCCGAATGTCGGCTGGCCGGGCGCATCAACGATCTTGAGCGCCTTGAAGACTTCAAGCGCCTCCTCGGCCTCATCGGCGAAGAGCGGGGAGGGTATCAGGCTTCGCCGGGCGACAATCCGGTCTCGCCAGTCCAGGCAGGCGGTGGACCATTCCATCAGTGCCGATTATCCACGATCAACTTCGGAGCCGATGGAGTGGCGAAACGGCTACTGGTCTTCGCGATATGCTCCCCGGCGGCCTGACGCTGCTTCTTGACCCCAGGCGCCGCTCCAGATTCACCGAGCGTCTTCGCCGCCGTCGCCAGGGCCTTCAGAACCTCTGACCGGTTCTTGAGCGAGACCGCCGCAAGCGCCGCCTGCCTCGCCTTGTCGTCGTCGCCTGTGTCGTAGGCAGACTCGATCAGTCCCTCCAGTTCGCCGATCCGAGAGGTCGAGGCGTCCAGTTCGTCCAGCATCCGCATCACGAGATTTCGACCCCGGCCGATAATCGCTTCAGGCGTTGTGTTCTCAGGCGTCAGGACGGTGCCGACGTAGACCTTCGGCGGCTCCGGTTCGCGGGCTTGTTCGCGCGCACTCTCGGGCTTCTCAGGCCGCTCCCAGCCATCACGCCCGGCCCGCTTCCGAATAGCGGCCTCGCTGATCCCGTACCAACGGGCCATTTCCCGCACAGACATTGGACTTGAGCGGTAATCGCGCTCGATCTCAGACCAATCAATCGGCTTCTTTTCGTCGGTCATGGAGCCCTCGTTCGCGGCCGGTGCGCGCGCCCCAAAAGCGCCCAGGGGGATTTTTTCTGTCCGTGAGGGGGCCGCCGGTCTCTAAGCCACGGACTTTTCAGACTTTTTATAGCCCCCCCGGTCGGCTCAGCTCCAGTCGCCCCGCTGGTGCAGGCTGGCCTGCTCTTCGGCCTGAATGGTTGAGTCGTGAACGGCCTTGCTGACCGTCTCCAGGTTGTTGATGTCCCAGAACAGCCGCTCATCTCCACGATGGGGGCGCTTGTGGTTGACCACGGGGCTGTCAGGGGCCGGGTGCTTTCCGGCCAGGACTTGGCCTGTCCTCTGACAGGTGTAGGCGTCCCTGATCAGGACTTGCTCCCGGAGCCGACGCCAGCGGGCGGTCTTGTACCACGCCTTCCAGGGGGAGGAGTGCTGGATCGGGGCCGGGCCTTTGGCTGCGTCAGTGGGGAAGGTTCGACGATCGGGGGCGAAGCTCACCCGAGATGATAGGTGAGATAGCCGGGCCAT

Protein sequences of DBSCAN-SWA_2

>NZ_CP012897|1613330:1620529|1619440_1620022_-|WP_054765154.1|DBSCAN-SWA
MTDEKKPIDWSEIERDYRSSPMSVREMARWYGISEAAIRKRAGRDGWERPEKPESAREQAREPEPPKVYVGTVLTPENTTPEAIIGRGRNLVMRMLDELDASTSRIGELEGLIESAYDTGDDDKARQAALAAVSLKNRSEVLKALATAAKTLGESGAAPGVKKQRQAAGEHIAKTSSRFATPSAPKLIVDNRH
>NZ_CP012897|1613330:1620529|1614186_1614378_-|WP_054765151.1|DBSCAN-SWA
MIQKYEVTRQVLFDRLYHAGETYEGNAAEVSHLVANGVLKPIRAKADAAPKNKAEPKLKNKAG
>NZ_CP012897|1613330:1620529|1617755_1619441_-|WP_054765153.1|terminase|DBSCAN-SWA
MEWSTACLDWRDRIVARRSLIPSPLFADEAEEALEVFKALKIVDAPGQPTFGEACEDWVFDFVRAIFGAFDRDAGRQLIREFFLLISKKNSKSTIAAGIMVTALIRNWRHSAELLILAPTIEVANNAFQPAWDMIKADDELGELLQVQSHVRTITHRGTGAALKVVAADSDTVSGKKAGYIFVDELWVFGKRAKADAMLREATGGLVSRPEGFVIWASTQSDEEPAGVFKAKLDYFRGVRDGKIKDRESLPVIYEFPEDMAETEAYLDPKNFYITNPNIGRSVDVAYLERELEKVRDANDGTRQVFLAKHLNVEIGLKLANNRWAGADYWEGAADKSLTLDEVLRRSEVCTVGIDGGGLDDLFGLAVLGRCSETQKWLLWTHAWAHDDVLKRRQDIASRLKDFETDGDLTISEDPMAPIMEAAAYIERVKEAGLLPEAEGVGIDPIGVAALVDELEARGIAPGQQVAIRQGFALSPASWGSEIKLKNGSLKHGGQRMMAWCVGNAKVEVRGGAVIITKQSAGRAKIDPLVAAFNAMMLMSRKPMAKGAGWKEYLASLGVAA
>NZ_CP012897|1613330:1620529|1613869_1614184_-|WP_054765150.1|head,tail|DBSCAN-SWA
MALNVVVLTTGPLLSLDEAKQHLRVDIDDEDELIQLYTDAAVQACLTYCDLKLVPVGAEPSFKAAALLNLGDLYASRESVTAGQSYDVNPTAENLLRPFRTIRI
>NZ_CP012897|1613330:1620529|1615864_1616527_-|WP_054765152.1|head,protease|DBSCAN-SWA
MTLQFKDAGLPLDVKAVGDDGVIEGYASAFGVVDSYNEVVEPGAFTASLVDGRRKGRSVKMLWQHDPAHPIGVWEDIAEDAKGLYVKGRILKDASTQAAEAYGLLKGGALDELSIGYRTVQTAPDDDRAGVLRLIKLDLREVSLVTFGALGRAARVTDVKSILAGGNLPTVREFEAFLRDEGGFSKALATAIAAKATPHLRGEPEAKADDVLEFLERLRG
>NZ_CP012897|1613330:1620529|1616526_1617795_-|WP_082382633.1|portal|DBSCAN-SWA
MEGISREPGGRGLIAKALSALGLKSWDPPSRQLSLTNTDGWLDPVNAGVPVTEVGILGLSAAWACVNLLAGTIASLPLMVYRTDAAGNRVAARDHPLYRVLHDSPNYDQTALDFWEGGQAALELRGNMHARIERIGGRVVALHPIYSPSITRQADGSLRYRWTDNGTAYDEPQENVFHVRGFGGSPLGGLSTLSYGRQVFGLSLAVNAAAQTTFANGVRPSLILTTPAEKTLGESIRVPLEKALQEKHAGAMNAGRPMLLEGGIVPHQISFTPEDAQMLESRSFSVEEICRFFEVPPHMIGHTEKSTSWGTGLEEQTLRFQKFTLRRRLKRIEQAIMKQLLSPADRAAGIVVEFNLEGLLRADSKGRSEFYQKMTQIGAMTINEVRALENLPPVPGGDVPRMQSQNIPINMANPPALVAGGE
>NZ_CP012897|1613330:1620529|1613330_1613690_-|WP_054765148.1|head,tail|DBSCAN-SWA
MPKPKGAGDLKHRVSFSRRKEGGDIYGNPVEDWAPLGISRAASLLPTRGSETVQSDRLSGRVQWDCWVRSDSGTRSLQTGDRMVDARDTSRTFNIGFIGDMDGDRTWLLIQATSGGADG
>NZ_CP012897|1613330:1620529|1620148_1620529_-|WP_082382634.1|DBSCAN-SWA
MARLSHLSSRVSFAPDRRTFPTDAAKGPAPIQHSSPWKAWYKTARWRRLREQVLIRDAYTCQRTGQVLAGKHPAPDSPVVNHKRPHRGDERLFWDINNLETVSKAVHDSTIQAEEQASLHQRGDWS
>NZ_CP012897|1613330:1620529|1614471_1615803_-|WP_082382632.1|capsid|DBSCAN-SWA
MTNRHSLAVGALALAATRAMAFQVVGAPLMLRGLQVAYGPDDDRGQKSAADLAAEIKGDFEKKFDEVKGLAEKAVAEAQKGVDASASQKETIDGALTAMNEAKARLDDLEQKMARGGGNADDRQKSIGEQFVESEGFKNFEATGFSKSARGGDLQIKATLTSATTDAAGSVGDAVQTTRLPGILPLPQRRLTVRDLLSQGRMDGSTLEYVKETGFTNSAAPVAEGAAKPESDLKFDLVTTSAKVIAHWMKASKQILSDVSQLRSTIDQRLLYGLAYVEEQQLLNGSGSGQNLHGIIPQATAYSAPITLSSPTSIDLMRLAMLQAALAEYPATGHVMNPIDWAWIETLKDGEGRYIIGNPQGTISPTLWGLPVVATQAIAVDKFLTGAFRMGAQVFDRWDARVETGYVNDDFTKNLVTILAEERLALAVYRPEAFIYGDFGRVT
>NZ_CP012897|1613330:1620529|1613676_1613859_-|WP_054765149.1|DBSCAN-SWA
MRVRFTDDFPYTPADNHRVLIEYRKGHELTVKREAGEAAVAAGKAVEVKAPARKSDDAEA

Homologous phage analysis in the prophage region

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_054765148.1|1613330_1613690_-|head,tail	head-tail adaptor protein	NA	NA	NA	NA
WP_054765149.1|1613676_1613859_-	hypothetical protein	NA	NA	NA	NA
WP_054765150.1|1613869_1614184_-|head,tail	phage gp6-like head-tail connector protein	A0A2D1GNK0	Pseudomonas_phage	4.7e-07	40.0
WP_054765151.1|1614186_1614378_-	hypothetical protein	NA	NA	NA	NA
WP_082382632.1|1614471_1615803_-|capsid	phage major capsid protein	A0A0U2C0U7	Paracoccus_phage	3.8e-130	63.3
WP_054765152.1|1615864_1616527_-|head,protease	HK97 family phage prohead protease	A0A0U2BX10	Paracoccus_phage	7.6e-39	46.2
WP_082382633.1|1616526_1617795_-|portal	phage portal protein	A0A0U2BXP2	Paracoccus_phage	2.1e-106	52.6
WP_054765153.1|1617755_1619441_-|terminase	terminase large subunit	Q3HQS7	Burkholderia_phage	2.3e-180	57.0
WP_054765154.1|1619440_1620022_-	hypothetical protein	NA	NA	NA	NA
WP_082382634.1|1620148_1620529_-	hypothetical protein	A0A286N2R3	Klebsiella_phage	5.8e-07	39.5