CRISPRimmunity

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Overview of predicted results

Overview of the results

Contig_ID	Contig_def	CRISPR array number	Contig Signature genes	Self targeting spacer number	Target MGE spacer number	Prophage number	Anti-CRISPR protein number
NZ_CP022986	Chryseobacterium camelliae strain Dolsongi-HT1 chromosome, complete genome	5 crisprs	DEDDh,PD-DExK,WYL,csa3,cas3,c2c10_CAS-V-U3	0	1	3	0

Results visualization

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CRISPR-Cas detection and classification

Crispr_ID: NZ_CP022986_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP022986_1

404028-404122

Orphan

Consensus_repeat	Method
CCCTTGTCTATCATCTCTCCGTCT	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP022986_1

>merge|NZ_CP022986|1|404028-404122|CRISPRCasFinder
CCCTTGTCTATCATCTCTCCGTCTATTATCTTTCATCTAAAATTCAAAATCTATAATCTATAATTCATAGTTCCCTGTCTATCATCTCTCCGTCT

>NZ_CP022986|1|1|404028-404122|CRISPRCasFinder
CCCTTGTCTATCATCTCTCCGTCT	ATTATCTTTCATCTAAAATTCAAAATCTATAATCTATAATTCATAGT
TCCCTGTCTATCATCTCTCCGTCT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP022986.1\|WP_100074236.1\|402997_403465_-\|nucleoside-triphosphate-pyrophosphohydrolase-family-protein	unknown	unknown	gnl\|CDD\|212137
NZ_CP022986.1\|WP_100074228.1\|394501_395479_+\|membrane-dipeptidase	unknown	unknown	gnl\|CDD\|238626
NZ_CP022986.1\|WP_100077452.1\|415636_416578_+\|type-VI-secretion-system-baseplate-subunit-TssG	unknown	unknown	gnl\|CDD\|377755
NZ_CP022986.1\|WP_100074234.1\|401813_402425_-\|DUF4230-domain-containing-protein	unknown	unknown	gnl\|CDD\|379417
NZ_CP022986.1\|WP_100074244.1\|414501_415293_-\|S1/P1-nuclease	unknown	unknown	gnl\|CDD\|211382
NZ_CP022986.1\|WP_100074238.1\|407369_408509_-\|acyl-CoA-dehydrogenase-family-protein	unknown	unknown	gnl\|CDD\|173847
NZ_CP022986.1\|WP_100074239.1\|408699_410583_+\|endonuclease	unknown	unknown	gnl\|CDD\|367881
NZ_CP022986.1\|WP_100074237.1\|404214_407142_-\|T9SS-type-A-sorting-domain-containing-protein	unknown	unknown	gnl\|CDD\|316139
NZ_CP022986.1\|WP_100074242.1\|412283_412685_+\|helix-turn-helix-transcriptional-regulator	unknown	unknown	gnl\|CDD\|378971
NZ_CP022986.1\|WP_100077451.1\|398347_399736_+\|3-isopropylmalate-dehydratase-large-subunit	unknown	unknown	gnl\|CDD\|235490
NZ_CP022986.1\|WP_100074235.1\|402427_402991_-\|thioredoxin-family-protein	unknown	unknown	gnl\|CDD\|239245
NZ_CP022986.1\|WP_100074240.1\|410743_411532_+\|SDR-family-oxidoreductase	unknown	unknown	gnl\|CDD\|187602
NZ_CP022986.1\|WP_100074232.1\|400328_401453_+\|3-isopropylmalate-dehydrogenase	unknown	unknown	gnl\|CDD\|234832
NZ_CP022986.1\|WP_100074229.1\|395475_397026_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022986.1\|WP_100074241.1\|411811_412246_+\|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|378971
NZ_CP022986.1\|WP_100074243.1\|412745_413333_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022986.1\|WP_100074231.1\|399739_400339_+\|3-isopropylmalate-dehydratase-small-subunit	unknown	unknown	gnl\|CDD\|179314
NZ_CP022986.1\|WP_002979276.1\|413421_414288_-\|RNA-polymerase-sigma-factor-RpoD/SigA	unknown	unknown	gnl\|CDD\|223642
NZ_CP022986.1\|WP_100074230.1\|397173_398337_+\|2-isopropylmalate-synthase	unknown	unknown	gnl\|CDD\|234864
NZ_CP022986.1\|WP_100074233.1\|401555_401744_-\|hypothetical-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_CP022986.1\|WP_100074236.1\|402997_403465_-\|nucleoside-triphosphate-pyrophosphohydrolase-family-protein	gnl\|CDD\|212137	cd11530, NTP-PPase_DR2231_like, Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in Deinococcus radiodurans DR2231 protein and its bacterial homologs. This family includes a MazG-like NTP-PPase from Deinococcus radiodurans (DR2231), a putative NTP-PPase YP_001813558.1 from Exiguobacterium sibiricum and their bacterial homologs. DR2231 shows significant structural resemblance to MazG proteins, but is functionally related to the dimeric dUTPases. It can hydrolyze dUTP into dUMP. DR2231-like proteins contain a well conserved divalent ion binding motif, EXXEX(12-28)EXXD, which is the identity signature for the all-alpha-helical NTP-PPase superfamily. Unlike normal dimeric dUTPase-like proteins with a central four-helix bundle forming the active site, YP_001813558.1 displays a very unusual interlaced segment-swapped dimer. It potentially prefers to hydrolyze dCTPs or its derivatives. YP_001813558.1-like proteins contain a variant divalent ion binding motif, EXXEX(12-28)AXXD.	2.02987e-30
NZ_CP022986.1\|WP_100074228.1\|394501_395479_+\|membrane-dipeptidase	gnl\|CDD\|238626	cd01301, rDP_like, renal dipeptidase (rDP), best studied in mammals and also called membrane or microsomal dipeptidase, is a membrane-bound glycoprotein hydrolyzing dipeptides and is involved in hydrolytic metabolism of penem and carbapenem beta-lactam antibiotics. Although the biological function of the enzyme is still unknown, it has been suggested to play a role in the renal glutathione metabolism.	1.40691e-43
NZ_CP022986.1\|WP_100077452.1\|415636_416578_+\|type-VI-secretion-system-baseplate-subunit-TssG	gnl\|CDD\|377755	pfam06996, T6SS_TssG, Type VI secretion, TssG. This is a family of Gram-negative bacterial proteins that form part of the type VI pathogenicity secretion system (T6SS), including TssG. TssG is homologs to phage tail proteins and is required for proper assembly of the Hcp tube in bacteria.One other member in this family, SciB (Q93IT4) from Salmonella enterica, is thought to be involved in virulence.	0.00069203
NZ_CP022986.1\|WP_100074234.1\|401813_402425_-\|DUF4230-domain-containing-protein	gnl\|CDD\|379417	pfam14014, DUF4230, Protein of unknown function (DUF4230). This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 203 and 228 amino acids in length.	2.917e-10
NZ_CP022986.1\|WP_100074244.1\|414501_415293_-\|S1/P1-nuclease	gnl\|CDD\|211382	cd11010, S1-P1_nuclease, S1/P1 nucleases and related enzymes. This family summarizes both S1 and P1 nucleases (EC:3.1.30.1) which cleave RNA and single stranded DNA with no base specificity. S1 nuclease is more active on DNA than RNA. Its reaction products are oligonucleotides or single nucleotides with 5' phosphoryl groups. Although its primary substrate is single-stranded, it may also introduce single-stranded breaks in double-stranded DNA or RNA, or DNA-RNA hybrids. It is used as a reagent in nuclease protection assays and in removing single stranded tails from DNA molecules to create blunt ended molecules and opening hairpin loops generated during synthesis of double stranded cDNA. P1 nuclease cleaves its substrate at every position yielding nucleoside 5' monophosphates, and it does not recognize or act on double-stranded DNA. It is useful at removing single stranded strands hanging off the end of double stranded DNA and at completely cleaving melted DNA for simple DNA composition analysis.	2.49743e-80
NZ_CP022986.1\|WP_100074238.1\|407369_408509_-\|acyl-CoA-dehydrogenase-family-protein	gnl\|CDD\|173847	cd01158, SCAD_SBCAD, Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA dehydrogenases. Short chain acyl-CoA dehydrogenase (SCAD). SCAD is a mitochondrial beta-oxidation enzyme. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of SCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. This subgroup also contains the eukaryotic short/branched chain acyl-CoA dehydrogenase(SBCAD), the bacterial butyryl-CoA dehydorgenase(BCAD) and 2-methylbutyryl-CoA dehydrogenase, which is involved in isoleucine catabolism. These enzymes are homotetramers.	2.08006e-180
NZ_CP022986.1\|WP_100074239.1\|408699_410583_+\|endonuclease	gnl\|CDD\|367881	pfam04231, Endonuclease_1, Endonuclease I. Bacterial periplasmic or secreted endonuclease I (EC:3.1.21.1) E. coli endonuclease I (EndoI) is a sequence independent endonuclease located in the periplasm. It is inhibited by different RNA species. It is thought to normally generate double strand breaks in DNA, except in the presence of high salt concentrations and RNA, when it generates single strand breaks in DNA. Its biological role is unknown. Other family members are known to be extracellular. This family also includes a non-specific, Mg2+ activated ribonuclease precursor.	3.27407e-72
NZ_CP022986.1\|WP_100074237.1\|404214_407142_-\|T9SS-type-A-sorting-domain-containing-protein	gnl\|CDD\|316139	pfam13583, Reprolysin_4, Metallo-peptidase family M12B Reprolysin-like. This zinc-binding metallo-peptidase has the characteristic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B.	1.24195e-32
NZ_CP022986.1\|WP_100074242.1\|412283_412685_+\|helix-turn-helix-transcriptional-regulator	gnl\|CDD\|378971	pfam12844, HTH_19, Helix-turn-helix domain. Members of this family contains a DNA-binding helix-turn-helix domain. This family contains many example antitoxins from bacterial toxin-antitoxin systems. These antitoxins are likely to be DNA-binding domains.	3.08414e-05
NZ_CP022986.1\|WP_100077451.1\|398347_399736_+\|3-isopropylmalate-dehydratase-large-subunit	gnl\|CDD\|235490	PRK05478, PRK05478, 3-isopropylmalate dehydratase large subunit.	0
NZ_CP022986.1\|WP_100074230.1\|397173_398337_+\|2-isopropylmalate-synthase	gnl\|CDD\|234864	PRK00915, PRK00915, 2-isopropylmalate synthase; Validated.	0
NZ_CP022986.1\|WP_100074232.1\|400328_401453_+\|3-isopropylmalate-dehydrogenase	gnl\|CDD\|234832	PRK00772, PRK00772, 3-isopropylmalate dehydrogenase; Provisional.	0
NZ_CP022986.1\|WP_100074241.1\|411811_412246_+\|helix-turn-helix-domain-containing-protein	gnl\|CDD\|378971	pfam12844, HTH_19, Helix-turn-helix domain. Members of this family contains a DNA-binding helix-turn-helix domain. This family contains many example antitoxins from bacterial toxin-antitoxin systems. These antitoxins are likely to be DNA-binding domains.	6.78403e-06
NZ_CP022986.1\|WP_100074231.1\|399739_400339_+\|3-isopropylmalate-dehydratase-small-subunit	gnl\|CDD\|179314	PRK01641, leuD, 3-isopropylmalate dehydratase small subunit.	8.00984e-101
NZ_CP022986.1\|WP_002979276.1\|413421_414288_-\|RNA-polymerase-sigma-factor-RpoD/SigA	gnl\|CDD\|223642	COG0568, RpoD, DNA-directed RNA polymerase, sigma subunit (sigma70/sigma32) [Transcription].	6.70382e-90
NZ_CP022986.1\|WP_100074235.1\|402427_402991_-\|thioredoxin-family-protein	gnl\|CDD\|239245	cd02947, TRX_family, TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a TRX domain; and Group II, which are composed of fusion proteins of TRX and additional domains. Group I TRX is a small ancient protein that alter the redox state of target proteins via the reversible oxidation of an active site dithiol, present in a CXXC motif, partially exposed at the protein's surface. TRX reduces protein disulfide bonds, resulting in a disulfide bond at its active site. Oxidized TRX is converted to the active form by TRX reductase, using reducing equivalents derived from either NADPH or ferredoxins. By altering their redox state, TRX regulates the functions of at least 30 target proteins, some of which are enzymes and transcription factors. It also plays an important role in the defense against oxidative stress by directly reducing hydrogen peroxide and certain radicals, and by serving as a reductant for peroxiredoxins. At least two major types of functional TRXs have been reported in most organisms; in eukaryotes, they are located in the cytoplasm and the mitochondria. Higher plants contain more types (at least 20 TRX genes have been detected in the genome of Arabidopsis thaliana), two of which (types f amd m) are located in the same compartment, the chloroplast. Also included in the alignment are TRX-like domains which show sequence homology to TRX but do not contain the redox active CXXC motif. Group II proteins, in addition to either a redox active TRX or a TRX-like domain, also contain additional domains, which may or may not possess homology to known proteins.	1.28434e-06
NZ_CP022986.1\|WP_100074240.1\|410743_411532_+\|SDR-family-oxidoreductase	gnl\|CDD\|187602	cd05344, BKR_like_SDR_like, putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR. This subgroup resembles the SDR family, but does not have a perfect match to the NAD-binding motif or the catalytic tetrad characteristic of the SDRs. It includes the SDRs, Q9HYA2 from Pseudomonas aeruginosa PAO1 and APE0912 from Aeropyrum pernix K1. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.	2.63185e-93

>NZ_CP022986.1|WP_100074236.1|402997_403465_-|nucleoside-triphosphate-pyrophosphohydrolase-family-protein
MDKIDSLNQVAEFHTTFKAPILETPQIPSEDRCNLRVALLQEELNELKQAIEDNNLVEIADALCDLQYVLSGAVLEFGLGSKFVTLFDEVQRSNMSKACDNEEQAQETVAFYQEKGVESFYEKSGEKYNVYRKADHKVLKNKYYSPADLKSIIED
>NZ_CP022986.1|WP_100074235.1|402427_402991_-|thioredoxin-family-protein
MKKFITHIFFAAVFTGSMQQVSAQKVVVNREVETQNDGKMLLGVQMKDQFTKAPYADWYTKEHDEYALDQKAISELRKQKINSYNLIVFMGTWCEDSHRDFPRLMKILEELKYPEGKMTIIAVNRKKESPSGEEATYNIQKVPTIIVQKYGKEIGRIIEMPTTGYIERDLVEILKKDDQSVIKEIFK
>NZ_CP022986.1|WP_100074234.1|401813_402425_-|DUF4230-domain-containing-protein
MKKYRLPLAFVAGALVMLMLFFGVRSCLNLSPVEKKEQSDYYILTNQISKMNKMVVMEQDVSSMQKTKMSYELFGKEMSSNNIVTYTKTNAQVSYDLNKMKMVVDSVNKKLVITELPDADIRITPSVEVQSLDDSFFNRISEKDIKNVTQKAKTTAIQSIDQNRLRKEGHQQLMDNLNQIFVLAKALNYTIEDQTGKIGVLPL
>NZ_CP022986.1|WP_100074233.1|401555_401744_-|hypothetical-protein
MDPKEKNKDHESANSAETKKQNEDFRGIPAASEKTNPSDVDKEDVKKSSENNESGKTDNTEE
>NZ_CP022986.1|WP_100074232.1|400328_401453_+|3-isopropylmalate-dehydrogenase
MSDNTFKIAVLPGDGIGPEVVAESIKILDAIGEAFQYSFRYRYALMGADAIYKTGSPLPDETLAICRESDAVLFGAIGDPAFDNNPDAKVRPEQGLLKLRKELGLFANIRPLKTYASLIEKSPLKKEIIEGTDIQIFRELVSGIYFGEKFTEENAAYAYDVCRYSREDILPITHMAFKEAQKRRKKLTLIDKANVLDTSRLWRKIVQEIAAEYPDVQLDYMFVDNAAMQLILNPKQFDVILTENMFGDIISDEASVIGGSIGLLPSASVGKENALFEPIHGSYPQAKGKGIANPIASILSTAMMLDYLQLDQAADKLRESVEHAIENRYVTVDLNAEQPSSTAEAGSFIADYIKYSEKSYYNFENVKIGKSTIV
>NZ_CP022986.1|WP_100074231.1|399739_400339_+|3-isopropylmalate-dehydratase-small-subunit
MKKLITIQSRAIPLPAENIDTDQIIPARFLKSIDRKGFGNNLFRDWRFNVHTGEPNPEFVLNKPEFTGEILVAGNNFGCGSSREHAAWALTDYGFKVIVSSYFADIFKGNALNNGLLPVKVSEDFLKAILEGITNDPQLEIKVDVEQQSVTCNGKTENFELDSYKKICLLNGYDDIDFLISRKKAIQEFELKTQEIYER
>NZ_CP022986.1|WP_100077451.1|398347_399736_+|3-isopropylmalate-dehydratase-large-subunit
MNNNRKTLFDKVWDAHVVETVPDGPQIIYIDKHLIHEVTSPQAFAELEARNLKVFRPEQIVATADHNVPTQHQELPIRDELSRNQVEQLTENCVKNGIELFGLGHPYQGIVHIIAPELGITQPGMSIVCGDSHTSTHGAFGAIAFGIGTSQVAQVFASQCLLLNKPKSMRITVNGTLNKDVQPKDVILYIISKVGTDGGTGFFCEYAGDVFENMSMEGRMTVCNMSIEMGARGGMIAPDAVTFDYVKGRAFAPEGEDWEEKVAYWKTLKTDEGAVFDAEFTFDASEIQPMVTYGTNPGMGISVHESIPAPRNESEAKALQYMGLQAGQSMSDIRVNYVFIGSCTNARIEDFRSVAEYIKGKSRSGHVHALIVPGSQQVVKQMYEEGLDAVFREAGFEIRQPGCSACLAMNDDKIPEGEYCVSTSNRNFEGRQGQGARTILASPLTAAKVAVEGKISILQHLN
>NZ_CP022986.1|WP_100074230.1|397173_398337_+|2-isopropylmalate-synthase
MNSEKVEIFDTTLRDGEQVPGCKLNTEQKLIIAERLDDLGIDIIEAGFPVSSPGDFHSVSEISKLVRNATVCGLTRANQKDIEVAAEALKFARKPRIHTGIGTSDSHIKYKFNSTREEIIERAIKAVKYSKTFVEDVEFYAEDAGRTDNEYLARVCEAVIKAGATVINIPDTTGYCLPEEYGAKIRYLKENVKGIEKAVISCHCHNDLGLATANSVAGAINGARQIECTINGLGERAGNTALEEVVMIFNQHKDLHLHTDVHSRMLNPMSALVSELMGMPVQPNKAIVGANAFAHSSGIHQDGVIKNRETYEIIDPEEVGVSSSSIVLTARSGRSALAYRFKHIGFEVTKNELDILYQEFLKVADRKKEVDNDDLNMMMEVFARKIG
>NZ_CP022986.1|WP_100074229.1|395475_397026_-|hypothetical-protein
MAELHKDFLFVLIKSMTTSEKRQFRLFVNRLGINTDAKFLLLFSEMDRMKEYDENSILAKKISTKQQLSNLKAHLYKQILVSLRMNPSLQNNRIQLREQLDFANILYQKGLYKQALKILDKTKQTALDLDEKSIAMEIIDLEKVIESQYITRSIEGRADELIRQSKAISKQNQYTTDLSNLSLKLYSEMLSHGYVKNDEDRLKILEIFSTQIKKINFHKLKFTEKLWYYKAHVWKNQLLQEYKYTLKYAYLWVDLFHKNPDMILNHPVWYIKGNTYLLKILFLYGNVETLDEHFSNFNERVHSQNFLQNENLQALIFLTHSNTLMNIHFIKGEFFQGTKVIPGIELKMNKFRDKIDEHHFMILYLKMAAMFFGSKKYGEAIEYAMKIIESKKNVQEDLLFHTRILILMSKHESGNDEDYDEFIKATSKFATKMKKPEAFHFESIDFFKNLNGLVLSKQQKAFEAFDQKLESFSENQYYRRSLLYIDIHGWVKSKVQHVDVIEIIKRKVRYTRRLKD
>NZ_CP022986.1|WP_100074228.1|394501_395479_+|membrane-dipeptidase
MESTFNIDLHCDLLAYLLKANTSADDGQPGCSLPYLREGHVRLQVMAIYASTAPGSIDKGIRQSDYFKEFLNSPDFFLFDEQSSHAPEHADRIGVFAAIENASVFCEEDMHLDTGFKNLETIIQNTRKIFYLGITHHTENRFGGGNFTDIGLKDDGKILIDYITGRKIAIDLAHTSDQLAYDILDYIDRKNYDVPILASHSNYRRVYENQRNLPDELVQELIRRKGLIGLNFIKDYIDHHHPERLYEHIQYALSLGAENCIAYGGDFFYDKDHPEQSRIPFFFDEFKDATAYNMINRRVSEDFSPEVMRKISHQNVLDFLSRNGF
>NZ_CP022986.1|WP_100074237.1|404214_407142_-|T9SS-type-A-sorting-domain-containing-protein
MKKQLLLIGMLVISGISSAQTDRLWSASSPKTSSDIFENKTGILQPRIFSLDINGLKNTLATAPQRLSIGEKSEVIISFPNADGRMENFKVRENPNFDPQLAAKYPEIKSYVGEGLEDPSSTVYFSISPLGLSSMEIYGDKSAVFIEPYTKDLSSYVVYKKSDKKDNLNKFECTVIDVAQKGVAGSDLAARPNADDAKLRTFRLALSCTGEYASYFGGTKANALAAMNNTMTRVNGVFEKDFSARMVLISNNDAVIYTNASTDPYSPASGMSNWNSQLQNTLTSVIGEANYDIGHLFGASGGGGNAGCIGCVCVNGSKGSGYTSPADSVPSGDNFDIDYVAHEMGHQFGGNHTFSMSNEGTGVNMEPGSGSTIMGYAGITSQDVQPHSDAFFHAVSIQQVTDNIKSKTCPVSTSTGNSIPTANAGADYTVPKGTPFMLTGTGTDANGDALTYVWEQMDNASNSQTGASSAASGTKTSGPTFRSWTPTASPVRYFPRMASVLAGSTTTAGSEITVEAVPTVARTLNFRFTVRDNRSGGSGNNSDDMVVTVNGTAGPFSITSQNSATTYSGGTSQTITWNVAGTTSNGVNASNVDILWSTDSGTTWTTLLSGTPNDGSQAVTIPNASTSTGRIMVKGSNHIFFDVNNANITVNAGSGTTDTTAPTAPVLSASGTTATSTNLSWSGATDDTGVTGYDVFQAGSLLGSTSSASYTVTSLSPSTTYSFTVKAKDAAGNTSSSSNTVSVTTSAGSTVMYCSASASNTADERISNVKFGSINNSSTGTAGYENFTSVSTNVTRGTAYTISVTPVWTSTKYNEAYAVYIDYNGDGDFTDSGELAWSKSGSTTSPATGSITIPSTAVLGSTRMRVMMQYNSIPSSSCGTYTYGQVEDYTLNIVSSGRGEISTGDLLTDVKLYPNPVKDVLNISNAPAKDYKIFDMGGKLIQSGQIERGAVNVSSLIKGVYTISMGDVSKRFIKQ
>NZ_CP022986.1|WP_100074238.1|407369_408509_-|acyl-CoA-dehydrogenase-family-protein
MSTETIDNIKMIAETAKEFAEKNIRPHIMEWDESQTFPKELFHQLGEMGFMGIVIPEEYGGSGLGYHEYVAILDEISQVDPSIGLSVAAHNSLCTNHIYEFGNEEQKKRWLPQLATGKVIGAWGLTEHNTGSDSGGMSTTAVRDGDDWIINGAKNFITHAISGDIAVVMTRTGEKGAKNNSTAFVLEKGMPGFSSGKKENKLGMRASETAELIFDNVRVSDANRLGEVGEGFKQAMKILDGGRISIAALSLGTARGAYKAALKYAKERHQFGKAISEFQAINFMLADMATEIDAAELLIQRASTLKNTKQKMTKEGAMAKLYASEACVRIANNAVQIFGGYGYTKDFPAEKFYRDSKLCTIGEGTSEIQRLVIGRDITK
>NZ_CP022986.1|WP_100074239.1|408699_410583_+|endonuclease
MKKLLLSGIIFSSLLHAQAPSGYYDGTAGLSGYALKSKLHDIVSARNINWNYGDLTNYYNQTDLDRYYDHGASNTTILLDMYSEIPSGPDAYEYTTANIIGSASAEGQGWNREHMMPQSTFYSNYPMYSDLFYVVPTDARINQLRSNYPYGISTTTASNIYYTFTNTSKIGKSAIPNWVYTGRVYEPIDEFKGDVARSLLYFAVRYEGKLGTFNFDNNVSPASDTNPLDGTEERAFDPAYIAMLMQWHAQDPVSQREIDRNNAVYAIQHNRNPFIDNPAWVSAIWGQAPDAVAPQVPGNAAAIQTGAHFATLSWSASTSSDVIGYKIYQNGNLAGATRGTSISIDHLTPSTAYTFTVKAYDNGYLYSADSNTVSVTTAASDAYAKDLFISKYLEGTSNNKALEITNKTGHPVNLSDYRLSIQMPSSSSFYFPDPYELEGILQNNQTAVILNPGANFSCYTLDQARFVTAAPQMTFSGNQYVELRYKSNATVDAIGVTGQNNSSVLANVSLYRKSSINQPAVTFDINEWEVYGTNYCQNLGVLGTSDILSASNENNNLKLYPNPVSETIFVNGKTDAVRTAEILDYSGKQIYLEKDPFRYKNSIPVQGLPTGSYLLRLDDKTYPFIKK
>NZ_CP022986.1|WP_100074240.1|410743_411532_+|SDR-family-oxidoreductase
MNIQLNSKNALVGAATDGIGAGIATELARCGANVTVMARNEEKLKSFTASLPIVHQGQHHRYLVADFSDFDKFRQIITDYFNESEVDILVNNTNGPKAGKDSDLNTEDYQSAFDLLFKTVCETTHLAIPGMIKRGSGRIINVSSSSVKEPIPNLALSNSIRSAVVAWAKTLSLEVGAHQITVNTILTGSFDTRRIESLINEEAEKTGKSIEEIRKAREDKIPMKRLGKPEEYGHLVAFLASDYASYITGTSIPLDGGMMNTY
>NZ_CP022986.1|WP_100074241.1|411811_412246_+|helix-turn-helix-domain-containing-protein
MEQKIHQGRNVKRFREMLGVKQEALALDLGDEWNQKKVSLLEQKDVIEEAILQKISEILHIPVEAFQNFDEEQAITVIANTFNTHDQSSGVSIHPINNINPIEKWLEALEEIKKINDEKMSLYERMLREKDEVIVRLEKLIQDK
>NZ_CP022986.1|WP_100074242.1|412283_412685_+|helix-turn-helix-transcriptional-regulator
MKHKIHQGHNVKRFREMLGVKQENLALDLGDGWDQKKISLLEQKDLIEEILLQKISKVLNIPIEVFQNFEEEQAVNVIANTYSFQDFKDHAVASGFSYQPSFNPIDKIVELYERMIQQQKEMIDKLENLMQNK
>NZ_CP022986.1|WP_100074243.1|412745_413333_-|hypothetical-protein
MKKIIIPCLLLVVLSCGGPAAENKTAVDQAINKSESVASIDSYSRNVNRVISIYNELVKKDPQLQALEKKIDAIKEETSAVTSKYTDIITQSETYYEDARTLAKSVTDSVSRQAIEQQISSSSEQYNARIKHIRDLISSIQNNAVMINDQHTLFMISKTLPEIRKYQDAHSLKPDSLISFINKQNTLLHELKNIK
>NZ_CP022986.1|WP_002979276.1|413421_414288_-|RNA-polymerase-sigma-factor-RpoD/SigA
MRQLKITKQVTNRETASLDKYLQEIGKVELITADEEVELAQRIRAGDRAALEKLIKANLRFVVSVSKQYQNQGLSLPDLINEGNLGLMKAAKRYDETRGFKFISYAVWWIRQSILQALAEQSRIVRLPLNKIGSINKINKAYAHLEQENERPPSPEELAEVLDMSEEDIKESMKNSGRHLSMDAPLVEGEDSNLYDVLRSGESPSPDKDLMLESLQIEIERALNTLTPREADLVRLYFGLNGKHPMTLEEIGETFDLTRERVRQIKEKAIKRLKHNTRSKILKSYLGK
>NZ_CP022986.1|WP_100074244.1|414501_415293_-|S1/P1-nuclease
MKSMYSKLLMLAFISSSLYSYAWGLTGHRIIAEIAENHLSGKARREIKKMMGRERLAYWANWPDFIKSDTTGAWKQASAWHYVNIDPQTDFKTFEQKLKMQAGPSLYTQVNTLSSQIKDSRTSEKDRKIALIFLIHIMGDLAQPLHVGRAEDLGGNKINVTYFGEKTNLHSVWDGKLVDSQKYSYTEYSRLLDIKSDDEVKKIQSGTLEDWLYDSHTIANRIYAQTPDGSKLSFDYQYKFNDTVERQLLYGGLRLAKWLNDLF
>NZ_CP022986.1|WP_100077452.1|415636_416578_+|type-VI-secretion-system-baseplate-subunit-TssG
MYENSVATLHYNQLQTDFKAEAVAVNLLKYHRAVSNIFIERLGINDRAYLKDIRRITSQYLGFDEEVYTIETYREGIYDYLPEGLFHPPSLGASRKNVDHIVREIRKQKKVEEDARKFFRPFELEIFFTEVSALLKEFDFDIASDTHTLLNTVSELWPLLRMLDRHHASIFIYILPFFHQIRGDKAWFERCMSAFLMVPVEVTFAPNVIDRIEQEDDSMLLGNSRLGVTYIPSGRHMDGERNWVVNIGPIPYMEMKNYIEGSPFRNVLRALYDHFLPVTVDVEENFITEKQDFSFSLEDDERNASRLGYSTFL

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Crispr_ID: NZ_CP022986_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP022986_2

2751435-2751559

Orphan

Consensus_repeat	Method
GGAAGTTCCAACGTATTTATGGG	CRISPRCasFinder

2 spacers

The CRISPR arrays of NZ_CP022986_2

>merge|NZ_CP022986|2|2751435-2751559|CRISPRCasFinder
GGTAACCTGAACGTATTTATGGGCACTAATGCGGGCTTCGCTAATACACTGGGAAGTTCCAACGTATTTATGGGACCTTATGCAGGGACTTCCAATACCACCGGAAATTCCAACGTATTTATGGG

>NZ_CP022986|2|2|2751435-2751559|CRISPRCasFinder
GGTAACCTGAACGTATTTATGGG	CACTAATGCGGGCTTCGCTAATACACTG
GGAAGTTCCAACGTATTTATGGG	ACCTTATGCAGGGACTTCCAATACCACC
GGAAATTCCAACGTATTTATGGG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP022986.1\|WP_100076119.1\|2742586_2743483_-\|AraC-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|225117
NZ_CP022986.1\|WP_100076118.1\|2740150_2742373_-\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|372685
NZ_CP022986.1\|WP_100076120.1\|2743662_2744166_+\|superoxide-dismutase-family-protein	unknown	unknown	gnl\|CDD\|376292
NZ_CP022986.1\|WP_100076134.1\|2758791_2761236_+\|bifunctional-UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine-ligase/alanine-racemase	unknown	unknown	gnl\|CDD\|237026
NZ_CP022986.1\|WP_100076136.1\|2763402_2763807_+\|rRNA-maturation-RNase-YbeY	unknown	unknown	gnl\|CDD\|272871
NZ_CP022986.1\|WP_100076125.1\|2749634_2749877_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022986.1\|WP_100076137.1\|2763956_2765819_+\|tRNA-uridine-5-carboxymethylaminomethyl(34)-synthesis-enzyme-MnmG	unknown	unknown	gnl\|CDD\|235362
NZ_CP022986.1\|WP_100076133.1\|2757997_2758591_+\|thymidine-kinase	unknown	unknown	gnl\|CDD\|235272
NZ_CP022986.1\|WP_100076135.1\|2761238_2763398_+\|patatin-like-phospholipase-domain-containing-protein	unknown	unknown	gnl\|CDD\|132844
NZ_CP022986.1\|WP_100076131.1\|2755829_2756504_-\|16S-rRNA-(cytidine(1402)-2'-O)-methyltransferase	unknown	unknown	gnl\|CDD\|381175
NZ_CP022986.1\|WP_100076122.1\|2746686_2747466_+\|5'/3'-nucleotidase-SurE	unknown	unknown	gnl\|CDD\|234732
NZ_CP022986.1\|WP_100076117.1\|2739409_2740057_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022986.1\|WP_100076121.1\|2744219_2746349_-\|carboxy-terminal-processing-peptidase	unknown	unknown	gnl\|CDD\|236873
NZ_CP022986.1\|WP_172954700.1\|2749873_2750638_-\|prolipoprotein-diacylglyceryl-transferase	unknown	unknown	gnl\|CDD\|234599
NZ_CP022986.1\|WP_100076123.1\|2747455_2748112_+\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|225928
NZ_CP022986.1\|WP_100076129.1\|2753779_2754820_+\|GMP-reductase	unknown	unknown	gnl\|CDD\|235343
NZ_CP022986.1\|WP_100076130.1\|2754882_2755626_-\|3-oxoacyl-[acyl-carrier-protein]-reductase	unknown	unknown	gnl\|CDD\|187594
NZ_CP022986.1\|WP_100076124.1\|2748172_2749576_-\|radical-SAM-protein	unknown	unknown	gnl\|CDD\|224875
NZ_CP022986.1\|WP_100076132.1\|2756506_2757937_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022986.1\|WP_157761419.1\|2752294_2753629_+\|hypothetical-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_CP022986.1\|WP_100076119.1\|2742586_2743483_-\|AraC-family-transcriptional-regulator	gnl\|CDD\|225117	COG2207, AraC, AraC-type DNA-binding domain-containing proteins [Transcription].	3.08108e-25
NZ_CP022986.1\|WP_100076118.1\|2740150_2742373_-\|TonB-dependent-receptor	gnl\|CDD\|372685	pfam13715, CarbopepD_reg_2, CarboxypepD_reg-like domain. This domain family is found in bacteria, archaea and eukaryotes, and is approximately 90 amino acids in length. The family is found in association with pfam07715 and pfam00593.	5.18646e-13
NZ_CP022986.1\|WP_100076120.1\|2743662_2744166_+\|superoxide-dismutase-family-protein	gnl\|CDD\|376292	pfam00080, Sod_Cu, Copper/zinc superoxide dismutase (SODC). superoxide dismutases (SODs) catalyze the conversion of superoxide radicals to hydrogen peroxide and molecular oxygen. Three evolutionarily distinct families of SODs are known, of which the copper/zinc-binding family is one. Defects in the human SOD1 gene cause familial amyotrophic lateral sclerosis (Lou Gehrig's disease). Structure is an eight-stranded beta sandwich, similar to the immunoglobulin fold.	7.76097e-46
NZ_CP022986.1\|WP_100076136.1\|2763402_2763807_+\|rRNA-maturation-RNase-YbeY	gnl\|CDD\|272871	TIGR00043, Endoribonuclease_YbeY, rRNA maturation RNase YbeY. This metalloprotein family is represented by a single member sequence only in nearly every bacterium. Crystallography demonstrated metal-binding activity, possibly to nickel. It is a predicted to be a metallohydrolase, and more recently it was shown that mutants have a ribosomal RNA processing defect. [Protein synthesis, Other].	4.97241e-30
NZ_CP022986.1\|WP_100076137.1\|2763956_2765819_+\|tRNA-uridine-5-carboxymethylaminomethyl(34)-synthesis-enzyme-MnmG	gnl\|CDD\|235362	PRK05192, PRK05192, tRNA uridine-5-carboxymethylaminomethyl(34) synthesis enzyme MnmG.	0
NZ_CP022986.1\|WP_100076133.1\|2757997_2758591_+\|thymidine-kinase	gnl\|CDD\|235272	PRK04296, PRK04296, thymidine kinase; Provisional.	2.07005e-81
NZ_CP022986.1\|WP_100076135.1\|2761238_2763398_+\|patatin-like-phospholipase-domain-containing-protein	gnl\|CDD\|132844	cd07205, Pat_PNPLA6_PNPLA7_NTE1_like, Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1. Patatin-like phospholipase domain containing protein 6 (PNPLA6) and protein 7 (PNPLA7) are included in this family. PNPLA6 is commonly known as Neuropathy Target Esterase (NTE). NTE has at least two functional domains: the N-terminal domain putatively regulatory domain and the C-terminal catalytic domain which shows esterase activity. NTE shows phospholipase activity for lysophosphatidylcholine (LPC) and phosphatidylcholine (PC). Exposure of NTE to organophosphates leads to organophosphate-induced delayed neurotoxicity (OPIDN). OPIDN is a progressive neurological condition that is characterized by weakness, paralysis, pain, and paresthesia. PNPLA7 is an insulin-regulated phospholipase that is homologus to Neuropathy Target Esterase (NTE or PNPLA6) and is also known as NTE-related esterase (NRE). Human NRE is predominantly expressed in prostate, white adipose, and pancreatic tissue. NRE hydrolyzes sn-1 esters in lysophosphatidylcholine and lysophosphatidic acid, but shows no lipase activity with substrates like triacylglycerols (TG), cholesteryl esters, retinyl esters (RE), phosphatidylcholine (PC), or monoacylglycerol (MG). This family includes subfamily of PNPLA6 (NTE) and PNPLA7 (NRE)-like phospholipases.	4.97377e-57
NZ_CP022986.1\|WP_100076134.1\|2758791_2761236_+\|bifunctional-UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine-ligase/alanine-racemase	gnl\|CDD\|237026	PRK11930, PRK11930, putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine racemase; Provisional.	0
NZ_CP022986.1\|WP_100076122.1\|2746686_2747466_+\|5'/3'-nucleotidase-SurE	gnl\|CDD\|234732	PRK00346, surE, 5'(3')-nucleotidase/polyphosphatase; Provisional.	4.58285e-129
NZ_CP022986.1\|WP_100076130.1\|2754882_2755626_-\|3-oxoacyl-[acyl-carrier-protein]-reductase	gnl\|CDD\|187594	cd05333, BKR_SDR_c, beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs. This subgroup includes the Escherichai coli K12 BKR, FabG. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. 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 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. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.	9.47181e-126
NZ_CP022986.1\|WP_100076121.1\|2744219_2746349_-\|carboxy-terminal-processing-peptidase	gnl\|CDD\|236873	PRK11186, PRK11186, carboxy terminal-processing peptidase.	2.0559e-132
NZ_CP022986.1\|WP_172954700.1\|2749873_2750638_-\|prolipoprotein-diacylglyceryl-transferase	gnl\|CDD\|234599	PRK00052, PRK00052, prolipoprotein diacylglyceryl transferase; Reviewed.	8.43153e-18
NZ_CP022986.1\|WP_100076123.1\|2747455_2748112_+\|GNAT-family-N-acetyltransferase	gnl\|CDD\|225928	COG3393, COG3393, Predicted acetyltransferase [General function prediction only].	1.40285e-14
NZ_CP022986.1\|WP_100076129.1\|2753779_2754820_+\|GMP-reductase	gnl\|CDD\|235343	PRK05096, PRK05096, guanosine 5'-monophosphate oxidoreductase; Provisional.	0
NZ_CP022986.1\|WP_100076131.1\|2755829_2756504_-\|16S-rRNA-(cytidine(1402)-2'-O)-methyltransferase	gnl\|CDD\|381175	cd11648, RsmI, Ribosomal RNA small subunit methyltransferase I (RsmI), also known as rRNA (cytidine-2'-O-)-methyltransferase. RsmI is an S-AdoMet (S-adenosyl-L-methionine or SAM)-dependent methyltransferase responsible for the 2'-O-methylation of cytidine 1402 (C1402) at the P site of bacterial 16S rRNA. Another S-AdoMet-dependent methyltransferase, RsmH (not included in this family), is responsible for N4-methylation at C1402. These methylation reactions may occur at a late step during 30S assembly in the cell. The dimethyl modification is believed to be conserved in bacteria, may play a role in fine-tuning the shape and functions of the P-site to increase the translation fidelity, and has been shown for Staphylococcus aureus, to contribute to virulence in host animals by conferring resistance to oxidative stress.	1.07523e-117
NZ_CP022986.1\|WP_100076124.1\|2748172_2749576_-\|radical-SAM-protein	gnl\|CDD\|224875	COG1964, COG1964, Predicted Fe-S oxidoreductases [General function prediction only].	1.01378e-54

>NZ_CP022986.1|WP_172954700.1|2749873_2750638_-|prolipoprotein-diacylglyceryl-transferase
MDFPVTFHIFGKSILAHPLFEAVGMFVGMRYYFYLKRKSPEKLSFNTSAAVLIGATAGALIGSKLIGNLENPFILFSEKFSLARFWSNNTIVGGLAFGLAGVELAKKIVGHRESTGDLIVFPLMLAIIIGRIGCFLTGIYEETYGIPTRFIFGMHLGDQYLRHPVALYEIAFLIMLWIFLKKIQNSRKYVSGFVFQLFMVAYFMFRFCLDFIKPRVELVWSLGTIQLVCLCVIIYYIFKIKDTKSVHSHQISNI
>NZ_CP022986.1|WP_100076125.1|2749634_2749877_-|hypothetical-protein
MKTLTLLEVNNLGLGGFLLIIILIILFVALVVSVIITLIVKLIYESGNNNTFSKKQFIQTMLICMLVFGLISGYICGGGF
>NZ_CP022986.1|WP_100076124.1|2748172_2749576_-|radical-SAM-protein
MPVRNYTYYDYTISLCPECLKRVGAKIIIEEDSVFMTKRCPDHGFFKTKIASDVHYYKNIRNYNKASEMPLHFGTDVEYGCPYDCGLCVDHEQHSCLSIVEVTDRCNLTCPTCYAMSSPHYGSHRSLEEIEAMFDVIVKNEGEPDVVQISGGEPTIHPEFFRIMDIAKSKPIKHLMLNTNGIRIANDPGFAEKLAGYAPEFEIYLQFDSFKPEVLQDFRGKDLTDVRMRALEKLNALNLSTTLVVVLQKDKNIDEIGKIIEFALRQKCVRGITFQPVEIAGRNRADSPYEKITLTEVRQEILNQFPLLNSDDIIPVPCNPDALAMGYILKLEGETIPLTRYINPADLLNNETRNTIVYEQDTGLQMQLLDIFSTGISVDKVQPKVNQLLCCLPEVCAPDLDYDNLFRIIIMNFMDAHDFDVRAVKKSCVHIVNKDLKLIPFETMNLFYRDDKIKYLEELRKEDKVLF
>NZ_CP022986.1|WP_100076123.1|2747455_2748112_+|GNAT-family-N-acetyltransferase
MYSKLDSPVYHALNEFHEKFCLHFGDTKFYTPEVAAFGGSAHVSGEKDITAYAKSCDDFLIFGAKPKTDQSLSRLVCDQYVLEKMITLDYTEEIIQLKEEHYEELLAFIAKFYPYYFKNRTPELGRYFGIFKEGILVAVTGERMQMNDMTELSAVITDTGYLGKGYAKQLVAHVSGKIQEDNKTPFLHVAESNAGAIKLYEKLGFSHRGKIDVWGIKR
>NZ_CP022986.1|WP_100076122.1|2746686_2747466_+|5'/3'-nucleotidase-SurE
MEKPLILVTNDDGITAPGIRNLVSFMNEIGDVIVVAPNSPQSGKGHAITINSTLSYEEVHLDGPQKDFSCSGTPVDCVKMALDKILPRRPDIVVSGINHGANSSINVIYSGTMSAAVEGGVEGLPSIGFSLLDFSWEADFTQAKEYIQNIVKRVLEQPMPKGIVLNVNIPKLSKEEIKGVKVCKQAHAKWEESFDERVNPHGKKYYWLTGYFNNMDESEDADETALANGYISIVPVKFDLTAYEYMNTLSEVMKFDHVQ
>NZ_CP022986.1|WP_100076121.1|2744219_2746349_-|carboxy-terminal-processing-peptidase
MWKNFKLNKFLLLIPLTSLMFCFNSPKNDDEKMQTIMVSVKNTLSYLHYSPKPINDAYARDVYKQYFEMIDPAKRYFLQSDMDEFAKHETKLDDYLNTGDLTFYKLTVDRLYQRVDEIDKVTQDIFSKPINLNEDETLTLEPKLKKVPSNKQEQYNEWKKFIKYNILQEIESMNSKEEAQKEKKDSVQQYKLKDTIKLKILTPDEKVKKATDEVKDLVKETFTRFKKRKKMDWFTVYMNAYTEVFDPHTNYYSPKDKEDFDTSFTGKVIGIGAIIQEKKGYLYLGALTIGAPAWKSKQLSEGDKILKVKSKPKEDAVNVVGMLSDEAVRLIRGEKGTPVTLTVQKKDGTIKDVTMIREEVAIEDTFARSIIVNAPNGKKYGFINLPSFNADFENEKGRNASDDIKNEIIKLKAQNIQGIILDLRNNGGGSLTEVGDIMGLFMKSGPYVQVKDGNGKIQTLKNKNETPIWTGPLVIMQNELSASASEILAGVMQDYGRAIIVGSPQSFGKGTVQSFVDLNRFLNTEDDFGSLKLTIQKFYRITGESTQRKGIVSDIQMKDFFTYAEIGERFDDYALAWDKIPGTSFEKLNYFDIKALEKASADRMAKNTNYQLLLESAQWREKLDKEETITLNINKFNELMKQRKAQIEKFKSLTKFENGLQFMMYQNEIEREKKDEAFKKKSELWIKNLKKDLYLQEAMNIIADMNAKA
>NZ_CP022986.1|WP_100076120.1|2743662_2744166_+|superoxide-dismutase-family-protein
MNLKTLTLLAGSALFAVSCGTSHTYQVMSKSNTQTGGTAKFTQKGNDVIMKLDVTNLTPGIHAVHIHEKGDCSAPDGTSAGGHWNPAKDDHGKWGAEHFHMGDIGNLNADQSGNATLTFKTDKWCLGCEDASKNIMGKGLIIHADKDDFHTQPTGNAGGRVGCVEIR
>NZ_CP022986.1|WP_100076119.1|2742586_2743483_-|AraC-family-transcriptional-regulator
MHKQSIIKAIRYIEDHLDSELSLENVSGAGAYSPFHFHRIFRLITGETLQNYTARRRTEKSAFYLALRKDISIADVYHQSGFSSHSAFNKAFKKYYGISPSGFRKAAPENFHRIAIKESKKGHRDAIFSQYIYNTENLLNWMNMNLKIKVGHLPEMHLAAVMSLGIAHVESSFGTLIDWAKSKNLFPRDQVKMLSVYHDSFKVTPPDKVRIHACMLLDEPLQKQEGEVFPETVETGKFIIGSGEVTLDDFEQCWVSLFLWMKEHHHSVRKAFPFEIYHTNFREHPEGKMTVDFCIPIH
>NZ_CP022986.1|WP_100076118.1|2740150_2742373_-|TonB-dependent-receptor
MKTKLLFLISFLCSMLSLAQIKVSGKVTYKSKGVADVNITLKNTYDGATTDAEGNFSFETNEKGSQAITFTHPKYDDVEKPVMIQDQAITVNAELKEQINEIDAIVVSAGSIEASDKKRATALLTPIDIYTTAGADGQISSALTYLPGVQKVGESEGLFIRGGTGAESKIFMDGSLINNYFSNSVPGIAGRDRFNTSLFKGNIFSSGGYSALYGQALSGALMLESVDLPNESSYDIGVSPIFIDAGFQRLSKNKNYSYGATAGYSNLELMQNVLHFNTDFIQSPRSMNGDLNFRIKTKSGGFFKYYGKYDTNRMAVRTESLEPQYDAALIRLKGTNTYHNLSFRQKFGKYLLNIGSSYSYNRSDLNFSTENAGQESARTQLLTDGNYINLKAVLERKINRISALRGGFEFNNSDEQLHFQQVNKKYNDLISSAFVESDLGFSNQLSAKIGVRAEHSSFLDKNNIAPRLALAYRLDKNWTSSIAYGLFYQNPESRYINAPANLGFQQSQHYIFQIQRASEGRSLRLEAFYKKYDQLIKTFTLNPGESQNQQIQTALNNDGYGYAKGAEFFWRDKKTFKNIDYWISYSYLDSKRDFMNYPVSLKPNFAAEHTLSVVAKRFITEWKLGANLSYTYAKGRPYYDIVSQQNSNVIRNEGRLKDYSSLNLSFNYLPNLGKKDAKAFTIFVLSISNVLGTKNMYGYNFSGDGARSSAVVPPSNTFVFIGAFISFGVDKTEDAINNNL
>NZ_CP022986.1|WP_100076117.1|2739409_2740057_-|hypothetical-protein
MKKYLLSFALAFVSLTAFAQTDYEKVMTEKVARIETAKTAEDFQALANDFHRIAGKDENNWLPFYYAALANIQKGRVLMQQGKTQDLDFIAGQAEKYIGAASHVAPTDNAELHLLSKMAYSLKMMVNPQQRYMTDGAKATEELKKAEKLDPNNPRIALIKAEDVYFMPEQYGGSKVKGMEMFKDALNKFKSYTPKTALDPNWGKSEAEYFVSQAK
>NZ_CP022986.1|WP_157761419.1|2752294_2753629_+|hypothetical-protein
MRIILCLFFLLGLSALHAQIPGTPIIPLKENRNVFGGTSVDFARSAVATTDGGYALAGYSASSDGDVSANNGNIDFWIIKVSSSGNLQWKKTLGGSDNDEARSIVQTADGGYAIAGITASNNGDVSGNHGGNDFWIVKLDSSGALHWQKTLGGPADDNAYSLVQTSDGGYAIAGFTASNSGDVSGNLGGFDFWVVKLDQFGALQWQKTLGGSGTESALSIVQTTDGGYAVAGYSDSTNGDGVGNNGNQDYLIVKLSNTGTVEWHKVFGGTDTDLANAVIQTADGGFAVAGYALSNNGNVSGNHGVYDSWIIKLDNIGNLQWQKALGGSGSENTFAILQDTDGTYVVAGDTRSNDGNVSGNHGVVDAWVVKLSTTGNLLWQKAIGGTLGDSATAVARSQNGYVIAGRSNSTDGDITGPVNGSSDFLLLKIDTNGNIIRFWDDTAP
>NZ_CP022986.1|WP_100076129.1|2753779_2754820_+|GMP-reductase
MRIEYDIKLGFKDVMFRPKRSTLKSRSEVDLEREFTFLHTQKKWKGIPVIAANMDTVGTFEMAVELAKEKIITAVHKHYSPEEWDAFLDSQPESIYQYIALSTGTGNADKEKIRHILEKHPKIEFLCIDVANGYSEHFVDFVKAARSNFPDKIIIAGNVVTGEMVEELLLVGADIIKVGIGPGSVCTTRVKTGVGYPQLSAIIECSDAAHGLGGHIIADGGCKVPGDVAKAFGGGADFVMLGGMFAGHDESGGEIVEENGKKFRLFYGMSSKTAMDKHSGGVAEYRASEGKTVRVPYKGPVAGTVKDILGGVRSTCTYVGASKLKELSKRTTFIRVQEQENQVFKD
>NZ_CP022986.1|WP_100076130.1|2754882_2755626_-|3-oxoacyl-[acyl-carrier-protein]-reductase
MKLLEGKVALITGATRGIGKGIAEVFAQHGAKIAFTYAGSVDKAKELEAALSSVTQIKGYQSDASDYDAAQKLIDEVMAEFGQIDILINNAGITKDNLLLRMSKEDWDVIMRVNLDSVFNLTKAVIKPMMKAKSGSIINMTSVVGISGNAGQANYAASKAGVIGFTKSVALELGSRNIRCNAIAPGFIETEMTAALDEKTTQTWREGIPLKRGGKPEDVANACVFLGSDMSAYVTGQTLNVDGGMLT
>NZ_CP022986.1|WP_100076131.1|2755829_2756504_-|16S-rRNA-(cytidine(1402)-2'-O)-methyltransferase
MSGILYFVPTPVGNLEDMTFRAVKVLKEVDYILCEDTRTSGILLKHFEISKPLKSYHLHNEHQATEKVIADLKSGQNIAIITDAGTPGISDPGYLLGKAGADHDIEMICLPGATALIPALVVSGLPNNEFLFAGFLPQKKGRQTKLKQLAEEKKTIVLYESPHKINTTLEQIKEFFGENTRASLSREISKKFEETKRGTITELIEFSKSKTLKGEIVLIVNNSI
>NZ_CP022986.1|WP_100076132.1|2756506_2757937_-|hypothetical-protein
MQNIQDLKEKIFFESRNIIGILDKINHADELASCQDLVNDLAERITLLSLLQKHAAHRPEEKGDFQPFVTKSASYEPYEPVTEEEAIFNNEFNEIPEYEKQAFKGVTEEEAIFNNQLNEIVENELHETVVHFVEEQSQEPEGHQEAVSGQNWNEDVASHKETEPEDSGISGVPESTDEAMEEEAVFNNQLNEIEGFENEISDEGNVPNNDFEEEERIRDGFDASGQEEEKKADMKAVIPSIFDTGMTEDEILIEEHENQFLSSSTTNMEQGEMVTETSSVDHMLSEIKNEPSEEEGKEKESTLAEINDRRKITDIFNPHITSDHKDSEHKPSDKNFEDLDAYQQEKKIRLAHIKGMKAVQSLFDDDHLQIGHSHEKTDEIRPDAGSILKTNIPTNFMEAEKARPQFKLDLNDRIAFTKMLFGGSQTDLNEVIGNLNSFKSLDEAKEYLSDLYYERKWNKVDEYAQRLWILVENKFI
>NZ_CP022986.1|WP_100076133.1|2757997_2758591_+|thymidine-kinase
MFLENTINHSKQSGWMEVICGSMFSGKTEELIRRLRRAEMAGQNVEIFKPKMDIRYSEEDIVSHNQNKIRSTAVDYPGEILLLASNCDVVAIDEAQFFDDSIVDVANTLANGGIRVVIAGLDMDFLGRPFGPMPNLMATAEYVTKVHAICRRTGNLANYSMRTSQGNDLVELGETESYEAVSRRVFIDEVLSRQRTK
>NZ_CP022986.1|WP_100076134.1|2758791_2761236_+|bifunctional-UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine-ligase/alanine-racemase
MNYTVQEISAITQSRSIGNKKLIVRNIAFDSRTIYSIQDTAFIAINTHKNSGEKFIESAVDRGIQVIISEHHYPRFDQVTWIIVENAVDFLQRLAAHHFGHAHIKSIGITGSNGKTILKEWLYQCLWNEFSTVKSPKSFNSQIGLPLSLLQINDTHELGIFEAGISKPGEMQKLEHIFHPQIGLLTHMGNAHAANFRSEQQLIEEKIILFKNSEVIIYNGDNILTDKKIKDLYSGRKLISYGLSTANDVFLKKNVKDEDIIVQYFQEEISFPAHQRDEATLTNAMALITVLKELNLDHAKIVEKINALRSVEMRLEAIEGIKGNIVINDSFNLDLDSLKTALQFLKEYNKPQKSLVLTDIVGVNSNSEELYTEVADLVNEQHFNTVFLIGEEITSFSHLLTPETFTFNNTQELIDSKRLTEINNQIILLKGARKFGIERLKDILELRKHDTVLEVNLNAILHNINYHKSLLNPGTRMMAMVKANAYGLGSYEIAEFLQHHHIDYLGVAYADEGVELRKKGITAPIIVMNPEQHSYEAIIEYSLEPEIYSLRVLELFNDAVQKAGYDERYPIHIKLETGMNRLGFKEADLAPLLEALRHKNLRVESIFSHLSSSDIPSEKEFTLRQMAVFRKNSDILIKNLGYQPIRHILNSSGITEYPDYQYDMVRIGIGMLGESQNSDIKKQLRPVVSFKTVISQISQVQEGESVGYSRKYKADHPTRIATIPVGYADGIPRLIGNQVGKVGIGKKLAPIVGNICMDMMMINIDGIPHVKEGDPVILFNGQPSLKEFAGYCNTITYEVLTSISPRVKRIYIKD
>NZ_CP022986.1|WP_100076135.1|2761238_2763398_+|patatin-like-phospholipase-domain-containing-protein
MKKKFLVLFCLFLLHAMHAQIRKDLKIPKNPRIGLSLAGGGAKGFAHVGVLKVLDSLGVKVDYIAGTSMGAIVGGLYASGYSAKDIEKIVMDTDFYSLILDPKSRQESTFFNKSVDKYLFSIPLKNGKITLPSSISTGQKNVYLLKELLKNVSNINDFSKLPIPFMCVATNLESGDMKIFESGDLVQSIMASSAFPSLMDPVKVGDSIYIDGAMSVNYPSKPLKDKGIDIVIGVDLNQDLSKREDLNSIIAILNQVIDFGIRRDTKRQYEYTDINIKPNLTGMSATSYDDKKKILDSGYTEGKKYSAILNELPKRTYDRLRQPMSPIYSNVYKIDSIELIGSRIYGENYVLGKMGLRLPSMQTYGSVNKMIDKLVATNNYRFINYDIVTQNNSNYLKLYVTEDDTRHFLKFGLHYDEVFKTGLLVNYSAKRLLFRNTNLSLDVIVGDKPRYYLNYFIDNGYIPGFGIYSSGMNFDLRDQQNNEIDNWEWYRNEAYIQSIWRDKFAIGGGISHDYFEANMNGSNKRYSRFLNPYVFVKSDTQDDKEFPTKGFYLSAEGKVIDILSSEMRDKPVQVQADIRINIPVSRQFSYHLNLYGGITIGEELPEYYRYRLGGIFEQNVINFRSFGGFYFAQLATNNILMASNDLQFRFNKNYFITGTFTFANLSDSISVEQAVKLNYSSLGITAGYKSPFGQIKVNFSHSLRNNQKGIFSVILGHWF
>NZ_CP022986.1|WP_100076136.1|2763402_2763807_+|rRNA-maturation-RNase-YbeY
MIQFFYETQPESVNTDYKQWLEAIIISEGKKPGEINYIFCDDEYLLKINQDYLQHDYYTDIITFDYVKGKTINGEIFVSLQRISDNASTLSREYEEELRRVLAHGILHLSGYKDKTEEEEKLMRSKEDFYLKQY
>NZ_CP022986.1|WP_100076137.1|2763956_2765819_+|tRNA-uridine-5-carboxymethylaminomethyl(34)-synthesis-enzyme-MnmG
MISEVYDVIVVGAGHAGCEAAAAAANMGSKTLLITMNMQTIGQMSCNPAMGGIAKGQIVREIDAMGGYSGIVADKSAIQFKMLNLSKGPAMWSPRTQNDRMLFAEEWRLALENTPNLDFFQDMVKQLIVENNTVKGVVTSLGIEIKGKSVVLTNGTFLNGLIHVGDKQLGGGRMGEPRAFGITEQLVSLGFEAGRMKTGTPPRVDGRSLDYSKMEEQKGDEHPQKFSYLDTPKLTKQLSCHIVYTNETVHDILREGFDRSPMFNGTIQSLGPRYCPSIEDKINRFAERNRHQLFVEPEGWKTVEIYVNGFSSSLPEDVQIKAMKHIPGFENVKVFRPGYAIEYDYFPPTQLKHTLETKLIDNLYFAGQINGTTGYEEAAGQGLMAGINAHNKVHEKDEFILNRDEAYIGVLIDDLITKGTEEPYRMFTSRAEYRLLLRQDNADIRLTEKAYHLGLAKEERLKLVEKKVAQSEELEAFLRETSLKPGIINPILESIESSPVDQAYRASQILTRPNMTLEKLEAVESINDFISQYNEEVREQAEVNIKYRGYIEKEKENVAKLNRLENIKIPEDFDFTKLSSLSAEAKQKMTRVRPKTIAQAGRISGVSPADINVLLVYLGR

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Crispr_ID: NZ_CP022986_3

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP022986_3

3156870-3156992

Orphan

Consensus_repeat	Method
TGCTGACGCTGCTAAAGATGCTGC	CRISPRCasFinder

2 spacers

The CRISPR arrays of NZ_CP022986_3

>merge|NZ_CP022986|3|3156870-3156992|CRISPRCasFinder
TGTAGACGCTACTAAAGATGCTGCTTCTGCTACTACTGCTGCTGGTGCTGACGCTGCTAAAGATGCTGCTAAGAACGCTGGTGAAGCTGCTAAAGGAGCTGCTGACGCTGCTAAAGATGCTGC

>NZ_CP022986|3|3|3156870-3156992|CRISPRCasFinder
TGTAGACGCTACTAAAGATGCTGC	TTCTGCTACTACTGCTGCTGG
TGCTGACGCTGCTAAAGATGCTGC	TAAGAACGCTGGTGAAGCTGCTAAAGGAGC
TGCTGACGCTGCTAAAGATGCTGC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP022986.1\|WP_100076457.1\|3145341_3145596_-\|30S-ribosomal-protein-S20	unknown	unknown	gnl\|CDD\|178943
NZ_CP022986.1\|WP_100076472.1\|3162247_3162724_-\|DNA-starvation/stationary-phase-protection-protein	unknown	unknown	gnl\|CDD\|223854
NZ_CP022986.1\|WP_100076463.1\|3152872_3154249_+\|rhodanese-related-sulfurtransferase	unknown	unknown	gnl\|CDD\|234663
NZ_CP022986.1\|WP_100076465.1\|3154778_3155363_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022986.1\|WP_100076464.1\|3154254_3154830_+\|5-formyltetrahydrofolate-cyclo-ligase	unknown	unknown	gnl\|CDD\|274270
NZ_CP022986.1\|WP_100076470.1\|3159858_3160512_+\|SGNH/GDSL-hydrolase-family-protein	unknown	unknown	gnl\|CDD\|239945
NZ_CP022986.1\|WP_100076466.1\|3155346_3156510_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022986.1\|WP_100076458.1\|3146074_3147361_-\|N-acetylmuramoyl-L-alanine-amidase	unknown	unknown	gnl\|CDD\|119407
NZ_CP022986.1\|WP_100076462.1\|3150958_3152494_-\|trypsin-like-peptidase-domain-containing-protein	unknown	unknown	gnl\|CDD\|273938
NZ_CP022986.1\|WP_100076460.1\|3150057_3150438_+\|RidA-family-protein	unknown	unknown	gnl\|CDD\|129116
NZ_CP022986.1\|WP_100076474.1\|3164140_3166258_+\|elongation-factor-G	unknown	unknown	gnl\|CDD\|237185
NZ_CP022986.1\|WP_002661363.1\|3166276_3166582_+\|30S-ribosomal-protein-S10	unknown	unknown	gnl\|CDD\|179076
NZ_CP022986.1\|WP_100076461.1\|3150441_3150897_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022986.1\|WP_100076473.1\|3163657_3164134_+\|30S-ribosomal-protein-S7	unknown	unknown	gnl\|CDD\|235398
NZ_CP022986.1\|WP_100076468.1\|3157253_3158024_-\|RNA-methyltransferase	unknown	unknown	gnl\|CDD\|349977
NZ_CP022986.1\|WP_100076459.1\|3147414_3150003_+\|LPS-assembly-protein-LptD	unknown	unknown	gnl\|CDD\|224369
NZ_CP022986.1\|WP_157761432.1\|3160593_3160839_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022986.1\|WP_100076469.1\|3158117_3159620_-\|DNA-recombination-protein-RmuC	unknown	unknown	gnl\|CDD\|376878
NZ_CP022986.1\|WP_002983146.1\|3163220_3163634_+\|30S-ribosomal-protein-S12	unknown	unknown	gnl\|CDD\|235355
NZ_CP022986.1\|WP_100076471.1\|3160976_3162155_-\|nicotinate-phosphoribosyltransferase	unknown	unknown	gnl\|CDD\|235406

Protein	Function_ID	Function_description	E-value
NZ_CP022986.1\|WP_100076457.1\|3145341_3145596_-\|30S-ribosomal-protein-S20	gnl\|CDD\|178943	PRK00239, rpsT, 30S ribosomal protein S20; Reviewed.	1.82133e-22
NZ_CP022986.1\|WP_100076472.1\|3162247_3162724_-\|DNA-starvation/stationary-phase-protection-protein	gnl\|CDD\|223854	COG0783, Dps, DNA-binding ferritin-like protein (oxidative damage protectant) [Inorganic ion transport and metabolism].	8.52937e-58
NZ_CP022986.1\|WP_100076463.1\|3152872_3154249_+\|rhodanese-related-sulfurtransferase	gnl\|CDD\|234663	PRK00142, PRK00142, rhodanese-related sulfurtransferase.	1.12933e-145
NZ_CP022986.1\|WP_100076474.1\|3164140_3166258_+\|elongation-factor-G	gnl\|CDD\|237185	PRK12739, PRK12739, elongation factor G; Reviewed.	0
NZ_CP022986.1\|WP_100076464.1\|3154254_3154830_+\|5-formyltetrahydrofolate-cyclo-ligase	gnl\|CDD\|274270	TIGR02727, Uncharacterized_protein_YqgN, 5,10-methenyltetrahydrofolate synthetase. This enzyme, 5,10-methenyltetrahydrofolate synthetase, is also called 5-formyltetrahydrofolate cycloligase. Function of bacterial proteins in this family was inferred originally from the known activity of eukaryotic homologs. Recently, activity was shown explicitly for the member from Mycoplasma pneumonia. Members of this family from alpha- and gamma-proteobacteria, designated ygfA, are often found in an operon with 6S structural RNA, and show a similar pattern of high expression during stationary phase. The function may be to deplete folate to slow 1-carbon biosynthetic metabolism. [Central intermediary metabolism, One-carbon metabolism].	2.13818e-37
NZ_CP022986.1\|WP_100076470.1\|3159858_3160512_+\|SGNH/GDSL-hydrolase-family-protein	gnl\|CDD\|239945	cd04501, SGNH_hydrolase_like_4, Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid.	1.30174e-65
NZ_CP022986.1\|WP_100076458.1\|3146074_3147361_-\|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.	5.86847e-58
NZ_CP022986.1\|WP_100076462.1\|3150958_3152494_-\|trypsin-like-peptidase-domain-containing-protein	gnl\|CDD\|273938	TIGR02037, Probable_periplasmic_serine_protease_do/HhoA-like, periplasmic serine protease, Do/DeqQ family. This family consists of a set proteins various designated DegP, heat shock protein HtrA, and protease DO. The ortholog in Pseudomonas aeruginosa is designated MucD and is found in an operon that controls mucoid phenotype. This family also includes the DegQ (HhoA) paralog in E. coli which can rescue a DegP mutant, but not the smaller DegS paralog, which cannot. Members of this family are located in the periplasm and have separable functions as both protease and chaperone. Members have a trypsin domain and two copies of a PDZ domain. This protein protects bacteria from thermal and other stresses and may be important for the survival of bacterial pathogens.// The chaperone function is dominant at low temperatures, whereas the proteolytic activity is turned on at elevated temperatures. [Protein fate, Protein folding and stabilization, Protein fate, Degradation of proteins, peptides, and glycopeptides].	1.37136e-134
NZ_CP022986.1\|WP_100076460.1\|3150057_3150438_+\|RidA-family-protein	gnl\|CDD\|129116	TIGR00004, RutC_family_protein, reactive intermediate/imine deaminase. This protein was described initially as an inhibitor of protein synthesis intiation, then as an endoribonuclease active on single-stranded mRNA, endoribonuclease L-PSP. Members of this family, conserved in all domains of life and often with several members per bacterial genome, appear to catalyze a reaction that minimizes toxic by-products from reactions catalyzed by pyridoxal phosphate-dependent enzymes. [Cellular processes, Other].	1.50592e-56
NZ_CP022986.1\|WP_002661363.1\|3166276_3166582_+\|30S-ribosomal-protein-S10	gnl\|CDD\|179076	PRK00596, rpsJ, 30S ribosomal protein S10; Reviewed.	6.42028e-62
NZ_CP022986.1\|WP_002983146.1\|3163220_3163634_+\|30S-ribosomal-protein-S12	gnl\|CDD\|235355	PRK05163, rpsL, 30S ribosomal protein S12; Validated.	9.21734e-88
NZ_CP022986.1\|WP_100076473.1\|3163657_3164134_+\|30S-ribosomal-protein-S7	gnl\|CDD\|235398	PRK05302, PRK05302, 30S ribosomal protein S7; Validated.	3.412e-92
NZ_CP022986.1\|WP_100076468.1\|3157253_3158024_-\|RNA-methyltransferase	gnl\|CDD\|349977	cd18104, SpoU-like_RNA-MTase, SAM-dependent RNA methylase related to SpoU-TrmH. RNA 2'-O ribose methyltransferase catalyzes the methyltransfer from S-adenosyl-L-methionine (AdoMet) to the 2'-OH group of ribose in tRNA or rRNA. It is part of the SpoU family of MTases, a subfamily of the SPOUT methyltransferase superfamily. The SPOUT methyltransferase superfamily is a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot.	3.81738e-69
NZ_CP022986.1\|WP_100076459.1\|3147414_3150003_+\|LPS-assembly-protein-LptD	gnl\|CDD\|224369	COG1452, Imp, Organic solvent tolerance protein OstA [Cell envelope biogenesis, outer membrane].	4.71356e-10
NZ_CP022986.1\|WP_100076471.1\|3160976_3162155_-\|nicotinate-phosphoribosyltransferase	gnl\|CDD\|235406	PRK05321, PRK05321, nicotinate phosphoribosyltransferase; Provisional.	0
NZ_CP022986.1\|WP_100076469.1\|3158117_3159620_-\|DNA-recombination-protein-RmuC	gnl\|CDD\|376878	pfam02646, RmuC, RmuC family. This family contains several bacterial RmuC DNA recombination proteins. The function of the RMUC protein is unknown but it is suspected that it is either a structural protein that protects DNA against nuclease action, or is itself involved in DNA cleavage at the regions of DNA secondary structures.	2.74615e-111

>NZ_CP022986.1|WP_100076466.1|3155346_3156510_-|hypothetical-protein
MTDLDLLHFEQLKKEVQAQYLEEYTPSHDDISKWKGIDIIYFQEDLRKKAKGNISEKSFYTYFKNSPVTKLPRIDMLNLLSIYAGYDSWYEFKKQHLFAGELLQQDEELSEEEIKELEHLTEIAPDLPKTEQNPEKTVQKQPEIPNLQKSDTENQPVNTPINVSTTQLPNAVSEPKNFFRKNAWIMLTAVLVTISGVLGFKDELFSKNYTFCFTDADRGVNVINTLEIKVIKENESPLLYKIKPGECFEYSTKDKILKMQISAPFYETLDVNRNLETAPDKEMIELKPDDYKMAVNYFSVKDANGNPELLKQKRKQLENLISDRAIIYQVYDNATYGIETLDKQKYITLVTTPTTSLKNLSVIEMKKDKGKIVSIKFKIASTNENKQ
>NZ_CP022986.1|WP_100076465.1|3154778_3155363_-|hypothetical-protein
MKINNNFLLFAILVCSLLACTKKTTEVSDLDKLRNSNNKASYPAVQMDSAQAINFITRQKVQELLDLSTLYLSGNRKTEIDSVIYSQMESYFHKPDSLTFNRLFRELDSLKVKTAKVKSLEVYKDYYKEDTLDFARFDVEYFDDKNRSLGNYEKNAQYILVSKPIQFKKEFKFYFLNFYAPPLKKDTTSVGVTR
>NZ_CP022986.1|WP_100076464.1|3154254_3154830_+|5-formyltetrahydrofolate-cyclo-ligase
MLKAELRKKYMQKRQALSMDEAFLLSEAVFRNFIDYFNPVPGQTMHVYIPIGKFREMDTRPLIDYCLSRNVRVFVPKVEGIGMISVEITKDTVFAVNHWGISEPVSDQDAGLSDFDYIITPLLYCDNKGNRVGYGKGFYDGLFSSLSGKSKKIGINYFNPDEPIEDVWEYDIPLDYLVTPTEVVSFFNGGA
>NZ_CP022986.1|WP_100076463.1|3152872_3154249_+|rhodanese-related-sulfurtransferase
MQLYNTLSAEERAQLIDEAGKERLTLSFYAYAKIQDPKKFRDELFIAWNALDALGRIYVAHEGINAQMSVPADQFEAFRTTLEAYDFMKGIRLNVAVEQDNHSFLKLTIKVRNKIVADGLNDETFDVTNKGIHLKAKEFNELLEDPNTIVVDFRNHYESEVGHFEGAITPDVENFRESLPIINDQLQDFKEDKNLLMYCTGGIRCEKASAYFKHQGFKNVYQLEGGIIEYTRQIKEENIPSKFIGKNFVFDHRLGERITDDIIAQCHQCGKPCDNHTNCANDACHLLFIQCDECKAAMENCCSTECLETIHLPWEQQVALRKGLQVGNKVFRKGKSEALKFKHSGDLKTQTLAKATKAETKDIRQKLKVKKTLIGKAEHYYSRSKIAQFLIENSTLSVGDKVLISGPTTGDQEITVTQIFVNGNFSDMAAAGDQITFELPFRVRLSDKLYKITGTENA
>NZ_CP022986.1|WP_100076462.1|3150958_3152494_-|trypsin-like-peptidase-domain-containing-protein
MKSTLKKLLPFAVVGVLSGATTVGALQFLDHHSNTEDQSYFTKSANTSFAGMNTAAVGDDFVKAAKTTVPAVVTIKNYQSRSTSRASEQDLFDFFFGDPFGGNGRGQQRQRQQQQVPDNMPSGMGSGVIISPDGYIISNNHVVAGANKLEVVLSNKKSYIATLVGTDPNTDISLLKIEEKGLPYLNFANSDNIEVGQWVLAVGNPLGLNSTVTAGIISAKGRGIGILGSQGKAANPIESFIQTDAAINPGNSGGALVNTNGDLIGINSAIQSTTGYYQGYGFAVPSNLARKIIEDIKKFGIVQRGFLGVTSLDLSDEMQVAAYNKQKKANIKAGSGVYVTGFGESSGAEDAGLKTGDIITKVDNYPITDFSDLSVSIGSKRPGDKVMVTYMRNGKEYTTTVTLKDQKGGTSTRTKADLSVTEKIGAEFDILSDRFKTDYGLNSGVIAKNVMEGGEMAKIGIVDNYIIVEINGKPVNSQKDVEKILDRYQGNVQVKFVDEYGRIYTKGFRMP
>NZ_CP022986.1|WP_100076461.1|3150441_3150897_+|hypothetical-protein
MSFIRNTFAILVGLGIAALTITLGIRVFPQWVTFDAFAPFEHWQHFLESMQGEDAFFGFLLFISGLGTTIGGVATAIIVKYAKVAYAILIGFIMLFIAMLDVIVFPYHPTFYKISIFLTFFPFSWIGGKIVEVIYEKKKRRMLAEKIIKRQ
>NZ_CP022986.1|WP_100076460.1|3150057_3150438_+|RidA-family-protein
MKQVINTVNAPAAIGPYSQANMANGVLYISGQIPVDPSTGKLVEGIEKETHQVMKNLEAILTEAGMTFKNVVKATIFLKSMDDFAVMNDIYASYLDADSYPARETVQVSCLPKNVDIEISMIAHQD
>NZ_CP022986.1|WP_100076459.1|3147414_3150003_+|LPS-assembly-protein-LptD
MAKTVFKNILQILIILIFNNFLAQENPGKLSENAANDTIPKRDTIAVKKEALEDVLRTKADDQRRDVPKKMTFLNKNAQVKYQDMQIDADYISIDDNKNLIYARGKQDSLGKIIEPVITTQAGKKYETDQFSYNTKTRQAIAYNARTEESQGVIIANKTKKYNDSVFAMRHALYTTDEYFLKKKDTAADYHLLASNIKLVKTKQKSQIITGPIQMYIEQVPTPLIMPFAILPFSDKRSAGILIPSFGERQDVGFFLNGLGYYQPIGEHFDLKVLADIYTKGSWNLRPEMNYVKKYRYSGNFTADIGNTVRGIKGLDNYSKSSTYRIAWRHTQDTKANPFLTFSASVDIVSNKFYNNTVNNNYIFNQNVLNTQQNSTVTVTKRFLTLPVTITGTASYSQNFATGNSDLRLPQMNVAINQFYLFKSRTGVRRGLIENITVNTGFNLTNYVQTNEGELFTQAMWDKLQTGLKNNIALGTNTSFAKYFTFSLAANIDNALTTKTTRKYYDPLKNVTVNEVEKGISGYSTFSTTASVQTTLYGMLKFKKGSAIEAIRHMMTPSIGFTYSPDFGGSNFGYYRNYYDANGAQTPYSIFDGGIVGSPTSGMVGALGFNIGNNIEMKVRSKKDSTGIKKMKLFESLNLAGNYNFAAKTHPWSVLTVNGQSSFFNNKLSVNTSLSIDPYRIIYIPGQDAGIRTENFGHFSIQGFNVQMSYPLSNEIFGEKTDYSKKYKTKGEIRNENYYFDDDNYAHFEQAWTLNINANYAFTRTLASRTPNRIASVGLDGSIKLTPYWNINGSTHYDMITQQLAYTRIGFARDQRSFTINFNWVPFGQYKVYDFFIGIKANILSDALKYKDRSFTQPNAPF
>NZ_CP022986.1|WP_100076458.1|3146074_3147361_-|N-acetylmuramoyl-L-alanine-amidase
MYKQNFKIILSFLLILLSNFIFSQKKFTIVLDAGHGGSDHGANRSYNDIGRVAEKDITLAIVLKLGSMLEKNKDFKVIYTRKIDEYPSLSDRTNLANRSKADLFVSVHCNASGRSGPYGTETYVQGPDQNDTNLEVAKRENDVIYLDEKDKQTFGSYDPGSPESLIALKLQQSKYLESSLLLGGFVENNFVNKDKRFSRGVFQKNLHVLRMNAMPSVLIETGFINHPEESHYLASDRGQEEIASSIYDAIISYKKAVDRKSGGPIAVRKPEPEKPAEVPLKNDFRILLMSSPTKFNDGDPALKGLNYILEIKENGQYKYYYGVTNMASVRDINLKTAKDAGFRNAFAVGFMPNQKLSSGYYTIELHAGEKLNGNSPILLAYKNAERNKENGVFYYTYGKVYTLEDAVKLQKEIEAKGIRNTVIQKVYK
>NZ_CP022986.1|WP_100076457.1|3145341_3145596_-|30S-ribosomal-protein-S20
MANHKSALKRIRQNEVRRLRNRYYHKTARTALKALRNEEDKAVAAEQLPKVISLLDRLAKKNIIHKNKAANLKSKLTKHVNKLA
>NZ_CP022986.1|WP_100076468.1|3157253_3158024_-|RNA-methyltransferase
MLIESFQNDKIKNVTRLLTDNRFRKKSGLFTVEGQQENERAIRYAYEPTEYFICESIFNGDIPQAGKIHYVSDKVYEKIAYRGTSEGIIGVYETKELPISSLMPAEQSTVIVVEGIEKPGNLGAILRSCEAFGIDALIITDGKTDFYNPNVIRSSVGCLFGMKVFQAGNAEVLEFLQNNGFNLYTTLMDETAEDICTRDFRKRSAVLFGTEHSGLSDFWIGKGKNTLIPMAGSIDSLNLSNAVAITCYEALRQKKQ
>NZ_CP022986.1|WP_100076469.1|3158117_3159620_-|DNA-recombination-protein-RmuC
MTYLIIGCIAGGITGAIVAYFALKSSMVSRNSYDDLNSVYIKSQSDLENSQLKIQELIQNTNREKELIQQQSDLMSDLKNELAKISAEHASLHIQFQEQKQAMIKQVSQIDNLLTEKQAIFARNAELSAINESLQQSLETQKKEIAKIQDEAKLQFENLASKILEEKTEKFTLLNQNNLKTILEPFQEKINDLKNRVNEAYEKENKERFSLAEKVKELAELNQQISEDAKKLTRALKGESKTQGNWGEMILESILEKSGLTKGQEYFLEHELRDEDNKALFSEFSGKKMRPDAVVKYPDERNVIIDSKVSLTAFTELVDETDQEVYIIKLNQHLSSIKNHIQQLSQKAYDDYGKSLDFVMMFIPSEPAYIAAMQADQNLWNYAYDRRILLLNPSNLITSLKLIADLWKREYQNRNSMEIAERGAKLYDKFVGFIENLEKVGKNLDLAKNFYNDAYKQLSTGNDNLVIQTQKLKSLGIKNKKELPQSLIDSAYISGILPEE
>NZ_CP022986.1|WP_100076470.1|3159858_3160512_+|SGNH/GDSL-hydrolase-family-protein
MKFLTFTAIVFSALFSAQDFANYAKYEKQNQEIISKNITPNSVLMGDSITEGWFSTDPDFFKKNNFVGRGIGGQVTSQMLLRFREDVIKLKPKRVIILAGTNDIAENQGPISLDKVFGNIVSMAELAKANHIKVVLCSVLPAYNFGWRKDMHPAEKVITLNAMIKSYAGKNQIPYVDYHSQMKDSRNGLDKMYTEDEIHPTAKGYEKMEAILMQKIK
>NZ_CP022986.1|WP_157761432.1|3160593_3160839_-|hypothetical-protein
MKKLKLTKLSRLALKDVFGGGGDLYPALECYSSRDCSHYGEALIMCPDGTTSMTNYSCMGGHCMLNTGSCAPEIPSPVPIP
>NZ_CP022986.1|WP_100076471.1|3160976_3162155_-|nicotinate-phosphoribosyltransferase
MNEVRLNSILDNDFYKITMQNAVVKLFPGSIVKYEFINRGKHQFPEGFDHALREAVNKMAELKLTKEEKKYMARTCPYIDLPYLDFLEGYHYDPSEVKIHQEGSELSVVVEGLWYRTILWEVPLLALISELHYEMNHMERDSNEVVMHKTIEKADSLARLGVTFAEFGTRRRHSYKVQNLVMEALTQKKESTFIGSSNVHFAMKYGVKPIGTHAHEWFMFHAAEYGFKTANDLALEHWVDVYRGDLGVALSDTYTTDVFFQQFDKKFAKLFDGVRHDSGDPLEFADKTIAHYQKHGINPLFKYIIFSDALNLEKVEEITNYCRGKIGISFGIGTNLTNDVGLKPMNIVMKLIGVQAPNLEWIPTVKLSDEHGKYTGDPKMIELAKEFLRIKD
>NZ_CP022986.1|WP_100076472.1|3162247_3162724_-|DNA-starvation/stationary-phase-protection-protein
MKNASIIGLNEADCQQIAEKLNVLLANYSVFYQNTRGSHWNIKGDQFFTLHPKFEELYNSLVLKIDEIAERILTLGAVPAHNYSDYLKVSTIQESTDVSDATVSVQNILNSFKVVIDLQRELLDITEKAGDEGTNSQMSDYITEQEKEVWMYNSYLGK
>NZ_CP022986.1|WP_002983146.1|3163220_3163634_+|30S-ribosomal-protein-S12
MPTIQQLVRKGRATLAKKSKSAALDSCPQRRGVCTRVYTTTPKKPNSALRKVARVRLSNGKEVNAYIPGEGHNLQEHSIVLVRGGRVKDLPGVRYHIVRGALDTAGVNGRTQRRSKYGAKRPKPGQAAAAPAKGKKK
>NZ_CP022986.1|WP_100076473.1|3163657_3164134_+|30S-ribosomal-protein-S7
MRKTKAKKRPLLPDPQFNDQLVTRFVNNLMLDGKKSIAFKIFYDALEIVENKKGENEKSSLEIWKDALTNVMPHVEVRSRRVGGANFQIPMPIRADRKISMAMKWLIKYARARNDKSMALKLSNEILAASREEGAAYKKKSDTHKMAEANKAFSHFKF
>NZ_CP022986.1|WP_100076474.1|3164140_3166258_+|elongation-factor-G
MGRDLKYTRNIGIAAHIDAGKTTTTERILFYTGVNHKIGEVHDGASTMDWMEQEAERGITITSAATTCSWNFPTDQGKPVAETKPYHFNIIDTPGHVDFTVEVNRSLRVLDGLVFLFSAVDGVEPQSETNWRLADNYKVARMGFVNKMDRQGADFLNVVKQVKEMLGSNAVPIVLPIGAEEDFKGVVDLIKNRAIIWDEAGQGATFEVVPIPEDMKAEVLEYREKLVEAVADYDETLMEKFFEDPDSISEEEINEALRKATIDLSIIPMTCGSSFKNKGVQFMLDAVCKYLPSPLDKDDIKGTDPRTDAEITRKPSVDEPFSALAFKIATDPFVGRLAFFRAYSGRLDAGSYILNTRSGDKERISRIYQMHANKQNPVEYIEAGDIGAAVGFKSIKTGDTMCDEKNPIVLESMVFPDPVIGIAVEPKTKADQDKMGNALAKLAEEDPTFTVRTDEASGQTIISGMGELHLDIIVDRMKREFKVEVNQGQPQVEYKENLTKVAQHREVYKKQSGGKGKFADIVFELGPAEEGKVGLEFINEIKGGNVPREFVPAIEKGFKAAMKNGPLAGFEVEGIKVVLKDGSFHAVDSDALSFEMAAKLGFKEAGRAAKPVIMEPIMKLEVVTPEEYMGNIIGDLNKRRGTISGQEEKNGAVVIKGSVPLSEMFGYVTTLRTLSSGRATSSMELEKYQATPQNVAEDIIAKAKG
>NZ_CP022986.1|WP_002661363.1|3166276_3166582_+|30S-ribosomal-protein-S10
MSQRIRIKLKSYDYNLVDKSAEKIVKTVKATGAVVNGPIPLPTNKRIFTVLRSPHVNKKAREQFQLSAHKRLMDIYSSSSKTVDALMKLELPSGVDVEIKV

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Crispr_ID: NZ_CP022986_4

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP022986_4

3215725-3215871

Orphan

Consensus_repeat	Method
TCAATCCGTTGCGCTGTCAATTTTATACTGGAAAGATTCACAATTGACTTG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP022986_4

>merge|NZ_CP022986|4|3215725-3215871|CRISPRCasFinder
TCAATCCGTTGCGCTGTCAATTTTATACTGGAAAGATTCACAATTGACTTGCGGAGCAAAATTCACGGTTGACTGAGGTTGTGAATGAGTCAATGATCAATCCGTTGCGCTGTCAATTTTATACTGGAAAGATTCACGATTGACTTG

>NZ_CP022986|4|4|3215725-3215871|CRISPRCasFinder
TCAATCCGTTGCGCTGTCAATTTTATACTGGAAAGATTCACAATTGACTTG	CGGAGCAAAATTCACGGTTGACTGAGGTTGTGAATGAGTCAATGA
TCAATCCGTTGCGCTGTCAATTTTATACTGGAAAGATTCACGATTGACTTG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP022986.1\|WP_100076523.1\|3214400_3215372_+\|glycosyl-transferase	unknown	unknown	gnl\|CDD\|273203
NZ_CP022986.1\|WP_100076527.1\|3217739_3218702_+\|DUF4013-domain-containing-protein	unknown	unknown	unknown
NZ_CP022986.1\|WP_100076521.1\|3212779_3213520_+\|YebC/PmpR-family-DNA-binding-transcriptional-regulator	unknown	unknown	gnl\|CDD\|237084
NZ_CP022986.1\|WP_100076520.1\|3211201_3212686_+\|OmpA-family-protein	unknown	unknown	gnl\|CDD\|143586
NZ_CP022986.1\|WP_100076529.1\|3219508_3220669_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022986.1\|WP_100076518.1\|3208919_3210542_-\|ATP-binding-cassette-domain-containing-protein	unknown	unknown	gnl\|CDD\|237894
NZ_CP022986.1\|WP_100076531.1\|3221902_3223225_+\|DUF58-domain-containing-protein	unknown	unknown	gnl\|CDD\|224635
NZ_CP022986.1\|WP_100076525.1\|3215995_3216745_-\|RDD-family-protein	unknown	unknown	gnl\|CDD\|377640
NZ_CP022986.1\|WP_100076526.1\|3216772_3217756_+\|stage-II-sporulation-protein-M	unknown	unknown	gnl\|CDD\|376676
NZ_CP022986.1\|WP_100076533.1\|3223778_3225476_-\|T9SS-type-A-sorting-domain-containing-protein	unknown	unknown	gnl\|CDD\|275036
NZ_CP022986.1\|WP_100076522.1\|3213576_3214404_+\|UDP-2,3-diacylglucosamine-diphosphatase	unknown	unknown	gnl\|CDD\|277343
NZ_CP022986.1\|WP_100076534.1\|3225678_3228294_-\|glucosidase	unknown	unknown	gnl\|CDD\|367389
NZ_CP022986.1\|WP_100077610.1\|3207430_3208783_-\|alpha-glucosidase-C-terminal-domain-containing-protein	unknown	unknown	gnl\|CDD\|200452
NZ_CP022986.1\|WP_100076524.1\|3215360_3215651_-\|N-acetyltransferase	unknown	unknown	gnl\|CDD\|225261
NZ_CP022986.1\|WP_100076519.1\|3210665_3211124_+\|SsrA-binding-protein-SmpB	unknown	unknown	gnl\|CDD\|376590
NZ_CP022986.1\|WP_100077609.1\|3204803_3205388_-\|nicotinate-nucleotide-adenylyltransferase	unknown	unknown	gnl\|CDD\|234611
NZ_CP022986.1\|WP_100076517.1\|3205495_3207208_-\|single-stranded-DNA-specific-exonuclease-RecJ	unknown	unknown	gnl\|CDD\|273193
NZ_CP022986.1\|WP_100076528.1\|3218694_3219492_+\|DUF4129-domain-containing-protein	unknown	unknown	unknown
NZ_CP022986.1\|WP_100076530.1\|3220749_3221781_+\|MoxR-family-ATPase	unknown	unknown	gnl\|CDD\|223786
NZ_CP022986.1\|WP_100076532.1\|3223284_3223704_+\|OsmC-family-protein	unknown	unknown	gnl\|CDD\|224679

Protein	Function_ID	Function_description	E-value
NZ_CP022986.1\|WP_100076523.1\|3214400_3215372_+\|glycosyl-transferase	gnl\|CDD\|273203	TIGR00661, conserved_hypothetical_protein, conserved hypothetical protein. This model represents nearly the full length of MJ1255 from Methanococcus jannaschii and of an unpublished protein from Vibrio cholerae, as well as the C-terminal half of a protein from Methanobacterium thermoautotrophicum. A small region (~50 amino acids) within the domain appears related to a family of sugar transferases. [Hypothetical proteins, Conserved].	1.06379e-44
NZ_CP022986.1\|WP_100076534.1\|3225678_3228294_-\|glucosidase	gnl\|CDD\|367389	pfam03200, Glyco_hydro_63, Glycosyl hydrolase family 63 C-terminal domain. This is a family of eukaryotic enzymes belonging to glycosyl hydrolase family 63. They catalyze the specific cleavage of the non-reducing terminal glucose residue from Glc(3)Man(9)GlcNAc(2). Mannosyl oligosaccharide glucosidase EC:3.2.1.106 is the first enzyme in the N-linked oligosaccharide processing pathway. This family represents the C-terminal catalytic domain.	2.11319e-09
NZ_CP022986.1\|WP_100076521.1\|3212779_3213520_+\|YebC/PmpR-family-DNA-binding-transcriptional-regulator	gnl\|CDD\|237084	PRK12378, PRK12378, YebC/PmpR family DNA-binding transcriptional regulator.	2.15886e-110
NZ_CP022986.1\|WP_100076520.1\|3211201_3212686_+\|OmpA-family-protein	gnl\|CDD\|143586	cd07185, OmpA_C-like, Peptidoglycan binding domains similar to the C-terminal domain of outer-membrane protein OmpA. OmpA-like domains (named after the C-terminal domain of Escherichia coli OmpA protein) have been shown to non-covalently associate with peptidoglycan, a network of glycan chains composed of disaccharides, which are crosslinked via short peptide bridges. Well-studied members of this family include the Escherichia coli outer membrane protein OmpA, the Escherichia coli lipoprotein PAL, Neisseria meningitdis RmpM, which interact with the outer membrane, as well as the Escherichia coli motor protein MotB, and the Vibrio flagellar motor proteins PomB and MotY, which interact with the inner membrane.	1.0283e-28
NZ_CP022986.1\|WP_100076518.1\|3208919_3210542_-\|ATP-binding-cassette-domain-containing-protein	gnl\|CDD\|237894	PRK15064, PRK15064, ABC transporter ATP-binding protein; Provisional.	0
NZ_CP022986.1\|WP_100076531.1\|3221902_3223225_+\|DUF58-domain-containing-protein	gnl\|CDD\|224635	COG1721, COG1721, Uncharacterized conserved protein (some members contain a von Willebrand factor type A (vWA) domain) [General function prediction only].	1.09586e-60
NZ_CP022986.1\|WP_100076525.1\|3215995_3216745_-\|RDD-family-protein	gnl\|CDD\|377640	pfam06271, RDD, RDD family. This family of proteins contain three highly conserved amino acids: one arginine and two aspartates, hence the name of RDD family. This region contains two predicted transmembrane regions. The arginine occurs at the N-terminus of the first helix and the first aspartate occurs in the middle of this helix. The molecular function of this region is unknown. However this region may be involved in transport of an as yet unknown set of ligands (Bateman A pers. obs.).	9.86478e-20
NZ_CP022986.1\|WP_100076526.1\|3216772_3217756_+\|stage-II-sporulation-protein-M	gnl\|CDD\|376676	pfam01944, SpoIIM, Stage II sporulation protein M. SpoIIM is on e of four stage II sporulation proteins that is necessary for the forespore inside the mother-cell to be properly internalized through the breakdown of peptidoglycans trapped between the membranes of the septum separating the forespore and the mother-cell. The four proteins working in sequence are SpoIIB, pfam05036, SpoIIM, SpoIIP, pfam07454, and finally SpoIID, pfam08486. D, M and P are in a complex with each other and the complex assembles in a hierarchical manner such that M, which serves as a membrane anchor, recruits P to the septum and P, in turn, recruits D to the septum.	6.74807e-25
NZ_CP022986.1\|WP_100076533.1\|3223778_3225476_-\|T9SS-type-A-sorting-domain-containing-protein	gnl\|CDD\|275036	TIGR04183, hypothetical_protein, Por secretion system C-terminal sorting domain. Species that include Porphyromonas gingivalis, Fibrobacter succinogenes, Flavobacterium johnsoniae, Cytophaga hutchinsonii, Gramella forsetii, Prevotella intermedia, and Salinibacter ruber average twenty or more copies of a C-terminal domain, represented by this model, associated with sorting to the outer membrane and covalent modification.	1.78016e-06
NZ_CP022986.1\|WP_100076522.1\|3213576_3214404_+\|UDP-2,3-diacylglucosamine-diphosphatase	gnl\|CDD\|277343	cd07398, MPP_YbbF-LpxH, Escherichia coli YbbF/LpxH and related proteins, metallophosphatase domain. YbbF/LpxH is an Escherichia coli UDP-2,3-diacylglucosamine hydrolase thought to catalyze the fourth step of lipid A biosynthesis, in which a precursor UDP-2,3-diacylglucosamine is hydrolyzed to yield 2,3-diacylglucosamine 1-phosphate and UMP. YbbF belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.	4.53839e-51
NZ_CP022986.1\|WP_100077610.1\|3207430_3208783_-\|alpha-glucosidase-C-terminal-domain-containing-protein	gnl\|CDD\|200452	cd11313, AmyAc_arch_bac_AmyA, Alpha amylase catalytic domain found in archaeal and bacterial Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes firmicutes, bacteroidetes, and proteobacteria. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.	1.88013e-175
NZ_CP022986.1\|WP_100076524.1\|3215360_3215651_-\|N-acetyltransferase	gnl\|CDD\|225261	COG2388, COG2388, Predicted acetyltransferase [General function prediction only].	9.0403e-16
NZ_CP022986.1\|WP_100076519.1\|3210665_3211124_+\|SsrA-binding-protein-SmpB	gnl\|CDD\|376590	pfam01668, SmpB, SmpB protein.	1.7267e-71
NZ_CP022986.1\|WP_100077609.1\|3204803_3205388_-\|nicotinate-nucleotide-adenylyltransferase	gnl\|CDD\|234611	PRK00071, nadD, nicotinate-nucleotide adenylyltransferase.	3.70913e-79
NZ_CP022986.1\|WP_100076517.1\|3205495_3207208_-\|single-stranded-DNA-specific-exonuclease-RecJ	gnl\|CDD\|273193	TIGR00644, recJ, single-stranded-DNA-specific exonuclease RecJ. All proteins in this family are 5'-3' single-strand DNA exonucleases. These proteins are used in some aspects of mismatch repair, recombination, and recombinational repair. [DNA metabolism, DNA replication, recombination, and repair].	3.82114e-164
NZ_CP022986.1\|WP_100076530.1\|3220749_3221781_+\|MoxR-family-ATPase	gnl\|CDD\|223786	COG0714, COG0714, MoxR-like ATPases [General function prediction only].	3.05081e-100
NZ_CP022986.1\|WP_100076532.1\|3223284_3223704_+\|OsmC-family-protein	gnl\|CDD\|224679	COG1765, COG1765, Predicted redox protein, regulator of disulfide bond formation [Posttranslational modification, protein turnover, chaperones].	3.2688e-26

>NZ_CP022986.1|WP_100076524.1|3215360_3215651_-|N-acetyltransferase
MRTENNKSGNGGVITLNNDIKEVGRLTYTVFPEQNRLVISFVLVHPEFEGRGMGKFLVEEAIKFARENQWKVYPHCSYARAVMKRMHDVEDVFLSA
>NZ_CP022986.1|WP_100076523.1|3214400_3215372_+|glycosyl-transferase
MKILYAFQGTGNGHMARAQEIVPILKKYASVDTLISGHQSQLKADFEITFQYSGISLLYNKSGGLSYFKTLTGNNFLEAARVIRSLDLSGYDLIINDFEPLTSWICKLKGFPMVGLSHQASMSFKETPKPRKKDFFGELVLQYYAPFRKRIGFHFESYHADIKKPVIRKKIRNLQPDKKGYYLVYLPSYSDENIIGILKDIPAQWKVFSRYAPQAFTIGNIDVFPIDEQQYLKYFESCNGILCNAGFETPAEALFMDKKLFVIPIHNQYEQECNACALDKMGIPNSKVLKEQEIRDWVASDFHYQVDYPDNIEEILLQEVLGR
>NZ_CP022986.1|WP_100076522.1|3213576_3214404_+|UDP-2,3-diacylglucosamine-diphosphatase
MKRNVELVVISDVHLGTYGCKAKELLRYLNSIQPGTLILNGDIIDIWQFKKSYFPKPHLKVIKKILSLATKSTDVYYITGNHDEMFRKFTDFELGKLKVCNKLCLTINHKKTWIFHGDVFDASVQHSKWIAKLGGKGYDLLIVINNVVNWFLERMGREKYSFSKKIKNNVKKAVKYIGDFELTASELAIDNHYDYVICGHIHQPQMREVVNKKGSCVYLNSGDWIENLSALEYHNGEWNIFHYEEHKHLLKDDVHDEIQDINSAELMKIVTSFSS
>NZ_CP022986.1|WP_100076521.1|3212779_3213520_+|YebC/PmpR-family-DNA-binding-transcriptional-regulator
MGRAFEYRKASKMARWDKMAKTFSKIGKDIALAVKAGGPDPESNPALRRCIQNAKGANMPKDNVERAIKKASGADAENYEEVTYEGYGQGGVAFFVECTTNNTTRTVANVRAVFNKFDGNLGKNGELAFIFDRKGIFTIDLAQIKMDWDEFEMEMIDGGAEDVEKDEEEVMITTAFEDFGSLSHKLDELGIEAKSAELQRIPNITKEVTEEQFRANMKMLERFEEDDDVQNVYHNMEITEDMMSAL
>NZ_CP022986.1|WP_100076520.1|3211201_3212686_+|OmpA-family-protein
MKNLKLGISALALTVASTVFAQTTNNPWLIGVGAHAENHMAQRNNFSNTFSANNLTKTMFNVNNFSITPPLSKLTVARNVAKGFVVDWQTSVGNVENKRFNMGKEFFLMTGLGLQAKAAGILWNEESWFDPYLRVGANYLRHDYTSLTFPRMDANGYMVPNGDNGNENGKANFFTVSTGAGANFWVTKNFGLGIQGDYVSTPGDKSNVANFWQASASLLFRFGNRDRDKDGILDKDDLCPDTPGLPEFQGCPDTDGDGVPDKDDQCPDVAGPVENNGCPWPDTDGDGVIDKDDACPTVAGPAENNGCPWPDTDGDGILDKDDACPTVPGLPEYNGCPKPKSVSATEIEENFRSVYFDFNKATIKPESKPALDKAAEIIKKDGGHYLLEGRTDAKGSEVYNLKLSRQRAASVVAALDARGVDPNALKSVGVGKAKATVPATASDAERQADRKVVVTAIEDDAQWNTMQKKDYEDEPVKKAPAKKTTKKKVVKKRK
>NZ_CP022986.1|WP_100076519.1|3210665_3211124_+|SsrA-binding-protein-SmpB
MKIEKTVSIVNRRARFEYEILEEMEAGMVLTGTEIKSLRSSKASIAESFCQFIDGELYIINMMIDEYKLGTFYNHKTKRERKLLLHKKELQKLEKKLKDAGNTIIPLKLYINDRGKAKVLIALGRGKKLYDKRESIKDRENKRNLDRVLKKS
>NZ_CP022986.1|WP_100076518.1|3208919_3210542_-|ATP-binding-cassette-domain-containing-protein
MLTVSNLSLQFGKRVLFDEVNIMFTKGNCYGIIGANGAGKSTFLKILTGKQDPTTGHVSLEPGKRMSVLEQDHFAYDQYNVLEAVLRGNKKLFEIKEEMDALYAKEDFSDEDGIKAGELGVIYDEMGGWTAESDAQTMLSNVGIKDDMHWQMMNELENKDKVKVLLAQALFGNPDVLILDEPTNDLDIETISWLEDFLADYENTVIVVSHDRHFLDTVCTHIGDLDYAKLNLYTGNYSFWYQASQLATKQRAQANKKAEEKKKELQDFIARFSSNVAKAKQATARKKMIDKLNIDDIKPTSRRYPAIIFEMEREAGDQILDVKGLEKTKDGELLFSNIDLNLKKGDKVAVLSKNSLAITEFFEILAGNVAADKGNVAWGVTTTQSHMPLDNTHFFQEDLSLVDWLRQFTKNDEERHEEFMRGFLGRMLFSGDEALKSCKVLSGGEKMRCMFSRMMLQKANVLLLDEPTNHLDLESITTLNNSLSNFKGNLLLASHDHEMLSTVCNRIIELTPKGIIDREMTYDEYLADKKVKELKEKMYS
>NZ_CP022986.1|WP_100077610.1|3207430_3208783_-|alpha-glucosidase-C-terminal-domain-containing-protein
MFTVFSGGVHAQENDVRYQPKPYIEITHPEWSKNATIYEVNIRQYTQEGTFKAFEKHLPRLKKMGIDIIWLMPIHPIGKLNRKGTLGSYYSVKDFKGINPDFGTLNDFKNLVRKIHSMGMHVIIDWVGNHSAWDNPLTREHPDWYTKTREGNFQPTPWYDWDDVIDFDYNKPAFRRYMTEALKYWVSETDIDGYRCDVAGFIPVDFWENARTELDQLKPVFMLAEWESRDLYKKSFDMTYSWTLWDKMKQATIEKKGAPALFEYMAHDVNSFPYDSYRMTFTDNHDKNSWEGNQFSNFGDGLEAAMVFCSTVNGMPLVYSGQEAGLDRSLAFFEKDPMVWKEHRFAGIYETLFKLKHSNQALWNGHWGGEMERVHNDNMNNVLSFYREKNGDAVMTVINFSGQDAKVNLDTKYFKNKYRELFSGTPYVMSGNQTPMTLKPWEYRVLVKTK
>NZ_CP022986.1|WP_100076517.1|3205495_3207208_-|single-stranded-DNA-specific-exonuclease-RecJ
MSQKWIYKPEPDEEIVDGLSSSLGFGTFESKLLVLRGIDNYQKAREFFKPNLTDIHNPFLMADMQKAVERIATAIENGEKILIYGDYDVDGTTAVALVYLYLSKIVQKKYLDYYIPDRNSEGYGISTEGIDFARDNGFSLIIALDCGIKAIDMINYAKESGIDFIICDHHLPGEEIPDAVAVLDPKRTDCRYPFKELSGCGVGFKLCQGLNTIYRIPEAELFELTDLLAISIAADIVSMTGENRVLAKMGLKTLRKTRNLGLRLLIPDDKLSHFEISNIVFEIAPKINAAGRISHGKAAVELMVSDNLKHAHQIVSDIMDLNDERRELDMNSTLSALNQIIESQQESRLTTIVYHPEWNKGVIGIVASRLIETYYRPTLVFTDGNNGEMVASARSVADFDVHEALDLCSEYFLKFGGHHAAAGLSMEKEKFEAFKEKFERIVSEKIKDHQKEPSITIDSEIHIDEINREFINFHRKLAPFGPHNMKPILALTRQRVSGYIKTMGKDNNHLKFYIRQESTGRNIECVGFKLGQFADDFRTKSFDLVFTLEENHWKGNVTHYLNIKDVRFRN
>NZ_CP022986.1|WP_100077609.1|3204803_3205388_-|nicotinate-nucleotide-adenylyltransferase
MKKIGLFFGSFNPIHIGHLILANYILENSDMDELWFVVSPQNPFKDKKTLLSDHNRLDMVQLAVKNYPNMRASNIEFSLPKPSYTVDTLTYLHEKYPDHSFSLIMGEDNLSSLHKWKNADRLVESHHIIVYPRLSEGPKADSPYSNHSNISLVKAPVIELSATEIRAMIREGKNVRPMLPPEVFEYLDGSSFYK
>NZ_CP022986.1|WP_100076525.1|3215995_3216745_-|RDD-family-protein
MSQIAINTSQNVNINFSIASVGERMLAFIIDLLIKVAYIIVILYVFFGFLGLGRLLSGMDRWSVIAVYIALTFPVYIYPVVLESLMEGQTPGKKLMKIRVVKIDGYQASFGDYMIRWVFRLIDTSFAGVIGLISMIVSKDNKRLGDMAAGTAVISLKNNINISHTILENLKEDYLPSFPQVIALSDNDMRIIKDNFLKAVRTDDRQVINRLSEKIKSILKLDIDHSKMTERQFINVIIKDYNYYTGKDS
>NZ_CP022986.1|WP_100076526.1|3216772_3217756_+|stage-II-sporulation-protein-M
MREVYFIKQNKEKWLGIEQVIQGKVKKNPDDLSSLYINLINDLSFAQTYYPKSNTTVYLNHLSSQIFQKIYKTRRIEQNRITYFFGTEVPLLVYEYRRYLLYAFLFFILFTLIGVVSSIYDKDFVNIILGEGYVNETIENIKKGNAVGVYQSGSTWGSTIGIIFNNIGVGAKLYIYGIFAGIGTLYHLLSNSVMLGSFQYFFYDYGALKDSARGIWLHGVFEIFSMVVEAMCGLILGASILFPKTFSRFQSFKNGFRDSFKIFLSTVPFTVCAGIIEGYVTRHALKMPLVLNLIIIFGSLAVIGFYYFVYPSIVNKKINHYIHDAVV
>NZ_CP022986.1|WP_100076527.1|3217739_3218702_+|DUF4013-domain-containing-protein
MMQLYKKRDFGSFISDTFSFFKQYGRNYFRNYMLLNGLLLILMVVVIVFGFREFFGVLFGSNISGQSYYFEEYFQNNLAVFIVIGIFLALLSTALMTINFLFPVFYMKRVSQGQEKIGTDDLMTDFKTNIKKVMILYAGLNFLVMPVALVIFMISYALILIFIGLILLLFIVPTLVNVINFLCFDYFNSNKGFFESLSYAVRSQFSYRNGRESSPYWKYWGATLIMAIICQVIISIFTAIPMVIFFIKLTTTASNADFEQNPAENGLGIIFFVIYGISMLMSLLLMNMQYVNSGLMYYDSRTDLHQKTELAEIETIGTHE
>NZ_CP022986.1|WP_100076528.1|3218694_3219492_+|DUF4129-domain-containing-protein
MNKVLICLLVYCFSGYISAQERDSMPPPAEAYVDSMSTGHYKNMNLADSVLAKNPVTENTLYPKKFRANLQQRYKGGEFDYSTTKPRESFWQKLMNKIYRILQGIFGQKVFSGSANIAGILIRLFAIILVGLLLYFIIRYILVKNGGFFFSRKNRRIQINQEELHENIHEINFPKSIADFEAAGDFRSAIRYQFLFALKKLSDKKLIVWNPEKTNKDYVSELKAPHIKSDFSALSYVFDYVWYGEFSIDQDSYMKFRQQYQSFNP
>NZ_CP022986.1|WP_100076529.1|3219508_3220669_+|hypothetical-protein
MNKTFKIYAYIFIIIMVILALFEVNKKETTDWRKNFDVNKKSPFGLFVFGKEAKGLFGNDLKKIEETPYDYYNEHTKGGHNILVIEKSIDAESWKAILDQVSAGADAMLIVSEMPKEISDSIGFYDSQLSFEEQNVLKLTDKGYQNDFIKLDKFPSGKGFTYIKPGVEVLGKTVEKNNSDQVNFIKAKFGKGTVYVHCEPLFLTNYYLLKRGNTKYAEDVLSYLKDRETVWFIESSAGGKSQFFMRFILSNPALKYAWWVFLGGMLLFILFNAKRKQRIVPVIETLKNTSVDFIRSIGNLYLQEGDFHDMMGKKAQYFLNRVRMDLLIDTQHLDEEFIKKLQLKTGKPIEMIQEAVALIKKAQDPYAAVMNEDLGKMNALLDKILK
>NZ_CP022986.1|WP_100076530.1|3220749_3221781_+|MoxR-family-ATPase
MDNIENLNPESGQPALPDNNENQFETRIDMIELRASLEKVKHEISKVIVGQESMIEHLLAALLSNGHVLIEGVPGVAKTITAKLLAKTIDVGFSRIQFTPDLMPSDILGTSVFNVKTSEFEFKQGPVFSNFILIDEINRSPAKTQAALFEVMEERQITMDGTRYPMEEPFLVVATQNPIEHEGTYRLPEAQLDRFLFKINVSYPDLQQEIEIIRNQHENRAEDKTEAVNRVISAGQLKNYQKLVKEIIVESQLIEYIAKITVNTRENQFLYLGASPRASLALLTASKAFAALRGRDFVTPEDIKEASYAVLRHRVIVSPEREMEGLTADEIIRQILEGIEIPR
>NZ_CP022986.1|WP_100076531.1|3221902_3223225_+|DUF58-domain-containing-protein
MKNLYINTRFFFALIGVGILYVFAFFFPFLMWVAHILLLLCFFTAMVEYLLLFNAKNGISAQRILPEKLSNGDENPVKVDIRNNYDFTLNVRVIDEIPFQFQKRDFLIEKQIEPGRNTYFQYILEPKERGEYSFGNLNIYASSPVGFISKRFTFQKDALLPAYPSFIHLRKYELMALQSEFLLGGIKRIRKLGHTMEFEQIKEYVPGDDIRTINWKATSKTNRLMVNQFQDEKSQRIFMLIDTGRTMKMPFKGLSLLDYSINATMALSHIILKKGDRAGMMTFSKKTENKIAADNKSGQLRKISEALYNIKTDFFESDFSRLYQDVKYTLNQRSLILLFTNFETLDGLNRQMKYLRGIARNHLLVVVFFKNAELQTLLNGNPENMQEIYDEIVAEKFEFEKKLIIQELRKYGIYTVYTLPENLNVDVINKYLEIKARGIL
>NZ_CP022986.1|WP_100076532.1|3223284_3223704_+|OsmC-family-protein
MKITLNRINDEYLFQCINAQGNSILLDNTTQPGAKGVSPMESMLMAVAGCSGIDVVSILKKQRQEITGFSAEVEGERVVVDDAKPFKSIMVKFMLEGIIDPKKAFKAAELSFEKYCSVSKTLEPNVEISYEVFVNGEKV
>NZ_CP022986.1|WP_100076533.1|3223778_3225476_-|T9SS-type-A-sorting-domain-containing-protein
MKGKLFPIAGIALLSLAFTSAQAQQYQTVPLSGFNADVIANGVGSSATSTNSDVDGVNYAFVSKDFQLTASSATLTYGLPTNGLINSAAASPAGLNYQLASYSGNNSLRLLNIGDNGTLTFTTPKAAVNLYMLATSGSGDSQVDVVVNFSDATIQTFSGIDISDWYGGSNFAIQGIGRIKKTTDGLEADTSNPRLYQIPLAISAANQSKTIQSVKVTKVNPQPSGTTVGNIPNIFAFSADVYNSCPTPTNVTSTTTTGGATINWTAPSSAPASGYQYYMSTSATAPTAATAPTGSTAAGVTSVTLNSLTTGQTYYFWVRSNCGSTQSYWTMTQFTPGQVSATYTAGDISTLFASAASITTTSTTTCPGTLTISIPSGYKIKSTDVSYKMSTVSNGYMEEQRSILACTTNNTTEASITSGSGGSTGTYSYNRTGLTMANNLTGNVTFELRAWRTYGSSGCTVTHNKVDNNTFKITVTLEPLQLATSEVKASAKELIAYPNPFVDAVTIEKANDVRAATITDLSGITVRTIEKPASTVHLGDLKTGVYILTLTMKDGSVKSSKMIKK
>NZ_CP022986.1|WP_100076534.1|3225678_3228294_-|glucosidase
MIAEKQRLEDSKWKNWGPYVSNRQWGNVREDYSPNGNAWHFANHNNAESYAYRWGEEGIAGISDTKQLLSFALSFWNKKDKMVKERFFGLSNPQGNHGEDIKEIFYYLDNTPTHSYMKMVYKYPINEFPYDDILTENARRNKKQPEYEIFDTGVFDQDEYFDIFIEYCKADHHDILVRVTVCNRSDRDAPIIVIPTAWFRNNWKWGYNDYKGQLTASHEGCIDVHHDSIDIKKIYSKNINAESVFCENETNTPKLQDVPASEKAYYKDGINNYIIHKTPTVNPEKRGSKASFLVHETISAGGSRTFDFRLSPEELDDPFRDFDEVFAARMAEADEFYQEIQHDTADEDERNVQRQAFAGLLWNKQFYHYNVGKWLKGDPNYDAPRDFTNYVRNTEWNHLHNKDIISMPDKWEYPWYATWDLAFHCVPYALIDAEFAKGQLLLLTKEWYMHPNGQLPAYEWNLSDVNPPVHAWSCFRVFKIDEKQNGKPDLLFLEKVFQKLLLNFTWWVNRKDKNGKNIFGGGFLGLDNIGAFDRNMILKDGQHLEQADGTSWMAMYALNMMRIAMELAQYYKVYEDMAIKFFEHYLYIAEAMENLGDGTKGLWNEEDGFFYDVLQLGNGEGVSLKLRSIVGLIPLFAVEIIEHKLLENMPNFRERMDWVLKNKPELTKLVSHWDEEGQGRKHLMSILRKNRLTKVLNRMLDEKEFLSTYGIRAMSKIYEEKPFIFSVHGTENVVHYTPAESDSRMFGGNSNWRGPIWFPINFLIVESLQRFHYYYGSSLKVELPTGSGDQKDLDEVAQDISNRLCSIFLKDGNGQRPFNGGNTKFNYDEHFKDYIMFFEYFHGDNGRGVGASHQTGWTATVAKLMKPKLSI

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Crispr_ID: NZ_CP022986_5

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP022986_5

3928177-3928276

Orphan

Consensus_repeat	Method
GTGAATTCCTTCGGGTGAATGGT	CRISPRCasFinder

1 spacers

WYL

The CRISPR arrays of NZ_CP022986_5

>merge|NZ_CP022986|5|3928177-3928276|CRISPRCasFinder
GTGAATTCCTTCGGGTGAATGGTATTTACCGGTAATTGACTTGCTACGCAAAATTGACGATTGACAGATGGTCAATTGTGAATTCCTTCGGGTCAATGGT

>NZ_CP022986|5|5|3928177-3928276|CRISPRCasFinder
GTGAATTCCTTCGGGTGAATGGT	ATTTACCGGTAATTGACTTGCTACGCAAAATTGACGATTGACAGATGGTCAATT
GTGAATTCCTTCGGGTCAATGGT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP022986.1\|WP_100077086.1\|3925286_3925913_+\|YceI-family-protein	unknown	unknown	gnl\|CDD\|377274
NZ_CP022986.1\|WP_100077655.1\|3931505_3933788_-\|cation:proton-antiporter	unknown	unknown	gnl\|CDD\|215608
NZ_CP022986.1\|WP_100077089.1\|3928553_3929972_+\|L-serine-ammonia-lyase	unknown	unknown	gnl\|CDD\|273233
NZ_CP022986.1\|WP_100077654.1\|3918587_3919607_+\|WYL-domain-containing-protein	WYL	pfam13280_WYL_CAS-I:CAS-III	gnl\|CDD\|379100
NZ_CP022986.1\|WP_100077096.1\|3936318_3937512_-\|alanine-dehydrogenase	unknown	unknown	gnl\|CDD\|240630
NZ_CP022986.1\|WP_100077090.1\|3929987_3930371_-\|nuclear-transport-factor-2-family-protein	unknown	unknown	gnl\|CDD\|378915
NZ_CP022986.1\|WP_100077083.1\|3922775_3923339_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022986.1\|WP_100077653.1\|3918005_3918338_+\|HopJ-type-III-effector-protein	unknown	unknown	gnl\|CDD\|378082
NZ_CP022986.1\|WP_100077095.1\|3935947_3936319_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022986.1\|WP_100077091.1\|3930394_3931240_-\|prephenate-dehydrogenase	unknown	unknown	gnl\|CDD\|181452
NZ_CP022986.1\|WP_100077085.1\|3924641_3925208_+\|YceI-family-protein	unknown	unknown	gnl\|CDD\|377274
NZ_CP022986.1\|WP_100077094.1\|3935149_3935920_-\|histidine-kinase	unknown	unknown	gnl\|CDD\|225814
NZ_CP022986.1\|WP_100077087.1\|3925985_3926630_+\|alpha/beta-hydrolase	unknown	unknown	unknown
NZ_CP022986.1\|WP_100077081.1\|3919960_3921145_-\|DUF1501-domain-containing-protein	unknown	unknown	gnl\|CDD\|226587
NZ_CP022986.1\|WP_100077082.1\|3921165_3922551_-\|DUF1800-domain-containing-protein	unknown	unknown	gnl\|CDD\|378055
NZ_CP022986.1\|WP_100077092.1\|3933894_3934284_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022986.1\|WP_100077084.1\|3923452_3924499_+\|glucokinase	unknown	unknown	gnl\|CDD\|367143
NZ_CP022986.1\|WP_100077097.1\|3937581_3937989_-\|tRNA-(adenosine(37)-N6)-threonylcarbamoyltransferase-complex-ATPase-subunit-type-1-TsaE	unknown	unknown	gnl\|CDD\|376771
NZ_CP022986.1\|WP_100077093.1\|3934461_3935172_-\|response-regulator-transcription-factor	unknown	unknown	gnl\|CDD\|381087
NZ_CP022986.1\|WP_100077088.1\|3926730_3928074_+\|ammonium-transporter	unknown	unknown	gnl\|CDD\|223083

Protein	Function_ID	Function_description	E-value
NZ_CP022986.1\|WP_100077655.1\|3931505_3933788_-\|cation:proton-antiporter	gnl\|CDD\|215608	PLN03159, PLN03159, cation/H(+) antiporter 15; Provisional.	1.01671e-81
NZ_CP022986.1\|WP_100077089.1\|3928553_3929972_+\|L-serine-ammonia-lyase	gnl\|CDD\|273233	TIGR00720, hypothetical_protein_NEICINOT_00681, L-serine dehydratase, iron-sulfur-dependent, single chain form. This enzyme is also called serine deaminase and L-serine dehydratase 1. L-serine ammonia-lyase converts serine into pyruvate in the gluconeogenesis pathway from serine. This enzyme is comprised of a single chain in Escherichia coli, Mycobacterium tuberculosis, and several other species, but has separate alpha and beta chains in Bacillus subtilis and related species. The beta and alpha chains are homologous to the N-terminal and C-terminal regions, respectively, but are rather deeply branched in a UPGMA tree. This enzyme requires iron and dithiothreitol for activation in vitro, and is a predicted 4Fe-4S protein. Escherichia coli Pseudomonas aeruginosa have two copies of this protein. [Energy metabolism, Amino acids and amines, Energy metabolism, Glycolysis/gluconeogenesis].	0
NZ_CP022986.1\|WP_100077654.1\|3918587_3919607_+\|WYL-domain-containing-protein	gnl\|CDD\|379100	pfam13280, WYL, WYL domain. WYL is a Sm-like SH3 beta-barrel fold containing domain. It is a member of the WYL-like superfamily, named for three conserved amino acids found in a subset of the superfamily. However, these residues are not strongly conserved throughout the family. Rather, the conservation pattern includes four basic residues and a position often occupied by a cysteine, which are predicted to line a ligand-binding groove typical of the Sm-like SH3 beta-barrels. A WYL domain protein (sll7009) is a negative regulator of the I-D CRISPR-Cas system in Synechocystis sp. It is predicted to be a ligand-sensing domain that could bind negatively charged ligands, such as nucleotides or nucleic acid fragments, to regulate CRISPR-Cas and other defense systems such as the abortive infection AbiG system.	1.30122e-24
NZ_CP022986.1\|WP_100077090.1\|3929987_3930371_-\|nuclear-transport-factor-2-family-protein	gnl\|CDD\|378915	pfam12680, SnoaL_2, SnoaL-like domain. This family contains a large number of proteins that share the SnoaL fold.	8.1323e-12
NZ_CP022986.1\|WP_100077653.1\|3918005_3918338_+\|HopJ-type-III-effector-protein	gnl\|CDD\|378082	pfam08888, HopJ, HopJ type III effector protein. Pathovars of Pseudomonas syringae interact with their plant hosts via the action of Hrp outer protein (Hop) effector proteins, injected into plant cells by the type III secretion system. The proteins in this family are called HopJ after the original member HopPmaJ.	1.19622e-68
NZ_CP022986.1\|WP_100077091.1\|3930394_3931240_-\|prephenate-dehydrogenase	gnl\|CDD\|181452	PRK08507, PRK08507, prephenate dehydrogenase; Validated.	1.01045e-139
NZ_CP022986.1\|WP_100077085.1\|3924641_3925208_+\|YceI-family-protein	gnl\|CDD\|377274	pfam04264, YceI, YceI-like domain. E. coli YceI is a base-induced periplasmic protein. The recent structure of a member of this family shows that it binds to poly-isoprenoid. The structure consists of an extended, eight-stranded, antiparallel beta-barrel that resembles the lipocalin fold.	3.24919e-27
NZ_CP022986.1\|WP_100077094.1\|3935149_3935920_-\|histidine-kinase	gnl\|CDD\|225814	COG3275, LytS, Putative regulator of cell autolysis [Signal transduction mechanisms].	1.53059e-08
NZ_CP022986.1\|WP_100077086.1\|3925286_3925913_+\|YceI-family-protein	gnl\|CDD\|377274	pfam04264, YceI, YceI-like domain. E. coli YceI is a base-induced periplasmic protein. The recent structure of a member of this family shows that it binds to poly-isoprenoid. The structure consists of an extended, eight-stranded, antiparallel beta-barrel that resembles the lipocalin fold.	1.40864e-20
NZ_CP022986.1\|WP_100077081.1\|3919960_3921145_-\|DUF1501-domain-containing-protein	gnl\|CDD\|226587	COG4102, COG4102, Uncharacterized protein conserved in bacteria [Function unknown].	2.00249e-52
NZ_CP022986.1\|WP_100077082.1\|3921165_3922551_-\|DUF1800-domain-containing-protein	gnl\|CDD\|378055	pfam08811, DUF1800, Protein of unknown function (DUF1800). This is a family of large bacterial proteins of unknown function.	1.98997e-135
NZ_CP022986.1\|WP_100077096.1\|3936318_3937512_-\|alanine-dehydrogenase	gnl\|CDD\|240630	cd05305, L-AlaDH, Alanine dehydrogenase NAD-binding and catalytic domains. Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyruvate to L-alanine via reductive amination. Like formate dehydrogenase and related enzymes, L-AlaDH is comprised of 2 domains connected by a long alpha helical stretch, each resembling a Rossmann fold NAD-binding domain. The NAD-binding domain is inserted within the linear sequence of the more divergent catalytic domain. Ligand binding and active site residues are found in the cleft between the subdomains. L-AlaDH is typically hexameric and is critical in carbon and nitrogen metabolism in micro-organisms.	4.065e-164
NZ_CP022986.1\|WP_100077084.1\|3923452_3924499_+\|glucokinase	gnl\|CDD\|367143	pfam02685, Glucokinase, Glucokinase. This is a family of glucokinases or glucose kinases EC:2.7.1.2. These enzymes phosphorylate glucose using ATP as a donor to give glucose-6-phosphate and ADP.	8.40849e-71
NZ_CP022986.1\|WP_100077097.1\|3937581_3937989_-\|tRNA-(adenosine(37)-N6)-threonylcarbamoyltransferase-complex-ATPase-subunit-type-1-TsaE	gnl\|CDD\|376771	pfam02367, TsaE, Threonylcarbamoyl adenosine biosynthesis protein TsaE. This family of proteins is involved in the synthesis of threonylcarbamoyl adenosine (t(6)A).	2.14758e-43
NZ_CP022986.1\|WP_100077093.1\|3934461_3935172_-\|response-regulator-transcription-factor	gnl\|CDD\|381087	cd17532, REC_LytTR_AlgR-like, phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR. Members of the LytTR/AlgR family of response regulators contain a REC domain and a unique LytTR DNA-binding output domain that lacks the helix-turn-helix motif and consists mostly of beta-strands. Transcriptional regulators with the LytTR-type output domains are involved in biosynthesis of extracellular polysaccharides, fimbriation, expression of exoproteins, including toxins, and quorum sensing. Included in this AlgR-like group of LytTR/AlgR family response regulators are Streptococcus agalactiae sensory transduction protein LytR, Pseudomonas aeruginosa positive alginate biosynthesis regulatory protein AlgR, Bacillus subtilis sensory transduction protein LytT, and Escherichia coli transcriptional regulatory protein BtsR, which are members of two-component regulatory systems. LytR and LytT are components of regulatory systems that regulate genes involved in cell wall metabolism. AlgR positively regulates the algD gene, which codes for a GDP-mannose dehydrogenase, a key enzyme in the alginate biosynthesis pathway. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.	1.19152e-30
NZ_CP022986.1\|WP_100077088.1\|3926730_3928074_+\|ammonium-transporter	gnl\|CDD\|223083	COG0004, AmtB, Ammonia permease [Inorganic ion transport and metabolism].	3.17748e-139

>NZ_CP022986.1|WP_100077088.1|3926730_3928074_+|ammonium-transporter
MKVGLKWIVSFSMITLVAIGGLFWSPIVDFPNTGEFLSEDKIVGADVAWILAAAGLVLLMTPGLSFFYGGMVGKKNVISTMLQSFIALGVISILWVVVGFSLSFGDSLGFTVNGEHYGIIGNPLSYPFFSRVGVLPHKMMASTIPFILFALFQMKFAVITPALITGSFAERVRFISYLLFMVLFSLFIYTPLCHMVWYPDGLLNKYFRVKDFAGGTVVHMSAGFAALAGAMVVGNRKNPHHEPSNVPYVLLGTGMLWFGWFGFNAGSALSANATAAMAFGTTTIASGSAMMTWILFDRINCRSVSAMGACIGAVVGLVAITPGCGFVSIPESIFIGFISAIVSNLMVNWKALKKIDDTLDVFACHGVGGIMGMILTAIFAHGENASLLHGGIEVFAHHMMALILVSAFAFFGSLFLYKVTNRIINLRVSEESENDGLDLSQHGERLY
>NZ_CP022986.1|WP_100077087.1|3925985_3926630_+|alpha/beta-hydrolase
MKIYVVSGLGADFKVLEKLRFPEHLKVVFIDWLIPERNEPFEHYVCRMAEKINGAEPFFLLGYSFGGIMVQEIHKIKPAQKVVILGSLKSHKEKSRLIKTGQLTGVVRFFPERFFDIAAAQAFPAVRKFFDFNNANLVRYFQVRDPYYLKWSVEKIAAWKSEENPDVIQIMGDRDLVFPLKNSRPDYIIKEGTHLFPATRPKEVSKILAEILKL
>NZ_CP022986.1|WP_100077086.1|3925286_3925913_+|YceI-family-protein
MKRLLLLIMMCVGMSFVFAQKKGDKVVKVTSSEIRWWGYKVVKTVASSHSGTVKLKSGKFTFDKTVLVDGEFVIDMRSLMAGDVSEEDQIKLTNDLKSSNFFDVKKFPIAKFHLTKIIPLANSEFNSTVYGDVTIKGVRKTISFPANVYITQFTVVIESAKFSLNRRDFKVFYQSSLKDYFIKNEMDIQFRISTEKLDNENRTPVKKK
>NZ_CP022986.1|WP_100077085.1|3924641_3925208_+|YceI-family-protein
MKKIFLLAVLAGGLAFGQTKKVVASDVHWWGYKVAKSEASSHDGTVKVKSGDMVMKGNQLVGGTFVLDMTSINSTDLSGEYQGKLNGHLKNGDFFEVEKYPTATFKITSVKKNNDKIYNSLVTGNLTVKGKTNPVSFPAKISYSKGVVSLVSNKFTIDRQKFDVAYKSTMQDVFVKDDIDMLVKVTAK
>NZ_CP022986.1|WP_100077084.1|3923452_3924499_+|glucokinase
MNLNPKFPLYLPGVKDSSNNNISIIGANLREDISTIGYFQSVNEGIEMKMHSSYATNDYASFSDILRKFIQENNLTDINRVGISVPGPVIHGKSSPERLGWNLDVEEIRRDFGFENIQLVNDLESSAYGMALLRDEDLEAVYTGGHLEKGNVAILAPGNGLGEAGYFFDGKYLRPFATEGGHSEFSPRTNVEVEFYQFLNNIYGIVSWENVLSKDGLFNIYRFLRDVKRHPEPEGLGERLSNGNFVQELYKAAEEGVLICKIAIDTFLEFLAREANNLTLKLKATGGLFISGDIPQMIRQYLDKDKFYEKFKISDKMEHMLKDIPIYLVKSDNTSLNGVVLYTAYYQD
>NZ_CP022986.1|WP_100077083.1|3922775_3923339_+|hypothetical-protein
MKMFKQAIVLAGVLTAGVLSAQSAQMNNMIKVGANVGLAVPSDNLSAAVGVDVSYQNLITPGFGLGIATGYTHYFAKNDNGYDNNDVGVIPVGALLRIYPKQTGFYFGTDLGYGILVGNDRVASNSTVSRPNGGFYIKPEIGYHNRDWNFFVQYQKVFVGSKGDLPGQDYNVGNIGVGFAYNIALGK
>NZ_CP022986.1|WP_100077082.1|3921165_3922551_-|DUF1800-domain-containing-protein
MAIPSLLNNKHLLWRAGFGPAAGQYAQLAGRETRSLLADLFKHYDFNEIRYSTPDLPDAPANMMDSKSAADRKKEMQKTYSKQNNELNLAFLDRMIHSDDQLREKMAFFWHGHFACRVNNPQYNRQLLNTIRKNALGSFRDLLFEVSQSPAMLNFLNNQQNKKDHPNENFAREVMELFTMGRGNYTENDIREGARAFTGWSYDKEGNFQEKVKVHDEGIKTFLGKTGNFNGADVLNIILDRKATAHFITAKIYRFFVNEKMDEAIIDELSESFYHSGYDIQKLMKTIFSSSWFYDPMNIGNRIKSPIELMAGISRTLPMTVQNPENLIVYQKLLGQMLLYPPNVSGWPSGKSWIDSSTLMLRLQIPQIWSGLRPLEYTPRPDDDIEMGIKSRETALNKMFKNPNIVIDWPQVEKIFTDKNCEDYLIQSPVSLDMNTVQSFSDRSVKMNIINLMSTPEYQLM
>NZ_CP022986.1|WP_100077081.1|3919960_3921145_-|DUF1501-domain-containing-protein
MLIKRRDFLKISSLATASFMMPNFLKAMTLDNALEADDKILVVLQFTGGNDGLNTIIPVRNDIYFRDRKNIAIRNALALNDEAGIHPSLSYFKELYDNGELSVLNNVGYPDPDKSHFRSMDIWQSASKSNEYLDTGWLGRYLDEECYRCERPTQALEVDDMLSLALKGENNKAFAFKDPKRLYQTSQEKYFKSLYDHHHDDETVSYLYQTLGSTINNAGYIFKESQTKKTDQTYPGSQLGKDFKTVASLIKSDINTRVYYLSVGSFDTHVNQNDRQQKLFDDINESVQSFVKDMKSNGLFDKIMLMTFSEFGRRVAQNASNGTDHGTANQMFFISGGLKKKGLLNPLPDLQKLNEGDLIYSEDFRKVYATILKKWLRADSSKVLGWKNGIYDFV
>NZ_CP022986.1|WP_100077654.1|3918587_3919607_+|WYL-domain-containing-protein
MSSNKNALIRYKTLDRCLKNRYRKYTLEDLIDACSEALFEFEGKESYVSRRTVQLDLQNMRSEKFGYEAPIEVYDRKYYRYSDPDYSIHNISVNESDLKAMNNAVQILKQFKDFSMFKEMNGVIQKLEDSIHATHQKSIIHLDKNEQLRGLEHIDILYESIAGKKVLRILYKSFTAREANSFTVHPQLLKEYNNRWFLICLYKGKIYNLALDRMEDIQTDEQAAYIDHHLDGDDYFKDVIGVTVSETLKPKNVVFFVDASNAPYVKTKPLHSSQEIISETEEGTLFKICVQVNYELERLLLGFGDCLVVHQPRKLRLRLQEKFRAGSRNYEKLEIENEQ
>NZ_CP022986.1|WP_100077653.1|3918005_3918338_+|HopJ-type-III-effector-protein
MLPEQLKNAPETIQFKEIIAYIDEHYDFTPVKFTNGDTVNEAGQNNGSCKVFSFARLNSLSKQETLNLFGEFYREDVLKNPEGTDHQNIRNFMQYGWDGIAFEGEALHRK
>NZ_CP022986.1|WP_100077089.1|3928553_3929972_+|L-serine-ammonia-lyase
MESISVFEIIKVGIGPSSSHTMGPWNAAAAFIRIIKRERSIEDVQEVFLEFFGSLAKTGIGHGTDIAGMLGLNGEDFRTIDTSKIDEEVDRIKTTQVLNLGGEKEIPFVYGYHLVLNMQKSLEFHPNGMIFRAVFEDGTELIQDFYSVGGGFIMSQEKKSIEKHCVRTLYPCHKSADIQKYCQKLGLDKISDLILMNEESWRSQEETRQEALYIWQQIKECIYKGVNKEGVLPGGLNVSRRAAAINRKFLGDKVYKNIDEWFRLVVDAEENFTNINKWIACFALAVNEENASFGRIITAPTNGASGVIPAVLMYAQAFTPFTSEDDIVRFLLVAGEIGTLFKKNATISAAMGGCQAEVGVSSAMAAAGLTEILGGSVGQVLMAAEIAMEHHLGLTCDPIKGLVQIPCIERNSMGAIKAITAANIALESDPAKARVTLDEVIQTMWETAQAMSDRFKETSEGGLAIAVNVPEC
>NZ_CP022986.1|WP_100077090.1|3929987_3930371_-|nuclear-transport-factor-2-family-protein
MTQKDQSDIISKYIEAYNHFDIDGMTGCLHEDVIFENISEGKTGLKTEGKEAFRAQAETAATYFSSRHQAVDHWTFSGESVTVSITYEAVLATDFPNGMKKGATLSLKGESEFTFSDGKIIRITDRS
>NZ_CP022986.1|WP_100077091.1|3930394_3931240_-|prephenate-dehydrogenase
MKISIIGVGLIGGSIALKLKKKGITQRILGIDQNGQHLQQAIELGIIDGAADLEDGIKNADLIILAIPVDAARRLLPDVLDLVTGQQTVMDAGSTKAGIVHSVHDHPQRARYVAFHPMWGTENSGPRAAVAESFAGKAGVICNKELSAPDALQTAETIIEALEMHPVYMDAEDHDIHTAYISHISHITSYALANTVLEKEREEETIFQLASSGFSSTVRLAKSHPEMWVPIFKQNRDNVLDVLNEHISQLRKFKSALEKENYDYLEELIANANKIRGILDK
>NZ_CP022986.1|WP_100077655.1|3931505_3933788_-|cation:proton-antiporter
MGKYKNIIFYISTIVFFSCLMYWFFIEGKTLEIGENIAVPKTTGSTMWENFTDSFLTNLHHPLALLLAQIVTIILVAKLFGWICVKLKQPSVIGEMIAGIVLGPSLFGLYFPELSAFIFPKESLPNLQFLSQIGLILFMYIVGMELDLGVLRKKAHDAVVISHASIIFPFALGVGLSYFIYQEFAPDGIQFSSFALFIAIAMSITAFPVLARIVQERNLHKTKIGTVVITCAAADDITAWCILAAVIAVVKAGSFSGSVFVILMAILYVFIMIKAVRPFLQRIVETQKGKGFISKALVAVFFLILIISSYATEVIGIHALFGAFMAGAIMPENVKFRNLFIEKVEDVALVLLLPLFFVFTGLRTQIGLLNDPHLWKIGGFIILTAVTGKFVGSALTAKFLRLSWKDSLTIGALMNTRGLTELIVLNIGYDLGVLGPELFAMLVIMALFTTFMTGPSLDLINYLFKGKTSMTEEEDHGNDNTKYRVLLSFETAKSGSTLLKLADHLTRKMNGNKSITAMNIAPVDELHAFEIDEFEKEQFRSVVETSQDLNLEITTLFKASTDMESDLTGISNKGNYDLLLIMLGKSMYEGSLLGRLLGFTTKIINPEKLLNTVKGKGNIFNTSPFDDFTLQILDKTNIPVGVLVERNFSSADRVFIPMFKLSDFYLLEYAKRLINNNNSQIIILDVTGQIRNNIEVKELIRSIEQVAPNHITLYNEKKIEKEFLQSQDLMLVSSKSWKSLIDTKSLWLSDIPSTLIISNP
>NZ_CP022986.1|WP_100077092.1|3933894_3934284_-|hypothetical-protein
MKKLLCTATVLISGLCFCQSTETEIKAAFFDGTIVAGYADHGAFINCTGPNISLKNKSFKLMLGMLPSLRIKEDRAEGTRNSLIMPALGAGMTAVYKRLAVQLPVYYNAKTPSQNGSWKAGIGLGYSFR
>NZ_CP022986.1|WP_100077093.1|3934461_3935172_-|response-regulator-transcription-factor
MIRCAILDDELLAISYLKLLCEQIEDVEVIKAFNDPRAFLNEVNTLGCNVCILDIEMPGMNGLQVAELISGFVKIIFTTAYKEYAAEAFDLNVVDYVRKPIKKERLVQAFDKARDLISQSQKKDFIEWNTNIGKTIIFTDQIAYIKTSEIDSRDKDITLHDGTVIVLKNLSFKNLLDILPPKDFAQVNKKEIIARSSVKVFSTNEIITSIPAENGHFLKLQIGETYKNALLEMFGK
>NZ_CP022986.1|WP_100077094.1|3935149_3935920_-|histidine-kinase
MDGNYYMIQDYLIFIGVFAIFLLASISIYLFSWNKRYKKLNKKLSETNKIIEQRLNEVQLEHIGTKLNPHLFKNILNSVQSHAYQTYMSLDKLANVLDYILYESNTRFVSPKEELNFALSLIEINKIKINPLFDFRIKFNVNKSDPMYEEKVFAPLISVDLIENAFKHTDFLAQDCFIAVQIELENRVFSMNVSNKASEKNTLEKERSGFGSQSLDQRLKMIYNNYYHLSRSSKNGIFTAELTINLGEFYDQMRYS
>NZ_CP022986.1|WP_100077095.1|3935947_3936319_-|hypothetical-protein
MKKLKFYAIGLVPGCLIVLFILNKKGASCSGYLPNSRVIAETLSKEFRYSDGFSEEMKSYGVTEKFLKDSIITQGKVDFDRSHAQNKPCPDYLLSYPEKSPVYEITFDKCAETATMKSLKKIR
>NZ_CP022986.1|WP_100077096.1|3936318_3937512_-|alanine-dehydrogenase
MSTTNIFTPFTEEELMPKEEKLEVIKKGRQFSIGIPKETSLHERRTCITPDAVQVLVEHGHEIIIEAGAGEGSFFTDLQYSESGARITQDPKEAFGQDLVLKINPPTEDEIDFMRPNTYLVSALQINLRDKSYFLKLAEKKINAIAFEFIVDEYKQLALVRLVGEIAGTVSILYASELLALSNGLMLGGLTGVRPAEVVILGAGIVGEFATKASIGLGASVRVFDNSLSKLRRLHTIVDSRVPTSIIDPKELKKALRRADVVIGALPRLNMTPIVTEDMVMSMKKGSVIIDITIDNGKVIETSELTNMENPYIIKHGVIHCGLPNLTSRMPRTTTKAISNFFLSYILNYDEEGGFENMLVRKNEMKQSLYMYKGRHTKKVICDRFGLTYHDINLLIF
>NZ_CP022986.1|WP_100077097.1|3937581_3937989_-|tRNA-(adenosine(37)-N6)-threonylcarbamoyltransferase-complex-ATPase-subunit-type-1-TsaE
MVFNITTYDEWQDVTEAILPQLKHNIVLLKGNLGAGKTTFTQFLLKKLGTGDEVNSPTYSIVNEYNTPKGKVFHFDLYRLKSIEEVYDIGMEEYLDNGYLCIIEWPEVYEEDLDGLDYHTMTIENTGDSREILFE

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Self-targeting detection

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_ID	Protospacer_location	Mismatch	Identity

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity
NZ_CP022986_3	3.2\|3156939\|30\|NZ_CP022986\|CRISPRCasFinder	3156939-3156968	30	MK448993	Streptococcus phage Javan616, complete genome	15545-15574	6	0.8
NZ_CP022986_3	3.2\|3156939\|30\|NZ_CP022986\|CRISPRCasFinder	3156939-3156968	30	NC_048677	Lactobacillus phage LpeD, complete genome	25810-25839	6	0.8
NZ_CP022986_3	3.2\|3156939\|30\|NZ_CP022986\|CRISPRCasFinder	3156939-3156968	30	NZ_CP034782	Pseudomonas sp. MPC6 plasmid pMPC6-328K, complete sequence	262861-262890	7	0.767
NZ_CP022986_3	3.2\|3156939\|30\|NZ_CP022986\|CRISPRCasFinder	3156939-3156968	30	NZ_CP040856	Lactobacillus johnsonii strain G2A plasmid unnamed2, complete sequence	58687-58716	7	0.767
NZ_CP022986_3	3.2\|3156939\|30\|NZ_CP022986\|CRISPRCasFinder	3156939-3156968	30	MN693609	Marine virus AFVG_250M479, complete genome	51742-51771	8	0.733
NZ_CP022986_3	3.2\|3156939\|30\|NZ_CP022986\|CRISPRCasFinder	3156939-3156968	30	NZ_CP007129	Gemmatirosa kalamazoonesis strain KBS708 plasmid 1, complete sequence	1001012-1001041	8	0.733
NZ_CP022986_3	3.2\|3156939\|30\|NZ_CP022986\|CRISPRCasFinder	3156939-3156968	30	CP046513	Bacillus cereus strain JHU plasmid p2, complete sequence	242311-242340	9	0.7
NZ_CP022986_3	3.2\|3156939\|30\|NZ_CP022986\|CRISPRCasFinder	3156939-3156968	30	NC_048773	Aeromonas phage 4_4572, complete genome	34109-34138	9	0.7
NZ_CP022986_3	3.2\|3156939\|30\|NZ_CP022986\|CRISPRCasFinder	3156939-3156968	30	NC_048775	Aeromonas phage LAh_8, complete genome	61339-61368	9	0.7
NZ_CP022986_3	3.2\|3156939\|30\|NZ_CP022986\|CRISPRCasFinder	3156939-3156968	30	NC_048774	Aeromonas phage LAh_6, complete genome	22813-22842	9	0.7
NZ_CP022986_3	3.2\|3156939\|30\|NZ_CP022986\|CRISPRCasFinder	3156939-3156968	30	MK838115	Aeromonas phage LAh_9, complete genome	87695-87724	9	0.7

1. spacer 3.2|3156939|30|NZ_CP022986|CRISPRCasFinder matches to MK448993 (Streptococcus phage Javan616, complete genome) position: , mismatch: 6, identity: 0.8

taagaacgctggtgaagctgctaaaggagc	CRISPR spacer
ttcaaacgctgctgaagctgctaaagaggc	Protospacer
*  .******* **************..**

2. spacer 3.2|3156939|30|NZ_CP022986|CRISPRCasFinder matches to NC_048677 (Lactobacillus phage LpeD, complete genome) position: , mismatch: 6, identity: 0.8

taagaacgctggtgaagctgctaaaggagc	CRISPR spacer
taaagccgctggtgaagatgctaaagcaga	Protospacer
***.. *********** ******** **

3. spacer 3.2|3156939|30|NZ_CP022986|CRISPRCasFinder matches to NZ_CP034782 (Pseudomonas sp. MPC6 plasmid pMPC6-328K, complete sequence) position: , mismatch: 7, identity: 0.767

taagaacgctggtgaagctgctaaaggagc	CRISPR spacer
cattggcgctggtgaagctgctcaaggtgc	Protospacer
.*  ..**************** **** **

4. spacer 3.2|3156939|30|NZ_CP022986|CRISPRCasFinder matches to NZ_CP040856 (Lactobacillus johnsonii strain G2A plasmid unnamed2, complete sequence) position: , mismatch: 7, identity: 0.767

taagaacgctggtgaagctgctaaaggagc	CRISPR spacer
gattgaagctgatgaagctgctaaagcagc	Protospacer
 *  .* ****.************** ***

5. spacer 3.2|3156939|30|NZ_CP022986|CRISPRCasFinder matches to MN693609 (Marine virus AFVG_250M479, complete genome) position: , mismatch: 8, identity: 0.733

taagaacgctggtgaagctgctaaaggagc	CRISPR spacer
agcagacgctagtgaagctgctaaagcaga	Protospacer
 . ..*****.*************** **

6. spacer 3.2|3156939|30|NZ_CP022986|CRISPRCasFinder matches to NZ_CP007129 (Gemmatirosa kalamazoonesis strain KBS708 plasmid 1, complete sequence) position: , mismatch: 8, identity: 0.733

taagaacgctggtgaagctgctaaaggagc	CRISPR spacer
tgcacgcgctggtgaagctgctcgaggagg	Protospacer
*. . .**************** .*****

7. spacer 3.2|3156939|30|NZ_CP022986|CRISPRCasFinder matches to CP046513 (Bacillus cereus strain JHU plasmid p2, complete sequence) position: , mismatch: 9, identity: 0.7

taagaacgctggtgaagctgctaaaggagc	CRISPR spacer
ctcaaccgttggtgaagctgctaaaggcaa	Protospacer
.  .* **.****************** .

8. spacer 3.2|3156939|30|NZ_CP022986|CRISPRCasFinder matches to NC_048773 (Aeromonas phage 4_4572, complete genome) position: , mismatch: 9, identity: 0.7

taagaacgctggtgaagctgctaaaggagc	CRISPR spacer
aaagaatgctggtgaagcagctaagatgaa	Protospacer
 *****.*********** *****.. ..

9. spacer 3.2|3156939|30|NZ_CP022986|CRISPRCasFinder matches to NC_048775 (Aeromonas phage LAh_8, complete genome) position: , mismatch: 9, identity: 0.7

taagaacgctggtgaagctgctaaaggagc	CRISPR spacer
aaagaatgctggtgaagcagctaagatgaa	Protospacer
 *****.*********** *****.. ..

10. spacer 3.2|3156939|30|NZ_CP022986|CRISPRCasFinder matches to NC_048774 (Aeromonas phage LAh_6, complete genome) position: , mismatch: 9, identity: 0.7

taagaacgctggtgaagctgctaaaggagc	CRISPR spacer
aaagaatgctggtgaagcagctaagatgaa	Protospacer
 *****.*********** *****.. ..

11. spacer 3.2|3156939|30|NZ_CP022986|CRISPRCasFinder matches to MK838115 (Aeromonas phage LAh_9, complete genome) position: , mismatch: 9, identity: 0.7

taagaacgctggtgaagctgctaaaggagc	CRISPR spacer
aaagaatgctggtgaagcagctaagatgaa	Protospacer
 *****.*********** *****.. ..

Prophage detection

Region

Region Position

Protein_number

Hit_taxonomy

Key_proteins

Att_site

Prophage annotation

DBSCAN-SWA_1

2789188 : 2795623

Moumouvirus(16.67%)

The bacterium proteins that are colored denote the protein is present at specific phage-related keywords (such as 'capsid', 'head', 'integrase', 'plate', 'tail', 'fiber', 'coat', 'transposase', 'portal', 'terminase', 'protease' or 'lysin' and 'tRNA')

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_100076159.1\|2789188_2789740_+	2OG-Fe(II) oxygenase	M1PY53	Moumouvirus	4.4e-16	30.5
WP_100076160.1\|2790685_2791765_+	adenylosuccinate synthetase	NA	NA	NA	NA
WP_100077590.1\|2791820_2792294_+	macro domain-containing protein	A0A2L1IVW3	Streptomyces_phage	8.4e-32	45.6
WP_100076161.1\|2792352_2792859_+	O-acetyl-ADP-ribose deacetylase	A0A0K1L687	Scale_drop_disease_virus	1.8e-32	52.8
WP_100076162.1\|2792858_2793269_+	SMI1/KNR4 family protein	NA	NA	NA	NA
WP_100076164.1\|2793441_2794128_+	NAD-dependent deacylase	R9TG77	Vibrio_phage	1.3e-28	38.3
WP_100076165.1\|2794127_2795069_+	ADP-ribosylglycohydrolase family protein	A0A1S6UB21	Serratia_phage	6.8e-41	34.6
WP_100076166.1\|2795074_2795623_+	RNA 2'-phosphotransferase	A0A2R2ZGT8	Clostridioides_phage	1.7e-44	52.0

DBSCAN-SWA_2

3109001 : 3116308

Tupanvirus(16.67%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_100076429.1\|3109001_3110087_-	DegT/DnrJ/EryC1/StrS family aminotransferase	A0A2K9L0G1	Tupanvirus	9.6e-31	31.0
WP_100076430.1\|3110086_3110860_-	FkbM family methyltransferase	A0A0N9QAD0	Chrysochromulina_ericina_virus	9.6e-09	28.2
WP_100076431.1\|3110843_3112070_-	ABC transporter ATP-binding protein	A0A2H4PQG7	Staphylococcus_phage	3.5e-13	28.6
WP_157761431.1\|3112071_3112812_-	ABC transporter permease	NA	NA	NA	NA
WP_100076433.1\|3113032_3113896_-	glucose-1-phosphate thymidylyltransferase RfbA	H9NC64	Sphingomonas_phage	1.0e-99	63.1
WP_100076434.1\|3113910_3114990_-	dTDP-glucose 4,6-dehydratase	I7HTA3	Enterobacteria_phage	2.8e-83	47.2
WP_100076435.1\|3114994_3116308_-	UDP-glucose/GDP-mannose dehydrogenase family protein	A0A127AXI2	Bacillus_phage	6.1e-80	38.5

DBSCAN-SWA_3

3495461 : 3502533

Beihai_hepe-like_virus(33.33%)

transposase

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_172954739.1\|3495461_3495755_+	hypothetical protein	A0A142EZZ6	Stenotrophomonas_phage	1.0e-19	52.2
WP_100076742.1\|3496002_3496539_+	exonuclease domain-containing protein	A0A1L3KJF4	Beihai_hepe-like_virus	8.7e-09	28.9
WP_172954740.1\|3496559_3497111_+	exonuclease domain-containing protein	A0A1L3KJF4	Beihai_hepe-like_virus	1.7e-12	35.3
WP_100076744.1\|3497209_3497536_-	hypothetical protein	NA	NA	NA	NA
WP_100076745.1\|3497548_3497977_-\|transposase	transposase	NA	NA	NA	NA
WP_100076746.1\|3498367_3499954_+	SulP family inorganic anion transporter	A0A2H4J153	uncultured_Caudovirales_phage	2.1e-82	38.2
WP_100076747.1\|3500072_3501002_-	T9SS type A sorting domain-containing protein	A0A1B1IUC7	uncultured_Mediterranean_phage	5.4e-06	26.0
WP_100077626.1\|3501498_3502533_+	TerC family protein	A0A291LBC5	Escherichia_phage	1.0e-42	33.5

Anti-CRISPR protein detection

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

Overview of predicted results

Overview of the results

Cas Category Instructions

Results visualization

1. NZ_CP022986

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CRISPR-Cas detection and classification

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Click the colored protein region to show detailed information

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Self-targeting detection

MGE targeting detection<

Prophage detection

Anti-CRISPR protein detection