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_LT906468	Sphingobacterium mizutaii strain NCTC12149 chromosome 1	18 crisprs	WYL,cas3,DEDDh,PrimPol,csa3	1	3	0	0

Results visualization

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CRISPR-Cas detection and classification

Crispr_ID: NZ_LT906468_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LT906468_1

373249-373340

Orphan

Consensus_repeat	Method
ACCAAACCGACGAAGGAGCTCAGGGATACCA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_LT906468_1

>merge|NZ_LT906468|1|373249-373340|CRISPRCasFinder
ACCAAACCGACGAAGGAGCTCAGGGATACCAATTCTTCTGTTACTTTTGAAGCCCAAAAGTACCAAACCGACGAAGGAGCTCACGGATACCA

>NZ_LT906468|1|1|373249-373340|CRISPRCasFinder
ACCAAACCGACGAAGGAGCTCAGGGATACCA	ATTCTTCTGTTACTTTTGAAGCCCAAAAGT
ACCAAACCGACGAAGGAGCTCACGGATACCA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LT906468.1\|WP_093101191.1\|368519_369893_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906468.1\|WP_093101186.1\|364545_365271_+\|YebC/PmpR-family-DNA-binding-transcriptional-regulator	unknown	unknown	gnl\|CDD\|237084
NZ_LT906468.1\|WP_093101182.1\|362232_363222_-\|aspartate-semialdehyde-dehydrogenase	unknown	unknown	gnl\|CDD\|237845
NZ_LT906468.1\|WP_093101217.1\|381309_381849_+\|TetR/AcrR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224228
NZ_LT906468.1\|WP_093101205.1\|375309_376281_+\|rhodanese-related-sulfurtransferase	unknown	unknown	gnl\|CDD\|234663
NZ_LT906468.1\|WP_093101193.1\|369892_371347_-\|lipopolysaccharide-biosynthesis-protein	unknown	unknown	gnl\|CDD\|240532
NZ_LT906468.1\|WP_093101199.1\|373359_373593_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906468.1\|WP_093101213.1\|377535_378330_+\|M48-family-metallopeptidase	unknown	unknown	gnl\|CDD\|320691
NZ_LT906468.1\|WP_093101180.1\|360887_361880_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|276965
NZ_LT906468.1\|WP_093101207.1\|376366_376708_+\|TM2-domain-containing-protein	unknown	unknown	gnl\|CDD\|377473
NZ_LT906468.1\|WP_093101211.1\|377095_377539_+\|DUF4870-domain-containing-protein	unknown	unknown	unknown
NZ_LT906468.1\|WP_093101203.1\|374983_375220_+\|DUF3820-family-protein	unknown	unknown	gnl\|CDD\|378970
NZ_LT906468.1\|WP_093101195.1\|371471_372395_+\|glycosyltransferase	unknown	unknown	gnl\|CDD\|133007
NZ_LT906468.1\|WP_093101184.1\|363593_364544_+\|NAD-dependent-epimerase/dehydratase-family-protein	unknown	unknown	gnl\|CDD\|187580
NZ_LT906468.1\|WP_093101209.1\|376712_377120_+\|DUF2752-domain-containing-protein	unknown	unknown	gnl\|CDD\|378499
NZ_LT906468.1\|WP_093101215.1\|378326_381059_-\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|379720
NZ_LT906468.1\|WP_093101197.1\|372391_373084_-\|FkbM-family-methyltransferase	unknown	unknown	gnl\|CDD\|377448
NZ_LT906468.1\|WP_093101188.1\|365391_366621_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|173412
NZ_LT906468.1\|WP_093101189.1\|367420_368542_-\|CapA-family-protein	unknown	unknown	gnl\|CDD\|214858
NZ_LT906468.1\|WP_093101201.1\|374250_375003_+\|glycosyltransferase	unknown	unknown	gnl\|CDD\|133055

Protein	Function_ID	Function_description	E-value
NZ_LT906468.1\|WP_093101186.1\|364545_365271_+\|YebC/PmpR-family-DNA-binding-transcriptional-regulator	gnl\|CDD\|237084	PRK12378, PRK12378, YebC/PmpR family DNA-binding transcriptional regulator.	2.31705e-114
NZ_LT906468.1\|WP_093101182.1\|362232_363222_-\|aspartate-semialdehyde-dehydrogenase	gnl\|CDD\|237845	PRK14874, PRK14874, aspartate-semialdehyde dehydrogenase; Provisional.	0
NZ_LT906468.1\|WP_093101217.1\|381309_381849_+\|TetR/AcrR-family-transcriptional-regulator	gnl\|CDD\|224228	COG1309, AcrR, Transcriptional regulator [Transcription].	3.36828e-14
NZ_LT906468.1\|WP_093101205.1\|375309_376281_+\|rhodanese-related-sulfurtransferase	gnl\|CDD\|234663	PRK00142, PRK00142, rhodanese-related sulfurtransferase.	4.00944e-154
NZ_LT906468.1\|WP_093101193.1\|369892_371347_-\|lipopolysaccharide-biosynthesis-protein	gnl\|CDD\|240532	cd13127, MATE_tuaB_like, Uncharacterized subfamily of the multidrug and toxic compound extrusion (MATE) proteins. This family might function as a translocase for lipopolysaccharides and participate in the biosynthesis of cell wall components such as teichuronic acid. The integral membrane proteins from the MATE family are involved in exporting metabolites across the cell membrane and are responsible for multidrug resistance (MDR) in many bacteria and animals. A number of family members are involved in the synthesis of peptidoglycan components in bacteria.	1.38393e-90
NZ_LT906468.1\|WP_093101213.1\|377535_378330_+\|M48-family-metallopeptidase	gnl\|CDD\|320691	cd07332, M48C_Oma1_like, Peptidase M48C Ste24p, integral membrane endopeptidase. This subfamily contains peptidase M48C Oma1 (also called mitochondrial metalloendopeptidase OMA1) protease homologs that are mostly uncharacterized. Oma1 is part of the quality control system in the inner membrane of mitochondria, with its catalytic site facing the matrix space. It cleaves and thereby promotes the turnover of mistranslated or misfolded membrane proteins. Oma1 can cleave the misfolded multi-pass membrane protein Oxa1, thus exerting a function similar to the ATP-dependent m-AAA protease for quality control of inner membrane proteins; it cleaves a misfolded polytopic membrane protein at multiple sites. It has been proposed that in the absence of m-AAA protease, proteolysis of Oxa1 is mediated by Oma1 in an ATP-independent manner. Oma1 is part of highly conserved mitochondrial metallopeptidases, with homologs present in higher eukaryotes, eubacteria and archaebacteria, all containing the zinc binding motif (HEXXH). It forms a high molecular mass complex in the inner membrane, possibly a homo-hexamer.	3.81441e-46
NZ_LT906468.1\|WP_093101180.1\|360887_361880_+\|hypothetical-protein	gnl\|CDD\|276965	sd00038, Kelch, Kelch repeat. Kelch repeats are 44 to 56 amino acids in length and form a four-stranded beta-sheet corresponding to a single blade of five to seven bladed beta propellers. The Kelch superfamily is a large evolutionary conserved protein family whose members are present throughout the cell and extracellularly, and have diverse activities. Kelch repeats are often in combination with other domains, like BTB and BACK or F-box domains.	3.39128e-16
NZ_LT906468.1\|WP_093101207.1\|376366_376708_+\|TM2-domain-containing-protein	gnl\|CDD\|377473	pfam05154, TM2, TM2 domain. This family is composed of a pair of transmembrane alpha helices connected by a short linker. The function of this domain is unknown, however it occurs in a wide range or protein contexts.	6.58675e-14
NZ_LT906468.1\|WP_093101203.1\|374983_375220_+\|DUF3820-family-protein	gnl\|CDD\|378970	pfam12843, QSregVF_b, Putative quorum-sensing-regulated virulence factor. QSregVF_b is a family of short Pseudomonas proteins that are potential virulence factors. The structure of UniProtKB:Q9HY15 a secreted protein has been solved and deposited as Structure 3npd, from pfam13652. It is predicted that these two adjacent proteins form a single transcriptional unit based on the prediction that together they interact with their adjacent protein PotD, which is the putrescine-binding periplasmic protein in the polyamine uptake system comprising PotABCD. These two adjacent proteins are predicted to be quroum-sensing-regulated virulence factors.	4.5534e-34
NZ_LT906468.1\|WP_093101195.1\|371471_372395_+\|glycosyltransferase	gnl\|CDD\|133007	cd02514, GT13_GLCNAC-TI, GT13_GLCNAC-TI is involved in an essential step in the synthesis of complex or hybrid-type N-linked oligosaccharides. Alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase (GLCNAC-T I , GNT-I) transfers N-acetyl-D-glucosamine from UDP to high-mannose glycoprotein N-oligosaccharide, an essential step in the synthesis of complex or hybrid-type N-linked oligosaccharides. The enzyme is an integral membrane protein localized to the Golgi apparatus. The catalytic domain is located at the C-terminus. These proteins are members of the glycosy transferase family 13.	9.1141e-05
NZ_LT906468.1\|WP_093101184.1\|363593_364544_+\|NAD-dependent-epimerase/dehydratase-family-protein	gnl\|CDD\|187580	cd05272, TDH_SDR_e, L-threonine dehydrogenase, extended (e) SDRs. This subgroup contains members identified as L-threonine dehydrogenase (TDH). TDH catalyzes the zinc-dependent formation of 2-amino-3-ketobutyrate from L-threonine via NAD(H)-dependent oxidation. This group is distinct from TDHs that are members of the medium chain dehydrogenase/reductase family. This group has the NAD-binding motif and active site tetrad of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.	1.66334e-166
NZ_LT906468.1\|WP_093101209.1\|376712_377120_+\|DUF2752-domain-containing-protein	gnl\|CDD\|378499	pfam10825, DUF2752, Protein of unknown function (DUF2752). This family is conserved in bacteria. Many members are annotated as being putative membrane proteins.	2.90153e-12
NZ_LT906468.1\|WP_093101215.1\|378326_381059_-\|TonB-dependent-receptor	gnl\|CDD\|379720	pfam14905, OMP_b-brl_3, Outer membrane protein beta-barrel family. This family includes proteins annotated as TonB dependent receptors. But it is also likely to contain other membrane beta barrel proteins of other functions.	3.5217e-28
NZ_LT906468.1\|WP_093101197.1\|372391_373084_-\|FkbM-family-methyltransferase	gnl\|CDD\|377448	pfam05050, Methyltransf_21, Methyltransferase FkbM domain. This family has members from bacteria to human, and appears to be a methyltransferase.	9.05786e-24
NZ_LT906468.1\|WP_093101188.1\|365391_366621_+\|hypothetical-protein	gnl\|CDD\|173412	PTZ00121, PTZ00121, MAEBL; Provisional.	3.4096e-05
NZ_LT906468.1\|WP_093101189.1\|367420_368542_-\|CapA-family-protein	gnl\|CDD\|214858	smart00854, PGA_cap, Bacterial capsule synthesis protein PGA_cap. This protein is a putative poly-gamma-glutamate capsule biosynthesis protein found in bacteria. Poly-gamma-glutamate is a natural polymer that may be involved in virulence and may help bacteria survive in high salt concentrations. It is a surface-associated protein.	4.19858e-61
NZ_LT906468.1\|WP_093101201.1\|374250_375003_+\|glycosyltransferase	gnl\|CDD\|133055	cd06433, GT_2_WfgS_like, WfgS and WfeV are involved in O-antigen biosynthesis. Escherichia coli WfgS and Shigella dysenteriae WfeV are glycosyltransferase 2 family enzymes involved in O-antigen biosynthesis. GT-2 enzymes have GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.	2.28376e-72

>NZ_LT906468.1|WP_093101197.1|372391_373084_-|FkbM-family-methyltransferase
MSKIKKAVLTYFPIHKFFHARSFSQEGEDMVLRGFYEGRKNYKGFYVDVGAHHPYRFSNTMYFYKKGWRGINIEPSPEAMKWFNWFRTKDVNLNIGISESPQELTYYCFNEPALNGFSQEISEKRDGLNAKYHLIKTIPVPTLPLKEVLQKHLPKGKKIDFLSVDAEGFDLIVLNSNDWQQYRPTFVLVEEELSIADLNKSEVFQLMLEKGYSLVAKTKRTLFFKNLEEN
>NZ_LT906468.1|WP_093101195.1|371471_372395_+|glycosyltransferase
MLAPIALFVYNRPVHTRKTLSALEANSLAEQSDIYIFSDGAKTAQDIDSVNQVRSIIREPWKFKHIYIIERSQNKGLANSIIEGVTQVVQKHGKIIVLEDDLETSSFALQYFNDALNQYQDQEKVMEISGYMYPVDKPKKLPQSFFFRVANSWGWATWDRAWQHFNPDIEELTKDFTRKQRKAFSVDNSENFWKQVKQFKAGKINSWAIRWYLSVFNKGGLVLYPRFSFIQNTGTDGSGTHSDVDKVYRVELSKKPVRKFPIILEEDPLAFQAIKHFYKNRKGTFFERLAKFIEKKLLERKMRKLKA
>NZ_LT906468.1|WP_093101193.1|369892_371347_-|lipopolysaccharide-biosynthesis-protein
MSENTKKITLNGLFWNALDRFGNQAIVTIVAIITARIISPDEFAVIAALAIFSIIATTFVDSGLATSLVRTKVVDELDYSSMFIFNLSVSAIIYLILYFASPYIEKYYNIPGLALYARVLFLQIIIQSFSIVQYVKILKKFQFHLTTRVNVLAVLFAGIIVIIVALLGYGVWALILQPLLYTLFRTIMLWIWGDWKVNFAFSAASLKKHLSFSLSFMVSNMLGKILSPFYASFIGKHYTADQVGYYYQGNKWGETAGQTITAILQGTTLSTLTPIQDDLPRFLNASRKTLSSLAFALIPISFLAIAVAKPGFVFFLTDTWVSSIILFQILCFASIFTSLTDLNANFLNIKGRSKFFLSLEIIKVSLAIIALFLTYKHGLVMIALGLVAVRIICYIIAASMSGRVYGYNLFMQVKDLLPTTLISIIAAGLAYLPLYFNLIPNYLLLIIVQSLIFVVIYVGANHMIKNDIWMEILGMLKKKLAKKS
>NZ_LT906468.1|WP_093101191.1|368519_369893_-|hypothetical-protein
MEVAKGNWVGYQTVFYNLKTGKYSQEINEVIDYANLEIDPEGLAAYLDFGYSVFGHTPVKDVKYLLPNQILSLENDRLSIKEGNDDTLNLLGKKSHEDDVFHKLSTALQNWADGFKDDILIPTSGGFDSRLMNVLLEDKSRIHAYTYGTSLNQDESREAVYAGLLSKRLHTQWKRIPLGKFNVYMDQWYDQFGPAVAASGTYHMEFYDKIKQLEAGNPMHLLSGIIGDAWAGAVKVPMIDSSASYRTLGYTHGMSADSKLAMDIDYSSIVEPIYDRQKEHLGSPEYRIITAMRTKMMMLQYLISVPAKMGYPGYSPFVDEDIAISMLNLPVERRENRAWQRDFFRKNNLLFEEEKHKYTYQNSLNYYALLNETLTPLNVDLLKECLNPEYLNWINQKIMHIGRKEKIFQTLMHTPKVKGVLKLLGAKNDLLEAYFAYITIKPIENLLIRRNASHIQA
>NZ_LT906468.1|WP_093101189.1|367420_368542_-|CapA-family-protein
MPATSKHKFVFVGDIVCEKAPQFSPSLKELFNSADLKSCNFEAPLQGLGQPIHKTGPLVAQNKNAPNWLQELGFNCFSLANNHIYDFGEDALLKTMEQFPRKEILGVGSEEEAYGLKTWTFDEVKYGFLAYGENGYGALNGDRLVGHAWVNAKRVNADIQQYKKQVDVLIVQIHAGVELLDVPIPEWKDRYKELIDLGVDVIIAHHPHVVQGIEEYNGKLIAYSLGNFYFEYPANHPQWNVGGVLELEFENKKLSKHFLHIVEKKKQLVELKDEKLSANFVKPLSAKLGNEEYLEYVNRKALEEWKKHHASYYAKPFNGIAGYSVFKLLKHAKRTLFNRRINYNLIWHNLFIESNKWLVERAIRLKTFGKKPN
>NZ_LT906468.1|WP_093101188.1|365391_366621_+|hypothetical-protein
MLSFTEFFTKKKIDINALQKAKPDLYHEFDRDYALMGEKSFDHSKKFWFNRLRKDYLLKEIEITEPKKGEVKAESTAPATAASTSTAPAAAKPAGFRPKFKAAVKTVEEKAIEPTAETEEKPAAKAPAGFKPRFKAAAPPERLDGPMEGNVSDKPADGPKDSEEAVAKPKGFTPRFKAANLPKKIESEKPEDSQAETPADNTEENKEAAAPAKPKGFTPRFKASNLPKKVEDENKEESAPEAQEEATIEAPKPKGFTPRFKAANLPKKVESEAQEESAPEAKEEASIEASKPKGFTPRFKAANLPKKLEEKEEPSAESVQENKVAEEPSASDDAATTATEEVTSKPTGFKPRFKAGVTKAATNQEDQDPNPEQSSTPTEEPSTQTTTKPVGFKPRFVAKKSSDQKDKED
>NZ_LT906468.1|WP_093101186.1|364545_365271_+|YebC/PmpR-family-DNA-binding-transcriptional-regulator
MGRAFEFRKERKFKRWAKMAVQFTRLGKEIAIAVKEGGPHPENNSRLRTAIQNAKAVNMPKDRVEAAIKRASEKDSKGYEEFVYEGYGPHGVPVLIETATDNTNRTVANVRSYFTKAGGSLGKTGSLDFIFQRKSVFRFPATDELDVEELELELIDGGLEELYVEADEEGNDIIVVQTSFEDFGNMQRLLEEKGIEVSSAKTERIALSHTTLSEEQAADVLKLIDKIEEDDDVQAVYHNMD
>NZ_LT906468.1|WP_093101184.1|363593_364544_+|NAD-dependent-epimerase/dehydratase-family-protein
MKEVILMIGANGQIGSELAAALRIKFGNENVITSDIREPKEIAEGEIFETLNVLDKEAIKALILKYKPTQIYLLAAMLSATGEQYPQKAWDLNMNGLLNVLDLAVELGIKKIFWPSSIAVFGPHSPKENTPQYCVMDPNSIYGISKLAGERLCEYYHNKYGLDIRSVRYPGIISWRTEPGGGTTDYAVHIFFEAIRQGKYTSFLNAGTELPMLYMDDAVRGTIELMDAPSAGLTIRSSYNLSGVSFTPTEIAEEIKKILPNFEISYSDNDPRQAIADSWPKSINDDQARADWGWKPTFDLAGMAKDMLENLKTKLK
>NZ_LT906468.1|WP_093101182.1|362232_363222_-|aspartate-semialdehyde-dehydrogenase
MKVAVVGATGLVGSEMLTVLAERNFPVTELIPVASERSKGKEIEFKGKKYKVVTASEAIALKPDVALFSAGGSTSTEYAPLFAEAGITVIDNSSAWRMDPSKKLIVPEVNGDVLTAEDKIIANPNCSTIQMVVVMKPLHEKYKIKRVVVSTYQSVTGTGVKAVDQLMNERKGIEGEKAYPYQIDLNVIPHIDVFQDNGYTKEEMKMIQETNKIMGDDSIKVTATTVRIPVIGGHSESVNIEFENEFDLADVRAALAAQEGVVVVDNPANLEYPMPKDAHGKDEVFVGRIRRDETQEKTLNLWVVADNLRKGAATNAVQVAELLSAKGLI
>NZ_LT906468.1|WP_093101180.1|360887_361880_+|hypothetical-protein
MNKRNWLVLLLIGAFAITTFNSCKKEESTDTDSGPTEWEKSIVFTGKPRNLAATFTISDVAYLVGGQMKTNELLSDSYAFDGSSWVKKAEFTGPKRHSAVGFAVAGKGYIGLGYGTDGETSAPFKDFYQYDPATNTWKKVADFPGDARHGAVAFTLGNAAYVGLGKVQATDETFSDFYKYDPATDKWTEIKTSFSNKKGDAYAFVINNVAYVGGGYSNGVPTEDFYSFDGTNWVPKKALNADNKDARRFRAGAFAIGNNGYVVSGRSQSGVVTTVWKYNPSDDSWSDGSQSLPSARENAVSFAIKGKGYITTGNNGTTFFDDTYVFTPVR
>NZ_LT906468.1|WP_093101199.1|373359_373593_+|hypothetical-protein
MDGRIDQDFNQSYRWKIPNTVGAYRIRPPDLNQDEWDKRIDQELVLNQDALRQSSGYRMGGLTKILINHIAGKSPIL
>NZ_LT906468.1|WP_093101201.1|374250_375003_+|glycosyltransferase
MAYPKVSIITIVYNNVRDIGFTLASVDQQTYPNIEYIVVDGKSTDGTMDVIAEYKETINILVSEKDNGIYDAMNKGLALATGDYVLFLNSGDELFAANTLEKIFGNEDNADIYYGETKLINEDREIIGDRRHKTPDHFDWQSFKYGMNVCHQAIYIKRSLTAPYDLQYKLSSDIDWVIRAAQKANKVVNVKDYVAKYLVGGMSQQRHKQSLKERYDIFKKYYGFVPNLINHGVIAMRLVVHRLKHGKTRD
>NZ_LT906468.1|WP_093101203.1|374983_375220_+|DUF3820-family-protein
MAKQETNFLNPNLLVELANSRMPFGKYQGYLLMNLPEPYLAWFKQKGFPPGKIGILLETLYEIKLNGLEYLLKPLVKK
>NZ_LT906468.1|WP_093101205.1|375309_376281_+|rhodanese-related-sulfurtransferase
MAQYQTLLYYCYSPIENAEKFAEDHLEFCKSLGLLGRIIVAEEGLNGTVSGTPEACKAYMEHVHADPRFAKTEFKVDDVEELSFIKMHCRYKEEIVHSGLRNPAEIDPNKQTGKHLEPKDFLAMKDQEDVVILDVRSNYEHNVGRFKNAVTLDIENFREFPEKVKELEHLKGKKILTYCTGGIKCEKASALLLKEGFEDVYQLHGGIIKYGKEAAGEDFEGECYVFDNRVTVPVNSVNPTVVSTCKNCGKITSKMINCANPICNEHFTQCDECGWELDGCCSDACKSHPKKREYDGTGYYVKVPQPVNIEKISKRKHKKLVKN
>NZ_LT906468.1|WP_093101207.1|376366_376708_+|TM2-domain-containing-protein
MDSQKVDMFLMSNNKFFESYQLMEIKDLLTRSDESKYTNVQIQQYKDPTTVLIVSILAGSFGIDRFMIGDTGLGIAKLLTCGGLGIWTIIDWFLIMGATKTKNFEKLITSLNY
>NZ_LT906468.1|WP_093101209.1|376712_377120_+|DUF2752-domain-containing-protein
MRGPRNRLYITTGIVCFFGIVWLLLDYYAAANVTLCPVKLVTGYPCPSCGTTRSISALFNGKIVDAFMINPLGIVSSIIIITVLLLMLLDLLTKRDYYFKVYSRAEKFLQQHKAFSAILVLLIILNWAWNISKGL
>NZ_LT906468.1|WP_093101211.1|377095_377539_+|DUF4870-domain-containing-protein
MEHIEGSLDFSPREITEDEREYASNSYLMSLFALFIGLPLPIFNLLATVIFYLGNRKSTRFVKWHCTQALISQFAIFFFNTVGFWWTLAIIFHKQEVSNAYIAYIILILLLNGIEIVSTIYTSIKTRKGIHVRWFLFSDITDNLLKK
>NZ_LT906468.1|WP_093101213.1|377535_378330_+|M48-family-metallopeptidase
MKILGKFLILAAGIAVCYLLLLQVNWTSLFQVQQNQVRLESKLGKLVLEQVRDLYDVIEDEQIDSTLDSLFIPLLKENYIPTKNYDLLLVESEEVNAFALPDDKIIVTTALINFLDSADYMSAILAHEIAHCEKNHVMRSLITNFGLDLLLSGSGTGEVTNFLTGQAFSRKLEKEADEMAVEYLEEAHIDPNSLMKVMELFDVYLSSDGDVSWISSHPIPTDRKKYLGQKINRIETDPKSYKSPISSKSWSDLQGLVSAYGNQD
>NZ_LT906468.1|WP_093101215.1|378326_381059_-|TonB-dependent-receptor
MKYLLTLCLVLLSCACVLAQVNIAGKVQDKTKGSNLQDASIQLLNLKDSTIRTAKSNEKGDFSIPRVANGNYKLTGTLLGFKKFERNIVVKPSMETLMVGLEPGEIVIEEITIAPPPSVAVKGDTMEFNSRNFATREYADADEMVAQVPGVTIDEDGKVTAHGEEVTKIMVDGKEFFSTDPKVALKTLPADIIDKLQIIDEKSEQTKFSGFDDGKRSKVINIVTKPDKKKGLFGKFNAGKGDSDKFSINSGVNAFRGDEKISINVMANNINETEFSEQGRGGFRRGNNNTDRGLSDTYAAAANYTNTFLDKKMEVNGNYRFRNSSTFTNTLSDIEFTTGSRANQFQNQQQTGNNGNISHNLRGRLKWDIDSMNRIDINPNLSYTKTDLANSSISSMSKDRTEPLNNSNRNFNNNNEALNFGGGMTYMHRFKKAGQTISLSLDGNKSSNEALGKTLAFNQYYKDAVLDRIDTNNRESTTYGYGNGYNGRLSYTYNVSKISRLQANYSMRNTSNYSDRKTMEFLAETGQYEELNDRLSNEFRNDFTHHSAGLSYSYNKQDTFRFQAGMNYEHGYRVNNRTVPINLRTTADFGAFLPELTVAYYFNKERRLEFNYNGATNTPSIDQLQDYIDNSNELFVRNGNPNLSQEYTHRLRLQYRDVNRSNGRSFNSSLNFDYTNNKIINSTMTTDSTITLFEDIILGAGGQYMVPENIDGVFQLRANNNYGLPLKKLGFNLNLNNYMYYNRNYAILNKVLMPNHSYGFSQHVGIFTNFSKKIIIGFNYNLNMNFTNNPMSEITHYRITNHRISNSLNLEFFKNMTLGYNYSFYRNGGIMGAEAISTNLLNASIGYKILKKRNAEISLKAFDLFNNARNVNRRASEISISNITSNTLTRYFLLSLNYNLRSFGGRSDRD
>NZ_LT906468.1|WP_093101217.1|381309_381849_+|TetR/AcrR-family-transcriptional-regulator
MKETTLSRKEKILQTALQLFAIKGYLDTSTKEIAAKAGVSEALIFKHFGNKDALLAHIVKSGYRKVLLHHKGMMTYKGAKDFLKNMVQFPSKLVADDPLFWKLQERLSHHSFSKSQHELFIKPVQPIVHKAFEELGYANPDLETQYLLLIIDMLWKKEACGELENASELASLVEEKYNL

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Crispr_ID: NZ_LT906468_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LT906468_2

619419-619512

Orphan

Consensus_repeat	Method
TTGGTATCCGTGAGCTCCTTCGTTGGTTTGGT	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_LT906468_2

>merge|NZ_LT906468|2|619419-619512|CRISPRCasFinder
TTGGTATCCGTGAGCTCCTTCGTTGGTTTGGTTACTTTTGCGCTTCAAAAGTAACAATAGAATTGGTATCCGTGAGCTCCTTCGTAGGTTTGGT

>NZ_LT906468|2|2|619419-619512|CRISPRCasFinder
TTGGTATCCGTGAGCTCCTTCGTTGGTTTGGT	TACTTTTGCGCTTCAAAAGTAACAATAGAA
TTGGTATCCGTGAGCTCCTTCGTAGGTTTGGT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LT906468.1\|WP_093101637.1\|620602_622672_+\|beta-galactosidase-jelly-roll-domain-containing-protein	unknown	unknown	gnl\|CDD\|236657
NZ_LT906468.1\|WP_093101632.1\|625505_625985_-\|cation:proton-antiporter-regulatory-subunit	unknown	unknown	gnl\|CDD\|223564
NZ_LT906468.1\|WP_093100492.1\|617254_617833_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|377943
NZ_LT906468.1\|WP_093100504.1\|607368_608454_+\|metallophosphoesterase	unknown	unknown	gnl\|CDD\|277344
NZ_LT906468.1\|WP_093100495.1\|614647_615703_+\|4-hydroxythreonine-4-phosphate-dehydrogenase-PdxA	unknown	unknown	gnl\|CDD\|377232
NZ_LT906468.1\|WP_093101635.1\|622681_624184_+\|alpha-L-fucosidase	unknown	unknown	gnl\|CDD\|214829
NZ_LT906468.1\|WP_093100501.1\|610785_611673_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|260130
NZ_LT906468.1\|WP_093101628.1\|628685_629420_+\|LPS-export-ABC-transporter-ATP-binding-protein	unknown	unknown	gnl\|CDD\|213185
NZ_LT906468.1\|WP_093101629.1\|626953_628654_+\|single-stranded-DNA-specific-exonuclease-RecJ	unknown	unknown	gnl\|CDD\|273193
NZ_LT906468.1\|WP_093101638.1\|619591_620383_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906468.1\|WP_093101625.1\|631575_632646_+\|branched-chain-amino-acid-aminotransferase	unknown	unknown	gnl\|CDD\|237363
NZ_LT906468.1\|WP_093101634.1\|624193_625498_-\|cation:proton-antiporter	unknown	unknown	gnl\|CDD\|223551
NZ_LT906468.1\|WP_093100497.1\|613729_614509_-\|16S-rRNA-(adenine(1518)-N(6)/adenine(1519)-N(6))--dimethyltransferase-RsmA	unknown	unknown	gnl\|CDD\|234708
NZ_LT906468.1\|WP_093101631.1\|626058_626838_-\|MBL-fold-metallo-hydrolase	unknown	unknown	gnl\|CDD\|293839
NZ_LT906468.1\|WP_093101626.1\|629444_630962_+\|GH3-auxin-responsive-promoter-family-protein	unknown	unknown	gnl\|CDD\|377019
NZ_LT906468.1\|WP_093100498.1\|612573_613728_-\|FAD-dependent-monooxygenase	unknown	unknown	gnl\|CDD\|168661
NZ_LT906468.1\|WP_093100494.1\|615773_617177_+\|HD-domain-containing-protein	unknown	unknown	gnl\|CDD\|131739
NZ_LT906468.1\|WP_093100500.1\|611637_612564_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|240656
NZ_LT906468.1\|WP_093100503.1\|608688_610605_-\|acetate--CoA-ligase	unknown	unknown	gnl\|CDD\|234677
NZ_LT906468.1\|WP_093100490.1\|617912_618842_+\|tRNA-(adenosine(37)-N6)-dimethylallyltransferase-MiaA	unknown	unknown	gnl\|CDD\|234626

Protein	Function_ID	Function_description	E-value
NZ_LT906468.1\|WP_093101637.1\|620602_622672_+\|beta-galactosidase-jelly-roll-domain-containing-protein	gnl\|CDD\|236657	PRK10150, PRK10150, beta-D-glucuronidase; Provisional.	1.75301e-47
NZ_LT906468.1\|WP_093101632.1\|625505_625985_-\|cation:proton-antiporter-regulatory-subunit	gnl\|CDD\|223564	COG0490, COG0490, Putative regulatory, ligand-binding protein related to C-terminal domains of K+ channels [Inorganic ion transport and metabolism].	2.74601e-49
NZ_LT906468.1\|WP_093100492.1\|617254_617833_+\|hypothetical-protein	gnl\|CDD\|377943	pfam07929, PRiA4_ORF3, Plasmid pRiA4b ORF-3-like protein. Members of this family are similar to the protein product of ORF-3 found on plasmid pRiA4 in the bacterium Agrobacterium rhizogenes. This plasmid is responsible for tumorigenesis at wound sites of plants infected by this bacterium, but the ORF-3 product does not seem to be involved in the pathogenetic process. Other proteins found in this family are annotated as being putative TnpR resolvases, but no further evidence was found to back this. Moreover, another member of this family is described as a probable lexA repressor and in fact carries a LexA DNA binding domain (pfam01726), but no references were found to expand on this.	1.6287e-11
NZ_LT906468.1\|WP_093100504.1\|607368_608454_+\|metallophosphoesterase	gnl\|CDD\|277344	cd07399, MPP_YvnB, Bacillus subtilis YvnB and related proteins, metallophosphatase domain. YvnB (BSU35040) is an uncharacterized Bacillus subtilis protein with a metallophosphatase domain. This family includes bacterial and eukaryotic proteins similar to YvnB. YvnB 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.	4.66092e-20
NZ_LT906468.1\|WP_093100495.1\|614647_615703_+\|4-hydroxythreonine-4-phosphate-dehydrogenase-PdxA	gnl\|CDD\|377232	pfam04166, PdxA, Pyridoxal phosphate biosynthetic protein PdxA. In Escherichia coli the coenzyme pyridoxal 5'-phosphate is synthesized de novo by a pathway that is thought to involve the condensation of 4-(phosphohydroxy)-L-threonine and 1-deoxy-D-xylulose, catalyzed by the enzymes PdxA and PdxJ, to form either pyridoxine (vitamin B6) or pyridoxine 5'-phosphate.	5.25991e-141
NZ_LT906468.1\|WP_093101635.1\|622681_624184_+\|alpha-L-fucosidase	gnl\|CDD\|214829	smart00812, Alpha_L_fucos, Alpha-L-fucosidase. O-Glycosyl hydrolases (EC 3.2.1.-) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families. This classification is available on the CAZy (CArbohydrate-Active EnZymes) web site. Because the fold of proteins is better conserved than their sequences, some of the families can be grouped in 'clans'. Family 29 encompasses alpha-L-fucosidases, which is a lysosomal enzyme responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins. Deficiency of alpha-L-fucosidase results in the lysosomal storage disease fucosidosis.	2.82038e-92
NZ_LT906468.1\|WP_093100501.1\|610785_611673_+\|hypothetical-protein	gnl\|CDD\|260130	cd13967, PT_UbiA_5, UbiA family of prenyltransferases (PTases), Unknown subgroup. Many characterized members of the UbiA prenyltransferase family are aromatic prenyltransferases and play an important role in the biosynthesis of heme, chlorophyll, vitamin E, and vitamin K. They contain two copies of a motif similar to the active site DxxD motif of trans-prenyltransferases and are potentially related. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways. The function of this subgroup is unknown.	4.42886e-20
NZ_LT906468.1\|WP_093101628.1\|628685_629420_+\|LPS-export-ABC-transporter-ATP-binding-protein	gnl\|CDD\|213185	cd03218, ABC_YhbG, ATP-binding cassette component of YhbG transport system. The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.	1.85699e-145
NZ_LT906468.1\|WP_093101629.1\|626953_628654_+\|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].	2.85177e-171
NZ_LT906468.1\|WP_093100500.1\|611637_612564_-\|hypothetical-protein	gnl\|CDD\|240656	cd12179, 2-Hacid_dh_14, Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains. 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.	6.45126e-160
NZ_LT906468.1\|WP_093101625.1\|631575_632646_+\|branched-chain-amino-acid-aminotransferase	gnl\|CDD\|237363	PRK13357, PRK13357, branched-chain amino acid aminotransferase; Provisional.	1.26812e-163
NZ_LT906468.1\|WP_093101634.1\|624193_625498_-\|cation:proton-antiporter	gnl\|CDD\|223551	COG0475, KefB, Kef-type K+ transport systems, membrane components [Inorganic ion transport and metabolism].	4.31788e-54
NZ_LT906468.1\|WP_093100497.1\|613729_614509_-\|16S-rRNA-(adenine(1518)-N(6)/adenine(1519)-N(6))--dimethyltransferase-RsmA	gnl\|CDD\|234708	PRK00274, ksgA, 16S rRNA (adenine(1518)-N(6)/adenine(1519)-N(6))-dimethyltransferase RsmA.	7.52843e-106
NZ_LT906468.1\|WP_093101631.1\|626058_626838_-\|MBL-fold-metallo-hydrolase	gnl\|CDD\|293839	cd16281, metallo-hydrolase-like_MBL-fold, uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain. Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.	9.58789e-32
NZ_LT906468.1\|WP_093101626.1\|629444_630962_+\|GH3-auxin-responsive-promoter-family-protein	gnl\|CDD\|377019	pfam03321, GH3, GH3 auxin-responsive promoter.	2.16954e-161
NZ_LT906468.1\|WP_093100498.1\|612573_613728_-\|FAD-dependent-monooxygenase	gnl\|CDD\|168661	PRK06753, PRK06753, hypothetical protein; Provisional.	2.02742e-134
NZ_LT906468.1\|WP_093100494.1\|615773_617177_+\|HD-domain-containing-protein	gnl\|CDD\|131739	TIGR02692, putative_tRNA_nucleotidyltransferase, tRNA adenylyltransferase. The enzyme tRNA adenylyltransferase, also called tRNA-nucleotidyltransferase and CCA-adding enzyme, can add or repair the required CCA triplet at the 3'-end of tRNA molecules. Genes encoding tRNA include the CCA tail in some but not all bacteria, and this enzyme may be required for viability. Members of this family represent a distinct clade within the larger family pfam01743 (tRNA nucleotidyltransferase/poly(A) polymerase family protein). The example from Streptomyces coelicolor was shown to act as a CCA-adding enzyme and not as a poly(A) polymerase. [Protein synthesis, tRNA and rRNA base modification].	6.12658e-102
NZ_LT906468.1\|WP_093100503.1\|608688_610605_-\|acetate--CoA-ligase	gnl\|CDD\|234677	PRK00174, PRK00174, acetyl-CoA synthetase; Provisional.	0
NZ_LT906468.1\|WP_093100490.1\|617912_618842_+\|tRNA-(adenosine(37)-N6)-dimethylallyltransferase-MiaA	gnl\|CDD\|234626	PRK00091, miaA, tRNA delta(2)-isopentenylpyrophosphate transferase; Reviewed.	1.13515e-139

>NZ_LT906468.1|WP_093100490.1|617912_618842_+|tRNA-(adenosine(37)-N6)-dimethylallyltransferase-MiaA
MSTELNRQKTLIVVVGPTAVGKTALAIQLANHFKTSIISADSRQFYQEMSIGTAKPNAEELAQANHYFINSRSIAEDYTAGDFEREALVRLAVLFKSTDVVIAVGGSGLFVRALTEGLDDLPKAGEEIRDKLNEWFRNEGLEPLKQRLQEIDPAYYDKADIDNPQRVIRAIEVFEASGKPISYFMNKQKTERPFQVITIGLNTDREWLYNRINQRVDLMMEAGLLEEVKSLLPFRNKPALLTVGYAEIFEYLDGKISLEDAVSQIKQNSRRYAKRQITWFKKYGNTVWFEPQAKDEIFAYLDQTLKNKG
>NZ_LT906468.1|WP_093100492.1|617254_617833_+|hypothetical-protein
MAIYRFRVTFEDYEDVYREIDMPSKSTFLDLHTQIQKSTGYDQERSSSFYVSNDQWKKGTEIAYLPNERKKAAGVLIVEDVRLSKFIDDPHQKFYYTYNFDRPYDFHVELIKILKEEEGKEYPALFKKIGEAPRNLTAANFPVTADDEDDDEFVPEDAEEYGVDEEDDYDMFDDEEGEESEGESNKSNEEDY
>NZ_LT906468.1|WP_093100494.1|615773_617177_+|HD-domain-containing-protein
MSENLSHPIFSIIRELAHQEGVSCFVIGGYVRDRIMGRPFKDDIDILVLGSGIDFANKLGEKLHTKVAVYKSFGTAMLVYEGLQVEFVGARKESYRKDSRKPIVEDGTLEDDQNRRDFTINAMAFSLNESNYGELIDPFQGLNDIQNRLIKTPLSPDITFSDDPLRMMRAIRFATQLNFRIDSTALNAISENADRIQIISKERITDELNKIILAEKPSIGFKYLFDTGLLERIFPAMYQLYGVEYVDGKGHKDNFYHTLEVLDNVAEMSNDLWLRWAAIMHDIAKPATKRFDKKVGWTFHGHEDRGAKMVPKLFAELKLPLNEKMKFVQKLVMLHLRPIVLAKDIVTDSAVRRLLFEAADDIDDLMLLCHADVTTKNEYKKRKYRDNFELVKQKLKDVEERDHLRNWQPPVDGDDIMKTFGIGPGKHVGIIKKAIREAILEGEIPNSRQEALSLMIEKGKTLGLTKV
>NZ_LT906468.1|WP_093100495.1|614647_615703_+|4-hydroxythreonine-4-phosphate-dehydrogenase-PdxA
MSEKLKIGISVGDINGIGLEVIIKSLMDNRVMDFFTPIVYGNTKVASFHRKAIGVNDFSFNVINSADQANPKRPNMINCWQEDVKISLGEQNEIGGKYAFVSLQKATEDLKAGLIDALVTAPINKHNIQQEGFNFPGHTEYLQNAFEAKDVLMFMVSDDLRVGVVTGHIPVKEVAASITEESILHKLRMMNESLKKDFWIQKPKIAVLGLNPHAGDDGLIGTEDRDIIKPAIEKANEEDIFCFGPFPADGFFAADAYTKFDAVLAMYHDQGLIPFKHIAARNGINFTAGLPVVRTSPDHGTGYDIAGKNLASHASFLEAIFEAVHIVNRRREQEVLTENPLAFRRLSKDRD
>NZ_LT906468.1|WP_093100497.1|613729_614509_-|16S-rRNA-(adenine(1518)-N(6)/adenine(1519)-N(6))--dimethyltransferase-RsmA
MGSVRAKKHLGQHFLNDKNAAQRIVDALTPSLGFKQVLEVGPGMGVLSDFLLQNEAYETFLIDVDDESIEYLADKYPELGNRLIHGDFLNLDFSQYFGEKMAVIGNFPYNISSQILFKVLEERNRVVEMVGMFQKEVAERCVAKPGNKEYGILSVFLQAYYDVSYLFTVKAGAFNPPPKVLSGVMRMVRNNRETLDCDEKLFWRVVKAGFNQRRKTLRNALSAVVPKDRMSDNPLYELRAERLSVQDFEILTNEISKSL
>NZ_LT906468.1|WP_093100498.1|612573_613728_-|FAD-dependent-monooxygenase
MEVQREFTIIGAGVAGLTAAIALQNLNREFTLFEQSKAIKGIGAGFGLAANAMHALEYIGIREEVEEIGYYLDSFAILDQKGNILVNPNTTKLSDKYEQKNFAIHRADLHLYLLSKVKQESIALGKKACNLLQKSDYVEIQFEDGSSHRTKYLIIADGVKSPLRQKLLPASKPRYAGYSCWRATIDNSDLQLKRGSETWGNKGRFGLTPLVNQRIYWYACINGPQQNPVFRDYKVQDLKRQFGNYHQPIQEVLDKTLDADLIWSDIIDIQPIKNFAFGNILIIGDAAHACTPNMGQGACQAMEDVAVLHNELQNEQSVEQAFLAFEKRRLARTKYITDTSKLIGDVAQWENKFLISIRNNLMKIMPDSMNQKSLIKLFKEDFMK
>NZ_LT906468.1|WP_093100500.1|611637_612564_-|hypothetical-protein
MNILIVDDIHEVLLQKLGRAAIAYSYQPDFSRADAEKAIVDYDGLIIRSKFQVDKEFIDLNPNLKMIGRAGAGMDNIDEAYANSKGIKLIPANEGNRDAVGEHMIGMLLSLMNNLNRGDREVRSGEWKREENRGHELKGKTVALIGYGHNGQAMAKKLSGFDVKVIAYDKYKTGFSDLYATEVSMEEVVRRADVLSFHIPLTRETRGMVDDEYLFHFRKPIFFLMGARGGIVKIPAVLKKLDEGKIIAAAFDVLPVEKFPALAEEAWYEDLIKRDNVLLSPHVAGWTFESYYKLSEVLADKVIAYEYQ
>NZ_LT906468.1|WP_093100501.1|610785_611673_+|hypothetical-protein
MTSVLKRIYYFLVHTNLLIALAAVAQCALTYYILQFPVNNDILIIEGATTLLLYNLSLYLSLPKDPSKSPFQRTRWIGKNMWLFWLLSGLSVLVTVWTLLHVHILTLFFLGFIGAMSLAYAVPLIKINDRWVGMRQIPGLKVFYIALVWSLSSVGLPVVELFANGEQIDWYAANYLGLVKIVFLVLCTLPFDIRDFEQDSLYNLKTVPILLGKQRAINLSYGIGVFHLILILLSPNTWGVKIGLLITTILILIMFRIIIFSKEKHYHHVYLLDLALVLQWFFVWLLILVSNNLVG
>NZ_LT906468.1|WP_093100503.1|608688_610605_-|acetate--CoA-ligase
MNFQLKSFEEYQEAYKRSVEEPEAFWSDVADHFFWKRKWNNVLNWNFRDPDINWFEGAKLNITENCLDRHIYKLGDQPAIIWEPNDPNEAHRILTYKQLLQKVEQFANVLKNNNIRKGDRVCIYLPMVPELVIAVLACARIGAIHNVVFGGFSARSIADRINDAECKLVITSDGGFRGQKILELKSIVDDALMQCDTVEKVIVLTRTRTPVSMIKGRDVWWEDEIKKVETQGNPACPAEEMDAEDTLFILYTSGSTGKPKGVVHSTAGYMVYTGYTFANTFQYQPGEVFFCTADIGWITGHSYIVYGPLSQGATSLMFEGIPTYPDASRFWDIVDKYKVNILYTAPTAIRSLMAFGDDFLEGKDLSSLRVLGTVGEPINEEAWNWYHDKVGHGKCPIVDTWWQTENGGHLITPIAGITKEIPGYAMLPLPGIQPCLMDENGEEIKGNDVSGNLCIKFPWPGMLRTTWGDHERCRQTYFSTYQDMYFTGDGCYRSPEGYYRITGRVDDVLNVSGHRIGTAEVENAINMHSDVVESAIVGYPHPVKGQGIYAYVIANHHIDAEKTRQDILQTVTRIIGAIAKPDIIQFVTDLPKTRSGKIMRRILRKVAEGELSNLGDTSTLQDPTVVEAIIEGAKEMKK
>NZ_LT906468.1|WP_093100504.1|607368_608454_+|metallophosphoesterase
MNLKSISVLSTLLALLLFSQQLIAQQSYVKPKLTNSKSWSLVLIPDPQTYVKYDRNVGILNLMTSWVRENADSLNTQFVLCTGDLVEQNDLLNPDTKAANQNSKQQWTNTSEAFRKLDNRVPYVLATGNHDYGHVSAEYRATQYDKYFSPEQNGFNAKALREVGPSLNGNSSAVNAVYEFETPHPKKLLVMVLEFAPRNEVLAWAKKTLDQQKYENHDVILLTHTYLDSKSNHIQKEGYKIEDANYGAAVFEKLVKPSKNIRMVFSGHIGDPDNFDGHIGFRQDKNAAGKTVSQMTFNAQAMGGGWFGNGGDGWLRYLEFLPDGKTVKVKTFSPLFAISPATQNLAYKTEKNQEFQFSLED
>NZ_LT906468.1|WP_093101638.1|619591_620383_-|hypothetical-protein
MKKKIRIPFVVLLSLVLAFAISSCSKDDKDDEIEIVEDLPGKIPGLGNTDGEPTGQKYSLPEGIELQGEITGYEGDYNTTARASAKKAMVAKRASNLKAEVAADLSPDFSRGSGYFVRLGIKLKNSTSSTKKLELPAGLIIKSRTGDYQNGVLLKKVSIDIPANKTIYLDLHMYCGNESKYASSETEKYDFAVISNSSSLHDLINRLKNKKINIEQYFKNNQVDQNYNAITGKLQDILWTITDTEKGLQEDDIKYINEYLPND
>NZ_LT906468.1|WP_093101637.1|620602_622672_+|beta-galactosidase-jelly-roll-domain-containing-protein
MMVGLLANSIGFAQSRMEKSFNEGWKFYKANNSTFFTDFENGQKYFENQGQWTKLEIWEDITLPHTYNKDDMQKDRNFFEGKAVYQKTFHPDEADKNRRTFLKFEGVGAVAQLFVNGNYIGEHKGGYSMFVFEISNSIEYGKDNSITVIADNKSRKDIIPINHFLFPVYGGIYRPVHLITTNKTNFVVTDQAAPGIFIRQKNVSSKSADIQVEAKLETKEKTIQEVELSLEIKDDQGKTVETQKYPVKISPQGVTYVNETIKMKSPHLWDGIRDPYLYSLTAKITANGKELDAVKQPLGIRHIEMIANKGVFLNGKKYPMYGVTRHQDREGFGSALSFEQHKEDMMLIKEMGATTIRLAHYQQSPQMYALADSIGFLTWAEIPFVNRVSYYENDNAKQQMVELVKQNFNHPSIYIWGVHNEVYSKTADEQVPVLSRELNDIAKTLDPDRYTVAVTGYNVIDRQENLSTDVQGINHYFGWYGGKIEDLGPWAQKVQKDFPEYKIILSEYGADGNIDIGKEEVEAPKDVISGKAFPENYQTETHIQQWAAIEKNPIILASYLWNSFEFAVPAWNRGGVNARNLKGLITFDRKRKKDSFYWYKANWNPEPMIYLANRRDSIRTHKNSKIQLFSNLSKVQLIVNGKEYQAKQGVNSKHWVVDNVELKQGENKIQAKGNSGNEVLTDEMTWTLQ
>NZ_LT906468.1|WP_093101635.1|622681_624184_+|alpha-L-fucosidase
MKSILKTICVAVLGLIFSQDSYGQWTGPKVKPTKHTEVKYGSLTPEHRTDANMEAFRNYGLGQFIHWGLYAIPGNEWEGVSARKGAAASEWIRTWSGPTAPKNWKETYDNLYKKFDPKDFDAKQWAKQAKDMGAKYMIFTTKHHDGFALWPTKYSGYNITKSPYKKDIVKEVVDAYTAEGIDVYLYFSILEWNNPDYLSKEPKTEDEKKKYDRFLQYTKNQLLELLANYPQIKGFWFDGTWDQSWVKAYDFTYNLEKELRAKHPGLIIGSRFRNDEHGKRHFDSNGKILGDYEQGWERKLPQEFEWLDGNDWDAVMTIPPNGWGYMKDWSGIYTKTTDDLLDMLMHTVSLNGNFVLNFGPDGQGLMHPEEDKIAKELGDWMKVNGEAVYGVRHADLPKTKLGYLTQKDKNLYLTVFNRPVNNIARIAIPKKATEVPVEAVLLSNGQKLQVKHSDIGLDLDKNTYYDVIIPADFKAERAFVIKMTTGAPATKSEKLMDAKM
>NZ_LT906468.1|WP_093101634.1|624193_625498_-|cation:proton-antiporter
MHSNLIIEIGIAVLLVASVGLLANRLKFSVIPFFIVIGMVLGNQSYPKFIADFLASVNNEGLTSTVDSVWSFLTFTESKPFIDFMGRLGVLFLLFYLGLEFSVGRLIKSGKSIVAGGSIYVVLNFFSGLLVGWMMNLPFKEMMVLCGIMTSSSTAIVAKVLTDLKRTANPETEVIMGMIMFDDLFIAMHISFLSGLILTGGGSFWTVAGTSLLALGFILSFLILGRKLVPFIDKLLQEKSSELFILIIFSLLFVIAGFSETIHVAEAIGALMAGLVFADSKYLKKIEGMVLPFKDFFGAMFFFSFGLSIDMYSLGGAVGWATFAAAITVVGNVASGYFASRFSGLKPKNSVDIGFTLSARGEFSIIMANIGKAGKLLPVIQSFVVVYVLILSIISPLLTKESRKIWNKLAGQDDTVKKPKKKLSDLEASVQEKN
>NZ_LT906468.1|WP_093101632.1|625505_625985_-|cation:proton-antiporter-regulatory-subunit
MSIVRESDLIGIGKKYQIETDAGDNMVVVIHDDGRRELYRHEDDDNETHCVMTLSDEESRQVAGILGGLSYKPKALETIEVALDDLRIEWYKVGESNDGVNKSIGQLEVRQRTGASIIAAIREEETIINPGPDYVITPGTTLVIAGKQKNIKLLKEILL
>NZ_LT906468.1|WP_093101631.1|626058_626838_-|MBL-fold-metallo-hydrolase
MARAHSLFEGSYSVDISKQFIPFDPKKDDPKDRPGSLFIHVHPFLIETKDGLIVLDTGLGLRNENNELVIHENIKKLGFSIDDVRYVLMSHLHKDHASGMVDIKDGVKRLAFPNAEYVIQEQEWEAAYSSESPSYRTEVFDVLQRSGNILFVNGDGQLTPEIRYELSGGHSEFHQVFHVETEGEHFFFGGDELPEPEEIFRSFIAKYDFDGRKARDLRAKYWAAGAPEGWVFLFYHSKNIAVGRPEQKPDGSYKIVNAE
>NZ_LT906468.1|WP_093101629.1|626953_628654_+|single-stranded-DNA-specific-exonuclease-RecJ
MQKRWVLKPKKNVEQAKKLQQELGVNHIIAELLINREVETFDQAKDFFRPSLDHLHDPFLMKDMDRAIDRIERAIGNKEKILIYGDYDVDGTTAVSVVYSFFRDFHTGLEFYIPDRYAEGYGISNKGIDYAKENGFSLIIALDCGIKAVDKIEYANAKGIDFIIGDHHLPGDILPNAVAVLDPKRVDCPYPYKELSGCGIGFKIIQAFIKQNKMSMDLAYQYLDLVAVSIASDIVPITGENRILTHFGLKKLNSNPCCGLQALINLSTHKSGHFTVNDIVFQIGPRINAAGRIDHAKDAVKLLIAKTLPEARVFSASVDDQNKARKDFDLKITKEALDLLDNNVHLQTRNTTVLYKEDWHKGVIGIVASRLTERYYRPTIILTNTNGHIAGSARSVLGFDLYEALSECSDLLDQYGGHKYAAGLTMPTDNIGLFQQRFEEVVSKSIKPEMLQQEVSIEKEIRLSEIDPKFYRILSQFQPFGPQNEAPTFLCRGVTMGNNANVVGSTHLKFSVKQEDSAIFECIGFGLGEFAELINSGKPFDICFSIEENSWRGKKNLQLNVKAIRF
>NZ_LT906468.1|WP_093101628.1|628685_629420_+|LPS-export-ABC-transporter-ATP-binding-protein
MILRAEHLIKKYKQRTVVNDVSFHVEQGEIVGLLGPNGAGKTTSFYMIVGLIKPNDGHVYLDDLEITQDPMYKRAQRGIGYLAQEASVFRKLSVENNILAVLEIHYPNKEERKAKLEELLTEFSLHRVRKNRGDLLSGGERRRTEIARALAANPNFILLDEPFAGVDPIAVEEIQTIVAKLKTRNIGILITDHNVQETLSITDRAYLLTEGKIMLTGTPEEIADNELARKFYLGRHFELRRKKF
>NZ_LT906468.1|WP_093101626.1|629444_630962_+|GH3-auxin-responsive-promoter-family-protein
MALLNSLFTWIMKKRMHQIDLFMKYPHDVQDEWFQSLVSAAEATEWGKKYGYNSIFTPDEFKERVPIQDYDDIKGYVDRMIKGEQNILWPSDIKWFAKSSGTTSDRSKFIPVSIEALEECHYQGGKDMLSIYCHNKPENKVFTGKSVVIGGSSQINNFSPDSYYGDLSSILIRNLPFWAEFKRTPNIEVTLNPNFEEKIEQIAQITIKENVTSLAGVPTWNMVMANRILEITGKDNLLEVWPNLEFYSHGGVSFKPYREQFKKLIPSDNMYYLENYNASEGYFGLQDRSDSEDLLLMLDYGIYYEFLPMDQINEEHPKTLCLHEVELGKNYALIISTNAGLWRYKIGDTIRFTSLSPYRFQISGRTKQYINTFGEEVIVDNADQALQVACKATGATIQDYTAGPVYFNDKTAGAHEWIIEFEQEPDDFQRFGEILDATLREINSDYDAKRYKNMALSFPIIHNAAKGSFYTWMKSRGKLGGQNKVPRLANSREYLEPLLKLIQAS
>NZ_LT906468.1|WP_093101625.1|631575_632646_+|branched-chain-amino-acid-aminotransferase
MSAIDNFTIQVEPTQQSRISQVDFDHLVFGKIMSDHMLVANYDNGQWEDVKIVPYGNLSVSPSMSALHYGQAIFEGIKGYKFQDGTVSIFRPDKNWERFNKSAKRLEMPEVPQEIFLDGLKKLLDVDRNWIPSKEGTALYIRPFMFGTEAALGVHPSKSYQFIIITCPVGAYYSKPISLKVETHYTRAAEGGVGFSKNAGNYALSLYPTQLANNEGYDQIMWTDALEHKYIEEAGTANLIFRIGDTIITPHGDTILHGVTRRTIMELAEKWGYKAEQRKVSVKELIDGIEAGDVTEAFAAGTAATITHIDRIGFNGQDYTLPPVEGREFSNKVLAYLNELRYGKIDDPFGWNYIVK

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Crispr_ID: NZ_LT906468_3

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LT906468_3

946591-946666

Orphan

Consensus_repeat	Method
AAATATTTCACCCACCCTGTGGGTT	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_LT906468_3

>merge|NZ_LT906468|3|946591-946666|CRISPRCasFinder
AAATATTTCACCCACCCTGTGGGTTCGCCTTTTCAAACATCCAAATTCTACAAATATTTCACCCACGCTGTGGGTT

>NZ_LT906468|3|3|946591-946666|CRISPRCasFinder
AAATATTTCACCCACCCTGTGGGTT	CGCCTTTTCAAACATCCAAATTCTAC
AAATATTTCACCCACGCTGTGGGTT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LT906468.1\|WP_093098691.1\|952007_952889_+\|ATP-synthase-F1-subunit-gamma	unknown	unknown	gnl\|CDD\|376304
NZ_LT906468.1\|WP_093098669.1\|933876_934794_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906468.1\|WP_093098678.1\|940725_942621_-\|type-IIA-DNA-topoisomerase-subunit-B	unknown	unknown	gnl\|CDD\|235501
NZ_LT906468.1\|WP_093098681.1\|943795_946000_+\|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|350795
NZ_LT906468.1\|WP_093098679.1\|943179_943686_-\|phosphoheptose-isomerase	unknown	unknown	gnl\|CDD\|380343
NZ_LT906468.1\|WP_093098690.1\|950280_951855_+\|F0F1-ATP-synthase-subunit-alpha	unknown	unknown	gnl\|CDD\|236448
NZ_LT906468.1\|WP_093098672.1\|935745_936510_+\|ATP-binding-cassette-domain-containing-protein	unknown	unknown	gnl\|CDD\|213228
NZ_LT906468.1\|WP_093098676.1\|939829_940672_-\|formyltetrahydrofolate-deformylase	unknown	unknown	gnl\|CDD\|235676
NZ_LT906468.1\|WP_093098688.1\|949676_950222_+\|ATP-synthase-F1-subunit-delta	unknown	unknown	gnl\|CDD\|365949
NZ_LT906468.1\|WP_093098684.1\|947724_948810_+\|F0F1-ATP-synthase-subunit-A	unknown	unknown	gnl\|CDD\|237381
NZ_LT906468.1\|WP_093099062.1\|953540_954185_+\|sterol-desaturase-family-protein	unknown	unknown	gnl\|CDD\|178053
NZ_LT906468.1\|WP_093098670.1\|935004_935739_+\|ABC-transporter-permease	unknown	unknown	gnl\|CDD\|376777
NZ_LT906468.1\|WP_093098667.1\|931847_933848_-\|(E)-4-hydroxy-3-methylbut-2-enyl-diphosphate-synthase	unknown	unknown	gnl\|CDD\|179361
NZ_LT906468.1\|WP_093098685.1\|948848_949040_+\|ATP-synthase-F0-subunit-C	unknown	unknown	gnl\|CDD\|349414
NZ_LT906468.1\|WP_093098693.1\|954243_955293_-\|ketoacyl-ACP-synthase-III	unknown	unknown	gnl\|CDD\|236475
NZ_LT906468.1\|WP_093098675.1\|937816_939598_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906468.1\|WP_093098687.1\|949148_949649_+\|F0F1-ATP-synthase-subunit-B	unknown	unknown	gnl\|CDD\|184695
NZ_LT906468.1\|WP_139185476.1\|947230_947635_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906468.1\|WP_093099061.1\|947064_947238_+\|AtpZ/AtpI-family-protein	unknown	unknown	gnl\|CDD\|378198
NZ_LT906468.1\|WP_093098673.1\|936571_937516_+\|class-I-SAM-dependent-methyltransferase	unknown	unknown	gnl\|CDD\|224017

Protein	Function_ID	Function_description	E-value
NZ_LT906468.1\|WP_093098678.1\|940725_942621_-\|type-IIA-DNA-topoisomerase-subunit-B	gnl\|CDD\|235501	PRK05559, PRK05559, DNA topoisomerase IV subunit B; Reviewed.	0
NZ_LT906468.1\|WP_093098681.1\|943795_946000_+\|helix-turn-helix-domain-containing-protein	gnl\|CDD\|350795	cd18037, DEXSc_Pif1_like, DEAD-box helicase domain of Pif1. Pif1 and other members of this family are RecD-like helicases involved in maintaining genome stability through unwinding double-stranded DNAs (dsDNAs), DNA/RNA hybrids, and G quadruplex (G4) structures. The members of Pif1 helicase subfamily studied so far all appear to contribute to telomere maintenance. Pif1 is a member of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.	5.86772e-48
NZ_LT906468.1\|WP_093098679.1\|943179_943686_-\|phosphoheptose-isomerase	gnl\|CDD\|380343	cd02213, cupin_PMI_typeII_C, Phosphomannose isomerase type II, C-terminal cupin domain. This family includes the C-terminal cupin domain of mannose-6-phosphate isomerases (MPIs) which have been classified broadly into two groups, type I and type II, based on domain organization. This family contains type II phosphomannose isomerase (also known as PMI-GDP, phosphomannose isomerase/GDP-D-mannose pyrophosphorylase), a bifunctional enzyme with two domains that catalyze the first and third steps in the GDP-mannose pathway in which fructose 6-phosphate is converted to GDP-D-mannose. The N-terminal domain catalyzes the first and rate-limiting step, the isomerization from D-fructose-6-phosphate to D-mannose-6-phosphate, while the C-terminal cupin domain (represented in this alignment model) converts mannose 1-phosphate to GDP-D-mannose in the final step of the reaction. Although these two domains occur together in one protein in most organisms, they occur as separate proteins in certain cyanobacterial organisms. Also, although type I and type II MPIs have no overall sequence similarity, they share a conserved catalytic motif.	1.48785e-15
NZ_LT906468.1\|WP_093098690.1\|950280_951855_+\|F0F1-ATP-synthase-subunit-alpha	gnl\|CDD\|236448	PRK09281, PRK09281, F0F1 ATP synthase subunit alpha; Validated.	0
NZ_LT906468.1\|WP_093098672.1\|935745_936510_+\|ATP-binding-cassette-domain-containing-protein	gnl\|CDD\|213228	cd03261, ABC_Org_Solvent_Resistant, ATP-binding cassette transport system involved in resistant to organic solvents. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.	2.07458e-111
NZ_LT906468.1\|WP_093098676.1\|939829_940672_-\|formyltetrahydrofolate-deformylase	gnl\|CDD\|235676	PRK06027, purU, formyltetrahydrofolate deformylase; Reviewed.	2.91991e-133
NZ_LT906468.1\|WP_093098688.1\|949676_950222_+\|ATP-synthase-F1-subunit-delta	gnl\|CDD\|365949	pfam00213, OSCP, ATP synthase delta (OSCP) subunit. The ATP D subunit from E. coli is the same as the OSCP subunit which is this family. The ATP D subunit from metazoa are found in family pfam00401.	2.20756e-52
NZ_LT906468.1\|WP_093098684.1\|947724_948810_+\|F0F1-ATP-synthase-subunit-A	gnl\|CDD\|237381	PRK13419, PRK13419, F0F1 ATP synthase subunit A; Provisional.	5.2478e-72
NZ_LT906468.1\|WP_093099062.1\|953540_954185_+\|sterol-desaturase-family-protein	gnl\|CDD\|178053	PLN02434, PLN02434, fatty acid hydroxylase.	6.95561e-54
NZ_LT906468.1\|WP_093098670.1\|935004_935739_+\|ABC-transporter-permease	gnl\|CDD\|376777	pfam02405, MlaE, Permease MlaE. MlaE is a permease which in E. coli is a component of the Mla pathway, an ABC transport system that functions to maintain the asymmetry of the outer membrane. In NMB1965 it is involved in L-glutamate import into the cell. In Arabidopsis thaliana TGD1 it is involved in lipid transfer within the cell.	2.25707e-64
NZ_LT906468.1\|WP_093098667.1\|931847_933848_-\|(E)-4-hydroxy-3-methylbut-2-enyl-diphosphate-synthase	gnl\|CDD\|179361	PRK02048, PRK02048, 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase; Provisional.	0
NZ_LT906468.1\|WP_093098685.1\|948848_949040_+\|ATP-synthase-F0-subunit-C	gnl\|CDD\|349414	cd18121, ATP-synt_Fo_c, membrane-bound Fo complex of F-ATP synthase, subunit c. Subunit c (also called subunit 9, or proteolipid) of the Fo complex of F-ATP synthase. The F-ATP synthase (also called FoF1-ATPase) consists of two structural domains: the F1 (factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha, beta, gamma, delta, and epsilon subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons though the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Methanosarcina acetivorans.	4.22008e-09
NZ_LT906468.1\|WP_093098693.1\|954243_955293_-\|ketoacyl-ACP-synthase-III	gnl\|CDD\|236475	PRK09352, PRK09352, beta-ketoacyl-ACP synthase 3.	1.17388e-158
NZ_LT906468.1\|WP_093098691.1\|952007_952889_+\|ATP-synthase-F1-subunit-gamma	gnl\|CDD\|376304	pfam00231, ATP-synt, ATP synthase.	1.2161e-129
NZ_LT906468.1\|WP_093098687.1\|949148_949649_+\|F0F1-ATP-synthase-subunit-B	gnl\|CDD\|184695	PRK14471, PRK14471, F0F1 ATP synthase subunit B; Provisional.	1.22663e-53
NZ_LT906468.1\|WP_093099061.1\|947064_947238_+\|AtpZ/AtpI-family-protein	gnl\|CDD\|378198	pfam09527, ATPase_gene1, Putative F0F1-ATPase subunit Ca2+/Mg2+ transporter. This model represents a protein found encoded in F1F0-ATPase operons in several genomes, including Methanosarcina barkeri (archaeal) and Chlorobium tepidum (bacterial). It is a small protein (about 100 amino acids) with long hydrophobic stretches and is presumed to be a subunit of the enzyme. It carries two transmembrane helices and is a magnesium or calcium uniporter. The atp operon of alkaliphilic Bacillus pseudofirmus OF4, as in most prokaryotes, contains the eight structural genes for the F-ATPase (ATP synthase), which are preceded by an atpI gene that encodes a membrane protein with 2 TMSs. A tenth gene, atpZ, has been found in this operon, which is upstream of and overlapping with atpI.	5.07739e-07
NZ_LT906468.1\|WP_093098673.1\|936571_937516_+\|class-I-SAM-dependent-methyltransferase	gnl\|CDD\|224017	COG1092, COG1092, Predicted SAM-dependent methyltransferases [General function prediction only].	6.13724e-36

>NZ_LT906468.1|WP_093098681.1|943795_946000_+|helix-turn-helix-domain-containing-protein
MSQAFDTQNDIFAKAVAFVNQTQQPIFLTGKAGTGKTTFLKFIRENSYKKMAITAPTGVAAMNAGGTTLHALFWLPFGVFIEDYPLQWGESDQFIYNKHRLFSTIKLTKNRRAILQELELLVIDEVSMVRADTLDAIDVILKSVRRDMRPFGGVQVLFIGDLYQLPPVVQDREWQVLRDYYSSVFFFDAKVFKQQPPVLIELQKIYRQQDSAFINILNKIRNNETTNSDLDELNTHYKPDFIAPEGEQYITLTSHNRLADQINQEKLESLETKLHQIKSIIKDEFQNGLFPAEETLSLRVGAQVMFIKNDVGDERRYFNGKIGTVKDIQVEKHKIIVSFPNGEEDVEVKRETWENIRYSYNKGDDKIEEEVLGTFSQFPLRLAWAITIHKSQGLTFEKAIIDAGTSFAAGQVYVALSRLTGLEGLVLRSRVPSYAIRTDFQVVSFMKQMEAITDLDPILQEAQKRYLGQILLQSFRWNQMCEELESLIVEQEGKKIEGKDEAVAFLKDMLGKLKAQEIVANKFITQLYKMLGQVEIDYEKICERSKAAVSWFIPTFEKECLMPMEKHIEAWVVKKRTKKYVATLKSILLDFKRKHEQLKHSLTIAEALNKSSDELTEELLQWNKPKENLEKEVEEKEKDTKQISLDMFMDGMDIEEIATKRDMVVGTIYGHLINFIGSDIEASDLIPDAELQNIVKVIKAHPDASATELRTLMDMKVDYPQIKIAQKYLEVAGK
>NZ_LT906468.1|WP_093098679.1|943179_943686_-|phosphoheptose-isomerase
MTYIDKSELFQEISTKLTNKGFKIESEDQNRPWGGFFVINEDQAQEFADAYFEGLNVQDLKISGKLSPKVLIVGPNKRLSWQYHHRRAEIWRVIRGEVGVVTSPTDEEHELKILKEGDSIRLSQGERHRLVGLGSYGVVAEIWQHTDSANPSDEEDIVRVQDDFGRGV
>NZ_LT906468.1|WP_093098678.1|940725_942621_-|type-IIA-DNA-topoisomerase-subunit-B
MSTYNEDSIRSLDWKEHIRLRPGMYIGKLGDGSAYDDGIYVLLKEVVDNSIDEFVMGAGKIIDITVNENRVTVRDYGRGIPIGSVVDVVSKINTGGKYDSKAFQKSVGLNGVGTKAVNALSNQFSVQSYRQNVTRIAQFSKGELVSDEQKDTTQRNGTSVTFYPDDSIFRNYKYRLEFVENMIWNYVFLNSGLTINFNGQRFISENGLKDLLERNVDTEGMRYPIIHLKGDDIEIAMTHGQQYGEEYYSFVNGQHTTQGGTHQAAYREAVVKTIREFYKKEFDASDVRASIIGAIAIKVQEPVFESQTKTKLGSQSVGPDGPTVRTFINDFVKKALDDYLHKNPATADALQKRIMQSERERKDIAGIKKLANERAKKASLHNRKLRDCKVHFSDKHERNLETTLFITEGDSASGSITKSRDVYTQAVFSLKGKPLNSYGLTKKIVYENEEFNLLQHALNIEDGIEGLRYNNIVIATDADVDGMHIRLLLMTFFLQFFPELVKAGHVSILQTPLFRVRNKKETIYCYSDEERVNAIKKLGAKPEITRFKGLGEISPSEFGMFIGENIRLEPVILSKDNKLPQLLEYYMGKNTPDRQVHIVNNLRVELDTEDDLVTTKDGVEEAAIESIQEAV
>NZ_LT906468.1|WP_093098676.1|939829_940672_-|formyltetrahydrofolate-deformylase
MNTQTLILIQCTDAVGLVAIISNVLAEQELNIVSMREFVDEANKKFFVRVVCAGELYHKEVLQQAFTDRLPSNSQVMINPDQRKRLVVLVTKEHHCLADILVRNYFGTFQAEVLAVVGNYDNLQEFTEKFNLPFHYISHENKSKEQFEEELAEVVSSYHADYIVLAKFMRILSPTFVSKFKGKLINIHHSFLPAFIGANPYKQAHDRGVKIIGATAHFVTDDLDEGPIIVQNTKSVDHSYDVSGMRTAGTEIEKAVLSRAIQLLSEDRVMLHGNRTIVFK
>NZ_LT906468.1|WP_093098675.1|937816_939598_-|hypothetical-protein
MTHSFHIPVLGLAFSIDTPIKVAQFGISSVISIVDDELIERMREYYSKKYELAFEAISKKHADYRATRICKYLDLVQDLVSEQVERLKRVDWKEDKEAQRYFELLPESHPSKENYARWKSLKHGYEKHLVANDIREAMVAGEIDVNIMSKVDKINRDADGNELPEVFSDASAAVRGFAMSKLQSSLVLSAGMNPRLYAYLSELGTFFPDADGNFKKKITLKVSDYRSALIQAKYLAKRGIWISEYRIESGLNCGGHAFATDGFLLGPILEEFKNNKEALIADIFPLYQQALQDLGLNSENAPAIKFSVQGGVGTSQEHSFLLDYYNMDAVGWGSPFLLVPEATTVDEETLNNLATATADDFYISQASPLGVPFNNFRKSTAELNRLKRIEQGKPGFPCTKKYLVSDTSNSTEPVCTASRVYQLNKINELKQQELDEASYQLAYNKIVEKQCLCEGLAAPAYLKYGILKPRERDAVAICPGPNTAYFNKVYSLKEMVDHIYGRINVLNDVNRPSFFINELDLYVKHLAGYINENLSNLDVKKQKYIQKFHTQLLDGISYYRSLQSKVNSAFGESKTAFYEQLNRLESQLSPLNV
>NZ_LT906468.1|WP_093098673.1|936571_937516_+|class-I-SAM-dependent-methyltransferase
MFYERLLWSFKYCNLNNDTQIQLLTPQHWKDYELIDCGDFEKLERFGELILIRPEPQAVWPKALGDAEWNKRYHIKFKGRSATSGDWMKKNPKTPDRWHIQYKNEDVAIKFRLGLTSFKHVGIFPEQAVNWDYISDSVKSFKTPKPKVLNLFAYTGGASLIAKAAGADTTHVDSIKQVVTWANENQELSGISDIRWVVEDALKFVKRELKRGNTYNGIILDPPAYGHGPKGEKWKLEDHIMEMMRDVVQLLDPKEHFLILNTYSLGFSSVIVENLIKTSFPKVENLEIGELYLQATAGPKLPLGVFGKFRKIAK
>NZ_LT906468.1|WP_093098672.1|935745_936510_+|ATP-binding-cassette-domain-containing-protein
MIEITNIHKSFGDNVVLDGIDAIFEPGKVSQIIGGSGSGKSTLLKCIVGLHQPNQGKVFFDKQEFTKMDFEEKVPIRKEIGMLFQNSALFDSMTVEQNIVFTLDMFTEMSKSEKIDKANSCLERVNLAGKNNLFPSELSGGMKKRVGIARAISMNPKYLFCDEPNSGLDPATSILIDELVQDLTEEYQCTTVVVTHDMNSVMGIGDYILFLYKGKKYWEGSNQDMLKSDNKELNDFVFASPLMKAARNTLKKEQ
>NZ_LT906468.1|WP_093098670.1|935004_935739_+|ABC-transporter-permease
MIFYYFGEYLLLLKKVFRKPEKMKIYLKEIFHEMTEIGVGSLGLIVIISTFIGAVMTMQIAFQLVSDLIPTSVIGQINRDSNILELGPTISALVLMGKVGSSISSQIGSMRVTEQIDALEIMGINAAGYLILPKIIAGLIMVPALVIIAISCALVGGLLGGALSGAVTPDDYIEGIRGGFNGFTMVVAMVKATVFGFIITSVPAYKGFYVRGGALEVGQAGTRAVVIGCISILACDYLITALML
>NZ_LT906468.1|WP_093098669.1|933876_934794_-|hypothetical-protein
MNNKIATGIWLVFAGLVFLLHNLKVIDFNFFSIISLWPLILVSIGISLLLQGRTYGKYIVIGSNILLCGFIFFKGVTSKESMYDHIGNIDVSTGDDVKGPFTQVVSHPIGSETESAKLTINGGAAKYNFAPGTDSSLVLSAKTAQPTASLNLQTKGDREVKMELTSKMKNNKYNNSLIEVGLSNKPVWDLEFNVGAAAITGDFKQMKISKLEVNSGASSLNLYLPKPINGTCDIEVNTAASKVILYLPKGAACQVETDALFSNNKYEDVDVVLDDVRKSKNYDQESNKYDIKIAGAANSLSILRY
>NZ_LT906468.1|WP_093098667.1|931847_933848_-|(E)-4-hydroxy-3-methylbut-2-enyl-diphosphate-synthase
MESKPLTTLAGGYCNSKTAYSRFYTREVQIGDIPMGGNNPIRIQSMTTVDTMDTMGSVEQTIKMVDAGCEYVRITAPSIKEAENLANIKKELRARGYTVPLVADIHFTPNAAEVAARIVEKVRVNPGNYADKKKFDQINYTDAAYQAELDRIHKKFSPLVKICKEYGTAMRIGTNHGSLSDRIMSRYGDTPEGMVESALEFIRICEDLNYYNLCVSMKSSNPMVMVQAYRLLVEKMVAENMNYPLHLGVTEAGDGEDGRIKSAVGIGTLLEDGLGDTVRVSLTEEPEKEAPVAIALVNRYSKRVHDLAESQEREIIQIAPDQETKPYTSQEINAFIGGSLVPRIIVDLSSKNLKDPFILSDVGYKYDALLDKYHMGDQSVDFVYFGDALPSFTMPGNLKQLYNYRTWKELKNKTNIHPIYTLEEFNKAELKDPAMNLIYVSNDLLETEEFANLQMDKTTVFILETDHLHGMADQRQFFANLQEIGIDCPVIIKRSYAASEFSGPIGDIMNPEEPISKIQLYAATDFGALLIDGLGSGIWLDSEATATDKIASISFGILQATRSRISKTEYISCPSCGRTLFDLQETTQMIRSRTNHLKGLKIGIMGCIVNGPGEMADADYGYVGAGPDKITLYRGKEVVKRNVSSAKALDELIDIIKSDGLWVEEG
>NZ_LT906468.1|WP_093099061.1|947064_947238_+|AtpZ/AtpI-family-protein
MPFQMGVTIYVFYWLGTWLDEKYAVEGEWWMKGLTMFGVGLSLYQFIKQVNYINRNE
>NZ_LT906468.1|WP_139185476.1|947230_947635_+|hypothetical-protein
MNRYLLLLLVLLGVTGVCFGIHYAVLKMNHQDHWWIGSGYSLEGMYVFGAIASIVMVLILLVIDYTMPVQVGFAFLVGMTLKAVGSYVFIHEGINLLENDFIELNFLIVFFVYLLYDAFAAYYIVNQQETVSKN
>NZ_LT906468.1|WP_093098684.1|947724_948810_+|F0F1-ATP-synthase-subunit-A
MVSLKKVLLLFAVILFTVNPFRSVAEEGHAHGETSSSEEINAHIQHHLKDDYYFNFFTDSKTGKSYGFPLPVILIDGGLKVFSAGEFEHGEKVVEKDGQYYKLYHSKIYKTDAAGTITYDDKHHPTNAKPWDFSITKNVVGLLLAALLLFIGFTSLAKTYKNGPNAVPKGIGRALEPLVLYVRDEMAVPNIGHRYKEFMPYLLSVFFLIFLLNLLGLTPLGVNVTGNISVTLCLALFTFFITNFKANKDYWKHIFWMPGVPVPFKFVLAPIEVLGMFTKPFSLMVRLFANITAGHTVVMGLIAVVYLLQHQLTVVGSVSVSLLLTLLLFFLELLVAFLQAFIFTMLSSLFIGMAVEEHSHH
>NZ_LT906468.1|WP_093098685.1|948848_949040_+|ATP-synthase-F0-subunit-C
MIPNLVGAGLIVIGAGLGLGKIGGSAMEAIARQPEAASKIQTAMIIIGALLEGLAFGALLLGK
>NZ_LT906468.1|WP_093098687.1|949148_949649_+|F0F1-ATP-synthase-subunit-B
MDALIHDFSFGLFFWQLIILLIVIFLLGKFAWKPIVNALEEREKGITDALASAEKAKLEMARLTNENENLLKQAREERDVILKEAKVLKDKIVAEAKEVAQVEGGKLIEQAKREIEDQKLKALAEVKNQVSTLSLEIARKVLTKEFEDQGKQEALVADLMKDVKLN
>NZ_LT906468.1|WP_093098688.1|949676_950222_+|ATP-synthase-F1-subunit-delta
MSVFKVASRYAKSLIDLSLEQESLDAVKADIEGVIAIIKSNTELQAVLNNPIIKTDKKLAILKALFQGKIRPEILEFFNIMVRKGRAELVYATALEFVREYNEVKGIVHAEVVSASPLSEANLQALKEQIAAQINAQVILANKVDKSLIGGFVVKVGDKQIDASIQGKLNKLERHFENQGV
>NZ_LT906468.1|WP_093098690.1|950280_951855_+|F0F1-ATP-synthase-subunit-alpha
MIEVRPDEVSAILREQLSGFKSAADLEEVGTVLQVGDGIARIYGLTKVQSGELVEFANGLQGIVMNLEEDNVGVVLLGPSDEIKEGDTIKRTNRIASIKVGEGMLGRVVNTLGQPIDGKGPITGETFEMPIERKAPGVIYRQPVTEPLQTGLKAIDAMIPIGRGQRELVIGDRQTGKTAVCIDTILNQKEFYEAGQPVFCIYVAVGQKNSTVANIVRTLEEKGAMPYTVIVSASAADPAPMQFYAPMAGAAIGEYFRDTGRPALIVYDDLSKQAVAYREVSLLLKRPPGREAYPGDVFYLHSRLLERAAKINSSDEIARNMNDLPESLKDKVKGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESNLFNAGIRPAINVGISVSRVGGNAQIKSMKKVAGTLKLDQAQYRELEAFAKFGSDLDAATKAVLDKGIRNVEILKQGQYSPVSVEKQVAIIYAGTKGLLRNVPVNKVREFEEEYLTQLEQRHPEVLSALKAGKFSDELTDVLEKVAKELASKY
>NZ_LT906468.1|WP_093098691.1|952007_952889_+|ATP-synthase-F1-subunit-gamma
MANLKEVRNRITSVTSTQQITKAMKMVSAAKLKRATNAIIQLRPYATKLREILAQVSASVEGNNSPFTQDRIPTKVLIIVVTSNRGLAGAFNANAIKTANNLIATKYADQFARGDVSIIAIGKRGQDFFSKRDFKVIGNNNELFNNLDFENVSKITEYVMDQFKEGNIDRVEVVYNQFRNAAVQILTSEQILPLLPENKEDDNVAELDYIIEPSKEKIIEELIPKAIKIQLYKAVLDSHASEHGARMTAMDKATENAGDLLRQLKLSYNQARQAAITTELTEIVSGAAALSNG
>NZ_LT906468.1|WP_093099062.1|953540_954185_+|sterol-desaturase-family-protein
MFKNDFLESLTKVHYSVPLIFWIPVKIFFIWRALVPGGLSVGTVVMYYIFGLLFWTLAEYVLHRWVFHYEPSSKFGKRVHFIFHGVHHDFPKDRLRLVMPLSASIPMAAVIYFIFSFFFSPYTLAAFFSGFLLGYLIYDECHYAMHHANFKSGLFKRIKDHHMLHHYSEPEKGFGVSSAIWDVIFGSGFSKKKAGQSEKKKGNELKEVQEQQLN
>NZ_LT906468.1|WP_093098693.1|954243_955293_-|ketoacyl-ACP-synthase-III
MFQSKIAGLGYYVPKNVYTNNDLTRFMETSDEWIQERTGIKERRFADRVGETTTSMAVEASKIAIERANTTAEEIDFVIFATLSPDYYFPGCGVLLQREMGMKEIGALDVRNQCSGFIYALSIADQFIKTGMYKNILVVGSEKHSFALDFSTRGRSVSVIFGDGAGAVVLQPTNEEGKGILSTHLHSDGAEAEKLAMYFPGASAGYYLGEQMPQWPDVELGGMLMTKEMLEDGSAFPYMDGQAVFKKAVVKFPEVIGEALAKNNLKTTDIDMLIPHQANLRISQFVQKTLGLSDDQVFNNIQKYGNTTAASVPIALCEAWEEGKIKDGDLVCLAAFGAGFTWGSALIRW

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Crispr_ID: NZ_LT906468_4

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LT906468_4

992271-992362

Orphan

Consensus_repeat	Method
TTTGGTTACTTTTGGGCTCCAAAAGTAACA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_LT906468_4

>merge|NZ_LT906468|4|992271-992362|CRISPRCasFinder
TTTGGTTACTTTTGGGCTCCAAAAGTAACAATACGATTGGTGTCACTGAGCTCCTTCGTCGGTTTGGTTACTTTTGGGCTTCAAAAGTAACA

>NZ_LT906468|4|4|992271-992362|CRISPRCasFinder
TTTGGTTACTTTTGGGCTCCAAAAGTAACA	ATACGATTGGTGTCACTGAGCTCCTTCGTCGG
TTTGGTTACTTTTGGGCTTCAAAAGTAACA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LT906468.1\|WP_093098731.1\|984317_984920_-\|alpha-ketoglutarate-dependent-dioxygenase-AlkB	unknown	unknown	gnl\|CDD\|372627
NZ_LT906468.1\|WP_093098735.1\|986917_987982_-\|AI-2E-family-transporter	unknown	unknown	gnl\|CDD\|223701
NZ_LT906468.1\|WP_093098750.1\|998727_999243_-\|phosphoribosyltransferase	unknown	unknown	gnl\|CDD\|224976
NZ_LT906468.1\|WP_093098734.1\|986004_986748_-\|SDR-family-oxidoreductase	unknown	unknown	gnl\|CDD\|180440
NZ_LT906468.1\|WP_093098755.1\|1002869_1003862_+\|homoserine-kinase	unknown	unknown	gnl\|CDD\|234920
NZ_LT906468.1\|WP_093098741.1\|990748_991192_-\|50S-ribosomal-protein-L13	unknown	unknown	gnl\|CDD\|181703
NZ_LT906468.1\|WP_093098732.1\|984906_985773_-\|methylated-DNA--[protein]-cysteine-S-methyltransferase	unknown	unknown	gnl\|CDD\|185333
NZ_LT906468.1\|WP_093098752.1\|999346_999922_-\|C40-family-peptidase	unknown	unknown	gnl\|CDD\|236773
NZ_LT906468.1\|WP_093098744.1\|992935_994642_+\|tetratricopeptide-repeat-protein	unknown	unknown	gnl\|CDD\|274350
NZ_LT906468.1\|WP_093098740.1\|990350_990737_-\|30S-ribosomal-protein-S9	unknown	unknown	gnl\|CDD\|376328
NZ_LT906468.1\|WP_093098737.1\|988497_989334_-\|elongation-factor-Ts	unknown	unknown	gnl\|CDD\|236491
NZ_LT906468.1\|WP_093098728.1\|982021_982558_-\|dihydrofolate-reductase-family-protein	unknown	unknown	gnl\|CDD\|223340
NZ_LT906468.1\|WP_093098747.1\|996864_997080_+\|twin-arginine-translocase-TatA/TatE-family-subunit	unknown	unknown	gnl\|CDD\|224739
NZ_LT906468.1\|WP_093099065.1\|994631_995402_+\|DUF4292-domain-containing-protein	unknown	unknown	gnl\|CDD\|372917
NZ_LT906468.1\|WP_093099067.1\|1003878_1005186_+\|threonine-synthase	unknown	unknown	gnl\|CDD\|236418
NZ_LT906468.1\|WP_093098753.1\|1000402_1002850_+\|bifunctional-aspartate-kinase/homoserine-dehydrogenase-I	unknown	unknown	gnl\|CDD\|181856
NZ_LT906468.1\|WP_093098738.1\|989525_990332_-\|30S-ribosomal-protein-S2	unknown	unknown	gnl\|CDD\|235396
NZ_LT906468.1\|WP_093098749.1\|997231_998683_+\|lytic-transglycosylase-domain-containing-protein	unknown	unknown	gnl\|CDD\|381615
NZ_LT906468.1\|WP_093098729.1\|982574_984164_-\|ABC-F-family-ATP-binding-cassette-domain-containing-protein	unknown	unknown	gnl\|CDD\|223562
NZ_LT906468.1\|WP_093098746.1\|995511_996789_+\|peptidoglycan-DD-metalloendopeptidase-family-protein	unknown	unknown	gnl\|CDD\|227278

Protein	Function_ID	Function_description	E-value
NZ_LT906468.1\|WP_093098731.1\|984317_984920_-\|alpha-ketoglutarate-dependent-dioxygenase-AlkB	gnl\|CDD\|372627	pfam13532, 2OG-FeII_Oxy_2, 2OG-Fe(II) oxygenase superfamily.	5.83931e-29
NZ_LT906468.1\|WP_093098735.1\|986917_987982_-\|AI-2E-family-transporter	gnl\|CDD\|223701	COG0628, yhhT, Predicted permease, member of the PurR regulon [General function prediction only].	1.07052e-30
NZ_LT906468.1\|WP_093098750.1\|998727_999243_-\|phosphoribosyltransferase	gnl\|CDD\|224976	COG2065, PyrR, Pyrimidine operon attenuation protein/uracil phosphoribosyltransferase [Nucleotide transport and metabolism].	8.26627e-25
NZ_LT906468.1\|WP_093098734.1\|986004_986748_-\|SDR-family-oxidoreductase	gnl\|CDD\|180440	PRK06172, PRK06172, SDR family oxidoreductase.	9.28081e-74
NZ_LT906468.1\|WP_093098755.1\|1002869_1003862_+\|homoserine-kinase	gnl\|CDD\|234920	PRK01212, PRK01212, homoserine kinase; Provisional.	1.29027e-110
NZ_LT906468.1\|WP_093098741.1\|990748_991192_-\|50S-ribosomal-protein-L13	gnl\|CDD\|181703	PRK09216, rplM, 50S ribosomal protein L13; Reviewed.	3.51256e-96
NZ_LT906468.1\|WP_093098732.1\|984906_985773_-\|methylated-DNA--[protein]-cysteine-S-methyltransferase	gnl\|CDD\|185333	PRK15435, PRK15435, bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada.	5.60971e-59
NZ_LT906468.1\|WP_093098752.1\|999346_999922_-\|C40-family-peptidase	gnl\|CDD\|236773	PRK10838, spr, bifunctional murein DD-endopeptidase/murein LD-carboxypeptidase.	7.74357e-32
NZ_LT906468.1\|WP_093098744.1\|992935_994642_+\|tetratricopeptide-repeat-protein	gnl\|CDD\|274350	TIGR02917, TPR_domain_protein, putative PEP-CTERM system TPR-repeat lipoprotein. This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.	3.06742e-31
NZ_LT906468.1\|WP_093098740.1\|990350_990737_-\|30S-ribosomal-protein-S9	gnl\|CDD\|376328	pfam00380, Ribosomal_S9, Ribosomal protein S9/S16. This family includes small ribosomal subunit S9 from prokaryotes and S16 from eukaryotes.	8.51987e-67
NZ_LT906468.1\|WP_093098737.1\|988497_989334_-\|elongation-factor-Ts	gnl\|CDD\|236491	PRK09377, tsf, elongation factor Ts; Provisional.	1.71644e-124
NZ_LT906468.1\|WP_093098728.1\|982021_982558_-\|dihydrofolate-reductase-family-protein	gnl\|CDD\|223340	COG0262, FolA, Dihydrofolate reductase [Coenzyme metabolism].	4.71891e-18
NZ_LT906468.1\|WP_093098747.1\|996864_997080_+\|twin-arginine-translocase-TatA/TatE-family-subunit	gnl\|CDD\|224739	COG1826, TatA, Sec-independent protein secretion pathway components [Intracellular trafficking and secretion].	1.12992e-13
NZ_LT906468.1\|WP_093099065.1\|994631_995402_+\|DUF4292-domain-containing-protein	gnl\|CDD\|372917	pfam14125, DUF4292, Domain of unknown function (DUF4292). This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 243 and 287 amino acids in length.	3.25043e-38
NZ_LT906468.1\|WP_093099067.1\|1003878_1005186_+\|threonine-synthase	gnl\|CDD\|236418	PRK09225, PRK09225, threonine synthase; Validated.	0
NZ_LT906468.1\|WP_093098753.1\|1000402_1002850_+\|bifunctional-aspartate-kinase/homoserine-dehydrogenase-I	gnl\|CDD\|181856	PRK09436, thrA, bifunctional aspartokinase I/homoserine dehydrogenase I; Provisional.	0
NZ_LT906468.1\|WP_093098738.1\|989525_990332_-\|30S-ribosomal-protein-S2	gnl\|CDD\|235396	PRK05299, rpsB, 30S ribosomal protein S2; Provisional.	7.58421e-146
NZ_LT906468.1\|WP_093098749.1\|997231_998683_+\|lytic-transglycosylase-domain-containing-protein	gnl\|CDD\|381615	cd16894, MltD-like, Membrane-bound lytic murein transglycosylase D and similar proteins. Lytic transglycosylases (LT) catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc). Membrane-bound lytic murein transglycosylase D protein (MltD) family members may have one or more small LysM domains, which may contribute to peptidoglycan binding. Unlike the similar "goose-type" lysozymes, LTs also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, as well as the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL).	1.06909e-57
NZ_LT906468.1\|WP_093098729.1\|982574_984164_-\|ABC-F-family-ATP-binding-cassette-domain-containing-protein	gnl\|CDD\|223562	COG0488, Uup, ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only].	2.67078e-107
NZ_LT906468.1\|WP_093098746.1\|995511_996789_+\|peptidoglycan-DD-metalloendopeptidase-family-protein	gnl\|CDD\|227278	COG4942, COG4942, Membrane-bound metallopeptidase [Cell division and chromosome partitioning].	6.28531e-36

>NZ_LT906468.1|WP_093098741.1|990748_991192_-|50S-ribosomal-protein-L13
MNTLSYKTVSANKNTVNKEWIVVDAEGEILGRLASEIAKVIRGKHKPSFTPHVDCGDNVIVINADKVRLTGNKLGDKVYVRYTGYPGGQRFVSPKELMAKHPERIIEKAVRGMLPKNRLGRQLFKNLYVYAGTEHKHEAQNPKPVKF
>NZ_LT906468.1|WP_093098740.1|990350_990737_-|30S-ribosomal-protein-S9
MSTTNTSGRRKTAVARIYLTAGNGNITVNGKDYKEYFPTLPLQYIVTQSLLVADSLANFDINVNVQGGGVKGQAEAVRLAIAKALVELNPEVKPALRAKGLMTRDDRMVERKKPGRRKARRRFQFSKR
>NZ_LT906468.1|WP_093098738.1|989525_990332_-|30S-ribosomal-protein-S2
MARTTYQELLDAGVHFGHLTRKWDPKMAKYIFMERNGIHIIDLNKTLTKLEEAASAIKQIVKSGRKVLFVATKKQAKEIVAEQAKAVNMPFVTERWLGGMLTNFATVRKSIKKMSNIDKMQKDGTYDVLSKKEKLMIQRERIKLENLLGGIADLNRLPAALFIIDVKKEHIAVAEAMKLNIPTFAMVDTNSDPTNIDFPIPANDDATKSISLIASVIGKAIIEGLEERKRDKEEDAEKEAAAAKAAVDNGEATEATPGKRTRKAKDVE
>NZ_LT906468.1|WP_093098737.1|988497_989334_-|elongation-factor-Ts
MSVQISASDVNKLRQQTGAGMMDCKKALVEANGDFEAAVDYLRKKGAKVAASRQDRDSNEGVIIAKAAADGKSGIVVEVNCETDFVAKNADFVAFAESVADAALANSPATLEDLKALEIGGTKIADLLIEQTGKIGEKIDVSKFETVAADKVVAYIHGNYRLGVLVGLSADAAGVEEAGKDVAMQIAAMNPVAIDKDGVDTKTIERELEIAKEQIRAEGKPEEMVEKIAQGKLNKFYKENTLLNQEFVKDSSKSIAQFLDSVAKGLTVTAFKRVQLGA
>NZ_LT906468.1|WP_093098735.1|986917_987982_-|AI-2E-family-transporter
MRTKQINNNSINQIMLIIIIILVCILIFKNLYYYLPGFLGAITLYVLFRNSYFKLTERRKWNKILTSLLFILISIVFIVLPIWALVDYLVPQITSFLNNTDKIVSQFNLLKEYMADKPFLKDIDMSDEALLNMLQRFTKYVPSILNSVAEVMINIIVALFVLYFMLVYGRQMESYISSGVPFSPKSKLELWKEFDSMVRSNAIGIPILGFFQGLVAMLGYWIFGVDNFILMGMLTGIASIVPVLGTMTIYVPLGIITLAGGETANGIGILLYGFLLIGSIDNILRFTILKTLGNVPPLITVFGVLLGLKLFGMLGLIFGPLILSSVGVLIKVYSNEYGKGDSIILSTDSPEKTE
>NZ_LT906468.1|WP_093098734.1|986004_986748_-|SDR-family-oxidoreductase
MKQLNDKVAIVTGGVSGIGKAIVELFVKEGAKVVIADLNEKLGEELINNLGEGNVIFIKADASSAEDNKKIVEAAIENFGALHIAVNNAGIGGESNAVADLSIEGWKKVIDINLNGVFYGMHYQIPEIEKVGGSIINMASILGAVGFAKSSAYVAAKHGVVGLTQAAGWEYATKGVRINAIGPGFIATPLVEANLDADSLKYLETQHAFQRLGKPEEVAELALWLASDKASFVTASYYPVDGGYLAK
>NZ_LT906468.1|WP_093098732.1|984906_985773_-|methylated-DNA--[protein]-cysteine-S-methyltransferase
MEKSQQELNYDRIAKAILFIQDHFQEKPSLEEIAEHVHLSPFHFQRLFSDWVGTSPKKFLQYTQVNYAKKLLKEEKRTLFDTHILTGVGSTSRLHDMFVQIEGMTPAEFKQGAEGLSIAYSFQDSPFGKCLIASTEKGICYLAFVDDDAAGLAELEHSFEKAVFIAEEKAIHREALSIFNLEDSSLKRIKLHLKGTAFQLKVWQALLSIPMGELNSYKEIAEKVGNPSASRAVGTAIGSNPIAYLIPCHRVIQTSGHTGGYRWNPLRKTLMLGWEFAKTDKENHNEVI
>NZ_LT906468.1|WP_093098731.1|984317_984920_-|alpha-ketoglutarate-dependent-dioxygenase-AlkB
MKLFNTADPSKNLLPYDGCVNYYGIVCDSEKGYFEKLMYGIEWKNDQAVIFGRHIETKRKVAWYGDKRFEYSYSNILKIAQPWTEVLLELKEIVERESGETFNSCLLNLYHDGSEGMAWHSDGEKDLKKHGAIASLTFGAERKFSFKHKNSKEKIDIFLEDGSLLIMKDQTQDHWLHRLPPTKTIHGARINLTFRTIENA
>NZ_LT906468.1|WP_093098729.1|982574_984164_-|ABC-F-family-ATP-binding-cassette-domain-containing-protein
MVIIQNATYIHPNKDILFQGLNLVVNKQEKIALIGNNGVGKSTLLKAIASEVKLHAGSIDCASTPYYIPQLLDKYNAMSIAQVLAIEDKLKAFHAILEGQMDEQLLDILNDDWTIEDRVQQALNRWNLIGLKLDQPLSTLSGGQKTKVFLAGIDIHDPELILMDEPSNHLDLESRELLYQFIENCNKTLLLVSHDRALLRLIPEMAEMSKNGISKYGGNYEFFAEQKEIALNALDHDVKSKEKELRKAKDREREALERQNKLNARGKKKQEKAGIPKILMGALKNKAEGSSAKLKGVHQEKITGIQQNLRDLRSNLPEIDQMKFGFEESGLPVGKILLEIDGVNLQINGNDLWKQNLDFQLKYGDRIAIKGNNGSGKTSLIKLMIGEIAPSEGKIKKADFNYVYVDQDYSMVSSSKSVYEMAQSFNQSGLLEHEVKIRLNRFLFPKESWDKSCLVLSGGERMRLLLCCLNISSKSPDIIILDEPTNNIDIQNIEILTAAIQSYQGTLIVVSHDQYFLEDIGIKENITLH
>NZ_LT906468.1|WP_093098728.1|982021_982558_-|dihydrofolate-reductase-family-protein
MKKIIYYVASSVDGFISGEQDNVSGFTYEGEAIKQYIEDLKAFNHVLMGRKTYEFGYQFGVKPGDPSPTYAHMTQYILSNNLTFENKHEQVKVVPLEIERIQKLKEKADTDIYLCGGGQLAGWLLNNNLLDEVKIKLNPVIIGSGTKLFEGVKKNYALSLISDKNYDDGMKIVHYAIK
>NZ_LT906468.1|WP_093098744.1|992935_994642_+|tetratricopeptide-repeat-protein
MRILQWCKPLVLGIMLMAGQVLFAQELKDDKGYKEQLASIESKLKSGDLANALQSIEETLEKYPNGAEVYYAKSLLYAQARNFDVALPAAEEAVKISPENILYNNHLLELYKSKGDFASAVELLDEFIKKQPNNPQVYREKIMMQHAGKKSEDALKTYEETKAKFGETDTLDVLKAEILMDMDRPREANEVLQQWRKKKSPIRQVYSSLSYILMDEKKPKDALNVLEEGLSTTKDDLLYLDMADANMAMKKGSQAFENIKKAFQSDAVTFIDKHRVMMNLVNNNKDFTKDQLQDLANTLVLKHPRMPDSHMFKGDILWMRGDLDQAKSLYLTTVSMNPQHVDAWRKLINVELAQNKLDEAIVDGKEALSHNPGNVIITYFVGVAYMMKKDTNNARLFLERALDQSGNENDFVKSMIYGGLGDLYHEIKMESASEVAYDEAIKLDSNNVTVMNNAAYYLSLQKKDLEKAAEYAKKANEMEPNSGTFQDTYAWVLFQQGKYQEALVWIEKAIKNSEPSGVLFDHYGDILIKLGKTKEALKQWEKAMTFSEGSALDKEKLKQKISEKKYIE
>NZ_LT906468.1|WP_093099065.1|994631_995402_+|DUF4292-domain-containing-protein
MLSKISLVLAVLMLASACASKKATVKKDNAGTTAKGKDLLSTYELNNLNFITFSGRAKARVQFGEETQNVTLNVRMERDKAIWISVTALLGIEAARVLITPDSVKIINRLQSEYIAKPFSYIYRYTNPGISFRMLQDILVGNISTEMLRTDQLQIATSEEDVQVIGVKDGLTFHYGVNKSNRPTLFNLMELGKSNKLEAQYSEFAVIDGHNFPQRFTLNIEGSGAKVSSDMLYNKSEFNKGVELNFSIPSRYRAIN
>NZ_LT906468.1|WP_093098746.1|995511_996789_+|peptidoglycan-DD-metalloendopeptidase-family-protein
MDFKKIVLSIFSLLLFVGLSYGQSSLELKKQRERIDREIAELQKILSAKTQEKILSQKEVSALSKQLDLRENKISTINSELRIINKNISSNNAIVDKLKGELEKMRQDYEKMILFAFRNKNSYNKMMFIFASKDFNQAFKRVKYLQQFTDARKVKVAEIEGTKKQIELKIAQLERDKKTQQSLLKEQEAERNTIAKDKAAHSQELNQLAREERTFRGQLTKKQQEKKRLDAAIKTAIAREVEAARRAEEERRRRLAEAEAKKTGTTVTEAEKKIEKKTGSAVLNNSPEATKLSAGFSSNRGRLPWPVGQGNIVRNYGSVTVERGVRDFYDYIRIRTSDGAPVKTVFEGTVLQVINIGSYAVVVQHGEYLTAYSNLKSVNVSKGQKISTGTVIGAADSDPEVGYSYIDLSVYRGTTSMNPSIWIAR
>NZ_LT906468.1|WP_093098747.1|996864_997080_+|twin-arginine-translocase-TatA/TatE-family-subunit
MYTSGLLFIGTNEIIIIVVLALLLFGGKKIPELMRGLGRGVKEFKEGQKDDPNAEGNTNTTANNDTVNKQG
>NZ_LT906468.1|WP_093098749.1|997231_998683_+|lytic-transglycosylase-domain-containing-protein
MNKKISFLVTIGLCVLKFGYAQEQQSDPSFFGDTFQANIIDQLEKDKEKTFLMLDSVKQLAGGGVVFSEEDVNIAQRIQRIQKTVPLEYNARVKAYLDKYISRNYKPYMEKLLGLSEYYFPIYDQIFAEQGVPDEVKYLSVIESSLNPHTVSTSGAVGPWQFIYGTAKVYNLTMDSNFDERKDVYSTTYAVSSYLKEAYDEFNDWLLALASYNCGRGCVRRAIIRSGLNSPNYWELSPFLPKETQNYIPKFIAMTYVLNHAELYGLNTEVNDLQTDHRVLMLDKSINMKQLASALTCSPELLKQLNPGYKREVVIASPEKQRRLVIPVNEAMSDSLIYAALHNPQDEAIQKAIAAVDVKEDKNHEVAKGETLQTISRKYGVTVQNLMAWNNLTSRSSITGKSLVVSRAIDEELTKNVVAATRAKATVKSNPTYVTYVVRKGDTLSEIAGKHRGATVNKIKSDNNLRGSNLRIGQKLKIYKGKS
>NZ_LT906468.1|WP_093098750.1|998727_999243_-|phosphoribosyltransferase
MSSKKTLILNKEQIHQKSKRIAYQIVEDNFDESTIVLVGLADRGYVFAERLQKILMEIAPDKTFELIKVTVQKTKRNLEATTDVPVETAKDKVIILIDDVLNSGRTLAYGLGVFLNVPLKRMRTAVLIDRSHHQFPVFSDYYGLKLSTILKEHVEVVLEEFDKKEDAAYLS
>NZ_LT906468.1|WP_093098752.1|999346_999922_-|C40-family-peptidase
MKTKKLVAVMLFIGLCLFSQAQTSQKSSDPDNLAKEYFSQIMGVASNATTNTKLYQFVYEWLGTPYRLGGDSKRGIDCSKFSLAVYENVFNTTIGYNSRNQYSNVTPIRKNDLQAGDLVFFKIRSRSITHVGVYLGDDKFAHASSSKGVMVSNLNEAYWKRYYYNGGRPKLEDGERIMTADANPNQKSNLH
>NZ_LT906468.1|WP_093098753.1|1000402_1002850_+|bifunctional-aspartate-kinase/homoserine-dehydrogenase-I
MKILKFGGTSVGSVESIKAVLAIVKESYEAGEKPLVVLSAMSGITNLLTKMAEDAAEGKPFAEDLKLLEEKHFEVVKKLIAVKFQNPVLTRLKLLVNELEDLLQGVTALKELSNQSKDLIISYGERCSNYLVAKIMEQEVPEAEYINASHYIKTDSNFGNAHLNEPLTAQLIQALSQTHADKLLFVTGFIGSNDKGRITTLGRGGSDYTAAIFGSVLNATAIEIWTDVNGMLTADPRIVKKAFSLPVLSYTEAMELSYFGAKVIYPPTMVPAFMKKIPIVIRNTFQPKFPGTVIQFETGKSGFPIKGISSISDVSVINLTGSGMVGKSGFSGRLFTLLAREQINVILITQSSSEHSITFAVNPSDSQKAVELIQNEFELELLANKLSLPVVESDLSILAIVGENMKRTPGMSGKLFHALGRNGINVRAIAQGSSEFNISVIINKEDLSKALNAVHDAFFAELKKTLHVFNIGTGNIGSTLFSQLHKQHAFLEEQNDIEVKVVGISNSRRMYFNADGVDLGNWKEEMDANGEVADLATFIAKMQEMNLPNCVFIDNTASKLPSTYYENIFKSNISIVTCNKIANSGDYAQYKLLHETARKHGVDFFYETNVGAGLPIVRVLKDLMMSGDRLLKIEAILSGTISYIFNNFRGDASFYDVVKKAQELGFTEPDPRDDLGGIDFMRKMLILGRDAGYPIESSDVQLGNILPESCLKANSVDEFYAELLKADEYFNNLKEEAEKQGKVIRYIGTLENGKVAISLQMVDESHPFYALSGSDNIISFTTERYKERPLVVKGPGAGAEVTAGGVFADLVNVGA
>NZ_LT906468.1|WP_093098755.1|1002869_1003862_+|homoserine-kinase
MSNPEQLIKKENTLNPDKWLKEVRVFAPATVANMICGFDILGFAVDKPGDEVYMQRVEESGVRIRSIQGDDGRLPLDPDKNTVSACVKMLLSHLGLEEEVGIEIDLIKHMPIGSGLGSSSASTVAGLFAINALLGNPLTKNELMPFCVEGERLACGHGHADNVAPALMGGITLIRGYEPLDIINLPVPEDLVAGIVFPQVDVPTRDARQLIKEKVSLKDAVNQWGNIAGLVAGLYRSDYELIGRSMHDVLIEPTRAILIPEFYEMKRIAMEAGVLSFGISGSGPSVVAISKGSEAAQVAVDRIQEHLTANGIESLQFVSAVNAEGPKILS
>NZ_LT906468.1|WP_093099067.1|1003878_1005186_+|threonine-synthase
MQFYSTNNKDLRVSFQEAVFNSLPQDKGLYMPENIPSLDPYFIKNIQQYSFQEIAFQIANAIIGNDIAEKDLKAIINEAINFDAPVKFLSPDTAVLELFHGPSYAFKDFGARFMSRVMGYFSKQGEQLLDVLVATSGDTGGAVALGFLAVEGTRVTILYPKGKVSKVQEEQLTTNGQNIRALEVEGTFDDCQALVKQAFNDPELNQKLRLTSANSINIARLIPQTFYYFWAYAQLKAQGMQEVVFTVPSGNFGNIGAGLLAYKMGLPVSHFVAGTNVNDTVPRFLQSGQYEPKASVQTLANAMDVGNPSNWVRIQDLFHNNLSELQGMISSYTYNDEETKKGMDELYEQFKYVACPHTAIAYLASKAYRKDHPGEYASVFLSTAHPCKFPEAISKDVYKEVKLPAGAEKLQGKPKLAEELKVDYDAFKAYLIENN

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Crispr_ID: NZ_LT906468_5

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LT906468_5

1018576-1018683

Orphan

Consensus_repeat	Method
ATATCTCATATCTCAATACTCATATCTCAATACTAAT	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_LT906468_5

>merge|NZ_LT906468|5|1018576-1018683|CRISPRCasFinder
ATATCTCATATCTCAATACTCATATCTCAATACTAATGATATGAGATGTGAGGTTTGAGATAGAAAGGTTAATATCTCATATCTCAATACTCAAATCTCAATACTAAT

>NZ_LT906468|5|5|1018576-1018683|CRISPRCasFinder
ATATCTCATATCTCAATACTCATATCTCAATACTAAT	GATATGAGATGTGAGGTTTGAGATAGAAAGGTTA
ATATCTCATATCTCAATACTCAAATCTCAATACTAAT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LT906468.1\|WP_093098782.1\|1023518_1023863_-\|50S-ribosomal-protein-L19	unknown	unknown	gnl\|CDD\|235418
NZ_LT906468.1\|WP_093098762.1\|1010009_1010444_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906468.1\|WP_093098761.1\|1008700_1009888_-\|aspartate-aminotransferase-family-protein	unknown	unknown	gnl\|CDD\|99735
NZ_LT906468.1\|WP_093098788.1\|1035274_1036069_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|182179
NZ_LT906468.1\|WP_093098767.1\|1011962_1012916_-\|transketolase-family-protein	unknown	unknown	gnl\|CDD\|226467
NZ_LT906468.1\|WP_093099070.1\|1029199_1032238_+\|glycoside-hydrolase-family-127-protein	unknown	unknown	gnl\|CDD\|369609
NZ_LT906468.1\|WP_093098771.1\|1014280_1014835_-\|NifU-family-protein	unknown	unknown	gnl\|CDD\|378032
NZ_LT906468.1\|WP_093098776.1\|1017103_1018453_+\|acyl-CoA-dehydrogenase-family-protein	unknown	unknown	gnl\|CDD\|173840
NZ_LT906468.1\|WP_093098773.1\|1014909_1016259_-\|adenylosuccinate-lyase	unknown	unknown	gnl\|CDD\|236452
NZ_LT906468.1\|WP_093098765.1\|1011410_1011956_-\|RNA-polymerase-sigma-factor	unknown	unknown	gnl\|CDD\|224511
NZ_LT906468.1\|WP_093098785.1\|1033436_1034057_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906468.1\|WP_093098783.1\|1024251_1027491_+\|SusC/RagA-family-TonB-linked-outer-membrane-protein	unknown	unknown	gnl\|CDD\|274948
NZ_LT906468.1\|WP_093098777.1\|1018727_1020563_-\|membrane-protein-insertase-YidC	unknown	unknown	gnl\|CDD\|234942
NZ_LT906468.1\|WP_093098774.1\|1016648_1016867_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906468.1\|WP_093098764.1\|1010440_1011376_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906468.1\|WP_093099068.1\|1027546_1028989_+\|SusD/RagB-family-nutrient-binding-outer-membrane-lipoprotein	unknown	unknown	gnl\|CDD\|378943
NZ_LT906468.1\|WP_093098779.1\|1020601_1022212_-\|CTP-synthase	unknown	unknown	gnl\|CDD\|235437
NZ_LT906468.1\|WP_093098768.1\|1012941_1013790_-\|transketolase	unknown	unknown	gnl\|CDD\|238970
NZ_LT906468.1\|WP_093098786.1\|1034113_1035229_+\|DUF4861-family-protein	unknown	unknown	gnl\|CDD\|379779
NZ_LT906468.1\|WP_093098780.1\|1022452_1023442_+\|aldo/keto-reductase	unknown	unknown	gnl\|CDD\|381369

Protein	Function_ID	Function_description	E-value
NZ_LT906468.1\|WP_093098767.1\|1011962_1012916_-\|transketolase-family-protein	gnl\|CDD\|226467	COG3958, COG3958, Transketolase, C-terminal subunit [Carbohydrate transport and metabolism].	2.35435e-132
NZ_LT906468.1\|WP_093098761.1\|1008700_1009888_-\|aspartate-aminotransferase-family-protein	gnl\|CDD\|99735	cd00610, OAT_like, Acetyl ornithine aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to ornithine aminotransferase, acetylornithine aminotransferase, alanine-glyoxylate aminotransferase, dialkylglycine decarboxylase, 4-aminobutyrate aminotransferase, beta-alanine-pyruvate aminotransferase, adenosylmethionine-8-amino-7-oxononanoate aminotransferase, and glutamate-1-semialdehyde 2,1-aminomutase. All the enzymes belonging to this family act on basic amino acids and their derivatives are involved in transamination or decarboxylation.	1.24774e-145
NZ_LT906468.1\|WP_093098782.1\|1023518_1023863_-\|50S-ribosomal-protein-L19	gnl\|CDD\|235418	PRK05338, rplS, 50S ribosomal protein L19; Provisional.	2.42714e-59
NZ_LT906468.1\|WP_093099070.1\|1029199_1032238_+\|glycoside-hydrolase-family-127-protein	gnl\|CDD\|369609	pfam07944, Glyco_hydro_127, Beta-L-arabinofuranosidase, GH127. One member of this family, from Bidobacterium longicum, UniProtKB:E8MGH8, has been characterized as an unusual beta-L-arabinofuranosidase enzyme, EC:3.2.1.185. It rleases l-arabinose from the l-arabinofuranose (Araf)-beta1,2-Araf disaccharide and also transglycosylates 1-alkanols with retention of the anomeric configuration. Terminal beta-l-arabinofuranosyl residues have been found in arabinogalactan proteins from a mumber of different plantt species. beta-l-Arabinofuranosyl linkages with 1-4 arabinofuranosides are also found in the sugar chains of extensin and solanaceous lectins, hydroxyproline (Hyp)2-rich glycoproteins that are widely observed in plant cell wall fractions. The critical residue for catalytic activity is Glu-338, in a ET/SCAS sequence context.	3.71209e-112
NZ_LT906468.1\|WP_093098771.1\|1014280_1014835_-\|NifU-family-protein	gnl\|CDD\|378032	pfam08712, Nfu_N, Scaffold protein Nfu/NifU N terminal. This domain is found at the N-terminus of NifU and NifU related proteins, and in the human Nfu protein. Both of these proteins are thought to be involved in the the assembly of iron-sulphur clusters.	4.26722e-30
NZ_LT906468.1\|WP_093098779.1\|1020601_1022212_-\|CTP-synthase	gnl\|CDD\|235437	PRK05380, pyrG, CTP synthetase; Validated.	0
NZ_LT906468.1\|WP_093098773.1\|1014909_1016259_-\|adenylosuccinate-lyase	gnl\|CDD\|236452	PRK09285, PRK09285, adenylosuccinate lyase; Provisional.	0
NZ_LT906468.1\|WP_093098765.1\|1011410_1011956_-\|RNA-polymerase-sigma-factor	gnl\|CDD\|224511	COG1595, RpoE, DNA-directed RNA polymerase specialized sigma subunit, sigma24 homolog [Transcription].	1.59862e-41
NZ_LT906468.1\|WP_093098783.1\|1024251_1027491_+\|SusC/RagA-family-TonB-linked-outer-membrane-protein	gnl\|CDD\|274948	TIGR04056, OMP_RagA_SusC, TonB-linked outer membrane protein, SusC/RagA family. This model describes a distinctive clade among the TonB-linked outer membrane proteins (OMP). Members of this family are restricted to the Bacteriodetes lineage (except for Gemmatimonas aurantiaca T-27 from the novel phylum Gemmatimonadetes) and occur in high copy numbers, with over 100 members from Bacteroides thetaiotaomicron VPI-5482 alone. Published descriptions of members of this family are available for RagA from Porphyromonas gingivalis, SusC from Bacteroides thetaiotaomicron, and OmpW from Bacteroides caccae. Members form pairs with members of the SusD/RagB family (pfam07980). Transporter complexes including these outer membrane proteins are likely to import large degradation products of proteins (e.g. RagA) or carbohydrates (e.g. SusC) as nutrients, rather than siderophores. [Transport and binding proteins, Unknown substrate].	3.97625e-178
NZ_LT906468.1\|WP_093098788.1\|1035274_1036069_-\|hypothetical-protein	gnl\|CDD\|182179	PRK09980, ompL, porin OmpL.	0.004073
NZ_LT906468.1\|WP_093098777.1\|1018727_1020563_-\|membrane-protein-insertase-YidC	gnl\|CDD\|234942	PRK01318, PRK01318, membrane protein insertase; Provisional.	9.77479e-120
NZ_LT906468.1\|WP_093099068.1\|1027546_1028989_+\|SusD/RagB-family-nutrient-binding-outer-membrane-lipoprotein	gnl\|CDD\|378943	pfam12771, SusD-like_2, Starch-binding associating with outer membrane. SusD is a secreted starch-binding protein with an N-terminal lipid tail that allows it to associate with the outer membrane.	5.23462e-79
NZ_LT906468.1\|WP_093098776.1\|1017103_1018453_+\|acyl-CoA-dehydrogenase-family-protein	gnl\|CDD\|173840	cd01151, GCD, Glutaryl-CoA dehydrogenase. Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, which catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and carbon dioxide in the catabolism of lysine, hydroxylysine, and tryptophan. It uses electron transfer flavoprotein (ETF) as an electron acceptor. GCD is a homotetramer. GCD deficiency leads to a severe neurological disorder in humans.	7.06649e-159
NZ_LT906468.1\|WP_093098768.1\|1012941_1013790_-\|transketolase	gnl\|CDD\|238970	cd02012, TPP_TK, Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK catalyzes the transfer of a two-carbon unit from ketose phosphates to aldose phosphates. In heterotrophic organisms, TK provides a link between glycolysis and the pentose phosphate pathway and provides precursors for nucleotide, aromatic amino acid and vitamin biosynthesis. In addition, the enzyme plays a central role in the Calvin cycle in plants. Typically, TKs are homodimers. They require TPP and divalent cations, such as magnesium ions, for activity.	6.96076e-127
NZ_LT906468.1\|WP_093098786.1\|1034113_1035229_+\|DUF4861-family-protein	gnl\|CDD\|379779	pfam16153, DUF4861, Domain of unknown function (DUF4861). This family consists of uncharacterized proteins around 400 residues in length and is mainly found in various Bacteroides species. The function of this family is unknown. However, in many instances the domain lies upstream of a glycosyl hydrolase family, usually family 88, so it might be involved in carbohydrate binding.	9.82901e-78
NZ_LT906468.1\|WP_093098780.1\|1022452_1023442_+\|aldo/keto-reductase	gnl\|CDD\|381369	cd19143, AKR_AKR6C1_2, AKR6C family of aldo-keto reductase (AKR). Voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa are founding members of aldo-keto reductase family 6 member C1 (AKR6C1) and C2 (AKR6C2), respectively. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.	0

>NZ_LT906468.1|WP_093098776.1|1017103_1018453_+|acyl-CoA-dehydrogenase-family-protein
MLERLQNILKLMKSVDLEQLEKISKKVDLAEVLGAVSKMDENQLKMAMKMLTGSKKKKDPPPINADFYDISAKLSEEDRALQMKVRTFLETEIQPIVNKYWLHDEFPFEIIPKLRELNVCGYVYDGYGCAGGTSLMDGIIAAEFGRVDPSIATFLGVQSGLAMGSIYMCGSDEQKNEWLPAMQQLNKIGAFGLTEPLVGSATAGGLTTTCKRDGDNWILNGQKKWIGNSTFSDITIIWARDLDDQQVKGFIVRKENPGFSVEKIKDKMALRIVQNGLITLTDCVVPESDRMPNANSFKDTAKVLQMTRAGVAWMAVGCARGAYENALDYTIKREQFGKPIASFQLIQNHLVEMLSNLTAMQTLVFRLSELQDDEKLKDEHASLAKVFCTLRMRDIVSKAREVMGGNGILLEYNVARFLADAEAIYSYEGTKEINSLIVGRSITGFSAFV
>NZ_LT906468.1|WP_093098774.1|1016648_1016867_-|hypothetical-protein
MKNLFKFGFLGLALTIAVASCNNAETKTEATADSLSNVVDSTTENVADSLENVADSVRATGDSIADSLKNVQ
>NZ_LT906468.1|WP_093098773.1|1014909_1016259_-|adenylosuccinate-lyase
MTLSPLTAITPIDGRYYNTSKDLSNYFSEFALIKYRVLVEVEYFIALSESGIPQLSHFDGSLNDKLRDIYKNFSLEDAQWIKETEKVTNHDVKAVEYFLKNEFEKLGLHDSLEFIHFGLTSQDINNTAIPHSWKDALKDVYHPAINELLEELKKLSAEWENVSMLARTHGQPASPTRLGKEIKVFVERIEKQLTLLKQVPFSAKFGGATGNFNAHHVAYPNNDWVAFGNKFVNETLGLDRSQTTTQIEHYDNFAASCDGLKRINNIIIDLCRDVWTYISMDYFKQKITAGQIGSSAMPHKVNPIDFENAEGNLGLANAVLEHLAAKLPISRLQRDLTDSTVLRNIGVPFSYTLIAIKSTLRGLRKLILNEAAFQADLENNWAVVAEAIQTILRREGYPKPYEALKDLTRTNTHVTKDTIAAFVDQLNVTEEVKEEIKAISPSNYTGVKL
>NZ_LT906468.1|WP_093098771.1|1014280_1014835_-|NifU-family-protein
MATINVYTESTPNPATMKFLVNKLLINGSLDYPDREKAQESAFAKELFKFNFVNGVFFASNFVTITKTEDAEWDDIEALLKEFVKGAVESELAVKPVEHSEDVVFEGNDVEIKIQQVLHDYVRPAVEQDGGAIAYKSFDNGTVTVELRGSCSGCPSSTITLKAGIEGLLKRMVPEVEEVVANAM
>NZ_LT906468.1|WP_093098768.1|1012941_1013790_-|transketolase
MSADINKLEQIASQVRRDIVRMVHACQSGHPGGSLGCTDYFVALYFHAMKHDPSFNMDGIGEDIFFLSNGHISPVFYSTLARAGYFPVSELATFRKINSRLQGHPTTHEHLPGIRIASGSLGQGLSVSIGAAQAKKLNKDNSLVYVLMGDGELQEGQVWEAAMYAPHNKVDNLIAAVDYNRAQIDGSTDDVLSLGNLRAKWEAFGWDVLEVDKGNDMASVIAGLDEAKSRTGKGKPVIILLHTEMGSGVDFMMGSHKWHGVAPNDEQLESALNQIPRTVGDY
>NZ_LT906468.1|WP_093098767.1|1011962_1012916_-|transketolase-family-protein
MKKYTYTESKDTRSGFGAGLLEAGQKNENVVALCADLIGSLKMNDFIKAYPERFFQIGIAEANMMGIAAGLTIGGKIPFTGTFANFSTGRVYDQIRQSIAYSGKNVKICASHAGLTLGEDGATHQILEDIGLMKMLPGMTVINPCDFNQTKAATIALVDHEGPVYLRFGRPVVPNFTPADQKFEIGKAVMLNEGTDVTIVATGHLVWEAIQAGEELEKLGINAEIINIHTIKPLDEEAILKSVTKTGCVVTAEEHNRLGGLGDSVAQLLAQKLPTPQEYVAVNDSFGESGTPAQLMEKYGLNAANIVNAVRKVITRK
>NZ_LT906468.1|WP_093098765.1|1011410_1011956_-|RNA-polymerase-sigma-factor
MEDSLIIAKFADEKTREEAFRLLLKKYQQKIYWHVRRMVIDHDDADDVVQDIFIKVWRNLEKFREDSQLYTWLYRIATNECITFLNKKKQKQSVSLDDESSAYLSDSLADGAYFNGDKAQMKLQQALLTLPDKQRLVFNMKYFEDMKYEEISDVLGTSVGALKASYHLAVKKIENFFASND
>NZ_LT906468.1|WP_093098764.1|1010440_1011376_-|hypothetical-protein
MKENNTYYENLGGNQLPNSLRVNPFIVPENYFEKLTERSLFFAKLDQISDTGKAGLSTPNGFFEQQESQLLGQIKIDQYRVAESFSVPEQYFDQLSEQILGQVHIDGHKEVEETEVPAGYFDNLTARILNRIEEEELTLEIAEPGFTVPEGYFEEADDQIMASIYTEELKSKVQADGFEVPAGYFDQMSTAILDKVQDKKVITLPSRNESETSVSGKKGKVYAWLTTAAAACLAAVIAVSVYNAEYNQPMPTEKVSLNEIPEDEIINYLSSYSDASDIEYYAEYIYQPEEALNVGEGIDKEVLEDYLNYNL
>NZ_LT906468.1|WP_093098762.1|1010009_1010444_-|hypothetical-protein
MMIRLKHIISTLCLIWIACFVANGQSRQERFDAIEKQKAAYITKQLRLTPTEAQQFFPLYNQYSKEIRGVKSKKSQGHNNSGNRGNSFRPGNDVIEYDAQEVDIKKRYRTKFADVLGQSRASQFFAVEQEFIELLYKELNSRRH
>NZ_LT906468.1|WP_093098761.1|1008700_1009888_-|aspartate-aminotransferase-family-protein
MISNRELFLKNTAQTSDSPRLLEIDRAEGIYLYGPNGEKYMDLVSGFNVSNIGHRHPQVLKAIQEQLDRFMHVTVYGEFVQSPQVLLATELLEVLPDSFQSVYFTNSGAEAVEGSMKVAKKFTGRREIIAAKHAYHGSTQGALSLIGNDEYRVAYAPLLPEISFIEYNSLPDLEKISDKTAAVIVEAIQGEAGIRVPSKDYMQALRQKCTEKGALLIFDEIQTGFGRTGKLFAFEHFGIVPDILMLAKGIGGGMPLGAFVAPKEMMDVIKANPMLGHITTFGGHPVSCAAARASLKVIQDEKLIEDVDRKAKLFRSELQIPQIREIRGLGLMMCLQLDNFDQVYQVSNYCASKGLIIDWYLHCETALRIAPPLTISEDEIIHSCKIIREGIEKFC
>NZ_LT906468.1|WP_093098777.1|1018727_1020563_-|membrane-protein-insertase-YidC
MDRNNILGFIFIFAILAGSFYFLKPSDAEIKKEQQHQDSIKRAKEGLAPISDSLKAATTTTPAVPDSVLLSQPFGSASVGSEQIVTLENELLKVNVSNKGGRVKSVELKGETNFDGSKLILFEGDENRFGLEFNIPGKAVKTNDLFFQAQGASFSVAGQDAKSLTMRLSYAADKYIDYIYTLKGNDYNVQFDIKTVGIGSLVDVSSNKMLLNWETTLMQKERNVKSEREKSGIFYKEVDGSVDHLSETSDDEEKLEKKVSWIAFKQHFFSSILTSKEGFVNADLKSTLITQDSVVKHYRASTELALNKQNESLHGFSFFFGPNKYKTLKAEGNGFDKIINMGWGPMGWINKFITVPIFDFLDGFNMNYGIVILILTLFLKLLMFPLTYKSYQSMGKMRVLKPQLDEIKAKVGDDNPMLLQQEQMKLYKQAGVNPLGGCLPLLLQMPFTLAFFFFFPNLFELRGESFLWIKDLSTYDAPITFAPLPLLGVDHISFMCILMTLTTLLTTWYNNSTSGAVNNQMKYIGYIMPLVFFFVLNSFPAGLNYYYFLSAVLTFLTQVIIRQFVNDDKILAGIEANKKKPASEKKQSSFQKKMEEMMRAQQAAQQNKDKK
>NZ_LT906468.1|WP_093098779.1|1020601_1022212_-|CTP-synthase
MTKYIFVTGGVTSSLGKGIIAASLAKLLQARGLKVTIQKFDPYINIDPGTLNPYEHGECYVTEDGAETDLDLGHYERFLNVPTSQANNVTTGRIYSHVIEQERAGAYLGKTVQVVPHITDEIKRRMLLLGQSGEYDIVITELGGTVGDIESLPFIEAVRQLRWELGNNDSLVIHLTLVPYLAAAGELKTKPTQHSVKTLLEYGVQPDILVCRTEHKLNNDIRKKLALFCNVNINAVVESIDAPTIYDVPLNMLKEQLDKTVLAKLKLSTKNEPDLENWKSFLGRLKNPTDEVNIGLVGKYVELPDAYKSIAEAFIHAGATNETRVKVKYIAAESVNQENVGEKLKGLDGVLVAPGFGERGLDGKLETIRYVRENKIPFFGICLGMQCSVIEFGRNVLGLKGANSFEMDENTPHPVINLMEEQKNIKNMGGTMRLGAYDCEIKKGTKAYGVYGKSKITERHRHRYEFNNAYLKDYEKAGMIASGINPSTGLVEIVELKDHPFFVAGQFHPELKSTVVNPHPLFVSFVAAALTHKKSK
>NZ_LT906468.1|WP_093098780.1|1022452_1023442_+|aldo/keto-reductase
MEYRRMGKSGLQLSALSFGSWVTFARQTDDNTNERLMAQAYESGVNFFDNAEVYSAGLSEEMMGRVLKKLNWDRSSYVLSSKAYFGWKGVDKKPNQHGLSRKHLMEACHEALERMQVEYLDLYYCHRPDQNVPIEEVVRTMNTLIQQGKVFYWGTSEWSAAEIMEAHMIAKELGLEGPSVEQPEYNLFNRRKIEVDYAPIFRNVGMGTTIWSPLASGLLTGKYNDGIPEGSRMSLEGYEWLRDKAVVNEKLNRVKALGDFANELGVSLPTLCIAWCISNPNVTTAILGATKESQLTENLKALDVLPLITTEVKEKIDEIMGTKPEVIQN
>NZ_LT906468.1|WP_093098782.1|1023518_1023863_-|50S-ribosomal-protein-L19
MDLVKFVEEQAVVKNENPAFKAGDTISVHYKIREGNKERVQVYQGVVIQLNSEGANATFTVRKISNGIGVERIFPVNSPNIEKIEVNSIGKVRRAKLFYLRGLTGKAARIKSKR
>NZ_LT906468.1|WP_093098783.1|1024251_1027491_+|SusC/RagA-family-TonB-linked-outer-membrane-protein
MNKRLITSLAASLFFSTVLFAQTQLKGRVVDESGAPISGVTLTLKNGTATQTGANGEFTLSYDQAGQLNVSALGYSRKVINLSNQTTLEIILDPSTEGLDEVVVTALGISREKKSLPFTVQEVGAKELTQAGQLNVTSALSGKVAGVQVNQFGGTVGASSRISLRGNSSVKADQQPLIVVDGVPISNDTQRSGDNTYSGVDYGSGINDINPEDIETITVLKGGSAALYGMRAGNGVILITTKSGKRGDKGIQLSYDGNFSVDQAAYLPKVQNLYGQGYNGDEKHYNDFQASNGKISYQDYAQTKGFAYVDGTGQTGVWDGFDESWGPRLDVGLNLPQFDSPVNNGVRTPTPWVSQKDNIRDFFQPGFSMNHNLSILAQSDKSSTRASLSFRDQNGTVPNTDQKRYSLQLNNNTNISEKVSFDVSTNYTRTESDNILNQGYDGNNPMNGFIWSGRQINMQSLKDNWDQRDEQGNYTYYNWNTNYHVNPYFNIYENTNSYKRDRFFGKSSLYYQPFEFLKFEGRAGLDYYNLKAFEKNYYNSAFPYGGFRDRKTDNTELNLDFIATFNKQFGDFNVLASAGANYRNLMWETNVMGADALTVLGVYTIANRVGDAVTTMDHSHVRSNSVFATANLGWKDQIYMDLTARNDWSSTIKDDFFYPSISMSWLPTSSFPSLRNSVLNFWKIRGGWAEIGAGTTAYQNRAYYYPQNNAFGGVAQMFRSMVFPNANLRPEQIRTWEIGTEIGFLDDRIHADVVYYYKSTKDQILAVTTSNVVGFSSMLLNAGEIENKGIEVQLRGDVIRKEEGFNWTTYINYAKDNSKVIELYPELDLNVYQIGWTWGIANVARKGERWGSLIGGGYDRVEDGPMKGAIKVNNRGLVVNKNAQIIGNTTPKFLASWRNDFRYKDFSMGFMFDLRVGGDIWSQTMSHSYTAGVAAITAENGIREKAIVAGRDVMTDEKFVMQDANGNWVENTIETDAQTWFESGGIAQTYVFDGSFLKLREAYLSYNVPSRYLQNMRGIKRVNLSLIGSNLALLWTHKSNTMRIDPETGGVSSDSRGVGFEQASVPSSRSIGLKLGVTF
>NZ_LT906468.1|WP_093099068.1|1027546_1028989_+|SusD/RagB-family-nutrient-binding-outer-membrane-lipoprotein
MIGLATSSCTKSFEEVNTDPDALTEVPPTNILANVLRNTGESFGGDVDGYGTFAGYIVKIQYMDYMGGLVPTNNTFGNRWAACYYNNTQLQELMKLTDASPDGYKNIRFVSRIWQNYMWSYLTDGWRNVPYSEALKGAEDKGNILKAAYDKQEDIYPKILQDLKTIADEMAAGLGTDELGAGDFIYKGDMEKWQKFCNSLRLRLAMRISGVAPALAKSTIEEIAGNSTKYPVLETNAENCYLKYPGAAPYYEPWYNNGIVGKRIDNFGMADIFIDHLLETEDPRIAKVANKTSDGVYRGFQNGAKSGPTPLTSISFIGDKYMNDPVGFTPFYKSSETFYILAEAAMLGYNVKMTAQQAYEKAVRISMEDNQIAEADIVKYLAGKGKWNNTKERIYWDMWVALFKNNFEAWTLYRRTGIPSTNYPSLNSIYGNAHNDQPFRLPYPNNEYLYNAVNVNKEAEKLKDFVWGEQMWWDKRTGKF
>NZ_LT906468.1|WP_093099070.1|1029199_1032238_+|glycoside-hydrolase-family-127-protein
MAKIFGLLIIWIGGVNLLVAQESGDQILDGIGETGMIARYVFDGNLKDWSRNGLHANSKNNQPKFIKDEKFGNVLSLSGAKDDYLTLPSGTLNGLESLSISVWLSLKSDGTGQYIFDFGKDKNQHFFAAPFGTSAQKGFQALITDQGETKAGAIAPVPALNKWLHVAIVVDVFSKNIVTYADGKQVAEGNKIPQEIAKLFDSSGKFNIGKSLSAEGPTLNALVHDFRIYRVALTKKQVSGIYFNGQNAVRQDKKTMGKAEDDLPTYELTKAQLYNQYLLKVSDVKVETGLGELPRLPSYVDGDYKEGMKGPKVRVLWPADIDNDAVLKAGEYVVTGRIPGTDLKPKAFVTVKGFANTKAPTEKLLPFELSQVTLNSDSHNEETKFIENRDKFVNTLAKTDPNSFLYMFRHAFGQKQPVGAIPLGVWDSQDTKLRGHATGHYLTAIAQAYASTAYDKALQDNFAQKMDYMVNTLYDLAQLSGKAKENEGEHVSDPTAIPVGPGKTAFDSDLTEAGIRTDYWNWGEGFISAYPPDQFIMLENGATYGTKVTQVWAPYYTLHKILAGLIDIYQVSGNKKALQVAEGMGEWVYQRLNKIPKDNLIKMWNTYIAGEFGGMNESMARLYEITKNPHFLSTAQLFDNIKMFYGDPEHSHGLAKNVDTFRGLHANQHIPQIVGSIEMYKASNDPNYFKIADNFWYKAVNDYMYSIGGVAGARNPANAECFISQPATLYENGFSAGGQNETCATYNMLKLTSDLFRFDQRAELMDYYERGLYNHILASVAENSPANTYHVSLRPGANKQFGNPDMKGFTCCNGTAIESSTKLQNTIYFKSKDNNSLYVNLFIPSTLDWKEKGITVTQTTSYPKQNSTRLDIKGNGKFAVNVRVPNWAKKGFFVKINGKDQKVDAKPGSYLAIERDWKNGDTIELTMPFDFHLDPVMDQPNIASLFYGPILLAAQETEPQKEWRKVTLDAKDLGKSISGNPEALEFKIDGVVYKPFYDTYGRHSVYLDVTLK
>NZ_LT906468.1|WP_093098785.1|1033436_1034057_+|hypothetical-protein
MRIKSIIIALLIPFLFLSCEKSDIKFESEFKDSYDVFQKFKASSNNSYFYIVTGTSFFGYSWETKLTVKSGKVVKREFYFTKFESVQLPPNGWTAKELDEILKKRGKEFEESLKKDGITLLEYLQWVEDENNLGKLGTKVDYASQIKTLDEIYKLAETDWIIKRANAKVYFETKNNGMISTAGYVVGNCQDGCFNGINIKSIQAIR
>NZ_LT906468.1|WP_093098786.1|1034113_1035229_+|DUF4861-family-protein
MKRILLTCLIIVNCLAFCQAQFIQVKNPSKHARKELISIPFQNFKEHFKVDTVFTIRDENNQLIPFQLEKLGTAIPVNVLIQVELPARSTIKYKLEKEPGNRIEPMTFARYVPERLDDFAWENDVVAFRLYGKALEGRKDDGQGMDYWAKRTDKLIVNKWYKVENYHQDTGEGMDYYTVGQTLGAGDVALLSNNGLHYTKHYRRYQVLDNGPLRSTFKLEYDPEELDGQEVKLTKIISLDAGSNFNKIVLQVQNKMANSTAIAIGVARRKEDQPKFTIGPKNETLAYWEPEIAKNGQTGIAVIIPKKKISIDANRPEQFLLSSQAVNGQDFVYYNGAVWNRAGKVSSAEEWNKAVEQKHEKIKKPLKWVLK
>NZ_LT906468.1|WP_093098788.1|1035274_1036069_-|hypothetical-protein
MKTLKIKSLLFGLALIGLNYLQSSCSRYYYQPNAVNAPMMKEKGDLKIGISGTTSSEDLNGTNTSSSIINLQTAYSPIKYLGVMVNYSNYNYNFNEEDPSKGNVDAHAGLFEGGVGGYYPIIARENGFGLIADTYVGYGGGKLSSDVNMNFNRTFIQPGINLTFPYFDVGLATRISGIKYSNFDANGMTPEYISEHKLDNITDKRHYFFEPAFTLRAGYKFVKAELQVVGSTPMSEVDWESKGTVVTFGIHFSLMDAIKFAKEK

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Crispr_ID: NZ_LT906468_6

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LT906468_6

1066405-1066481

Orphan

Consensus_repeat	Method
TGAGATATGAGATATGAGATAGAAAGG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_LT906468_6

>merge|NZ_LT906468|6|1066405-1066481|CRISPRCasFinder
ATAGATATGAGATGTGAGATATGAGATATGAGATAGAAAGGTTATAGATATGAGATGTGAGAAATGAGATGTGAGAT

>NZ_LT906468|6|6|1066405-1066481|CRISPRCasFinder
ATAGATATGAGATGTGAGATATGAGAT	ATGAGATAGAAAGGTTATAGATA
TGAGATGTGAGAAATGAGATGTGAGAT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LT906468.1\|WP_093098820.1\|1071679_1073131_-\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	unknown	unknown	gnl\|CDD\|185760
NZ_LT906468.1\|WP_093098804.1\|1053812_1054229_+\|cytochrome-C	unknown	unknown	unknown
NZ_LT906468.1\|WP_093098832.1\|1083248_1085996_+\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|372685
NZ_LT906468.1\|WP_093098817.1\|1066726_1068148_-\|SusD/RagB-family-nutrient-binding-outer-membrane-lipoprotein	unknown	unknown	gnl\|CDD\|378943
NZ_LT906468.1\|WP_093098803.1\|1053550_1053829_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906468.1\|WP_093098822.1\|1073149_1076323_-\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|274948
NZ_LT906468.1\|WP_093098810.1\|1061721_1062441_+\|ATP-binding-cassette-domain-containing-protein	unknown	unknown	gnl\|CDD\|213185
NZ_LT906468.1\|WP_093099071.1\|1056162_1059276_+\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|274948
NZ_LT906468.1\|WP_093098826.1\|1077451_1078669_-\|C40-family-peptidase	unknown	unknown	gnl\|CDD\|366353
NZ_LT906468.1\|WP_093098807.1\|1059289_1061059_+\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	unknown	unknown	gnl\|CDD\|369630
NZ_LT906468.1\|WP_093098831.1\|1081776_1083174_+\|fimbrillin-family-protein	unknown	unknown	gnl\|CDD\|372499
NZ_LT906468.1\|WP_093098806.1\|1054321_1055689_+\|sulfatase-like-hydrolase/transferase	unknown	unknown	gnl\|CDD\|293763
NZ_LT906468.1\|WP_093098824.1\|1076396_1077449_-\|dipeptide-epimerase	unknown	unknown	gnl\|CDD\|239435
NZ_LT906468.1\|WP_093098818.1\|1068159_1071312_-\|SusC/RagA-family-TonB-linked-outer-membrane-protein	unknown	unknown	gnl\|CDD\|274948
NZ_LT906468.1\|WP_093098812.1\|1062513_1063848_+\|dihydroorotase	unknown	unknown	gnl\|CDD\|181716
NZ_LT906468.1\|WP_093098801.1\|1052549_1053548_+\|cytochrome-c	unknown	unknown	gnl\|CDD\|225540
NZ_LT906468.1\|WP_093098809.1\|1061447_1061738_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906468.1\|WP_093098828.1\|1078840_1079875_+\|N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase	unknown	unknown	gnl\|CDD\|271335
NZ_LT906468.1\|WP_093098813.1\|1063851_1064898_+\|LD-carboxypeptidase	unknown	unknown	gnl\|CDD\|132882
NZ_LT906468.1\|WP_093098829.1\|1080182_1081745_+\|DNA/RNA-non-specific-endonuclease	unknown	unknown	gnl\|CDD\|366523

Protein	Function_ID	Function_description	E-value
NZ_LT906468.1\|WP_093098820.1\|1071679_1073131_-\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	gnl\|CDD\|185760	cd08977, SusD, starch binding outer membrane protein SusD. SusD-like proteins from Bacteroidetes, members of the human distal gut microbiota, are part of the starch utilization system (Sus). Sus is one of the large clusters of glycosyl hydrolases, called polysaccharide utilization loci (PULs), which play an important role in polysaccharide recognition and uptake, and it is needed for growth on amylose, amylopectin, pullulan, and maltooligosaccharides. SusD, together with SusC, a predicted beta-barrel porin, forms the minimum outer-membrane starch-binding complex. The adult human distal gut microbiota is essential for digestion of a large variety of dietary polysaccharides, for which humans lack the necessary glycosyl hydrolases.	4.03806e-45
NZ_LT906468.1\|WP_093098824.1\|1076396_1077449_-\|dipeptide-epimerase	gnl\|CDD\|239435	cd03319, L-Ala-DL-Glu_epimerase, L-Ala-D/L-Glu epimerase catalyzes the epimerization of L-Ala-D/L-Glu and other dipeptides. The genomic context and the substrate specificity of characterized members of this family from E.coli and B.subtilis indicates a possible role in the metabolism of the murein peptide of peptidoglycan, of which L-Ala-D-Glu is a component. L-Ala-D/L-Glu epimerase is a member of the enolase-superfamily, which is characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.	1.57454e-118
NZ_LT906468.1\|WP_093098832.1\|1083248_1085996_+\|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.	8.72057e-08
NZ_LT906468.1\|WP_093098817.1\|1066726_1068148_-\|SusD/RagB-family-nutrient-binding-outer-membrane-lipoprotein	gnl\|CDD\|378943	pfam12771, SusD-like_2, Starch-binding associating with outer membrane. SusD is a secreted starch-binding protein with an N-terminal lipid tail that allows it to associate with the outer membrane.	2.08924e-58
NZ_LT906468.1\|WP_093098826.1\|1077451_1078669_-\|C40-family-peptidase	gnl\|CDD\|366353	pfam00877, NLPC_P60, NlpC/P60 family. The function of this domain is unknown. It is found in several lipoproteins.	2.73073e-24
NZ_LT906468.1\|WP_093098822.1\|1073149_1076323_-\|TonB-dependent-receptor	gnl\|CDD\|274948	TIGR04056, OMP_RagA_SusC, TonB-linked outer membrane protein, SusC/RagA family. This model describes a distinctive clade among the TonB-linked outer membrane proteins (OMP). Members of this family are restricted to the Bacteriodetes lineage (except for Gemmatimonas aurantiaca T-27 from the novel phylum Gemmatimonadetes) and occur in high copy numbers, with over 100 members from Bacteroides thetaiotaomicron VPI-5482 alone. Published descriptions of members of this family are available for RagA from Porphyromonas gingivalis, SusC from Bacteroides thetaiotaomicron, and OmpW from Bacteroides caccae. Members form pairs with members of the SusD/RagB family (pfam07980). Transporter complexes including these outer membrane proteins are likely to import large degradation products of proteins (e.g. RagA) or carbohydrates (e.g. SusC) as nutrients, rather than siderophores. [Transport and binding proteins, Unknown substrate].	0
NZ_LT906468.1\|WP_093098810.1\|1061721_1062441_+\|ATP-binding-cassette-domain-containing-protein	gnl\|CDD\|213185	cd03218, ABC_YhbG, ATP-binding cassette component of YhbG transport system. The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.	8.75769e-25
NZ_LT906468.1\|WP_093099071.1\|1056162_1059276_+\|TonB-dependent-receptor	gnl\|CDD\|274948	TIGR04056, OMP_RagA_SusC, TonB-linked outer membrane protein, SusC/RagA family. This model describes a distinctive clade among the TonB-linked outer membrane proteins (OMP). Members of this family are restricted to the Bacteriodetes lineage (except for Gemmatimonas aurantiaca T-27 from the novel phylum Gemmatimonadetes) and occur in high copy numbers, with over 100 members from Bacteroides thetaiotaomicron VPI-5482 alone. Published descriptions of members of this family are available for RagA from Porphyromonas gingivalis, SusC from Bacteroides thetaiotaomicron, and OmpW from Bacteroides caccae. Members form pairs with members of the SusD/RagB family (pfam07980). Transporter complexes including these outer membrane proteins are likely to import large degradation products of proteins (e.g. RagA) or carbohydrates (e.g. SusC) as nutrients, rather than siderophores. [Transport and binding proteins, Unknown substrate].	0
NZ_LT906468.1\|WP_093098831.1\|1081776_1083174_+\|fimbrillin-family-protein	gnl\|CDD\|372499	pfam13149, Mfa_like_1, Fimbrillin-like. A family of putative fimbrillin proteins found by clustering human gut metagenomic sequences. Analysis of structural comparisons shows this family to be part of the FimbA (CL0450) superfamily of adhesin components or fimbrillins.	1.75388e-45
NZ_LT906468.1\|WP_093098807.1\|1059289_1061059_+\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	gnl\|CDD\|369630	pfam07980, SusD_RagB, SusD family. This domain is found in bacterial cell surface proteins such SusD and SusD-like proteins, as as well RagB, outer membrane surface receptor antigen. Bacteroidetes, one of the two dominant bacterial phyla in the human gut, are Gram-negative saccharolytic microorganisms that utilize a diverse array of glycans. Hence, they express starch-utilization system (Sus) for glycan uptake. SusD has 551 amino acids, and is almost entirely alpha-helical, with 22 alpha-helices, eight of which form 4 tetra-trico peptide repeats (TPRs: helix-turn-helix motifs involved in protein-protein interactions). The four TPRs pack together to create a right-handed super-helix. This is predicted to mediate the formation of SusD and SusC porin complex at the cell surface. The interaction between SusC and TPR1/TPR2 region of SusD is predicted to be of functional importance since it allows SusD to be in position for oligosaccharide capture from other Sus lipoproteins and delivery of these glycans to the SusC porin. The non-TPR containing portion of SusD is where starch binding occurs. The binding site is a shallow surface cavity located on top of TPR1. SusD homologs such as SusD-like proteins have a critical role in carbohydrate acquisition. Both SusD and its homologs, contain about 15-20 residues at the N-terminus that might be a flexible linker region, anchoring the protein to the membrane and the glycan-binding domain. Other homologs to SusD have been examined in Porphyromonas gingivalis such as RagB, an immunodominant outer-membrane surface receptor antigen. Structural characterization of RagB shows substantial similarity with Bacteroides thetaiotaomicron SusD (i.e alpha-helices and TPR regions). Based on this structural similarity, functional studies suggest that, RagB binding of glycans occurs at pockets on the molecular surface that are distinct from those of SusD.	9.77689e-55
NZ_LT906468.1\|WP_093098806.1\|1054321_1055689_+\|sulfatase-like-hydrolase/transferase	gnl\|CDD\|293763	cd16144, ARS_like, uncharacterized arylsulfatase subfamily. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.	3.75687e-122
NZ_LT906468.1\|WP_093098818.1\|1068159_1071312_-\|SusC/RagA-family-TonB-linked-outer-membrane-protein	gnl\|CDD\|274948	TIGR04056, OMP_RagA_SusC, TonB-linked outer membrane protein, SusC/RagA family. This model describes a distinctive clade among the TonB-linked outer membrane proteins (OMP). Members of this family are restricted to the Bacteriodetes lineage (except for Gemmatimonas aurantiaca T-27 from the novel phylum Gemmatimonadetes) and occur in high copy numbers, with over 100 members from Bacteroides thetaiotaomicron VPI-5482 alone. Published descriptions of members of this family are available for RagA from Porphyromonas gingivalis, SusC from Bacteroides thetaiotaomicron, and OmpW from Bacteroides caccae. Members form pairs with members of the SusD/RagB family (pfam07980). Transporter complexes including these outer membrane proteins are likely to import large degradation products of proteins (e.g. RagA) or carbohydrates (e.g. SusC) as nutrients, rather than siderophores. [Transport and binding proteins, Unknown substrate].	0
NZ_LT906468.1\|WP_093098812.1\|1062513_1063848_+\|dihydroorotase	gnl\|CDD\|181716	PRK09236, PRK09236, dihydroorotase; Reviewed.	0
NZ_LT906468.1\|WP_093098801.1\|1052549_1053548_+\|cytochrome-c	gnl\|CDD\|225540	COG2993, CcoO, Cbb3-type cytochrome oxidase, cytochrome c subunit [Energy production and conversion].	4.39313e-33
NZ_LT906468.1\|WP_093098828.1\|1078840_1079875_+\|N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase	gnl\|CDD\|271335	cd04513, Glycosylasparaginase, Glycosylasparaginase and similar proteins. Glycosylasparaginase catalyzes the hydrolysis of the glycosylamide bond of asparagine-linked glycoproteins. This enzyme is an amidase located inside lysosomes. Mutation of this gene in humans causes a genetic disorder known as aspartylglycosaminuria (AGU). The glycosylasparaginase precursor undergoes autoproteolysis through an N-O or N-S acyl rearrangement of the peptide bond, which leads to the cleavage of a peptide bond between an Asp and a Thr. This proteolysis step generates an exposed N-terminal catalytic threonine and activates the enzyme.	1.76059e-149
NZ_LT906468.1\|WP_093098813.1\|1063851_1064898_+\|LD-carboxypeptidase	gnl\|CDD\|132882	cd07025, Peptidase_S66, LD-Carboxypeptidase, a serine protease, includes microcin C7 self immunity protein. LD-carboxypeptidase (Muramoyltetrapeptide carboxypeptidase; EC 3.4.17.13; Merops family S66; initially described as Carboxypeptidase II) family also includes the microcin c7 self-immunity protein (MccF) as well as uncharacterized proteins including hypothetical proteins. LD-carboxypeptidase hydrolyzes the amide bond that links the dibasic amino acids to C-terminal D-amino acids. The physiological substrates of LD-carboxypeptidase are tetrapeptide fragments (such as UDP-MurNAc-tetrapeptides) that are produced when bacterial cell walls are degraded; they contain an L-configured residue (L-lysine or meso-diaminopimelic acid residue) as the penultimate residue and D-alanine as the ultimate residue. A possible role of LD-carboxypeptidase is in peptidoglycan recycling whereby the resulting tripeptide (precursor for murein synthesis) can be reconverted into peptidoglycan by attachment of preformed D-Ala-D-Ala dipeptides. Some enzymes possessing LD-carboxypeptidase activity also act as LD-transpeptidase by replacing the terminal D-Ala with another D-amino acid. MccF contributes to self-immunity towards microcin C7 (MccC7), a ribosomally encoded peptide antibiotic that contains a phosphoramidate linkage to adenosine monophosphate at its C-terminus. Its possible biological role is to defend producer cells against exogenous microcin from re-entering after having been exported. It is suggested that MccF is involved in microcin degradation or sequestration in the periplasm.	1.13821e-110
NZ_LT906468.1\|WP_093098829.1\|1080182_1081745_+\|DNA/RNA-non-specific-endonuclease	gnl\|CDD\|366523	pfam01223, Endonuclease_NS, DNA/RNA non-specific endonuclease.	1.48174e-43

>NZ_LT906468.1|WP_093098813.1|1063851_1064898_+|LD-carboxypeptidase
MDKRSFIKSLGIGLAAMPLFGKSEAMAVANQIQPLLKGKVLKTGDTIGIIAPASAVTGEDSITQTKEVLEYFGFKVKEGKYIRERYGNLAGTDDQRLEDLHAMFADKSVAGILCIRGGAGASRLLKRIDYNLVAKNPKALLGYSDITALIMAFQAKIGMVTFHGPVGTSTWSNFVAKTFTDQFIENKLVSYSNPVKKGDDIIQYKDRITTINPGVAEGKLLGGNLTLISGLCGSEFLPDFKDSILFLEEINESPEKVDRMFCQLMNAGILSQIKGFVFGKCTDCSPSGGYGSLNLDQILRDFIKPLNIPSYSGAVIGHINDQFLLPVGVKARIDANKGTIEILEKALV
>NZ_LT906468.1|WP_093098812.1|1062513_1063848_+|dihydroorotase
MSTILIKNAHVVNEGSIQVQDLFIKNGRIEKIAETIETNADQIINAEGLHLFPGLIDDQVHFREPGLTHKADIFTESRAAVAGGTTSFMEMPNTVPNTLTQKLLQDKYDIAQDNSLANYSFFMGAANDNLDEVLKTNPRDVCGIKVFMGSSTGNMLVDNEKALEAIFSQAPTLIATHCEDEATIQANLAKFKEQYGENVSIEMHPLIRSAEACYLSSSKAVELAKKNNTRLHILHISTARETGLFENNIPLEQKRITAEACIHHLWFSDADYKKKGNFIKWNPAVKTADDRDAILNAVLDGHIDVIATDHAPHTFEEKSQPYLQAPSGGPLVQHALQALLDLVKEGKLTLEQLVQKTAHNTAILFQIEQRGYIREGYWADLVLVDLNKPYTVTKENILSKCGWSPFENHTFTSTIEHTIVSGLLAYTDGKIQEVGSGHRLLFNR
>NZ_LT906468.1|WP_093098810.1|1061721_1062441_+|ATP-binding-cassette-domain-containing-protein
MDIKDKELFVDSVQFSYTSNNQLLTGGYLGLKVGDIIGLLGRNGTGKTTLMKIIFGSLRAQNAYIRVNGKKVSQAFPTREVCYLPQDSFLPTSFRVKNAISFMLSDQESRAIVESDELIKPILDNKIADLAGGELRYLEIMLLVEQKATFLLLDEPFSGISPILKEKIQALLVEKSKVKGFLVSDHDYMNVLDVATQLLLLENGGCRKINRKEELEQFYVPLGTFDHGNTPDTDSKNSF
>NZ_LT906468.1|WP_093098809.1|1061447_1061738_+|hypothetical-protein
MPIELKHLWQFYKPILFINLVLSLAMSIQYFGYFPYVFMTVGYLCSAALVRFFEGNTKYLFFNLGLSRKHLVIYTFLANLLISFLLILIVHYGYKG
>NZ_LT906468.1|WP_093098807.1|1059289_1061059_+|RagB/SusD-family-nutrient-uptake-outer-membrane-protein
MKKILLVALGLSTIFTSCKNVLDIEDLQSLDEEKVWKDPNLVNAYMANLYTVFGNWSAGADVYSEQLVGVPFQLNTISPTAGGFKTWDYTNIRKINTAIQKVQESTSLSQEVKNSTLGEAYFLRAFVYFDMLRLYGGIPYITVPQNQATDDLNTPRNSTKESFELLVKDLDEAIKLLPQTIEKSSSNYGRIDGNFATAFKAKVLLYKASPQFNPANPYNNAYWKEANAANKAAYEQLIKNNYTLTPDYANITLQEKGPEVVFAVINTYPNKVAAWDYGVRPGSESRGPAGAVPTWDFVKEFPMKDGKLYSDPTGKYFKSDDDFLQSYWLNRDPRFDKSIVWNGKIYEVSGKAGKRQYTSLGIADALDNFGINPAAGINSTNQDRYSGFFILKNSKLSLKQTEVETQYDVDFVLMRLAEVLLNYAETANETGDLGTAQDMLNQLRKRAGIEAGTDGKYGITATNRDQMREAILAERNIELCFEGHRFWDLRRSRKLKTLDKGTKFGVEAIAIDADGSDMDIKQANALAKTYQLKEANFKYSILQVPKNGVKVSEVPDTYYFFPIQQSIIDRNPKVLQNKDWGGAFNPTME
>NZ_LT906468.1|WP_093099071.1|1056162_1059276_+|TonB-dependent-receptor
MSGSVKDDGGNPIVGATVLVKGTTRATSTDANGEFSITANNGDVIVIRNLGYLTQEITVSNAQNINISLAPDNANIDEVVVVGYGTQKRANITSAISTVNGDALKNVSPSNLSNAIAGRAPGVKVTGTSGLSGATSKIRFRGSFAEPLFVIDGIVRDKAAFDALEANEVDQMSFLKDAGAAAVYGTRAGNGVVIVTTKKGTVKKPEFNIQSNVAISNPTMTPLADLTTATDELTYQNRVAEFQGLPIPNGEEEFAYFKDKSYSVNDVIWRNPVSHRQSISVSGGSEKITYYNLLSFRNENGSYKSVDHQKFNLRSNVSANITDAFSIDMNISANQQNSNRFYWPFSTSSNDDDFDVSDFYRVTFNWPKMYPFYLTQDGTPSNEPTEYPVQTPMGSWQAWNVIDQVIGDRYIDRKVRQINPILSLNLKLDKLIPGLSTKFVGSYIAEDYLRKRYMSFQKNYTFTSLDPDGNPFIPAPPSEDRINIFTFSQQNPFMDYYTQRKWEYQMNFFINYMQTFGKHDVGATLVFEQGEKGYTNITSTAQSPITALDQMHVYPTDRNFRYTNGLEGIDARQSIIGRFNYAYGSKYLAEASFRYDGAALFPEQKRFGFFPSVSAAWRISEEEFFAGIKDKISDLKLRFAYGATGNYLDVNGNAINPFSFAEKYATTTGFIFGDRYYNGLAYGSTPNPNITWTRSESYNLGLDYGFINNKLNGSIEVFKRAETNILGPRTVLLPDTYGRALAPENYAARSYKGGEVSVNWNDRVGEVAYGISANLGYAVDQWDVFDEPAAYAEGGLEHFRSRIGRPNNVIYGLNSLGLVRTQAELDDLLAKGFKTYGRDPYLGMILYEDIRGQGYSDTPDGKIDGNDVTLLSTNNSPRWDYGLGLNGSWKGISINALFQGVFNYDRMISNQEGGGMRQHGGTFRPYYPIWADDVWTPENPNAQYPRPIGYNWAESGTNPSSFWMRSGAFFRLKDLNVAYQLPTSFTEKIKMNSINLFFNGTNLFVFSPMTEFHDPEQLNYDSYPLMKTFTFGLDIKF
>NZ_LT906468.1|WP_093098806.1|1054321_1055689_+|sulfatase-like-hydrolase/transferase
MKNALRPAILVLWCLCFHLSFAQQHQQPNIILILADDLGIGDLSSYYHQYETPNLDKLGKEGIRFNNYYSASPICSPSRAGLLTGQRPAKLHFTTFLNTREDNRKKEQVDFLDPSVLTMADVLKANGYATAHFGKWHLGGGRDVNNAPNFDQYGFDAWSGTYESPDPDPAITATDWIWSDQDSVKRWNRTKYFVDKTLDFLQKNKDKPCFINVWTDDVHTPWIAGDDEKGRFDWKPQEERSFKFVLQEYDREIGRLMQGLKEMGLDENTLVIFISDNGPLPNFRQDRSAGLRGSKLSLYEGGIRMPLLMRWPAKIKAGQVDEQTIISALDFLPSLAKLAKAPLKNAKGLDGQDLSKAMLGNPIARNKALIWEYGRNDSTAFSFPKKVNRSPALAIRDQDWKFMMNSDGSDPELYDLKADPNERTNLAANRKQLVIKYTKALSQWWKGLPPYRKIE
>NZ_LT906468.1|WP_093098804.1|1053812_1054229_+|cytochrome-C
MSQRSKIFIFIDDENIPIAETYSPVNFELDTRKLVDGKHQLRIVSKDPGGKEGVRIIPFEVRNGPAIEITGIKENAVIDDLVPIMINAYGKGNSETFMIDGSETPQGIPWWVWIIIIVFMGWAMYYVFMYLYLPTSVN
>NZ_LT906468.1|WP_093098803.1|1053550_1053829_+|hypothetical-protein
MKKIQLTLLFSICISFLMACPVCERNQPKILRGWVHGTAPKSDLEYIMVIAIILISLIALGMFLKMIIKPGEKQTDHIKRFILNSDNYEPKK
>NZ_LT906468.1|WP_093098801.1|1052549_1053548_+|cytochrome-c
MEFFDDHKKLFITAAVFFIVLTIFVAILPALNNQLKNAPLPQSEPLSPDAVAGKSIFIANGCVACHTQQVRNVDMDKVFGQRPSVAADYAHNERLDVWRNTATLMGTERTGPDLTDVGNRQPSKEWNLVHLYNPRIVVKESIMPAYPFLFEYKSIPAKEDVVVNIPEDFAPSNGKKVVASKEAMQLIAYLQSLKQVKLEADVPEFLYKRKAQAAAGQGAAEEELDGEALYVAHCQACHQADGNGLPGAFPPLKGSPVVTGDDLELYVDIIMNGYDSRPEYGVMAAVGVNAGFTEKEVAAIINYERTSWGNNGKKVKAEDIKQIVDFVKTQSN
>NZ_LT906468.1|WP_093098817.1|1066726_1068148_-|SusD/RagB-family-nutrient-binding-outer-membrane-lipoprotein
MNKFIKIGKISLLALALFSLNSCKDYFELTDNPNLVQTPPLNALLTTATHKAAFNNYRIAYFNNQYSQYFASPSGGSDTDTYQITNNSSTWNNLFYSLADLYDFMVKSEEAGATHHLAVAQALTAYQLALVADTWGSVPFSKAFGKEETLTVPFDSEEDLYKAQVDLINKALENFKKTDATQELSEKDDLLCGGDLDKWIKLTNGLKARVLNKISKKAAYNPKQVLAAAQASLESNAEDVGMSTFDGVNPWASISISNLLNNLDGWLGSNFIDQMNGKTYGIEDPRISKITEKTVHGVYVGTVSGQGNVGAANTVRDECYISSKSPVSSESSPLMILTYAEVKFIEAEAAFRDNNKPVAYAAFLAGVQASMDKLGVLEVDATKYIKAISVGQANLTLLDIFREKYIVTYLNAEAWNDVRRFDYKYKDFKLPIGAVLGDKFIRRVAYPADEITENGSNVPAEVPLSTELWWDKP
>NZ_LT906468.1|WP_093098818.1|1068159_1071312_-|SusC/RagA-family-TonB-linked-outer-membrane-protein
MNLPTCLSIAVASLCSIQMLSAQQLSIAGKVTNAEGEPIVGASIFVKGTQQGTSSNESGLFTLNAPSSGTLLIRAVGYAPLEVPISGRTNISIQLQHDDSEIDEVVVTALGIQRSEKSLGYGAQSVNSATLNSNKQPNLVNALQGKIAGATISSTGGAPGQGANIQIRGINSIDPTRDNQPLFVIDGILMDNSTSTQGGAEVRGMSNRSVDINPDDIETINILKGGAATALYGLRGANGVVIITTKSGKAGSLKIDYQGTVGFENVNKFPKMQDTYTQGWKGVYDKDDFWPAWGPTIADAIKVDPTHPTTLYKPFEEAFETGNQFRNSLSFSGGSEKFSFLTSVSQLKHNGVLPATDFKNYQARLNTNFTLSEKLKGGSSLAVTNSGGYRGNANRYAEQLIYWTPRYNVRDYLMDNGTMKSYGETDNPIYVAHTNRFKDDVLRVIGGFDLTYSPAKWVDLMYRVGIDAYRDNREGTAIGYQGLADERLVYDNGVEGADGRGFYNVYNNNFRALTSTFIATFKHDFNDDLNATLRVGQDVYDRFIKRTATEGGDLTVYNWFDLGNANIIKAATYNEKYRLMGFFGELNLAYKDYLFLTLTGRNDITSTLSKNNRSFFYPSATLSYVLSDQFSMPEAINFAKLRLSYAQIGKDAAPYSTSAGFAPYTNLPTGYIGFTRPSLLGDPQLKPEFTDTYEVGMEMKFLNSRLGLDVNFYNSVSKDQIIQVPVSSTTGFVTASINAGSIRNRGLEITLNTTPVKKDNFSWNSDINFSFNRNKILYIREDLDDEIVVSSEYGYLNSTVSMRIRPGESYGTLYGRTYKRYYTPDEIAQGLDKTREYDESRPMLIGANGFPVLESTSVPKKLGNVQPSWVGGWNNTFNYKSLSLNVLVDARVGQYRYNQLGNFMAAFGEADYTENRNDYKVFDGVLADGSKNTKEVWLGQGKDPKNGVDYGNGYYRDNFRGNSQAFVEDASWLRLRSVSIGYSLPQQWLENKFVKNARVSLIGNNLALWTKYSGYDPENSTTASGSNIEGFAGMTYPAVRSFLFSLNVGF
>NZ_LT906468.1|WP_093098820.1|1071679_1073131_-|RagB/SusD-family-nutrient-uptake-outer-membrane-protein
MKKNSLYIIALASLSLFSCKDFLDVKPTNSTDSSVTIQTVADAKVMINGLTRQIVKSSLFGRNLMLYGDAKGGDLTIVSQGRGLDALYVFNHSINNNNYSDFWADGYNAIMQANNIIKSIDDLQAAGTELDFNNFEGQALTIRALLHFELVKLYGKTYTQDPNALGVPIVTEALSTSAQPLRNKVSEVYGQIVKDLTAAADLLPKTKANGYINYYANRVILSRVYMTMGDFDKALAAAEEVIDSKVYSLYSNAEWVPSWANQFGKESIFEITLAKDQGDLGSASLGFYYLRNKDNNALGNFTASDYFLSRLGQDEEDVRWGIFTKDELDRQAACYKYVGSVEKDGDGKDTYTAVNIKVARLSEVYLNAAEAALKKPSADKAKAATYLNEIRKRAPELAPATAATVTEAMILDEKSKELYGEGQRYWDMIRTNKTITFNDEHVGVTMSHREKSINRTFFKTILPIPQVEINANPGLEAQQNPGY
>NZ_LT906468.1|WP_093098822.1|1073149_1076323_-|TonB-dependent-receptor
MKHHLLTTLCVVACTSMQVVNAQQIAVAGKVSGSDGTPLIGVTVSVKGTTISTSTNENGLFSLNADHNATLVVSYIGYTSQEIPLNGRKAINITLNQDDQAIDEVMVVAYGTAKKSSFTGSAATVNYEKEAKDIPVTSFEQALTGRVPGVQINTTSGQAGSTSSIRVRGIGSMNASNEPLYVVDGVPVVSGNVGQMSGALSGSSNNIMSTINPNDIESISILKDAAASSLYGSRAANGVVIITTKSGKAGKPKIDFRTSYAVTPTWATDNYKPGNPQEQIQYFYQIFHDYRTSNGYTQEQANQYALNRMNTRFGIHGYEFSSEGTGLYDKIIIKGKTDGVENRDGQYFDWNEALFRTGKYQTNDLAVSGASDKTKYYSSLSYTTDKGRAYTNEFERIGGRLNFSQKLSEKVEFATNFNLNHNNKEGYNDTRNTGTNYMYLANNLLFPFYWPTDYKTGKEYTTRYNSLGYNPLYYDKQWENTSKTLRIVAAPSLTVKFLPELTGKTIFSYDNAEVKDHLYYSPLHYHTTYGATANGTVFEYSTNYKKLISSSTLNYNKTFATEHTLDLLVGFEAEKNETNYQFASGSNLPSSSLHTVATAGIKDADAYMWGNNMMSIFSRAEYNYKNTYFLSGSLRRDGNSRLGPDTRWGNFWSLSAAWNLKNESFISEIEQINLLKLKASYGTNGTLPTSNFGWRSLASYGYNYMDQPGGILTTIADKDLKWEKSHTFNVGAEFGLFNNRLYGTVEYFNRDSKDLLQDVNISLVTGFNSTLLNVGEINNKGIEISLGGDLIKKDDFRWSANVNTSFLKSKVSKLYGGKDITWWDPTGGDARVQFIYKEGEDVYSYYMAEWAGVDASNGKPMWYTNDGTEGEFLHNGRGATNKVSDAKQVIVGSPIPKAYGGFNTDIEYKGFSLGLNFTYKIGGKLFDAGSRDVAEDGYYWERIRSYYAIQNVWTPDNPNSLYPFVSGNDPEDGITRSTRHLYDASFLRLKNVNVSYRLPNTVVSKIGFSNARIFFNGTNLLTASKFKWADPEVNQYGTRGWETPFGKTYTFGLEVSL
>NZ_LT906468.1|WP_093098824.1|1076396_1077449_-|dipeptide-epimerase
MNSNEWQSKKMGKFTLRFKPYTLELRHVFTVASFSRSTTPVVLTELEYDGIIGYGEASMPPYLGESQESVMNFLNKIDLSRFNSPFQTEEILHYIDQVDAKNTAAKAAVDIALHDVLGKIMGQPFYKIWGLNPDLIPPTSYTIGIDTEEMIRKKVAEAQQFKILKVKLGLDTDKMIIDTIRSVTDVPLCADVNQGWKNKEEALEMSHWLKERNVVFLEQPMPKEMIDENAWLTERSPIPTIADEGCQRLADVPALKDVYTGINIKLMKCTGMREAKRMAELARSLEMKVMLGCMTETSCAITAAAQLAPLVDWADLDGALLIGNDIYDGMTVKDGLCHLPDRPGIGILKI
>NZ_LT906468.1|WP_093098826.1|1077451_1078669_-|C40-family-peptidase
MMIRITALFCTFFCLNTTSYAQTDSTIYKKVDQIVQDAKQQFAPDKRTKIVALTEANAINNQYVIESSVAEASNYIKVQSANIPATIRINALPDSSVGKKVHGVVNLSVANFRTKPGNASEMATQAILGTEVDLLQKVDGEYRARTPEGYISYVPASSIAAMDQADLEKWRKLPKLIYTAEFGKSLSKADPKSVRVSDLVYGNILGLLAEEGNYYKVTYPDHRIAFIPKDEALTFDKWLNSRELTADNVISSAKTMMGLPYLWGGTSVKGVDCSGFTKTAYYMNGYIIPRDASQQVLAGQNIDILDKDGHFDAKKALKNLKPADLLFFASGKNSNPNARVTHVALYIGNGEFIHSAGTVRINSMLKDAANYDDFQTRTVVAAKRYIGVKDQQVQKIQENPYYNQK
>NZ_LT906468.1|WP_093098828.1|1078840_1079875_+|N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase
MHSRRKFIKQGIIGAASIGTVASAISCQATEKAAKSVRKPIVISTWDFGVAANQAAWEILKKKGRALDAVEAGVKIPEADLKNVTVGKGGYPDRDGHVTLDACIMDELGNCGSVAAMEDIAHPISVARLVMEKTPHVMLVGDGARQFALENGFQAENLLTPSSEEAWKEWLKEKNYKPVMNIENKSFATERLPGNKYNHDTIGMLALDADGNLSGACTTSGMAFKMHGRVGDSPIIGAGLYVDNEVGGATSTGVGEEVIRNVGSFLVVELMRQGYSPEDACKEAVMRIVKKKPEIAKDIQVGFLALNKNGEYGSYALQDGFTFAICDDKQQDLIEKGKFHYKPK
>NZ_LT906468.1|WP_093098829.1|1080182_1081745_+|DNA/RNA-non-specific-endonuclease
MFRRLLFIFTVTLLFFSSCRKDFGWVPDQQKKSILFSSKISGQVLTRMSGSQWDNNDSISVFMYHGDALNQNTVLSEGFNKQFITNSSGNFSPKTTADAMNFPADKEVRFVAFYPYKNSLDFHRDLDISDQEDQDQIDYLLGKSASTLGYQQGAVQLKFERVMAKIQVRVKAKGIQAVTAKLSPLLTAATFQIGQAELNPQKTFKDVSGKVISTGDETVIEWVVFPGKLESQSRMVFKSNTGETYTWEIGKLGTEYEQGNRYSYDINLSDGGIVDPKPAVSYMELPVISNSTELEYNFKMTPDRSKRNYSMLYDKKNRIAHWVAYPLSKDYLGRQSRTNRWAFDPNFPDYTQPLLRKGFGVSGIDRGHQIPSADRTRNAAENATTFYYTNMTAQTSSLNQGVWAKLENQIRSWTTVSGVDTMYVVTGAGLSFANGSIDYVQDNQGNRVAKPKYYYKALAVKRGTAYYTIGFYMENKVTPTKANFSSYRMTVSELERKTGYQFFPGIPRETKNKINDAIWR
>NZ_LT906468.1|WP_093098831.1|1081776_1083174_+|fimbrillin-family-protein
MKTKQLLGAALAFIALVSSCKKDDYRKLEKTNPSEVQFTSRILGTQATKANGNTWDSNDEIGVFMKQGTGLSNILAGNKKYSTNGNGNFSASGNNVINYPEAGQVDFIAYYPYSADLKGTSLGFNISEQSNPAKIDVMYSNNAKSLSKGSKTASLEFAHKLAKVELIVKAGKGVSNLTGLKTAYNNIPTLSNMDLATGTIANGSGAANVQAKVTAQQENQLVEAILIPGEYSAKEVVFSIGSDNYKWTLPANLNYESGKKYTYNITLQLGGSVAVTGNAIITDWISVTGGTHTIGKDGGTVTPPVPTGTEQTIYEENFGDLGAGNRIKIDQYTGFSNKTVKYSNLYTTGWVDIRKISTQDAHVWFAANRTTGLKIEGINTTGYRDLKLTYILAANGSGEPVEGLKVRINGNELQPKGVLGGQNEFSVQTISSGIPAAAITIEFDAQSANNKNGYRVDDIKLVGTK
>NZ_LT906468.1|WP_093098832.1|1083248_1085996_+|TonB-dependent-receptor
MQKIFSIIFLLTCLCTTVFGQGGIQLTGKVVHSRTKVPLLGISVTLEQNKMNSSTNEEGEFVFVNLKAGPEKIIIQSAGFRNYEMDFELKDSTSMKLEDIALVAENQIDVQTVLGVIDDDVISSDGDKSSQDIQASVILSNDLYLNKVGFKLFPYRFRVRGYDPNYEQIYINGILANDQYRRVFNYASIGALNDLTRNGDVVNYNQIGTYTFGTIGGSENINMRASSYAKGGKLTMSYTNRNYYARSMFSYSTGLNEKGWAFTGAVGGRFSDKGYIPGTSYRNLSYALSMEKQWQDGDHSLSVLTFGSPVIRGQQGSSFQEVYDLVGNNLYNPNWGYQNGKVRNSRMVHAFDPTMVISHRWKIDERSSLTSGGILHYGRYSNSALNWYNAMDPRPDYYRYLPSNFSRFTPNLDARTIQQYTQLWKSRDPNVTQLNWEELYRQNLNTENKRKMNGAALYTLERRHSDLLEGTVNVTFNKLYQNNFNLTAGIEARKTRSYQYKTIDDLLGADHVLDLDKFAERENPGNENVKQNDLQFPNRKVYEGDIFGYDYDIDIQAVNAWVSNSFQSRNLELYYGTKISYTDFRRVGNMRNGRFPDHSFGKGPKYDFVDFTVKAGLTYKFDGRNFLSANSAYITEPPAPDRSFVMPRVTDRVVQGLSSGRIFHNDINYVFSLPHLSGRLSLFQTNFYDQLERMNYYHDSQRTFVFHNLSGVDRKHRGVEASLTYSLNQNWNFDFIGTLAEYFYSNNPMGTMNSENGLLLNREEKVYMKNLFVSGTPQAAGIIAARYFYDYWFLEMSGNLVGWNYMSSAALRRMASVYATVSPQQENFESYRKLTSQERLQSNFTIDASVGKMIYLKKRRSLNFNLSIMNLLNQKNIGTGGFEQGRLDLVYPERFSSRYFYMQGFNVFFNTSYRF

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Crispr_ID: NZ_LT906468_7

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LT906468_7

1227443-1227526

Orphan

Consensus_repeat	Method
GTTACTTTTGAAGCCCAAAAGTA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_LT906468_7

>merge|NZ_LT906468|7|1227443-1227526|CRISPRCasFinder
GTTACTTTTGAAGCCCAAAAGTACCAAACCGACGAAGGAGCTCACGGATACCAATCTCATTGTTACTTTTGGAGCCCAAAAGTA

>NZ_LT906468|7|7|1227443-1227526|CRISPRCasFinder
GTTACTTTTGAAGCCCAAAAGTA	CCAAACCGACGAAGGAGCTCACGGATACCAATCTCATT
GTTACTTTTGGAGCCCAAAAGTA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LT906468.1\|WP_093098991.1\|1224478_1225180_-\|ATP-dependent-Clp-endopeptidase-proteolytic-subunit-ClpP	unknown	unknown	gnl\|CDD\|184722
NZ_LT906468.1\|WP_093098995.1\|1226776_1227343_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906468.1\|WP_093099004.1\|1235313_1235892_-\|TetR/AcrR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224228
NZ_LT906468.1\|WP_093098984.1\|1217965_1219465_+\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	unknown	unknown	gnl\|CDD\|185760
NZ_LT906468.1\|WP_093099003.1\|1233976_1235308_-\|TolC-family-protein	unknown	unknown	gnl\|CDD\|224455
NZ_LT906468.1\|WP_093099010.1\|1238053_1238575_-\|YiiD-C-terminal-domain-containing-protein	unknown	unknown	gnl\|CDD\|239524
NZ_LT906468.1\|WP_093098993.1\|1225221_1225692_-\|type-I-restriction-enzyme-HsdR-N-terminal-domain-containing-protein	unknown	unknown	gnl\|CDD\|372640
NZ_LT906468.1\|WP_093099001.1\|1232779_1233934_-\|efflux-RND-transporter-periplasmic-adaptor-subunit	unknown	unknown	gnl\|CDD\|273776
NZ_LT906468.1\|WP_093099000.1\|1229580_1232751_-\|multidrug-efflux-RND-transporter-permease-subunit	unknown	unknown	gnl\|CDD\|273335
NZ_LT906468.1\|WP_093099009.1\|1237616_1238042_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906468.1\|WP_093098985.1\|1220151_1220853_-\|FkbM-family-methyltransferase	unknown	unknown	gnl\|CDD\|273628
NZ_LT906468.1\|WP_093099006.1\|1236536_1236962_-\|cytochrome-c	unknown	unknown	gnl\|CDD\|224921
NZ_LT906468.1\|WP_093099012.1\|1238667_1239891_+\|MFS-transporter	unknown	unknown	gnl\|CDD\|340874
NZ_LT906468.1\|WP_093098987.1\|1220899_1222264_-\|pyridoxal-phosphate-dependent-enzyme	unknown	unknown	gnl\|CDD\|273464
NZ_LT906468.1\|WP_093098998.1\|1228737_1229511_+\|CDGSH-iron-sulfur-domain-containing-protein	unknown	unknown	gnl\|CDD\|378163
NZ_LT906468.1\|WP_093098988.1\|1222313_1223153_-\|AMP-nucleosidase	unknown	unknown	gnl\|CDD\|235940
NZ_LT906468.1\|WP_157739393.1\|1214840_1217948_+\|SusC/RagA-family-TonB-linked-outer-membrane-protein	unknown	unknown	gnl\|CDD\|274948
NZ_LT906468.1\|WP_093098990.1\|1223222_1224473_-\|ATP-dependent-Clp-protease-ATP-binding-subunit-ClpX	unknown	unknown	gnl\|CDD\|235422
NZ_LT906468.1\|WP_093099007.1\|1236961_1237606_-\|SCO-family-protein	unknown	unknown	gnl\|CDD\|376869
NZ_LT906468.1\|WP_093098994.1\|1225764_1226772_+\|DNA-polymerase-III-subunit-delta	unknown	unknown	gnl\|CDD\|273455

Protein	Function_ID	Function_description	E-value
NZ_LT906468.1\|WP_093098991.1\|1224478_1225180_-\|ATP-dependent-Clp-endopeptidase-proteolytic-subunit-ClpP	gnl\|CDD\|184722	PRK14514, PRK14514, ATP-dependent Clp endopeptidase proteolytic subunit ClpP.	1.23973e-118
NZ_LT906468.1\|WP_093098990.1\|1223222_1224473_-\|ATP-dependent-Clp-protease-ATP-binding-subunit-ClpX	gnl\|CDD\|235422	PRK05342, clpX, ATP-dependent Clp protease ATP-binding subunit ClpX.	0
NZ_LT906468.1\|WP_093099004.1\|1235313_1235892_-\|TetR/AcrR-family-transcriptional-regulator	gnl\|CDD\|224228	COG1309, AcrR, Transcriptional regulator [Transcription].	1.1977e-18
NZ_LT906468.1\|WP_093098984.1\|1217965_1219465_+\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	gnl\|CDD\|185760	cd08977, SusD, starch binding outer membrane protein SusD. SusD-like proteins from Bacteroidetes, members of the human distal gut microbiota, are part of the starch utilization system (Sus). Sus is one of the large clusters of glycosyl hydrolases, called polysaccharide utilization loci (PULs), which play an important role in polysaccharide recognition and uptake, and it is needed for growth on amylose, amylopectin, pullulan, and maltooligosaccharides. SusD, together with SusC, a predicted beta-barrel porin, forms the minimum outer-membrane starch-binding complex. The adult human distal gut microbiota is essential for digestion of a large variety of dietary polysaccharides, for which humans lack the necessary glycosyl hydrolases.	2.05092e-36
NZ_LT906468.1\|WP_093099003.1\|1233976_1235308_-\|TolC-family-protein	gnl\|CDD\|224455	COG1538, TolC, Outer membrane protein [Cell envelope biogenesis, outer membrane / Intracellular trafficking and secretion].	2.48848e-45
NZ_LT906468.1\|WP_093099010.1\|1238053_1238575_-\|YiiD-C-terminal-domain-containing-protein	gnl\|CDD\|239524	cd03440, hot_dog, The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase) structure and subsequently in 4HBT (4-hydroxybenzoyl-CoA thioesterase) from Pseudomonas. A number of other seemingly unrelated proteins also share the hotdog fold. These proteins have related, but distinct, catalytic activities that include metabolic roles such as thioester hydrolysis in fatty acid metabolism, and degradation of phenylacetic acid and the environmental pollutant 4-chlorobenzoate. This superfamily also includes the PaaI-like protein FapR, a non-catalytic bacterial homolog involved in transcriptional regulation of fatty acid biosynthesis.	2.32889e-05
NZ_LT906468.1\|WP_093098993.1\|1225221_1225692_-\|type-I-restriction-enzyme-HsdR-N-terminal-domain-containing-protein	gnl\|CDD\|372640	pfam13588, HSDR_N_2, Type I restriction enzyme R protein N-terminus (HSDR_N). This family consists of a number of N terminal regions found in type I restriction enzyme R (HSDR) proteins. Restriction and modification (R/M) systems are found in a wide variety of prokaryotes and are thought to protect the host bacterium from the uptake of foreign DNA. Type I restriction and modification systems are encoded by three genes: hsdR, hsdM, and hsdS. The three polypeptides, HsdR, HsdM, and HsdS, often assemble to give an enzyme (R2M2S1) that modifies hemimethylated DNA and restricts unmethylated DNA.	1.16746e-42
NZ_LT906468.1\|WP_093098998.1\|1228737_1229511_+\|CDGSH-iron-sulfur-domain-containing-protein	gnl\|CDD\|378163	pfam09360, zf-CDGSH, Iron-binding zinc finger CDGSH type. The CDGSH-type zinc finger domain binds iron rather than zinc as a redox-active pH-labile 2Fe-2S cluster. The conserved sequence C-X-C-X2-(S/T)-X3-P-X-C-D-G-(S/A/T)-H is a defining feature of this family. The domain is oriented towards the cytoplasm and is tethered to the mitochondrial membrane by a more N-terminal domain found in higher vertebrates, MitoNEET_N, pfam10660. The domain forms a uniquely folded homo-dimer and spans the outer mitochondrial membrane, orienting the iron-binding residues towards the cytoplasm.	1.15402e-14
NZ_LT906468.1\|WP_093098985.1\|1220151_1220853_-\|FkbM-family-methyltransferase	gnl\|CDD\|273628	TIGR01444, 2-O-methyltransferase_NoeI, methyltransferase, FkbM family. Members of this family are characterized by two well-conserved short regions separated by a variable in both sequence and length. The first of the two regions is found in a large number of proteins outside this subfamily, a number of which have been characterized as methyltransferases. One member of the present family, FkbM, was shown to be required for a specific methylation in the biosynthesis of the immunosuppressant FK506 in Streptomyces strain MA6548.	6.52948e-11
NZ_LT906468.1\|WP_093099006.1\|1236536_1236962_-\|cytochrome-c	gnl\|CDD\|224921	COG2010, CccA, Cytochrome c, mono- and diheme variants [Energy production and conversion].	9.12313e-09
NZ_LT906468.1\|WP_093099012.1\|1238667_1239891_+\|MFS-transporter	gnl\|CDD\|340874	cd17316, MFS_SV2_like, Metazoan Synaptic vesicle glycoprotein 2 (SV2) and related small molecule transporters of the Major Facilitator Superfamily. This family is composed of metazoan synaptic vesicle glycoprotein 2 (SV2) and related small molecule transporters including those that transport inorganic phosphate (Pht), aromatic compounds (PcaK and related proteins), proline/betaine (ProP), alpha-ketoglutarate (KgtP), citrate (CitA), shikimate (ShiA), and cis,cis-muconate (MucK), among others. SV2 is a transporter-like protein that serves as the receptor for botulinum neurotoxin A (BoNT/A), one of seven neurotoxins produced by the bacterium Clostridium botulinum. BoNT/A blocks neurotransmitter release by cleaving synaptosome-associated protein of 25 kD (SNAP-25) within presynaptic nerve terminals. Also included in this family is synaptic vesicle 2 (SV2)-related protein (SVOP) and similar proteins. SVOP is a transporter-like nucleotide binding protein that localizes to neurotransmitter-containing vesicles. The SV2-like family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	8.28271e-31
NZ_LT906468.1\|WP_093098987.1\|1220899_1222264_-\|pyridoxal-phosphate-dependent-enzyme	gnl\|CDD\|273464	TIGR01137, Cystathionine_beta-synthase, cystathionine beta-synthase. Members of this family closely resemble cysteine synthase but contain an additional C-terminal CBS domain. The function of any bacterial member included in this family is proposed but not proven. [Amino acid biosynthesis, Serine family].	8.84859e-164
NZ_LT906468.1\|WP_093099000.1\|1229580_1232751_-\|multidrug-efflux-RND-transporter-permease-subunit	gnl\|CDD\|273335	TIGR00915, Probable_aminoglycoside_efflux_pump, The (Largely Gram-negative Bacterial) Hydrophobe/Amphiphile Efflux-1 (HAE1) Family. Proteins scoring above the trusted cutoff (1000) form a tight clade within the RND (Resistance-Nodulation-Cell Division) superfamily. Proteins scoring greater than the noise cutoff (100) appear to form a larger clade, cleanly separated from more distant homologs that include cadmium/zinc/cobalt resistance transporters. This family is one of several subfamilies within the scope of pfam00873. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate].	0
NZ_LT906468.1\|WP_093098988.1\|1222313_1223153_-\|AMP-nucleosidase	gnl\|CDD\|235940	PRK07115, PRK07115, AMP nucleosidase; Provisional.	4.20551e-177
NZ_LT906468.1\|WP_157739393.1\|1214840_1217948_+\|SusC/RagA-family-TonB-linked-outer-membrane-protein	gnl\|CDD\|274948	TIGR04056, OMP_RagA_SusC, TonB-linked outer membrane protein, SusC/RagA family. This model describes a distinctive clade among the TonB-linked outer membrane proteins (OMP). Members of this family are restricted to the Bacteriodetes lineage (except for Gemmatimonas aurantiaca T-27 from the novel phylum Gemmatimonadetes) and occur in high copy numbers, with over 100 members from Bacteroides thetaiotaomicron VPI-5482 alone. Published descriptions of members of this family are available for RagA from Porphyromonas gingivalis, SusC from Bacteroides thetaiotaomicron, and OmpW from Bacteroides caccae. Members form pairs with members of the SusD/RagB family (pfam07980). Transporter complexes including these outer membrane proteins are likely to import large degradation products of proteins (e.g. RagA) or carbohydrates (e.g. SusC) as nutrients, rather than siderophores. [Transport and binding proteins, Unknown substrate].	0
NZ_LT906468.1\|WP_093099001.1\|1232779_1233934_-\|efflux-RND-transporter-periplasmic-adaptor-subunit	gnl\|CDD\|273776	TIGR01730, COG0845:_Membrane-fusion_protein, RND family efflux transporter, MFP subunit. This model represents the MFP (membrane fusion protein) component of the RND family of transporters. RND refers to Resistance, Nodulation, and cell Division. It is, in part, a subfamily of pfam00529 (Pfam release 7.5) but hits substantial numbers of proteins missed by that model. The related HlyD secretion protein, for which pfam00529 is named, is outside the scope of this model. Attributed functions imply outward transport. These functions include nodulation, acriflavin resistance, heavy metal efflux, and multidrug resistance proteins. Most members of this family are found in Gram-negative bacteria. The proposed function of MFP proteins is to bring the inner and outer membranes together and enable transport to the outside of the outer membrane. Note, however, that a few members of this family are found in Gram-positive bacteria, where there is no outer membrane. [Transport and binding proteins, Unknown substrate].	2.67166e-79
NZ_LT906468.1\|WP_093099007.1\|1236961_1237606_-\|SCO-family-protein	gnl\|CDD\|376869	pfam02630, SCO1-SenC, SCO1/SenC. This family is involved in biogenesis of respiratory and photosynthetic systems. SCO1 is required for a post-translational step in the accumulation of subunits COXI and COXII of cytochrome c oxidase. SenC is required for optimal cytochrome c oxidase activity and maximal induction of genes encoding the light-harvesting and reaction centre complexes of R. capsulatus.	3.76721e-29
NZ_LT906468.1\|WP_093098994.1\|1225764_1226772_+\|DNA-polymerase-III-subunit-delta	gnl\|CDD\|273455	TIGR01128, DNA_polymerase_III_subunit_delta, DNA polymerase III, delta subunit. DNA polymerase III delta (holA) and delta prime (holB) subunits are distinct proteins encoded by separate genes. The delta prime subunit (holB) exhibits sequence homology to the tau and gamma subunits (dnaX), but the delta subunit (holA) does not demonstrate this same homology with dnaX. The delta, delta prime, gamma, chi and psi subunits form the gamma complex subassembly of DNA polymerase III holoenzyme, which couples ATP to assemble the ring-shaped beta subunit around DNA forming a DNA sliding clamp. [DNA metabolism, DNA replication, recombination, and repair].	5.41819e-41

>NZ_LT906468.1|WP_093098995.1|1226776_1227343_+|hypothetical-protein
MQKLFSFFILMLISSLGFAQSSFYTLIQGGGNLGVRNPGYEGTFNGYSLHFIFGKNFDDKAYLGLGIGNETLKGDYTKSGEAGNTEVRKSKYDRNLFPIFIDGRLPVKDFGQASRVGIVANAGYSASIGPVYDKGFMGKAGLFYLYDSLSKTKFTVSATYAYQQLHGSFYTSNFDHQHLNVSVGIMLK
>NZ_LT906468.1|WP_093098994.1|1225764_1226772_+|DNA-polymerase-III-subunit-delta
MNVQSILSDIKKKKLAPVYLLHGEEPYFIDLISDAIEQTVLDDSQKGFDQSVVYGKDADFSNIISMAKRYPMMSNHQVIIVKEAQNLKWKDDEFLLKYLEQPTPSTVLVFAHKYSKFDKRKKSYKSMEKAGIVLESNKLYEDKVAGWINEQLNASGRKVHPQAAALMAEYLGTDLSKIANEIEKLQLNIPAEKEITAVDVEQNIGISKDFNVFELNTALSKRNALKAFQIVDYFAANPKSNPMPVVIGSLGTYFTKILKYHYLPDKSSAVAAKQLGVHPFFVREYEYAARNFNRRKTFEIIHLIKEFDLKSKGMNVGHLTESGDLLTELIYKILN
>NZ_LT906468.1|WP_093098993.1|1225221_1225692_-|type-I-restriction-enzyme-HsdR-N-terminal-domain-containing-protein
MFRPVPLNLPPFPAKISKKQDQYFIFDELRKKHLLLTPEEWVRQHWVSHLNKHYQYPMALMKIEGGLSLNSLQKRSDLVVYDREGSRVLLAEFKAPSVKITEKTFEQIANYNSIYKIPLLLVSNGIEHYYCRIDFEEEKFTFITELPSFGQENFGY
>NZ_LT906468.1|WP_093098991.1|1224478_1225180_-|ATP-dependent-Clp-endopeptidase-proteolytic-subunit-ClpP
MNIDKNEFRKYAIKHHRIGSQHVDGYISRLQQQIPSNLTPYIIEERQLNVAQMDVFSRLMMDRIIFLGDGINDQVANIVQAQLLFLQSTDAQRDIQIYINSPGGSVYAGLGIYDTMQYISPDVATICTGMAASMGAVLLVAGAKGKRAALRHSRVMIHQPSGGAQGVAADMEINLREMLKLKEELYTIIADHSGQTYDWVEKSSDRDYWMRAAEAKEFGMIDEVLLPKKKETK
>NZ_LT906468.1|WP_093098990.1|1223222_1224473_-|ATP-dependent-Clp-protease-ATP-binding-subunit-ClpX
MSKSNNRDIHCSFCGISKNEAQMLIAGDGAHICDRCVQQAGEILAEELKQRKNKSIQTALKLIRPKEIKEHLDQYVIGQDDAKKVISVAVYNHYKRLNQRVESDETEIEKSNLIIVGETGTGKTLLAKTVAKILNVPFCIVDATVLTEAGYVGEDVESILTRLLQAADYDVAAAERGIIYIDEIDKIARKSDNPSITRDVSGEGVQQALLKILEGTNVNVPPQGGRKHPDQKMISVNTSNILFICGGAFDGIQKKIANRLRTQTVGYKMKDEDQEIDLNNLYKYITPQDLKNFGLIPELIGRLPVLTHLNPLDKETLLSILTKPKNALVKQYIKLFEYEGIKLSFEPEVYDFIVDKAWEFKLGARGLRSICEAIMLDAMFETPSNKENSEDKTLQISLDYAKNKFAKTDFKKLQVA
>NZ_LT906468.1|WP_093098988.1|1222313_1223153_-|AMP-nucleosidase
MTKKKDEKQENIEEVNSPITAGLKTKEDIVNNWLPRYTGRPLEEFGEYILLTNFSNYVKLFSQMHGDAPILGEDKPMQTCSADGITIINFGMGSPVAATVMDLLTAIHPKAVLFLGKTGVLKKKIDVGELILPIAAIRGEGTSNDYLPPEVPSLPAFALQKAISTTIRDHSRDYWTGTVYTTNRRVWEHDKQFKKYLKSIRAMAVDMETATIFSVGFANKIPTGALLLVSDQPMVPEGVKTDKSDVTVTKSYVETHVKIGIDALKQLINNGLTVKHLKF
>NZ_LT906468.1|WP_093098987.1|1220899_1222264_-|pyridoxal-phosphate-dependent-enzyme
MWYNNILETIGNTPLVKLNKITENLKGTILAKIETSNPGNSIKDRMALKMIEDAEEAGLLKPGGTIIEGTSGNTGMGLAMAAVVKGYRCIFTTTDKQSKEKIDALRAFGAEVIVCPTNVDPEDPRSYYSVSSRLEKEVPNAWKANQYDNLSNSKAHYEQTGPEIWEQTEGKITHLVVGVGTGGTISGTAKYLREQNPNIKVWGIDTYGSVFKKYKETGIFDKNEIYPYITEGIGEDFLPKNVDFSVIDLFEKVTDKDAALMTRDLARKEGIFAGNSAGAALAGLLQLGKDLKEDDVVVVIFHDHGSRYMGKMYNEDWLRERGFLKDEKLTAKSILKKRGEQAIVTADANQTVVETFNIMKSLNISQIPVTQQGMVIGKVTESDILSALLENPSLKSSAVEEITSKPFPFVDLNTSIDKISGLINKDTQAVLVEDDFGRINIITQYDIINAISEV
>NZ_LT906468.1|WP_093098985.1|1220151_1220853_-|FkbM-family-methyltransferase
MERNDKLKRLEYWIKARIGKIAFIDVEEKRAKEWYGNGYGGFYVDPSLVTVNAIVYSFGIGEDISFDKAIIAKHGAKVFGFDPTPKSINYVRNNETPEQFYFHPFGLGEKTEMVTFHLPKNKEHVSGSVYDHSLVDEHDSVDVLLKEFKEIVHDLGHQSIDVLKMDIEGSEYAVMEGILNSGIPIKQILVETHERFFANGKEKGKEFFKLLHDHGYRIFAISDTYQEISLVKG
>NZ_LT906468.1|WP_093098984.1|1217965_1219465_+|RagB/SusD-family-nutrient-uptake-outer-membrane-protein
MKKRNLTIYASVLLLALSGCKKDYLETAPTDKVSQDEIFSSIANANTALNGIYRFMFERTTVVDWNVQNKPGVGGIMLGLDFMGEDLGISDANWFGSTGEGNWQGGRNDNHKLTEYYYRTFYKIIGDSNFILDNVDGLPGTDEEKNNLKAQALTLRAYAYSNLVQLYAKRYDASTANDQLGVPLVLKSSDGALPRSTVKDVYASIIKDLDDAVALNVQTRVNKSHINVYVTYGIRARVALTMQDYPNAIKFANLVIESGSFPLMNQDTYMKGFNDAPSMSEFMWASMPTQDQMDAFGSYFAQIAYNANTSFMRANPKRINSALYEKISDTDIRKKLWEPKPTAANFPLPLASFARQEYMSRKFAIKSPGGALGDVPLMRSAEMHLILAEAYASSNQTANAQEALFNFVKVRDLEATKSTNTGAALLEEIWTNRRTELWGEGFRFYDLKRLNQPLDRTVVPNYAPGSVNGMVKVAAGAKDWQFLFPLLELNANPEIKQND
>NZ_LT906468.1|WP_157739393.1|1214840_1217948_+|SusC/RagA-family-TonB-linked-outer-membrane-protein
MSGTVTSANDGQALPGVSVRVSGSTNATQTDANGKYTLTNVASGSSITFSFIGYASQTVTVSNNNIINVQLSLSGEELDEVVVVAYGTAKKSEVTGSMATMSAEDLDKRTVSNVSNALAGMAPGISVSSGNGQPGSGASVRLRGIGSMSASSSPLYVVDGAVFDGNIGDLNADDIESISILKDATSAALYGSRAGNGVIMITTKKGRGATKLNVGLTQGITQRGIQEYETVGINDYYPVAFQAIKNSRMFPANGSQGASEADANKYAFDNIKRFLAYNPFNVADNEIVSLDGTMNPNAGLKYDDFNWFDAIQRVGKRTDANINIGGSNEKTDYYVSLGYLNDQGYILNSDFQRFNGRINVNSQIKDWLKAGVNISGAMSEGSLASDASTGNANSYVNPFSFIRGLGSIYPVHAFDATTGAPVVDPVTGEQYYDYGMHPGAINRPSGASPGRHVIYETILNTRLNKRTMLGGRAFMEIKFLKDFTFTPTVTIDLSNRNFDYSWNNKVGDGVSYNGLGSAENYITKSYTFNQVLQYRKSFDLHNVSAIAGHENYDYQFSSRNATKTGQITSGITELDNYVTPLSAGGYKNVNRLESYFARASYNYDEKYYADASFRTDGSSIFDDSKRWGNFFSVGAAWAINKEDFMSSATWVNDLRLKASYGQVGNNHLLDVNGNRIYYGYQALYNLGWSNGGLPGTVLSSLANPNLTWESSNTFNVGVNFSLFNNRLRGEAEYYKRGSDELLLSVPRPLSSAVSTEFRNVGSMYNTGFELSLTGDIVRNDNFTWTLTKNFTTFKNEITKMPVETPVITAGNKRREVGRDYYAFWLRQYAGVDHADGSALYIPADGTAQENIRVVDGKEYVTNQNYAKFDYSGTSIPDVMGSIINTFDYKAFTLSFLLNYQIGGKIYDGNYVGLMSTNSYGKSYHVDAMKAWTTTNTTSDIPRLDQANSNNINAASTRWLTSASYFSIQNVNFQYRLPSSLLNKIDLSTARVFFTGENLALFSKRKGMNPTESFDGSVSSTYLPTRIFSIGVNVGF
>NZ_LT906468.1|WP_093098998.1|1228737_1229511_+|CDGSH-iron-sulfur-domain-containing-protein
MKLEKDKLDIQLGTILNKESIFMEVTKDGPYVLHGKAPIVQQFIVANSAGISVAYQEGKEFKTEDSDIYLCRCGLSKYKPYCDNSHLKAAENGVDLTETATFNPEFATAEIIKGPVVSLSDDEKLCAFARFCDNGQRIWNEVQESKHESVELTVGMAHHCPAGRLIVWDGGKPIEDKDIKPRIGLIEDMPNNCAGPLALWGAIPVKSSNGKYYEVRNRQTLCRCGQSSNKPFCDGTHASMGFQDGLDKQPNPEGNLF
>NZ_LT906468.1|WP_093099000.1|1229580_1232751_-|multidrug-efflux-RND-transporter-permease-subunit
MISEVFIKRPVTAMVVSILISIIGVIAITTLPISQYPNIAPPTVSVSATYTGADAQTVEKTVTTPIESQINGTPGMIYMSSNSTSDGGSRITVTFEVGTDIDIATLDVQNRVSIAEPVLPEAVRRLGVTTRKVNTDILMMVSLVSPDGSRDINFLSNYINLYLKDALLRVPGVGDVQAFGQPFAMRVWLDANKLANIGMSPADVNTAIQEQNSRMPGGSVGARPQENMQVFEYPIVMDSDLEEVDQFENIVVKTNADGSIVLLKDIARVELGQFNYGITNKVNGNTASGMMISQTPGGNAVETADGIYKTLEELKKSFPSGVDYVVGYETVSVVNASISSVIHTLIEALILVTLVVFFFLQSWRATLIPLLAIPVSIVGTFIFFTLFGFSINNLTMLAFVLAIGIVVDDAIVVVEAVQHYIDHYKMDAKEATMRAMKDITAPVIAIALILAAVFVPVGFIPGMVGKLYQQFAITIAVSVMLSAFIALSLTPALCSIMLKPSATTKDSKGLNKFFYKFNVWFDKVTYRYSKGVKKAIKSAPLVLIILVCIFVGTGWMFTAKKAGFIPNEDGGIFFMGVSLPEGASSARTEEVLTELTNDLRKEFPEINYVTSINGMNLLNRSAKPNGASLFVSLKPWDERQKTVSDITGAIMGKYRGYSKATVIAATPPPIPGLGTAGGFTMEIQDRQTVDIKDFEAMVGRFLAAANQRPEIGMAYTLFNSNSPNYKLQVDREMAKRMGVPVSNIYSTISSYLGSSYVNDFTKYGRNFRVVTQADTSYRMHIEDINKLYVKNVQGQPVPISNLVRYELTTNPSIVNHFNIFRSIQISGEAGPGYSSGDAIRALEEVAAQTLSDGYSYEFSGLSLQEKQSGSKTIQIFALCILFVFLLLASLYESWSVPFSILLSVPLGIFGAILALTLLPNLDNNIYAQIGLVTIIGLAAKNAILIVEFAKERVDIGMNLVEATLDAVKLRLRPIIMTSLAFILGIIPLMLSTGAGAVSRQTIGWTVFGGMTAATFLAIFIVPVLFVVITRLAYGKKKLAELEASFDEEKKKSLSAH
>NZ_LT906468.1|WP_093099001.1|1232779_1233934_-|efflux-RND-transporter-periplasmic-adaptor-subunit
MNTTRLFSTILLGSGLFFTACGNKEGAKQQGPGQMQAQAMPVTMAVVQHEIVSGQHSYPANVVPLQETEIRAEVSGYITNISVADGAHVSKGQKLYDIDRVRYAAAVDQAKANLEIARANLARVEKDLQRYQTLADKDAIAKQTLDYAFTDVNNQKAQVQAAEAALTTARVNLQRSSIVAPFSGTVGISQVRNGALVSAGTTLLNTISSTNPIAVEFQINEKEIMEFSNLQSGKSSTQINLTLPDASTYGSHGRISTIDRAVDPQTGTLKVRATFDNPNNTLRAGMNLNLNVVSTSKEEAVVIPYRAIFEQLGSFSVYTVTDSNTVDLKQVTLGQKLGDRVVIAKGINPGEKVVVDGVTSLKPGAKVVDKATMAPQQPQAQPKK
>NZ_LT906468.1|WP_093099003.1|1233976_1235308_-|TolC-family-protein
MNFRIKDLVVYLSFTAISVGSVFAQTTNNLNSNATLDELIQYALENKIEIRQAQIDQEIGEREIASALSGWFPQINANGSLTHFMQLPTANINGQNIAMGQRNTSALTFQADQAIINPGLFQASKAAKYIRQQNDLSVEDTKINTVVDVSKAYYDILTSEEQINIIQENISRLNRQYTEANARYETGLVDKTDYKRAQISLNNAKAELKTALEFRKYKYDYLKTLLGMNPTNGLTLSFENQNMESNVLMDTTDVLNYNNRVELRQLQTMKDIQKLNTQYQKWQFLPRLGAFANYGLNYRNNSFSDLYGDNFPQSSFGLSLTFPIFQGGKRVQEIKRSELLESRIDMDIENLENQIGAQYSAAMANYRANINEWRNAKENVELSEEVYNTIKLQYDAGVKTYLELMTAETDLKTSQLNYLNSLYAVLSSKLDIQKALGTVNFAN
>NZ_LT906468.1|WP_093099004.1|1235313_1235892_-|TetR/AcrR-family-transcriptional-regulator
MNIQLTEKKEQIFFSTLKLINTYGFHGSPMSKIAKDADVAVGSIYHYFPSKEDLIVELYWYCKEKLNHQVFSAIDPTLGYEKKFKQIWRNLVWYYLDNLDHFGFLEQFYGSPFYEGIRTNIFQQKSERNVLLHFLDEGVHLKHLKDLNVRLLISAYLGVAISLVRGCLYEKSKPTDQEIETMVDIIWNGVKK
>NZ_LT906468.1|WP_093099006.1|1236536_1236962_-|cytochrome-c
MITRYFIGSIALVSMLYFLFSCNTDLSVETMQYATNGQKIYVKHCQNCHGANGEGLGKLYPPLTDANFLNENRSKLACIVKNGMSGEIKVNNTLFNQQMPGVPELSSVDIAYVLTYVTTYFGDSKTHFKKEEIEGFLKNCK
>NZ_LT906468.1|WP_093099007.1|1236961_1237606_-|SCO-family-protein
MKKYLGGAFAACMASILLFSCGPTERKLPIYGERSPVEKEVDGKTVVDTIYHTIPNFSFLNQDSTNLTQDFFKDKIYVANFFFTHCPSICPTMQRNLLKAYEKYKGNAKIAFLSHSIDFKYDQPSVLKDYATKLGVDNDQWQFVTGSKADIYGISEKYMVFTKEDPNAPGGYDHQGYLVIIDPEKRIRGAYDGTNDEQVKQLLEDLDVILAEYK
>NZ_LT906468.1|WP_093099009.1|1237616_1238042_-|hypothetical-protein
MKKLILLSAAFSIAFVSCQNKQVENKDQKLSEQAIAIHDEIMPQISQFDKSTIKIDSIISNLAAIKGEKADLDTAKTRVDLTNLKDSIEDATDHMMTWMKDYDATNEDEAYQQKEVDKISAMKKQFDRVAEQIKTSLAAFN
>NZ_LT906468.1|WP_093099010.1|1238053_1238575_-|YiiD-C-terminal-domain-containing-protein
MKVSPSTLKWGLRLYPPFFFQRIWVRRILNSFLGADVKINRSILNINSNRTIFGGTIFSAIDPFYPILLDQYFKHQGITRTVAWLKTAHIDYIKPGRFDLEVRIRLDQEILDETLQTIKKEGKVVRTFQTQVFDKHGTLCAIAHNEIYIRDLDFNFESLNPAPTQIENSSIEL
>NZ_LT906468.1|WP_093099012.1|1238667_1239891_+|MFS-transporter
MDSQKPNKNVWILIFVAALGYFVDIYDLIIFSIVRIQSFSDIGVPADQMRSKGEFVLNMQMGGLLIGGVIWGVLGDKYGRLKVLFGSILLYSIANIANGFVHDVTSYGIIRFIAGIGLAGELGAGITLVSESMHRKKRGYGTMIVAGVGVLGAILAYFISEWFSWRTAYFVGGGMGILLLFMRVGVFESGMFSSLENKSVQKGKISMLFNNGDRFRRYLYCLCIGLPIWFVVGVLVTQAPEIGQALHAQTTLSAGKGVMFTYIGISLGDFLAGWLAQVFKSRRKVVFIYQILILLFSCIYLTRQGISENEFMWLAFLMGLGVGYWATFITIAAEQFGTNIRSTVTTTAPNFVRGALIPSTLMYGVLVNWVGIIGAAMIMIVLLSLIAIFALTQLKESFDKDLDYVEE

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Crispr_ID: NZ_LT906468_8

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LT906468_8

1367627-1367714

Orphan

Consensus_repeat	Method
GTTACTTTTGGAGCCCAAAAGTAAC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_LT906468_8

>merge|NZ_LT906468|8|1367627-1367714|CRISPRCasFinder
GTTACTTTTGGAGCCCAAAAGTAACTAAACCGACGAAGGAGCTCAGGGATACCAATTCTCATTGTTACTTTTGGAGCCCAAAAGTAAC

>NZ_LT906468|8|8|1367627-1367714|CRISPRCasFinder
GTTACTTTTGGAGCCCAAAAGTAAC	TAAACCGACGAAGGAGCTCAGGGATACCAATTCTCATT
GTTACTTTTGGAGCCCAAAAGTAAC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LT906468.1\|WP_093094961.1\|1363742_1364894_-\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|366183
NZ_LT906468.1\|WP_093094967.1\|1369605_1369824_-\|DUF2892-domain-containing-protein	unknown	unknown	gnl\|CDD\|378561
NZ_LT906468.1\|WP_139185397.1\|1361701_1362292_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906468.1\|WP_093094953.1\|1359774_1361061_-\|leucine-rich-repeat-domain-containing-protein	unknown	unknown	gnl\|CDD\|372554
NZ_LT906468.1\|WP_093094971.1\|1370165_1373366_-\|efflux-RND-transporter-permease-subunit	unknown	unknown	gnl\|CDD\|223911
NZ_LT906468.1\|WP_093094965.1\|1368777_1369137_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906468.1\|WP_093094975.1\|1376273_1377005_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906468.1\|WP_093094966.1\|1369249_1369501_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906468.1\|WP_093094958.1\|1362303_1362894_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906468.1\|WP_139185395.1\|1358406_1359060_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906468.1\|WP_093094972.1\|1373410_1374496_-\|efflux-RND-transporter-periplasmic-adaptor-subunit	unknown	unknown	gnl\|CDD\|273776
NZ_LT906468.1\|WP_093094978.1\|1378535_1378973_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906468.1\|WP_139185396.1\|1361084_1361627_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906468.1\|WP_093094951.1\|1359088_1359772_-\|outer-membrane-beta-barrel-protein	unknown	unknown	gnl\|CDD\|335531
NZ_LT906468.1\|WP_093094969.1\|1369841_1370147_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906468.1\|WP_093094973.1\|1374504_1375815_-\|TolC-family-protein	unknown	unknown	gnl\|CDD\|224455
NZ_LT906468.1\|WP_093094959.1\|1362896_1363679_-\|class-I-SAM-dependent-methyltransferase	unknown	unknown	gnl\|CDD\|379312
NZ_LT906468.1\|WP_093094976.1\|1377010_1378411_+\|RtcB-family-protein	unknown	unknown	gnl\|CDD\|224604
NZ_LT906468.1\|WP_093094963.1\|1366397_1367408_+\|helix-turn-helix-transcriptional-regulator	unknown	unknown	gnl\|CDD\|225117
NZ_LT906468.1\|WP_169918980.1\|1364942_1366172_-\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|238657

Protein	Function_ID	Function_description	E-value
NZ_LT906468.1\|WP_093094961.1\|1363742_1364894_-\|TonB-dependent-receptor	gnl\|CDD\|366183	pfam00593, TonB_dep_Rec, TonB dependent receptor. This model now only covers the conserved part of the barrel structure.	2.20713e-25
NZ_LT906468.1\|WP_093094967.1\|1369605_1369824_-\|DUF2892-domain-containing-protein	gnl\|CDD\|378561	pfam11127, DUF2892, Protein of unknown function (DUF2892). This family is conserved in bacteria. The function is not known.	4.55386e-07
NZ_LT906468.1\|WP_093094951.1\|1359088_1359772_-\|outer-membrane-beta-barrel-protein	gnl\|CDD\|335531	pfam03922, OmpW, OmpW family. This family includes outer membrane protein W (OmpW) proteins from a variety of bacterial species. This protein may form the receptor for S4 colicins in E. coli.	1.04859e-12
NZ_LT906468.1\|WP_093094976.1\|1377010_1378411_+\|RtcB-family-protein	gnl\|CDD\|224604	COG1690, RtcB, Uncharacterized conserved protein [Function unknown].	5.61633e-85
NZ_LT906468.1\|WP_093094973.1\|1374504_1375815_-\|TolC-family-protein	gnl\|CDD\|224455	COG1538, TolC, Outer membrane protein [Cell envelope biogenesis, outer membrane / Intracellular trafficking and secretion].	4.40386e-30
NZ_LT906468.1\|WP_093094953.1\|1359774_1361061_-\|leucine-rich-repeat-domain-containing-protein	gnl\|CDD\|372554	pfam13306, LRR_5, Leucine rich repeats (6 copies). This family includes a number of leucine rich repeats. This family contains a large number of BSPA-like surface antigens from Trichomonas vaginalis.	1.20572e-26
NZ_LT906468.1\|WP_093094959.1\|1362896_1363679_-\|class-I-SAM-dependent-methyltransferase	gnl\|CDD\|379312	pfam13649, Methyltransf_25, Methyltransferase domain. This family appears to be a methyltransferase domain.	4.88886e-13
NZ_LT906468.1\|WP_093094971.1\|1370165_1373366_-\|efflux-RND-transporter-permease-subunit	gnl\|CDD\|223911	COG0841, AcrB, Cation/multidrug efflux pump [Defense mechanisms].	0
NZ_LT906468.1\|WP_093094963.1\|1366397_1367408_+\|helix-turn-helix-transcriptional-regulator	gnl\|CDD\|225117	COG2207, AraC, AraC-type DNA-binding domain-containing proteins [Transcription].	9.76296e-23
NZ_LT906468.1\|WP_093094972.1\|1373410_1374496_-\|efflux-RND-transporter-periplasmic-adaptor-subunit	gnl\|CDD\|273776	TIGR01730, COG0845:_Membrane-fusion_protein, RND family efflux transporter, MFP subunit. This model represents the MFP (membrane fusion protein) component of the RND family of transporters. RND refers to Resistance, Nodulation, and cell Division. It is, in part, a subfamily of pfam00529 (Pfam release 7.5) but hits substantial numbers of proteins missed by that model. The related HlyD secretion protein, for which pfam00529 is named, is outside the scope of this model. Attributed functions imply outward transport. These functions include nodulation, acriflavin resistance, heavy metal efflux, and multidrug resistance proteins. Most members of this family are found in Gram-negative bacteria. The proposed function of MFP proteins is to bring the inner and outer membranes together and enable transport to the outside of the outer membrane. Note, however, that a few members of this family are found in Gram-positive bacteria, where there is no outer membrane. [Transport and binding proteins, Unknown substrate].	4.24483e-52
NZ_LT906468.1\|WP_169918980.1\|1364942_1366172_-\|TonB-dependent-receptor	gnl\|CDD\|238657	cd01347, ligand_gated_channel, TonB dependent/Ligand-Gated channels are created by a monomeric 22 strand (22,24) anti-parallel beta-barrel. Ligands apparently bind to the large extracellular loops. The N-terminal 150-200 residues form a plug from the periplasmic end of barrel. Energy (proton-motive force) and TonB-dependent conformational alteration of channel (parts of plug, and loops 7 and 8) allow passage of ligand. FepA residues 12-18 form the TonB box, which mediates the interaction with the TonB-containing inner membrane complex. TonB preferentially interacts with ligand-bound receptors. Transport thru the channel may resemble passage thru an air lock. In this model, ligand binding leads to closure of the extracellular end of pore, then a TonB-mediated signal facillitates opening of the interior side of pore, deforming the N-terminal plug and allowing passage of the ligand to the periplasm. Such a mechanism would prevent the free diffusion of small molecules thru the pore.	2.50295e-17

>NZ_LT906468.1|WP_093094963.1|1366397_1367408_+|helix-turn-helix-transcriptional-regulator
MELIWTNRKGAEEASIVVPDVYDLGSELKELLLGNEELSDGLFRLFHTDGLILIDVHSHLSQRATANLSFKDNVLLIVFHLEGDVRIMDMGSSHDSGLKLQRGEHKFEIFNANNLKIIYEPALMLNSFIVVLSPEFSHRIIPHNYSNQDGLIKAVKEGERISLPLDFAPLSLDMKQIIEKVRNCSRKGSFHRLCLEIKIAELLMLQLEQQASLHSEQLARPAMHDADIEKIEEAKNILEDQYTQPPTIKDLAGMVGLNETKLKTNFKKTFNSTIHAYTQRIRMQKAHELLTQKNLLLKEIAMQVGYQKPSNFTNAYKDFFGIHPGDVARNRKKREY
>NZ_LT906468.1|WP_169918980.1|1364942_1366172_-|TonB-dependent-receptor
MMNTICQIVYGNISISQQQFLIEGKVLTNEKEPIPNVSICLKADHKISTKTDANGSFKLSLPEGSHTLVFSHQSYQSFEGIFRIAGNESNKHSYDIYLKEKRIEIQEVDIKGQKVLSAAPSLKTIKLEHKQIAGGTSVAVMTPEVQRLETIKDALKYEPGVVIQEFFGANDQPRLSIRGSGIQSNPQRRGVYLLQDGIPINFADGSFIIGVMDPAITESIETFKGANALRYGAATLGGAVNFNSHIGRFTKGLQGKVEGGSFGYTQGNLMAGKHWGKSDAFLSVSGSHQDGFRQHNNNRKMNVAGNFGHRFSNNIDSRLYLNYSYIKFDVPGPLTMQMLLEDPAQINKGIALPYYMGPNIERDKPGREAEVLRIANRTAFRISANTDITVSAYYQLIKDRFVFPIVLST
>NZ_LT906468.1|WP_093094961.1|1363742_1364894_-|TonB-dependent-receptor
MDKGRLMVGFLESHGNIDRRGHINVNGLDSYMFSKDKLNAVNLTFYTEYQHRFNERFQLIANIQAVNNERNSEDVFPDPELRPWYSHSSHKYRYFHSYSQSLDQQFRSVNPRIGAIYNAGRNKDIQFFGNVSTSYEPPTFDELVGTKVTANINTSPKEFFAIKLDKQSSTTVEIGTRHENTRYSWNISLYRSWVKNELLEVKDFVLGVKQTKNYPQTIHQGIEFAAMGIPFQGVLYPKDQISVKGMYTYSDFFFSAGDYEGKKLAGVPPHYLTAAIEYKNPGKFFVSLNAESQPLKSPIDHTNTVFQKPFTILGMRAGVDGWKNFSFYVEGKNILNRYYASSYIISDQILLPPIPFPEFTVNNVAFFMPGQTRAFYAGLTYKF
>NZ_LT906468.1|WP_093094959.1|1362896_1363679_-|class-I-SAM-dependent-methyltransferase
MSIEEKLNEKQGHWILAKVGKKVLRPGGRELTKKLMDNMDINSADDVVEFAPGLGFTASIACAKKPNSYTGVDNNHQAAELARKNVKYDKVKFIVADASDTTIPSGYATKVYGEAMLTMQPLEHKKAIIKEASRLLKPGGYYGIHELGLQPENISEEIKQSVYKDLSSNIRVHARPLTISEWSQLLVDEGFEIVKVDSNAMALLEPKRVLADEGFFRTMKIIFNVLTHGDLRKRILQMRQTFKKHKNDINAVAIVARKKI
>NZ_LT906468.1|WP_093094958.1|1362303_1362894_-|hypothetical-protein
MRAFGFIGMMLMLLCGCSGDDYLSPDLNDPSLLPDRSDYLSKDYGTQALAKEIFEAYTGYKNDSVLIKMIMYDDATRKQPLLTFTEQKWPINMRWLANGALELGYRNFQTEMMPLKMTANINVLLELNSTKDTIWLRGTDGKIRTAEASGQAIGTPLPQSDDAELQGYYVRSSKKLSVLLDLMLPIPIKAHITGSK
>NZ_LT906468.1|WP_139185397.1|1361701_1362292_-|hypothetical-protein
MFTTSIIRKLTYFLFFLLSGLMLFSCSKEDEDTGGSTLIKQYGLTGQYRFQVIPTMMGTIPIATGTVDGTVSDEGNGVLRLRFNGFRANPMPFEMSVDASFTISETAKGLLVQNIEGKSFFDADPPAGGADPDVDPGFEIPEEALKKGLHSNGKSKLTGTIDKNPNGSGAMQYDLKLDPAVSLPVVVIIKSVQKLN
>NZ_LT906468.1|WP_139185396.1|1361084_1361627_-|hypothetical-protein
MSANQSTGASSLTGIFQVKVFFDPMGDLFTNLAKGLLNPDGYHYIKLSAKTSEITKVEFCDANGNISGLNPGNPPSSYGDFDYASTKHYWKNQMPMALALQDVSFTFNPATGNISQGNPLKALARRNGNPGSSIPPFINPSQDSDGSAAIITTTGNSAQAFSIRIKLGFQIPFQIVLTKI
>NZ_LT906468.1|WP_093094953.1|1359774_1361061_-|leucine-rich-repeat-domain-containing-protein
MATRSILGFLSIALLLLASCNKEEFPINSSFFNNPENDSKTLVYEGKKAGDFEHAADQMDWSGIKKLILKGHINNKDIGIIKRYIAETFDGELRELDFRDADVFEGQFINSPFHKLKNLEHFVYPKKIKSTGDNVMSESFWVREIIIPQDVEIIGDRTFEIVSFRIDFQGTGQVFPIDIPYMAKERYQLPKTVKEIGEFAYRYYPYQELSLPESVETIKRGCFANSKLTSFTFPAKVTAVPDECFFLSNDLESINLPEGLTSIGSAAFEGTKIQELLMPDGVNQVGEGFLSGIKLKKIKWSQSLTELSVRAMRGSQLDELHIPDQITKIGESCFYQSTIKRIWFHKNISSLGLGFINGMSNLEEVHITWAIPPAANSLFNDILISPLGKPEYNKSPDFEKVKLFVPKGTSIAYKNAAGWKNFKQIIEE
>NZ_LT906468.1|WP_093094951.1|1359088_1359772_-|outer-membrane-beta-barrel-protein
MLRNNRNMTLPLLVIVVHLFTSNALYAQDDGFKRFTIKLFGGFSRTNESSHLQKVGGIYELNNSPSVGFGIAWFLSPSWSTEVSASAGHYRMSMKNGDYSSMKVLRDEIPLGRVWLAPISLSIRYHVNRWNKIKPYLAAGRSFLLFDQEDPGWAADAVEYHSRSALHLGLGLDYQLHESWFLQLDLKHFLANRAKVNPDFTKSVGWKLNGQLKPDPTQMTIGIGYRF
>NZ_LT906468.1|WP_139185395.1|1358406_1359060_-|hypothetical-protein
MNRRQFSSRLFVGAFALMTLGIASCNKDKDEVTVTPVVPKTDAEILAELKEELRTSMKYNSNYKQLQYSSNLNPDFKAAKDFSESLKSIQWDHNENKYMASNLVIDKKAKLYFSVGGSYYFFENFGLKKENDLYTITAKLEDMFQITQEGTTTKPTGMGFSMSATYNVKTGKTIQILEAMANETVVMVIASVWVQDKSITKPTKSPVGKDPNDFIDF
>NZ_LT906468.1|WP_093094965.1|1368777_1369137_+|hypothetical-protein
MKPWLLAILFIFISCQTNYVGKKEPRSLYINTTIPAKSSLEISTEDNKSFSIDAQNISSDPIIVSIATIDTAMTKNSKYSFNVGDNGIVLLKNSSNQEAAIKVRIYNHSSKVQQKTSAL
>NZ_LT906468.1|WP_093094966.1|1369249_1369501_+|hypothetical-protein
MTKNKKLQELSLEELYLEKKKRKGMLTVLGITMLIVCFALVVLAVKSGNYALIAVACGSFITLLPSFTYLSQLETEIKTREQK
>NZ_LT906468.1|WP_093094967.1|1369605_1369824_-|DUF2892-domain-containing-protein
MTRERYIKMIAGAMVLISSLGAYFININWIWLAVFVGANLLQFSITQWCLLNIILKALGIKSEIECCGTEKC
>NZ_LT906468.1|WP_093094969.1|1369841_1370147_-|hypothetical-protein
MKLLIITAANSYQYSVKNLLAENNVITYSYSAVTGYRDSTKDAVKDNWFASEMNKTESLLFFAFVQDEQSDQIFTAVEELNRTMDLHSKVHIAISSIEKSN
>NZ_LT906468.1|WP_093094971.1|1370165_1373366_-|efflux-RND-transporter-permease-subunit
MQNGLSGKIASMFLNSKLSILLMVGLMIIGVYSSSLIPREEEPQINVPMADIMVGYPGASPEEVERRVLEPLEKIISNIKGVEHLHSTAMNGQAMIIVQFYVGEDIERSYVKLYDELIKNQHIFPQGVYPPVVKTRSINDVPMLALTLWSDRYDDFQIRQMAEEVSSEIKKIKDVSTIKEIGGRSRELKVVLDKDKMAENGVDALSIMQMIQANNGSMQSGSFVQHDQEFLLTTGQFLASKEDMENLVVGVHQQMPVYLKQVAQINDAAGTAKSYVSFGYSKNNENFESNPSEYPAVTLSIAKVQGADAMQISEQILKRVEKLQDNLIPKDVKVEVTRNYGETASHKVNELLFHLGVAIVAVTALVMLAMGWRGGLVVFLSVPLTFALTLFSYYMLGYTLNRITLFALVFVVGIVVDDSIIIAENMHRHFKMRKLPFKDAAIYAINEVGNPTILATFTVIAAILPMAFVSGMMGPYMSPMPIGASIAMLLSLFVALTITPYLGYHLLNEKEKQHEKEEQGHQTSWIYKIYNKFEKPLLDNSKKRWLVLGLTVVLLFGSVGMFFTKSVAVKMLPFDNKNEFQVVIDMPEGTTLERTSAVAKEISQYLTTVPEVVNYQNYIGTSAPITFNGLVRHYDLRGGSNMADIQVNLLDKTDRDEQSHAIAKRIRPAIQAIAQKHHANVKIVEVPPGPPVLSTIVAEVYGPDYQEQIKVAYQVKEILKKTNDVVDVDWGVEDVQTEYKLEVDKEKAMLNGIAPQQVVGNLTYLLREYPISNLYDEKSVNPVGIVMALDDKDKTNIDDIQNLKIKGQQGNMVPVRDIVQVKQDTLRKSISRKDQQRVVYVLADMAGDLESPAYAILGMEETLKQMKLPTGYEISDLYMGQPKETSNFTVKWDGEWQITLEVFRDLGIAFMVVIIIIYMLIVGWFQDFKTPIVMMVAIPLSLIGIVLGHWLLGAFFTATSFIGMIALAGVMVRNSVLLIDFIEIRLKDGIPLKQAIIDAGAVRTTPILLTTGAVVLGASVILFDPIFQGLAISLVGGAIVSTILTLFVVPLVYYIVERKKWANNKD
>NZ_LT906468.1|WP_093094972.1|1373410_1374496_-|efflux-RND-transporter-periplasmic-adaptor-subunit
MKTILTSISFLALLGSLSSCSNQAEQKKVELPAISATIGQTAGSNQGKYVTASGKIEAENSAMISTRLMGFVTDITVKTGQKVSQGQLLARISSNDLAAKKAQAEAGIAQANAGYNNARKDYERFEALFAQKSASQKELDDMSTRMEMAKAGLEAAKQMRNEVMAQFSYSNITAPFSGVITGTFMKKGDMANPGMPIISMEGASKLQAVVMVSESEILNIKNGMKADVTIKSTQKTIKGRVAEMSSSAQNTGGQYIVKINLDEPAQILSGMFVQAVFPIERSASAESATSMTLIPKEAIIEEGQLKGIYVLNDQNIALLRWVRLGKTYGNDVEVLSGLSENEKYVLKADGRLFNGVQIKAK
>NZ_LT906468.1|WP_093094973.1|1374504_1375815_-|TolC-family-protein
MYKRFIVLIIILSSLSSYLKAQQPLSLEEAISQMKQNNSQLRVQQKEIDFSNAELEGTKSGFLPKVSVSHTAFFTNDPLNSFGFKLQQKTVTAADFNPDLLNNPDDMAHFNTKLAFQQPLLNFDVYSARKALKEKIAANQYQKKFAEEMLVVEIEKAYSNLQFLYEAKKAVEKGQIAYEEVLRNTRNMEQQGYAKASDVYLVQVGLSEVQNKGIEVDNHISNLSDYLNWLMGKPANEIYIPDTPLASMSLATDQLTFSQERADIRAMVSGLAAQGQMIDMNRKKLLPRINAFGEYNFNDKKIVGFGANGYLAGISLSWDIFNGNETQNKIKQSQISYAKAESEMLVYVEKHELELQKAKRDLVANQAKIRLTETAQKQASESLRILENRYSQGLEKTSDLLVAQAKDFEKQVELLEAIKEYNLSIIQIKFLTQPSN
>NZ_LT906468.1|WP_093094975.1|1376273_1377005_+|hypothetical-protein
MSNLDWSRGMKSARRKKQLVKKDRDKRLIALWRRYSKLSKYKWSLPFVEIEQPYQRGWKRYFVLHDDLRYNPRKDFFEALLEKINTVEYHHDQDFKFKKRKKKRSGYEYKRQFLREFASYEWIDNKMKLTEEERAYFMEVETYNVYAKRTSISYVFTEPWRYKLKVAPHFVTHARKLDIEVERELAFVNNHINKNFLWPRIDRLTSGKGYRGNRFLDEKPKYKNRIKNIPRYSSKERFLELDI
>NZ_LT906468.1|WP_093094976.1|1377010_1378411_+|RtcB-family-protein
MGNLRTKDLSKIGYQNDQLRSLVINIASKNFKHHSKQELLDLLVEIKNNPEAFLENEETKKIAEKIIGKVKEQNFKVYELREEPIPCKIYGSKGIESSAKKQMEIACMLPVSVQGALMPDAHMGFGLPIGGVLATEQAIIPYAVGMDIGCRMALSILDAAAGFTKKYEYQIVQAIKNHTHFGMEGGLEIRQDHEILDHSLFNELPFLKPLRGKAARQLGTSGNGNHFVEFGEIELMENNGLGLEPKVYTALLTHSGSRGLGAAIAKQYTQIAMESCKLPRHAQQLAWLDMESEAGQEYWLAMNLAGDYAKACHDRIHKNLLSALGLKAMAMVENHHNFAWKDVLSDGKETIIHRKGATPAHQGELGIIPGSMTTAAYLVSGRGIENALNSASHGSGRAMSRQKANDNMTNSAMKKLISSANVKLIGGSVEENPLAYKDIEQVMLSQRELVDIQGKFIPKIVRMHKE
>NZ_LT906468.1|WP_093094978.1|1378535_1378973_+|hypothetical-protein
MKNTGQSLIIFFSILSIVFLQSCSDLNQQDLIEKKLVSYQGRDTVTIDLILHEKRFVGKYKVNGPGDYLITGEVEGEIKADTLLGSLYYTPFGWRDKKRKAFALLAKNDQYFSGKGTELIYMGIPYFVPTTLSFGPDKGVYQVVD

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Crispr_ID: NZ_LT906468_9

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LT906468_9

1433722-1433809

Orphan

Consensus_repeat	Method
TGGTTCCTTCCCAGATCTTGGCC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_LT906468_9

>merge|NZ_LT906468|9|1433722-1433809|CRISPRCasFinder
TGGTTCCTTCCCAGATCTTGGCCTTCCTCTCATCCATGTTGGCTGAGCGGAGGCGGAGCCCATCCTGGTTCCCTCCCAGATCTTGGCC

>NZ_LT906468|9|9|1433722-1433809|CRISPRCasFinder
TGGTTCCTTCCCAGATCTTGGCC	TTCCTCTCATCCATGTTGGCTGAGCGGAGGCGGAGCCCATCC
TGGTTCCCTCCCAGATCTTGGCC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LT906468.1\|WP_093095052.1\|1438353_1439100_+\|phosphate-ABC-transporter-ATP-binding-protein	unknown	unknown	gnl\|CDD\|224042
NZ_LT906468.1\|WP_093095040.1\|1432958_1433426_+\|DsrE-family-protein	unknown	unknown	gnl\|CDD\|224334
NZ_LT906468.1\|WP_093095030.1\|1426210_1426612_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906468.1\|WP_093095044.1\|1434396_1435470_-\|DUF3667-domain-containing-protein	unknown	unknown	gnl\|CDD\|378853
NZ_LT906468.1\|WP_093095058.1\|1440931_1441603_+\|ABC-transporter-ATP-binding-protein	unknown	unknown	gnl\|CDD\|213222
NZ_LT906468.1\|WP_093095046.1\|1435761_1436637_+\|phosphate-ABC-transporter-substrate-binding-protein	unknown	unknown	gnl\|CDD\|270371
NZ_LT906468.1\|WP_093095038.1\|1432377_1432953_+\|TlpA-family-protein-disulfide-reductase	unknown	unknown	gnl\|CDD\|239264
NZ_LT906468.1\|WP_093095061.1\|1444195_1446460_+\|S9-family-peptidase	unknown	unknown	gnl\|CDD\|224423
NZ_LT906468.1\|WP_093095057.1\|1440203_1440890_-\|arylesterase	unknown	unknown	gnl\|CDD\|238860
NZ_LT906468.1\|WP_093097681.1\|1421250_1424562_-\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|274948
NZ_LT906468.1\|WP_093095049.1\|1437506_1438364_+\|phosphate-ABC-transporter-permease-PstA	unknown	unknown	gnl\|CDD\|223654
NZ_LT906468.1\|WP_093095059.1\|1441599_1444131_+\|FtsX-like-permease-family-protein	unknown	unknown	gnl\|CDD\|225669
NZ_LT906468.1\|WP_139185399.1\|1433439_1433652_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906468.1\|WP_093095034.1\|1428112_1431268_+\|efflux-RND-transporter-permease-subunit	unknown	unknown	gnl\|CDD\|223911
NZ_LT906468.1\|WP_093095032.1\|1426748_1428104_+\|TolC-family-protein	unknown	unknown	gnl\|CDD\|224455
NZ_LT906468.1\|WP_093095036.1\|1431271_1432360_+\|efflux-RND-transporter-periplasmic-adaptor-subunit	unknown	unknown	gnl\|CDD\|273776
NZ_LT906468.1\|WP_093095027.1\|1419544_1421242_-\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	unknown	unknown	gnl\|CDD\|373012
NZ_LT906468.1\|WP_093095048.1\|1436626_1437517_+\|phosphate-ABC-transporter-permease-subunit-PstC	unknown	unknown	gnl\|CDD\|223646
NZ_LT906468.1\|WP_093095028.1\|1424917_1426105_-\|FecR-family-protein	unknown	unknown	gnl\|CDD\|226235
NZ_LT906468.1\|WP_093095054.1\|1439326_1439776_+\|hypothetical-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_LT906468.1\|WP_093095052.1\|1438353_1439100_+\|phosphate-ABC-transporter-ATP-binding-protein	gnl\|CDD\|224042	COG1117, PstB, ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism].	7.30619e-150
NZ_LT906468.1\|WP_093095040.1\|1432958_1433426_+\|DsrE-family-protein	gnl\|CDD\|224334	COG1416, COG1416, Uncharacterized conserved protein [Function unknown].	1.37604e-19
NZ_LT906468.1\|WP_093095044.1\|1434396_1435470_-\|DUF3667-domain-containing-protein	gnl\|CDD\|378853	pfam12412, DUF3667, Protein of unknown function (DUF3667). This domain family is found in bacteria and eukaryotes, and is approximately 50 amino acids in length. There is a single completely conserved residue P that may be functionally important.	4.37156e-11
NZ_LT906468.1\|WP_093095058.1\|1440931_1441603_+\|ABC-transporter-ATP-binding-protein	gnl\|CDD\|213222	cd03255, ABC_MJ0796_LolCDE_FtsE, ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and cell division protein. This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. An FtsE null mutants showed filamentous growth and appeared viable on high salt medium only, indicating a role for FtsE in cell division and/or salt transport. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.	1.19009e-110
NZ_LT906468.1\|WP_093095046.1\|1435761_1436637_+\|phosphate-ABC-transporter-substrate-binding-protein	gnl\|CDD\|270371	cd13653, PBP2_phosphate_like_1, Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 periplasmic binding fold superfamily. This subfamily contains uncharacterized phosphate binding domains found in PstS proteins that serve as initial receptors in the ABC transport of phosphate in eubacteria and archaea. After binding the ligand, PstS interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The PstS proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.	5.82384e-73
NZ_LT906468.1\|WP_093095038.1\|1432377_1432953_+\|TlpA-family-protein-disulfide-reductase	gnl\|CDD\|239264	cd02966, TlpA_like_family, TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are bacterial protein disulfide reductases with important roles in cytochrome maturation. They are membrane-anchored proteins with a soluble TRX domain containing a CXXC motif located in the periplasm. The TRX domains of this family contain an insert, approximately 25 residues in length, which correspond to an extra alpha helix and a beta strand when compared with TRX. TlpA catalyzes an essential reaction in the biogenesis of cytochrome aa3, while ResA and DsbE are essential proteins in cytochrome c maturation. Also included in this family are proteins containing a TlpA-like TRX domain with domain architectures similar to E. coli DipZ protein, and the N-terminal TRX domain of PilB protein from Neisseria which acts as a disulfide reductase that can recylce methionine sulfoxide reductases.	1.23874e-36
NZ_LT906468.1\|WP_093095061.1\|1444195_1446460_+\|S9-family-peptidase	gnl\|CDD\|224423	COG1506, DAP2, Dipeptidyl aminopeptidases/acylaminoacyl-peptidases [Amino acid transport and metabolism].	1.45349e-81
NZ_LT906468.1\|WP_093095057.1\|1440203_1440890_-\|arylesterase	gnl\|CDD\|238860	cd01822, Lysophospholipase_L1_like, Lysophospholipase L1-like subgroup of SGNH-hydrolases. The best characterized member in this family is TesA, an E. coli periplasmic protein with thioesterase, esterase, arylesterase, protease and lysophospholipase activity.	2.13395e-81
NZ_LT906468.1\|WP_093097681.1\|1421250_1424562_-\|TonB-dependent-receptor	gnl\|CDD\|274948	TIGR04056, OMP_RagA_SusC, TonB-linked outer membrane protein, SusC/RagA family. This model describes a distinctive clade among the TonB-linked outer membrane proteins (OMP). Members of this family are restricted to the Bacteriodetes lineage (except for Gemmatimonas aurantiaca T-27 from the novel phylum Gemmatimonadetes) and occur in high copy numbers, with over 100 members from Bacteroides thetaiotaomicron VPI-5482 alone. Published descriptions of members of this family are available for RagA from Porphyromonas gingivalis, SusC from Bacteroides thetaiotaomicron, and OmpW from Bacteroides caccae. Members form pairs with members of the SusD/RagB family (pfam07980). Transporter complexes including these outer membrane proteins are likely to import large degradation products of proteins (e.g. RagA) or carbohydrates (e.g. SusC) as nutrients, rather than siderophores. [Transport and binding proteins, Unknown substrate].	0
NZ_LT906468.1\|WP_093095049.1\|1437506_1438364_+\|phosphate-ABC-transporter-permease-PstA	gnl\|CDD\|223654	COG0581, PstA, ABC-type phosphate transport system, permease component [Inorganic ion transport and metabolism].	1.44572e-90
NZ_LT906468.1\|WP_093095059.1\|1441599_1444131_+\|FtsX-like-permease-family-protein	gnl\|CDD\|225669	COG3127, COG3127, Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, permease component [Secondary metabolites biosynthesis, transport, and catabolism].	3.22448e-130
NZ_LT906468.1\|WP_093095034.1\|1428112_1431268_+\|efflux-RND-transporter-permease-subunit	gnl\|CDD\|223911	COG0841, AcrB, Cation/multidrug efflux pump [Defense mechanisms].	0
NZ_LT906468.1\|WP_093095032.1\|1426748_1428104_+\|TolC-family-protein	gnl\|CDD\|224455	COG1538, TolC, Outer membrane protein [Cell envelope biogenesis, outer membrane / Intracellular trafficking and secretion].	1.56501e-18
NZ_LT906468.1\|WP_093095036.1\|1431271_1432360_+\|efflux-RND-transporter-periplasmic-adaptor-subunit	gnl\|CDD\|273776	TIGR01730, COG0845:_Membrane-fusion_protein, RND family efflux transporter, MFP subunit. This model represents the MFP (membrane fusion protein) component of the RND family of transporters. RND refers to Resistance, Nodulation, and cell Division. It is, in part, a subfamily of pfam00529 (Pfam release 7.5) but hits substantial numbers of proteins missed by that model. The related HlyD secretion protein, for which pfam00529 is named, is outside the scope of this model. Attributed functions imply outward transport. These functions include nodulation, acriflavin resistance, heavy metal efflux, and multidrug resistance proteins. Most members of this family are found in Gram-negative bacteria. The proposed function of MFP proteins is to bring the inner and outer membranes together and enable transport to the outside of the outer membrane. Note, however, that a few members of this family are found in Gram-positive bacteria, where there is no outer membrane. [Transport and binding proteins, Unknown substrate].	1.37435e-42
NZ_LT906468.1\|WP_093095027.1\|1419544_1421242_-\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	gnl\|CDD\|373012	pfam14322, SusD-like_3, Starch-binding associating with outer membrane. SusD is a secreted polysaccharide-binding protein with an N-terminal lipid moiety that allows it to associate with the outer membrane. SusD probably mediates xyloglucan-binding prior to xyloglucan transport in the periplasm for degradation. This domain is found N-terminal to pfam07980.	9.58812e-28
NZ_LT906468.1\|WP_093095048.1\|1436626_1437517_+\|phosphate-ABC-transporter-permease-subunit-PstC	gnl\|CDD\|223646	COG0573, PstC, ABC-type phosphate transport system, permease component [Inorganic ion transport and metabolism].	7.41973e-94
NZ_LT906468.1\|WP_093095028.1\|1424917_1426105_-\|FecR-family-protein	gnl\|CDD\|226235	COG3712, FecR, periplasmic ferric-dicitrate binding protein FecR, regulates iron transport through sigma-19 [Inorganic ion transport and metabolism, Signal transduction mechanisms].	2.14031e-20

>NZ_LT906468.1|WP_139185399.1|1433439_1433652_+|hypothetical-protein
MIKKATQNGLLFLNQDGKDRRIDQDYELNQDGKDRRIDQDYELNQDGKDGRIDQDIHFKKKIALSILNEL
>NZ_LT906468.1|WP_093095040.1|1432958_1433426_+|DsrE-family-protein
MKYIIIMVLLAGLHADDAFGQTREELIAKNQQYTGAETQKEHYKAVYQLDTDNPDIVKKAFRNINNLLKDPRLSGKLEVELVTFSGGTEVMRKDNKYEEQLLGLIDKGVRVVQCLNSLDERGYKKDELFDFIGYTPSGNGELVILNNEGWTVVKP
>NZ_LT906468.1|WP_093095038.1|1432377_1432953_+|TlpA-family-protein-disulfide-reductase
MKTKQMILGISMLALFAVGCSSATNKEGSADSTAQVDKTEEVQEAKMVGKQNDLKASFTNINGETVALSDLKGKVVVMNFWATWCPPCIAEMPSLQKLHEELKSEKDIVFMAIEVDQDIDKAAKFMAKNKYTLPLYTVGSELPEELMSNSIPMTVILAKNGDIIGKQVGMMDFKSEKLKQGLIDLTKENER
>NZ_LT906468.1|WP_093095036.1|1431271_1432360_+|efflux-RND-transporter-periplasmic-adaptor-subunit
MKKLSIFGLILLLAGCQANSKDTDTKKESPSNTNISVKVTQPIEQQPSYTLKLPAELHPYESVDVFAKIKGFVRKINVDVGDQVSKGQILAVLEAPEMDIQSTADRAKSQQLSANFEVSKSRFDRLKKVKNQSSGAVSDLEYEQAYGSMLRDSAALEESNFSYKKSNQMREYLVVRAPFSGIITQRNFSVGALMGDTGMPFFKLVDNNNLKLKVVVPELHAQSISDSTVAKFKVLSKPDTVFTAQLKRNALVIDPVSRSLALEFDVPNKSRALNGGDYTDVQLNLKRKRPTVFVPQSAVVNSQSGIFVLKLVEGNKVERVPVVLGQAQDKLMEVFGDLHPSDQIIEKGSEEINSGQIVQIIK
>NZ_LT906468.1|WP_093095034.1|1428112_1431268_+|efflux-RND-transporter-permease-subunit
MNLIRFALRKPIAIIMVIFAIAYFSWPVIKKIKVDIFPEIESPAMYIAMPYGGLSPAYMDGFMANEFQKVLLFVNGVKELDFKSVQGLSLMKLTFYPGTDMSQASAEISMQVSRAMGFLPSGAVPPMVVRFDGSSLPVGQLVFDSDQHTVTELQTMAVTKVRPMFVNIPGITAPAPFGGNMRSLVVNIDPQKMKAHGLSPEEVTLAVTKNSMPSPAGNVRIGDKNLMAPINSISNGVEEFLQTPIKSLNGRTILIGDVATVMDAADQTVGYAIINGKRSVYLPIIKKPDASTLDAVDNLKKALPMLESLLPEGVKITYAFDQSVYISRSLSNLIFEGALGALLTGLMVFLFLRDPRGALIVILTIPIAIITAVITLHMFGQSINIMTLSGLALSIGILVDEATVTIENIHQHMELGKKKARAILDALLEISAPKLLILLSILAVLTPAFMMEGIPRDMFMPLSMAVAFAMIASFISSQTFVPIMANWIMKTKKHHAGKYKRSFVDKVGVKYVYRLRYYFAKSKLISILYVVVALFLVFGAVNILGTDIMPKSEGGDFQLRLRMPDGTRLERTEETVKAMTKSLVAELPENSLKISSSFVGMHPSANPINPIFLFTSSTGEAVMQFSLDKKKLGMKTDEFKEFVRSHVKEKYPEARINFEPIELMEKIIGQGSMTPVEVKVSSAQLKNAEAFAEKIKKELTTYPFLKDVQIAEPLHYPTIDIKIDRRRLAEFGLTVQEVSRNLAATTSSTRFTDKNLWVDPKSGLVFQVQVQVPENMIQTLQDLRSIPVKAGSSTPLLEDIATITANEVPAQVNRRGPNRYVSIIADVHEKDLGAANKAVNESLERVGEAPRGTRIWKEGTLTLLEDTLSGLLSGLSIAIVVIFFMMSAYYQSVRVSLVILSVVPAVIAGSSIMIWISGSTLNLQSYMGIIMSIGVSVSNAVLLINQAEWYRKKLNLSASRSALLAAKSRFRPILMTALAMLAGMTPMALGMGDGGEQVAPLGQAVIGGLISSTFTILLIIPLIFSLIMNKASYGSPSLDPDDSNSKFYLEK
>NZ_LT906468.1|WP_093095032.1|1426748_1428104_+|TolC-family-protein
MGLKFKSLLILLGLFIAMDSHAQSLQDLWDKTRNYYKGFEVQKQQILLAKQDSIAQQIKYKPQVQAQFQQGFSSVEGTSGAFLPLPGIMNISGPNQLDGASSTFNHFLSGSMNWDLINFGRKGLDKDISSTKIDYTKLKEQDFSYNVQQKLTRRYIEFLFFQVMDDWYQKHSERYQSIVDITKGLARAGIVPGADTLLATSSLKNVESNLLQIQGKLNGAKILLKEFTNEEVLSAGNNNPEAFLQLIGSQQTSTLEHPLLMMKKKEEESLTLLEKKQGKELFPRVMLLGGLANRSSGVTANGYVHGNYGEIYNDFANNYFVGVGVTWNLQDMFRSKSDKKQYNLKLQNNLFEQELLQNEINSNLNQLNAEISAAADGIKESNISRQQAEDAYQLYKARYEGGLINLSELLQVQEILLQTERQNLTAYLNYWNLMVNKSYQQADFSQLFTHF
>NZ_LT906468.1|WP_093095030.1|1426210_1426612_+|hypothetical-protein
MLNTTIGFNQQFPLIAKVLGIVLLFVLTSCPIKASIKQNLYQDTKTESRSNKSAKPDSWIDYEAVDCSVANEQIKAHDLVVKDFQVQPAVIALFSLALILFSFLPRKEVENYHWNSQKTNSNDLFLQFRRLNL
>NZ_LT906468.1|WP_093095028.1|1424917_1426105_-|FecR-family-protein
MKTSREVAALIKKYIEGNISSLESIQLDQWIKEKPEHEEFFKKILIEDELFEDALTWVNLNQTDHTEWLEDIKSHTLQKIRKAEPKPIRSKKRVWIYYAAAAILLFGLGYSFLNYRSQTITEVDAELSAVQPGSNKAELSLSDGRTINLRSDKDGIVIDQDLAYSDGTPLLEVNKKELTKIMATIQVPKGGKYQIKLPDGSKVWLNSMSKLEYPLAFDPNRRTVKLEGEGYFEVAKLNKNDKRVPFEVISSSQTIEVTGTQFNVSAYPEDAQTVSTLVEGSINVHSASGKISLSPNQQAINSANGLSKRAVEVESFIAWKNNKFMFYETELRDVMKGLSRWYDIQVEYQGNIPATYFYGEIGRDKNLAEVIRLIEKSGVKFKLKQKGSTYKLIII
>NZ_LT906468.1|WP_093097681.1|1421250_1424562_-|TonB-dependent-receptor
MQSIQKQSGIPFFLNGKDIANTKINADIKNEKLETALTNLFTGKPISWELVDGTIILRRSENPTLGAQVSAVENRAAQQRRISGKVSDESGNPIQGASVVVTGTSNGTSTDANGNFSLEVSGSNISLSVSYIGFLKSEVSIGNQQNINIILKEDLGDLDEIVVVGYGTQKKKLNTGATIEVKGEDLEKLSTPSILEALQSQSPGVQITQSSGMPGESFKVTIRGLGTIGNSSPLYVIDGIAGGDINMLNPSDIERIDVLKDAASAAIYGARAANGVVLVTTKQGKDGKMSLHIDNYLGFQNAYKLPSLLTAKEYMTIQDERRFNEGGAPYDWANLIPKQYQQIQDGTWNGTNWMKEIHNDDAILQNTSLNLMGGNEQSKFSMGYSITNREGIIGKPVQPDFQRHTVRLNSDHILLKNDEFNIIKIGENINYGYNNRSGIGIGNIYWNDVHNMLVGNPLLPAFNENGDYYDQPSKVADKWALDGAISNPMAEMVFRRGQNKAKSHSLFANAYMEIQPIKNLIFKSNFGYRMSASTYRQYTDVYNLSTTVQNAVDDISQNQSVGYNWVLENTLSYHFEPITGHQFDVVAGQSMEKSGIGEDLSVTTSNSSFPGQWEKAWVSNGQGYDGFIPTVNGVHWPMGSIASVFGRVNYNYNETYMATLTLRADGSSNFAPGKRWGYFPSASVGWVLSNEDFLQGNEGINFFKLRASWGQNGNASISPFQYLATIAINNKNGYYFGNNMNTLLRGAYPDILPNPDVSWETSEQINVGFDSRFVDNKLSVVFDWYKKSTVDWLVQAPVLAIYGTSAPFINGGDIVNKGFELGLNWSDRNDNFSYSIGLNGAYNKNEVVRIANSEGIIHGEENVLSQGTKEMYRAQVGFPIGYFYGFKTDGIFQNQDQIDAWRAAGKGVLPTAQPGDVAFVDANMDGSITDADKMMIGNPHPDFSGGMNISLGYKGFDLGITAHGSFGHQIAKSYRSFADSPLQNYTTEIFERWHGEGTSNKLPRLTSGSHTNNQYISDIYIEDADFVKIQNITVGYDFSKLWNKSPFSQIRLYGTVQNLYTFTKYSGMDPEIGYGYDKSWVTGIDLGFYPQPRTIMFGLNLKF
>NZ_LT906468.1|WP_093095027.1|1419544_1421242_-|RagB/SusD-family-nutrient-uptake-outer-membrane-protein
MKKTILLLMAVGFLSSCEKFLDSESYDKKNTANFPVNVSDANSMLTGIYSSLSAAISNVANTHFYMAELASDDRFGGGGENDRDMQGLDHLMNTQPDRFLTFWTARYQGIFRANTALETLDQVQGWTNEGQKNQVLGEVHFLRALYYFELSQMFGEVPLVTSTQVTNIPKNPAAETYALIAEDLKTAISLMPATPYNSVPSGHATKWAAEALMARVFLFYTGYYKKADLPLASGGSVTKAQVIQWLDDCIKNSGHDLVSDFRNLWPYSNEFTKLDYKYAQDNNLKYEGEGHKETVFAVKFGTLVDWGDQYNLGYSNQYNLHFGLRSNNGLAGTFPFGQGWGAGPVNSNLWNEWKQAEPTDVRRTGSIINMATDVDSYIFGADNQMEETGFWQKKYISITAYDKETGALLPSYAILANAAQSEMQLAHTQDLALIRFADVLLMHAELTETATNLNRVRARAKLTPVAYSLAALKRERRWELSFEGLRYFDLMRWNDAGTALAKQEGVDIKNKGIDTKMKAFGGGYKARYEATGGFWPIPSSQIALSEGVLVQNKGWGDSSNEFPGW
>NZ_LT906468.1|WP_093095044.1|1434396_1435470_-|DUF3667-domain-containing-protein
MSHGKLREDKTCLNCGHFVEERFCPHCGQENTENRQPFHYLFTHFFEDFTHYDGQFWKTMKYLMFYPGKLTKIFLSGKRQGYVPPEKLYIFISFVTFFIASFVGTNSHSKNSGNVSLDSLQKEILKKEINQDLLGNGSNGVLDSSKLNSQLDRVFRLDSIQNDPDADLSKTKLFDFNSLAEYDSISLDNPSFIRKIFRPYVNKYFELKDKQVPLNKIAQSFVSIFMHTFPKALFFYLPIFAFILYLFHNKKKWWYYDHGVFTLHYFSFLLMIATLFLIMNLIEPSLHAYVWFNHLSTWIYTIAMIYAGIYFFIAHHRFYATRKRRSILIGILVFIVNSFVFSILLMILVSISLLLIH
>NZ_LT906468.1|WP_093095046.1|1435761_1436637_+|phosphate-ABC-transporter-substrate-binding-protein
MRNSIIRIFPILTLLGTTFFYSCSNNSNSIKMKGSDTEVNLAVNLAEKFTKLDPTFSIAISGGGSGLGITSLMNGQADIANSSRPLSEEEVQQFKDKNIDIKTVVFAEDATAFIVHKDLPMDSIDVETLAKIMDGSIKNWSEVSEVDYPVNIYGRQSSSGTHSFVKKKLKIEFANTAKEMTGNAQIIEGVKADKTGIGYVGAGYVSPDPQEAQGIKILKIKKDKASHSISPLDQDAINNGTYYFQRPLYQFILTKSWEKVRPFINFERSPAGRVLIEDHGYYILENQKNEI
>NZ_LT906468.1|WP_093095048.1|1436626_1437517_+|phosphate-ABC-transporter-permease-subunit-PstC
MKYRARLSLDVFFKFVFKATGFLVLALLGGILAMLIYNSFSFFLDVKPLDFITGMEWNPTGKNPKYGMLPLIISTTIVTFGAMLIAIPLGIGTAAFIAEYASPKLKNFLKPAIEMLAAIPSVVIGFLGIVVVSPGIASLADLSNGLNALNGAILLAVMALPTIITVAEDAIHAVPKTYKEASYGVGATKWQTLCKVVIPAAAPGIIAAVMLGVGRAIGETMTVLMATGNASILPTSMFDSVKTMTATIAIEMGEVPYQTTHYFALYAIATVLFIMTLAANMLGEYFINRFRKYHAA
>NZ_LT906468.1|WP_093095049.1|1437506_1438364_+|phosphate-ABC-transporter-permease-PstA
MQRRTLRLSSIIEWGTLLTSTLLVCFFLVVVIWEIVSKGASQLSWDFVTKVPSDGMTKGGILTPVIGTVLLTLITALFSIPFGVACAIYLQEYAEDSWLTRTIRASIRNLSGVPSIIYGLFGLALFVQAMHFGTSLIAAGLTLGLLSLPYIITTTEEALMRIPNSTREAALAVGATKFETIKDVIIPSAMSGILTGVVLTLSRAAGETAPILFTGAAFYINGTSAYINQEFMALPYHLYMLSTQHQSIDEVRPIAYGTALVLIIVVFLLNLTAFYIRYKYRKNEN
>NZ_LT906468.1|WP_093095052.1|1438353_1439100_+|phosphate-ABC-transporter-ATP-binding-protein
MKTKLSAENLNISFGTKHVLNNVNVQFAENEITALIGPSGCGKSTLLRSFNRMHDLSADAKITGSLKLEDLDLYSRAVPVTEIRKRIGMVFQKANPFPKSIYENIAYGLKINNLPHDKAIIEKALREAFLWEEVKNDLKMPATRLSGGQQQRLCIARAVALRPEVILMDEPCSALDPVSTLKIEELIMHLKEKYTIVIVTHNMQQAQRIADKTVFMYLGEVKEEGLTKQIFGNPVNEVTANYITGQFG
>NZ_LT906468.1|WP_093095054.1|1439326_1439776_+|hypothetical-protein
MRKLIVFCGLCALVFSSCGLKGSGEVVKGPQLLTVEFVGQQDSVIQNTKGKVKLFAVPANVADVSATMIDEVEFEAAQVPFTVDFEIPMDHQTMIKPEVQEGDSIKYYVSMEWDSNADGQLDSLDMAIDFDKQFPDIDINQLHQQVFLK
>NZ_LT906468.1|WP_093095057.1|1440203_1440890_-|arylesterase
MNHIKSLISAVFVVFLLASCNNSSPQQNSQAPSDSTSQDTAKTESSKRILFFGNSLTAGLGLDDQTEAFPALIQAKIDSLGLGYTCINAGLSGETSAGGKDRIDWLLKDKIDVFVLELGANDGLRGISPDATYQNLNEIVNKVKKAYPDCKLVLTGMMVPPSMGDQYFKDFAAIFPKLAKEQNMTLVPFLLDKVAGIQSLNQGDGVHPTKEGQQILAENVWTHLKTIL
>NZ_LT906468.1|WP_093095058.1|1440931_1441603_+|ABC-transporter-ATP-binding-protein
MSSTMILQVQHVFKNYQIGDHKIPVLNDINFEIEEGSTVSIVGPSGSGKTTLLGLCAGLDQSSEGDIILNGIKLTGLSEDKLAQVRNEHVGFVFQNFQLLPTLTALENVLVPMELRGMRNKQKEALELLEKVGLSARADHYPSQLSGGEQQRVSLARAFANKPKILFADEPTGNLDAETSAIIEDMLFQLNKESGTTLVIVTHDLDLAAKTQKIIPIKGGKIQ
>NZ_LT906468.1|WP_093095059.1|1441599_1444131_+|FtsX-like-permease-family-protein
MNWRWILLMAWRDSRKNRSRLFLFISSIILGIAALVAMNSFNVNLKKDIDSQAAELIGADLELESRREPSEEAMKFIDSLKGLSEDYAKEERFMSMIRFPKADGSRLVQVRAIEGNYPFYGKVETSPTDSYQDFGNKAGVYVENSLLLQFNAAVRDSVHLGNNSYQILGNVLSQPGQAAIAGAMAPSVFVPIAQLANSGLQQKGSRIEYHYYFKLPKNFAVDREVEKLDKKITELQLRASTIQTTKENTGRSFADMASFMELVGFVALLLGCIGVSSSVQIYVREKLLSVAVLRCLGTTAKQAFYIFLVQFAGIGLIGGIIGAILGSLIQYLIPVVMQDVIPVSLTTGVSWLAIIEGIGLGIVIAVLFALLPLLAVRNISPLNSIRISDKEESMFKDKMSWWVYLLILVFITGFARLQMADWVQTLVFVAGVGITFLLLYGVAKAFTYLIKKFFPKGWPYLWRQGLSNLYRPNNQTVILMISIGLGTALISTMFLVQDLLINRVKISSEQSQANMLMFDIQPSQRESLSEMAKAEGYPILESVPVVTMQLQSVNGVTLKDVVADTSQEVSSRAFRGEIRATYRDSLTASERVTSGKWAGTVGSNDTALVSLDQNYADNIKVKVGDRLSFNVQGLIIPAKVSSIRQVDWNRFQSNFRVVFAKGSIDKAPQFYLMMTKVPTELESSKFQQKIVNNYPNVSVIDMNAVLTVLQEILDKIAFIIQFMGAFSILTGIIVLISSVRISKFQRIRENVLLRTLGASRKQIYLITISEYLFLGLLSALTGIIISLLASYLLAIFVFESVFVPSIGMIALLMFLIVGLTVLIGLINSLSVINRSPLEALRKE
>NZ_LT906468.1|WP_093095061.1|1444195_1446460_+|S9-family-peptidase
MKKLFTLLFVLLSMISTKAQVAGDWKGELEVQGTKMEMIFHISDKDGNLSATMDVPAQGASGLPMSTVKFENNKLNLAMEQAGIAYEGELKGESIEGKFKQGGMEFPLKLAKTKISKPGDPSLVSTEAELAKLIELGNGNYKYKVEDYFAKPKSSSFALSPNGKYISYREKDANNKRHVMVKEVATGKVVRAIEEKDELIRGMGWVNDERLVYIMDQGGNENYHLYAVNIDGTKNIDLTPFEGVQAGILNMLKEQKDIIIIQMNKDNKQVFEPYKVNVQTGEMEKLFTNTDPENAIVGYEFDKDGNLRGYAKMQNGINTQFFYKPNGKTEFELFGTTNWYDTFSILSFNYASKNPDEAYVLTNLDSDKARIVLYDLGKKKLIKEIYSNPDYDATILGLSRNRNWELDYVGYEGEKVEIEPKSETFKGIYSLFKKEFPNYEYSIVGKTDKEDQYLVVVQSDKLYGKYYHLDAGTKKITLLYDLMPQLKEADMSEMRPISFKSRDGLTMHGYITLPKEALEGKKVPLIVNPHGGPQGVRDSWGFNPEAQLFAAHGFATLQVNFRVSGGYGKDFLKAGFKEIGRKAMDDVEDGIKYVIDQGWIDKDNVAIYGGSHGGYAVLRGLTKTPDLYKAGVDYVGVSNIFTLMSSIPEYWKPYKEMLYQVWYDLDDPKEAEIAKEVSPIFHVDKIKAPLFVVQGANDPRVKIAEADQIVKALRDKGVDVPYMVKYDEGHGFGKEENQIEFYKAMMGFFHKHLN

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Crispr_ID: NZ_LT906468_10

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LT906468_10

1601434-1601543

Orphan

Consensus_repeat	Method
GTCATCCTGACGCAGGAAGGATCTCGGATCTAT	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_LT906468_10

>merge|NZ_LT906468|10|1601434-1601543|CRISPRCasFinder
GTCATCCTGACGCAGGAAGGATCTCGGATCTATACAAACTATTATTCTATTGGCGTACAGCCTTCAACCACGTTGGGGTCATCCTGACGCAGGAAGGATCTCGGAACTAT

>NZ_LT906468|10|10|1601434-1601543|CRISPRCasFinder
GTCATCCTGACGCAGGAAGGATCTCGGATCTAT	ACAAACTATTATTCTATTGGCGTACAGCCTTCAACCACGTTGGG
GTCATCCTGACGCAGGAAGGATCTCGGAACTAT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LT906468.1\|WP_093095250.1\|1596006_1596327_+\|zf-TFIIB-domain-containing-protein	unknown	unknown	gnl\|CDD\|226331
NZ_LT906468.1\|WP_093095242.1\|1587282_1589517_+\|S9-family-peptidase	unknown	unknown	gnl\|CDD\|366030
NZ_LT906468.1\|WP_157739417.1\|1612319_1612496_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|224007
NZ_LT906468.1\|WP_093095271.1\|1612524_1614231_+\|dihydroxy-acid-dehydratase	unknown	unknown	gnl\|CDD\|235708
NZ_LT906468.1\|WP_093095248.1\|1594208_1595819_+\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	unknown	unknown	gnl\|CDD\|380159
NZ_LT906468.1\|WP_093095247.1\|1591210_1594159_+\|SusC/RagA-family-TonB-linked-outer-membrane-protein	unknown	unknown	gnl\|CDD\|274948
NZ_LT906468.1\|WP_093095261.1\|1604182_1606870_-\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|379720
NZ_LT906468.1\|WP_093095272.1\|1614251_1615016_+\|SDR-family-oxidoreductase	unknown	unknown	gnl\|CDD\|212491
NZ_LT906468.1\|WP_093095266.1\|1608867_1609767_+\|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|225117
NZ_LT906468.1\|WP_093095243.1\|1589559_1590501_+\|ornithine-cyclodeaminase-family-protein	unknown	unknown	gnl\|CDD\|180421
NZ_LT906468.1\|WP_139185403.1\|1597917_1598835_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906468.1\|WP_093095268.1\|1610132_1611473_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|213250
NZ_LT906468.1\|WP_093095241.1\|1585870_1587286_+\|amino-acid-permease	unknown	unknown	gnl\|CDD\|273332
NZ_LT906468.1\|WP_093095265.1\|1608329_1608731_-\|heme-binding-protein	unknown	unknown	gnl\|CDD\|377163
NZ_LT906468.1\|WP_139185404.1\|1598844_1599669_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906468.1\|WP_093095263.1\|1607092_1608286_-\|formaldehyde-dehydrogenase,-glutathione-independent	unknown	unknown	gnl\|CDD\|274314
NZ_LT906468.1\|WP_093095258.1\|1599878_1601369_+\|sulfatase	unknown	unknown	gnl\|CDD\|293763
NZ_LT906468.1\|WP_093095260.1\|1602010_1604038_-\|FUSC-family-protein	unknown	unknown	gnl\|CDD\|130728
NZ_LT906468.1\|WP_093095253.1\|1596924_1597845_+\|family-43-glycosylhydrolase	unknown	unknown	gnl\|CDD\|350105
NZ_LT906468.1\|WP_139185405.1\|1611635_1612298_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|366542

Protein	Function_ID	Function_description	E-value
NZ_LT906468.1\|WP_093095250.1\|1596006_1596327_+\|zf-TFIIB-domain-containing-protein	gnl\|CDD\|226331	COG3809, COG3809, Uncharacterized protein conserved in bacteria [Function unknown].	8.06024e-17
NZ_LT906468.1\|WP_093095242.1\|1587282_1589517_+\|S9-family-peptidase	gnl\|CDD\|366030	pfam00326, Peptidase_S9, Prolyl oligopeptidase family.	5.82014e-51
NZ_LT906468.1\|WP_157739417.1\|1612319_1612496_+\|hypothetical-protein	gnl\|CDD\|224007	COG1082, IolE, Sugar phosphate isomerases/epimerases [Carbohydrate transport and metabolism].	0.000188212
NZ_LT906468.1\|WP_093095271.1\|1612524_1614231_+\|dihydroxy-acid-dehydratase	gnl\|CDD\|235708	PRK06131, PRK06131, dihydroxy-acid dehydratase; Validated.	0
NZ_LT906468.1\|WP_093095248.1\|1594208_1595819_+\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	gnl\|CDD\|380159	NF033071, SusD, starch-binding outer membrane lipoprotein SusD. SusD (Starch Uptake System D) is an outer membrane lipoprotein that binds starch and participates in a TonB-dependent nutrient uptake complex. Related proteins from similar TonB-dependent complexes that import other, usually multimeric nutrient substrates include RagB and NanU.	1.17354e-37
NZ_LT906468.1\|WP_093095247.1\|1591210_1594159_+\|SusC/RagA-family-TonB-linked-outer-membrane-protein	gnl\|CDD\|274948	TIGR04056, OMP_RagA_SusC, TonB-linked outer membrane protein, SusC/RagA family. This model describes a distinctive clade among the TonB-linked outer membrane proteins (OMP). Members of this family are restricted to the Bacteriodetes lineage (except for Gemmatimonas aurantiaca T-27 from the novel phylum Gemmatimonadetes) and occur in high copy numbers, with over 100 members from Bacteroides thetaiotaomicron VPI-5482 alone. Published descriptions of members of this family are available for RagA from Porphyromonas gingivalis, SusC from Bacteroides thetaiotaomicron, and OmpW from Bacteroides caccae. Members form pairs with members of the SusD/RagB family (pfam07980). Transporter complexes including these outer membrane proteins are likely to import large degradation products of proteins (e.g. RagA) or carbohydrates (e.g. SusC) as nutrients, rather than siderophores. [Transport and binding proteins, Unknown substrate].	0
NZ_LT906468.1\|WP_093095261.1\|1604182_1606870_-\|TonB-dependent-receptor	gnl\|CDD\|379720	pfam14905, OMP_b-brl_3, Outer membrane protein beta-barrel family. This family includes proteins annotated as TonB dependent receptors. But it is also likely to contain other membrane beta barrel proteins of other functions.	0.000155992
NZ_LT906468.1\|WP_093095266.1\|1608867_1609767_+\|helix-turn-helix-domain-containing-protein	gnl\|CDD\|225117	COG2207, AraC, AraC-type DNA-binding domain-containing proteins [Transcription].	3.07672e-24
NZ_LT906468.1\|WP_093095243.1\|1589559_1590501_+\|ornithine-cyclodeaminase-family-protein	gnl\|CDD\|180421	PRK06141, PRK06141, ornithine cyclodeaminase family protein.	1.76218e-148
NZ_LT906468.1\|WP_093095272.1\|1614251_1615016_+\|SDR-family-oxidoreductase	gnl\|CDD\|212491	cd05233, SDR_c, classical (c) SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.	5.64394e-71
NZ_LT906468.1\|WP_093095268.1\|1610132_1611473_+\|hypothetical-protein	gnl\|CDD\|213250	cd03283, ABC_MutS-like, ATP-binding cassette domain of MutS-like homolog. The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.	2.67547e-47
NZ_LT906468.1\|WP_093095241.1\|1585870_1587286_+\|amino-acid-permease	gnl\|CDD\|273332	TIGR00911, High-affinity_methionine_permease, L-type amino acid transporter. [Transport and binding proteins, Amino acids, peptides and amines].	7.2291e-55
NZ_LT906468.1\|WP_093095265.1\|1608329_1608731_-\|heme-binding-protein	gnl\|CDD\|377163	pfam03928, Haem_degrading, Haem-degrading. Haem_bdg is a bacterial protein that is up-regulated in response to haemin- and peroxide-based oxidative stress. It interacts with the SenS/SenR two-component signal transduction system. Iron binds to surface-exposed lysine residues of an octomeric assembly of the protein.	1.27251e-37
NZ_LT906468.1\|WP_093095263.1\|1607092_1608286_-\|formaldehyde-dehydrogenase,-glutathione-independent	gnl\|CDD\|274314	TIGR02819, formaldehyde_dehydrogenase_glutathione-independent, formaldehyde dehydrogenase, glutathione-independent. Members of this family represent a distinct clade within the larger family of zinc-dependent dehydrogenases of medium chain alcohols, a family that also includes the so-called glutathione-dependent formaldehyde dehydrogenase. Members of this protein family have a tightly bound NAD that can act as a true cofactor, rather than a cosubstrate in dehydrogenase reactions, in dismutase reactions for some aldehydes. The name given to this family, however, is formaldehyde dehydrogenase, glutathione-independent. [Central intermediary metabolism, One-carbon metabolism].	0
NZ_LT906468.1\|WP_093095258.1\|1599878_1601369_+\|sulfatase	gnl\|CDD\|293763	cd16144, ARS_like, uncharacterized arylsulfatase subfamily. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.	7.04032e-152
NZ_LT906468.1\|WP_093095260.1\|1602010_1604038_-\|FUSC-family-protein	gnl\|CDD\|130728	TIGR01667, Uncharacterized_protein_HI_1680, integral membrane protein, YccS/YhfK family. This model represents two clades of putative transmembrane proteins including the E. coli YccS and YhfK proteins. The YccS hypothetical equivalog (TIGR01666) is found in beta and gamma proteobacteria, while the smaller YhfK group is only found in E. coli, Salmonella and Yersinia. TMHMM on the 19 hits to this model shows a consensus of 11 transmembrane helices separated into two clusters, an N-terminal cluster of 6 and a central cluster of 5. This would indicate two non-membrane domains one on each side of the membrane.	2.06006e-34
NZ_LT906468.1\|WP_093095253.1\|1596924_1597845_+\|family-43-glycosylhydrolase	gnl\|CDD\|350105	cd08991, GH43_HoAraf43-like, Glycosyl hydrolase family 43 protein such as Halothermothrix orenii H 168 alpha-L-arabinofuranosidase (HoAraf43;Hore_20580). This glycosyl hydrolase family 43 (GH43) subgroup includes Halothermothrix orenii H 168 alpha-L-arabinofuranosidase (EC 3.2.1.55) (HoAraf43;Hore_20580). It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. This GH43_ HoAraf43-like subgroup includes enzymes that have been annotated as having xylan-digesting beta-xylosidase (EC 3.2.1.37) and xylanase (endo-alpha-L-arabinanase, EC 3.2.1.8) activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.	1.77698e-123
NZ_LT906468.1\|WP_139185405.1\|1611635_1612298_+\|hypothetical-protein	gnl\|CDD\|366542	pfam01261, AP_endonuc_2, Xylose isomerase-like TIM barrel. This TIM alpha/beta barrel structure is found in xylose isomerase and in endonuclease IV (EC:3.1.21.2). This domain is also found in the N termini of bacterial myo-inositol catabolism proteins. These are involved in the myo-inositol catabolism pathway, and is required for growth on myo-inositol in Rhizobium leguminosarum bv. viciae.	5.36077e-09

>NZ_LT906468.1|WP_093095258.1|1599878_1601369_+|sulfatase
MFSKKTLTILFLLIAFGSAHAQKKPNIIIFMVDDMGWQDTSYPFADQATDFNKKYHTPNMERLAQEGMSFTDAYSTPVCTPTRVSLITGMNASRHHVTNWTAPFKDNPTGNQDEQMEEPEWNHNGMSPIPNIAHTIYADALPQILKDNGYFTIQAGKAHWGSAGTPGSNPYSLGFTVNIAGTSTGRPASYWGEENFGRTGKDYHGIENLQEYFGEDINLTEALTREALKSLDYPIQHKTPFFLNLCHYALHDPLMEDRRFFQKYLDQGLSQNEAKYASMIESMDKSLGDVMDFLEQHKIKENTYIIFISDNGGLSTVPPRDGIAHTHNKPLRSGKGSIYEGGIRVPLIIKGINKDVKNKRSGVPVIVEDIFSTVLDMAQLKKVQTVQQVDGVSNLALLKNPQTSRADRALIFHIPNKWAKSDGDGFNYRSAISKGKYKLVWSLRNDTYELFDLEQDLGEQHNIIQQTRMTKIAEELKAELKATLEKNKAPMPKRKG
>NZ_LT906468.1|WP_139185404.1|1598844_1599669_-|hypothetical-protein
MNPIVHQVLEKDRKLKLIFRLDSLNEVQFYQNNDRNKVDSQQVKLIMQSKKDSLAKNKLYEFYFFRDSISDTTFSNSEISAVGTFELYGVPASYPRGINALLNVLHTEISANMDKDRIDYYDWGKAISFMVDKNGKLKFIKDNNLISLVDSTKVKKWQPAIKYGRPVPQYYTTEPINKEKFLFENQYRIELYSSYDLLSPSFKGYPIIISDDLIAEGNFQTIVSFVNAKGLFEPHLIKGTTKNATELIDFIKSNGMELSSIFSHFPGRVYVYYK
>NZ_LT906468.1|WP_139185403.1|1597917_1598835_-|hypothetical-protein
MRIQILMIVFMLGMSQVFSQDQQAAERLQAKFEKLISKGIKPDSTASIVILTDSNKSYEVSVSSNIHSYQLGIITGIDSIKSDLEKNYLYSYHLLKDSIRNKVYVKYGTEQLYVFGEYNALASYPGGINEFKKIIFAMMEENMDSSKLDQYDWGQKIQFKIKSSGEMIFMNKNNLADLIDLKKLRKWHPSIELGYLVTEYFETDTLFKEDFLKTKAFDFEVNRIDYFSIDSQNQEVKASKEKPDLSEQKIVLSYIFLYDEFLDPIILKGEPKASQELIDFLALKDYNFDNKLYSEYPVTVYIYQE
>NZ_LT906468.1|WP_093095253.1|1596924_1597845_+|family-43-glycosylhydrolase
MKRIYLLVFILLMAIGSQAQEKLVPLGDPFIMLYQGTYYAYGTNAANGIQVYTSNDLKEWSQESNLALKSEDSWGGKWFWAPEVYYIKEKKQFFMYYSANEHICVASSDSPLGPFVQEKKAPMLPNEKAIDNSLFIDSDGKPYLYFDRFNDGLNIWVAKLQDDLITIDTNSMKPCIHVSQDWETVWPRVNEGSFVIQHKGLYYMTYSANSYESQHYGIGFATSKSVEGPWTKYDKNPIFQMPEDLVGVGHSAMFRDKEGKLRIVFHAHHSKEKIHPRAMYIATVDFSKDKLPVMQITGKVLRPKLK
>NZ_LT906468.1|WP_093095250.1|1596006_1596327_+|zf-TFIIB-domain-containing-protein
MKCPNCNEILLMTERHQVEIDYCPNCRGVWLDKGELDKLMEYASNQTQARDPRDYDRQNSYQQDQREEYRDDRYDRDHRDHRDYRGQNQKYPRKKKSFLSDFFDFD
>NZ_LT906468.1|WP_093095248.1|1594208_1595819_+|RagB/SusD-family-nutrient-uptake-outer-membrane-protein
MKNLKLKNILLLSGLFGSIMTFNACTDLNEEVYSEVLGSTVDPKERDLPFIVAPTYSSFRSLMFGWQGYFDLQEESADHIITPVRPNGWDDGGTYRRMHQHMWTTEQWQPYNTWNQAYATITKVNMVIMQIEDGLLALPEETGKDAIAELRATRALAYYLLLDNHGNVPIVTDYRDDSLPQQKTRKELYDFVIKELEEVIPMLSEEVSSMYGRINIWAAKTLLAKVYLNAEVYIGVAQWDKVIKETNDIIASNEYRLDDDYKNVFSHTNQNSPEIIFSVPYDEVYGFGNQIHMKTLDPLSRLVYGMAAGPWGGNCAVPQFIDSYDKDDTRLYDTWIQGPQLNASTGAEVINYVKQVPGIGGDGTVAASNAGFRIGKYAIKQGATNNLDNDYPMFRYADVLMMKAEALLRTNKANEAAVLVSQVRARSFKDNPAKAQVTGAQLLLGSNYNYGWQEKNNTVSGANGGADVKYGRFLDELGWEFAAEARRRQDIIRFGVFQSKSWFNHKPHTNAQSRTLFPIPNAEITKNPNLKQNPGY
>NZ_LT906468.1|WP_093095247.1|1591210_1594159_+|SusC/RagA-family-TonB-linked-outer-membrane-protein
MKKPNIMLVILFSCIQVLFAQNKIQLNGEVVNTTGEKLSGVTISLSNSNQKYMTDENGSFSFEYVPGTNLTINSLGFATQQITLTNQTSLKVVLIESEENLEQIVVVGYGTQRKGETTGSVASVKSESFNQGAVKDAGQLIQGKVAGLRITTPSGDPNGSTQINLRGLNSIQGAVNPLVIIDGVPGDFNSVAPEDIESVDVMKDGSAAAIYGTRATGGVIFITTKQNRSTDGRTTIEYNNYASLQTLFRVPELMNAEDYRRLIAEGQNYTDLGHSTNWVDEVTQNPFSHNHNLSLFGGNARTNFTGTVNFRDWNGVLLKSGQQRLNARADLNHEMFDGKLRSRIQIISNSIKALQGGSSNYMWRQALIRNPTDRIYNDEGKWQENNAYMYDNPLGMINETVNDRIFRETRMNGSLDYRPIESLSFKAMFSRVQDNDLTGTSTSFNHVNTTKNNLNGTASRFTQAGVENLMELTGNFNKSFGDHNFAVLGGYSWQRNTFENFSAYNFNFPTDQYSYNSLESGMALKEGLATMDSYKQESTLVGFFGRLTYNYKEKYMAMLSLRREGSSTFGENNKWGNFPAVSVGWDMAKEDFLMDQTAINQLKLRAGYGVTGTIAGSPYNSQISYNYTFDQGAYINGKWVPGFVPARNFNPDLRWERKNEFNVGVDYSLANNRIYGSLDYYNRRVKDLLYWFEVPVPPYLTSTMFINAGEMSNSGFEALVNADVLNKAGGVQWKTGVVFSTNKNKLINLSNDRFGVTQEFFDAGYTGEPIQTFTHRVEVGRSIGDFYVWKTVGLDEDGKWLVESQNGEIIPIQDASVEDRQYYGNGIPDFNLGWNNNFQYKNIDLTINWRGAFGHQILNMPRMYYENPVNKAYNVLKTAYDPIDGKLLNNDLVYVSHYIEDADYFKLDNLTLGYTFNPQLIKGISNLRIYVSGLNLVTFTKYKGLDPEATSYEGEFQFAPGIEHRDRYPTTRTYTIGLNVKF
>NZ_LT906468.1|WP_093095243.1|1589559_1590501_+|ornithine-cyclodeaminase-family-protein
MRTIDNETIDQVLNYDKMLEALYKIFISKFTMPVRHHHFYNTPDSAENALILMPAWTDKYLGCKQVIVAPKNAEQHLPAIHALYTLFNAETGVPLAQMDATKLTSVRTACASALAAKYLARENAENLLVIGSGSVAYHLAQAHSSVRNYKHIEVWARNSDKAQALLESLKEQGFTNVSLANDLQEAIQKADVISSATLSKEPIIKGEWLKPGVHLDLIGSHTPKTREADDEVIRRSTIYADSREGALHETGELAIPIASGLLDPKDVQADLVELCKANKLARKNEEEITLFKSAGLAIEDLAAALMVYEAVAE
>NZ_LT906468.1|WP_093095242.1|1587282_1589517_+|S9-family-peptidase
MKLRITAFLLFILQVSSYAQGTLDDYKRAKEVRNNFGKIYNIPQQITWAEDGGSFVYKLKQKDNKSILVLVDAQTKSKKIIDLEAMSEQMSKLLSETVPLNNSWFVGLKPINNNEIEFTEKKKVWRWNVSENKLSIQKELNDNERGSGYWGQKWDDSKGEPIESPDKVYLAYIKNNNIYVRKKADLKSEKQMTFDGSPGLYYSARLDWSADSKKLSSSKVRKAEVRQLTLLESSPTDQLQPKLQYRDYAKPGDALSQYYPVIVNVESGQVVEVDPKQVENQFSLYNIRWRPDNNAITFEYNQRGHQRYDVLELDAVTGQTKPIISETSKTFIDYSGKKYRKDLEKSNEIVWTSERDGWNHLYLIDAKTGKVKNQITKGNWVVRKVINVNETDRKIIFEGSGRNKNEDPYLVRYYSIGLDGNGLKELSPEVANHQGYFNKDFSKFIDVYSLVDQAPKAVLRDAKTGKVELDLESADLSDLNASGWKAPEVFSTAGRDGKTDIWGVIIRPNNFDPNKKYPIVEYIYAGPHSSFVPKSFTSGLSGMYELAELGFIVVQIDGMGTSNRSKAFHDVAWKNLKDAGFPDRIAWMKAAAQKYPYMDIDKVGIYGTSAGGQSSTGAVLFHPEFYKVAVSSCGCHDNRMDKIWWNEQWMGWPIGPQYAECSNIENAHRLEGKLMLIVGELDDNVDPASTYQLVNQLIKNGKEHELIMVPGMGHSSGGDYGEKKRRDFFVKNLLGVEPPAWNLY
>NZ_LT906468.1|WP_093095241.1|1585870_1587286_+|amino-acid-permease
MEENKQEFKKSLGLLDATMLVAGSMIGSGIFIVSSDIARNTGSAGWLMIVWAISGFMTLAAALSYGELSSMFPKAGGQYVYLKEAYGPVVSFTFGWTFFAVIQTATIAAVGVAFAKFTAYLFPSLDEDVYLLTIGTYHISSAQVLAIAVILLLTFINTLGVQNGKVVQTTLTLIKILSLVLAVLFGFAAFDLEVWNHNWNSADTWNLSRLAVDGGKSDYTFLAGLGAISAGLVGALFSSDSWHSSSAVAGEIKNPQRNIGLSLALGTIIVTVIYLLTNLMYTGVLQMEEMASAPKDRVAMVAAQEIFGPIGITVLAIMIMVSTFGCNNGLIMAGARIYYSMAKDGLFFKKTKELNKHAVPSYALWLQGIIACVWCLTGKYGDLLDMITCVVVIFYVLCIIGIFILRKNRPDLPRPYKALGYPIIPAIYILLGISFILLLVFYKPQFTWPGIIITLLGIPIYFIVKSKKSSL
>NZ_LT906468.1|WP_093095260.1|1602010_1604038_-|FUSC-family-protein
MVAALFSRLLSFLKTESSLDALRNILVVLVPSFFIFFFIDGAIAVAFAVGALLAALTDVPGNKTDKLSTAAYCLPIFFITALSISTALSHQSWIIVPLLGLFGFIYTIIALLGFRVNVVGNLGLIVASFTIGLRPADPISFSLSVTAGAMFFFVVCIIQVYLHPHRSLRYAVDGGLKTMAQLIRLKIACYDELASLPKAYKELSALHTKLSDQLEAIRSILLRDKKLHSEADQESKIWLAKLYQLVDLYELLMAIDNDYEHIRETLKGGNTLKLIRQSLSLLSKETKRLTISNKKIRLNKFTKRYKLEELLLQLETEEADASPEKWALICSISTQLRHVADILQKIQAKEIYQDITLVESKNYADFVAPKSNIKTILQNLSFKSPIFSYAVRMSALLMAGGLIGNFLPEYRYASWILLTIILVARPSYTNTQKRNYERIVGSVIGIAISLLLLVYIKNAWVLIAIAAFCLYLFLLFNKPNYLVCVIFITITILLGQHIHEGNIQDLLGSRFAFTLLGSIFAVLGCLAIPINHYRSVEQSTNAMLQHFKSYLHKIEESYQTGNLNYYDLRLLRKSTQASLAQSYDSLDQFAKEPLKGKYLKADIAHFQTLAYRINALLVGLSVNMTKLGFTLEPEVMEEKVHYINNIISEAEDLSKKLAKGKKEKNGKTIQLEASK
>NZ_LT906468.1|WP_093095261.1|1604182_1606870_-|TonB-dependent-receptor
MQKIYLITFLVLTFSFAHAQNNAGIKGKVFDSELNPLEKATVSLVSEQDSLVVTYALTNEKGEFELVRIPTNKELTFYISHVNSSAFQKKINLKPNEKLKMDSIILKGNAIEAIEITAVPPIRLNGDTLEYKASYFKTRPNANVEELISLLPGLQVNSDGTIYYQGRQVQSVRVNNKDFFAQDLKIATRNLDASLIDVVQVIKDKGESKREILDDSQLPIVLNLKMKKEFLKANFGKLYGGAATRDRYEAGALINTFRDTLQVSFIGFANNINRQGFDYSELNEHGGMNRSENRSFTNYGTSGLMNQISAGVNINYDIEKKLKVNLMYNYGQHDFYYDSRSESNSFYNEIAEQNSNNNTSNDSRYTHELRGFMRYRLDTTSQVTFSPSLSGNRGKSTASGYGERWRENLQKVTQGEFQNDDSNKGLNYGHNLYAEKKFKNKWLLSLNQGISNQNGSSTDNNTSNTQFFLLDDSAFHQINRQRTNTSTFNLSHQLNLQIPLGKKVNFDVFGHQNLNEQTSTEDILNSINSDILQNRNDVANDKGLLNKNFIIGTKWNVQFIKNLPISLGLKWGSFSNHFDYYQKLENRKIEESHWLPDMNISYKGLNFNYHKDLEAPGYYSIVTVKSDLSPNYLRIASPFFENNLKENYRISYNKFFSKSKINLNVSAGWTKNSNSIAHSRTYDVQTSFSTGQYYQAGPTEVKNYYLSFSKTIIQNKVWNLNYNGYGYGVLQDTYSKVNGEENIGSVFFSNFNNTLTLTYKNVFTFTPMFEFNTNNTKFKFDSENFRDMNNNTKRYGATLLLNNIKKFRLESSYNIKNQVVGINNQRQNLHIVNASVYYPILGKGELKLSAFDILNQNVSNYFGSSSNSTYFNSTTTLRQYFLLGMVYKFLKTGDK
>NZ_LT906468.1|WP_093095263.1|1607092_1608286_-|formaldehyde-dehydrogenase,-glutathione-independent
MCQNHGVVYMGPGEVQVQEIDYPKLALGDRKCEHGVILKIVSTNICGSDQHMVRGRTTASAGLVLGHEITGQVVEKGRDVEFIDVGDIVSVPFNIACGRCRNCKEGKTGICLNVNPSRPGAAYGYVDMGGWVGGQAEYVMVPYADFNLLKFPDNEQAMEYIRDLTMLSDIFPTGFHGAVSAGVGPGSVVYVAGAGPVGLACAASCHLLGAAVVIVGDLNEERLAQAKSFGCETVNLNTGEELSEQIAAIVGVPEVDCFVDCVGFEARAHSHGGSSEEQPAVVLNQAMEITRAGGAIGIPGLYVTEDPGAVDGAAKQGNLKIRFGLGWAKSHCFHTGQCPVMKYHRQLMNAILYDKIKIADAVNVQVISLNEAPQGYADFDKGAARKYVIDPHGMIPA
>NZ_LT906468.1|WP_093095265.1|1608329_1608731_-|heme-binding-protein
MSNITLEQARKVVDAALKKSEELGVKMNIAVVDAGTNLVAFNKMDDAWLGSIDISQKKARTARYFNMDTGEIGKLSQPGGSLYNIEHSNNGLITFPGGVVIKDGSGKIIGAVGVSGSTVEDDHAVAAAGASAV
>NZ_LT906468.1|WP_093095266.1|1608867_1609767_+|helix-turn-helix-domain-containing-protein
MNNTIDLLSLQTPEHLRSGQEHQTRFDCGEFEVNIFETFQSSTKVKITYEGLSISSMIRGYKTVYTKKGESFKFLPGTSLILPEGETIYADFPEADLKNPVQCATILISRDSLENQFKFLNQNYPEKEQWNLDFSNFHFNNNPGLVRAFNELLQVATQTDPNIPLSDLLLKSLLIRIKESQKEHAKEQNSLTAKSQLHVIKNYIRENLGQTLNTELLMKIGNCSKSTLHRMFEAYCGKTPGAYILQERMLNARNLLLQADSNVSEVAYKTGFSSLSYFVKQFKAFHNCTPGDFIKKFGK
>NZ_LT906468.1|WP_093095268.1|1610132_1611473_+|hypothetical-protein
MSEKFLIDEQTLQDIQLRDRHNRTILEFFDHTITDGGMYYLMDVFYNPVLDVDVIKDRQTKIRRLEPVADQDFLFYRVIVKDLEKYVKSSHSGRAASLTLMDFIGVRSPVYYYKKRSIQEACDFMIKCRDYYLQINKDVKYPDVEEILQLIEDCLSMIFKKKKYDADKLRINIFNIENFDKMVRYTLAPKIKKIITFFYEIDAFLSVAKVSKAHGFCYPEVYPKNQTGVIEMKGVYHIFHKNPVKNDVRMARDKKIWFLTGANMAGKSSIIKTISSALYLTHIGFPVPADSIKTDLINGVFTSINLQDNLEMGYSHFYVEAMRLKTIVDQLPKDSNAVIILDELFKGTNHSDASNAILKVLQNLAEVDGPYVIVSSHITELSKELEHIPSVGFFKMNIESDPEGLPIFTYKIKEGVAEEKLGMWLLKKSGAFDSIDKIKNTADTTS
>NZ_LT906468.1|WP_139185405.1|1611635_1612298_+|hypothetical-protein
MKTFFRRTEMLAVMVVLSMLFFSCTGQTKPAKDQTLEVENMEVGVGLYSFNRFPFDKSVEMAKAANSQKVEGFSFHNLGERFGGKVIASLTDEEIAKMKGILDSNQVQMVSMYADGKTIEEWEQLFNQGQKLGLHFLVGEPDPQLLDKINELAGQYKLPLAIHEHAKGLSRYWHPDSAMAAVEGRDHLKVCADIGHWVRSGLDPVECLQKVEGKLLSLHV
>NZ_LT906468.1|WP_157739417.1|1612319_1612496_+|hypothetical-protein
MEAKDVAIGAGVIDYDKVFAELKRQHFSGDIFIECEHNWDNNFEEVKESVNYIRQKAK
>NZ_LT906468.1|WP_093095271.1|1612524_1614231_+|dihydroxy-acid-dehydratase
MKLRSKEWFARKGKDGFIYRAWMKNQGIPADMFEGKPVIGICNTWSELTPCNAHLRDLAEAVKKGVLEAGGFPLEFPVMSLGETLMKPTAMLFRNLASMDVEESIRANPMDGVVLLVGCDKTTPSLVMGACSVDLPSIVVSGGAMLTGKFRGKDIGTSDVWRFADDSKKGLISEEEMNMAEAGMCRSIGHCAVMGTASTMAGMVESLGITLPGNAAIPAADSRRKVLARMSGRRIVEMIKENLKLSDVLKREAFENAIKVNAAIGGSTNFAIHLMAIAGRIGVDLNLEDFDHYSKDIPLVANLQPSGQYFMEDLYYAGGIPAVMNSIKGSLNADILTVSGKTVAENIQDQESLNDDVISTKDNPFNPISGIVVLKGNLCENGAVLKPSAATPELMKHTGKAVVFENIEDYKNRIDSDDLDVDANSVLVLKNVGPKGYPGMPEVGNMGIPKKLLDMGVTDMVRISDGRMSGTGFGTVVLHVSPESAVGGTLALVQNGDLIELDVEARKLNLLLDDAELESRRQNLKVEGNPYTRGYCKLYVDHVEQAHLGADLDFLKGGSGSEVLRDSH
>NZ_LT906468.1|WP_093095272.1|1614251_1615016_+|SDR-family-oxidoreductase
MEQKRFVNKTAIVTGAGKGIGFEIAKSLVLEGATVVLNDVDPGLCDEATAQLKEIGNCYSFAGDVSTASFNQEIVDFAVSKTGTLDIVMANAGITLFGSFLEYKAEDLYKVLQVNIGGTFFLAQAAGKYFIEQKKRGSILFTSSVTGHQAHKELAAYGMTKAAVELLAKHLVLELSPFGINVNAVAPGATLTERTMEDPEYKKTWAHLTPIGSAAYPSDIAQTALFLVSEQARHITGQTIVVDGGWSAVSPSPY

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Crispr_ID: NZ_LT906468_11

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LT906468_11

1640347-1640472

Orphan

Consensus_repeat	Method
TTGGCGTACATTTCTTCAAACCTCGTTAACAACTCTGG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_LT906468_11

>merge|NZ_LT906468|11|1640347-1640472|CRISPRCasFinder
TTGGCGTACATTTCTTCAAACCTCGTTAACAACTCTGGAGTCATCCTGACGAAGGAAGGATCTCGGAGTTATACAAACAATGATTGTATTGGCGTACAGTTCTTCAAACCTCGTTAACAACTCTGG

>NZ_LT906468|11|11|1640347-1640472|CRISPRCasFinder
TTGGCGTACATTTCTTCAAACCTCGTTAACAACTCTGG	AGTCATCCTGACGAAGGAAGGATCTCGGAGTTATACAAACAATGATTGTA
TTGGCGTACAGTTCTTCAAACCTCGTTAACAACTCTGG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LT906468.1\|WP_093095297.1\|1634690_1636112_-\|DUF1501-domain-containing-protein	unknown	unknown	gnl\|CDD\|369346
NZ_LT906468.1\|WP_093095316.1\|1647540_1648575_-\|ThiF-family-adenylyltransferase	unknown	unknown	gnl\|CDD\|238386
NZ_LT906468.1\|WP_093095287.1\|1625782_1626811_-\|L-glyceraldehyde-3-phosphate-reductase	unknown	unknown	gnl\|CDD\|381376
NZ_LT906468.1\|WP_093095290.1\|1627868_1629443_-\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	unknown	unknown	gnl\|CDD\|380159
NZ_LT906468.1\|WP_093095305.1\|1642129_1642372_+\|MoaD/ThiS-family-protein	unknown	unknown	gnl\|CDD\|340452
NZ_LT906468.1\|WP_093095306.1\|1642373_1642790_+\|molybdenum-cofactor-biosynthesis-protein-MoaE	unknown	unknown	gnl\|CDD\|238385
NZ_LT906468.1\|WP_093095299.1\|1638873_1639857_+\|alpha/beta-hydrolase	unknown	unknown	gnl\|CDD\|369561
NZ_LT906468.1\|WP_093095303.1\|1641368_1642118_+\|sulfite-exporter-TauE/SafE-family-protein	unknown	unknown	gnl\|CDD\|376667
NZ_LT906468.1\|WP_093095286.1\|1624726_1625635_-\|NAD(P)/FAD-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|223566
NZ_LT906468.1\|WP_093095314.1\|1646622_1647540_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|226304
NZ_LT906468.1\|WP_093095312.1\|1644081_1646475_+\|FdhF/YdeP-family-oxidoreductase	unknown	unknown	gnl\|CDD\|273765
NZ_LT906468.1\|WP_093095288.1\|1627039_1627771_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906468.1\|WP_169918984.1\|1633826_1634642_+\|glycoside-hydrolase-family-16-protein	unknown	unknown	gnl\|CDD\|185693
NZ_LT906468.1\|WP_093095308.1\|1642836_1643712_+\|formate-dehydrogenase-accessory-sulfurtransferase-FdhD	unknown	unknown	gnl\|CDD\|234823
NZ_LT906468.1\|WP_093095310.1\|1643708_1644059_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906468.1\|WP_093095295.1\|1632906_1633779_+\|DNA-binding-response-regulator	unknown	unknown	gnl\|CDD\|225117
NZ_LT906468.1\|WP_093097707.1\|1636138_1638487_-\|DUF1549-domain-containing-protein	unknown	unknown	gnl\|CDD\|377872
NZ_LT906468.1\|WP_093095318.1\|1648564_1649194_-\|NTP-transferase-domain-containing-protein	unknown	unknown	gnl\|CDD\|237728
NZ_LT906468.1\|WP_093095292.1\|1629491_1632476_-\|SusC/RagA-family-TonB-linked-outer-membrane-protein	unknown	unknown	gnl\|CDD\|274948
NZ_LT906468.1\|WP_093095320.1\|1649171_1649648_-\|cyclic-pyranopterin-monophosphate-synthase-MoaC	unknown	unknown	gnl\|CDD\|236483

Protein	Function_ID	Function_description	E-value
NZ_LT906468.1\|WP_093095297.1\|1634690_1636112_-\|DUF1501-domain-containing-protein	gnl\|CDD\|369346	pfam07394, DUF1501, Protein of unknown function (DUF1501). This family contains a number of hypothetical bacterial proteins of unknown function approximately 400 residues long.	6.52394e-78
NZ_LT906468.1\|WP_093095316.1\|1647540_1648575_-\|ThiF-family-adenylyltransferase	gnl\|CDD\|238386	cd00757, ThiF_MoeB_HesA_family, ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis family. The common reaction mechanism catalyzed by MoeB and ThiF, like other E1 enzymes, begins with a nucleophilic attack of the C-terminal carboxylate of MoaD and ThiS, respectively, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of MoaD and ThiS. MoeB, as the MPT synthase (MoaE/MoaD complex) sulfurase, is involved in the biosynthesis of the molybdenum cofactor, a derivative of the tricyclic pterin, molybdopterin (MPT). ThiF catalyzes the adenylation of ThiS, as part of the biosynthesis pathway of thiamin pyrophosphate (vitamin B1). .	9.8879e-103
NZ_LT906468.1\|WP_093095287.1\|1625782_1626811_-\|L-glyceraldehyde-3-phosphate-reductase	gnl\|CDD\|381376	cd19150, AKR_AKR14A1, Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar proteins. Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo.	0
NZ_LT906468.1\|WP_093095290.1\|1627868_1629443_-\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	gnl\|CDD\|380159	NF033071, SusD, starch-binding outer membrane lipoprotein SusD. SusD (Starch Uptake System D) is an outer membrane lipoprotein that binds starch and participates in a TonB-dependent nutrient uptake complex. Related proteins from similar TonB-dependent complexes that import other, usually multimeric nutrient substrates include RagB and NanU.	4.83382e-32
NZ_LT906468.1\|WP_093095312.1\|1644081_1646475_+\|FdhF/YdeP-family-oxidoreductase	gnl\|CDD\|273765	TIGR01701, Hypothetical_protein_Rv2900c/MT2968/Mb2924c., oxidoreductase alpha (molybdopterin) subunit. This model represents a well-defined clade of oxidoreductase alpha subunits most closely related to a group of formate dehydrogenases including the E. coli FdhH protein (TIGR01591). These alpha subunits contain a molybdopterin cofactor and generally associate with two other subunits which contain iron-sulfur clusters and cytochromes. The particular subunits with which this enzyme interacts and the substrate which is reduced is unknown at this time. In Ralstonia, the gene is associated with the cbb operon, but is not essential for CO2 fixation.	0
NZ_LT906468.1\|WP_093095306.1\|1642373_1642790_+\|molybdenum-cofactor-biosynthesis-protein-MoaE	gnl\|CDD\|238385	cd00756, MoaE, MoaE family. Members of this family are involved in biosynthesis of the molybdenum cofactor (Moco), an essential cofactor for a diverse group of redox enzymes. Moco biosynthesis is an evolutionarily conserved pathway present in eubacteria, archaea and eukaryotes. Moco contains a tricyclic pyranopterin, termed molybdopterin (MPT), which carries the cis-dithiolene group responsible for molybdenum ligation. This dithiolene group is generated by MPT synthase in the second major step in Moco biosynthesis. MPT synthase is a heterotetramer consisting of two large (MoaE) and two small (MoaD) subunits.	8.15533e-52
NZ_LT906468.1\|WP_093095299.1\|1638873_1639857_+\|alpha/beta-hydrolase	gnl\|CDD\|369561	pfam07859, Abhydrolase_3, alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes.	2.89608e-85
NZ_LT906468.1\|WP_093095303.1\|1641368_1642118_+\|sulfite-exporter-TauE/SafE-family-protein	gnl\|CDD\|376667	pfam01925, TauE, Sulfite exporter TauE/SafE. This is a family of integral membrane proteins where the alignment appears to contain two duplicated modules of three transmembrane helices. The proteins are involved in the transport of anions across the cytoplasmic membrane during taurine metabolism as an exporter of sulfoacetate. This family used to be known as DUF81.	6.46946e-29
NZ_LT906468.1\|WP_093095286.1\|1624726_1625635_-\|NAD(P)/FAD-dependent-oxidoreductase	gnl\|CDD\|223566	COG0492, TrxB, Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones].	3.40689e-49
NZ_LT906468.1\|WP_093095314.1\|1646622_1647540_+\|hypothetical-protein	gnl\|CDD\|226304	COG3781, COG3781, Predicted membrane protein [Function unknown].	5.16465e-123
NZ_LT906468.1\|WP_093095305.1\|1642129_1642372_+\|MoaD/ThiS-family-protein	gnl\|CDD\|340452	cd00754, Ubl_MoaD, ubiquitin-like (Ubl) domain found in molybdenum cofactor biosynthesis protein D (MoaD) and similar proteins. MoaD, also termed molybdopterin synthase sulfur carrier subunit, or MPT synthase subunit 1, or MPT synthase small subunit, or molybdopterin-converting factor small subunit, or molybdopterin-converting factor subunit 1, is a conserved small sulfur carrier protein that has beta-grasp ubiquitin-like (Ubl) fold involved in biosynthesis of the molybdenum cofactor (Moco), an essential cofactor of a diverse group of redox enzymes. MoaD is activated in an ATP-dependent manner by sulfurtransferases similar to the activation mechanism of ubiquitin-activating enzyme E1.	1.13403e-20
NZ_LT906468.1\|WP_169918984.1\|1633826_1634642_+\|glycoside-hydrolase-family-16-protein	gnl\|CDD\|185693	cd08023, GH16_laminarinase_like, Laminarinase, member of the glycosyl hydrolase family 16. Laminarinase, also known as glucan endo-1,3-beta-D-glucosidase, is a glycosyl hydrolase family 16 member that hydrolyzes 1,3-beta-D-glucosidic linkages in 1,3-beta-D-glucans such as laminarins, curdlans, paramylons, and pachymans, with very limited action on mixed-link (1,3-1,4-)-beta-D-glucans.	1.57289e-98
NZ_LT906468.1\|WP_093095308.1\|1642836_1643712_+\|formate-dehydrogenase-accessory-sulfurtransferase-FdhD	gnl\|CDD\|234823	PRK00724, PRK00724, formate dehydrogenase accessory sulfurtransferase FdhD.	8.38947e-85
NZ_LT906468.1\|WP_093095295.1\|1632906_1633779_+\|DNA-binding-response-regulator	gnl\|CDD\|225117	COG2207, AraC, AraC-type DNA-binding domain-containing proteins [Transcription].	3.37922e-20
NZ_LT906468.1\|WP_093097707.1\|1636138_1638487_-\|DUF1549-domain-containing-protein	gnl\|CDD\|377872	pfam07583, PSCyt2, Protein of unknown function (DUF1549). A family of paralogues in the planctomyces.	4.24374e-65
NZ_LT906468.1\|WP_093095318.1\|1648564_1649194_-\|NTP-transferase-domain-containing-protein	gnl\|CDD\|237728	PRK14490, PRK14490, putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MobA; Provisional.	9.4417e-61
NZ_LT906468.1\|WP_093095292.1\|1629491_1632476_-\|SusC/RagA-family-TonB-linked-outer-membrane-protein	gnl\|CDD\|274948	TIGR04056, OMP_RagA_SusC, TonB-linked outer membrane protein, SusC/RagA family. This model describes a distinctive clade among the TonB-linked outer membrane proteins (OMP). Members of this family are restricted to the Bacteriodetes lineage (except for Gemmatimonas aurantiaca T-27 from the novel phylum Gemmatimonadetes) and occur in high copy numbers, with over 100 members from Bacteroides thetaiotaomicron VPI-5482 alone. Published descriptions of members of this family are available for RagA from Porphyromonas gingivalis, SusC from Bacteroides thetaiotaomicron, and OmpW from Bacteroides caccae. Members form pairs with members of the SusD/RagB family (pfam07980). Transporter complexes including these outer membrane proteins are likely to import large degradation products of proteins (e.g. RagA) or carbohydrates (e.g. SusC) as nutrients, rather than siderophores. [Transport and binding proteins, Unknown substrate].	0
NZ_LT906468.1\|WP_093095320.1\|1649171_1649648_-\|cyclic-pyranopterin-monophosphate-synthase-MoaC	gnl\|CDD\|236483	PRK09364, moaC, cyclic pyranopterin monophosphate synthase MoaC.	1.23332e-64

>NZ_LT906468.1|WP_093095299.1|1638873_1639857_+|alpha/beta-hydrolase
MSERKAEKDPQIIVQIREFLDGLNNSGGEPLETLSPEDARQVLVDAQKSVKVDYSGISESEREISQDGIKVNIHIVKPEKSKDKKLPVFIFIHGGGWILGDYPTHRRLVRDLVVNSGAAAVFVDYTPSPEAKYPVAINEIYAATKWVSENGDEIGVDGSNLAIAGNSVGGNMTAVTCLMAKDKGGPKIKFQLLLWPVTDADFSRDSWKKYAEGRFLTSNMMKWMWDNYLPEESKRKEYYATPFNASIEELKGLPPALVQLAENDILFDEGLAYARKLDEAGVPTTIQTYNGFIHDYGLLNPLDHIPAVKFSTELAALGLKKALFGLE
>NZ_LT906468.1|WP_093097707.1|1636138_1638487_-|DUF1549-domain-containing-protein
MLVHFPVALILVAGFMELAKLRSFQSNLRTGTNWLIYIGAVSAVLAAGLGLFLANTGTYSGETFEWHQWSGISTAVFGAITALVLLQIMKHDKKGLIPIYRTSLLLTVLSIFMAGHFGGSLTHGQDYLLSTTPWAPQDENLAEIAGGVSSAEFDFASFSTASDSLTTEQQVNLNLAVRTIFAHHCFQCHGSDKTEGELRLDQKDMVFKGGESGQVILPGDSEHSELLRRVSLPPGHKEAMPGKGKPLGEKDIAIIKLWIDKGAPWPDNIKGIFPNAPLEPRKPELPAVVAGMENPVDRLVNAYFKKNGIQWQKPVDDRTYIRRVYFDLIGLPPTDQEIKSFVADGNSDKREKLVNSLLAKDREYATHWTTFWNDLLRNDYSGTGYITGGRFNISDWLFKSLQTNKPYKQFAMELLDPTEESKGFIKGIAWRGAVNSSQTTAMQAAQNVSQALLGVNLKCASCHDSFVSDWKLDDAYAFANIFSEEQLEINRCDIPTGKMADTRILWPELGTISKTGTVKEKSKELSQLLTQPENGRLYRTLVNRIWAQLMGRGIVSPTDEMDKKPWSADLLDWMAVNFVEEGYDIKKLLYLITTSKTYQQPSIGLEDQSAINAPNFVFRGILKKKLTAEQFSDALSTVVSPVYTIDALKYNPLADPKAYMDASSFVRAALVQNDPFLTALGRPSRENVISVREGHVTLLQAMELTNGTKLNETLIQGAKKWLAQYKDPNELTQAIYGQTLGRKPSADELKIANKLFEGKLEEGSVQELLWAIVLLPEFQFIE
>NZ_LT906468.1|WP_093095297.1|1634690_1636112_-|DUF1501-domain-containing-protein
MKLNYNRRDFLRTAGVGTLAALAAGSPLSALLSSCSGKGTATADSVILLWMAGGMAHTETFDPKRYTPYEKGLDSNKVLSTFKSIPTALDGIEFSEGLESIAAMMDKGTLIRSYMAADLGHILHSRHQYHWHTCYEPPQTVAAPHIGSWIAQELGPKNPVIPAFINIGQRMTVGEAEELKAFHTAGILGSEFGPFMIPDPSSGLDSVKPPAGMSFSRFERRNQLYNELLGKNAIGDLGSDYQKESFKRSMEQAYRLLKSPEAKTFDLSEEPKETYDIYNTGKFGLGCLMARRLVEQGARFISVTSEYEPFMGWDTHENGHTRAKDMKKLIDAPIAQLLKDLERSGHLDRTLVILASEFSRDMVMEGRPGAEVLHQVDQPDIINDIKNYGMHRHFTDGSSILMFGGGVKKGFVYGKTADERPCKTIEKPIRIERIHQSIYHALGIDPQKNVVVEGRPFYTTPDGVHKAELELFI
>NZ_LT906468.1|WP_169918984.1|1633826_1634642_+|glycoside-hydrolase-family-16-protein
MKNLLHIAMLLLFSCISSTVFSQKMEKKNKKWKLVWQDEFNYEGLPDSTKWSFDTKGNAYNWGNNEAQHYTAHDTSNAYVKKGYLTITAKRQNAGGKKYTSARLRTIHKGDWKYGRFEIRAKVPTGRGTWPAIWMMPSADTYGGWPKSGEIDIMEYIGSHPDSVLGTVHTESYNHVIGTQKGKSTYLPDAHKKFHTYVLEWDANEIKIYADKKLYFTFKNEGKTAAEWPFDQKFHLLLNLAIGGGLGGQKGIDDSLFPQSYVIDYVRVYQR
>NZ_LT906468.1|WP_093095295.1|1632906_1633779_+|DNA-binding-response-regulator
MKPISVQFNTPCLIKKNSWNSTAEGSNLVDAELQKPQILLVESDKELLAYLYKELKSSYIILRAENMEEAEQILLKNNIQLVIAEILSPEMQGIQLCERIKSDPMHCHIPLIFLTEQRGYDLKIEVLRHGADVCIEKPFSLEYLLVQIENLLFNRQMIREYFSNLSIVGNRTDLEADTSDYFLEKLYTIVEEHIAEADMTVDLLAELMHMSRPTLYRKVSKFSDLKPNEIIKLVKLEKAAELIMLRQFTVSQIASMVGYSEQSNFSRDFHKHFGLRPSNFINRMGNNFAS
>NZ_LT906468.1|WP_093095292.1|1629491_1632476_-|SusC/RagA-family-TonB-linked-outer-membrane-protein
MKKTLLKKYLVTIMVILLSIPVFSQEKNITGSVKNEAGEALAGATIRVKGTSLAVTTDNLGAFNLAVPNAATALEVSFVGYQSKEVAIAGEHIDIQLQSSSDQGLDEVVVIGYGTARKKDLTGSLVTIQAKNFNKGLMTAPDQLIQGKTPGVMVINNTGQPGGSATVRIRGNSSIRASNNPLFVLDGVPMSGNSPLPAGRGGFSSDRGNPLTYLNPSDIASMDILKDASATAIYGSRGANGVVIITTKKGVAGEPVVQIGASAGVSGMRQYPDVLDAARFREALNYYTPSEAANSDFGGNEDAFKAITRQAITQNYYGDVSGGSEYGKYRLSAGYLNQNGIIRGSQLKKYTGNFTGNFNFLENKRLGLDVSLFLTQLDNRYAPINAMVGAEGNVISQAMQWNPTLPIRDENGNLTFVSTTTRNPLTSIDAFKDQSTTNTMVANLSPYYKITDDLEYRFIYSVMRQTGAREGMYRAGLIDPSASEVEQAFISNNAETNLQMTHTLSYNKQINPDWNINGLIGYEFLNYNYKNNMTFGGGFKYMGLDYFDYLQYSTVATRDISSYKSPTNELQSMFLRGGFNYKNRYLFTGTVRRDGSTKFGSNNKYAIFPSLAVAWNVNEEEFMQSNEIFDQLKLRLGWGKTGNQEFPSGASLNRFIFGNQSISQANYGNDDLRWETSSTINVGLDFAILKNRLYGSIDYFNKKTTDALFEQTLAQPSPAGLIWVNLDGEIVNKGLEVALTGTIVNTNDWTWDLTGNATFLQNSVSGLVGYYETGALRGQGFTGVLGQRMVNGQPLNVWYLAQYEGIDPDTGMSMYRGQDGSISSQNDPAINKFYSNSPNPTTLLGISTNVSYKKLTLSANMNGAFGHYLFNNTAATVLGLSNLSSRNIGEQFFDTSVKESTSNSSAPSTRFLEKGDYLKLANLSLSYSLGNIGKTFKNFNVSVTGQNLFIFTKYTGFDPEVNTDGSTNGIPSLGIEYLPYPPARNILLGVNFSL
>NZ_LT906468.1|WP_093095290.1|1627868_1629443_-|RagB/SusD-family-nutrient-uptake-outer-membrane-protein
MKLRTLLYIALAGTTFVGIHSCTKLNEEFRSEMEEGEASNINPAELLVTAYNSLNTPYQQEQRWVMQEISTDAAMAPTRGGDWDDNGMHRAIHLHTWNADNGYMNGTFVSLGTVIYNAGTVLRYNPNPQQGAEARFVRALAIFDLLDLYGVVPIREGESIEDFRIPPNVLQPQAAIDFLIKEMEEIINSLPDNGPNLAYVANKNAAKTLLMKVYLNKGTFLNRQQPTFAAEDMNKVIALAKEITSSGKYTVAAPGKYFDNFAPDNDVKSTENIFTLYNENGVRGGNVDRTWYTIAHYNLNPGGWNGWCTLSDYYDKFESIDERRGIYYNYPADTTSNRKKNYGRQNVGFFAGQQYNWTTNKPLMARNPANAPLVFTREVTIRTSGATLETAGIRPMKYAFDYAVDGQRNNDWVVYRYSDVLLMQAEAILRGGTGTAAEALTIVNSIRSNRGIAAFPSLTLENLLDERARELYWEGWRRQDLIRFGKFLDAWQEKAADPDPKTLVYPIPSQQISVNPNLVQNEGY
>NZ_LT906468.1|WP_093095288.1|1627039_1627771_+|hypothetical-protein
MKKICTKTFVLVLILAFAIQSCTQNSKQGTTQESQSDSTNAVSTDTIASTADTNPENIQLTDKKVKFLWREKKYNQEVKADVSSLVLNEDYIKTISDPERAVLGLIATFVGNECAWDGEAKEDRSNLKCKILWALDLGYQCSSKQMDFLRQWFRAEPKILEELKNCPTTPDGATIQDTFDEINLEVKGNQILVSFKANGINLRDATSWNWTEDHTYELRGDELFLINKKVSEKKQSKISVGEN
>NZ_LT906468.1|WP_093095287.1|1625782_1626811_-|L-glyceraldehyde-3-phosphate-reductase
MDWKPKSDRYDKMIYNRCGKSGLHLPAISLGLWHNFGDDTPHSRKVEICKTAFDLGINHFDLANNYGPPAGSAELAFGRILKEEFAGLRDELIISSKAGYLMWPGPYGEWGSRKYLISSCDQSLKRMGVDYVDIFYSHRFDPNTPLEETMLALDQIVRSGKALYVGISSYNTHRTKEAYDILKSLGTPFIIHQPSYSMLNRWVEEDHLLDTLEDLGLGSIVFSPLAQGMLTNKYLNEVPQDSRANQDKSLNKNFLTEENLKNIWALNEIAASRNQTLAQMAIAWVLKNGKVTSALIGASKVQQVIDCVGALDNLEFTETELKQVDQYAKDGGINIWQQSAEL
>NZ_LT906468.1|WP_093095286.1|1624726_1625635_-|NAD(P)/FAD-dependent-oxidoreductase
MELKPLYDVIIIGGSYAGLSAAMALGRSLKNTLIIDNGIPCNRQTPHSHNFITQDGEKPKVIAERAREQVAQYKSIEFLNAKAIKGKKLEGKFEIQTEEGDKIFAKKLIFATGIKDLLPEIKGFTACWGISVIHCPYCHGYEFKGKKTAIMIDNEKAFHIAQLVNNLTDNITILTSGKTYFSDVQLQKLKDHHIDIIDKEVLEIVHHLGNINAVTFTDGSQVPFDAIYASVPFIQHSQIPQELGCELNEQGYIKTDSFQMTNIEGVFACGDNTSPMRSVANAVAAGNLTGAMVNYILTEENF
>NZ_LT906468.1|WP_093095303.1|1641368_1642118_+|sulfite-exporter-TauE/SafE-family-protein
MEHWELLLIFLIIAFVYSSVGFGGGSSYLAVLAMYSLPYQEIRLTALICNVIVVVGGVIIYLRNKQVDWRKILPLTLISVPMAYLGAIMKLSQETFFMILGFTLILAAVLLWVQTDKKTNEERKDYFKPSLVQNSLLGGGIGFLSGLVGIGGGIFLSPLLNLIKWDTAKKIAATSSVFILVNSISGIAGQFSKLSVEMNFSRIGILCLSVFIGGQIGSRMSIKWNPLIVKRMTAALVFIAGINVLIKYW
>NZ_LT906468.1|WP_093095305.1|1642129_1642372_+|MoaD/ThiS-family-protein
MKITVLGFGIAKDIFGSSEIHLEVNEGLNVSDLRSVLEEGYPQLNKLKSYMLAIDEEYAEDSQIINSGNEIAVIPPVSGG
>NZ_LT906468.1|WP_093095306.1|1642373_1642790_+|molybdenum-cofactor-biosynthesis-protein-MoaE
MIEVKISADELDIVSCLAISKDLESGGIASFIGSVRNHSKGKAVVRLDFECYEAMAIKEMRKIAEAAISKYAVRNIVIQHRVGTLYPGEVAVIIVVNDGHRDSVFDACRFIIDSLKQTVPIWKKEIFENGEEWVSAHP
>NZ_LT906468.1|WP_093095308.1|1642836_1643712_+|formate-dehydrogenase-accessory-sulfurtransferase-FdhD
MNVEALKNNSIEKLEIIKVKEKSGSSFVDDVSVEEPLEIKVRYGEESEMKTKNLSVTMRTPGNDIELAAGFLFTEGIISNLGQIKTIEHAKSECSRNNENSIVVELVAGYIPDLMNVDRNFYTTSSCGVCGKGSIESIRTVSTFQSMSKKTLNIELDVLYQLSEKLRSLQDNFSSTGGIHASGIFDIEANLFGLREDVGRHNALDKLIGYFLLKDQLPLRERILVLSGRASFELVQKAAMAGIPVIAAIGAPSSLAIKLAKEFDISLLGFLGKNRFNIYHQGANLTIKNLS
>NZ_LT906468.1|WP_093095310.1|1643708_1644059_+|hypothetical-protein
MKIRIKDNSVRIRLTQSEVNSLYQDGNISSKTEFLEKSFVYAVEKAEVSELSVEYVDNKITLKIPVSMLEQLYSTDIVGFEGVTGKVKLLIEKDFVCLDNTLEDQSDNYPNPNMIC
>NZ_LT906468.1|WP_093095312.1|1644081_1646475_+|FdhF/YdeP-family-oxidoreductase
MEELDKNLIEQEIKTEPSAENPFRLLDLKLTPVEKKAAGIPAVLAVFSDLFEEKAVVRAGRALFKMNQMDGFDCPSCAWPDPDDERSVLGEYCENGAKALAEEATSKRVTPQFFKENSVADLAQLDDYQIGKMGRLTDPMFLPEGATHYQPISWDDAFKKIASHLNALESPDQAAFYTSGRTSNEASFVYQLFAKEFGTNNMPDCSNMCHETSGSALRPTIGIGKGTVTLEDFYDTDVIVIIGQNPGTNAPRMMSALAKGKKNGAKIIAINPLPEAGLMGFVDPQSVMGVLEGGVKLADLYLPVKINGDMALLKAIEMLLIDFEKKNPGSVFDEQFIENKTVGYDEFLQQFKDYDLDELAKEAAVDKDLIYEAAAMIAFKKRIIISWGMGLTQQPNGVDMIREILNILLLKGSIGIPGAGVCPVRGHSNVQGNRTMLIDEKPSNEQLDRIENFYGFQVPRKHGYDVVRAIKAMHEEKIKFMFCMGGNFLSATPDTTYTANALRKLNLLVCVSTKLNRGHLVHGKEALILPTYGRSDKDIVNGVLQIISTENSMGVVQQSKGMLDAVSDNLINETQIVCRMAMETLGNRSVVNWKRYHDSYDAVRDDIEQCIPGFDNYNVRVREKGGFYLPNEARDKQYFAKKLEGRAPFTLTEIPDNTLADDEYMMATTRTHDQFNTTIYGLDDRYRGIKNERRVIFMNQKDIDKAGLKAGDKVDLYNFDDGIERVAPLFIIVSYQIPEKNTVTYFPETNVLVSVNNVVKESNMPASKYVKIKIKPHDPAVYKKVDQMLYQGAIQRP
>NZ_LT906468.1|WP_093095314.1|1646622_1647540_+|hypothetical-protein
MIIRKKEHWFKMLFVWHGSVLPALVPRLLLLLVFSVLVAYFHGTVLDFKVPLNPAPLTLFGFVLALFLGFRNNASYDRFWEGRKLWGSLLNTSRALARQVMTLNNGEKNQEFVVGFIRLISAFVFALKHQLRGTDSKEDMEKRLDPESYELVMASKYKPVTIMRMMAEQLQGAKMEGRMDSIQQARMDENLDKLSDILGGCERIISTPLPYSYSVLLHRTVYIYCAMLPFGLVDSLGWFMPLIVVFIAYTFVAFEAIADEIEEPFGAEANDLALNSMSEMIEETIEELVGIPNTRKPKPYQEIID
>NZ_LT906468.1|WP_093095316.1|1647540_1648575_-|ThiF-family-adenylyltransferase
MDPNFERYQCQIALPGFGNKGQQLLQNAKVLIVGMGGLGCPAAQYLAASGIGTLGLVDDDLISLSNLHRQVLYGPQDIGNWKVEVAAEQLKMQNPEINIISYPIRLTSNNIMDLINEYDLILEGTDNLESKCLINDASVLAGKPLVYGAIYQYEGQVSIWNAKLPDGTYSSNYRDVFHDIENTAVPNCKEGGVIPSLAGIVGCMQANEAIKYLTGMQDILAGKLWIMDTSTGISRIIKLKKSNIQIKALQESNPTIALEEYELHPEKFVLYDVREPDEHEEFNIGGKNLPLNDLHQHLEEFATINAKVILYCMSGKRSKIAARVIKKAYPDLKVYSLKNGLLGL
>NZ_LT906468.1|WP_093095318.1|1648564_1649194_-|NTP-transferase-domain-containing-protein
MTSKDQNSVAEIYGLVLAGGKSRRMGKPKDQIHWHGKEQRYFAADLLAEYCEKVFISCREDQTQDFDPNYQALTDTFLNMGPFGGILSAFHAHRDKAWLVVACDLPLLDKDSLAKLLQNRDPDQIATTYKSPFDGHPEPLITIWEPKSYPLLLSFLANGITCPRKVLIHSDCLILDPNNPDALMNVNSPEDAEIADKTLQEQKKTIDGS
>NZ_LT906468.1|WP_093095320.1|1649171_1649648_-|cyclic-pyranopterin-monophosphate-synthase-MoaC
MTEFSHINKNQQPSIVNIMDKKVSQRHAVAKASIELPEMMMQKLTAENFNTAKGSIIHTAIIAGIMGAKKTGELIPLCHPIGLENCEVEIKFNSNSLDIYATAEVEAKTGVEMEAMTAVSIAALTIYDMCKALSHDIIIKEIKLMEKTGGKNDFKRSE

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Crispr_ID: NZ_LT906468_12

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LT906468_12

1782702-1782790

Orphan

Consensus_repeat	Method
GGGATGAGAGGATAGACCAAGATC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_LT906468_12

>merge|NZ_LT906468|12|1782702-1782790|CRISPRCasFinder
GGGATGAGAGGATAGACCAAGATCGGGGGAAGAACCAGGATTCCCCTAGGCTCCGCTCGGGGTACGGGATGAGAGGATGGACCAAGATC

>NZ_LT906468|12|12|1782702-1782790|CRISPRCasFinder
GGGATGAGAGGATAGACCAAGATC	GGGGGAAGAACCAGGATTCCCCTAGGCTCCGCTCGGGGTAC
GGGATGAGAGGATGGACCAAGATC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LT906468.1\|WP_093095527.1\|1775402_1775870_-\|response-regulator	unknown	unknown	gnl\|CDD\|381113
NZ_LT906468.1\|WP_093095532.1\|1780272_1781412_+\|NAD(P)/FAD-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|224983
NZ_LT906468.1\|WP_093095543.1\|1790429_1794332_+\|response-regulator	unknown	unknown	gnl\|CDD\|236848
NZ_LT906468.1\|WP_093095547.1\|1794693_1795761_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906468.1\|WP_093095533.1\|1781452_1782664_+\|MFS-transporter	unknown	unknown	gnl\|CDD\|225371
NZ_LT906468.1\|WP_093095549.1\|1795763_1799162_+\|sulfatase-like-hydrolase/transferase	unknown	unknown	gnl\|CDD\|293739
NZ_LT906468.1\|WP_093095523.1\|1770979_1772083_+\|ThiF-family-adenylyltransferase	unknown	unknown	gnl\|CDD\|236122
NZ_LT906468.1\|WP_093097713.1\|1775973_1777212_-\|DUF2264-domain-containing-protein	unknown	unknown	gnl\|CDD\|378358
NZ_LT906468.1\|WP_093095539.1\|1786920_1787763_-\|mechanosensitive-ion-channel-family-protein	unknown	unknown	gnl\|CDD\|223740
NZ_LT906468.1\|WP_093095524.1\|1772093_1774253_+\|sensor-histidine-kinase	unknown	unknown	gnl\|CDD\|226654
NZ_LT906468.1\|WP_093095551.1\|1799165_1800419_-\|YaiO-family-outer-membrane-beta-barrel-protein	unknown	unknown	gnl\|CDD\|275183
NZ_LT906468.1\|WP_093095542.1\|1789430_1790114_+\|TrkA-family-potassium-uptake-protein	unknown	unknown	gnl\|CDD\|223643
NZ_LT906468.1\|WP_093095529.1\|1777389_1778259_+\|helix-turn-helix-transcriptional-regulator	unknown	unknown	gnl\|CDD\|225117
NZ_LT906468.1\|WP_093095541.1\|1788041_1789427_+\|ATPase	unknown	unknown	gnl\|CDD\|273349
NZ_LT906468.1\|WP_093095538.1\|1786610_1786832_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906468.1\|WP_093095526.1\|1774302_1775391_+\|hybrid-sensor-histidine-kinase/response-regulator	unknown	unknown	gnl\|CDD\|381113
NZ_LT906468.1\|WP_093095530.1\|1778426_1779929_+\|acyl-CoA/acyl-ACP-dehydrogenase	unknown	unknown	gnl\|CDD\|224871
NZ_LT906468.1\|WP_093095536.1\|1783452_1785903_+\|ThuA-domain-containing-protein	unknown	unknown	gnl\|CDD\|377643
NZ_LT906468.1\|WP_093095545.1\|1794336_1794690_+\|response-regulator	unknown	unknown	gnl\|CDD\|381116
NZ_LT906468.1\|WP_093095522.1\|1770162_1770975_+\|hypothetical-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_LT906468.1\|WP_093095527.1\|1775402_1775870_-\|response-regulator	gnl\|CDD\|381113	cd17569, REC_HupR-like, phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar domains. This family is composed of mostly uncharacterized response regulators with similarity to the REC domains of response regulator components of two-component systems that regulates hydrogenase activity, including HupR and HoxA. HupR is part of the HupT/HupR system that controls the synthesis of the membrane-bound [NiFe]hydrogenase, HupSL, of the photosynthetic bacterium Rhodobacter capsulatus. It contains an N-terminal REC domain, a central sigma-54 interaction domain that lacks ATPase activity, and a C-terminal DNA-binding domain. Members of this family contain a REC domain and various output domains including the cyclase homology domain (CHD) and the c-di-GMP phosphodiesterase domains, HD-GYP and EAL. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.	2.17035e-58
NZ_LT906468.1\|WP_093095532.1\|1780272_1781412_+\|NAD(P)/FAD-dependent-oxidoreductase	gnl\|CDD\|224983	COG2072, TrkA, Predicted flavoprotein involved in K+ transport [Inorganic ion transport and metabolism].	7.04195e-41
NZ_LT906468.1\|WP_093095543.1\|1790429_1794332_+\|response-regulator	gnl\|CDD\|236848	PRK11107, PRK11107, hybrid sensory histidine kinase BarA; Provisional.	1.62864e-130
NZ_LT906468.1\|WP_093095533.1\|1781452_1782664_+\|MFS-transporter	gnl\|CDD\|225371	COG2814, AraJ, Arabinose efflux permease [Carbohydrate transport and metabolism].	3.45438e-51
NZ_LT906468.1\|WP_093095549.1\|1795763_1799162_+\|sulfatase-like-hydrolase/transferase	gnl\|CDD\|293739	cd16015, LTA_synthase, Lipoteichoic acid synthase like. Lipoteichoic acid (LTA) is an important cell wall polymer found in Gram-positive bacteria. It may contain long chains of ribitol or glycerol phosphate. LTA synthase catalyzes the reaction to extend the polymer by the repeated addition of glycerolphosphate (GroP) subunits to the end of the growing chain.	1.56575e-57
NZ_LT906468.1\|WP_093095523.1\|1770979_1772083_+\|ThiF-family-adenylyltransferase	gnl\|CDD\|236122	PRK07877, PRK07877, Rv1355c family protein.	4.68343e-148
NZ_LT906468.1\|WP_093097713.1\|1775973_1777212_-\|DUF2264-domain-containing-protein	gnl\|CDD\|378358	pfam10022, DUF2264, Uncharacterized protein conserved in bacteria (DUF2264). Members of this family of hypothetical bacterial proteins have no known function.	3.17127e-145
NZ_LT906468.1\|WP_093095539.1\|1786920_1787763_-\|mechanosensitive-ion-channel-family-protein	gnl\|CDD\|223740	COG0668, MscS, Small-conductance mechanosensitive channel [Cell envelope biogenesis, outer membrane].	7.03775e-56
NZ_LT906468.1\|WP_093095524.1\|1772093_1774253_+\|sensor-histidine-kinase	gnl\|CDD\|226654	COG4191, COG4191, Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal transduction mechanisms].	4.25618e-44
NZ_LT906468.1\|WP_093095551.1\|1799165_1800419_-\|YaiO-family-outer-membrane-beta-barrel-protein	gnl\|CDD\|275183	TIGR04390, hypothetical_protein, outer membrane protein, YaiO family. Members of this family share a domain of bacterial outer membrane beta barrel, up to the protein C-terminal residue (usually Phe or Trp). The member YaiO was shown experimentally to be localized to the outer membrane. [Unknown function, General].	8.19195e-55
NZ_LT906468.1\|WP_093095542.1\|1789430_1790114_+\|TrkA-family-potassium-uptake-protein	gnl\|CDD\|223643	COG0569, TrkA, K+ transport systems, NAD-binding component [Inorganic ion transport and metabolism].	4.8336e-40
NZ_LT906468.1\|WP_093095529.1\|1777389_1778259_+\|helix-turn-helix-transcriptional-regulator	gnl\|CDD\|225117	COG2207, AraC, AraC-type DNA-binding domain-containing proteins [Transcription].	2.2989e-22
NZ_LT906468.1\|WP_093095541.1\|1788041_1789427_+\|ATPase	gnl\|CDD\|273349	TIGR00933, Trk_system_potassium_uptake_protein_trkH., potassium uptake protein, TrkH family. The proteins of the Trk family are derived from Gram-negative and Gram-positive bacteria, yeast and wheat. The proteins of E. coli K12 TrkH and TrkG as well as several yeast proteins have been functionally characterized.The E. coli TrkH and TrkG proteins are complexed to two peripheral membrane proteins, TrkA, an NAD-binding protein, and TrkE, an ATP-binding protein. This complex forms the potassium uptake system. [Transport and binding proteins, Cations and iron carrying compounds].	9.18315e-71
NZ_LT906468.1\|WP_093095526.1\|1774302_1775391_+\|hybrid-sensor-histidine-kinase/response-regulator	gnl\|CDD\|381113	cd17569, REC_HupR-like, phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar domains. This family is composed of mostly uncharacterized response regulators with similarity to the REC domains of response regulator components of two-component systems that regulates hydrogenase activity, including HupR and HoxA. HupR is part of the HupT/HupR system that controls the synthesis of the membrane-bound [NiFe]hydrogenase, HupSL, of the photosynthetic bacterium Rhodobacter capsulatus. It contains an N-terminal REC domain, a central sigma-54 interaction domain that lacks ATPase activity, and a C-terminal DNA-binding domain. Members of this family contain a REC domain and various output domains including the cyclase homology domain (CHD) and the c-di-GMP phosphodiesterase domains, HD-GYP and EAL. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.	2.16279e-43
NZ_LT906468.1\|WP_093095530.1\|1778426_1779929_+\|acyl-CoA/acyl-ACP-dehydrogenase	gnl\|CDD\|224871	COG1960, CaiA, Acyl-CoA dehydrogenases [Lipid metabolism].	5.89936e-39
NZ_LT906468.1\|WP_093095536.1\|1783452_1785903_+\|ThuA-domain-containing-protein	gnl\|CDD\|377643	pfam06283, ThuA, Trehalose utilisation. This family consists of several bacterial ThuA like proteins. ThuA appears to be involved in utilisation of trehalose. The thuA and thuB genes form part of the trehalose/sucrose transport operon thuEFGKAB, which is located on the pSymB megaplasmid. The thuA and thuB genes are induced in vitro by trehalose but not by sucrose and the extent of its induction depends on the concentration of trehalose available in the medium.	9.6695e-99
NZ_LT906468.1\|WP_093095545.1\|1794336_1794690_+\|response-regulator	gnl\|CDD\|381116	cd17574, REC_OmpR, phosphoacceptor receiver (REC) domain of OmpR family response regulators. OmpR-like proteins are one of the most widespread transcriptional regulators. OmpR family members contain REC and winged helix-turn-helix (wHTH) DNA-binding output effector domain. They are involved in the control of environmental stress tolerance (such as the oxidative, osmotic and acid stress response), motility, virulence, outer membrane biogenesis and other processes. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.	5.28714e-34

>NZ_LT906468.1|WP_093095533.1|1781452_1782664_+|MFS-transporter
MTFSRYEALLVAMLTIVQFTVVLDFAVMAPLGAELIDSLNISTKQFGILVSAYALSAGASGFLLAGFIDRFDRKNILLMMYVGFIIGTVFCAIAPSYYFLLVSRIVAGVFGGVMSGITFATVTDFFRYEVRGRVMGFIQMAFSASQILGIPLGLYLAHIWSWHVPFYFIVGIGLVNIAMLLKYMQPIPSKTLEGEKSSYFQVIRRVFTNRKYLVAFSTTFFLSTGGFILQPYITPHLVFDLNYAEDQLPYVFFAAGIATLVGSPFFGKLSDSWGKYKLFVTGSLLAGICVIWFVNVPAGNLFMVAVAFSCMMLFVSSRIISATAMITAIPEASERGAFMNINSAIQQSSGGIASILGGIVLIEKEGNQGFENFQLLGWITFVSILLCILLMYRVNKIVEGKYL
>NZ_LT906468.1|WP_093095532.1|1780272_1781412_+|NAD(P)/FAD-dependent-oxidoreductase
MANQSKAGTAATTSLNGNGKLDVFYKVDIVVIGAGQAGLSAAYHLKREGIEPGKGFVVLDDEFGSGGAWQHRWDSLTLSNVNGINDLPGMGFSEAVNRDDKELRANVALPQYYEKYEKTFGLPVIRPVNVLEVTERNGRFLIHTNGLQFSARGIINATGTWKTPHCPKYPGWDKFEGRQLHTGEYKNAEEFIGKHVIIVGGGISAVQLLGELSKVTKTTWVTRRPPDFRPYEFNPELGREAVAMVDERVRMGLPPNSVVSVTGLPITPAIADMLKTGVLDRKPMFQEITAKGVKWEDGTEMEADVIFWNTGFRHSLDHLDPLGLKNEQGGITMGGSLATEVVQDPRIHLTGYGPSSSTIGANRAGRAAAKELIAYLKLK
>NZ_LT906468.1|WP_093095530.1|1778426_1779929_+|acyl-CoA/acyl-ACP-dehydrogenase
MNGVIENIDFENYISSFRKHLYHLFREEFDYSAISLKRDFPAEFLAEIMKKKPLAVAIPKLHGGRGVAVKDCLGVLSAASYESLALSLMFGINIALFLEPVAKYGNYSVQERVFKEFIENNAMGGLMITEKAYGSDALNMKTGYEQIGNSYKIKGEKHWQGLSGAADFWLVTARKFTPTGELTRDIDFFVTDNSNPEQHIPMVERYNNLGLYAIPYGINQIDVVVPEDQKLTPESTGIKLMLDMLHRSRLQFPGMGLGFIKRLLDESLQHCQNRIVSGSPLINIDSVKYQISRIQAAFAICSGMCAYSVATSGIENDLSGLSIEANTLKALITDLMQESAQISLQLAGANGYRLDHIAGRSVVDSRPFQIFEGSNEMLYAQIAEGISKMMRKAKEANLYEFLKNYPTANLSAAYFKEQLNFNLEAGINQRDMVTIGRMIARVISFQFVIQMEGFNAELVEITRQHILMDLTMFHGQYISKNSANPLVEYGLNSDWMNFVS
>NZ_LT906468.1|WP_093095529.1|1777389_1778259_+|helix-turn-helix-transcriptional-regulator
MEKNKISADEFVEKFMGGSLKHLTYIHTPIKIFPLRDIAPYLKTPIPPIFFGYNLLIYINKGYFKHQIESTSFMVQAPSVLISNYGNISAIDSVDKSAQGYCVLIKEQAMTSLFREQEILNIFTISPLLNLNKIDDVELNQLLDLLYKEIYTDKPYKEYYESIFKTVMLKIIKISDSNKTLGRRQEIAISFKQLVHLHYNKEKSVNFYADMLAVSVNYLNRCVSAVFKKSSKQLILEVAIIHSQLMLLETNKSVASIAYELEFDDPSYFTRLFKKIVGISPTEYRKTIN
>NZ_LT906468.1|WP_093097713.1|1775973_1777212_-|DUF2264-domain-containing-protein
MLGAFAMQKNMAYASDKVIDTADETNQDPTKNDRAYWVSILSKMAQPILENISKGTFQKNMPMVVSESYDSRNPKVGYLEAFGRLLAGMAPWLGLKDDDTEEGKLRKKYREQALLGIQHGFDPNSADYFDWRGKEGQTLVDAAHLALGILRAPQALWEPLPEKTKQQVIEEMKYIRWIKPGQNNWLLFASITETFLYTVGVEPNRESIDLAINKFDQDWYVGDGWYSDGSRFAFDHYNGYIIHCMLVETLKHNLKAGDYQEKYDRAYKRIQRYAHHLERMISPEGYFPIIGRSSTYRNGAFQPLAQVALDKKLPENLSYGQIRNGLTAILKNIYKHDLYDQYGWLILGFTSKEQGNIADTYTNTGSLYEATLSFLPLGLPADDEFWTAASEELTSQRAFSGKKFSKDYQVKY
>NZ_LT906468.1|WP_093095527.1|1775402_1775870_-|response-regulator
MNIENKINVLYLDDEENNLFSFKATFRFKYNVFTALTGAEALDIISKNDIQIIITDQRMPEMTGVEFLEKVIEIKPDPMRILLTGYTDMGAVVDAINKGKIFHYLNKPWSEEELTETIARAFEIYQNKKNIIDQKSKLEISNEQLEFLLRQKLLS
>NZ_LT906468.1|WP_093095526.1|1774302_1775391_+|hybrid-sensor-histidine-kinase/response-regulator
MDKNFEVLYIDDEYNNLVGFKAALRFHYDIHIASNTTDAENILMTNPNIRVIFCDQKMPGENGIDFFSRIKKEFPKPMRILITAFADMDTVIDSINRGHIFRFIKKPWEEAEIISCIEEANKFYVTNSLLDMRNMELQKAYEELDKFAYSVSHDLRDPLAGVLGAIRIALDFKSVEQVHEILNLMKTSIVKLEDYINSLRDYYLLRRGELNLSKIDFNSIFEDILDFYKMYSQNSGVEISFEVDQENTFINDKSILELILHNLVSNAIKYQKLDSLDKWVKLKAETENGHAKITVTDNGIGISESSINDIFRLFFRASDQAEGMGFGLYNVKTAVQKLKGGIEVDSAPENGSKFVVTIPSKE
>NZ_LT906468.1|WP_093095524.1|1772093_1774253_+|sensor-histidine-kinase
MSRYWLFPIMVLCCLFRFSAKASTDTVLYFNGSDVKNIGKYLSLYEENGESVSFKDVLEHPELFTKCETDVPNLGIVKKPHWIKFKIVNNSDEDRLIVDLSHPNIAEVKFYSIINSEIDSVGYNLKQGYSDRKYSHQFYLFDLQLKKGESAVCYMKLQSETQVIVPLSIHTPAGLFDFLQKEDVLSAIYIGLMLSLVLYNAFLYVATGEKHYLTYVNYIFWVFVAQMAVLGLFERVFPIRSEWLSARLLTFSGAMSGIGAILFVKSFLHTSVEAKGFNKLLNVFLLGYFFAIVLLIIGYIIPAYRIVNLVAGGGAAIVLIFAFELSRRKYSQTKFFLFAWCIFLISVLVYVLKDYGVLPTNVFTARSVQIGSVIEALLLSFALADKINTYRKEMLELQVRELAISQENEKLIREQNVILEQKVRERTEELQESNKSLSLTLSNLKDAQAQLVESEKMASLGQLTAGVAHEINNPINFVTSNVSPLRRDVNILWDIIDQVEMIALNNDLQPAEKQEKIQNIKNINDVDYLKSEINFLLKGIQEGAERTAEIVRSLRIFSRIDEDTLKRADLNECLDSTLVILNPMTKERIKILKKYHSIPMVECYAGKLNQVFMNILSNAIYAVEKKFNGKIGGEIKIETKLNDDLSKVIISIMDNGTGIPPEVIGRIFEPFFTTKDVGEGTGLGMSIAYKTIERHNGKIGLQSTVGEGTTFEIHLPIKQ
>NZ_LT906468.1|WP_093095523.1|1770979_1772083_+|ThiF-family-adenylyltransferase
MQDNHATLNNYLYKPLFFDKSNPADVIAIQELIDKQEIIFVYDQFERQLRDLFVCRNPTFSTNEEQFLEFVGLVCNQQPMEELGAWVYYPWRKTLVHILEREEFIEVRTNRNQLKISKSEQELLSTKTIGIIGLSVGQSVALTIAMERGCGKLKLADFDDLDLSNLNRLRAPIFSLGFPKVVLAAREIAEIDPYLEVEIYPEGIKEEDYQEFLIGSQKLDLLIEVCDNFEVKVESRIRAREFGIPVIMETNDRAMLDIERFDKIPDLKIFHGLVGDLTVEEIHALDKSERMGLLMKIVNAKDLSDRMKQSLPELGKSLKSWPQLASEVVLGGGISAWASRKLLLGQDLKSGRYYVDLEKILSAHPVN
>NZ_LT906468.1|WP_093095522.1|1770162_1770975_+|hypothetical-protein
MTLILKNGRPVVRLRAFRAIDDPETCLRFIKGHEHVLTSIGVKKVTSSKDEWMFNPASFVLIVESLDGENVYGGARIHVAGGTQPLPIEEATGMMDPKIFDLVWSYAQEGTGEGCGLWNSREIAGYGIGSIFLTRAAIAIAPRIGLKTLFALCAPYTINLTKAVGYRQEFGVGNNGTFYYPKLDLLATTMVLDDVLNVPTASEEDRNAILALRDMAVGPRIEVLRSKEIEIHYDLSLNDLKGWDLQKIINMANGPRSQDNGKNPDDIVIL
>NZ_LT906468.1|WP_093095536.1|1783452_1785903_+|ThuA-domain-containing-protein
MIKHCLSKISLLLILVAVLSSCQQKRSGKPRVLVFSKTAGFHHNSIEKGNAAIQKLGLENDFVVDTTSNADRFVEDSLKNYSAVVFLNTSGDVLNNYQEADFERYIQAGGGFVGIHSAADSETDWGWYGRLLGGYFGSEPELKQGKLTLVDKSHPSTKGLPDPWEITDEWYTFKKQPEGLKILMTVDKSVFPNKDEMEQAPVAWYQEYDGGRSFYTGLGHEDAEYSDPNFLKHILGGIQYAIGKNYELDYKKAKTLQVPAADQFKKVTLAEGEFFEPTEMAILPNLDILIAQRRGELLLYSKETNKVTQVGLLDVYHKTEVPNVNAEEGFMGLTADPDFAKNNYIYAYYSPKDTSVNRLSRFVFKDNKLDMASEKVVLELYSQRDICCHTGGSLAFGKDRNLFISTGDNSTPFDEPNQKYVSNGFSPKDSREGHEQYDAQRSSGNTNDLRGKVLRITVKEDGTYDIPAGNLFPKGTEKTRPEIYVMGNRNPYRVSIDKKNGFLYWGEVGPDANKDSLNRGPRGYDEVNQARKAGFFGWPYFVGNNYAYHAYNYETGEMGAAYDPKKPINDSRNNTGLRELPEAMPAFIWYPYAESPDFPQVGSGGRNAMAGPIYYTDMFPQETRYPDYYNGKLFIYDWIRGWFKAVTMLPNGDFDKMEPFMGGVKFNSPIDMEVGPDGKFYVLEYGSGWFSKNPDAGISRVDFVAASADHAANKGADGDASVAGPMGHQQGSKPKGEALIEASDCKACHALDKKSVGPSYVEIAKHYKDNKDAHSILVKKIKNGGSGVWGEVAMAAHPNMKDADLDEIVTWILSHK
>NZ_LT906468.1|WP_093095538.1|1786610_1786832_-|hypothetical-protein
MERIRGWTKIFSDGRAQSRPGTGSLLALYSTIISPKFVGAYRIRPQHGFEPGFPSTVIEAEMPLDIHRNQAQD
>NZ_LT906468.1|WP_093095539.1|1786920_1787763_-|mechanosensitive-ion-channel-family-protein
MQDANLNGIENKLEKFIDSAIAYAPVLLSSLISAALVLFLGLWLIKLFGKLLGKIFEKRDVDPSIRTFLGNLLNWVLKIMLFIVVVSQLGVQTSTFIAVIGAAGLAIGMSLQGSLSNFAGGVLILLFKPFRVGDYISSSSGVDGTVKVIDIFNTRLVTPQNQLVIIPNGELSNSNITNYSELGTRRTWFNIGVGYDTDLKAAKRLLLDTVSKNEFAFKEPAPDVVVTELGDSAINLSVRVTTSNENFWAMQEQLIIQCKEDLDKAGIEIPFPQTDIHIKK
>NZ_LT906468.1|WP_093095541.1|1788041_1789427_+|ATPase
MKNVKAFYNPAQLFTFSFIMIILTGCLLLMAPFSTQVPINFIDALFTATSAVCVTGLTTLDTGTAFTPIGHFIIILLIQIGGLGILTFTNYFAYFFKGASTYENQIATSNFSNNEKLGEVFLMLKRIIIITFSIELVGAIFIFLFTAKLMEQSFLEHLFFSVFHSISSFCNAGFSVVPDGLTNPLVIHNYAFQMVLIILIIFGGLGFPIVINILKYLKHVFNRIFKKIAYREFDYKPWVININSKINLITTLSITVFATILIFILEYDNILVTHEGIGKFVTALFTVVSPRTAGYNSIDYGSLHIYSILFIILLMWIGASPNSTGGGIKTSTFAVAVLNILSLVKGKERVEVFQREIAGITIKRAFAIMTLSLFVIGCCIVSISVFDPECTLVEIAFECFSAYSTVGLTLGITAKLSAGSKITLIILMFIGRVTMLTIMIAMFKKVKFTNYRYAKEELTIN
>NZ_LT906468.1|WP_093095542.1|1789430_1790114_+|TrkA-family-potassium-uptake-protein
MKFIIIGLGNFGASLAMKLTAQGNEVIGVDLRLERITALKEKITHTIALDAAEPSAFHSLPLKNTDVVIVAIGEDEGANIMVTALCKEAQVKRLVSRAVNALHEKVLNAIGVTEIVHPEEETAERWSKKLCLSGLVDSFELNANYSIVEAIIPQQYVGKTIQEIGFREKYEILVLTILKSAERDTLFGKSRIVTTILHGIPKPDTMLQEGEIIVIYGSNKNIKEFLK
>NZ_LT906468.1|WP_093095543.1|1790429_1794332_+|response-regulator
MSMPIVPENESERLNILYSFGLIAIGKMPELDVFAELACRITNCPSSIIAIMEKDQQRIQSCIGLDLDTVDRKNTVCQYTILSEEPLMIEDTFLDPRTANNPLIIAGQIRFYAGVPLLDERGHALGTLCVIDYHPKTLNQQQLKELQDLAKAALSVLLAKRKLNQAGYFKDILSVTQNMICVLNEDFTIKEVNPAFADLLQIPILAFSDLPFLEVLKIRDNKIASKIKSVSNSDLEVMVQTQTALSEEESVTIDWHLKHGQENKEIFAFGRNMTKENSERVKLEVSERRFRNFFENGIGLTSMHDIHGNILEVNEKGRQVLGYELEEIPNLNLRDLVPQENKSLIQPYLDRILKNGEDSGMMVLKKRTGEWIYWLYNNMLEKDQNGKKYIVSSALNLTDRIKLEKDLEHTKQILEQTNTVAQVGGWEVDVKKNEIYWSDSTRLIHGVSEDFEPNMENVFSFFDPAEREFIECKFAEAMETGHSYDFEMLMRKANAEQIWVRIKGIPEIIEGRCERVFGIIQDIDQSKKLYLDIELKEAMLQTFVKHVPAAVAMFDTDLNYLALSQQWIEEFHQGQNSEEKRNLFELFPNVPESRKQIYKRALEGVPYKNVDEVVQVEGAAENQHYNWEVRPWRISDQTIGGIIIFSQNITEQVENNEELRKAKQLADLASKAKSEFLANMSHEIRTPLNGVIGFSDLLLKTPLNDLQKQYLKYVNESGSNLLAIINDILDFSKIESGKLEFYIDQYNLYELVNQVIHVILYQAQNKDIELLLNIEQGLPTMIYIDESRVKQVLINLLGNAVKFTEKGEIELRVEETYKNEEKVGLRFTVRDTGIGIPEEKQQRIFDAFIQEDSSVSKRFGGTGLGLTISNNILNYMGSNLSLRSQVGVGSEFFFEIEVPYENPIEAEHNLAVQTALIVDDNASNRLILEHMLAYKGVETETAENGFEALQLLSIGKRFDVILMDYRMPILNGLETISKIKELYKQNVEDLPILILHTSSDDEEHIGHFRQEPNSFILTKPIISEDLYRILRKDSESNKSLNEAQVAEGNEEDKVFNKSYQVLLADDNPVNMALNNRLIENILPHCKTECVENGKLAVESCEKKHFDLILMDIQMPVMDGLEATKRIREIKKYKNVPIIGITAGNVVGERERCLQVGVNDFLTKPIKVETFKDVVYGSLLQAANKSLSKINEVKHIDFDVIEEATDSDPEFKQQFYGLIIQELQMQEMDIKQLIADRDENLLGRVLHKLKGTSGSAGLTELNHMLVELDSQFSRGIEVWEHLPKVLLEVEILQKLLIDIKE
>NZ_LT906468.1|WP_093095545.1|1794336_1794690_+|response-regulator
MVVLLAEDDELILKTIEHKLKKEGYEVILTRNGMEAIDLLNKEEIDLIISDIMMPFASGIEILSELKNLEKRIPIIMLSSMGQEETVLEAFDLGASDFMVKPFSPNELIIRVNRLLK
>NZ_LT906468.1|WP_093095547.1|1794693_1795761_+|hypothetical-protein
MEKMFTLHELTLGILTILILVFLFTLGLLIYSFRAYKLEINRKYWKNMLNEYLMQVIVEGNHKDLYIDPNLSELLKHENFRRFFLGQLIEADRKFSGVSAAVLQKVFYSYQLDQESYSLLRSYKGHLIARGIQALTIMNVREALPEIESKLQHRKMNVQHEVQYAMVYFNGFEGLSFLDSSEGILSNWQQLRILNNIKSLPKNAVEKISKWLGSNNPSVLHFALKLVRKFQIFELHDQVISLLGDDNEQIIKDAIKTLFSLDSQDTSKLLAIYYGKMQEDLQLEILKGFGQTRAFDQLDFLKSNLMENPSNRVKVSAAEALANLGEFKYLIDLSNQLAPEDPTLMVLNHALQKKS
>NZ_LT906468.1|WP_093095549.1|1795763_1799162_+|sulfatase-like-hydrolase/transferase
MAEIIYVIIVWLFLLYSIGIFSVYTWIALFSYGAVLRYKHGNIFTDYSIIASNPNAPSFSLIAPAYNEGMTVVENVRSLLSIYYHKLEIIIVNDGSKDDSMDRLIEAYQLEKVSYIIPGNIPTKEVRQVYKSKNPAFKKLIVVDKVNGGKADALNVGINISKAEYIVCIDVDCIIEQDAILRLAKPFMEQTDKRLIACGGTIRLANNCKIEKGKVVEVNLPKSWLGRSQALEYIRAFVLGRMAWSRASGLILISGAFGAFDKEIVLASGGYDPKTVGEDMELVVRMRRYMKEHKLPHQVITIPDPLCWTEVPEDKAVLKKQRNRWMRGTMETLWKHRKMMFNPRYGKMGMISLPYWFFFEFLGPLVEFSGYVIFWIFLFMGLLNWTFFFALFALVLFSSILYSIYAISVDLVSYQVYTKRKDLTKLILTAVIEPFYFHPIVTMAGIRGMVDYFKKGHTWGEMKRQGFSDQVHETFKEKAIRIAKSMFREFSSVASVFMILISVFSILEYFIYSHNIQQFSGLGSFFVLLLNNVLIGFVILVLFFVIYAILAIFNRNLSRIALHTLASLILVSQLVLAFYFAESRNLLGTDLFFYSADELKNILLASGVLNWLNVLILILGLGVLFLVFYKSSKRFKGSGKLAAVFLGLAILAFGYLTIGEEVKSSAKNEFLETAERSKLGFFMESNAKLLLEDIEEGLGMGSSTASYAQFSGEFPFMRVDQSKDLLGPLFHKSDSVPNLVIIIVEGLGEAYSNPNGYIGDFTPFLSSLKDSSLVWENNLSSSGRTFSVLPTLLGSLPFGNSGFLELKEYPDHFNLINILKQNGFSTAFFYGGNAEFDYMSKYLNANGIDRLVDEKSFPEGYKKLPSSNGESWGYEDQAVLDQLRLADQAKNNPHFHIALTLSTHNPFLINDEAKYAAMFDQRVQKIKLNNIQKNFALENRKQLISVLNVDDALKNFFQAYQQRSDFKNTIFIITGDHSMPEIPLQSKIDRYHVPLIVYSPLLKTKRRFQNVVSHFDLAPSILAYYKQNYQLKVPHEVTWVGQGLDIGASKKSLGIPMMQSKSQLIDFVSADLHLNSGAVYKLNKDLSEDRIDNKTSAEELSQRFETFKKMNRQFTSKMKLLPDSVFTSYFKR
>NZ_LT906468.1|WP_093095551.1|1799165_1800419_-|YaiO-family-outer-membrane-beta-barrel-protein
MNLKTQLLTILVFFLSFGMQELYAQESNLNADELFQAARKEAFDNKNYPAAVNLAKTALAKNPDYTDISVFLGRLYTWMDKIDSARIVFKQLEVKETKDPDFYFAFGSLEYWEDNYPEALRIVNKGMTYDAKSMDLLLLKSKIANSTKDYKTAKATLDEILEIDPKNADARTLQMAIKEQVGINEVGVTYNWMYFDKQFEDNWHNIALSYKRGTPIGSFIFRANLANKFGSNGTQFELEAYPRISKMFYMYLGTGYSNSTGLFPKFRTAASLYANLPASFEAEVGFRQLKFTDNVWMYTASIGKYYKNFWFNARTYLTPSENNISQSYAATVRYYTKGSDGYLGFIVGTGISPDQNRDFMLFDNLYKLKTFKSGLDYNFSIKSKNIFNISSTYYNVEYKPKTRDNQVDFTVGYRRRF

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Crispr_ID: NZ_LT906468_13

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LT906468_13

2279929-2280021

Orphan

Consensus_repeat	Method
TTTGGTTACTTTTGGGCTCCAAAAGTAACAT	CRISPRCasFinder

1 spacers

DEDDh

The CRISPR arrays of NZ_LT906468_13

>merge|NZ_LT906468|13|2279929-2280021|CRISPRCasFinder
TTTGGTTACTTTTGGGCTCCAAAAGTAACATTAGGATTGGTATCCCTGAGCTCCTTCGTCGGTTTGGTTACTTTTGCGCTCCAAAAGTAACAT

>NZ_LT906468|13|13|2279929-2280021|CRISPRCasFinder
TTTGGTTACTTTTGGGCTCCAAAAGTAACAT	TAGGATTGGTATCCCTGAGCTCCTTCGTCGG
TTTGGTTACTTTTGCGCTCCAAAAGTAACAT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LT906468.1\|WP_093096237.1\|2274658_2275150_-\|glutaminyl-peptide-cyclotransferase	unknown	unknown	gnl\|CDD\|368283
NZ_LT906468.1\|WP_093096236.1\|2274331_2274640_-\|glutaminyl-peptide-cyclotransferase	unknown	unknown	gnl\|CDD\|368283
NZ_LT906468.1\|WP_093096261.1\|2290023_2294445_+\|DNA-polymerase-III-subunit-alpha	DEDDh	cd06127_DEDDh_CAS-I	gnl\|CDD\|235554
NZ_LT906468.1\|WP_093096252.1\|2281636_2282350_+\|SOS-response-associated-peptidase-family-protein	unknown	unknown	gnl\|CDD\|376837
NZ_LT906468.1\|WP_157739477.1\|2275727_2275889_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906468.1\|WP_139185437.1\|2278100_2278457_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906468.1\|WP_093096257.1\|2286992_2289182_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|227662
NZ_LT906468.1\|WP_093097757.1\|2282433_2283192_+\|glycoside-hydrolase-family-16-protein	unknown	unknown	gnl\|CDD\|185693
NZ_LT906468.1\|WP_093096247.1\|2280154_2280670_-\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|366181
NZ_LT906468.1\|WP_139185435.1\|2275943_2277557_+\|fimbrillin-family-protein	unknown	unknown	gnl\|CDD\|372499
NZ_LT906468.1\|WP_139185438.1\|2283276_2284899_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906468.1\|WP_093096258.1\|2289236_2289755_+\|OmpA-family-protein	unknown	unknown	gnl\|CDD\|143586
NZ_LT906468.1\|WP_093096228.1\|2272413_2273136_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|187678
NZ_LT906468.1\|WP_093096244.1\|2278517_2278910_+\|barstar-family-protein	unknown	unknown	gnl\|CDD\|240166
NZ_LT906468.1\|WP_169918993.1\|2284933_2285080_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906468.1\|WP_093096230.1\|2273190_2273910_+\|DUF2071-domain-containing-protein	unknown	unknown	gnl\|CDD\|378271
NZ_LT906468.1\|WP_093096249.1\|2280755_2281274_-\|O-acetyl-ADP-ribose-deacetylase	unknown	unknown	gnl\|CDD\|394878
NZ_LT906468.1\|WP_139185436.1\|2277707_2278043_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906468.1\|WP_093096233.1\|2273948_2274335_+\|VOC-family-protein	unknown	unknown	gnl\|CDD\|366361
NZ_LT906468.1\|WP_093096263.1\|2294546_2294864_+\|thioredoxin	unknown	unknown	gnl\|CDD\|200072

Protein	Function_ID	Function_description	E-value
NZ_LT906468.1\|WP_093096237.1\|2274658_2275150_-\|glutaminyl-peptide-cyclotransferase	gnl\|CDD\|368283	pfam05096, Glu_cyclase_2, Glutamine cyclotransferase. This family of enzymes EC:2.3.2.5 catalyze the cyclization of free L-glutamine and N-terminal glutaminyl residues in proteins to pyroglutamate (5-oxoproline) and pyroglutamyl residues respectively. This family includes plant and bacterial enzymes and seems unrelated to the mammalian enzymes.	4.03806e-47
NZ_LT906468.1\|WP_093096233.1\|2273948_2274335_+\|VOC-family-protein	gnl\|CDD\|366361	pfam00903, Glyoxalase, Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily.	6.28732e-06
NZ_LT906468.1\|WP_093096261.1\|2290023_2294445_+\|DNA-polymerase-III-subunit-alpha	gnl\|CDD\|235554	PRK05673, dnaE, DNA polymerase III subunit alpha; Validated.	0
NZ_LT906468.1\|WP_093096236.1\|2274331_2274640_-\|glutaminyl-peptide-cyclotransferase	gnl\|CDD\|368283	pfam05096, Glu_cyclase_2, Glutamine cyclotransferase. This family of enzymes EC:2.3.2.5 catalyze the cyclization of free L-glutamine and N-terminal glutaminyl residues in proteins to pyroglutamate (5-oxoproline) and pyroglutamyl residues respectively. This family includes plant and bacterial enzymes and seems unrelated to the mammalian enzymes.	2.652e-32
NZ_LT906468.1\|WP_093096252.1\|2281636_2282350_+\|SOS-response-associated-peptidase-family-protein	gnl\|CDD\|376837	pfam02586, SRAP, SOS response associated peptidase (SRAP). The SRAP family functions as a DNA-associated autoproteolytic switch that recruits diverse repair enzymes onto DNA damage. We propose that the human protein Q96FZ2:UniProtKB, the eukaryotic member of the SRAP family, which has been recently shown to bind specifically to DNA with 5-hydroxymethylcytosine, 5-formylcytosine and 5-carboxycytosine, is a sensor for these oxidized bases generated by the TET (tetrahedral aminopeptidase of the M42 family) enzymes from methylcytosine. Hence, its autoproteolytic activity might help it act as a switch that recruits DNA repair enzymes to remove these oxidized methylcytosine species as part of the DNA demethylation pathway downstream of the TET enzymes.	1.77648e-36
NZ_LT906468.1\|WP_093096257.1\|2286992_2289182_+\|hypothetical-protein	gnl\|CDD\|227662	COG5368, COG5368, Uncharacterized protein conserved in bacteria [Function unknown].	1.90399e-24
NZ_LT906468.1\|WP_093097757.1\|2282433_2283192_+\|glycoside-hydrolase-family-16-protein	gnl\|CDD\|185693	cd08023, GH16_laminarinase_like, Laminarinase, member of the glycosyl hydrolase family 16. Laminarinase, also known as glucan endo-1,3-beta-D-glucosidase, is a glycosyl hydrolase family 16 member that hydrolyzes 1,3-beta-D-glucosidic linkages in 1,3-beta-D-glucans such as laminarins, curdlans, paramylons, and pachymans, with very limited action on mixed-link (1,3-1,4-)-beta-D-glucans.	7.573e-82
NZ_LT906468.1\|WP_093096258.1\|2289236_2289755_+\|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.	7.18235e-45
NZ_LT906468.1\|WP_139185435.1\|2275943_2277557_+\|fimbrillin-family-protein	gnl\|CDD\|372499	pfam13149, Mfa_like_1, Fimbrillin-like. A family of putative fimbrillin proteins found by clustering human gut metagenomic sequences. Analysis of structural comparisons shows this family to be part of the FimbA (CL0450) superfamily of adhesin components or fimbrillins.	1.74257e-05
NZ_LT906468.1\|WP_093096228.1\|2272413_2273136_+\|hypothetical-protein	gnl\|CDD\|187678	cd09620, CBM9_like_3, DOMON-like type 9 carbohydrate binding module. Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. CBM9 domains found in this uncharacterized heterogeneous subfamily may co-occur with various other domains.	1.15183e-09
NZ_LT906468.1\|WP_093096244.1\|2278517_2278910_+\|barstar-family-protein	gnl\|CDD\|240166	cd05143, Barstar_SaI14_like, Barstar_SaI14_like contains sequences that are similar to SaI14, an RNAase inhibitor, which are members of the Barstar family. Barstar is an intracellular inhibitor of barnase, an extracellular ribonuclease of Bacillus amyloliquefaciens. Barstar binds tightly to the barnase active site and sterically blocks it thus inhibiting its potentially lethal RNase activity inside the cell. The sequences in this subfamily are mostly uncharacterized, but believed to have a similar function and role.	1.58833e-14
NZ_LT906468.1\|WP_093096230.1\|2273190_2273910_+\|DUF2071-domain-containing-protein	gnl\|CDD\|378271	pfam09844, DUF2071, Uncharacterized conserved protein (COG2071). This conserved protein (similar to YgjF), found in various prokaryotes, has no known function.	0.000215451
NZ_LT906468.1\|WP_093096249.1\|2280755_2281274_-\|O-acetyl-ADP-ribose-deacetylase	gnl\|CDD\|394878	cd02908, Macro_OAADPr_deacetylase, macrodomain, O-acetyl-ADP-ribose (OAADPr) family. Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. This family includes eukaryotic macrodomain proteins such as human MacroD1 and MacroD2, and bacterial proteins such as Escherichia coli YmdB; these have been shown to be O-acetyl-ADP-ribose (OAADPr) deacetylases that efficiently catalyze the hydrolysis of OAADPr to produce ADP-ribose and free acetate. OAADPr is a sirtuin reaction product generated from the NAD+-dependent protein deacetylation reactions and has been implicated as a signaling molecule. By acting on mono-ADP-ribosylated substrates, OAADPr deacteylases may reverse cellular ADP-ribosylation.	8.72793e-96
NZ_LT906468.1\|WP_093096247.1\|2280154_2280670_-\|GNAT-family-N-acetyltransferase	gnl\|CDD\|366181	pfam00583, Acetyltransf_1, Acetyltransferase (GNAT) family. This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.	2.14105e-15
NZ_LT906468.1\|WP_093096263.1\|2294546_2294864_+\|thioredoxin	gnl\|CDD\|200072	TIGR01068, Thioredoxin-like_protein_slr0233, thioredoxin. Several proteins, such as protein disulfide isomerase, have two or more copies of a domain closely related to thioredoxin. This model is designed to recognize authentic thioredoxin, a small protein that should be hit exactly once by this model. Any protein that hits once with a score greater than the second (per domain) trusted cutoff may be taken as thioredoxin. [Energy metabolism, Electron transport].	8.68453e-50

>NZ_LT906468.1|WP_093096244.1|2278517_2278910_+|barstar-family-protein
MKKEIIIDGSRIHDKTSFYEEINRKFMQNESWQLAESLDAFDDLLYGGFGAIREKEEIRLIWECFEANRLSLGTEFTINYYQEKLAHPEDFDSSVIHKRLNELKAGKGQTYFEILEEIISEHSNIELIKK
>NZ_LT906468.1|WP_139185437.1|2278100_2278457_+|hypothetical-protein
MKNVIILLILFVGMSSCGKDEIVEDRTKASACLLKMRDYLAKELYCKEDAKTPYSSNLVRASYEGKIVYYSQISCAECLVVAAETGYTCDLEKINFEDPRKILDRKFVFDSCSKQYSE
>NZ_LT906468.1|WP_139185436.1|2277707_2278043_+|hypothetical-protein
MKRIMFLALAIILFTACEKDDVDVSTCAKKLKSHFNKELRCSEKGANETNLFKGTYKGETVYFANTICIYCLTAPPEYGYTCDLKKIDFENFNDVKDISEVYNSCSKKYTE
>NZ_LT906468.1|WP_139185435.1|2275943_2277557_+|fimbrillin-family-protein
MKFSIGFLAVLMLSFGSCKRSDDPVGGNGEAKLNVQIDGVSFEEDNIDFDKKSSTNGSVASGIVKDTSLVYDDFVVDVKMTQDNDRSNRTVSNHTVYRGSDANMAAAVTKTTELTKGTKYRLVAFNADGSFNQAKDYTYGNEGATSGMSLDAGKKYTFVAYSINSANDPLPDLVYTNSVTTFANAKLVDVSKDLMVFVLKDKQLTYGDNKLGVILKHRFSMITTRLTMDSKMTGSIKTLANTTIGKVDASATFNFNGETITYKNNQSTFAAINFPTLGTGLRDVTSYPTLLINPAATNKTLNFGTITIDDETKTNFSIANIRVNPGCKYNLNLNFRTCTQEVKLADDALNWRYPETGDRKGCYDPKTGEIWKNGTLLTKTLSAPASNYGFTFDITELDNAVNMEVNGVKILTDPKEGQIQFQTYDNTANGEGIITRNIKFADGTEYGTGNIGNIWTLKGSAATPLIRIIISKTGEVTMLGSKTSNGPLVQLVKKGSLKFNNVPWKTSGVNTIKVTQKVSNTTFVVGRGYGQAKIACK
>NZ_LT906468.1|WP_157739477.1|2275727_2275889_+|hypothetical-protein
MKKQYKTPRVHLVKVQMEVDIALGSAKVYPQNGNNVVEDQWTQEEDDNRNIDW
>NZ_LT906468.1|WP_093096237.1|2274658_2275150_-|glutaminyl-peptide-cyclotransferase
MKTYIISLSLFSLILIFSCQQESKSTTNQSNSENPIPEPTPLTFQIIKTLAHDTSAFTQGFIFDKGQLIEGTGLEKHTRINKIDTSSAKVEVLKSNYDNDIFGEGITILNNKLYQLTYLNNKIFTFDLDNLKQPIATHTWQNEGWGLTHDSTSLILSDGSSTL
>NZ_LT906468.1|WP_093096236.1|2274331_2274640_-|glutaminyl-peptide-cyclotransferase
MAIVKELKVQDNLGFVDSLNELEYVDGFIYANQWGSDFIYKIDPETGYVVGKLSFEGIIELYDKSFQPDHEKVLNGIAWDPENKFMFVTGKNWPLIFKIRVN
>NZ_LT906468.1|WP_093096233.1|2273948_2274335_+|VOC-family-protein
MKLDPIIAVQDVQKSAAWYKDLFNLHNNHGGEHFAVLQNSTGETILCLHQWGEHHHPSMVNPNLAHGNGLILYFKTNDYQAIYERAIELDIPMVEELHKNLNSQKMEFSFYDHDGYYISITEDHNYEG
>NZ_LT906468.1|WP_093096230.1|2273190_2273910_+|DUF2071-domain-containing-protein
MKIPKIHGVIERRILANYTADPEVLSKLLPAPFRPKLYKGKAIVGICLIRLKSIKPKDFPNFIGVSSENAAHRFAVEWTDESGQICEGVYIPRRDTNLYLNTLVGGRAFPGKHHFAKFNIHESNGNYHLDARSSDQNHIQIDARSTSTLTSASIFDNLQEVSQFFEKGSIGYSPNGKSFDGLKLNTYNWEVSPLEVLNIKSTYFDDKNRFPEGSIQFDHAVLMLNIEHEWQSLKSISCL
>NZ_LT906468.1|WP_093096228.1|2272413_2273136_+|hypothetical-protein
MLINPKPFLFTFILLIGLFSHPKFTIAQSTDTPIIPINKGLSITIDGNLSDWNNQNNLFSVNQFISPWGNQNFGKTIFKAFHDGSYFYFYFDIMDKNIIEKKFEKEADVGGGDRGEIFLSADTGLSEYYCFEISASAKVLDYRASHYRKFDYGWDLESLEVKSKIKTDGYILEGRIPMAFIKGLMASNSEQSLYLGLFRGEFDSMEWDEKTINWISWIRPTSEKPDFHITSAFKKVQFGQ
>NZ_LT906468.1|WP_093096247.1|2280154_2280670_-|GNAT-family-N-acetyltransferase
MIEIKVASIDDLLIIQKIGRETFLETFESRNSESDMSTYINDRFSENQVHHELKNLESIFYIAWDQGHPVGYLKLNIGQAQTEFKLEDHIEIERIYVYASHHGKQVGQLLFFKALETAKSLRVPTIWLGVWEENARAISFYKKNGFEEFDKHIFQLGSDEQTDILMRRAVG
>NZ_LT906468.1|WP_093096249.1|2280755_2281274_-|O-acetyl-ADP-ribose-deacetylase
MRDKINLELGDITKCQEDAIVNAANTSLLGGGGVDGAIHRAAGPTLVEECQKIRNRQGGCKTGEAVITHAGNLPCKFVIHAVGPVWKDGNHKEDELLYNAYHNSLVLASANNLKSIAFPNISTGIYGFPKERAAKNAIQAVKDYLSEDESIAEVKFICFDEENYNIYKKLLD
>NZ_LT906468.1|WP_093096252.1|2281636_2282350_+|SOS-response-associated-peptidase-family-protein
MCYHVGSPSKSELKNKLPKKKIYYPNENEIFHISGFTRPYLPVTLNKDSDSVIEARWKLIPGWVKNETEAGKYANTLNAEAESIFEKASYKNYILNNRGLLYVTGFYEPHKVVGKKESENYFIYAPKREIISLGILYSYFTDQETGETYPTFSVITTAANELLEEVHNEKKRMPLVIPEDSRDAWLFAQGKDEIKQLMIPYPMELNAHQVYRVTGDRTGNTNRPDIQKPWSGQTSLF
>NZ_LT906468.1|WP_093097757.1|2282433_2283192_+|glycoside-hydrolase-family-16-protein
MKDKPYVHIQKEDRAQKKWKLVWEDNFEGTAIDSTKWSRIPKGESDWNRHMSTSDAVFRMEDGKLVLLGINNPDQSSDPRPFITGGIWSKNKFAFQYGRIEIRAKLGSAQGAWPAMWMLAELDKYGKYPMNGEIDIMEHLNYDKIIYQTTHSHYTLNLGQQDNPPHSGTTAIEPSEFNVFGISWYPDKIVFQLNGKDTFTYPRIEGVDPTQWPYDQPFFILIDQQLGGNWVGKVDQSQLPVAMEIDWVRVYQ
>NZ_LT906468.1|WP_139185438.1|2283276_2284899_-|hypothetical-protein
MEFTLLNKMARLKSMFFIAILLLSFQSCKKSDSDSVSGELTTVKVKLSVGSPEEERIAYGSNKSTTKVKESNVQLSNVQISDNMSMEVMVIRDVEPSAIRGTSGSNNAAKAATQTVTNTLTPGVKYRIMVYDNGGAHKGNYDYIYGSEPTTGGIQLNAGETYTFVVYSVNSTSDLPDASNQGSLSTASLSNISSDLMFFKKTLTLNHGDNNLNAILVHKFSQITTTIEMDDSMTGSIEAISNTRFSPTKASGSLKFSDESLSFPNANGQTNVTFPAITPGLRTITSNPTFLISKSVTDAIFTFGSITLDSETKTGIEVKNVKITPGHKYSLVLRFRACTQNVTSDALNWRYAEATWKTWDFWNGWTTHIGIIKDNERIKNNEIITNSFSAPQANYGFQFDITELDNALNMRVNNQYIFGTSFSDQIQFQTNTKLGTQRNIVFEDGTEYATNGINEVFHLKGTLEKPLIRIMISRTGEVTMLGSKTNEGPLVPLRLKGGKQFNKVNWSATGPNTVVVSQKVDGRTIVIGKGYGRKRINCPN
>NZ_LT906468.1|WP_169918993.1|2284933_2285080_-|hypothetical-protein
MSPKIEILDIHLEEGIASGSAFVRPHNNENEMMDQWYQDDQETRNIDW
>NZ_LT906468.1|WP_093096257.1|2286992_2289182_+|hypothetical-protein
MQLRLFTILFFCFLAFNGKAESYPEVVFDNSLVKGTYARSIVNYSGDSWVENIQKNLLVSDTLFFTPGNALSLKYISAEMGDWDVLIKYSRQKFHYRVSFDDILSLKIFVGSAGTKPENLPSISIQQGMNQSVSIPLGDYIEDYNNSSWMSVKIPLKEFAGLNIDHNISGIILRQHHASEVTNQLFLDQIEFLPTKYSEAPLTSNAVLSKVTAYGKHVDLQWQVPLTPSIRYVKIYRSLDNKEFKAVAIRPTYMLRSLDYIPVLDKKYYYKIAWVDYNYRESPFSEVLEVEPKQLNEDQLLDLIQLANVNYFVENYDINSGMYMPYRMKDKAVVSVRETGGAMLSMLVGVEKGFVSKALFLSRVKRIVGFLGKAQNNKGFFPAYFDGRKGLPLYLDDIPRYDVQATSSLIEALLVIRQYLNTDAAEENKLRADITQLWERLDWRGVTLPNDPLVLRSAIDMLDEYFTFDPLVGINGGLNAYMLAIASTKSSLAPEAFTNALKYKFERPRGRNSIRRMNTEQESNVADSVNLMMHDEKVLVSVPGQDSIYKVASTHDTLMYGIKLPFGNYTTSLLDMYRPFNTINPNLSKVGDYDLKSVLQKYTQVAKRRDNEIGVGTSNSDIWGFYQYRDSIGTFRINPAIAISSMFLDESRSKRSLYAMYNQFGEYLFTEYGFRAWMDLRTDDVSDEYIANNQSNLAILLENARTGLIWNLYQAIPEIRSAEQRIFKK
>NZ_LT906468.1|WP_093096258.1|2289236_2289755_+|OmpA-family-protein
MKRINYLTLIFLAGLTLFSCKQQALVVNPGAVVSQDGTNDGLKNVKREFEDAKQTNEGILVSISSDLLFPTNSSYLTDGAKTELSKLVKVLKTSNANSKIRVDGHTDATGTAEYNVWLSDKRAASVEKFLVDAGISDARISTKGLGQTKPIADNKTPEGRQKNRRVEVVILK
>NZ_LT906468.1|WP_093096261.1|2290023_2294445_+|DNA-polymerase-III-subunit-alpha
MYIIFDTETTGLPKRWDAPITDTDNWPRCIQIAWQLHDEMGRLVEHQDYLIKPDGFNIPYDSEKIHGISTELAESEGIPLTDVLVKFNEALGKAKFVVGQNIGFDINIMGCEFYRYQVDSPMASMPILDTCTEVTADLLKLPGGRGGRYKLPNLTELHSYLFGVPFAEAHNATADVEATTRCFFELIRKEVFTPNELQVDTGYFVEFKKENPTVVESVGLKHVNLKAASDAIRQEESMGVKKVVIDPETLAKFEAAEFAHLHNHTQFSVLQSTISIDNLIQAAAKHKMSAVAMTDHGNMMGAFHFVSKTLGHNKDVEAKIKEAEENGETYDGRIIKPIVGCEFYVCENRKDKSRKDNGYQVVFLAKNKQGYHNMAKMASVAYTEGFYYVPRIDKETVERYKEDLIVLSGNLNGEVPSKVLNIGEAQAEEALIWWKEQFGEDFYIELMRHGQEDENRVNDTLVQLAEKHQVKVIGTNNTYYVNKADAHAHDILLCVKDGEKLSTPKGRGRGFRFGLPNQEYYFKSADEMKQVFKDTPQAIINIQEVLDKIEIYSLNRDVLLPKFEIPEQFQSEEDLVDGGKRGENAFLKHLTYIGAEKRYPEITDSIRERLDFELATIEKTGYPGYFLIVQDFIAAAREMGVSVGPGRGSAAGSAVAYCLGITNIDPILYDLLFERFLNPDRVSMPDIDIDFDDEGRGRVMQYVIDKYGASQVAQIITYGTMAAKSSIKDTARVLDLPLSDANEIAKLIPNLKLSKIFNLEDKALKEVLRSEELEAVNKLKSLADGAGIEAETIKQARVLEGSMRNTGIHACGVIITPDDITNFVPVSLAKDSDLYVTQFDNSVVESAGLLKMDFLGLKTLTLIKDTVINVKLSHDIDLDPDNFPIDDVKTYELFQRGETIGIFQYESPGMQKYMKELKPTVFADLIAMNALYRPGPMEYIPSFVKRKHGIEPITYDLDACEEYLSETYGITVYQEQVMLLSQKLAGFSKGDADVLRKAMGKKQKAVLDKMKPKFVSQAEANGHSAKVLEKIWTDWEAFASYAFNKSHSTCYAWVAYQTAYLKAHYPAEYMAAVLSNNMNDIKQVTFFMEECRRMGLTVLGPDVNESHYKFTVNDEGAIRFGIGAVKGVGAGAVETIVNSRADGPYKSIFDLAKRVDLRMINKKAFESLAYAGGFDSFSDTHRAQYFFSDTDSSSGIEKAIKFAHKFKENENSAQVSLFGAGGAVELPEPTLNPCPAWGLIEKLKYEKDVIGIYLTSHPLDNYKFEMRHFCPNNVTDLQMINKVKAAEVEQELLLEFNRIKNKEVVLGGIVAMANHRVAKSGKPFGSFIIEDYSDSFEIMVFGEDYVKFKGYLQEGYFVQIRGLVQERFKQVGNWGFELKGIQLLSDLREKMAKSFTIQFPLHILNQEFVKTLEELVSYTQLEGQEANCQLKFMIMDLQDELSIEMPVKRKKIFITNEFLDGLEALESVRYKLN
>NZ_LT906468.1|WP_093096263.1|2294546_2294864_+|thioredoxin
MALEITDGNFDEVVLKSDKPVLIDFWAEWCGPCRMVGPLVDEIATEYEGKAVVGKVNVDNNPDISVRYGIRNIPALLFFKNGEIVDKQIGAVPKSVLTDKLEKQL

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Crispr_ID: NZ_LT906468_14

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LT906468_14

2376621-2376744

Orphan

Consensus_repeat	Method
CGCATTTCTCCGAGATGTTTCGTGCCTCAACATGACAGG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_LT906468_14

>merge|NZ_LT906468|14|2376621-2376744|CRISPRCasFinder
CGCATTTCTCCGAGATGTTTCGTGCCTCAACATGACAGGTAGGAAGCAGATTGAAGAGCTGTACGCCATTGCAATGCTAAAAAAGCGCATTTCTCCGAGATGTTTCGTTCCTCAACATGACAGG

>NZ_LT906468|14|14|2376621-2376744|CRISPRCasFinder
CGCATTTCTCCGAGATGTTTCGTGCCTCAACATGACAGG	TAGGAAGCAGATTGAAGAGCTGTACGCCATTGCAATGCTAAAAAAG
CGCATTTCTCCGAGATGTTTCGTTCCTCAACATGACAGG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LT906468.1\|WP_093096412.1\|2376873_2377758_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|226304
NZ_LT906468.1\|WP_093096428.1\|2385894_2386545_+\|ligase-associated-DNA-damage-response-endonuclease-PdeM	unknown	unknown	gnl\|CDD\|274996
NZ_LT906468.1\|WP_093096407.1\|2372473_2373352_-\|FtsX-like-permease-family-protein	unknown	unknown	gnl\|CDD\|225088
NZ_LT906468.1\|WP_093096409.1\|2373523_2376307_+\|leucine--tRNA-ligase	unknown	unknown	gnl\|CDD\|178177
NZ_LT906468.1\|WP_093096402.1\|2371371_2372190_-\|undecaprenyl-diphosphate-phosphatase	unknown	unknown	gnl\|CDD\|234712
NZ_LT906468.1\|WP_093096394.1\|2368043_2368541_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|238207
NZ_LT906468.1\|WP_093096425.1\|2383457_2385902_+\|ligase-associated-DNA-damage-response-DEXH-box-helicase	unknown	unknown	gnl\|CDD\|274994
NZ_LT906468.1\|WP_093096424.1\|2382816_2383374_-\|NAD(P)H-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|223508
NZ_LT906468.1\|WP_093096421.1\|2382104_2382743_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|374294
NZ_LT906468.1\|WP_093096396.1\|2368590_2369310_+\|bacillithiol-biosynthesis-deacetylase-BshB1	unknown	unknown	gnl\|CDD\|274915
NZ_LT906468.1\|WP_093096390.1\|2365044_2367249_-\|bifunctional-(p)ppGpp-synthetase/guanosine-3',5'-bis(diphosphate)-3'-pyrophosphohydrolase	unknown	unknown	gnl\|CDD\|223394
NZ_LT906468.1\|WP_093096417.1\|2378751_2379048_+\|thioredoxin	unknown	unknown	gnl\|CDD\|239245
NZ_LT906468.1\|WP_093096391.1\|2367389_2368031_+\|DUF4294-domain-containing-protein	unknown	unknown	gnl\|CDD\|379485
NZ_LT906468.1\|WP_093096399.1\|2370453_2371176_-\|tRNA-pseudouridine(55)-synthase-TruB	unknown	unknown	gnl\|CDD\|211339
NZ_LT906468.1\|WP_093096415.1\|2377807_2378653_+\|glycoside-hydrolase-family-25-protein	unknown	unknown	gnl\|CDD\|119384
NZ_LT906468.1\|WP_093096398.1\|2369446_2370427_-\|bifunctional-riboflavin-kinase/FAD-synthetase	unknown	unknown	gnl\|CDD\|235536
NZ_LT906468.1\|WP_093097768.1\|2380987_2382103_+\|phosphotransferase	unknown	unknown	gnl\|CDD\|366736
NZ_LT906468.1\|WP_093096431.1\|2386650_2387814_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|350122
NZ_LT906468.1\|WP_093096404.1\|2372189_2372444_-\|DUF3098-domain-containing-protein	unknown	unknown	gnl\|CDD\|378629
NZ_LT906468.1\|WP_093096420.1\|2379446_2380766_-\|HlyC/CorC-family-transporter	unknown	unknown	gnl\|CDD\|224173

Protein	Function_ID	Function_description	E-value
NZ_LT906468.1\|WP_093096412.1\|2376873_2377758_-\|hypothetical-protein	gnl\|CDD\|226304	COG3781, COG3781, Predicted membrane protein [Function unknown].	1.34948e-55
NZ_LT906468.1\|WP_093096428.1\|2385894_2386545_+\|ligase-associated-DNA-damage-response-endonuclease-PdeM	gnl\|CDD\|274996	TIGR04123, hypothetical_protein, metallophosphoesterase, DNA ligase-associated. Members of this protein family are an uncharacterized putative metallophosphoesterase associated with a DNA ligase, a helicase, and a putative exonuclease. It may play a role in DNA repair. Its system is present in about 12 % of prokaryotic reference genomes.	5.43265e-67
NZ_LT906468.1\|WP_093096407.1\|2372473_2373352_-\|FtsX-like-permease-family-protein	gnl\|CDD\|225088	COG2177, FtsX, Cell division protein [Cell division and chromosome partitioning].	5.6283e-35
NZ_LT906468.1\|WP_093096409.1\|2373523_2376307_+\|leucine--tRNA-ligase	gnl\|CDD\|178177	PLN02563, PLN02563, aminoacyl-tRNA ligase.	0
NZ_LT906468.1\|WP_093096402.1\|2371371_2372190_-\|undecaprenyl-diphosphate-phosphatase	gnl\|CDD\|234712	PRK00281, PRK00281, undecaprenyl-diphosphate phosphatase.	4.56377e-84
NZ_LT906468.1\|WP_093096394.1\|2368043_2368541_+\|hypothetical-protein	gnl\|CDD\|238207	cd00340, GSH_Peroxidase, Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a variety of hydroperoxides including lipid peroxidases, using GSH as a specific electron donor substrate. GSH peroxidase contains one selenocysteine residue per subunit, which is involved in catalysis. Different isoenzymes are known in mammals,which are involved in protection against reactive oxygen species, redox regulation of many metabolic processes, peroxinitrite scavenging, and modulation of inflammatory processes.	3.61007e-59
NZ_LT906468.1\|WP_093096425.1\|2383457_2385902_+\|ligase-associated-DNA-damage-response-DEXH-box-helicase	gnl\|CDD\|274994	TIGR04121, ATP-dependent_helicase, DEXH box helicase, DNA ligase-associated. Members of this protein family are DEAD/DEAH box helicases found associated with a bacterial ATP-dependent DNA ligase, part of a four-gene system that occurs in about 12 % of prokaryotic reference genomes. The actual motif in this family is DE[VILW]H.	0
NZ_LT906468.1\|WP_093096424.1\|2382816_2383374_-\|NAD(P)H-dependent-oxidoreductase	gnl\|CDD\|223508	COG0431, COG0431, Predicted flavoprotein [General function prediction only].	4.41098e-41
NZ_LT906468.1\|WP_093096421.1\|2382104_2382743_+\|hypothetical-protein	gnl\|CDD\|374294	pfam16011, CBM9_2, Carbohydrate-binding family 9. CBM9_2 is a family of putative endoxylanase-like proteins that belong to the Carbohydrate-binding family 9.	1.95706e-63
NZ_LT906468.1\|WP_093096396.1\|2368590_2369310_+\|bacillithiol-biosynthesis-deacetylase-BshB1	gnl\|CDD\|274915	TIGR04001, thiol_BshB1, bacillithiol biosynthesis deacetylase BshB1. Members of this protein family are BshB1 (YpjG), an enzyme of bacillithiol biosynthesis; either BshB1 or BshB2 (YojG) must be present, and often both are present. Bacillithiol is a low-molecular-weight thiol, an analog of glutathione and mycothiol, and is found largely in the Firmicutes. [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs].	1.21874e-104
NZ_LT906468.1\|WP_093096390.1\|2365044_2367249_-\|bifunctional-(p)ppGpp-synthetase/guanosine-3',5'-bis(diphosphate)-3'-pyrophosphohydrolase	gnl\|CDD\|223394	COG0317, SpoT, Guanosine polyphosphate pyrophosphohydrolases/synthetases [Signal transduction mechanisms / Transcription].	0
NZ_LT906468.1\|WP_093096417.1\|2378751_2379048_+\|thioredoxin	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.	2.29382e-36
NZ_LT906468.1\|WP_093096391.1\|2367389_2368031_+\|DUF4294-domain-containing-protein	gnl\|CDD\|379485	pfam14127, DUF4294, Domain of unknown function (DUF4294). This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 192 and 226 amino acids in length.	5.27555e-63
NZ_LT906468.1\|WP_093096399.1\|2370453_2371176_-\|tRNA-pseudouridine(55)-synthase-TruB	gnl\|CDD\|211339	cd02573, PseudoU_synth_EcTruB, Pseudouridine synthase, Escherichia coli TruB like. This group consists of bacterial pseudouridine synthases similar to E. coli TruB and Mycobacterium tuberculosis TruB. Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi). E. coli TruB and M. tuberculosis TruB make psi55 in the T loop of tRNAs. Psi55 is nearly universally conserved. E. coli TruB is not inhibited by RNA containing 5-fluorouridine.	6.99603e-97
NZ_LT906468.1\|WP_093096415.1\|2377807_2378653_+\|glycoside-hydrolase-family-25-protein	gnl\|CDD\|119384	cd06524, GH25_YegX-like, YegX is an uncharacterized bacterial protein with a glycosyl hydrolase family 25 (GH25) catalytic domain that is similar in sequence to the CH-type (Chalaropsis-type) lysozymes of the GH25 family of endolysins.	3.76001e-75
NZ_LT906468.1\|WP_093096398.1\|2369446_2370427_-\|bifunctional-riboflavin-kinase/FAD-synthetase	gnl\|CDD\|235536	PRK05627, PRK05627, bifunctional riboflavin kinase/FAD synthetase.	6.93332e-120
NZ_LT906468.1\|WP_093097768.1\|2380987_2382103_+\|phosphotransferase	gnl\|CDD\|366736	pfam01636, APH, Phosphotransferase enzyme family. This family consists of bacterial antibiotic resistance proteins, which confer resistance to various aminoglycosides they include: aminoglycoside 3'-phosphotransferase or kanamycin kinase / neomycin-kanamycin phosphotransferase and streptomycin 3''-kinase or streptomycin 3''-phosphotransferase. The aminoglycoside phosphotransferases inactivate aminoglycoside antibiotics via phosphorylation. This family also includes homoserine kinase. This family is related to fructosamine kinase pfam03881.	4.10554e-17
NZ_LT906468.1\|WP_093096431.1\|2386650_2387814_+\|hypothetical-protein	gnl\|CDD\|350122	cd18610, GH130_BT3780-like, Glycosyl hydrolase family 130, such as beta-mammosidase BT3780 and BACOVA_03624. This subfamily contains glycosyl hydrolase family 130, as classified by the carbohydrate-active enzymes database (CAZY), and includes Bacteroides enzymes, BT3780 and BACOVA_03624. Members of this family possess 5-bladed beta-propeller domains similar to families 32, 43, 62, 68, 117 (GH32, GH43, GH62, GH68, GH117). GH130 enzymes are involved in the bacterial utilization of mannans or N-linked glycans. GH130 enzymes have also been shown to target beta-1,2- and beta-1,4-mannosidic linkages where these phosphorylases mediate bond cleavage by a single displacement reaction in which phosphate functions as the catalytic nucleophile. However, some lack the conserved basic residues that bind the phosphate nucleophile, as observed for the Bacteroides enzymes, BT3780 and BACOVA_03624, which are indeed beta-mannosidases that hydrolyze beta-1,2-mannosidic linkages through an inverting mechanism.	3.9339e-162
NZ_LT906468.1\|WP_093096404.1\|2372189_2372444_-\|DUF3098-domain-containing-protein	gnl\|CDD\|378629	pfam11297, DUF3098, Protein of unknown function (DUF3098). This bacterial family of proteins has no known function.	7.68013e-17
NZ_LT906468.1\|WP_093096420.1\|2379446_2380766_-\|HlyC/CorC-family-transporter	gnl\|CDD\|224173	COG1253, TlyC, Hemolysins and related proteins containing CBS domains [General function prediction only].	1.96861e-117

>NZ_LT906468.1|WP_093096409.1|2373523_2376307_+|leucine--tRNA-ligase
MEYNHQSIEQKWQKFWADNQTFKTSESTEKPKYYVLDMFPYPSGAGLHVGHPLGYIASDIFSRYKRLKGFNVLHPMGYDSFGLPAEQYAIQTGQHPAITTEANINRYREQLDNIGFSYDWSREVRTSEPDYYRWTQWIFMQLFDAWYNKESDKAESIAALIQNFETSGSEGIKAESDEDVLTFTADEWKAFSETEKQTELLKYRLAFLRESTVNWCPALGTVLANDEVINGLSERGGFPVEQKKMMQWSMRITAYADRLLRGLDTIDWPEPLVEMQRNWIGKSVGASVKFPVPQLNDNIEVFTTRVDTIFGVSFVVLAPEHELVSALTTDAQKAEIESYIDKTSKKSELDRLADTKTVSGAFTGSYAKHPLTGEDVQIWIADYVLAGYGTGAVMAVPSGDQRDYLFAKHFNLPIIPISDSQDISEAADPNKDGKYINSDFINGMSYQEAVPALIEKLEAIKLGKAKINFRMRDAIFGRQRYWGEPVPVYFKDGLPYLIKEEELPLLLPEVDKYLPTETGEPPLGRAEGWKYQDQYEYELSTMPGWAGSSWYWFRYMDPKNEKDFASKEAVDYWKAVDLYIGGSEHATGHLLYSRFWNKFLKDIGYHNEEEPFKKLINQGMIQGRSNFVYRVLDAEGKGTNQFVSLGLKDQYTVNPLHVDVNIVHNDVLDLEKFKQSRPDYNDAEFILENGKYICGTEVEKMSKSKFNVVNPDDIIEQYGADTLRLYEMFLGPLEQAKPWNTNGIEGVYKFLRKVWRLFHDAEGNFQVSDEEPSKAEYKALHKIIKKVEEDIERFSFNTSVSAFMICVNELTDLKTNKRKILQDLLIVLEPYAPHITEELWSKLGNEAGTISYADYPVFKPEYLVESEFAYPVSINGKMKMNLPLALDLDQQAVEGILKENADVQKLLDGKAVKKVIFVKGKIINIVV
>NZ_LT906468.1|WP_093096407.1|2372473_2373352_-|FtsX-like-permease-family-protein
MSVIEQGSPRKKTKSVYVSTVISIALVLLMTGLLGLILVHAKNLSRYVKENIVLNVIVNDNVNEGDVLSLQKDLEKDPYVLRSEYVSKELAAKNLREDLGEDFVEYLGRNPLLPSIDVYMKEQYANSDSIQTFINKIGKNSRIKEVVYQESLIDMVNKNIRVISIVILAFTVILLIIAVALINNTIRLAIYSQRFLIKSMQLIGATKGFIRKPYILYGIAHGLIGALIAILLLILTLQFAQKQVPELVFLRDWFEFAMIFAIVLGLGILISGASTYFAVTKYLRAKSASLYR
>NZ_LT906468.1|WP_093096404.1|2372189_2372444_-|DUF3098-domain-containing-protein
MSQTKNVKGTPANASNAGFVFKKINYQLFILSIVVVAIGFILMMGTEDIYSFTKITLAPIVVVAGFALGFVAILYKPKTKTTQE
>NZ_LT906468.1|WP_093096402.1|2371371_2372190_-|undecaprenyl-diphosphate-phosphatase
MSYLEAIILAIVEGLTEYLPISSTAHMGFTAALMGMEESEYLKMFQVSIQFGAILSIVVLYWRRFFDFKNLKFYYKLAIAVIPALVLGKLLDDKIEAVLGNQIAISTVLVLGGVVLLFVDKWFKNPKITDEKEIPVKKAFIIGFWQCLAMMPGTSRSAASIIGGLTQGLDRKAAAEFSFFLAVPTMLAVTVYSIFVKTWAEGTEHAQKGYEMIMASNENIMIFIIGNVVAFIVAMIAVKTFISVLTKYGFKFWGWYRIVIGIALLVFFYTQG
>NZ_LT906468.1|WP_093096399.1|2370453_2371176_-|tRNA-pseudouridine(55)-synthase-TruB
MSENIEGQAKPKFAFAEGEVLLIDKPLTWTSFDVVGKLRNSIKPLKVKVGHAGTLDPLATGLLIVCTGKMTKQIDGFQAEDKEYTGTITLGATTPSYDLETEIDQTFDYSFLTDEDILNTAASFVGVQDQFPPAHSAIKIGGERVYEKARRGEEVELKARRVEIMEFDVEKIELPKVYFRIKCSKGTYIRSIAHDFGKKLNCGGHLSSLRRTKSGDFDVKNAWELTELINQVKELKNQTV
>NZ_LT906468.1|WP_093096398.1|2369446_2370427_-|bifunctional-riboflavin-kinase/FAD-synthetase
MKIYRNLDEFKALDYAIVTIGTFDGVHVGHQKILNKLTELAKDNTGETVLLTFFPHPRLIINPDDDSLRLINDIEEKVERLALAGIDHLIITPFTRDFSNQNPEEYISDVLVNKIGCKKIVIGYDHHFGKDRKGTIKDLIHFSEIFDYTVDQIAEQDIEDVAVSSTRVRESLIKGDIITANKYLGYPFELTGTVIKGDQIGREIGFPTANLHVHESHKLIPAYGIYAVEVEIFPKTTEVVTGDYFEPVPERVAKGMCYIGTRPTVDGMNRKIEVNLLDFNDDLYTKTIRVKFLEFIRHDQWFESLELMQEQIKKDEADIRNYFEGK
>NZ_LT906468.1|WP_093096396.1|2368590_2369310_+|bacillithiol-biosynthesis-deacetylase-BshB1
MKLDLLVMTVHPDDAELGAGGVIAKYVAEGKIVGIVDLTLGELGTRGTPEIRAQEAQNAAKILGVAVRENLKLRDGFFQNNEEGQKEVIKAIRKFQPEIVITNAWEDRHPDHGRASKLVNDALFLAGLRRIETELDGIAQEPYRPRLQLQLIQDKYIQPDILIDITEYWDIKERSILAYTSQFNVENQDDEPQTYISNPDFMDSTKARGHEFGRSIQVKYAEGFTCRKILGVTDLFELL
>NZ_LT906468.1|WP_093096394.1|2368043_2368541_+|hypothetical-protein
MSKTVYDYDALEFSGQKRSLRDFEGKVLLIVNTASNCLFSGQFKTLENLYKKYKELGFEVLAFPSNDFRNQEPLTGRTLETYCRINRQVTFPVFKRIHVKGEFTDPLYRYLTNIEENGKIGTIPMWNFHKYLINKKGEVVDHFYSLTSPMSKKVHNRIEELLGDK
>NZ_LT906468.1|WP_093096391.1|2367389_2368031_+|DUF4294-domain-containing-protein
MCGSNIKWVFIVAILFAWPAFGFAQTLIKPQYGPGKPEVVEHYATTTLDNGEVVPWFPIEEVVIYAKRTFKTEEDRQKYLRLRRNVIRVLPYAIYAQKRYEQLDRDLALANSRREEKRLIKECEREIKDKITSEVKNLSVSQGKILIKLIERQTGNTSYDLVKDMKGGISAFVYQGVAKIFGHNLKSTYDPQEDYEIENIIREYERSRPMVKR
>NZ_LT906468.1|WP_093096390.1|2365044_2367249_-|bifunctional-(p)ppGpp-synthetase/guanosine-3',5'-bis(diphosphate)-3'-pyrophosphohydrolase
MEEYVIDIEAENKEIRKRYRALLRACKPTLQKGDKQQIRKAFDLALESHKDMRRKSGEPYIYHPIAVAQIAAEEIGLGTTSIVCALLHDVVEDTSVTLQDIEEQFGKKVVRIIDGLTKISGIFDPNSSMQAENFRKMLLTLADDVRVILIKLADRLHNMRTMEFMARHKQLKIASETSYLYAPLAHRLGLYAIKSELEDLSMKYTDPDTYKFIAKKLNEKKAEREKFIADFISPIQEILAEEGINASVFGRPKSIHSIWNKMRKKSIPFEEVYDLFAIRIIIDTDDEKEKTECWKVYSIVTDLYRPNPDRLRDWVSSPKANGYESLHTTVMGPRGQWVEVQIRTRRMNEIAEKGFAAHWKYKESNSDNGLDQWIQKVRDILSNPEPNALDFVDDFKMNLFSDEIFIFTPKGTLVQLPNGATALDFAFEIHTDIGATCIGAKVNHKLVPLSHELQNGDQVEIITSSKQTPKEDWLNFVVTAKAKSKIKSSLKEEKRRVAEDGKEILERKLKSLKITYNTENINKIANFFKFPSSQELFYNVAKGAIDIKNLRNFVANERSEDANQNQFQSHINGLVEKINKKDDTILIGDDYQKVDYTLAPCCNPIPGDDIFGFLTVNDGIKIHRTSCPNASKLMANYGYRILKAKWASLHNNVAFLTGLKIVGIDDVGLVNKITTVISQDFKVNIRSLSISSNEGIFEGDIMVFVNDTHQLDSLIKHLKQIPGITGVTRYESEN
>NZ_LT906468.1|WP_093096412.1|2376873_2377758_-|hypothetical-protein
MIVYNPKDWFKTIAYLHNSKIFKRLLPYLIISVLVSWALAYWELEYLKLSDRTWMKNITTVHNLLGFVLSLLLVFRTNTAYDRWWEARKQWGALTNTSRTLSIKLNAFLAPDDKVNRSFYKKSIALFAETLFSYLRSDYTKFMLDENEHPELQDLDDKKHGPNQVAALIYKKTNIIYKEGIITGDQLIVLNKELTSLTEITGACERIKNTPIPLGYSAFIKTFIVLYTATLPIGLVFSMGYFVVAAVPFIFYVLATLEMIGESIEDPFGSDSDDLPIDKIAANIKKHSNEILLG
>NZ_LT906468.1|WP_093096415.1|2377807_2378653_+|glycoside-hydrolase-family-25-protein
MTKKRKTVKKKVVSEREINRNLLFWSIAIPCLIVIGIFAWQHRAGLSYLMVKWFEKDKMIAEDNSKYDIRNVELMRRHDDKIFGIDISQYQGEISWDEVLTINDEFPIDFIYIRATMGEKAKDSKFKSNWKAVKNRNKLRGAYHYFRPNENSIKQANNFIKTVDLEPGDLPPVLDIEEMPRNQSMDSLKTGLKRWLVQVEKHFKIKPVLYSGDKYFADFLEKEFADYTLWIANYNFWVEKPKKHWNFWQFSEKGTVKGIKGPVDLNLFSGDIEELEKLSLE
>NZ_LT906468.1|WP_093096417.1|2378751_2379048_+|thioredoxin
MASFNDILQKNSLVLIDFSAAWCGPCQMLAPILKEVKDEMGEKLSIIKIDIDKNQAVASKFHVQGVPTLILYKDGNQVWRQSGLQPKHELLKIINSFS
>NZ_LT906468.1|WP_093096420.1|2379446_2380766_-|HlyC/CorC-family-transporter
MVTEIVIILILIVLNGILSASEIAIVSSRKARLQAASSKNKGARTALELKENPNNFLSTVQIGITLIGILTGFFSGGTISVYIAEQLNKIEALAPYSNQVSVLLVVLIITYLSLIIGELVPKRIGMAIPEKYASFISVPMNVLSKIVKPFVWLLSISTEFIVKLFNIKINQNAVTEEEIKALVDEGVDSGAIEGIEHDMVDRVLSLGDKKAINLMVHRSKITYLDIQDSFEENKACIIADEHTEYPVCDGNFDHVVGLVHVKTLLKEYLTSKEMDLSKLVTPIPFVNENTYAYNVLKTLKIAKVLQAVVVDEYGSPQGIITMTDIVASLVGGFDSPETEEKKTIRQREDGSFVIDGSFQLDDFIEMFNLDLTEEDEDEIGNLTTVAGLVFLLLDHIPEEGEKVMYKNLEFEVLDMDGHRIDKLSLIVKDPASDETANID
>NZ_LT906468.1|WP_093097768.1|2380987_2382103_+|phosphotransferase
MSTKKTENSIRSAKNFKLEGEIIDSVPFGSGHINDTFKITTNSLQNNLYLLQRINHHIFQDVEGLMNNIESVCKHLKEKLAHLGEKEVLKRTMTIVPTYDNKNYYQDENGDYWRVFHLIPETRSYDILETQEQAYSGGMAFGQFQKQLSDLDPKTIVEILPNFHNIEFRLSNLRDAIEKNPAKRVEKIQDLLDYIFEREEKMRTVLELGRSNKLPLRITHNDTKFNNVLLDKDDNVQCVIDLDTVMPGYVAYDFGDAIRTIINSAAEDEADVSKIVLNIPLFQSFTAGYLSEAKEFLTDAEVDSLIPAVHLLPYMQAVRFLTDYINGDTYYKIAYPEHNLVRTKAQLKLVHELEVNNDKLTGILAENLMSN
>NZ_LT906468.1|WP_093096421.1|2382104_2382743_+|hypothetical-protein
MKELEVKKIDLTGVELTYANLANSLFGLEWNQIDQAPWQTQFPINPEVKFQVAYDQESIYVHYDVQEEFVKAQYIRPNENIWEDSCVEFFISFDDRKTYYNLEFNVLGAGLIGYGTSDKASRNRLTSEEILSVSSFTQVKNLQGKKSWNIILAIPISLFGKTVDDLRGKTVQANFYKCGDSLPNPHFVAWNPIDVPNPNFHLPEFFGEIKFQ
>NZ_LT906468.1|WP_093096424.1|2382816_2383374_-|NAD(P)H-dependent-oxidoreductase
MANKKIGVFVGSLRKGSFNKKIANYLVSNPPAGLSLEILEIGQLPFYNEDLDQGNPPKEYVDFRKAVSELDAVLFITPEYNRGVTAVLKNAIDVASRPYGKNVWDGKPGGVISSSIGAIGGFGANHHLRQSLVFINVPAMAQPEAYIGNVAANFDEQGKLVNKDCQKFLSSFMAAYKEWIEKFLK
>NZ_LT906468.1|WP_093096425.1|2383457_2385902_+|ligase-associated-DNA-damage-response-DEXH-box-helicase
MSTVKNEFAEVWFFNQGWKAHEFQENCWEAISNGESGILNAPTGYGKTFAIWFGIIAQYYAKMADPKASKKKHLHALWITPLRALSKEIHKATNQVSVDLDLDYQIELRTGDTSTSIRQKQRKNPPQALITTPESVHLILATKSGQDYFKNLEFIVVDEWHELLGSKRGVLIELALSRLKAINPNLKIWGISATIGNLEEAKDILLGPGTSGTLIRADIHKKMDIQTVFPDNLEKFPWAGHLGIKLLDKVVDIINKYQTTLIFTNTRSQAEIWYQQIITHYPEFAGLLAIHHGSLSDEVRNWVEEALHEGKLKAVVCTSSLDLGVDFRPVDCVIQVGSPKGIARFLQRAGRSGHRPDATSIIYYVPTNSLEIIEGDSLKFAVKEKIVESRIPYLRSFDVLIQYLMTLAVGDGFYADEILQEVAQTHCFESITQEEFDQCMSLLIHGGSTLQAYDDFHRLVLEDGLYKVTSRKLAMRHRLSIGAIVSDLMMRVKFLSGKYLGSIEESFISKLNIGDVFWFSGRQLELVQIIANDAIVKASEKKKGVVPSWMGGRFAISPDLGIAIRHSFKSIHKTVGISPEIKFLKPLFKEQEQLSALPKEDELLVEYIQSKYGYHLFFYPFEGKLVHEGMAQVVAYRLSLLKPATFSIATNEYGIELLSETDYEIDTALLKQIFSPQNLHKDINSGINVQEMARRRFRDIAGIAGLIFQGFPGKQMKSKHLQANAGLFFSVFSEYEPSNLLLREAYDEVFDFQLEEGRMQLAFERISKHKIIFSRPIKLTPFAFPIFAESFRERYSNEDWQSRLEKLKNQLLDG
>NZ_LT906468.1|WP_093096428.1|2385894_2386545_+|ligase-associated-DNA-damage-response-endonuclease-PdeM
MAKRLELNGLEMYLLPQRVMYIPKYFMLIISDWHLGKLTHFRKEGLFVPAPNIDEELERMNLLIEDLDIKEIVFLGDLFHSEWNSDWEKLKSHINSISKQSIQFTLTKGNHDILKETHFRDMNMKIKDEVLLAEGIILSHEPLIGLPTYMYNIVGHIHPGCLIEAGGRQSFRLPCFFIQDKVLTMPAFGKYTGLHLIKKDRSNKIFVIVNDSVLEL
>NZ_LT906468.1|WP_093096431.1|2386650_2387814_+|hypothetical-protein
MSNRLFSIALLFLFVSCVSTKPDVATTKDIVWTLGGFERPNAVNPIILPDSNSTFMDPMSDSLLRWEENDTFNPGAVVKDGKVYVLYRAEDKFGIGIGFRTSRLGLAESSDGIHFKRRKEPVLFPDKDSQREYEWPGGLEDPRLAVTEDGTYVVFYTQWNRKMPRLGVATSKDLINWQKHGPIFKNAKYQKVYNEPHKSASIVTSLKNDKLVITKVNGKYLMYWGEHGVSGATSTDLINWEPILDEEGKLAKFITPREGYFDSALTECGPPAILTDKGILLLYNGKNHDKKELADPRFNIGTYSAGQVLFSSTDPSNVIQRMDVPFLRPMEDFEKSGQYKDGTVFIQGLTYFKNKWFLYYGCADSRVAVAVYDPTKLTDFDPVPESK

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Crispr_ID: NZ_LT906468_15

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LT906468_15

2526396-2526472

Orphan

Consensus_repeat	Method
TGAGATATGAGTATTGAGATATTAAA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_LT906468_15

>merge|NZ_LT906468|15|2526396-2526472|CRISPRCasFinder
TTAGATGTGAGATGTGAGATATGAGTATTGAGATATTAAACGTACTACAAATTAGATGTGAGATATGAGATATGAGT

>NZ_LT906468|15|15|2526396-2526472|CRISPRCasFinder
TTAGATGTGAGATGTGAGATATGAGT	ATTGAGATATTAAACGTACTACAAA
TTAGATGTGAGATATGAGATATGAGT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LT906468.1\|WP_093096723.1\|2531588_2534153_+\|DNA-gyrase-subunit-A	unknown	unknown	gnl\|CDD\|235502
NZ_LT906468.1\|WP_093096688.1\|2517905_2518112_-\|RNA-binding-S4-domain-containing-protein	unknown	unknown	gnl\|CDD\|379097
NZ_LT906468.1\|WP_093096720.1\|2530179_2531247_-\|3-phosphoserine/phosphohydroxythreonine-transaminase	unknown	unknown	gnl\|CDD\|235428
NZ_LT906468.1\|WP_093096705.1\|2523144_2523381_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906468.1\|WP_093096708.1\|2523745_2526346_+\|ATP-dependent-chaperone-ClpB	unknown	unknown	gnl\|CDD\|274529
NZ_LT906468.1\|WP_093096735.1\|2538465_2538936_-\|DNA-starvation/stationary-phase-protection-protein	unknown	unknown	gnl\|CDD\|153102
NZ_LT906468.1\|WP_093096700.1\|2521484_2522021_-\|RNA-polymerase-sigma-factor	unknown	unknown	gnl\|CDD\|224511
NZ_LT906468.1\|WP_093096697.1\|2520098_2521472_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906468.1\|WP_093096738.1\|2538966_2539926_-\|aldo/keto-reductase	unknown	unknown	gnl\|CDD\|381307
NZ_LT906468.1\|WP_093096732.1\|2537498_2538317_-\|ZIP-family-metal-transporter	unknown	unknown	gnl\|CDD\|223505
NZ_LT906468.1\|WP_093096685.1\|2516753_2517818_-\|3-dehydroquinate-synthase	unknown	unknown	gnl\|CDD\|341474
NZ_LT906468.1\|WP_093096694.1\|2519485_2520097_+\|HAD-IA-family-hydrolase	unknown	unknown	gnl\|CDD\|223710
NZ_LT906468.1\|WP_093096683.1\|2516023_2516749_-\|ThuA-domain-containing-protein	unknown	unknown	gnl\|CDD\|377643
NZ_LT906468.1\|WP_093096691.1\|2518207_2519398_+\|proline-dehydrogenase-family-protein	unknown	unknown	gnl\|CDD\|215366
NZ_LT906468.1\|WP_093096729.1\|2535266_2536442_+\|tetratricopeptide-repeat-protein	unknown	unknown	gnl\|CDD\|274350
NZ_LT906468.1\|WP_093096702.1\|2522293_2523142_+\|universal-stress-protein	unknown	unknown	gnl\|CDD\|366180
NZ_LT906468.1\|WP_093096717.1\|2529226_2530174_-\|D-2-hydroxyacid-dehydrogenase	unknown	unknown	gnl\|CDD\|240628
NZ_LT906468.1\|WP_093096714.1\|2527797_2529111_-\|aspartate-kinase	unknown	unknown	gnl\|CDD\|236376
NZ_LT906468.1\|WP_169918997.1\|2534136_2535249_+\|tetratricopeptide-repeat-protein	unknown	unknown	gnl\|CDD\|274350
NZ_LT906468.1\|WP_093096711.1\|2526625_2527792_-\|diaminopimelate-decarboxylase	unknown	unknown	gnl\|CDD\|143501

Protein	Function_ID	Function_description	E-value
NZ_LT906468.1\|WP_093096723.1\|2531588_2534153_+\|DNA-gyrase-subunit-A	gnl\|CDD\|235502	PRK05560, PRK05560, DNA gyrase subunit A; Validated.	0
NZ_LT906468.1\|WP_093096688.1\|2517905_2518112_-\|RNA-binding-S4-domain-containing-protein	gnl\|CDD\|379097	pfam13275, S4_2, S4 domain. The S4 domain is a small domain consisting of 60-65 amino acid residues that was detected in the bacterial ribosomal protein S4.	1.94981e-23
NZ_LT906468.1\|WP_093096720.1\|2530179_2531247_-\|3-phosphoserine/phosphohydroxythreonine-transaminase	gnl\|CDD\|235428	PRK05355, PRK05355, 3-phosphoserine/phosphohydroxythreonine transaminase.	0
NZ_LT906468.1\|WP_093096708.1\|2523745_2526346_+\|ATP-dependent-chaperone-ClpB	gnl\|CDD\|274529	TIGR03346, chaperone_ClpB, ATP-dependent chaperone ClpB. Members of this protein family are the bacterial ATP-dependent chaperone ClpB. This protein belongs to the AAA family, ATPases associated with various cellular activities (pfam00004). This molecular chaperone does not act as a protease, but rather serves to disaggregate misfolded and aggregated proteins. [Protein fate, Protein folding and stabilization].	0
NZ_LT906468.1\|WP_093096735.1\|2538465_2538936_-\|DNA-starvation/stationary-phase-protection-protein	gnl\|CDD\|153102	cd01043, DPS, DPS protein, ferritin-like diiron-binding domain. DPS (DNA Protecting protein under Starved conditions) domain is a member of a broad superfamily of ferritin-like diiron-carboxylate proteins. Some DPS proteins nonspecifically bind DNA, protecting it from cleavage caused by reactive oxygen species such as the hydroxyl radicals produced during oxidation of Fe(II) by hydrogen peroxide. These proteins assemble into dodecameric structures, some form DPS-DNA co-crystalline complexes, and possess iron and H2O2 detoxification capabilities. Expression of DPS is induced by oxidative or nutritional stress, including metal ion starvation. Members of the DPS family are homopolymers formed by 12 four-helix bundle subunits that assemble with 23 symmetry into a hollow shell. The DPS ferroxidase site is unusual in that it is not located in a four-helix bundle as in ferritin, but is shared by 2-fold symmetry-related subunits providing the iron ligands. Many DPS sequences (e.g., E. coli) display an N-terminal extension of variable length that contains two or three positively charged lysine residues that extends into the solvent and is thought to play an important role in the stabilization of the complex with DNA. DPS Listeria Flp, Bacillus anthracis Dlp-1 and Dlp-2, and Helicobacter pylori HP-NAP which lack the N-terminal extension, do not bind DNA. DPS proteins from Helicobacter pylori, Treponema pallidum, and Borrelia burgdorferi are highly immunogenic.	1.87653e-59
NZ_LT906468.1\|WP_093096700.1\|2521484_2522021_-\|RNA-polymerase-sigma-factor	gnl\|CDD\|224511	COG1595, RpoE, DNA-directed RNA polymerase specialized sigma subunit, sigma24 homolog [Transcription].	1.91326e-32
NZ_LT906468.1\|WP_169918997.1\|2534136_2535249_+\|tetratricopeptide-repeat-protein	gnl\|CDD\|274350	TIGR02917, TPR_domain_protein, putative PEP-CTERM system TPR-repeat lipoprotein. This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.	8.38158e-13
NZ_LT906468.1\|WP_093096738.1\|2538966_2539926_-\|aldo/keto-reductase	gnl\|CDD\|381307	cd19081, AKR_AKR9C1, AKR9C family of aldo-keto reductase (AKR). Haloferax volcanii aldo-keto reductase is a founding member of aldo-keto reductase family 9 member C1 (AKR9C1).	9.00333e-156
NZ_LT906468.1\|WP_093096732.1\|2537498_2538317_-\|ZIP-family-metal-transporter	gnl\|CDD\|223505	COG0428, COG0428, Predicted divalent heavy-metal cations transporter [Inorganic ion transport and metabolism].	1.30313e-55
NZ_LT906468.1\|WP_093096685.1\|2516753_2517818_-\|3-dehydroquinate-synthase	gnl\|CDD\|341474	cd08195, DHQS, Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway for aromatic compounds synthesis. Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway, which involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds, is found in bacteria, microbial eukaryotes, and plants, but not in mammals. Therefore, enzymes of this pathway are attractive targets for the development of non-toxic antimicrobial compounds, herbicides and anti-parasitic agents. The activity of DHQS requires nicotinamide adenine dinucleotide (NAD) as cofactor. A single active site in DHQS catalyzes five sequential reactions involving alcohol oxidation, phosphate elimination, carbonyl reduction, ring opening, and intramolecular aldol condensation. The binding of substrates and ligands induces domain conformational changes. In some fungi and protozoa, this domain is fused with the other four domains in shikimate pathway and forms a penta-domain AROM protein, which catalyzes steps 2-6 in the shikimate pathway.	1.83266e-147
NZ_LT906468.1\|WP_093096694.1\|2519485_2520097_+\|HAD-IA-family-hydrolase	gnl\|CDD\|223710	COG0637, COG0637, Predicted phosphatase/phosphohexomutase [General function prediction only].	5.82928e-33
NZ_LT906468.1\|WP_093096683.1\|2516023_2516749_-\|ThuA-domain-containing-protein	gnl\|CDD\|377643	pfam06283, ThuA, Trehalose utilisation. This family consists of several bacterial ThuA like proteins. ThuA appears to be involved in utilisation of trehalose. The thuA and thuB genes form part of the trehalose/sucrose transport operon thuEFGKAB, which is located on the pSymB megaplasmid. The thuA and thuB genes are induced in vitro by trehalose but not by sucrose and the extent of its induction depends on the concentration of trehalose available in the medium.	1.90927e-97
NZ_LT906468.1\|WP_093096691.1\|2518207_2519398_+\|proline-dehydrogenase-family-protein	gnl\|CDD\|215366	PLN02681, PLN02681, proline dehydrogenase.	9.74998e-108
NZ_LT906468.1\|WP_093096729.1\|2535266_2536442_+\|tetratricopeptide-repeat-protein	gnl\|CDD\|274350	TIGR02917, TPR_domain_protein, putative PEP-CTERM system TPR-repeat lipoprotein. This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.	3.77988e-14
NZ_LT906468.1\|WP_093096702.1\|2522293_2523142_+\|universal-stress-protein	gnl\|CDD\|366180	pfam00582, Usp, Universal stress protein family. The universal stress protein UspA is a small cytoplasmic bacterial protein whose expression is enhanced when the cell is exposed to stress agents. UspA enhances the rate of cell survival during prolonged exposure to such conditions, and may provide a general "stress endurance" activity. The crystal structure of Haemophilus influenzae UspA reveals an alpha/beta fold similar to that of the Methanococcus jannaschii MJ0577 protein, which binds ATP, though UspA lacks ATP-binding activity.	1.42225e-16
NZ_LT906468.1\|WP_093096717.1\|2529226_2530174_-\|D-2-hydroxyacid-dehydrogenase	gnl\|CDD\|240628	cd05303, PGDH_2, Phosphoglycerate dehydrogenase (PGDH) NAD-binding and catalytic domains. Phosphoglycerate dehydrogenase (PGDH) catalyzes the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDH comes in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases. PGDH in E. coli and Mycobacterium tuberculosis form tetramers, with subunits containing a Rossmann-fold NAD binding domain. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence.	6.35024e-149
NZ_LT906468.1\|WP_093096714.1\|2527797_2529111_-\|aspartate-kinase	gnl\|CDD\|236376	PRK09084, PRK09084, aspartate kinase III; Validated.	1.20927e-132
NZ_LT906468.1\|WP_093096711.1\|2526625_2527792_-\|diaminopimelate-decarboxylase	gnl\|CDD\|143501	cd06828, PLPDE_III_DapDC, Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase. Diaminopimelate decarboxylase (DapDC, EC 4.1.1.20) participates in the last step of lysine biosynthesis. It converts meso-2,6-diaminoheptanedioate to L-lysine. It is a fold type III PLP-dependent enzyme that contains an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. DapDC exists as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Homodimer formation and the presence of the PLP cofactor are required for catalytic activity.	3.35911e-151

>NZ_LT906468.1|WP_093096708.1|2523745_2526346_+|ATP-dependent-chaperone-ClpB
MNFNNFTIKAQEAIQKASEIASGHQQQAIEPAHIMKALLSVDENVISHLLKKLNVNISYLSQEVDKLIESYPKVSGSNVYLSNSATAVLQKAQSFLKEFNDEFVSIEHILLGLLLSGDKVSSLLKDQGVTEKDLKTAIKELRGNSRVTDQNAEATYNALNKYARNLNEYAESGKLDPVIGRDEEIRRVMQILSRRTKNNPILVGEPGVGKTAIAEGIAYRIIKGDAPENLKTKTVFSLDMGALVAGAKYKGEFEERLKAVVKEVSDSDGEIILFIDEIHTLVGAGGGEGAMDAANILKPALARGELRTIGATTLNEYQKYFEKDKALERRFQKVMVEEPDTQDAISILRGIKERYETHHKVRILDEAIISAVELSQRYITDRFLPDKAIDLVDEAASKLRLEMDSVPVVVDELERRIMQLEIEREAIKREKDEKKISELSETIANLSNERDSLRAKWQSEKTLVDQVNAEAQNIENYKLEAEQAERAGDYGKVAELRYGKIKEAQDKVDALKKELSEKQDSSRMLKEEVTSEDIADVVSKWTGIPVSKMIQSEREKLLNLEEELHKRVAGQDEAIEAIADAIRRSRAGLSDAKRPIGSFIFLGTTGVGKTELAKALAEYLFDDEQAMIRIDMSEYQERHAVSRLIGAPPGYVGYDEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGHLTDNKGRVVNFKNTIIIMTSNTGSHIIQENFSKLNDENREEVVAKTKDEVLDLLQKSIRPEFLNRIDEVIMFTPLSRTEIGDIVRMQFNRVEKQLAEQNIFLTASDEALDWLAQLGYDPVYGARPLKRVIQKRILNELSKEILSGKISRDSVIELDAFDGKFVFLNKDQE
>NZ_LT906468.1|WP_093096705.1|2523144_2523381_+|hypothetical-protein
MQQVIKKLESLNRINDKAEKYTEITDENFVEHGILFFIPLEKYEVKVLIPAPHHKALFQNGTPTFKQVLNHKEAMMLK
>NZ_LT906468.1|WP_093096702.1|2522293_2523142_+|universal-stress-protein
MRAILFPTDFSEIANNAFLYALHIAKSIDAKIYVLYSYLEPVLSATHGGQPELLGEVYQTIELNQFEVYKKKTQKLRDIAAEIGMQEVELVFLFEEGPVASVVKNIVTREKIHLVVMGTHGESGFLSKLIGTNTVSVIKSIQNPVLAVPPHAKYQGIKRTVFTTLFREKDKSALKEMLIMAKAVDAKIECLHVLHNDKVADVLLHSEAWQKEFPNENINYVLLDEVESIENTIANYILENNIDILGVVKRNRSFFDRLFNSSISNNLALHSKVPILVFHEEK
>NZ_LT906468.1|WP_093096700.1|2521484_2522021_-|RNA-polymerase-sigma-factor
MSNSEKSKSFLYKKFYGYVMAVVIRYMKHEMEAEELVNECFVKAFNKIGTFSLHEDPNVLEKTFKSWIARIAVNTSIDALRVRKQMYMLDDLSSSDTIHYSVDNGSKLEYEDMLSLIQQLPDIQRSIFNLYEIEGYSHEEIGKELGIPESTSRTYLTRAKQKLRKLYLSQIDLENIKS
>NZ_LT906468.1|WP_093096697.1|2520098_2521472_-|hypothetical-protein
MEEKNKKDIVEQIVEKMKSMEELPYKEGAWENFQSRYGGAPIKRNKPYYWAASAAAILLLGVATVKYWPDNNPADLNNQMASSQEATMDNRSTPQDNNGLQEGLSSQDVGVNPLQGSEIAGTDGWNASANGTNLIAQAQVQDAHDEVRGYQDLGLVSNYANQGVYPSTVQIPNSLHAYNLSDKRAKIDLEDDKLGFRENNINTELAYQAQEAKKGAEPTIKNRNFNFRERFDLGLFVSPNSTNERFNFGGGVLLAYNINKNVSVRTGLAYNRYDASQMKDPVANSETPVVASKEALQKITANGLTQNFASSNAIILPNVNAISGNVQALEVPLDVRVKSKSGYYASTGITYAAVFNQNRYAHYVENANTELFGNGLPESEAEVKTAVKQVSRAIKTEDENVSSNGFGGFVNFSIGKEMKMNKNINLSVEPYFKMPVGSFKRADMNYTNGGIRIITNF
>NZ_LT906468.1|WP_093096694.1|2519485_2520097_+|HAD-IA-family-hydrolase
MTEENYQKYLKLKEIAAPFKALLFDVDGTLADNMQAHKAAYVETAKEHGIVLNPDLIDETAGWPTVAVADEISSRYQVPLDRFEFAKRKSAIFIEQFIQKTQPVDFVRQILYDFAESRKIGIVSGGSRSTLNITLDVIKVVGKYETLVCAGDTPEGKPSPQPFLLAAEHLNVDPIDCLVFEDGDPGVQGAISAGMAWVRIDQM
>NZ_LT906468.1|WP_093096691.1|2518207_2519398_+|proline-dehydrogenase-family-protein
MDIASPLKLDFNNTEIAFQGKSDKDLNKAYWLFKMVASNTLIKIGTPITNFSLNIGLPIQGIIKNTIYKQFCGGESIQDCQTAIQDLGKGHVTTILDYSVEGEDSEESFDACCAEILRTVEAAKANPLISFCVFKPTGLGRFDLLAKIDAKESLSPEEQAEYNRMLERCDRICKACYDNNIRVLIDAEHSWIQDTIDDIAREMMEKYNSESPIVYNTYQMYRHDKLASIKADFAYAKTQGFHLGAKLVRGAYMEIERERAKENNYPSPIQPNKKASDTDYNAAVDFCLDNIDTVGLMAGTHNEESCRLLTNELEKRNIPHNLPNVFFAQLLGMSDNLSFNLAAAGYNVAKYMPYGPVKSVMPYLFRRAQENTSVGGQTGRELSLIMKELKRRKSEK
>NZ_LT906468.1|WP_093096688.1|2517905_2518112_-|RNA-binding-S4-domain-containing-protein
MQTFTLEGDYIQLIQLLKVMNWVEHGAMAQWVVEEGLVKYNGQVDYRKRLKVKVGDIVEFDGNKVKVQ
>NZ_LT906468.1|WP_093096685.1|2516753_2517818_-|3-dehydroquinate-synthase
MKKINSLGYEVVFDDELDELQSFLIDHDYSQLLILVDRNTNDHCLPVIQAAIPDIVDYDIIEVDPGEENKNIDFCIGVWKTMLDFGADRKALMLNLGGGVVTDMGGFAASTYKRGIDFLNVPTTLLSQVDASVGGKTGIDLDNVKNIIGTFSQPKAVFISNKFLETLDDRQVLSGFAEVIKHGLIQDKDLFNRCKTVNLPVIPEGMVYDSVLIKNKVVLEDPTEKGLRKILNFGHTIGHAIEGYSLVTDVNPLLHGEAIAIGMICEAYLSHKINNLDIAELDELVDYLLSIYPKYNLNSAVYPELLALMKNDKKNEGNKLGFALLRKIGDCDFNKYVEEDAIIESLDYYQSKTK
>NZ_LT906468.1|WP_093096683.1|2516023_2516749_-|ThuA-domain-containing-protein
MKRICILTLICCLSICFAFATGIEKPKKVLVFTKTAGFRHDNIEEGVKVLTKLLKDENIGMFHTEDANVFLADSLKNFDAVLFFSTTGTILDEEQKVAFQNFLKSGKGFMGIHAATDTEHDWPWYNNLVGAYFASHPAVQEAKIDVKNRKHLATKHLPKVWMHKDEWYDFSNVKPDLKILMTLDEKSYKNGKMGDFHPIAWYQKYDGIKVFYTGLGHTKESFYEPNFQKQIIGGLKYVLGY
>NZ_LT906468.1|WP_093096711.1|2526625_2527792_-|diaminopimelate-decarboxylase
MNINQIDLGRLKEYETPFYYYDLDLLNETLDKAKAAADKRGFHVHYALKANFNDRILGLIQSKGFGADCVSGNEVQKSIDSGFPANQITFAGVGKSDKEINLALSHNIFAFNVESIQELLVINELAAKQNVKAQVSLRINPNVDAHTHHYITTGLDENKFGVPNSELEKAASVLRECDHLDLLGLHFHVGSQITDINVFKSLCVKVNEWKNWFEERGTMIKVLNVGGGLGVDYHEPDAHPFADFEAYFDVFDKFLERTPQQEVHFELGRALVAQSGTLVSRVLYTKSGVKKNFLILDAGMTELMRPALYQAFHKIEKLGSNNNSTEKLNYDVVGPICESSDCFGKEVTLPVSERGDLIAIRTAGAYGEVMASKYNLRDEIRFVFSGEI
>NZ_LT906468.1|WP_093096714.1|2527797_2529111_-|aspartate-kinase
MKILKFGGTSVGSAERIQSLLDIVNPAERQIVVLSAVAGTTNALVEISKAYLNGKKDEAKELIKEHKNKYEALIKELFSTENGYKQGKELIDYHFNLIASLSNDLFTPTEEKIILAQGELMSTTLWHLYLSEKGIKSVLLPALDFMKIDEDNEPMVPFIKEKLEAILADYPDNSLFITQGYICRNSFGEIDNLRRGGSDYTASLIGAAIQADEIQIWTDIDGMHNNDPRIVKGTTPIAELSFDEAAELAYFGAKILHPQSVFPAQRYNVPVRLLNTLDPKAFGTLISKNGGQKGSIRAVAAKDDITAIHIHSSRMLLAYGFLRKIFEIFERYKTPIDMITTSEVAVSLTIDETKNLEDIIREVEDFGKVSVDRNQTIICVVGDFGANTHGYAARVLDAVKHLPLRMVSYGGSDYNVSILLDSEHKVEALRSLHNRIF
>NZ_LT906468.1|WP_093096717.1|2529226_2530174_-|D-2-hydroxyacid-dehydrogenase
MKILANDGIDPIGKKILEDAGFVVDTNHIPQDELINRLNEYDAVTVRSATKLRQPLIDACPNIKVIGRGGVGMDNIDVDYARSKGIAVVNTPAASSHSVAELVFAHLLNGVRFLYDSNRKMPVEGNSNFAGLKKAYAAGSELKGKVLGVVGFGRIGRETAKIGLGLGMTVIYSDLFEGPNSLTLDFAGDVSVNVPVEQVNIDTIFQKSDFISLHVPFTDKPVIGKEEFALLKDGVGLVNASRGGVIEELALVEALNSGKVGFAALDVFDNEPTPRAEILNHPRISLTPHIGAATNEAQERIGEELAQLLIDNLKK
>NZ_LT906468.1|WP_093096720.1|2530179_2531247_-|3-phosphoserine/phosphohydroxythreonine-transaminase
MKHNFGAGPCILPKEVFEEASRAVIDFNGTGLSILEISHRSKEFEEVVIETEKLVRELLEVPAGYSILFLQGGASQQFAMVPMNLLPENGKASYLDTGVWATKAAKEAKKVGQVEIVASSSDKNYTYIPKDFVVPSDAAYFHYTSNNTIYGTEVFEKPNTSVTTVVDMSSDILSRTINVSEFGLIYAGAQKNMGPAGVTLVIIKDDLFAKSGRTIPTIFDYEAHAKAGSMYNTPPVFSIYVSMLNLRWLKAKGGISVIEQENIIKARTLYDEIDRNPFFKGTAAVEDRSRMNVTFVMDTPELEAEFLALAKERNLIGIKGHRSVGGFRASIYNALSISSINALVDTMREFEEKKK
>NZ_LT906468.1|WP_093096723.1|2531588_2534153_+|DNA-gyrase-subunit-A
MAEETENENNLVPAENRIIPINIEDQMKSAYIDYSMSVIVSRALPDARDGLKPVHRRVLYGMLDLGVTSGKPYKKSARIVGDVLGKYHPHGDSSVYDTMVRMAQNWSMRYPLVDGQGNYGSIDGDPPAAMRYTEARLRKITEEMLADINKDTVDFQLNFDDSLEEPTVLPTRIPNLLVNGASGIAVGMATNMAPHNLSEVIDGTIAYIDNRDIEISELMTHVKGPDFPTGGLIYGYNGVKEAFETGRGRIVMRAKAEIETTKTGKEIIIVTEIPYQVNKSDMIKRTADLVQEKKIEGISEIRDESSKDIRVIYEIKRDANANVVLNNLYKHTALQTSFSVNNIALVKGRPQMLNLKDMIHEFVEHRHDVVIRRTKFELAEAEKRAHILEGYLIALDHLDEVIKLIRNSDTPEDARVGLMERFALSDIQARAILDMTLRRLTGLERDKIKEEYAELMKTIEYLKEVLADETLRFKIIKDELMEVKEKYGDERRSHIVHSAEDLRMEDFIDDEEVVITISHNSYVKRTPLTEYRVQGRGGKGAIGSTTRDEDFTEHIITASAHNYLLLFTEAGRCFWLRAFEIPEGSRTSKGRALQNIINIPKDEKIKAYIKVTNLKDQEYLENNFIIMCTKKGTIKKTSLEAYSRPRANGINAININDGDQLLEATLTNGTSEIVMALRSGRAIRFNESTVRPMGRTATGVRGITLAHENDEVVGMISVNNQETTVLVVSEKGYGKRTDIDDYRITNRGGKGVKTINVTDKTGELVAIKGVTDENDLMIINKSGIVIRIGVESLRVMGRATQGVKLITLKDNDEIASVTKVERQEEEEELDVEGAEGAENPTDNDSANTENEEQE
>NZ_LT906468.1|WP_169918997.1|2534136_2535249_+|tetratricopeptide-repeat-protein
MKNKNRYISSALGAILLLGANSAFGQSAYKEASNAFALYTQTGNIANLDNARKQIDNIYKTRRDSSKTRVNVLRAMVLSSIAYADSTRTIKLNADPIDLTYQTMDRIDKKDRSGYSGEISYVNQNLAAALIYRANKSLENKKFDEAFADFSKVDALDAKSGDVTYNLALLASKAGKPEEAIKYYGKIHESGNMTPNQYIELANLYDQLDEKQKALSTLEEGRTKYAEDKAILFLLIDKYAKSKAYDAIVPIIEQAIKLEPENIELNYLAGYANENANNLEIAKTYYEKVLELDPNNYESNLALGLINLNAFLKDAENQEAQYNAQNYLLKANEIKPYEINALKSLALFYQKTEDETQLDRVNLLLNQLTN
>NZ_LT906468.1|WP_093096729.1|2535266_2536442_+|tetratricopeptide-repeat-protein
MNLRKSILFVGLLFATSSTALFAQSGNVKKAKAAIVKFEELKGAGSAELGKSNLTAAKEAIDAAVVHDKTKDDPEAWTYYALVYSNLASLDKSAEDATKAQDAIKKATELDKDKKHAENIAVAGQTLGQYKFNQGVAAWDKQDFKTAYSDFSDALVYLPGDTTLTFYSGLAAVQNKEYDKAIEKYKELVPVKEYSSHKTIMVDLPKLYLQKGDTTSAIAAAAEAVAAYPNDNDAVVQNIELNLITGNEAKIVSDIESQVAKDPQNKSLHYYLGLAYGASGDAEKALASYQKAIEIDPNYLEANTNAAVVIMNGGRDELMKLNEDKSVPAAEYNKKVEAIKGKIARAVPYLEKAVELDAKNVDALRNLKNYYDFMNDEAKSAELQAKIEALN
>NZ_LT906468.1|WP_093096732.1|2537498_2538317_-|ZIP-family-metal-transporter
MIDELVEFLGKQDAVVAALFAGLFTWGVTAVGAAGVFLFKGVNKKLLNGMLGFTGGVMIAASFWSLLAPAIEMSSGEGFSKVMPSAIGFILGALFIFGLDKLMPHLHLNFLKTEGPKSSLHRTTLLTIAIALHNIPEGLAVGVLFGGAASGIPEASITGAVLLAMGIGLQNFPEGIAVSMPLRRMGLSRWKSFQYGQLSAVVEPVFAVLGAFAVGFFMPILPYALSFAAGAMIFVVIEEVIPETQQEEHSDIPILGFVLGFVVMMVLDVALG
>NZ_LT906468.1|WP_093096735.1|2538465_2538936_-|DNA-starvation/stationary-phase-protection-protein
MKTDIGIKENDTKVVAGLLNKLLSDENVLYTKVRNAHWNVEGPDFHAQHVFFEELYTELAEIIDEVAERVRAIGHYAVGTMKEFLELTQLTEMKYKKNDSQGLISELLNDYESLIISLREDIKLAEEHNDAGTEDFLVGLLEKHEKNAWMLRSHLR
>NZ_LT906468.1|WP_093096738.1|2538966_2539926_-|aldo/keto-reductase
MEKSVQLAHSDLNIVPIIFGGNVFGWTLDEKQSFEILDGFLDLGFDAIDTANNYSHWVPGNVGGESETIIGNWSKERKNRDKIVLMTKVGGRFSYDSKKNTSASYIKEQVELSLKRLQTDYIDLYQTHYDDTTTPVEETLRAYDDLVKEGKVRYIGASNISTDRLVESLDTSSKLSLPQYISLQPEYNLYDREKYEHEYEATVKEYGLAVIPYYSLASGFLSGKYLTDDDFSKSARGEGIEKRYWNERGKRIVAALNEVASAYRTSASSVALAWLLAQPSITAPIASATKDAHLQSFVAALQLRLGEEAIEKLNDASRY

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Crispr_ID: NZ_LT906468_16

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LT906468_16

2722248-2722358

Orphan

Consensus_repeat	Method
AGTATTTAGTAGAAAGTATTTAGTATTTAGACA	CRISPRCasFinder

1 spacers

WYL

The CRISPR arrays of NZ_LT906468_16

>merge|NZ_LT906468|16|2722248-2722358|CRISPRCasFinder
AGTATTTAGTAGAAAGTATTTAGTATTTAGACAAAAGGTCCTGTGAAACATCATAGGACCTTTTTTTATATCCGTAATAGTATTTAGTAGAAAGTATTTAGTATTTAGACA

>NZ_LT906468|16|16|2722248-2722358|CRISPRCasFinder
AGTATTTAGTAGAAAGTATTTAGTATTTAGACA	AAAGGTCCTGTGAAACATCATAGGACCTTTTTTTATATCCGTAAT
AGTATTTAGTAGAAAGTATTTAGTATTTAGACA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LT906468.1\|WP_093097121.1\|2721793_2722243_+\|PepSY-like-domain-containing-protein	unknown	unknown	gnl\|CDD\|371505
NZ_LT906468.1\|WP_139185450.1\|2729858_2730080_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906468.1\|WP_093097108.1\|2715808_2717098_+\|BamA/TamA-family-outer-membrane-protein	unknown	unknown	gnl\|CDD\|227116
NZ_LT906468.1\|WP_093097100.1\|2712850_2713708_-\|aminotransferase-class-IV	unknown	unknown	gnl\|CDD\|376449
NZ_LT906468.1\|WP_139185451.1\|2735324_2735552_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906468.1\|WP_093097800.1\|2733893_2735252_-\|Gfo/Idh/MocA-family-oxidoreductase	unknown	unknown	gnl\|CDD\|223745
NZ_LT906468.1\|WP_093097142.1\|2732915_2733884_+\|YafY-family-transcriptional-regulator	WYL	COG2378_WYL_CAS-I:CAS-III	gnl\|CDD\|225253
NZ_LT906468.1\|WP_093097124.1\|2723052_2723787_-\|SIMPL-domain-containing-protein	unknown	unknown	gnl\|CDD\|225414
NZ_LT906468.1\|WP_093097137.1\|2730228_2730681_-\|antibiotic-biosynthesis-monooxygenase	unknown	unknown	gnl\|CDD\|367760
NZ_LT906468.1\|WP_093097139.1\|2732071_2732908_+\|MBL-fold-metallo-hydrolase	unknown	unknown	gnl\|CDD\|293839
NZ_LT906468.1\|WP_093097111.1\|2719282_2719954_+\|response-regulator-transcription-factor	unknown	unknown	gnl\|CDD\|223816
NZ_LT906468.1\|WP_093097798.1\|2730743_2731775_-\|aldo/keto-reductase	unknown	unknown	gnl\|CDD\|381304
NZ_LT906468.1\|WP_139185449.1\|2717136_2719221_+\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|238657
NZ_LT906468.1\|WP_093097129.1\|2726884_2729074_+\|glutamine-synthetase-III	unknown	unknown	gnl\|CDD\|226477
NZ_LT906468.1\|WP_093097126.1\|2723886_2726682_+\|S9-family-peptidase	unknown	unknown	gnl\|CDD\|224423
NZ_LT906468.1\|WP_093097118.1\|2721313_2721757_+\|PepSY-like-domain-containing-protein	unknown	unknown	gnl\|CDD\|371505
NZ_LT906468.1\|WP_093097106.1\|2714819_2715710_+\|1-aminocyclopropane-1-carboxylate-deaminase/D-cysteine-desulfhydrase	unknown	unknown	gnl\|CDD\|225313
NZ_LT906468.1\|WP_093097098.1\|2712387_2712846_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906468.1\|WP_093097103.1\|2713723_2714755_-\|RluA-family-pseudouridine-synthase	unknown	unknown	gnl\|CDD\|223638
NZ_LT906468.1\|WP_093097114.1\|2719953_2721237_+\|HAMP-domain-containing-histidine-kinase	unknown	unknown	gnl\|CDD\|223715

Protein	Function_ID	Function_description	E-value
NZ_LT906468.1\|WP_093097121.1\|2721793_2722243_+\|PepSY-like-domain-containing-protein	gnl\|CDD\|371505	pfam11396, PepSY_like, Putative beta-lactamase-inhibitor-like, PepSY-like. This family of bacterial proteins is probably periplasmic. Members are found predominantly in microbes of the human gut and oral cavity. Structurally, one member of this family is found to show similarity to the beta-lactamase-inhibitor PepSY proteins, so the overall function may be inhibitory. There are tandem repeats of the domain on many family members.	1.3833e-21
NZ_LT906468.1\|WP_093097108.1\|2715808_2717098_+\|BamA/TamA-family-outer-membrane-protein	gnl\|CDD\|227116	COG4775, COG4775, Outer membrane protein/protective antigen OMA87 [Cell envelope biogenesis, outer membrane].	0.000112171
NZ_LT906468.1\|WP_093097100.1\|2712850_2713708_-\|aminotransferase-class-IV	gnl\|CDD\|376449	pfam01063, Aminotran_4, Amino-transferase class IV. The D-amino acid transferases (D-AAT) are required by bacteria to catalyze the synthesis of D-glutamic acid and D-alanine, which are essential constituents of bacterial cell wall and are the building block for other D-amino acids. Despite the difference in the structure of the substrates, D-AATs and L-ATTs have strong similarity.	3.98965e-57
NZ_LT906468.1\|WP_093097800.1\|2733893_2735252_-\|Gfo/Idh/MocA-family-oxidoreductase	gnl\|CDD\|223745	COG0673, MviM, Predicted dehydrogenases and related proteins [General function prediction only].	3.83308e-50
NZ_LT906468.1\|WP_093097142.1\|2732915_2733884_+\|YafY-family-transcriptional-regulator	gnl\|CDD\|225253	COG2378, COG2378, Predicted transcriptional regulator [Transcription].	2.92925e-54
NZ_LT906468.1\|WP_093097124.1\|2723052_2723787_-\|SIMPL-domain-containing-protein	gnl\|CDD\|225414	COG2859, COG2859, Uncharacterized protein conserved in bacteria [Function unknown].	2.27479e-25
NZ_LT906468.1\|WP_093097139.1\|2732071_2732908_+\|MBL-fold-metallo-hydrolase	gnl\|CDD\|293839	cd16281, metallo-hydrolase-like_MBL-fold, uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain. Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.	9.1749e-154
NZ_LT906468.1\|WP_093097111.1\|2719282_2719954_+\|response-regulator-transcription-factor	gnl\|CDD\|223816	COG0745, OmpR, Response regulators consisting of a CheY-like receiver domain and a winged-helix DNA-binding domain [Signal transduction mechanisms / Transcription].	4.14047e-69
NZ_LT906468.1\|WP_093097798.1\|2730743_2731775_-\|aldo/keto-reductase	gnl\|CDD\|381304	cd19078, AKR_AKR13C1_2, AKR13C family of aldo-keto reductase (AKR). The AKR13C family includes Helicobacter pyroli aldehyde reductase (AKR13C1) and Thermotoga maritima aldo-keto reductase (AKR13C2). Aldehyde reductase (EC 1.1.1.21), also called aldose reductase, is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides.	5.16362e-173
NZ_LT906468.1\|WP_139185449.1\|2717136_2719221_+\|TonB-dependent-receptor	gnl\|CDD\|238657	cd01347, ligand_gated_channel, TonB dependent/Ligand-Gated channels are created by a monomeric 22 strand (22,24) anti-parallel beta-barrel. Ligands apparently bind to the large extracellular loops. The N-terminal 150-200 residues form a plug from the periplasmic end of barrel. Energy (proton-motive force) and TonB-dependent conformational alteration of channel (parts of plug, and loops 7 and 8) allow passage of ligand. FepA residues 12-18 form the TonB box, which mediates the interaction with the TonB-containing inner membrane complex. TonB preferentially interacts with ligand-bound receptors. Transport thru the channel may resemble passage thru an air lock. In this model, ligand binding leads to closure of the extracellular end of pore, then a TonB-mediated signal facillitates opening of the interior side of pore, deforming the N-terminal plug and allowing passage of the ligand to the periplasm. Such a mechanism would prevent the free diffusion of small molecules thru the pore.	3.80542e-38
NZ_LT906468.1\|WP_093097129.1\|2726884_2729074_+\|glutamine-synthetase-III	gnl\|CDD\|226477	COG3968, COG3968, Uncharacterized protein related to glutamine synthetase [General function prediction only].	0
NZ_LT906468.1\|WP_093097126.1\|2723886_2726682_+\|S9-family-peptidase	gnl\|CDD\|224423	COG1506, DAP2, Dipeptidyl aminopeptidases/acylaminoacyl-peptidases [Amino acid transport and metabolism].	1.40589e-40
NZ_LT906468.1\|WP_093097118.1\|2721313_2721757_+\|PepSY-like-domain-containing-protein	gnl\|CDD\|371505	pfam11396, PepSY_like, Putative beta-lactamase-inhibitor-like, PepSY-like. This family of bacterial proteins is probably periplasmic. Members are found predominantly in microbes of the human gut and oral cavity. Structurally, one member of this family is found to show similarity to the beta-lactamase-inhibitor PepSY proteins, so the overall function may be inhibitory. There are tandem repeats of the domain on many family members.	1.11987e-24
NZ_LT906468.1\|WP_093097106.1\|2714819_2715710_+\|1-aminocyclopropane-1-carboxylate-deaminase/D-cysteine-desulfhydrase	gnl\|CDD\|225313	COG2515, Acd, 1-aminocyclopropane-1-carboxylate deaminase [Amino acid transport and metabolism].	1.72045e-65
NZ_LT906468.1\|WP_093097137.1\|2730228_2730681_-\|antibiotic-biosynthesis-monooxygenase	gnl\|CDD\|367760	pfam03992, ABM, Antibiotic biosynthesis monooxygenase. This domain is found in monooxygenases involved in the biosynthesis of several antibiotics by Streptomyces species. It's occurrence as a repeat in Streptomyces coelicolor SCO1909 is suggestive that the other proteins function as multimers. There is also a conserved histidine which is likely to be an active site residue.	1.88673e-07
NZ_LT906468.1\|WP_093097103.1\|2713723_2714755_-\|RluA-family-pseudouridine-synthase	gnl\|CDD\|223638	COG0564, RluA, Pseudouridylate synthases, 23S RNA-specific [Translation, ribosomal structure and biogenesis].	1.81139e-105
NZ_LT906468.1\|WP_093097114.1\|2719953_2721237_+\|HAMP-domain-containing-histidine-kinase	gnl\|CDD\|223715	COG0642, BaeS, Signal transduction histidine kinase [Signal transduction mechanisms].	2.25898e-26

>NZ_LT906468.1|WP_093097121.1|2721793_2722243_+|PepSY-like-domain-containing-protein
MKKLLLALTVLFSIATLTMSCDKESVITEDQLPQSANQFLKDNFSGVKILSVVEEKEGLSGKEFDVLLDNGIEIKFDKNGQWLDIDAKADTARLPENLIPTAINDYVKQNYANAGINSIERENHGYDVELTNGLDLVFDKDGKFVRIDP
>NZ_LT906468.1|WP_093097118.1|2721313_2721757_+|PepSY-like-domain-containing-protein
MKNLIKTLMVLFIAGFSFQAIAQEKVIEVANLPKTAQSFLQNHYNNDKVALTKSEKETLSPIEYKVVLASGTEVEFDSKGDWTEVDANTAAVPQDIVPAKIKSYVQKSFPDNKIVQIKKDKKGYEIELTNGIEVKFNKNADFIKIDD
>NZ_LT906468.1|WP_093097114.1|2719953_2721237_+|HAMP-domain-containing-histidine-kinase
MSVSIKYYTNKFLAIAILIIMAVWALLFYAFLMDEVYDNIDDGLKNQKLEIIREAYNNPDIINNNQEYGINQFKIYPIQPKEDIDKNHFSRELMYMPYDDEDEPYRILKTGFYSKDRKAYGLDIRTSTVEEDDYLINLAIALAVLYLVIVLSILVINYFVMSKGWQPFQKILRNLSNYRFGHSKTFEPTITKVKEFEELNSQIKQMIDRNEGLFEEQKLFLENASHELQTPLAITIGKLDLLLQEGDLPEEKTIKIAEAKQALHRMVALNKSLLMLSRIENNQYSSSTEVNFNDLIIKKLEELEDFIQFKEIKVDLVQNEQFIANLNLDLAHILISNLLRNAIKYNFQEGHIRITISNNVIDFANSSDSGALNPQYIFKRFHKGNQDSQSNGLGLSIVQTILDKYPHIHIEYEYAQAEQHFKLKKFK
>NZ_LT906468.1|WP_093097111.1|2719282_2719954_+|response-regulator-transcription-factor
MKILIIEDEKELLLTIEEFLKSENFLIESAMDYNTALEKAMNYQYDCILLDIMLPDGSGLDILRALKDEHKKQPVLILSAKDSVEDKVLGLEIGADDYLSKPFHLAELLARVKSIIRRNSNDGEQWVKYKNVSLNPESRIILINDTDIAFNRKEFDLFHYFLLRPNRLLEKTSLVESVWGDHTDQADNLDFIYSQIKNIRKKLKDSAADMDIQAVYGVGYKLV
>NZ_LT906468.1|WP_139185449.1|2717136_2719221_+|TonB-dependent-receptor
MYLKQLGLISFTTSISLLSANAQTITKDTSINEIAPIEIKAHFNSQAMLDLTTSAKVVTKKLIESQAPSSFLSAINTTSGLRMEERSPGSYRLALRGSMLRSPFGVRNTKIYLDEIPFTDASGNTYLNILDPVGINSIQIIKGPDGSLYGPNSGGVIRFIPEGFGQINNEKSLMISGGSFGLFHEQLQINHQVNENYNFSFDQAYLRSDGYRQHTAMDKLFFQTAHQWKYNAYGKLKGFALYSDMGYQTPGGLTQQQYDEDPTQFRPAGGPFPSAKDQKAAIYNKTFIGGLSNEYQISNRLKNVVSVFGSYTDLENPFITNYETRTEKNLGFRTYFSYENRDKEDFLWEMQLGGEGQKGWYNVNNYKNNLGVRGSQTDDDYLENLQHFYFYRFKTKLYQKLTAEASIGLNFNNINFKKSAEGEDNVNGEINFDKSWMPRLGLSYAATENFALRASISKGYSTPTIAEVRSSDNKINQNLNAETGINYEAGIRFETHDRRFIADLAAYNYQMDNAIIRQLNEAGNEFFQNAGKIDQKGIEAQILTQLIANENAQFLNGLILSSNLTYQDYKFKDYVIGENNFNGNKVTSVPNWIWANTLSFKFIKDIDLNLLHNFTSSIPLNDANTVSASKYHVLQAKISWLTPISSKYKLQVFTGADNILDEKYSLGNDINAMGNRYFNAAPTRNFYAGVKVIM
>NZ_LT906468.1|WP_093097108.1|2715808_2717098_+|BamA/TamA-family-outer-membrane-protein
MRIKLSLLLLFVLAQLPSFALQIQIHDTVSTKEQRDSVLPTAHLYDIVDAFRDINPFKKDNKKPSGKRSAISYLPNINYNPSIGAQIGIKAVGGKVLGNEPNTTMSIAATALSATTRGIIVGYLLHDIYTPGNKWNIKGGAMVAKAVGLDYGLGIGGTLENPTEEELIMNNPERQRFVNRYMAYTINERVYKQLFPGAFVGVGVFFELKRQLSTVGSAENMAPVEIYSRWNNFDPTRVNNNGFMLNMQYMTRDNPNSAYKGYYVDMVLRMNQTWLGSTHNAYQLQTDFRKYWQLSTDRPNHVIAFWNFGSYNLGGKLPYIDLPGTAKDTYARSGRGYTMGYFKGSSFFYSEVEYRYPILRNQFLSGVVFANIQTANDQMGTKLFQTWQPAAGAGLRLLFNKATRTNLCIDYAFGKFGQHGLFLGLNEAF
>NZ_LT906468.1|WP_093097106.1|2714819_2715710_+|1-aminocyclopropane-1-carboxylate-deaminase/D-cysteine-desulfhydrase
MHLPFQIFSPEEEIIDPIFEEKEIRLFIKRDDKIHPFISGNKWRKLKYQLEYAKSKDISHLVTFGGAWSNHLLACAAASATFGFKAIAYVRGEEVRNPVLDMCRIFGLQLIFVDRESYRNKEKIFSENHDSKTSLFIDEGGKSELGLLGCADIIKELNQHYDHIFVASGTGTTVAGLQLGIEQNNFHSQVHSIPVLKGADSLLQDFSQWNIDPQKIYMHLDYHFSGYAKTKPELIEFIKNFVSSTGIMIEPTYTGKLMYGVYDLIQKGYFKSKSKILVIHTGGITGLLGHLDLFSK
>NZ_LT906468.1|WP_093097103.1|2713723_2714755_-|RluA-family-pseudouridine-synthase
MVDHLDNEQEEQELYEHLRIVADKGQALLRIDKFLMNRVENTSRNRIQNAIDAGTVKVNDKVIKASYKVKPFDVITVVLPDPPRDTEVYPEDIPLDIIYEDDDVLLVNKEAGMVVHPGFNNYTGTLVNALTFHLNQLPTLPGNTGRPGLVHRIDKDTSGLLVIAKNEWAMTFLAKQFFEHSIARKYVALVWGDIAEDGTVSGYIGRNLKDRRIMDMYDDEEKGKWSVTHYRVLERLGYVTLIECQLETGRTHQIRAHMKSIGHPLFNDESYGGDKILKGTSFSKYKQFVENTFALLPRQALHAKSLGFIHPKSKEFLHFEVPMPEDFRLALEKWRSYSSINQS
>NZ_LT906468.1|WP_093097100.1|2712850_2713708_-|aminotransferase-class-IV
MPTHFINYNGTVVPQDMAILDVDSRAFRYGDGIFETMLWKDGDIRFLDLHLERLQESLSMLHFDDADQFNAFFIRSKVEELLRKNSMVGQQARVRLIVFRQGGGLYSPESNKAAYILQVDRKPETLRDKKTGLIIDIYTEYKKAYSELSKIKSNNALIYVMAGLFKKKNAFDEVLILNQSGNLCEALASNIFIYYDKVLYTPALSEGCIAGVMRRVVMDMAQEQGIEVVEAEIKPDIVKVADEIFCTNAVEGIQWVMGYKHKRYFNKVSRIFQDRLLSWSYETEE
>NZ_LT906468.1|WP_093097098.1|2712387_2712846_+|hypothetical-protein
MSKYLANRFREVMLSGTWIANTNWQKELKDVNLDLAMKKIPNINRIYDLTFHVLYYIKGINHFFKSGQLDIKDSLSFPSSELLNDEEWQQLKDELMDQSELFAKSIEDLHESKLQEKFFDEKYGSYIRNIDGQIEHAYYHLGQVILLKKMLM
>NZ_LT906468.1|WP_093097124.1|2723052_2723787_-|SIMPL-domain-containing-protein
MKNTGIIISIIAGLSIIVFAMIFGNAYKYKYKNSNTINVTGNAMTNFESDIVKWSAVFSRKSMDLSEASEQLKRDRELVKDFLVRQGINEKEILFNAVNIARDFNYHTDQNGNSFNTFTGYSLSQNVSIESKDLDKVANASREISTLISQGVELASNAPNYYFSGLEDLKLKLISEASQNAKVRAENIAKEAGSSLGSLVKADLGIFQITGQNENEEYSYGGAFNVTSRKKTANITVKTSYLSE
>NZ_LT906468.1|WP_093097126.1|2723886_2726682_+|S9-family-peptidase
MKRKFGLILLGLSAISLTYAQKKPIDHTVYDSWNVISKPEISKSGNLILYSITPQEGDATAILKNANNQNLIQIPRGADLKLTKDEKHLVSLIKASFQEVRQAKIKKKKPDEMPKDSLLVFNIAKNQTNKFGQVKSYKIARNGNDFVAFLHETKLPSTSDSSKTKSGSKKDKPTSTLTVLNLNTADTSNILKADSYEWSDDGKFLVYSIKGPEKDSLNESGLFIMDLANKSKKKISSGKGNYKNIQFDDATKQLSFLADKTAEKSLLKEFKLYYYTASQDSAVILADRNSNGIPQNWFVSGDGALTFSKSGKRLFFGLAPIPRVKDTTLVEFEHAKVDIWHWQDDYLQPMQLVNLKRDLSRNYTAMINLASNRNVIPLSDETFNRISLTGDADNEWAMATSDKEYRIETQWEGGMRSDIYAISTLTGKNKLVTKSNSGYASLSPNGDYIVYFNRSNGNWYSFNIASETSKQLNEGLPVSFVDEENDVPAAPGPYGIAGWSKDGKNIYINDRYDIWKLSLDGKTKTNLTNGQGRQNQMVYRIEELFKNDDPRINHNQIDESKTVFLNGFNKIDKIQGLYKLGKKDISKLWSGPHTYRMLSADEKLNKIIYTKEDYQHSPDLYLLANFKNETRLSDINPQQANYNWGTAELVHWTTPKGYKSEGILYKPEDFDPNKKYPIIAYFYETLSDGLYTYQAPAPTPSRLNIPYFVSNGYLVFAPDIRYETGYPGRSAEEFINSGMHFLARNNNWVDSTKMGIQGQSWGGYQVAHLITRTNMYAAAWAGAPVVNMTSAYGGIRWGTGMSRQFQYENTQSRIGKPLWEARDLYIENSPLFFMDKVNTPVAIMHNDNDGAVPWYQGIEFFTALRRLNKPVWLLNYNGDDHNLIQRQNRKDIQIREAQFFDHFLKGKAAANWIKKGVKATEKGIDWGLEVD
>NZ_LT906468.1|WP_093097129.1|2726884_2729074_+|glutamine-synthetase-III
MLNSRLSAVETASKHMFNETTEVNSERAIHIFNKNVFSISKMRDYLPKSTFSELKSSIDEGKQISRELADFIAQAMKTWALENGASHYTHWFQPLTGSTAEKHDAFFEPDSDGSAIEKFNADALVQQEPDASSFPNGGIRNTFEARGYTAWDPSSPAFIFETGAGKTLCIPTVFVSYTGESLDYKAPLLKAIASIDKAATDVAQYFDKAVTKVNASLGIEQEYFLVDLALYNARPDLQLTGRTLFGHMSAKGQQLEDHYFGAIPERVLAYMVDLENEALKLGIPLKTRHNEVAPSQFECAPMFEEINLAIDHNQLLMNVMEQVAIRHNFKVLLHEKPYSGVNGSGKHNNWSLITNTGVNLLSPGKTPKNNLMFLTFFVNTIKAVYEHADLLRASIASHSNDHRLGANEAPPAIISIFLGSQLDEILEEVESARVAKKVKADANLWHGIPKIPDLKLDNTDRNRTSPFAFTGNKFEFRAVGSSANSALPMTILNAIVATQLIEFKTEVDKQIKKGIKKDLAILNVVRKYIKDSKAIRFEGNGYSEEWEIEAAGRGLSNIKSTPKALDVYVKPESLELFETLGIFSRRESEARHEILLENFFKKLQIEARVIGDVVTSQIAPACLIYQNQLIENVKGLKDLGLSKEAYSSQLNYVERISKHVNIILEQAEEMRQARKKANTIEDMREKAIAYDEVVKPFFDEIRYHVNKLEKIVDDAKWPLPKLRELLFIH
>NZ_LT906468.1|WP_139185450.1|2729858_2730080_-|hypothetical-protein
MPLTHRMGQELVLSQDEMDKRMDQELVLNQDEMDKRMDQELVLNQDERDERMSQELVLNQDGMDWRMDQDHYA
>NZ_LT906468.1|WP_093097137.1|2730228_2730681_-|antibiotic-biosynthesis-monooxygenase
MEIKLNLRYLLGFILVFSFGNLFSQEKAVDLGGNKQIHLVRMAEIEVIPEYWEEYKEILLYGARESVEKEEGVISIFPMEIQAEKYKIRILEIHRDQKAYEDHIKSKHFQHYKTTTLKMIKDLKLVDMNALDVGLIKKIFIKEGIAEEKR
>NZ_LT906468.1|WP_093097798.1|2730743_2731775_-|aldo/keto-reductase
MEINKDSSLNFQETGKRLLGSGKHQLEVSAFGLGCMGMSYHRSFVPDRQVSINLIRKAAELGINFFDTAEAYGPWINEELVGEALQPIRKEILIATKFGFVDGTPAKGLDSRPETIRKVVDQSLKRLKTDYIDLLYQHRVDPNVPMEDVAGTVKELIQSGKVRNFGLSEASAENIRKAHAVQQVTALQSEYSLVTRQPETTVIPVCEELGIGFVPYSPLSRGLITGYINERTKYNANNDNRPALPRYQKDAIIANWTLIDALKDFGDLRGLTVAQVALAWLLAQKPFIVPIPGTTKLAHLKENFDSREFQFKPEELKELTAALDKIKIVGERAVGQQASQINN
>NZ_LT906468.1|WP_093097139.1|2732071_2732908_+|MBL-fold-metallo-hydrolase
MKLHSIDTGFFKLDGGAMFGVVPKSLWQRTNPADENNLCTWANRLMLIEDGKRLTLVDTGIGDKQDEKFFSHLHMHGDDTLDKSLAKLGFHRDDITDVVLTHLHFDHCGDAIKKEGDKLLPAFKNARYWSNKEHWEWAVNPNPREKASFLKENIMPIQESGQLNFIDIESPQYDTEIQMRFAYGHTEAMMLPQIQYKGKTILYMADLLPSVGHIPIAYVMGYDVRPLVTMQERQDYWKEIVDNEYIMFFEHDSVNECATLQYTEKGIRLKDTFKLSEI
>NZ_LT906468.1|WP_093097142.1|2732915_2733884_+|YafY-family-transcriptional-regulator
MSVDIKKRFDRIVEILIQLQSKRVVKAQELADRFDVSLRTIYRDIKSLEQAGVPLIGEAGMGYSIMDGYRLPPVSFSKEEALCFVATEKLAEKYLDQAGFSLYSSALMKIKAILKSNDQDMVTNMQEQIIMRKQHVPIFPEKVPHVLSSTIEAIANKTQIQIEYQGIKDDEAILRIIEPIGIVHEIGFWYIVAYCLQRMDFRQFRSDRIAQVTALENKFSKRHISIEEYMSNQKSPELPKIKSKILVSRDFAPFIRWQRNTYGYVSEAKVGDKIEMVFESRDIEHEFPRWLMMFGDHIEIKEPEELKHSFNKLFQAIQNNIK
>NZ_LT906468.1|WP_093097800.1|2733893_2735252_-|Gfo/Idh/MocA-family-oxidoreductase
MGNINLNRRQFIFGTGALLSIAALQQAGFAAEILKARTVALIGAGWYGKSDLFRLLQVSDVEVVAVCDVDKKHLEEAAELISQKQKSKKVPKKYSDYRKLLAENKLDLVLVGTPDHWHALIGIAAIESGAHVYLQKPISVDVLEGEAVVAAARKHNRKVQIGTQRRSTPHMIDAKENIVEKGLLGKISHVEMCCYYHMKSNANPPEEPVPDFLDYEMWTGPAPLRPYDGLPHGGWWRAFMEYGNGITGDMCVHMFDTVRWILGLGWPKKISATGGIYVQKEAKSNIADTQTAIFEYDDLNCVWTHRTWGTPADPEFPWAFVIYGDKGTLKGSTMKWEFIPTKGEKIVRDVVYEREKYPEDLKEPRIELNAAPATRGQMRNLLSAIDTNTLPVADVLQGHISTASCILANLSMELNRPLVYDPEKKVCVGDEEATKRLKREYRAPWKHPYQGA
>NZ_LT906468.1|WP_139185451.1|2735324_2735552_+|hypothetical-protein
MRYEIWDIFWRNMYSVSGGVNQDVRDGRIDQERGMNQDSMDGRIDQDQFQSSSGNSDSIGELTQQELTLIREHIT

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Crispr_ID: NZ_LT906468_17

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LT906468_17

2869897-2869984

Orphan

Consensus_repeat	Method
AGGATAAGAGGATGGGCCAAGAT	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_LT906468_17

>merge|NZ_LT906468|17|2869897-2869984|CRISPRCasFinder
AGGATAAGAGGATGGGCCAAGATCGGGGTGGAACCAGGATGTGGGTCGACTCCGCTCGCCAACCAAGGATAAGAGGATGGGCCAAGAT

>NZ_LT906468|17|17|2869897-2869984|CRISPRCasFinder
AGGATAAGAGGATGGGCCAAGAT	CGGGGTGGAACCAGGATGTGGGTCGACTCCGCTCGCCAACCA
AGGATAAGAGGATGGGCCAAGAT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LT906468.1\|WP_093097380.1\|2881146_2882421_-\|adenosylmethionine--8-amino-7-oxononanoate-transaminase	unknown	unknown	gnl\|CDD\|273109
NZ_LT906468.1\|WP_093097366.1\|2871268_2872324_+\|endonuclease/exonuclease/phosphatase-family-protein	unknown	unknown	gnl\|CDD\|377028
NZ_LT906468.1\|WP_093097376.1\|2876622_2879802_-\|SusC/RagA-family-TonB-linked-outer-membrane-protein	unknown	unknown	gnl\|CDD\|274948
NZ_LT906468.1\|WP_093097358.1\|2864169_2864595_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906468.1\|WP_093097816.1\|2870720_2871215_+\|N-acetyltransferase	unknown	unknown	gnl\|CDD\|224168
NZ_LT906468.1\|WP_093097359.1\|2866042_2866795_+\|class-I-SAM-dependent-methyltransferase	unknown	unknown	gnl\|CDD\|369777
NZ_LT906468.1\|WP_093097362.1\|2868233_2868497_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906468.1\|WP_093097373.1\|2874238_2874856_-\|protein-tyrosine-phosphatase	unknown	unknown	gnl\|CDD\|319973
NZ_LT906468.1\|WP_093097368.1\|2872338_2873142_+\|class-I-SAM-dependent-methyltransferase	unknown	unknown	gnl\|CDD\|379312
NZ_LT906468.1\|WP_093097370.1\|2873194_2874238_-\|ACR3-family-arsenite-efflux-transporter	unknown	unknown	gnl\|CDD\|213563
NZ_LT906468.1\|WP_093097356.1\|2862760_2863924_-\|acyl-CoA-dehydrogenase-family-protein	unknown	unknown	gnl\|CDD\|173849
NZ_LT906468.1\|WP_093097382.1\|2882402_2883401_-\|biotin-synthase-BioB	unknown	unknown	gnl\|CDD\|215219
NZ_LT906468.1\|WP_093097364.1\|2868760_2869387_+\|transcriptional-regulator	unknown	unknown	gnl\|CDD\|225222
NZ_LT906468.1\|WP_093097354.1\|2860636_2862736_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|236864
NZ_LT906468.1\|WP_093097378.1\|2880179_2881079_+\|SH3-domain-containing-protein	unknown	unknown	gnl\|CDD\|273068
NZ_LT906468.1\|WP_093097361.1\|2866938_2867469_-\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|366181
NZ_LT906468.1\|WP_093097351.1\|2857685_2859134_+\|bifunctional-2-methylcitrate-dehydratase/aconitate-hydratase	unknown	unknown	gnl\|CDD\|181845
NZ_LT906468.1\|WP_093097374.1\|2875072_2876611_-\|SusD/RagB-family-nutrient-binding-outer-membrane-lipoprotein	unknown	unknown	gnl\|CDD\|378943
NZ_LT906468.1\|WP_093097814.1\|2869397_2869733_-\|phosphoribosylpyrophosphate-synthetase	unknown	unknown	unknown
NZ_LT906468.1\|WP_093097350.1\|2856504_2857662_+\|2-methylcitrate-synthase	unknown	unknown	gnl\|CDD\|183463

Protein	Function_ID	Function_description	E-value
NZ_LT906468.1\|WP_093097380.1\|2881146_2882421_-\|adenosylmethionine--8-amino-7-oxononanoate-transaminase	gnl\|CDD\|273109	TIGR00508, hypothetical_protein_DESPIG_00326, adenosylmethionine-8-amino-7-oxononanoate transaminase. All members of the seed alignment have been demonstrated experimentally to act as EC 2.6.1.62, an enzyme in the biotin biosynthetic pathway. Alternate names include 7,8-diaminopelargonic acid aminotransferase, DAPA aminotransferase, and adenosylmethionine-8-amino-7-oxononanoate aminotransferase. The gene symbol is bioA in E. coli and BIO3 in S. cerevisiae. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin].	0
NZ_LT906468.1\|WP_093097366.1\|2871268_2872324_+\|endonuclease/exonuclease/phosphatase-family-protein	gnl\|CDD\|377028	pfam03372, Exo_endo_phos, Endonuclease/Exonuclease/phosphatase family. This large family of proteins includes magnesium dependent endonucleases and a large number of phosphatases involved in intracellular signalling. This family includes: AP endonuclease proteins EC:4.2.99.18, DNase I proteins EC:3.1.21.1, Synaptojanin an inositol-1,4,5-trisphosphate phosphatase EC:3.1.3.56, Sphingomyelinase EC:3.1.4.12, and Nocturnin.	3.93434e-27
NZ_LT906468.1\|WP_093097376.1\|2876622_2879802_-\|SusC/RagA-family-TonB-linked-outer-membrane-protein	gnl\|CDD\|274948	TIGR04056, OMP_RagA_SusC, TonB-linked outer membrane protein, SusC/RagA family. This model describes a distinctive clade among the TonB-linked outer membrane proteins (OMP). Members of this family are restricted to the Bacteriodetes lineage (except for Gemmatimonas aurantiaca T-27 from the novel phylum Gemmatimonadetes) and occur in high copy numbers, with over 100 members from Bacteroides thetaiotaomicron VPI-5482 alone. Published descriptions of members of this family are available for RagA from Porphyromonas gingivalis, SusC from Bacteroides thetaiotaomicron, and OmpW from Bacteroides caccae. Members form pairs with members of the SusD/RagB family (pfam07980). Transporter complexes including these outer membrane proteins are likely to import large degradation products of proteins (e.g. RagA) or carbohydrates (e.g. SusC) as nutrients, rather than siderophores. [Transport and binding proteins, Unknown substrate].	1.02667e-180
NZ_LT906468.1\|WP_093097351.1\|2857685_2859134_+\|bifunctional-2-methylcitrate-dehydratase/aconitate-hydratase	gnl\|CDD\|181845	PRK09425, prpD, bifunctional 2-methylcitrate dehydratase/aconitate hydratase.	0
NZ_LT906468.1\|WP_093097816.1\|2870720_2871215_+\|N-acetyltransferase	gnl\|CDD\|224168	COG1247, COG1247, Sortase and related acyltransferases [Cell envelope biogenesis, outer membrane].	2.74187e-49
NZ_LT906468.1\|WP_093097359.1\|2866042_2866795_+\|class-I-SAM-dependent-methyltransferase	gnl\|CDD\|369777	pfam08241, Methyltransf_11, Methyltransferase domain. Members of this family are SAM dependent methyltransferases.	8.4587e-17
NZ_LT906468.1\|WP_093097373.1\|2874238_2874856_-\|protein-tyrosine-phosphatase	gnl\|CDD\|319973	cd16345, LMWP_ArsC, Arsenate reductase of the LMWP family. Arsenate reductase plays an important role in the reduction of intracellular arsenate to arsenite, an important step in arsenic detoxification. The reduction involves three different thiolate nucleophiles. In arsenate reductases of the LMWP family, reduction can be coupled with thioredoxin (Trx)/thioredoxin reductase (TrxR) or glutathione (GSH)/glutaredoxin (Grx).	1.57598e-07
NZ_LT906468.1\|WP_093097368.1\|2872338_2873142_+\|class-I-SAM-dependent-methyltransferase	gnl\|CDD\|379312	pfam13649, Methyltransf_25, Methyltransferase domain. This family appears to be a methyltransferase domain.	2.02432e-16
NZ_LT906468.1\|WP_093097370.1\|2873194_2874238_-\|ACR3-family-arsenite-efflux-transporter	gnl\|CDD\|213563	TIGR00832, Uncharacterized_transporter_slr0944, arsenical-resistance protein. The Arsenical Resistance-3 (ACR3) Family (TC 2.A.59) The first protein of the ACR3 family functionally characterized was the ACR3 protein of Saccharomyces cerevisiae. It is present in the yeast plasma membrane and pumps arsenite out of the cell in response to the pmf. Similar proteins are found in bacteria, often as part of a four gene operon with an regulatory protein ArsR, a protein of unknown function ArsH, and an arsenate reductase that converts arsenate to arsenite to facilitate transport. [Cellular processes, Detoxification, Transport and binding proteins, Anions].	2.66426e-143
NZ_LT906468.1\|WP_093097356.1\|2862760_2863924_-\|acyl-CoA-dehydrogenase-family-protein	gnl\|CDD\|173849	cd01160, LCAD, Long chain acyl-CoA dehydrogenase. LCAD is an acyl-CoA dehydrogenases (ACAD), which is found in the mitochondria of eukaryotes and in some prokaryotes. It catalyzes the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of LCAD 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. LCAD acts as a homodimer.	7.19475e-144
NZ_LT906468.1\|WP_093097364.1\|2868760_2869387_+\|transcriptional-regulator	gnl\|CDD\|225222	COG2345, COG2345, Predicted transcriptional regulator [Transcription].	3.04467e-53
NZ_LT906468.1\|WP_093097354.1\|2860636_2862736_-\|hypothetical-protein	gnl\|CDD\|236864	PRK11154, fadJ, fatty acid oxidation complex subunit alpha FadJ.	6.21563e-96
NZ_LT906468.1\|WP_093097378.1\|2880179_2881079_+\|SH3-domain-containing-protein	gnl\|CDD\|273068	TIGR00418, Threonine--tRNA_ligase, threonyl-tRNA synthetase. This model represents the threonyl-tRNA synthetase found in most organisms. This protein is a class II tRNA synthetase, and is recognized by the pfam model tRNA-synt_2b. Note that B. subtilis has closely related isozymes thrS and thrZ. The N-terminal regions are quite dissimilar between archaeal and eubacterial forms, while some eukaryotic forms are missing sequence there altogether. . [Protein synthesis, tRNA aminoacylation].	0.00709836
NZ_LT906468.1\|WP_093097361.1\|2866938_2867469_-\|GNAT-family-N-acetyltransferase	gnl\|CDD\|366181	pfam00583, Acetyltransf_1, Acetyltransferase (GNAT) family. This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.	0.00284209
NZ_LT906468.1\|WP_093097382.1\|2882402_2883401_-\|biotin-synthase-BioB	gnl\|CDD\|215219	PLN02389, PLN02389, biotin synthase.	3.40746e-171
NZ_LT906468.1\|WP_093097374.1\|2875072_2876611_-\|SusD/RagB-family-nutrient-binding-outer-membrane-lipoprotein	gnl\|CDD\|378943	pfam12771, SusD-like_2, Starch-binding associating with outer membrane. SusD is a secreted starch-binding protein with an N-terminal lipid tail that allows it to associate with the outer membrane.	6.23371e-104
NZ_LT906468.1\|WP_093097350.1\|2856504_2857662_+\|2-methylcitrate-synthase	gnl\|CDD\|183463	PRK12351, PRK12351, methylcitrate synthase; Provisional.	0

>NZ_LT906468.1|WP_093097814.1|2869397_2869733_-|phosphoribosylpyrophosphate-synthetase
MEPRNRKSYDTLSEAVNDLQSMGYVEDFVIQEEGECLFCVGRSMELSPEQFVIDEIYRFEGMTDPGDESILFAISSTDNLIKGLVINSFGADFSFTASRLVEELNRRSRND
>NZ_LT906468.1|WP_093097364.1|2868760_2869387_+|transcriptional-regulator
MKKSNSDKIIMLMKMRGEIDAACIAEELGISKEGARQQLLKLSEEGLVHGVCKKSGVGRPFTFYSLSQTGLAKFPDNHADITVQLLQSIKSLLGDNALDLLITDREKSSYLRYEEKLKGSKSISDKLKKLAQIRSEEGYMAEWKKEGQTYYLIENHCPICAAATECQQFCRAELKNFRALLGEDLEVNRVKHILADDNRCVYKIEKKQ
>NZ_LT906468.1|WP_093097362.1|2868233_2868497_-|hypothetical-protein
MENYILSFRAPLNALLQRQQIFEKLAREYPQLGPISIDMDDKQYVMNVHAPGRLENDIQNTLLSYGFRVAFLKADLIKVLDPKVKIA
>NZ_LT906468.1|WP_093097361.1|2866938_2867469_-|GNAT-family-N-acetyltransferase
MSKEQFSGFTFRKALPEEAELIWSIMQEAIDKRREEGSNQWQDGYPNLDVVKTDIEKGYGYVSIDPRGKLTGYLALIFDGEPAYEAIADQWLTNRPFSVVHRIAVSQANYVKGQATWMLEEAQKLSFDNGYLSLKVDTNFDNTGMLRVLEKLGYVYCGEVYFRGSARKAFEKKLDD
>NZ_LT906468.1|WP_093097359.1|2866042_2866795_+|class-I-SAM-dependent-methyltransferase
MATFSDNFSKQASIYAQFRPSYPHELYDYLSNLTPAHDLAWDCGTGNGQSAIHLADFYNQVYASDPSEAQIKNAFEHEKVTYHVEKAEEPSLPEHAVDIITVAQAIHWFDIDKFYEAAKKVLKKDGIIAVWAYAVPQVDKNIDPITQNFHDKTVGPYWPSEIKLLQQGYTTIPFPFREIEPPEFYIHKKYKLQDFLGHLLSWSATQRYIQQEERNPLFKLKEELVPFWKDEEEAKQVTWKIIMRVGKLPS
>NZ_LT906468.1|WP_093097358.1|2864169_2864595_-|hypothetical-protein
MEIPNNTLEGQDLERKLQDVAANCFTTSKNLENLSVEQRSQIINLFERIKYKDIIDQGFWSLGGGLTHYKLSLNEIKLTLLEVLSSRSDDKERLILKEMFLFLNILDEPSFYQLFALRQLIHCPEEIFDEKIKEISGNYFE
>NZ_LT906468.1|WP_093097356.1|2862760_2863924_-|acyl-CoA-dehydrogenase-family-protein
MLSTPISPEHQFFRESLRSFIKKEILPHIDEWESTCKIDKAIWRKMGEMGYLGLIYPEEYGGLDLDFYYSLIFCEELSYCFSGGFTISALVIEYMSAPYLLKYGSTFLKEKYLSRVISGELVSAIAITEPGAGSDVQNIKTTAIDQGDYFLVNGSKTFITNGYYGDFYITVVKTDPKAGSSGISLLLIDKGSEGLTTNKIQKLGWHASDTAELGFDNVKVPKDHLIGELGKGFKYLMGGLQLERLTAAIHSLATAESAVEYTLNYLKERSAFNKQLKDFQVIRHRVSQMMADIEVLKSFVYHCCDLENQKKYAVKECSIAKLQCSELAIKIVGECLQLFGGYGFTEDYKISRLYRDVRVGTIIGGTSEIMLEILSKIFIDEVDYEKR
>NZ_LT906468.1|WP_093097354.1|2860636_2862736_-|hypothetical-protein
MSKIKERIKEQISVSKNADGVYQLRWINVRSRPHDLSLDEFKFCIELLLSVLKKSDCTSLQLILEGKFRDADYEELIYMAGKEGFLTKLEHIDEMIIELSEIEKPTVVLFDKACTGLAAAFLLLFDRRIGIGPKAKMGFPEGAFGMLTGNGSFSKLLGLVDAEFVFDLLNSGRLIKPEEAEKTGLIQDRISSWEQVQAWLQENSALNKSHKFKWKVDQGKLSEAIQKLNAKAIKPLLLTEVILSLIQGSEGQSYKELLTKEHLAYVGLLTAKETLTRVRTFHYAVEDAISMCKEVEDAEISKVAVIGAGMMGSGIAYEVAKAGIDVILKDVDLQNAEKGRAYSEKLCNKLIELNKMKEDDKPKILERILPTDQLEDLDGAEIIVEAVFEDKRLKAEVINDSKRYLAQSGLFASNTTSLPISKLSKSFDDPSRFIGLHFFSPVDRMALVEVIRGKETSEETLDKALSFVGKLKKIPIVVNDGPAFFTSRIFFYYLLEGITMLLEGVPMERIEEGAKLAGFAVGPLAVLDEISLPLMVHVYEQLPDMSFSQKRVYNYLQRMIKKGRTGRKSSRGFYDYPDNKPKKYYSDPELKDLDSQISAKDIQDRLLAVLALDSYRCLEEGILFSPIDGDLGSVMGLGYPVQTGGVFGYIDMIGLDEFVKICENFSQYGDEWEIPDSLVKLRDEGFQFYDGFESNWVDE
>NZ_LT906468.1|WP_093097351.1|2857685_2859134_+|bifunctional-2-methylcitrate-dehydratase/aconitate-hydratase
MSSHISNNRPNPDQVLVDIADYILDFKINSDLALKTAHYCFLDTIGCGFEALTYPACTKLMGPIVPGTVVPNGAKVPGTPFQLDPIQAAFNIGAMVRWLDFNDTWLAAEWGHPSDNLGGILAVADWISRNRIAAGKKPLVMLDVLESMIMAHEVQGVLALENSFNKVGLDHVILVKVASTAVVSKLLGLNREELINALSLAFVDGQSLRTYRHAPNTGSRKSWAAGDATSRAVRLALIAQKGEMGYPSVLTAPVWGFYDVSFKGNPFKFQRPYGTYVMENVLFKISFPAEFHSQTAVEAAMTLHQQLKDAGKTSDDIKSIKIRTHEAAIRIIDKKGPLHNPADRDHAIQYMVAVPLIFGRLTAADYEDNIASDPRIDALREKITCFEDPQFTKDYHDPEKRSIANALTLELNDGSIFEEVVVEYPIGHRRRRDEGIPKLIEKYKINLARVFAEKQQKTILENTLDYDKIKDIPVHELVDLMV
>NZ_LT906468.1|WP_093097350.1|2856504_2857662_+|2-methylcitrate-synthase
MKEANESGFKPKKSVALSGVPAGNTSLCTVGKSGNDLHYRGYDILDLAEQATFEEVAYLLIHEHLPTSKELETYQQKLIKDRGLPDPLKEVLKLIPEFAHPMDLLRTSVSVFGNLEPEPLQHEVETTRNIIDRLMASMGSALLYWYHYSHNQKEIDVKTDDATIGGHFLHLLHGKKPSDSWVHAMQVSLNLYAEHEFNASTFTARVIAGTGSDIYSCIAGAIGALRGPKHGGANEVAYEIQERYANADEAEADIKKRLANKEVIIGFGHPVYTIADPRNQVIKKIAKKLSEESGDMRLFDIAERIETVMWDEKRMFPNLDWFSAVAYHLMGIPTDMFTPLFVMSRISGWGAHVIEQRQDGKIIRPSANYTGPENREFIPLADRKN
>NZ_LT906468.1|WP_093097816.1|2870720_2871215_+|N-acetyltransferase
MKFREANYADLNQIVEIYNTTIASRMVTADLEPVSVESRNNWFYEHNAKHRPLWILEMENNTVGWLSFQSFYGRPAYNATAEISIYLDPTVRGMGLGKTALEYAISQAPGLGIKTLLGFIFSHNQPSLKLFQHFGFEEWANLPNIAQLDDTERGLIIMGKRIIP
>NZ_LT906468.1|WP_093097366.1|2871268_2872324_+|endonuclease/exonuclease/phosphatase-family-protein
MEIALIVFGSLLIIFTILPLIRLDYWTFRVFEYPRIQKLALSVLWIILYLIHADFHNSLLLVFGILILINIIYLLKQILPFTPLGKKQVYKADMIDDKNSLKVMISNVYEDNDDYKGCLSVVHSNKPDLLLLLETSHEWDRQTQSLETDYKYQVKIPIDNTYGMLFYSKFPIHNAEVKYLVEDEIPSIDCQIELPSGQLVQVFAVHPTPPVPNENPRSTERDKELLIVAEKAKKCDLPVIVIGDLNDVAWSYTTELFLKMSELLDPRRGRGFYNTFHAKQPLMQFPLDHAFISADFKLRELKKLDNYNSDHFPIFVHIQFEKSAEEEQEDNQLEANQEDKEMAAEKRNADT
>NZ_LT906468.1|WP_093097368.1|2872338_2873142_+|class-I-SAM-dependent-methyltransferase
MNEQHNYKEINKNLWNQKTAAHVDSDFYDNDGFLKGKSSLNPIEIELLGDVNGKKILHLQCHFGQDSLSLARLGAKVTGLDLSDRAIEQAQKINDQLGLDAQFICSDVYDAPASLNGLFDIVYTSYGTIGWLPDLNRWAEVISRCLKPDGELVFVEFHPVVWMFDYDFSKFQYSYFNDGAIIEVQEGTYADRNADIVAEEVSWNHSLSEVFQGLLNNGLQIESFAEYDYSPYNCFKNTVEIEAGKYQIKGLEKTIPMLYSITARKKS
>NZ_LT906468.1|WP_093097370.1|2873194_2874238_-|ACR3-family-arsenite-efflux-transporter
MNSKLKFLDRYLTLWIFLAMAIGVTIGKMFPSSSQWINHFQTGSTNIPLAIGLILMMYPPLAKVKYEHIGKVFRNIKVLTTSLILNWVIGPVLMFVLAILFLNGYPEYMTGLILIGLARCIAMVVVWNELAEGNREYAAGLIALNSIFQVILYSLFAYFFITVLPPYFGVAGISVDISILEIAKSVGIYLGIPFLMGIISRYTLIAIKGEDWFQNKFIPFISPITLISLLFTIIVMFSLKGEMIVQLPLDVLRVAIPLVIYFAIMFVVSFLAGKRVGADYSQSTAIAFTAAGNNFELAIAVAIAVFGINSGQAFVGVIGPLVEVPALIALVNLAFWFRKKYFMVKPV
>NZ_LT906468.1|WP_093097373.1|2874238_2874856_-|protein-tyrosine-phosphatase
MNANLTNSINQLNWKGFDNSSRKETLKPLIDFIQHKTDAKEKININFICTHNSRRSHLSQIWSQTAAAYFNIPHVNCYSGGTEETSLFPAVIDTLKPQGFEIFKLSESENPIYAIKYARTDPPIIGFSKKHDHPFNPASGFAAIMTCSQADAGCPFIAGAEKRIPITYEDPKISDGSPEQAAVYASRSLQIAEEMFYVFSQIKAE
>NZ_LT906468.1|WP_093097374.1|2875072_2876611_-|SusD/RagB-family-nutrient-binding-outer-membrane-lipoprotein
MKIKHILYTSLLSLSFISCSKDTLQEINVDPNRPSNVPTPSLFLSAERQVVNALRSESIHFRGAQLFAQYFSQNIYTDQSRYLISASYSDEYWTNTYKALSNLNEIIVLNEDEATKVQAQANGAGANSTQIAIARILKSFAFHSLTDVFGDIPYESYGNKDADFEALKRNPDILTPKYASQEKIYKDILNELKIAADTLAKYKSGVTFGTSDIVYQGKNEKWFKFANSLRLRLANRILTKDRALATQHIEDALKKGVFTSNADNAGFTYSSASPYEAPLFRATVTANRKDFAVSHVLIDVLKGNRGPFKIEDPRLNKYAKPNSKNIYKGQPYGLPLAAGNLFPLDSISLPGDLVNKANAVEVLQEYSEVEFLISEYKGWEQASYENGVKASLERWGASPAEVTAYLAKVPKANKENVLSQKYLALYGQGIESWTEIRRTGYPLFLVKKGDVVWSGTVEGKPVSYSFVPEIGDAIPSRLVYPLKEQSTNKTNYQSALSNQGDDVQFTKIWWNK
>NZ_LT906468.1|WP_093097376.1|2876622_2879802_-|SusC/RagA-family-TonB-linked-outer-membrane-protein
MNRTIYFYLVGLFFAIGIGQTQAQNIIKGKVLNELNQAISGATVIDKTTQKQTQTNAAGEFSIDSSNPKTQIKVRFLGYQDQDLEVGASESNTIKLVPSNDVLEEVVVTALGISREKKALGYAVQEVKSTELQTRPTNAMAALSGKVAGLQIVSSGGNMGGSTRTLLRGINSIAGSNQPLYVVDGTPIDNSDLNSSSTINGSAGKDVGNMIQDLNPDDIENISVLKGPSAAALYGSRASNGVILITTKRAGKGEQVSIDLNTGLEFENIVRLPKRQHLYGQGYSQNFQTVNIEGQDYKIVDYAADESWGPKLDGTPVLQWYNLNPEDAADYLNPSPWIYPEHDVSYFFNTGLANTNNLAIAGNSGNTNYRFSYTNKNVKGTVPNSTLGRNTLNFSGGTKLGKLSINSSINYIHNTSLGKPWTGASNRNIILEAFQWGAVQVDYKRLENYKRPDGTPLAWNRTGWQNTPAAEATRFIDNPYWSAYESYLEEKRDRFYGNIGAQYEVTDWLQIGAKVHGDIYQFGTQDRIAVYSRSASQYEETSNKLNEYNYEFLATAKKNWDKISLVANVGANLRDQNRKVDYAITQGGLIVPNYYNLKNASSVKIENFTYNRRIASLYGSASFGYNDLLFLDATVRNDWSSTLPSHANSFIYPSFTGSFVFSQLPVIQNLDWLSFGKVRLGWAQVGNDTDPYQLNKVYDVEQSFDGKPSNKLPSTLNNADLKPEITSSWETGLNLQFFKNRLGFDVTYYHNTSRNQILPIPVSSAFGYEAKVLNAGKVENKGIEVILNATPVRTEDFEWNSSINWARNRNKVLKLDELVNTLTLSSTLINLVAREGQPYGQLLGYDFVYADGQRVIKEDGTYQRTSQLVPLGSVLPDYLFGFQNSFRYKNFNFGFLIDGRVGGSFYSQTYNVGMYSGILERTAENNVREDGIILEGVKADVVFNADGTYSTSNIRPNDTRITAQQWGRNESSGPTTFSIFDGTFVKLREVTLGYTIPLNNPKVVKGVRLSAYARNVWNIYTKSKYIDPEFTNSSGNVQGIEGGNIPTPLTYGFNVNLKF
>NZ_LT906468.1|WP_093097378.1|2880179_2881079_+|SH3-domain-containing-protein
MKYFSTLLILFTLLSLHPQQLKAQEAAAYLVYDDFNLYHTSKDSSALVFVNMAYVRSEPSSKSELLDSIPLGTEVKFMEESSLNPISLRGMYLPWHKIEYHKDNQKKSGFIWLGLLSLDYELNKKSGETFLYGFAWKSNEELENYYWVEAKILNKNKEMIASKSFPYYPGEQSYTLGELNTKPGLNYAKSIYAIKFLGEACGIASEENYFAWDGEQLTTLPKTTSVSDAGVFYYAEELVYPNAHKLGKDIILKRSEEGEAEYEEDANPEAEIKFKVSKKEETYQRNGNAYLKVSEKTIQ
>NZ_LT906468.1|WP_093097380.1|2881146_2882421_-|adenosylmethionine--8-amino-7-oxononanoate-transaminase
MQQQWIDRDVAVNWHPYSQMKTSTHLPIVRGKDAYLFDMEGNRYLDMVSSWWVNLHGHSNSYIADKVYEQLNTLEQVIFAGFTHLPAITLSERLLELLPSNQEKVFYSDNGSTAVEVALKMCIQYAYNQGKQKNKIVAFKDGYHGDTFGAMSVSARGQWTAPFADLLFDVLFIDAPTAENLEANKKIIAEHADQIACFIYEPLVQGAGGMLMHQAEHLSDLMVYCKSQGVLLIQDEVFVGFGRTGTLFAADQLTEKPDVMCFSKGLTGGTMPMGITTCTEELYQAFYSDDKKKALFHGHSFTASPIACAASLASMDLLLLDATQAKIKAIVESHYQFAEELKGYENAKNVRQTGTILAFDWETKSETSYFNRVQEKLFNEFMKRGVLLRPMGNVLYILPPYCTEKEDLEYTYQQILELLNNNDI
>NZ_LT906468.1|WP_093097382.1|2882402_2883401_-|biotin-synthase-BioB
MSASKTLKHDWTKEELLEIYNKPLLELVYEAATVHRQWHNPQEVQISTLLSVKTGGCPEDCSYCGQAARYHTDIKVQALLPTETVLAHAKKAKDSGSSRFCMAAAWREVRDNRDFDRIIEMVQGVNEMGLEVCCTLGMLTEDQANRLQEAGLYAYNHNLDTSEEFYDEIISTRKFDNRIETIKNVRKAGITVCSGGIIGLGEKAEDRISMLRTLANMEKHPESVPINALARVAGTPLENLPKIDTWEMVRMIATARIVLPSSMVRLSAGRIEMNEEEQAWCFMAGANSIFTGERQTLLVTPNPGVDEDMQMLKNLGLRPMEVKKEAVCNSNG

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Crispr_ID: NZ_LT906468_18

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LT906468_18

3787234-3787383

Orphan

Consensus_repeat	Method
AAAAAATAATTGAAATACTGCGGATTGCATTGACGAACAGGTCCT	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_LT906468_18

>merge|NZ_LT906468|18|3787234-3787383|CRISPRCasFinder
AAAAAATAATTGAAATACTGCGGATTGCATTGACGAACAGGTCCTCGAACCACGTTCACAATTATGCCGTTCATCCTGATGTAGGAAGGATCTTGAAACTATACAAAAAAATGATTGAAATACTGCGGATTGCATTGACGAACAGGTCCT

>NZ_LT906468|18|18|3787234-3787383|CRISPRCasFinder
AAAAAATAATTGAAATACTGCGGATTGCATTGACGAACAGGTCCT	CGAACCACGTTCACAATTATGCCGTTCATCCTGATGTAGGAAGGATCTTGAAACTATACA
AAAAAATGATTGAAATACTGCGGATTGCATTGACGAACAGGTCCT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LT906468.1\|WP_093100337.1\|3786909_3787161_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906468.1\|WP_093100341.1\|3791410_3792025_-\|superoxide-dismutase	unknown	unknown	gnl\|CDD\|223678
NZ_LT906468.1\|WP_093100333.1\|3782032_3783058_+\|recombinase-RecA	unknown	unknown	gnl\|CDD\|236476
NZ_LT906468.1\|WP_093100336.1\|3785293_3786772_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906468.1\|WP_093100343.1\|3792592_3792934_-\|tRNA-binding-protein	unknown	unknown	gnl\|CDD\|182232
NZ_LT906468.1\|WP_093100338.1\|3787541_3787907_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906468.1\|WP_093100330.1\|3779252_3780878_+\|S8-family-serine-peptidase	unknown	unknown	gnl\|CDD\|173809
NZ_LT906468.1\|WP_093100329.1\|3776971_3779128_-\|S9-family-peptidase	unknown	unknown	gnl\|CDD\|224684
NZ_LT906468.1\|WP_093100334.1\|3783257_3784445_+\|metallophosphoesterase	unknown	unknown	gnl\|CDD\|365906
NZ_LT906468.1\|WP_093100327.1\|3775428_3776145_-\|N-acetyltransferase	unknown	unknown	unknown
NZ_LT906468.1\|WP_093100483.1\|3796795_3797560_+\|succinate-dehydrogenase/fumarate-reductase-iron-sulfur-subunit	unknown	unknown	gnl\|CDD\|181038
NZ_LT906468.1\|WP_093100344.1\|3792944_3793160_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906468.1\|WP_093100345.1\|3793231_3793810_+\|PorT-family-protein	unknown	unknown	gnl\|CDD\|372635
NZ_LT906468.1\|WP_093100347.1\|3794802_3796737_+\|fumarate-reductase/succinate-dehydrogenase-flavoprotein-subunit	unknown	unknown	gnl\|CDD\|236054
NZ_LT906468.1\|WP_093100328.1\|3776649_3776898_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906468.1\|WP_093100339.1\|3788058_3789696_-\|L-glutamate-gamma-semialdehyde-dehydrogenase	unknown	unknown	gnl\|CDD\|143441
NZ_LT906468.1\|WP_093100346.1\|3793973_3794753_+\|succinate-dehydrogenase-cytochrome-b-subunit	unknown	unknown	gnl\|CDD\|239578
NZ_LT906468.1\|WP_093100342.1\|3792116_3792593_-\|nucleoside-deaminase	unknown	unknown	gnl\|CDD\|223663
NZ_LT906468.1\|WP_093100335.1\|3784570_3785269_-\|ABC-transporter-ATP-binding-protein	unknown	unknown	gnl\|CDD\|224054
NZ_LT906468.1\|WP_093100332.1\|3781230_3781893_+\|endonuclease-III	unknown	unknown	gnl\|CDD\|223255

Protein	Function_ID	Function_description	E-value
NZ_LT906468.1\|WP_093100341.1\|3791410_3792025_-\|superoxide-dismutase	gnl\|CDD\|223678	COG0605, SodA, Superoxide dismutase [Inorganic ion transport and metabolism].	1.21598e-102
NZ_LT906468.1\|WP_093100333.1\|3782032_3783058_+\|recombinase-RecA	gnl\|CDD\|236476	PRK09354, recA, recombinase A; Provisional.	0
NZ_LT906468.1\|WP_093100342.1\|3792116_3792593_-\|nucleoside-deaminase	gnl\|CDD\|223663	COG0590, CumB, Cytosine/adenosine deaminases [Nucleotide transport and metabolism / Translation, ribosomal structure and biogenesis].	1.39502e-51
NZ_LT906468.1\|WP_093100343.1\|3792592_3792934_-\|tRNA-binding-protein	gnl\|CDD\|182232	PRK10089, PRK10089, chaperone CsaA.	4.93025e-68
NZ_LT906468.1\|WP_093100330.1\|3779252_3780878_+\|S8-family-serine-peptidase	gnl\|CDD\|173809	cd07483, Peptidases_S8_Subtilisin_Novo-like, Peptidase S8 family domain in Subtilisin_Novo-like proteins. Subtilisins are a group of alkaline proteinases originating from different strains of Bacillus subtilis. Novo is one of the strains that produced enzymes belonging to this group. The enzymes obtained from the Novo and BPN' strains are identical. The Carlsburg and Novo subtilisins are thought to have arisen from a common ancestral protein. They have similar peptidase and esterase activities, pH profiles, catalyze transesterification reactions, and are both inhibited by diispropyl fluorophosphate, though they differ in 85 positions in the amino acid sequence. Members of the peptidases S8 and S35 clan include endopeptidases, exopeptidases and also a tripeptidyl-peptidase. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin.. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.	4.78231e-111
NZ_LT906468.1\|WP_093100329.1\|3776971_3779128_-\|S9-family-peptidase	gnl\|CDD\|224684	COG1770, PtrB, Protease II [Amino acid transport and metabolism].	0
NZ_LT906468.1\|WP_093100334.1\|3783257_3784445_+\|metallophosphoesterase	gnl\|CDD\|365906	pfam00149, Metallophos, Calcineurin-like phosphoesterase. This family includes a diverse range of phosphoesterases, including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD or yeast MRE11. The most conserved regions in this superfamily centre around the metal chelating residues.	6.28344e-15
NZ_LT906468.1\|WP_093100483.1\|3796795_3797560_+\|succinate-dehydrogenase/fumarate-reductase-iron-sulfur-subunit	gnl\|CDD\|181038	PRK07570, PRK07570, succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated.	0
NZ_LT906468.1\|WP_093100345.1\|3793231_3793810_+\|PorT-family-protein	gnl\|CDD\|372635	pfam13568, OMP_b-brl_2, Outer membrane protein beta-barrel domain. This domain is found in a wide range of outer membrane proteins. This domain assumes a membrane bound beta-barrel fold.	6.86972e-16
NZ_LT906468.1\|WP_093100346.1\|3793973_3794753_+\|succinate-dehydrogenase-cytochrome-b-subunit	gnl\|CDD\|239578	cd03498, SQR_TypeB_2_TM, Succinate:quinone oxidoreductase (SQR)-like Type B subfamily 2, transmembrane subunit; composed of proteins with similarity to the SQRs of Geobacter metallireducens and Corynebacterium glutamicum. SQR catalyzes the oxidation of succinate to fumarate coupled to the reduction of quinone to quinol. C. glutamicum SQR reduces low potential quinones such as menaquinone. SQR is also called succinate dehydrogenase (Sdh) or Complex II and is part of the citric acid cycle and the aerobic respiratory chain. SQR is composed of a flavoprotein catalytic subunit, an iron-sulfur protein and one or two hydrophobic transmembrane subunits. Members of this subfamily are classified as Type B as they contain one transmembrane subunit and two heme groups. The heme and quinone binding sites reside in the transmembrane subunit. The transmembrane subunit of members of this subfamily is also called Sdh cytochrome b558 subunit based on the Bacillus subtilis protein. The structural arrangement allows efficient electron transfer between the catalytic subunit, through iron-sulfur centers, and the transmembrane subunit containing the electron acceptor (quinone). The reversible reduction of quinone is an essential feature of respiration, allowing transfer of electrons between respiratory complexes. Proteins in this subfamily from G. metallireducens and G. sulfurreducens are bifunctional enzymes with SQR and QFR activities.	1.90751e-58
NZ_LT906468.1\|WP_093100339.1\|3788058_3789696_-\|L-glutamate-gamma-semialdehyde-dehydrogenase	gnl\|CDD\|143441	cd07123, ALDH_F4-17_P5CDH, Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17. Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), families 4 and 17: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), also known as ALDH4A1 in humans, is a mitochondrial homodimer involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. Also included in this CD is the Aldh17 Drosophila melanogaster (Q9VUC0) P5CDH and similar sequences.	0
NZ_LT906468.1\|WP_093100347.1\|3794802_3796737_+\|fumarate-reductase/succinate-dehydrogenase-flavoprotein-subunit	gnl\|CDD\|236054	PRK07573, sdhA, fumarate reductase/succinate dehydrogenase flavoprotein subunit.	0
NZ_LT906468.1\|WP_093100335.1\|3784570_3785269_-\|ABC-transporter-ATP-binding-protein	gnl\|CDD\|224054	COG1131, CcmA, ABC-type multidrug transport system, ATPase component [Defense mechanisms].	1.14349e-56
NZ_LT906468.1\|WP_093100332.1\|3781230_3781893_+\|endonuclease-III	gnl\|CDD\|223255	COG0177, Nth, Predicted EndoIII-related endonuclease [DNA replication, recombination, and repair].	4.898e-98

>NZ_LT906468.1|WP_093100337.1|3786909_3787161_+|hypothetical-protein
MNQDWVRLRSPNEDGRTDQDLGMNQDGWDGRTDEDYDMNQDSWDKRMDQDYDMNLVSLTIFDPKFVGAYSISPHPILNIISFH
>NZ_LT906468.1|WP_093100336.1|3785293_3786772_-|hypothetical-protein
MFKRLFLLEWRSFFRSADLGKSLSVRLLLAFLGIYFLGSAVTFGVSLHFLISELFPNQVPIHFVGKFLLYWFFLSFLIRLMMQKLPILNVKPLLVLNIPRSNIVNYTLLKSSNSFWNWMLLAVVVPYLIITARVTDFTNFQLLAWCIAVVGFEYVINYLNLYVQQNFDNGVLKTLPILALLAIIFGLDYFEIYSVSGLFGQYFDLVLQYSVLCLAAVVLAVLSYFLLYHDVKKNLFLDAYLQKERSVVKNYDLSWTNRFGELAPFLQLDMKLIWRSKRARTVIYSCLIFVLYGLLFYPQKEGNPTSLVFVGVFITGIFVINFGQFVPAWDSTYYAMLMTQNMPIKLYLESKAMLMYLSIAIMTVLSTGYLYFGWIIVWVNIACAIYNLGVNVPVILYFGSMNRKRIDLDNGNIFNYQGTGAAQWLVGIPLLIAPIIIWAIAYYAGGIHVANITLIVIGLIGFAMRNEILNRIAKKYQENKYKILIGFKEVNN
>NZ_LT906468.1|WP_093100335.1|3784570_3785269_-|ABC-transporter-ATP-binding-protein
MIEIKDIIKSYNGIRVLNIPSLHIGKGESVGVVGNNGAGKTTMFSLILDLIQPDSGEILLNGIPVHGQDGWKKFTTAFIDDSFLIGYLTPEEYFYFLGELRGMNKSDVDALLAEHAEFFNGEVLDKKVYVRDLSKGNQKKVGIVGALIGNPDLIILDEPFANLDPTTQFRLKKLIAKIRENKDVTLLISSHDLSHTVETADRIIALNMGLVVKDGIKTEETLAELNSFFAVE
>NZ_LT906468.1|WP_093100334.1|3783257_3784445_+|metallophosphoesterase
MSFNRRNFLKGIGLIGLGASTPAYAEKLVPKQNAAFSLACPPYLQNLNAETVTICAIFNKPCLAWIEVLDANNNTLKSVYQVEDGMRNANAELFKFQVNHKNGQLKYKVVAKEISKFEPYKIEYAGTIQSEPFDITLPQPKQDSIHCLILNDIHEDKDSYTYLFDKSKLAKKDLVFLNGDSFHYVTNQADLTEKLLKPVGNKFASTIPFLMIRGNHETRGAFARDYKKYFDYPENKFYQAFRMGPIYWIILDSGEDKPDDHEVYAGTVDYDNYRLEQKEWLSKVLQSKERKEAKHTLVITHIPFHHSDDWHGTKHNYECFHDILNSNKVDAVISGHTHKYSFHPPDNSHNYYVIIGGGPKAGNRTYVDITAQGKTLQVSLNLDDGSTINRFSKNV
>NZ_LT906468.1|WP_093100333.1|3782032_3783058_+|recombinase-RecA
MSNSDKLKALQLTLDKLEKNYGKGTIMKLGDTAVEPIEAISTGSLGLDIALGIGGVPKGRIIEIYGPESSGKTTLATHIVAEAQKKGGIAAIIDAEHAFDKYYAQKLGVDIENLLISQPDNGEQALEIADNLIRSGAIDVIVIDSVAALVPKGEIEGEMGESKMGLQARLMSQALRKLTGTISKTNCCCIFINQLREKIGVMFGNPETTTGGNALKFYASVRLDIRRTSQIKDSDEVSGNRVKVKIVKNKVAPPFRIAEFDIMFGEGISKVGEIIDLGVEYGIVKKSGSWFSYGDTKLGQGRDAVKTLLLDNPDLMDELEHKIRAEVSGVDLDQAAIREED
>NZ_LT906468.1|WP_093100332.1|3781230_3781893_+|endonuclease-III
MLIKERYKAFVEYFSTHNPDAQTELNYGNPFELLIAVILSAQCTDKRINQVTPALFERYPNPESLAASSSDEVFTYIKSVSYPNNKAKHLVGMAQKLLSEFHGEIPEKVEDLVKLPGVGRKTANVISSVVFHNPAMAVDTHVFRVADRIGLTNKATTPLAAEKQLVKHLPKDTIAMAHHWLILHGRYICLARSPKCDICPISYFCRYFERNKKAKLVHKD
>NZ_LT906468.1|WP_093100330.1|3779252_3780878_+|S8-family-serine-peptidase
MIGTNKFLCYLALGILPTLGFSQDKTATPPANWYNLDFQKDGVMGISTEKAQELLKGKKATPVVVAVLDGGVDIQHEDLKDVLWTNPKEIPGNGKDDDGNGYIDDVHGWNFIGGKDGLNVNQDNLEVTRLIRIYEPKYISVLPTTPLSEKERREFVAYQKMITDYTSKMEEASFGKLNYGRLKNEVDAVIKKIGKEPKDITKADLDAFQPEGDQQKMAVRIAKKELDNGSFDKFYTDINDAVTYFTDQADYHLNKEFDPRHVVGDNYEDASQRDYGNPDVKGPDAEHGTHVAGIIGAKRNNNKGVNGVADNVQIMAVRLVPNGDERDKDVANGIRYAVDNGARVINMSFGKGYAYNKKAVDEAIKYAESKDVLLVHAAGNDSQDNDIEKNYPTKYFTDSVDAIVGEAKNWITVGATGLKQDADLLASFSNYGYRSVDVFAPGVKINSTIPESKYKENQGTSMAAPVVAGLAAMIRAYYPSLTAEQVKDVIMKSVTKVDQKVKIKKDGNTKRVYLDEISVSGGIVNAYNAIVEANKLVSEKK
>NZ_LT906468.1|WP_093100329.1|3776971_3779128_-|S9-family-peptidase
MKDKYVIGLILSIMISSCSSDNKVQKEPLNWPDSSAPIAEKKAHERIIHGDTVSDPYYWMIDYFKKGADSAQVVAYLEAENKYTEAMMKDTESFQDILFKEMKGRIKETDESVPYLKNGYYYYQRTEEGKQYFKLCRKKGSLDAKEEVLLDVDKMAEGFAYYAIGGATVSPDNKLLAFSVDTVSRREYVIQFKNLETGELLADKIVRTSGGSVWASDNKTIFYTSKNPVTLLSEKIKRHTLGTDAGSDAVVYEEKDNTNYIGVSKSKNDQYIFIYSGGTLSSETRYIKADEPNAEFKVFQPRMKDVLYDVTPLADKFLIVTNDNAQNFKVMETPLDKTTKENWKEYIPHRQGVLVQGIDEFANYVAISERKNGLTQLAIRNLKDNSQHYLDFGEAAYTVYPSTNAEYNTDVIRYGYTSMVTPSSTFDYNMKTKDKTLMKQQEVLGGYDMKNYVTERVMAKVADGTEVPISIVYKKGTKKDGTAPLLLYAYGSYGNSMDPSFSSSRLSLLDRGFIYALAHIRGGEEMGRQWYEDGKMMKKKNTFTDFIDCGKFLIDQKFTAKEHLYAQGGSAGGLLMGAVINMSPEIWNGVIAQVPFVDVVNTMLDESIPLTTNEYDEWGNPNNKEAYDYMKSYSPYENIEAKEYPNLLVTTGLHDSQVQYFEPAKWVAKLRATKKGNNVILLKTDMDYGHGGASGRFDYLKDVALSYAFLFKLEGITK
>NZ_LT906468.1|WP_093100328.1|3776649_3776898_+|hypothetical-protein
MVGPSIFFYALFVIPYILFMYWLVKQDKKKYMWGVIVVTVVAIFGLVVSQRASKIAMENYKQHQIDAREIEAENRADSLNHK
>NZ_LT906468.1|WP_093100327.1|3775428_3776145_-|N-acetyltransferase
MTISDFLIIPATANHVKYADEVCNEMFESAKARGTGIARRKPEYVARKMEEGKAVIALHKDGTWAGFCYIETWSHGDYVANSGLIVNPQFRKVGLAKAIKKRVFDLSREKYPNAKIFGLTTGLAVMKINSDLGYEPVTYSELTQDEEFWKGCQSCVNFDILVSKDRKNCMCTAMLWDPVEKEKELKEKILRKAEAKERLDRISKKQSLLKRIEAKLWRSTKKMVAAVIPVGIRPVKGF
>NZ_LT906468.1|WP_093100338.1|3787541_3787907_+|hypothetical-protein
MREPFFIVYALKVELQKNISPLSRVPNFTNINPSAGTPLAPGSIPVAEKWKECRCLCDGIGLGILSEVHPIKRGDLLKDIPDNKAFYPCAGARAKSHLKWAEAFWLLLRSKSNEESIFCFF
>NZ_LT906468.1|WP_093100339.1|3788058_3789696_-|L-glutamate-gamma-semialdehyde-dehydrogenase
MLKGFFTVPTPANEPVYSYAPGTKERSLLKEAIAAARATEIDIPMYIGGEEVRTSKKVKITPPHDHKHVLGYFNQGTKENVKEAIDAALAAKNDWENLPWEQRAAIFLKAAELISTKYRYKLNAATMLGQSKNPYQAEIDSACEIADFLRFNVKYMSEIYQQQPPINPKNVWNRIEQRPLEGFVFALTPFNFTAIAGNLPTSAAMMGNVVVWKPANTQIYSANVLMEIFREAGVPAGVINLVYVSGPDAGDVIFKHPDFAGIHFTGSTGVFQDIWKTIGENIHLYKTYPRIVGETGGKDFILAHPSADLDVLNTALVRGAFEFQGQKCSAASRAYVPKSLWKELKEKMERDIKSFKIGGTEDFSNFINAVIDEKAFDKITKYIDRAKESKDAEVVIGGEYDKSKGYFINPTVIVAEKADYETMSEELFGPVLTIYVYDDKKWAETLKLVDTTSIYALTGSIISQDRYAIEEATHYLRNAVGNFYINDKCTGAVVGQQPFGGARGSGTNDKAGSMINLLRWVSPRTIKETFNPDVDYRYPFLSEEL
>NZ_LT906468.1|WP_093100341.1|3791410_3792025_-|superoxide-dismutase
MAFELEALPYPADALEPSIDKETMIIHHDRHHQAYVDNLNKAIAGTDAENLSLEEILKNVSKYPAAVRNNAGGVWNHDLFWKVLGPNAGGEPTGDLANDINAAFGSFAELKKKLQEAGAGRFGSGWSWLIVGQDGKLAVTSTPNQDNPLMDVAEVKGTPIFGIDVWEHAYYLKYQNKRPAYLEEIFNVVNWDDVAKRYAEAKKG
>NZ_LT906468.1|WP_093100342.1|3792116_3792593_-|nucleoside-deaminase
MKVYNFEENPQAGIPNLDEQYMQEALKLAKKAFEEDEIPIGAIIVSNGKIIGKGYNMTERLNDVTAHAEMQAFTAAANYLGGKYLKDCTLYVTVEPCVMCAGASYWTQISKIVYGARDEKRGYSSIHEKIIHPKTIIQSGVLETECAELMMSFFRNKR
>NZ_LT906468.1|WP_093100343.1|3792592_3792934_-|tRNA-binding-protein
MEKLISWEEFEQVDLRVGTILEVSDFPKARRPAYQLLVDFGEEIGTRKSSAQITAHYSKEELIGKQVVAVLNFPKKQIANFMSECLVTGFEDENGDIILTSVERKVPNGAKLK
>NZ_LT906468.1|WP_093100344.1|3792944_3793160_-|hypothetical-protein
MYNFKISADEWPILKLKLKRKYNTLSEEDLQFSPGQEEELLKRLAKRLNRNVDYVVFTLSKELTDLESNRL
>NZ_LT906468.1|WP_093100345.1|3793231_3793810_+|PorT-family-protein
MKKILLGLAALFFCVQATQAQLLPSLKLGIKGAVNFSSLKSDGSWLNSDTKAGFQAGIWGRVGVAGFHVQPELYYAQKKAGYETEDGTNSEATFKSVDLPVLLGTRIGLGPIGVRIQAGPVFSFAHDGDIKSVANTDAYKKSSTGIIGGVGADISKFTVDLRYEHGLSNISKDNAHKQKISMWSIGVGYSFL
>NZ_LT906468.1|WP_093100346.1|3793973_3794753_+|succinate-dehydrogenase-cytochrome-b-subunit
MSKSKPVLTSSLGKKLIMSLTGLFLCTFLIVHLIGNLQLFKDDAGYAFNNYAYFMTHFTPIKVVSYLLYLSIIVHAVYALILTIKNKAARPIGYNQYDGNANSAWNSRNMGILGTVLLIFIVTHMQNFWFQYKFGTTPYVEYRTELSTGNQEVLQLDDIPSDYNGYVQYQDAGFEVVKSKDLYRQVAVTFQNPLLVGLYVIAMAALAFHLIHGFQSAFQTIGFNHRRYKGIIRTIGIWVFGIIIPILFASMPLYFYFVK
>NZ_LT906468.1|WP_093100347.1|3794802_3796737_+|fumarate-reductase/succinate-dehydrogenase-flavoprotein-subunit
MLDSRVPSGPLAEKWSKHKFEMKLVNPANKRKFTIIVVGTGLAGASAAAALAELGYNVKTFCYQDSPRRAHSIAAQGGINAAKNYQNDGDSVYRLFYDTVKGGDYRAREANVYRLAEVSVNIIDQCVAQGVPFAREYGGLLDNRSFGGAQVSRTFYARGQTGQQLLLGAYSALNRQIEAGKVKSYTRHEMLDLVKIDGEARGIITRDLITGEIEAHEGHAVLLCTGGYGNVFFLSTNAMGCNVTAAWRAHKRGAFFANPCYTQIHPTCIPVTGDHQSKLTLMSESLRNDGRVWVPKTVELAEKLRKGELKPKDIKEDDRDYFLERKYPSFGNLVPRDVASRNAKEMVDEGRGVGKTGVAVFLDFAEAIQRLGKDVVEAKYGNLFDMYYQITDENPYEQPMRIYPAVHYTMGGVWVDYNLMTTVPGLYCLGEANFSDHGANRLGASALMQGLSDGYFVIPYTVGDYLAKIGNFKPVDKNNPAFEQTRKEVEERINKLLALKGSKTVDDIHKKLGHIMWEYCGMARTAEGLQKAKGLIQDLRKEFWSDAKVLGENEELNMSLEKAGRVADFLELGELMVDDALNRNESCGGHFRVESQTEEGEAKRNDDEYAYVAAWQYNGDNQPEILHKEELVFENVKLTQRSYK
>NZ_LT906468.1|WP_093100483.1|3796795_3797560_+|succinate-dehydrogenase/fumarate-reductase-iron-sulfur-subunit
MNLTLKVWRQKNSNDKGQFVTIQAKDIADDMSFLEMLDVVNEDLTRQGEDPIYFDHDCREGICGMCSLVINGRPHGPKYGITTCQLHMRSFHDGQTIVIEPWRAAAFPVLKDLAVDRTSFDRIQQAGGYININTGGPQDANNILIPKRIADEAFESATCIGCGACVAACKNASAMLFVSAKISQFALLPQGQTERYERAQAMVDQMDAEGFGNCTNTGACEAECPKGIKLTNIARMNREYFTAKFFRQEDVHQH

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Self-targeting detection

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_ID	Protospacer_location	Mismatch	Identity
NZ_LT906468_7	7.1\|1227466\|38\|NZ_LT906468\|CRISPRCasFinder	1227466-1227503	38	NZ_LT906468.1	503313-503350	1	0.974

1. spacer 7.1|1227466|38|NZ_LT906468|CRISPRCasFinder matches to position: 503313-503350, mismatch: 1, identity: 0.974

ccaaaccgacgaaggagctcacggataccaatctcatt	CRISPR spacer
ccaaaccgacgaaggagctcacggataccgatctcatt	Protospacer
*****************************.********

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity
NZ_LT906468_3	3.1\|946616\|26\|NZ_LT906468\|CRISPRCasFinder	946616-946641	26	NZ_CP047244	Trichormus variabilis 0441 plasmid unnamed2, complete sequence	201221-201246	5	0.808
NZ_LT906468_3	3.1\|946616\|26\|NZ_LT906468\|CRISPRCasFinder	946616-946641	26	NC_003240	Nostoc sp. PCC 7120 = FACHB-418 plasmid pCC7120beta, complete sequence	14574-14599	5	0.808
NZ_LT906468_3	3.1\|946616\|26\|NZ_LT906468\|CRISPRCasFinder	946616-946641	26	NC_007412	Trichormus variabilis ATCC 29413 plasmid C, complete sequence	38302-38327	5	0.808
NZ_LT906468_2	2.1\|619451\|30\|NZ_LT906468\|CRISPRCasFinder	619451-619480	30	AP013772	Uncultured Mediterranean phage uvMED isolate uvMED-CGF-C39-MedDCM-OCT-S34-C80, * SEQUENCING IN PROGRESS *	25381-25410	8	0.733
NZ_LT906468_2	2.1\|619451\|30\|NZ_LT906468\|CRISPRCasFinder	619451-619480	30	AP013773	Uncultured Mediterranean phage uvMED isolate uvMED-CGF-C39-MedDCM-OCT-S42-C70, * SEQUENCING IN PROGRESS *	12178-12207	8	0.733
NZ_LT906468_2	2.1\|619451\|30\|NZ_LT906468\|CRISPRCasFinder	619451-619480	30	AP014445	Uncultured Mediterranean phage uvMED isolate uvMED-CGF-C39-MedDCM-OCT-S35-C62, * SEQUENCING IN PROGRESS *, 4 ordered pieces	14145-14174	8	0.733
NZ_LT906468_2	2.1\|619451\|30\|NZ_LT906468\|CRISPRCasFinder	619451-619480	30	NZ_LR214986	Mycoplasma cynos strain NCTC10142 plasmid 13	642023-642052	9	0.7
NZ_LT906468_4	4.1\|992301\|32\|NZ_LT906468\|CRISPRCasFinder	992301-992332	32	NZ_AP022593	Mycolicibacterium arabiense strain JCM 18538 plasmid pJCM18538, complete sequence	98748-98779	9	0.719

1. spacer 3.1|946616|26|NZ_LT906468|CRISPRCasFinder matches to NZ_CP047244 (Trichormus variabilis 0441 plasmid unnamed2, complete sequence) position: , mismatch: 5, identity: 0.808

cgccttttcaaacatccaaattctac	CRISPR spacer
ctaattttcaatcatccaaattctag	Protospacer
*   ******* *************

2. spacer 3.1|946616|26|NZ_LT906468|CRISPRCasFinder matches to NC_003240 (Nostoc sp. PCC 7120 = FACHB-418 plasmid pCC7120beta, complete sequence) position: , mismatch: 5, identity: 0.808

cgccttttcaaacatccaaattctac	CRISPR spacer
ctaattttcaatcatccaaattctag	Protospacer
*   ******* *************

3. spacer 3.1|946616|26|NZ_LT906468|CRISPRCasFinder matches to NC_007412 (Trichormus variabilis ATCC 29413 plasmid C, complete sequence) position: , mismatch: 5, identity: 0.808

cgccttttcaaacatccaaattctac	CRISPR spacer
ctaattttcaatcatccaaattctag	Protospacer
*   ******* *************

4. spacer 2.1|619451|30|NZ_LT906468|CRISPRCasFinder matches to AP013772 (Uncultured Mediterranean phage uvMED isolate uvMED-CGF-C39-MedDCM-OCT-S34-C80, *** SEQUENCING IN PROGRESS ***) position: , mismatch: 8, identity: 0.733

tacttttgcgcttcaaaagtaacaatagaa	CRISPR spacer
tctagtaatgcttcaacagtaacaatagaa	Protospacer
* .  * ..******* *************

5. spacer 2.1|619451|30|NZ_LT906468|CRISPRCasFinder matches to AP013773 (Uncultured Mediterranean phage uvMED isolate uvMED-CGF-C39-MedDCM-OCT-S42-C70, *** SEQUENCING IN PROGRESS ***) position: , mismatch: 8, identity: 0.733

tacttttgcgcttcaaaagtaacaatagaa	CRISPR spacer
tctagtaatgcttcaacagtaacaatagaa	Protospacer
* .  * ..******* *************

6. spacer 2.1|619451|30|NZ_LT906468|CRISPRCasFinder matches to AP014445 (Uncultured Mediterranean phage uvMED isolate uvMED-CGF-C39-MedDCM-OCT-S35-C62, *** SEQUENCING IN PROGRESS ***, 4 ordered pieces) position: , mismatch: 8, identity: 0.733

tacttttgcgcttcaaaagtaacaatagaa	CRISPR spacer
tctagtaatgcttcaacagtaacaatagaa	Protospacer
* .  * ..******* *************

7. spacer 2.1|619451|30|NZ_LT906468|CRISPRCasFinder matches to NZ_LR214986 (Mycoplasma cynos strain NCTC10142 plasmid 13) position: , mismatch: 9, identity: 0.7

tacttttgcgcttcaaaagtaacaatagaa	CRISPR spacer
gataaagaagcttcaaaagaaacaatagaa	Protospacer
 *.    . ********** **********

8. spacer 4.1|992301|32|NZ_LT906468|CRISPRCasFinder matches to NZ_AP022593 (Mycolicibacterium arabiense strain JCM 18538 plasmid pJCM18538, complete sequence) position: , mismatch: 9, identity: 0.719

atacgattggtgtcactgagctccttcgtcgg	CRISPR spacer
ctgcagaaggtgtcactgagcttcctcgtcga	Protospacer
 *.*..  **************.*.******.

Prophage detection

Region	Region Position	Protein_number	Hit_taxonomy	Key_proteins	Att_site	Prophage annotation

Anti-CRISPR protein detection

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

Overview of predicted results

Overview of the results

Cas Category Instructions

Results visualization

1. NZ_LT906468

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CRISPR-Cas detection and classification

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Self-targeting detection

MGE targeting detection<

Prophage detection

Anti-CRISPR protein detection