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
CP024175	Bordetella bronchiseptica strain A345 chromosome, complete genome	8 crisprs	csa3,DEDDh,DinG,cas3,PD-DExK	3	0	2	0

Results visualization

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CRISPR-Cas detection and classification

Crispr_ID: CP024175_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

CP024175_1

1268649-1268743

Orphan

Consensus_repeat	Method
GCAGGCAGGCCTGCGCAGCGGGTGCCTGG	CRISPRCasFinder

1 spacers

The CRISPR arrays of CP024175_1

>merge|CP024175|1|1268649-1268743|CRISPRCasFinder
GCAGGCAGGCCTGCGCAGCGGGTGCCTGGAGAGAGTGCCTGGCTCCCGCCGCGCGGCTCGTCCCGTGCAGGCAGGCCTGCGCAGCGGGTGCCTGG

>CP024175|1|1|1268649-1268743|CRISPRCasFinder
GCAGGCAGGCCTGCGCAGCGGGTGCCTGG	AGAGAGTGCCTGGCTCCCGCCGCGCGGCTCGTCCCGT
GCAGGCAGGCCTGCGCAGCGGGTGCCTGG

Protein	Signature genes	Signature genes Name	Protein_function
CP024175.1\|AZW29801.1\|1261991_1264094_+\|CoA-binding-protein	unknown	unknown	gnl\|CDD\|223972
CP024175.1\|AZW29796.1\|1257624_1258365_-\|IclR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224332
CP024175.1\|AZW29813.1\|1275667_1276369_-\|riboflavin-synthase	unknown	unknown	gnl\|CDD\|183846
CP024175.1\|AZW29810.1\|1272186_1273089_-\|transcriptional-regulator-GcvA	unknown	unknown	gnl\|CDD\|182990
CP024175.1\|AZW29815.1\|1277772_1278234_+\|Lrp/AsnC-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224439
CP024175.1\|AZW29812.1\|1274252_1275626_+\|amidase	unknown	unknown	gnl\|CDD\|223232
CP024175.1\|AZW29807.1\|1269815_1270511_+\|ankyrin-repeat-domain-containing-protein	unknown	unknown	gnl\|CDD\|223738
CP024175.1\|AZW29809.1\|1271006_1272239_+\|MFS-transporter	unknown	unknown	gnl\|CDD\|340968
CP024175.1\|AZW29814.1\|1276682_1277672_+\|tripartite-tricarboxylate-transporter-substrate-binding-protein	unknown	unknown	gnl\|CDD\|270296
CP024175.1\|AZW29802.1\|1264148_1265120_+\|tripartite-tricarboxylate-transporter-substrate-binding-protein	unknown	unknown	gnl\|CDD\|270234
CP024175.1\|AZW29797.1\|1258493_1259270_-\|citryl-CoA-lyase	unknown	unknown	gnl\|CDD\|235748
CP024175.1\|AZW29800.1\|1260984_1261737_-\|3-oxoacyl-ACP-reductase-FabG	unknown	unknown	gnl\|CDD\|187594
CP024175.1\|AZW29808.1\|1270500_1271010_+\|nucleoside-deaminase	unknown	unknown	gnl\|CDD\|223663
CP024175.1\|AZW29811.1\|1273242_1274214_+\|tripartite-tricarboxylate-transporter-substrate-binding-protein	unknown	unknown	gnl\|CDD\|270296
CP024175.1\|AZW29806.1\|1268875_1269745_-\|LysR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|237907
CP024175.1\|AZW29799.1\|1259789_1260956_-\|acyl-CoA-dehydrogenase	unknown	unknown	gnl\|CDD\|173847
CP024175.1\|AZW29803.1\|1265131_1266181_+\|CoA-transferase	unknown	unknown	gnl\|CDD\|367110
CP024175.1\|AZW29804.1\|1266181_1266805_+\|flavin-reductase-family-protein	unknown	unknown	gnl\|CDD\|224766
CP024175.1\|AZW29798.1\|1259271_1259793_-\|acyl-dehydratase	unknown	unknown	gnl\|CDD\|239530
CP024175.1\|AZW29805.1\|1266726_1268577_+\|acyl-CoA-dehydrogenase	unknown	unknown	gnl\|CDD\|173842

Protein	Function_ID	Function_description	E-value
CP024175.1\|AZW29801.1\|1261991_1264094_+\|CoA-binding-protein	gnl\|CDD\|223972	COG1042, COG1042, Acyl-CoA synthetase (NDP forming) [Energy production and conversion].	4.18224e-121
CP024175.1\|AZW29796.1\|1257624_1258365_-\|IclR-family-transcriptional-regulator	gnl\|CDD\|224332	COG1414, IclR, Transcriptional regulator [Transcription].	9.43869e-43
CP024175.1\|AZW29813.1\|1275667_1276369_-\|riboflavin-synthase	gnl\|CDD\|183846	PRK13020, PRK13020, riboflavin synthase subunit alpha; Provisional.	1.94909e-108
CP024175.1\|AZW29810.1\|1272186_1273089_-\|transcriptional-regulator-GcvA	gnl\|CDD\|182990	PRK11139, PRK11139, DNA-binding transcriptional activator GcvA; Provisional.	5.55784e-93
CP024175.1\|AZW29815.1\|1277772_1278234_+\|Lrp/AsnC-family-transcriptional-regulator	gnl\|CDD\|224439	COG1522, Lrp, Transcriptional regulators [Transcription].	6.17932e-44
CP024175.1\|AZW29812.1\|1274252_1275626_+\|amidase	gnl\|CDD\|223232	COG0154, GatA, Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit and related amidases [Translation, ribosomal structure and biogenesis].	1.2509e-78
CP024175.1\|AZW29807.1\|1269815_1270511_+\|ankyrin-repeat-domain-containing-protein	gnl\|CDD\|223738	COG0666, Arp, FOG: Ankyrin repeat [General function prediction only].	7.41534e-19
CP024175.1\|AZW29809.1\|1271006_1272239_+\|MFS-transporter	gnl\|CDD\|340968	cd17410, MFS_CynX_like, Cyanate transport protein CynX and similar proteins of the Major Facilitator Superfamily of transporters. This subfamily is composed of Escherichia coli cyanate transport protein CynX and similar proteins. CynX is part of an active transport system that transports exogenous cyanate into E. coli cells. The gene encoding CynX is part of the cyn operon that also includes cynS, encoding cynase, which catalyzes the reaction of cyanate with bicarbonate to give ammonia and carbon dioxide, and cynT, which encodes a carbonic anhydrase. The CynX-like subfamily belongs to the 2-nitroimidazole and cyanate transporters like (NIMT/CynX-like) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	1.29905e-95
CP024175.1\|AZW29814.1\|1276682_1277672_+\|tripartite-tricarboxylate-transporter-substrate-binding-protein	gnl\|CDD\|270296	cd13578, PBP2_Bug27, Aromatic solutes transporter of Bug (Bordetella uptake gene) protein family; contains the type 2 periplasmic binding fold. Bug27 binds non-carboxylated solute nicotinamide, in contrast to BugD (aspartic acid transporter) and BugE (glutamate transporter) which both bind aliphatic carboxylated ligands. The Bug (Bordetella uptake gene) protein family is a large family of periplasmic solute-binding (PBP) receptors present in a number of bacterial species, but mainly in proteobacteria. Bug proteins are the PBP components of the tripartite carboxylate transporters (TTT). Their expansive expansion in proteobacteria indicates a large functional diversity.	3.38363e-150
CP024175.1\|AZW29802.1\|1264148_1265120_+\|tripartite-tricarboxylate-transporter-substrate-binding-protein	gnl\|CDD\|270234	cd07012, PBP2_Bug_TTT, Bug (Bordetella uptake gene) protein family of periplasmic solute-binding receptors; contains the type 2 periplasmic binding fold. The Bug (Bordetella uptake gene) protein family is a large family of periplasmic solute-binding (PBP) proteins present in a number of bacterial species, but mainly in proteobacteria. In eubacteria, at least three families of periplasmic binding-protein dependent transporters are known: the ATP-binding cassette (ABC) transporters, the tripartite ATP-independent periplasmic transporters, and the tripartite tricarboxylate transporters (TTT). Bug proteins are the PBP components of the TTT. Their expansive expansion in proteobacteria indicates a large functional diversity. The best studied examples are Bordetella pertussis BugD, which is an aspartic acid transporter, and BugE, which is glutamate transporter.	7.96886e-122
CP024175.1\|AZW29797.1\|1258493_1259270_-\|citryl-CoA-lyase	gnl\|CDD\|235748	PRK06224, PRK06224, citryl-CoA lyase.	8.96117e-110
CP024175.1\|AZW29800.1\|1260984_1261737_-\|3-oxoacyl-ACP-reductase-FabG	gnl\|CDD\|187594	cd05333, BKR_SDR_c, beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs. This subgroup includes the Escherichai coli K12 BKR, FabG. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.	1.64973e-100
CP024175.1\|AZW29808.1\|1270500_1271010_+\|nucleoside-deaminase	gnl\|CDD\|223663	COG0590, CumB, Cytosine/adenosine deaminases [Nucleotide transport and metabolism / Translation, ribosomal structure and biogenesis].	1.36331e-36
CP024175.1\|AZW29811.1\|1273242_1274214_+\|tripartite-tricarboxylate-transporter-substrate-binding-protein	gnl\|CDD\|270296	cd13578, PBP2_Bug27, Aromatic solutes transporter of Bug (Bordetella uptake gene) protein family; contains the type 2 periplasmic binding fold. Bug27 binds non-carboxylated solute nicotinamide, in contrast to BugD (aspartic acid transporter) and BugE (glutamate transporter) which both bind aliphatic carboxylated ligands. The Bug (Bordetella uptake gene) protein family is a large family of periplasmic solute-binding (PBP) receptors present in a number of bacterial species, but mainly in proteobacteria. Bug proteins are the PBP components of the tripartite carboxylate transporters (TTT). Their expansive expansion in proteobacteria indicates a large functional diversity.	4.35657e-136
CP024175.1\|AZW29806.1\|1268875_1269745_-\|LysR-family-transcriptional-regulator	gnl\|CDD\|237907	PRK15092, PRK15092, DNA-binding transcriptional repressor LrhA; Provisional.	1.54399e-44
CP024175.1\|AZW29799.1\|1259789_1260956_-\|acyl-CoA-dehydrogenase	gnl\|CDD\|173847	cd01158, SCAD_SBCAD, Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA dehydrogenases. Short chain acyl-CoA dehydrogenase (SCAD). SCAD is a mitochondrial beta-oxidation enzyme. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of SCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. This subgroup also contains the eukaryotic short/branched chain acyl-CoA dehydrogenase(SBCAD), the bacterial butyryl-CoA dehydorgenase(BCAD) and 2-methylbutyryl-CoA dehydrogenase, which is involved in isoleucine catabolism. These enzymes are homotetramers.	1.07883e-111
CP024175.1\|AZW29803.1\|1265131_1266181_+\|CoA-transferase	gnl\|CDD\|367110	pfam02515, CoA_transf_3, CoA-transferase family III. CoA-transferases are found in organisms from all lines of descent. Most of these enzymes belong to two well-known enzyme families, but recent work on unusual biochemical pathways of anaerobic bacteria has revealed the existence of a third family of CoA-transferases. The members of this enzyme family differ in sequence and reaction mechanism from CoA-transferases of the other families. Currently known enzymes of the new family are a formyl-CoA: oxalate CoA-transferase, a succinyl-CoA: (R)-benzylsuccinate CoA-transferase, an (E)-cinnamoyl-CoA: (R)-phenyllactate CoA-transferase, and a butyrobetainyl-CoA: (R)-carnitine CoA-transferase. In addition, a large number of proteins of unknown or differently annotated function from Bacteria, Archaea and Eukarya apparently belong to this enzyme family. Properties and reaction mechanisms of the CoA-transferases of family III are described and compared to those of the previously known CoA-transferases.	3.04119e-95
CP024175.1\|AZW29804.1\|1266181_1266805_+\|flavin-reductase-family-protein	gnl\|CDD\|224766	COG1853, COG1853, Conserved protein/domain typically associated with flavoprotein oxygenases, DIM6/NTAB family [General function prediction only].	7.59322e-32
CP024175.1\|AZW29798.1\|1259271_1259793_-\|acyl-dehydratase	gnl\|CDD\|239530	cd03446, MaoC_like, MoaC_like Similar to the MaoC (monoamine oxidase C) dehydratase regulatory protein but without the N-terminal PutA domain. This protein family has a hot-dog fold similar to that of (R)-specific enoyl-CoA hydratase, the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit.	3.23961e-45
CP024175.1\|AZW29805.1\|1266726_1268577_+\|acyl-CoA-dehydrogenase	gnl\|CDD\|173842	cd01153, ACAD_fadE5, Putative acyl-CoA dehydrogenases similar to fadE5. Putative acyl-CoA dehydrogenase (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position.	3.79673e-138

>CP024175.1|AZW29805.1|1266726_1268577_+|acyl-CoA-dehydrogenase
MPPRRPLVWRAGRAPGRAGSIHYFNLIAAFSMSQYRAPWDDIEFLLEHVFAPDARDGAALDLDLARSVAHEAAKFAQAFLEPANRAGDQAGARLEQGAVVTPPGFARAYAAFREAGWNGLRHPERFGGQGLSAVLSTLTEEIWHACNASFALCPMLTGGAIEALLAAADPALQARLLPRLVSGEWTGTMNLTEPGAGSDLGAVKTRAVARGDGSYAITGQKIFITYGDHDMAANIIHLVLARTPDAPAGVQGLSLFAVPRQLLRDDGSPGEPNRVACVALEHKLGIHGSPTAVMQFGDDEGATGYLVGALNDGLKTMFVMMNEARQAVGIQGLALSERAYQHAVWYAGERRQGRIVGEDGSRGDTILRHPDVRRLLLGIKCRIDAMRALAIYLALQRDQAHGGAQAQAGAAAQARLDLLVPVMKGWFTETAQRATCDAMQVFGGMGYIEETGAAQYYRDARILTIYEGTTAIQANDLVGRKTARDQGAEARRLLDEIAAAAPPGHDAEGLGEALRAACADLRAAIDAILEQAASAPRAAYAGGVPYLELWGVVAGGWMHALRARAAAHLPQARRQAVLASAGFYARHVLPQAAALRHAIVHGGTQADAYPDDCWVA
>CP024175.1|AZW29804.1|1266181_1266805_+|flavin-reductase-family-protein
MDASRTGLDAAALSARDTYRLLTSCLVPRPIAWVSTCDAQGTGNLAPFSFYTMVSTVPPLIALSISLHQGQEKDTLANIRQTGEFVVNVVTRELLAPMHACGERHAPEVDEAQLLGVQMRPSQRVRPAGVARSPVRLECRLSQVLEFGVHAARLVVGEVLHFSIASEYMRDGRLDGTRLDPVCRLGGPWYGVLGERLAAPDPSITST
>CP024175.1|AZW29803.1|1265131_1266181_+|CoA-transferase
MTHAAPLAGITVVDFSELLPGPFLTQNLLELGATVVKVERPPHGDNARRLYPGVFASVNRGKRSVMLDLKQADGRARARELVAQADVLVEGFRPGVMARLGLDYEQARALNGRLVYVSLSGYGQDGPQARQPGHDINYLAAAGALALAGSDPAEPAPGAGLPVADLCGAMYALSSTLAALLQRQHTGRGQWLDIALADCVMHWMNPRLGQFASAGLATLERQRHDVLCKPAYGVFRTADDAHVAIAALEDHFWQALRGALPLAGLAGPLATYREREAQAGPINDALARAVRGHACQALIDRLTAADVPVSRLEAPGELAQSALARQRGLFDAGDGYVRYPVRLDHMGAA
>CP024175.1|AZW29802.1|1264148_1265120_+|tripartite-tricarboxylate-transporter-substrate-binding-protein
MFNKHAFIAALAALAACVAAPALAQAYPERPIRFVVPFTAGGITDNVARTVGARAAELLGQPIIVENRAGAGGNIGTEYAANSKPDGYVIFLGTQGTQVTNPLLYTSAPSSADRLQAVQGLTAIPNIVVVNAERPYDTLAKLVDYARANPGKLNNSSAGAGTGTHLAAELFQSVVDVKFSHIPFKGSAPSITALIGGQVDLSFDYPVSTEAYVKAGKIRAVAVTGETRLGSLPDVPTLAELGYPQATSVSWMGVFVPAGTPDAVTARLRQAFAAAIAEPQIAAKLVEFGGVPLQKSGADFTAFVQDEAVKWGKVVKAAGVKLD
>CP024175.1|AZW29801.1|1261991_1264094_+|CoA-binding-protein
MFQSLAPLFAPESLVLIGASDRPASIGQRTLVNIVEHSRFDGELFLVNATKDEVMGRRAYRSVLDLPYAPQTAIVVVPAKAAVEVLAECGRKGVRFAIVLSSGFGETGEAGRQLEERMRAIVRETGLRIYGPNCPGMTNNNRGLGFTFSPAYQYDRMAGPIGLVTQGGGLGRTFLQACGRGVGIGLWCSSGNEADLTASDYINHMVAMPEIKVIVALLEGINDPPRFAQAALNAARQGKPIVALKVGKSAYGVQATQSHTAALSGSAEVNSAAFRQLGIVEVDDIDELIDTAALLARGAPTRPIRAAVYSFSGGTVALAADMLGSAGLELSRFEPATRQALADMLPSYAAIDNPVDTTAEILVQSDISYGSLLCVARDPNVDVVLYPIPMEYGDTTLAACRNMVRAQAEVDVPIVPVWMSDKLGAGFQCLVDAGLTPVRTLGKSVKALAHWNRHGQWVRRFERDWEPAVVRSAGAPAHAEPRTYAELEAKQMLAAAGVAVPFGQVCRSADEAVQAAAQCQGPVVAKIVSAQILHKSDIGGVAVGLQTPQQVREAWETISANARAACPDARIDGILVEQMIGGPGVETLVGVHEDPLFGHVMTFGLGGVYVEVFKDVSRRLLPLTPQDARDMIRETRCHRLLQGCRGQAAADIEALERLLLAVSDFVVDGPWHIKELDLNPVLAGPAGATALDAVLIGAPR
>CP024175.1|AZW29800.1|1260984_1261737_-|3-oxoacyl-ACP-reductase-FabG
MDLKIAGKVAVVTGSGRGIGAQTVRTLAEEGARVVVTDINEETARETAARLNADGHEAIGVKCDVCRREDVDALVAAAAKAYGGIDILVNNAGFTRDQYLGKMAEDDWDAVVDTIIKGAFHCSRAVLPGMMQKRWGRIVNIASRSVFGNPGQTNYTTAKLGLVGFTRALSLEQAKFGITVNAIAPGFVETELIQSLPTYERLREGALARNPVGFLGQPGDIADAVAFMASERARYITGVTLYVTGGRFSS
>CP024175.1|AZW29799.1|1259789_1260956_-|acyl-CoA-dehydrogenase
MDFDFDSNQQALRDSIRRYLKAEVAPRIDACEAERRIPQDVLQGLAQFGYIGGLLPEEAGGFDLDFVTWAMMVEEAGYCWGSLRTIVNITNIFLRIVQGHGTAQQRERFLAPVLASEKGVCVAISEPNHGSNVAGIECRADDRGDHYLLNGSKLWITNGVNADYAIVLARTYSDACAGKPSLFLVERAASPYAARLVDKMVLKASGTAELSFDDVRVPKENLLGAEGVALKTMLTGLNYGRLNIAMGAVGAAQAALDLSVEYARTRRQFGRPIGEFQLIQKHIVDMMVRTEAARALGYKAAAAMQKGQPARIECSIAKLYAAEAAHEVARIALSVHGGLGYSTEYPLERIFRDTSGGVIPEGTAEVQTLIVGREVLGMSAINAAEHKA
>CP024175.1|AZW29798.1|1259271_1259793_-|acyl-dehydratase
MTSLDTLAPAALETLRYDWDDLEPGLVVESAARTITESDVVGFAALSGDYNRLHTDAVYAGASKFGQRIAHGMLVASIMSGLNTRTVLNQCLEPSILGLLEMTYRFTRPTFVGDTIKVRITVTARRPSSDPRRGVVEFERLGINQHGDTVCACVAKLLVARRAPSPHLQPNEA
>CP024175.1|AZW29797.1|1258493_1259270_-|citryl-CoA-lyase
MVKTEIGYTTPERITVRGKDLANELLGQVDFVDMMLMTIFGHLPSPAEKTMVNHILVTACDHGLTPSAMSARLTYLGAPEAMQAAVAAGLLGAGSVFLGTTQNCAEILAAGGAGLAPDAPDAEVDAAARALMAASREKKQPIYGIGHPIHIDGDPRVPTLRRLAQELGYYGKHWRLMEAVQRVFLQDKGKNLPMNAVGAVGAIICDMGLDPMIARGLMLVGRAGGLVAHLYEERQDPIGQQLWDLVLAQDPRNVAPAR
>CP024175.1|AZW29796.1|1257624_1258365_-|IclR-family-transcriptional-regulator
MPTFVSAAARAMAVFEVFAREKRELSNSDLARLLELPDSSCLDLLHTLHQLGYLLRTQSRRYYPTGKLLQAAQQISTFDLVVHATRDALEQLSQQTGETAYVGRIEGAAVKIVAVREGRYPLRYILNLGDRIALHASAMGKALLGRLPPDEARKLLKTKQLRKLTATTVTEPEALVEEVVASRERGWYHTRGEGSDGADALAVSGLLSDEPIAIAISGPTDRFSANRDEYIAALRAEAARLFPNDA
>CP024175.1|AZW29806.1|1268875_1269745_-|LysR-family-transcriptional-regulator
MLDPVLLRSFVTVVDTGNFTRASEHLHLTQSTVSQHVIRLEESLGCRLLDRGQRHVLPTEEGERLLGYARSILRLADEARESVAAAQGNAVLRLGAPEDFMGAALMPVLAPLLARYPLLRLEFDSGLSHQLLRRYRDGELDLLLVKQWEVDADCQAHWPEPLCWVAARRGPTLPAGEAVPLVVFPAGALYRQEMTRTLEASGRPWHIRYASTSLAGLVAAVGAGLGVSLLPAASAGGELRVLRKRDGFPAVDGLQLGLYARTRLGAAGRDLRDALAAHCGQRAAAMASA
>CP024175.1|AZW29807.1|1269815_1270511_+|ankyrin-repeat-domain-containing-protein
MFKQGGLGMPIIRFYRCWLAACLVSLGGASAAAGDAGQALLQAAADGDAARVKTLLAGGAPLEARDAQGNTPLLRATQGNHAEAAGALIEAGADVNAQNGIQDSAYLLAGARGYRAILALTLAHGADLKSTNRYGGTALIPACERGHVEVVDMLLRAGVDPDHVNRLGWTGLLEAIILGDGGTRHQAIVARLIEGGADVNLADGDGVSPLRHARQRGQTAIVQLLEAAHAR
>CP024175.1|AZW29808.1|1270500_1271010_+|nucleoside-deaminase
MRADSNSNPGVATLDDDTLLREAIALARANARAGGRPFGALVAKDGVVLARGVNRMLADHDPTAHAELLALREAGRALRSARLDGCVVYASGQPCPMCLAAMRMSGVARAVYAYSNEQAEPYGLSTAALAAELALPPQRQPGFAFEHRPGAAAPDADLYREWQDGPQAP
>CP024175.1|AZW29809.1|1271006_1272239_+|MFS-transporter
MTAPRLGAAPRAWAMLALVALIGLNLRPFLTGPGTVLAGIEADTGLGHLGASMLTVLPMLLMGVGAFLAPAVQARVGTRRGVLAALLALALGSALRLAAWDGALLIATAALCGLGVAYIQAVFPGVIKDRFPGRMAAVMGVYSAMMMGGGALGARLTSRLAGGAGDSWRAALAWLAVPALIAFAAAWRHLAETPAARRDGALAGTLMRRPRTWLLIAAFGLVNGGYSSMVAWLAPAVQAQGWSIAQSGDLMVAMTIAQAAAALTLPALAARRPDRRPWLYATLAMQAMGFAGMAFWPAAAPLAWALIGGAGLGGCFALTFIAALDHFSQAEPAGVLAALMQGGGFLIAGLAPFAVAALRAATGGFAAGWTMHLACVAIACLLYQRLDPARYARVMAAEPGAAATRRVPSA
>CP024175.1|AZW29810.1|1272186_1273089_-|transcriptional-regulator-GcvA
MDGLPPLNAVRTFEVAGRLCSITEAAAELCVTPSAVSRQIRLLEEHLGRKLFIRQHRGVVLTTIGHQYLGDISKALVEVRRATSEAAKPRQRAVFTVRAPHSIAMRWLLPRLARFHAAHPHIDVKLHTSLTPPDFEREDLDAGVMLGRGQWKGLLSHMLIRNELIPVCAPHKARALRTPADLADETLLHVFGRPDDWVAWLGAAGVEHVDVHRGMKYESSALAYEAALEGYGIAIAQKALIDKDLQEGRLVTPFDLSVDQGDYTYYFVLPPEGYKRRSPALDTFRRWVRDVSLPRQAPPP
>CP024175.1|AZW29811.1|1273242_1274214_+|tripartite-tricarboxylate-transporter-substrate-binding-protein
MRLACARWLLACMAPLAGAAAVAETYPARPVTIVVPTTAGGTADILARLIGPKLTALWGQPVVVENRSGAGTLIGTEFAARAQPDGYTLMITYSELATLPALNKNARIDVVKDLTRVGKIGSLPVLILAHPSMPANTMDELVARLRADPGKYSYASNGIGSALQLYTEMFRQAAKVDIMHVPYRGALEASRAVLGGEVDLLVQLGNGNVIGYVTSGKAKAYAVASPQRLAALPDVPTTAEAGLPGLQLEAWYGLFAPAGLPPERVEKLNRDLATVLAMPDIRDRLVSFGMQVQPGTPQQFDAFFHDEYQRWTRLIEDAGIQIN
>CP024175.1|AZW29812.1|1274252_1275626_+|amidase
MNYHPSTHTPLTFHDRTQAFLDGGDSPRDYLERCLDTIARREPVVQGWVVLNEAGAREAADASARRYREGRPLSAIDGMPVGIKDLIETRDMPTQMGSPAYTGNFPKRDSAVVRALREAGAIVLGKTVTTALGFLDPGPTTNAFDPERTPGGSSSGSGAVVGANMVPVAVGSQLVGSMLRPASFNANWVLKPTYGGMNRGERQGFSQSHVGIHAGCAQDMWTTSIEIVRRVGGDPGHPGLYGEAAPPAGRKPARLAVLETEGWERLDAASRAAFEAALERIAGQGVRIVRRADCSLVDGLERAIAQAGALSMRLISWEHHWSLKNMAEQHPGTLGPSLVRQLELGQAMTLERYRHDMLEREAARQRLAALATQCDALVSLASSGPAPRIADLRGTPYPTGDYSFSCVSSLLGAPAISVPALGVDGMPVGLQVIGQPHGDEQVTAIGRWLHALLAAPR
>CP024175.1|AZW29813.1|1275667_1276369_-|riboflavin-synthase
MFTGIVQGTATIAGIADRQGLRTFTIDFPAGFCVDLAIGASVSVDGVCLTVTRIVSADTATFDVMLQSLDITTLGGYAVGARVNVERAARDGAEIGGHPLSGHIDFAAAVERVRNMDNNRVLRIGIPPAFRKYVFAKGYIAVNGASLTVSEVDREEGWFEVWLIPETRRMTVFEEKQAGDALNIEIERSTQVVVDTVREAVQESLGKLQPVLEAILKEKGLSLEDFVRPPALK
>CP024175.1|AZW29814.1|1276682_1277672_+|tripartite-tricarboxylate-transporter-substrate-binding-protein
MKSIQSRLLATWAVCAAAGMLAGPAVASGAAYPTKPVTMIVSFPPGGSSDFFTRLVANNLSKMWGQPVVVENRPGAGGNIGAQAGAHAPADGYTLYMSSINTHAINPGLYQNPGYDHIKDFAPISEIATVMNVLVVNPSVPAKSVSELLAYFKADPSKAFYASPGAGTSPHLSSELFKRMTDTPITHVPYKGSNAALTDVMAGMVPMAIDNLPAALAHIKAGKLRALAVTSPKRSPDLPDVPTMDEAGVKGYDVTTWWALFAPAGTPQPIIAKINKDVNALLALPDVKQSIAKQGAEPAPSTPEELARLVEQETARWGKVIKDAKVTID
>CP024175.1|AZW29815.1|1277772_1278234_+|Lrp/AsnC-family-transcriptional-regulator
MDATDRKIIAILQENAETPIQSIADQVSLSTTPCWRRVQKLKESGVIRRQVALCDPVALNVGVTVFISVKTNQHSQAWLDRFADHVTDIPEVVEFYRMSGDIDYLIRVVVPDISTYDTVYKKLIRIADLHDVSSSFAMEQLKYTTALPVDYAS

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Crispr_ID: CP024175_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

CP024175_2

1556780-1556878

Orphan

Consensus_repeat	Method
GCCGGTGCCAGTCCCCCTTGCGGGGACAGGCAC	CRISPRCasFinder

1 spacers

The CRISPR arrays of CP024175_2

>merge|CP024175|2|1556780-1556878|CRISPRCasFinder
GCCGGTGCCAGTCCCCCTTGCGGGGACAGGCACTTCGCGGATTGGGACAGGCACGCGGGGAGGTTTGCCGGTGCCAGTCCCCCTTGCGGGGACAGGCAC

>CP024175|2|2|1556780-1556878|CRISPRCasFinder
GCCGGTGCCAGTCCCCCTTGCGGGGACAGGCAC	TTCGCGGATTGGGACAGGCACGCGGGGAGGTTT
GCCGGTGCCAGTCCCCCTTGCGGGGACAGGCAC

Protein	Signature genes	Signature genes Name	Protein_function
CP024175.1\|AZW30048.1\|1554610_1556170_+\|acetolactate-synthase-large-subunit	unknown	unknown	gnl\|CDD\|236063
CP024175.1\|AZW30052.1\|1560151_1561039_+\|LysR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|182990
CP024175.1\|AZW33420.1\|1563281_1563683_+\|aryl-sulfate-sulfotransferase	unknown	unknown	gnl\|CDD\|226771
CP024175.1\|AZW30050.1\|1557026_1558283_-\|acyl-CoA-dehydrogenase	unknown	unknown	gnl\|CDD\|173840
CP024175.1\|AZW30046.1\|1553015_1553708_+\|amino-acid-ABC-transporter-permease	unknown	unknown	gnl\|CDD\|223836
CP024175.1\|AZW33419.1\|1562022_1562511_+\|Cys-tRNA(Pro)-deacylase	unknown	unknown	gnl\|CDD\|237976
CP024175.1\|AZW30044.1\|1551269_1552175_+\|agmatinase	unknown	unknown	gnl\|CDD\|212538
CP024175.1\|AZW30053.1\|1561076_1562009_+\|site-specific-tyrosine-recombinase-XerD	unknown	unknown	gnl\|CDD\|234713
CP024175.1\|AZW30055.1\|1563689_1564802_-\|D-alanyl-D-alanine-endopeptidase	unknown	unknown	gnl\|CDD\|236952
CP024175.1\|AZW30040.1\|1546742_1547933_+\|5-(carboxyamino)imidazole-ribonucleotide-synthase	unknown	unknown	gnl\|CDD\|235674
CP024175.1\|AZW30049.1\|1556201_1556747_+\|acyl-dehydratase	unknown	unknown	gnl\|CDD\|239538
CP024175.1\|AZW30042.1\|1549126_1550149_+\|amino-acid-ABC-transporter-substrate-binding-protein	unknown	unknown	gnl\|CDD\|270410
CP024175.1\|AZW30051.1\|1558299_1559994_-\|thiamine-pyrophosphate-binding-protein	unknown	unknown	gnl\|CDD\|181285
CP024175.1\|AZW30054.1\|1562630_1563209_+\|protease	unknown	unknown	gnl\|CDD\|153243
CP024175.1\|AZW30045.1\|1552201_1552993_+\|amino-acid-ABC-transporter-substrate-binding-protein	unknown	unknown	gnl\|CDD\|270248
CP024175.1\|AZW30041.1\|1547937_1548990_+\|L-threonylcarbamoyladenylate-synthase	unknown	unknown	gnl\|CDD\|223088
CP024175.1\|AZW30057.1\|1566894_1569555_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|274682
CP024175.1\|AZW30056.1\|1565488_1566691_+\|MFS-transporter	unknown	unknown	gnl\|CDD\|340913
CP024175.1\|AZW30043.1\|1550240_1551077_+\|IclR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224332
CP024175.1\|AZW30047.1\|1553729_1554482_+\|amino-acid-ABC-transporter-ATP-binding-protein	unknown	unknown	gnl\|CDD\|224051

Protein	Function_ID	Function_description	E-value
CP024175.1\|AZW30048.1\|1554610_1556170_+\|acetolactate-synthase-large-subunit	gnl\|CDD\|236063	PRK07586, PRK07586, acetolactate synthase large subunit.	0
CP024175.1\|AZW30052.1\|1560151_1561039_+\|LysR-family-transcriptional-regulator	gnl\|CDD\|182990	PRK11139, PRK11139, DNA-binding transcriptional activator GcvA; Provisional.	1.14336e-66
CP024175.1\|AZW33420.1\|1563281_1563683_+\|aryl-sulfate-sulfotransferase	gnl\|CDD\|226771	COG4321, COG4321, Uncharacterized protein related to arylsulfate sulfotransferase involved in siderophore biosynthesis [General function prediction only].	8.03867e-42
CP024175.1\|AZW30050.1\|1557026_1558283_-\|acyl-CoA-dehydrogenase	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.	0
CP024175.1\|AZW30046.1\|1553015_1553708_+\|amino-acid-ABC-transporter-permease	gnl\|CDD\|223836	COG0765, HisM, ABC-type amino acid transport system, permease component [Amino acid transport and metabolism].	1.52172e-80
CP024175.1\|AZW33419.1\|1562022_1562511_+\|Cys-tRNA(Pro)-deacylase	gnl\|CDD\|237976	cd00002, YbaK_deacylase, This CD includes cysteinyl-tRNA(Pro) deacylases from Haemophilus influenzae and Escherichia coli and other related bacterial proteins. These trans-acting, single-domain proteins are homologs of ProX and also the cis-acting prolyl-tRNA synthetase (ProRS) inserted (INS) editing domain. The bacterial amino acid trans-editing enzyme YbaK is a deacylase that hydrolyzes cysteinyl-tRNA(Pro)'s mischarged by prolyl-tRNA synthetase. YbaK also hydrolyzes glycyl-tRNA's, alanyl-tRNA's, seryl-tRNA's, and prolyl-tRNA's. YbaK is homologous to the INS domain of prolyl-tRNA synthetase (ProRS) as well as the trans-editing enzyme ProX of Aeropyrum pernix which hydrolyzes alanyl-tRNA's and glycyl-tRNA's.	9.78705e-67
CP024175.1\|AZW30044.1\|1551269_1552175_+\|agmatinase	gnl\|CDD\|212538	cd11592, Agmatinase_PAH, Agmatinase-like family includes proclavaminic acid amidinohydrolase. This agmatinase subfamily contains bacterial and fungal/metazoan enzymes, including proclavaminic acid amidinohydrolase (PAH, EC 3.5.3.22) and Pseudomonas aeruginosa guanidinobutyrase (GbuA) and guanidinopropionase (GpuA). PAH hydrolyzes amidinoproclavaminate to yield proclavaminate and urea in clavulanic acid biosynthesis. Clavulanic acid is an effective inhibitor of beta-lactamases and is used in combination with amoxicillin to prevent the beta-lactam rings of the antibiotic from hydrolysis and, thus keeping the antibiotic biologically active. GbuA hydrolyzes 4-guanidinobutyrate (4-GB) into 4-aminobutyrate and urea while GpuA hydrolyzes 3-guanidinopropionate (3-GP) into beta-alanine and urea. Mutation studies show that significant variations in two active site loops in these two enzymes may be important for substrate specificity. This subfamily belongs to the ureohydrolase superfamily, which includes arginase, agmatinase, proclavaminate amidinohydrolase, and formiminoglutamase.	1.51723e-115
CP024175.1\|AZW30053.1\|1561076_1562009_+\|site-specific-tyrosine-recombinase-XerD	gnl\|CDD\|234713	PRK00283, xerD, tyrosine recombinase.	1.37589e-163
CP024175.1\|AZW30055.1\|1563689_1564802_-\|D-alanyl-D-alanine-endopeptidase	gnl\|CDD\|236952	PRK11669, pbpG, D-alanyl-D-alanine endopeptidase; Provisional.	1.04924e-102
CP024175.1\|AZW30040.1\|1546742_1547933_+\|5-(carboxyamino)imidazole-ribonucleotide-synthase	gnl\|CDD\|235674	PRK06019, PRK06019, phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed.	0
CP024175.1\|AZW30049.1\|1556201_1556747_+\|acyl-dehydratase	gnl\|CDD\|239538	cd03454, YdeM, YdeM is a Bacillus subtilis protein that belongs to a family of prokaryotic proteins of unkown function. YdeM has sequence similarity to the hot-dog fold of (R)-specific enoyl-CoA hydratase. Other enzymes with this fold include the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit.	1.10995e-70
CP024175.1\|AZW30042.1\|1549126_1550149_+\|amino-acid-ABC-transporter-substrate-binding-protein	gnl\|CDD\|270410	cd13692, PBP2_BztA, Substrate bindng domain of ABC glutamate/glutamine/aspartate/asparagine transporter; the type 2 periplasmic binding protein fold. BztA is the periplamic-binding protein component of ABC transporter specific for carboxylic amino acids, glutamine and asparagine. The BZtA domain belongs to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.	7.2809e-119
CP024175.1\|AZW30051.1\|1558299_1559994_-\|thiamine-pyrophosphate-binding-protein	gnl\|CDD\|181285	PRK08199, PRK08199, thiamine pyrophosphate protein; Validated.	0
CP024175.1\|AZW30054.1\|1562630_1563209_+\|protease	gnl\|CDD\|153243	cd03169, GATase1_PfpI_1, Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus. Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus. PfpI is an ATP-independent intracellular proteases which may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.	1.34539e-109
CP024175.1\|AZW30045.1\|1552201_1552993_+\|amino-acid-ABC-transporter-substrate-binding-protein	gnl\|CDD\|270248	cd13530, PBP2_peptides_like, Peptide-binding protein and related homologs; type 2 periplasmic binding protein fold. This domain is found in solute binding proteins that serve as initial receptors in the ABC transport, signal transduction and channel gating. The PBP2 proteins share the same architecture as periplasmic binding proteins type 1, but have a different topology. They are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the family includes ionotropic glutamate receptors and unorthodox sensor proteins involved in signal transduction.	9.69108e-62
CP024175.1\|AZW30041.1\|1547937_1548990_+\|L-threonylcarbamoyladenylate-synthase	gnl\|CDD\|223088	COG0009, SUA5, Putative translation factor (SUA5) [Translation, ribosomal structure and biogenesis].	9.95619e-71
CP024175.1\|AZW30057.1\|1566894_1569555_+\|hypothetical-protein	gnl\|CDD\|274682	TIGR03623, TIGR03623, probable DNA repair protein. Members of this protein family are bacterial proteins of about 900 amino acids in length. Members show extended homology to proteins in TIGR02786, the AddB protein of double-strand break repair via homologous recombination. Members of this family, therefore, may be DNA repair proteins.	0
CP024175.1\|AZW30056.1\|1565488_1566691_+\|MFS-transporter	gnl\|CDD\|340913	cd17355, MFS_YcxA_like, MFS-type transporter YcxA and similar proteins of the Major Facilitator Superfamily of transporters. This group is composed of uncharacterized bacterial MFS-type transporters including Bacillus subtilis YcxA and YbfB. YcxA has been shown to facilitate the export of surfactin in B. subtilis. The YcxA-like group belongs to the Monocarboxylate transporter -like (MCT-like) family of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	1.91228e-73
CP024175.1\|AZW30043.1\|1550240_1551077_+\|IclR-family-transcriptional-regulator	gnl\|CDD\|224332	COG1414, IclR, Transcriptional regulator [Transcription].	1.50542e-66
CP024175.1\|AZW30047.1\|1553729_1554482_+\|amino-acid-ABC-transporter-ATP-binding-protein	gnl\|CDD\|224051	COG1126, GlnQ, ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism].	1.23529e-151

>CP024175.1|AZW30049.1|1556201_1556747_+|acyl-dehydratase
MPPRNTREARLVYPAALARLGSNGLPAAFQQGRSMKFADLRAGMVITGGPLQVTEAEILEFARKFDPQWFHTDVQRAAEGRWGGLIASGWHTCALAMRMAVDAILHDSESFGSPGLGEVSWRVPVRPGDTLTLHARVQGARVSASRNDLGIVNWAWVVDNQHGETVLELDATSLFDLSGDS
>CP024175.1|AZW30048.1|1554610_1556170_+|acetolactate-synthase-large-subunit
MNGADSLCDTLLANDIDVCFANPGTSEMHFVAALDRKPRMRCVLGLFEGVVTGAADGYARMADKPAATLLHLGPGLGNGLANLHNAKRARTPMVNVVGDHATYHVQYDAPLTSDVEAVAQPMSHWVGRIRDAASVAAQTSEAIQVARQEPGNVSTLILPADAAWTDLPDDTPAPQPVRQAPQAQADAQAIRAAAQAIRSGQATTLLLGGAALRGRALAAAGRIAHATGVRLAAETSSRRTERGANRPPVVRLPYPVDLAVAFLKDVRHLVLVGSRSPVAFFAYPGKPSLLAPQECDQIVLAEPEQDLHHALEWLADELGIPADAPQTRPAALTEAVPAEGRLTSAAVNRVAAALLPDNAIVCDESITQGREFGIYSVHSAPHDWLQLTGGAIGIGLPLATGAAVACPDRKVVLLQADGSGMYTVQALWTQARERLDCLTIIYANRTYATLHGEMKNVGVIQPGENAKRMLDLVDPHIDWVQVSQGLGVEAVRVDTVEGFTQAMRAALARKGPFLIEAVI
>CP024175.1|AZW30047.1|1553729_1554482_+|amino-acid-ABC-transporter-ATP-binding-protein
MDACNQPAPVITLRGVSKWYGDFQVLRDLDLDVYQGERVILCGPSGSGKSTTIRLLNRLEEHEKGEIVVNGITLDGELRNIERIRADVGMVFQHFNLFPHLTVLENCTLAPMRVKGLDEGEAARRAMQFLERVRIAQLADKYPGQLSGGQKQRVAIARALCMQPRIMLFDEPTSALDPEMVKEVLDTMVELARDGMTMICVTHEMGFAREVGDRVVFMDGGSIVESDTPERFFSAPRSSRAQAFLGQILG
>CP024175.1|AZW30046.1|1553015_1553708_+|amino-acid-ABC-transporter-permease
MNLETLRMYLTPLAEGTMWTLALFFCSAVLAVALGLLVCLCRLSKSRVLSRGARLYIDIIRGTPLLLQLFYIYYGMPELGVVINAFVAGVLGLTLNFGAYLAELFRSGIQSVDSGQYEAARALGLNKVDRLRRVVLPQAVRTVFPALGNYALVLIKETSLVAVISVYELMRAGEMLAGATFQALTVYTMVGAIYFAMCSVLAHLFRRSEKRLTVPGYWSGAGENHDISKA
>CP024175.1|AZW30045.1|1552201_1552993_+|amino-acid-ABC-transporter-substrate-binding-protein
MKIKAALGILATVGMLAHAGSAAARTLDEVRAAKSANVVTTASAPPHGFKNPASNQLEGIMVDVGAAVAKHLGVAMNLKDVPFSGLIPTLTSGRADVMSAPLFVTPERAKVIDFSAPVYEWGEGLVLREQNPDDIKRFEDLQGRRIGVLVDSVQFNMIKDMPDTKVSTYQDYSTLLADVRAGRIELGIIDPPSIIYQIRTKKIPGVKLATQYQPQKKWHVGLAVQKDNKALLDAVNAALAEMKRNGELAEIGRKWGVADLISK
>CP024175.1|AZW30044.1|1551269_1552175_+|agmatinase
MGVPARRPAGEAALACVLGIPFDCGTHPFRVGARQGPDAIREQSRLLRPYDLARRAGVDNPVEFLRLLDLGNVACVPGDPQASYPAIEQAVAQVLQAGAIPITMGGDGAVTLPQLRAVARRWPGVAVLHFDSHTDTYPIAGYNTATTFTRAAEEGLIDLSHSFHVGTRGNSFMGGVIEYGREVGYTVIPYDDFDRDQAGTLARLRGQLGDRPVYLCFDMDIFDPSCAPGVCTPEWGGLSPKEGLNLLRALSGLNFVAFDVNTVSPPQDVGGATAFLAASVMQEFCALAAAAVQAYPQGRPD
>CP024175.1|AZW30043.1|1550240_1551077_+|IclR-family-transcriptional-regulator
MTTVAPEDSPLFVAALARGLTLLAAFSEGRPAMTLPELAEATGLTKSAAQRFAHTLWTLGYLRKNPDSKKFSLSPQSLQLGMQYAQTSPLVLGGNPFLHSLNRTSQETCSLAEPDGLDMVYVARFATHKQMFVHMPVGMRIPMYCAAAGRAVLARLEPDRARRLLQQSPRAARTATTLTDLDALMAELAFTREHGYARSNGEYYPGDITISAAVLDNAGTPAGSVNISVPSSRWSFEEAQAVFGPQVLETAHAISASRTLGVLPPFYRMAPPSALNSD
>CP024175.1|AZW30042.1|1549126_1550149_+|amino-acid-ABC-transporter-substrate-binding-protein
MKRHIAMAAGALALALGAQAAHAGPTLDAVKKKGFVQCGLTDGVAGFSATNSKGEWEGMDVDICRAVAAAVFGDAGKFKGTALSTQQRFTALQSGEVDVLLRTVTLTQTRDTSLGLAAVAASFYDGQGVLVRKALGVKSAKELDEATICVQPGTTTELNLADWFRANGIKFTPVVIDKVTEVVRAFESGRCDAFTDDASQLAAVRATQVAKPDDFEILPERFSKEPLGPMVRQGDENWLGIVRWTLFALMEAEEYGITQQNVDEMLKSKNPNVLRILGVTPGAGKNMGLDEKWAYNAIKAVGNYSQIFERNVGKDSRLGLQRGVNALWSQGGAMYPWPIR
>CP024175.1|AZW30041.1|1547937_1548990_+|L-threonylcarbamoyladenylate-synthase
MIPAPMNVADPAVAHAAACLLAGELAAFPTETVYGLGADAENPQAVARIYAAKGRPSNHPVIVHIAPEGDVDYWASDVPAAARQLIQAFWPGPLTLILKRAPHIGAAVSGGQDSIGIRCPSHPVAQALLRAFAAGKPNGQGGVAAPSANTFGHVSPTRAEHVRAEFPREVAAGMPVLDGGDAEVGIESTIIDLSRLDQGVGPVLLRPGHISAAQVAAVLGMPVARPDAAAPRASGTLKAHYAPRTPLELLDAAQLPRALAAAPAGVRQAVVALAPAPAGLPADVHWRMAPADPARYAQALYALLRELDRQGYARILVEQPPRSGDWDAVNDRIGRAAAAFSLDTTDLPGT
>CP024175.1|AZW30040.1|1546742_1547933_+|5-(carboxyamino)imidazole-ribonucleotide-synthase
MTQSSTFDPIAPGDWLGLLGGGQLGRMFCHAAQSLGYKVAVLDPADECPAGMVADLHIQAAYDDADGLARLAGRCRAVTTEFENVPADSLRALAARCRVSPAADAVAVVQDRIAEKTFIAGQGIEVAPHAAIRARDDLLAAPQALFPGILKVARLGYDGKGQARIASREEALAAFDEFGGVPCVLEALLPLDYEISVVIARGFDGASMVFPIARNVHRDGILAVSSVTPGTADASHAARQVQATQAAQAIAQGLGYHGVLCVEFFVLGDGRLVVNEIAPRPHNSGHYTIDACVTSQFEQQARVMAGLPLGSADLLAPAVMLNILGDAWFEPGAHAPREPDWSAALAVPSAKLHLYGKREARRGRKMGHVTIVAATPEQARDDAARVARALGMAAPF
>CP024175.1|AZW30050.1|1557026_1558283_-|acyl-CoA-dehydrogenase
MPRPHIHDPDLSFSYLHWSTRMSSTPSFHWQDPLLLDQQLTEEERMVRDAAVAYSQDKLAPRVLEAFRHEKTDPAIFAEMGELGLLGATIPTEYGGAGLNYVCYGLIAREVERVDSGYRSMMSVQSSLVMVPINEFGSEAQKRKYLPKLAAGEWIGCFGLTEPNHGSDPGGMETRATKTPDGYKLTGNKMWITNSPIADVFVVWAKCVGGDFDGKIRGFILEKGMKGLSAPAIHGKVGLRASITGEIVMDEVEVSEEQMMPGVSGLKGPFTCLNSARYGIAWGALGAAEACWHTARQYTMDRKQFGRPLAANQLIQKKLADMQTEITLGLQGCLRLGRMKDEGTAAVEITSIMKRNSCGKALDIARLARDMLGGNGISDEFGVARHLVNLEVVNTYEGTHDVHALILGRAQTGLQAFY
>CP024175.1|AZW30051.1|1558299_1559994_-|thiamine-pyrophosphate-binding-protein
MTTANHSTPASRLGGHILVDQLAAHGVKHVFCVPGESYLAVLDGLHDASIDVTVCRQEGGAAMMADAHGKLTGEPGICMVTRGPGASNALAGVHIAKQDSTPMILFVGQIERGMREREAFQEMDYRAVFGTQAKWVTEIDQVERIPELISRAFHVATSGRPGPVVIALPEDVLVETASVPDAPRYEVIDAAPAAGQMDQLAQMLAQARAPVAILGGSRWNAQAVQQFADFAQRHALPTAVSFRRQMLFPADHPCFIGDVGLGINPALLKRIEQADLVLMVGGRMSENPSQAYTLLDIPVPRQKLVHVHPDSAELGRVYRANLAINTSPAAFCAALAQAHGPSQPAWADDTQAMRASYLQWSDPAAIRTPGALQLGEVMAFLEKTLPADAIMANGAGNYATWLHRFHRYTRYGTQLAPTSGSMGYGLPAAVGAKRIWPQKTVVCFAGDGCFLMHGQEFATAVQYDLPIVVVLIDNGMYGTIRMHQEKHYPGRISATSLKNPDFAEYARAFGGHGERVETTEQFAPAFERALASGKPAILHCLIDPETITPSTTLEKIRAAALKAQ
>CP024175.1|AZW30052.1|1560151_1561039_+|LysR-family-transcriptional-regulator
MRNGIPNLSALQAFEATARLGSFSRAAEELSLTHSAVYRQVASLEDRLGVQLFTRVRRRIVLTDHGAEYAGRIRHHLDQIEKDTFGLVSRTGMGRSIHIAVVPTLATTWLIPRLADFQRVQPDITVSLSVRTLPFQFKDQPFDGALYHGDGIWPGTQGVLLFPERELVPVCAPELAERASGRDDGALGGMMHLHLYSRPDAWRQWYAANQYAYGPQAAGGPRYDLFTMMLAAVQAGLGVGLMPRFLVQDALDAGTLVMPVPQALSVSQGYYFGYPQRSERSGALKAFEVWLKSAV
>CP024175.1|AZW30053.1|1561076_1562009_+|site-specific-tyrosine-recombinase-XerD
MSSSAPLASQADLDAFIDAVWLEDGLAANTLAAYRRDLSAFAQWLENPACHPGLATGASLREAGKGDIEAWFAARHAESRATTANRRLAALRRFYAWALRERLTPSDPCLTLVTAKQPPRLPKTLSEAQVDALLQAPDLDTARGLRDRAMLETLYATGLRVSELVSVKALDVSLNEGVVRVVMGKGGKDRLVPLGAEAAHWIERYAGSARPELLGARVADALFVTARAEPMSRQAFWQLVKKYALAADIHAPLSPHVLRHAFATHLLNHGADLRVVQMLLGHADISTTQIYTHVARERLKALHAAHHPRA
>CP024175.1|AZW33419.1|1562022_1562511_+|Cys-tRNA(Pro)-deacylase
MSKNRHVSETPATQLLRQRKVAFTEHTYDYVDHGGAGEAARQLGLDPHAVVKTLIMEDEGGHPLVVLMHGDREVSTKNLARQAGLKKVAPCQPEVAQRHSGYQVGGTSPFGTRKRMPVWVEASVLDFPQIYVNGGRRGYLVGIAPQALVDLLGARAVQVALP
>CP024175.1|AZW30054.1|1562630_1563209_+|protease
MSKKLLMLVGDYAEDYETMVPFQTLLAVGHTVHAVCPDKKAGDTVATAIHDFEGAQTYSEKRGHNFTLNHDFAKVEPQHYDGLVIPGGRAPEYLRLDERVLDIVRHFDQAGKPIAAVCHGAQLLAAAGILQGRTCSAYPACAPEVRLAGGTYAEIGIDQAHTDGNLVTAPAWPAHPAWLAQFLAVLGTRISH
>CP024175.1|AZW33420.1|1563281_1563683_+|aryl-sulfate-sulfotransferase
MSCINRVPGILMCEIFIRANQRSYSVQARSLRLHGVATSVRLEQLFWDVLEEIAARDGMRVTQLIERLYDELVQYRGEAANFTSFLRVCCLRYQVLQAEGRIPADATVPIRSLDAQAVLRGLPANLYDSRPLG
>CP024175.1|AZW30055.1|1563689_1564802_-|D-alanyl-D-alanine-endopeptidase
MAFHWTRAVARALAPLALAIGALLPYAAHAAKADPCRTNAKSAACKSQQAKKASAKKAPAKTASSKKSASTAKKKSASSKKTASAKKGSTRKSTIRARTRTARASAAATAAMPPAAASPAAEAAALRSSTAYVQDLETSTVLFAKNENVVRPIASISKLMTALVVVDANLPMDEMIEITDDDVDTLKHTTSRLRVGTVLSRGDMLHLALMSSENRAAHALGRNYPGGMPAFVAAMNAKARSLGMLNTRFVEPTGLSSENVSSPRDLARMLRAASQRPLIHRYSTDTEYEVEINNRTQTFRNTNLLVRKPDWDIKVSKTGFINEAGECLVMLARINGRDMAIVLLDSQGKLSRIGDAVRIRRIVQNDVAML
>CP024175.1|AZW30056.1|1565488_1566691_+|MFS-transporter
MSTSEKPSLRILFIGTGVVLLAMGVRATFGLFMQPMGLAHGWGREVFSMAFALQNLVWGAACIGMGILADRYGSGRTIVLGAVLYALGMIGTRFATDEATLYLTAGVLVGLGQAGTTFPVILPVVARSVPAAYRSTAMGIASAGGSLGQFLVVPAGQQLITGLDWPGALWVLSLLVAVGAPLAYFLRGKPGVHGGVQQSLGAAVRQAMAHPSFHFLSWSYFVCGFHTAFITLHLPAYVVDAGMKASHGATAIALIGLCNVIGSFYAGKLGGVYSKRLLLAAIYGLRAFGMLLLLAVPLTPLVLYVFAGWMGLFWLGTVPLTQGLIGQIYGLRYAATLSGIAFLGHQVGSFIGVWMGGAVYARTGNYDLVWWTGVALAVVAALLCLPVREQPLAQPAAARA
>CP024175.1|AZW30057.1|1566894_1569555_+|hypothetical-protein
MSDDFRTDFPSCTLRDLGELPAIDTLVLTVNNRLSRRLTLDLAAQLRSERQVSELPRIMPLSAWLADCAAELAFDERYEVPAYRLSSFATQLVWREAIRLEEADRALLDADQAARLALDADLLVDEWQAHVPAGAETDEYRGFSRWRARYRAMLGELDAEDANQGYERVLEALRQGALRAPRHVALAGFVDISPRFARLLRALADGGADVVAWRDAVREPAWPQRFEAADRGAEWRAAARWAADRLRADPRGRYAIVSPQLEAEAPFARRVLGQALAGQDAPLPFNVAVGRALDEWPAVRAALAWLALLAEVAARGAGEPALFGAALLAGHCAGDLQEGPRHAALDARWRRQALAHVGPADWQRGLEECPRLAEGWSQAMAIWQAGQRSDTCDAWAPRFKAALTALGFPGERALDSVAYQVMGALGDLLAEFTALAPAAGRLDGRAAVRLLASAARAGSFQPQRDPSARLDVLGLLEAEGGAWDGIWVLGLTDDVLPASPKPNPLLPLAVLRQVGAPRATPEREREWAEGMFMALRRCAPEMIASHAAMDGERELRPSPLIARAAPADWQPGADAQAAALEQEILDDSQGPPLQAERQSRGGLDVLDTQARNPLWAFVRHRLGGRAMAPYADAATVSVRGQFLHRALELVWRMLPDQEALHAAMAEGRLAALVEQAIGEAARTELAGYPAALRELECARAAAVLANWFDSEAQRQPFEVAQIEQEHSWQRGALALKVRLDRMDRLADGRALIVDYKTGAAPGRPESDWARARPVNLQLPFYASVLADGADTEVAGLMLAQIHARQVSAQGLAADDLGIEGVTPVEQSKVFEGQPWPRILQRWRAAVEMLADEYANGYAANVALRQDDLKFCDAMPFLRLHLDDEDA

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Crispr_ID: CP024175_3

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

CP024175_3

4114154-4114235

Orphan

Consensus_repeat	Method
CTGTCCCCGCCGGGACAGGCACC	CRISPRCasFinder

1 spacers

The CRISPR arrays of CP024175_3

>merge|CP024175|3|4114154-4114235|CRISPRCasFinder
CTGTCCCCGCCGGGACAGGCACCCGTCGTGCGCCATGAGCGCCACTGCCAAGACGGCGTCTGTCCCCGCCGGGACAGGCGCC

>CP024175|3|3|4114154-4114235|CRISPRCasFinder
CTGTCCCCGCCGGGACAGGCACC	CGTCGTGCGCCATGAGCGCCACTGCCAAGACGGCGT
CTGTCCCCGCCGGGACAGGCGCC

Protein	Signature genes	Signature genes Name	Protein_function
CP024175.1\|AZW32274.1\|4111306_4114057_+\|insulinase-family-protein	unknown	unknown	gnl\|CDD\|223685
CP024175.1\|AZW32272.1\|4110006_4110561_-\|N-acetyltransferase	unknown	unknown	gnl\|CDD\|224168
CP024175.1\|AZW32269.1\|4107032_4107395_-\|cytochrome	unknown	unknown	gnl\|CDD\|225418
CP024175.1\|AZW33518.1\|4118564_4118807_-\|hypothetical-protein	unknown	unknown	unknown
CP024175.1\|AZW32273.1\|4110598_4110973_-\|hypothetical-protein	unknown	unknown	unknown
CP024175.1\|AZW32271.1\|4108830_4110003_+\|VWA-domain-containing-protein	unknown	unknown	gnl\|CDD\|226346
CP024175.1\|AZW32275.1\|4114242_4115364_-\|molecular-chaperone-DnaJ	unknown	unknown	gnl\|CDD\|236757
CP024175.1\|AZW33519.1\|4123963_4124383_-\|transcriptional-repressor	unknown	unknown	gnl\|CDD\|366663
CP024175.1\|AZW33517.1\|4107921_4108809_+\|MoxR-family-ATPase	unknown	unknown	gnl\|CDD\|223786
CP024175.1\|AZW32267.1\|4105097_4106354_-\|isocitrate-dehydrogenase-(NADP(+))	unknown	unknown	gnl\|CDD\|180792
CP024175.1\|AZW32281.1\|4121153_4122053_+\|NAD-kinase	unknown	unknown	gnl\|CDD\|179379
CP024175.1\|AZW32270.1\|4107407_4107761_-\|cytochrome-C	unknown	unknown	gnl\|CDD\|225418
CP024175.1\|AZW32276.1\|4115464_4117390_-\|molecular-chaperone-DnaK	unknown	unknown	gnl\|CDD\|234715
CP024175.1\|AZW32280.1\|4120034_4121039_-\|HrcA-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|234621
CP024175.1\|AZW32278.1\|4117868_4118423_-\|nucleotide-exchange-factor-GrpE	unknown	unknown	gnl\|CDD\|237621
CP024175.1\|AZW32268.1\|4106556_4106982_+\|DUF1841-domain-containing-protein	unknown	unknown	gnl\|CDD\|370177
CP024175.1\|AZW32282.1\|4122068_4123730_+\|DNA-repair-protein-RecN	unknown	unknown	gnl\|CDD\|223571
CP024175.1\|AZW32279.1\|4118888_4119977_-\|ferrochelatase	unknown	unknown	gnl\|CDD\|234585
CP024175.1\|AZW32277.1\|4117480_4117861_-\|thioredoxin	unknown	unknown	gnl\|CDD\|239245
CP024175.1\|AZW32266.1\|4103918_4104899_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|340821

Protein	Function_ID	Function_description	E-value
CP024175.1\|AZW32274.1\|4111306_4114057_+\|insulinase-family-protein	gnl\|CDD\|223685	COG0612, PqqL, Predicted Zn-dependent peptidases [General function prediction only].	3.06874e-64
CP024175.1\|AZW32272.1\|4110006_4110561_-\|N-acetyltransferase	gnl\|CDD\|224168	COG1247, COG1247, Sortase and related acyltransferases [Cell envelope biogenesis, outer membrane].	1.87052e-61
CP024175.1\|AZW32269.1\|4107032_4107395_-\|cytochrome	gnl\|CDD\|225418	COG2863, COG2863, Cytochrome c553 [Energy production and conversion].	2.60442e-23
CP024175.1\|AZW32266.1\|4103918_4104899_-\|hypothetical-protein	gnl\|CDD\|340821	cd03789, GT9_LPS_heptosyltransferase, lipopolysaccharide heptosyltransferase and similar proteins. Lipopolysaccharide heptosyltransferase (2.4.99.B6) is involved in the biosynthesis of lipooligosaccharide (LOS). Lipopolysaccharide (LPS) is a major component of the outer membrane of gram-negative bacteria. LPS heptosyltransferase transfers heptose molecules from ADP-heptose to 3-deoxy-D-manno-octulosonic acid (KDO), a part of the inner core component of LPS. This family also contains lipopolysaccharide 1,2-N-acetylglucosaminetransferase EC 2.4.1.56 and belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.	3.59109e-14
CP024175.1\|AZW32271.1\|4108830_4110003_+\|VWA-domain-containing-protein	gnl\|CDD\|226346	COG3825, COG3825, Uncharacterized protein conserved in bacteria [Function unknown].	0
CP024175.1\|AZW32275.1\|4114242_4115364_-\|molecular-chaperone-DnaJ	gnl\|CDD\|236757	PRK10767, PRK10767, chaperone protein DnaJ; Provisional.	0
CP024175.1\|AZW33519.1\|4123963_4124383_-\|transcriptional-repressor	gnl\|CDD\|366663	pfam01475, FUR, Ferric uptake regulator family. This family includes metal ion uptake regulator proteins, that bind to the operator DNA and controls transcription of metal ion-responsive genes. This family is also known as the FUR family.	1.74636e-59
CP024175.1\|AZW33517.1\|4107921_4108809_+\|MoxR-family-ATPase	gnl\|CDD\|223786	COG0714, COG0714, MoxR-like ATPases [General function prediction only].	1.30038e-45
CP024175.1\|AZW32267.1\|4105097_4106354_-\|isocitrate-dehydrogenase-(NADP(+))	gnl\|CDD\|180792	PRK07006, PRK07006, isocitrate dehydrogenase; Reviewed.	0
CP024175.1\|AZW32281.1\|4121153_4122053_+\|NAD-kinase	gnl\|CDD\|179379	PRK02155, ppnK, NAD kinase.	0
CP024175.1\|AZW32270.1\|4107407_4107761_-\|cytochrome-C	gnl\|CDD\|225418	COG2863, COG2863, Cytochrome c553 [Energy production and conversion].	6.05638e-23
CP024175.1\|AZW32276.1\|4115464_4117390_-\|molecular-chaperone-DnaK	gnl\|CDD\|234715	PRK00290, dnaK, molecular chaperone DnaK; Provisional.	0
CP024175.1\|AZW32280.1\|4120034_4121039_-\|HrcA-family-transcriptional-regulator	gnl\|CDD\|234621	PRK00082, hrcA, heat-inducible transcription repressor; Provisional.	5.93958e-145
CP024175.1\|AZW32278.1\|4117868_4118423_-\|nucleotide-exchange-factor-GrpE	gnl\|CDD\|237621	PRK14139, PRK14139, heat shock protein GrpE; Provisional.	1.18525e-78
CP024175.1\|AZW32268.1\|4106556_4106982_+\|DUF1841-domain-containing-protein	gnl\|CDD\|370177	pfam08897, DUF1841, Domain of unknown function (DUF1841). This family of proteins are functionally uncharacterized.	2.9417e-76
CP024175.1\|AZW32282.1\|4122068_4123730_+\|DNA-repair-protein-RecN	gnl\|CDD\|223571	COG0497, RecN, ATPase involved in DNA repair [DNA replication, recombination, and repair].	0
CP024175.1\|AZW32279.1\|4118888_4119977_-\|ferrochelatase	gnl\|CDD\|234585	PRK00035, hemH, ferrochelatase; Reviewed.	3.4326e-159
CP024175.1\|AZW32277.1\|4117480_4117861_-\|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.	1.07863e-05

>CP024175.1|AZW32274.1|4111306_4114057_+|insulinase-family-protein
MRLPLLSRRLNALLVSSFLAFQAGAASLPAGVSEVSSIEGITEYRLANGLRVLLAPDASKPTTTVNMTYLVGSRNENYGQTGMAHLLEHMLFKGTPAIRNALGEFSRRGLQANGSTSSDRTNYFASFAANPETLKWYLGWQADAMVNSLIAKEDLDSEMTVVRNEMESGENNPFRVLMQKMQAAAYQWHNYGKSTIGARSDVENVDIAQLRAFYHEYYQPDNAVLIVAGKFDPQTALADIQSSLGKLPKPKRTLPPEYTVEPVQDGERSVTLRRAGGTPLVAAMYHLPAAGSPDFVGLDLAATILADTPSGRLYHALVPTKLASGVFGFTMDQLDPGLAMFGAQLQPGMDQDKALQTLTATLESLSSKPFSQEELERARSKWLTAWQQTYADPEKVGVALSEAIASGDWRLFFLQRDRVRDAKLDDVQRAAVAYLVRSNRTEGRYIPTEKPQRAPLAQRADLAAVFKDYKGDPNFKAVEAFDPSPANIDKRTLRRTLDLPNGQVELALLPKATRGDRVQAELLIQFGDAEALRGQRVPLAAAAALLDRGTDKLSRQAIQDRLDQLQAEAAINGSGTNLVVNISTLGKNLPDVMALVLDVVRNASFPQDQVEEYKRQAITMVQDAMTDPTALASRALARHNNPWPADDVRYVPTFDEALEQLRSLSRDDLAAVSGKLYGAGRIKFSAVGEFDPAAVEAVLRKGLDGWRSAPAYTRLPDPYRAVPAQQFDIATPDKANAFYISRMPLQLQDTNADYPALYLANFLLGTSETSRLWHRVRETEGLSYNVRSNLSVSSYEPSANWTIYAIYAPQNRARLEKAISEELARALKDGFTDQEVRDGVVALLNYRNLARAQDDVLADTWVNYMQTGRSFQWSADMDRKLEALTPDQVNAALRKYLKPDAFSTAVAGDFTKKSAP
>CP024175.1|AZW32273.1|4110598_4110973_-|hypothetical-protein
MLTDIVTRALSQLLGNSLSGDVIKGRFRYAYASDDGRFVAILGHDLTTYVVDVDAQRYFAECAGVPCGFAGHVLEMEGAQEHGHPWPAVNDLFDLDMDGDEIAWRRCPGAVALAATRQAQSRVA
>CP024175.1|AZW32272.1|4110006_4110561_-|N-acetyltransferase
MNATPSPAPTGATLVDCTHDRHAAAILDIFNDAILTSTALYDYQPRALASMEAWFQAKRQGGFPVVGFEDAAGVLMGFASYGTFRAWPAYKYSVEHSVYVDRRYRGRGLGEALLRALIERARLQQVHVLVGGIDATNAGSVALHRKLGFVHAGTITQAGFKFGRWLDLAFYQLTLDTPLRPVDG
>CP024175.1|AZW32271.1|4108830_4110003_+|VWA-domain-containing-protein
MLIDFFYHLRAHKLPVSVQEYLTLLEALRQRLMAPTLDDFYFLARTALVKDESLYDRYDAAFGAYYRGIAAALPADRDIPLDWLIKEFEKTLTPEEKAAIEAHGWDKLMELFKQRLEEQQERHAGGSKWIGTGGTSPFGNGGYHPEGIRVGGDSAGNRTAVKVWDMRQFRDYDDQLELGTRNFKVALRRLRRFARQGADLELDLDDTIASTARNAGHLDLRLVPERRNTVKVLMLLDVGGSMDDHIARVEELFSAARSEFRHLDVYYFHNCPYENLWQNNRRRQNERFDTWDVLRKYNADWRLIIVGDATMSPYEILQPGGSVEHYNKEAGAVWLRRLLDAWPKAAWLNPEPTASWRYRQSIALLRDIMQDRMYPVTVAGLEQAMRQLSK
>CP024175.1|AZW33517.1|4107921_4108809_+|MoxR-family-ATPase
MPTSASSSSAPAQSARFEGTDRYVATDDLKLAVNAALTLQRPLLIKGEPGTGKTMLAEEVARALDRPLLQWHIKSTTKAHQGLYEYDAVSRLRDSQLGDEKVRDIRNYIVQGTLWQAFEAPEPVVLLIDEIDKADIEFPNDLLRELDRMEFHVYETRQTVQARHRPLVIITSNNEKDLPDAFLRRCFFHYIRFPDRDTMRDIVGVHYPDIRQDVLRAALDTFFALREAPGLKKKPSTSELLDWLRLLLAEAIPAAEIDAHAATAVPVLAGALLKNEQDVHLLERLGAMARGAQRR
>CP024175.1|AZW32270.1|4107407_4107761_-|cytochrome-C
MKLRISMTRTVSVLAVLASCAIAGPAAAADAAPVGNAQNARDKVSMCIGCHGIPGYKASFPELYHVPMIAGQNAKYIEAALNEYRKGARSHPTMDAVAGSLSDQDIADLAAYYSSLK
>CP024175.1|AZW32269.1|4107032_4107395_-|cytochrome
MKRFTFALAGIVLATAGVSAQAQDVVAGKAVFDKFNCASCHGADAKTSVQPEYPVLAGQHADYLAHALKAYKRGAAGSAATANVRKNPIMGAFAAQLSDQDIRNVAAWLAAQPSDLGVRQ
>CP024175.1|AZW32268.1|4106556_4106982_+|DUF1841-domain-containing-protein
MFNPSRDQVREFFIETWRKHRATEVLTPLESMALDWILEHPEYHGDLESPEAMTAEYPVEHGRTNPFLHLSMHLAIAEQLSIDHPRGIRAAYQRLVGRGDAHQAAHEIMECLGQVVWEAQRLGTPLDSDAYIELIRQRAER
>CP024175.1|AZW32267.1|4105097_4106354_-|isocitrate-dehydrogenase-(NADP(+))
MSYQHIKVPTGGQKITVNADYSLNVPDQVIIPVIEGDGTGADITPVMIKVVDAAVQKAYAGKRKIHWMEVYAGEKATKVYGPDVWLPEETLDAVKDYVVSIKGPLTTPVGGGIRSLNVALRQQLDLYVCLRPVRYFKGVPSPVREPEKTDMVIFRENSEDIYAGIEYMAESEQAKDLIQYLQTKLGATKIRFPNTSSIGIKPVSREGTERLVRKALQYAIDNDRASVTLVHKGNIMKFTEGGFRDWGYALAQNEFGAQPIDGGPWCKFKNPKTGREIIVKDSIADAFLQQILLRPAEYDVIATLNLNGDYISDALAAQVGGIGIAPGANLSDSVAMFEATHGTAPKYAGKDYVNPGSEILSAEMMLRHMGWTEAADLIIASMEKSILSKKVTYDFARLLEGATQVSCSGFGQVMIDNM
>CP024175.1|AZW32266.1|4103918_4104899_-|hypothetical-protein
MAKPASDMPPYDKAAALRGLAGARRVALLMAPRLGDTLLMMNMARNLAAHGREVSIFGDYIHGLRDWFPGLDIRPSLSEEQAGQVLPGYDCAAQMHVGWPYALHAHQPNYFYYDAHVVITGRGFVKLFQIRDFCREQLGLAQAGADNGLRPPPQVQPHRSHPRRVALHPTSTGAQRCWAPRHFKELGLRLLHEGYEPNYIVAPHERAEWSWVLDHGLHLPQFPSLSEVAGFIHASGWFIGNESGIGHLASNVGVPTLSLTGRPTRTRAWRPAWSTSRIVYPALIPGGRWRDRLWREWLSPRRVMSAFHKLQADDRRQPVGVPWGKI
>CP024175.1|AZW32275.1|4114242_4115364_-|molecular-chaperone-DnaJ
MAKRDYYEVLGVAKNASDEDLKKAYRKLAMKYHPDRNPDSKEAEEKFKEAKEAYEVLGDEQKRAAYDRYGHAGVDPNAAGMGGGMGGGFADAFGDIFGEIFGAGRRGGGGPQVYRGADLKYALEITLEQAASGFDTEIRVPSWENCDTCHGSGAKAGTSPKTCRTCGGSGAVRMQQGFFSVQQTCPTCHGTGKEITDPCPSCDGVGRTRRNKTLQVKIPAGIDDGMRIRSSGNGEPGINGGPPGDLYVEIHIKQHKIFQRDGDDLHCELTIPFTTAALGGELQVPTLGGKAEISIPEGTQSGKTFRLRAKGIRGVRGSYPGDLYCHVVVETPVRLSDEQKAILRQFEASLNDGGDRHSPQSKSWTDRVKEFFS
>CP024175.1|AZW32276.1|4115464_4117390_-|molecular-chaperone-DnaK
MSKIIGIDLGTTNSCVAVLDGGQVKIIENAEGARTTPSIVAYMDDGETLVGAPAKRQAVTNPKNTLYAVKRLIGRKFDEKAVQKDIDLMPYSIVKADNGDAWVEVRGKKLAPPQVSAEVLRKMKKTAEDYLGEEVTEAVITVPAYFNDSQRQATKDAGRIAGLEVKRIINEPTAAALAFGLDKTEKGDRKIVVYDLGGGTFDVSIIEIADVDGEMQFEVLSTNGDTFLGGEDFDQRIIDYIISEFKKEQGVDLSKDVLALQRLKEAAEKAKIELSSSQQTEINLPYITADASGPKHLNLKITRAKLEALVEELIERTIEPCRVAIKDAGVKVSDIDDVILVGGMTRMPKVQDKVKEFFGREPRKDVNPDEAVAAGAAIQGSVLSGERKDVLLLDVTPLSLGIETLGGVMTKMIQKNTTIPTRYSQTFSTADDNQPAVTIKVFQGEREIAAGNKGLGEFNLEGIPPAPRGLPQIEVTFDIDANGILHVSAKDKGTGKENKITIKANSGLSEDEIQRMVKDAEANAEEDHRLAELAQARNQADALVHATRKSLTEYGDKLEAAEKESIEAAIKDLEDILKTGDKAEIDAKVEALSTASQKLGEKMYADMQAQQQAQQQQAADNAKPVDDNVVDADFKEVKRDQ
>CP024175.1|AZW32277.1|4117480_4117861_-|thioredoxin
MAAAPFDPAEVFQVFGMRRVDSASFDEQVVQAPGDDLRCVFLWGQDCYNCGIFKQTALLQRQALLALELSWFEADVYADEALGRRFSLHGVPTFVLYRSGKRLGRVTGWPGLPQFSAAMQRLRDGT
>CP024175.1|AZW32278.1|4117868_4118423_-|nucleotide-exchange-factor-GrpE
MTAPQEPVDSTPESGENAATPGLEDDLSAELAALRAELEAAQATVKAQQEQVLRAAAEAENVRRRAQEDVAKARKFGIESFAESLVPVKDSLEAALAQPDQAAQAWREGVEVTLKQLTAAFERNLLKEIAPAQGDKFDPHLHQAISSVPADQPANTVLQLLQKGYVIADRTLRPALVVVSAGQG
>CP024175.1|AZW33518.1|4118564_4118807_-|hypothetical-protein
MNPPRKPTIGTSGPPGHANLEEDQLERELDEALLETFPASDPIAITSEDERDEPDDKVDEALEDTFPASDPPAPAQPGKK
>CP024175.1|AZW32279.1|4118888_4119977_-|ferrochelatase
MFLRLFKYLWPERYLPETPAQDPFDENPPPCGPGRVGVLLVNLGTPDEPTRGAIRQYLGEFLSDPRVIEIPRYLWMPILHGLVLTMRPKKLAPRYAGIWMEEGSPLLVYSQRQAAGVRQGLAARGVHAEVELAMRYGKPSIPAAIAALRERGCDHILAVPLYPQYAASTTATVVDAVTRHAGRLRDQPALRFVKRFHNDPAYVEAQAGRIAEFWQAHGRPQKLVMSFHGLPRYSIELGDPYYRDCLDTARLLRERLGLREDEVEVTFQSRFGSARWLEPYTEPTLAELARQGVTEVDVVCPGFVADCLETLEEISQECRDAFVAAGGRQFRYIPALNDCPPWIEGLTDLVERQLRGWPTGNP
>CP024175.1|AZW32280.1|4120034_4121039_-|HrcA-family-transcriptional-regulator
MDDRARALLKALIERYIADGQPVGSRTLSKVFDLSPATIRNVMADLEELGLIHSPHTSAGRVPTPRGYRMFVDSLLAVRAYQFEPAHIGELLPVSEPSRAVNAAAALLSNLTQFAGVVLTPKRTQIFRQIEFIRLSDKRVLLIIVTPEGDVQNRILSAQRDYTEAELLEAGNFFNVHFSGKSFDAVRRTLSTELAQLRDDISRLMQAAVEAGAEAADDGEAVVISGERKLLDVTDIASDMDRLRKMFSLFEKKTDLLQLLDVSSRAQGVQIYIGGDSQLVPMEEVSVITAPYGLDGKVIGTLGVIGPTRMAYERVIPIVDITARLLSNALSHNQ
>CP024175.1|AZW32281.1|4121153_4122053_+|NAD-kinase
MYFPIVALIGRYQDTGLDAPLTALAQMLTQAGRRVLVEAETARNAGVSGYPVADWDEIGRTATLAVVMGGDGTVLGAARHLAPYGVPLIGINHGRLGFITDIPLQDAHDALGRVLEGNYQAEDRMLLQGGVWRGEQQMYSASAVNDVVLNRAGRGGMIEVRVELDGAFMYTQRADGLIIATPTGSTAYSLSANGPILHPGMNAMVLVPVAPQTLSNRPIVIPDSGVLNMTLTAMGRVEIGASVHFDMQTWSDLQPGDRITVQRAPHTIRFVHPEGYSFFSTLRRKLHWNLMPQATDNLE
>CP024175.1|AZW32282.1|4122068_4123730_+|DNA-repair-protein-RecN
MLRTLHIRDFVIVEQTELHFGDGFTVFSGETGAGKSILIDALALTLGERGDASMLREGAARADITAVFDAPPALRDWLAERELDSGDELALRRVIDSQGRSRAYINGMPATIAQLRELGDGLVDIHGQHAHQSLMRPDAQRDLLDAHGGHAELRQTVAQAWKQWRALARQLDTAEQDAEALAAERDRLQWQSDELDRLGLGPDEWDALQTEHTRLSHAQSLLDGASRILEALDGEHDSAQHRLNGAAHQLQQMLRHDPALQGIGDELESARIAITEAVSDLNNYVSRVELDPQRLADVEARLSAVFETARKFKCEPHDLPALRDSLHGKLAEMQAASDVQALRAQAEAAQARYEAAAARLSAARRKIAKDLGKQVTQAMQTLSMQGGRFEAALTGGAPSAHGSEQVEFLVAGHAGSTPRPLAKVASGGELSRISLALSVIASRAARVPTLIFDEVDSGVGGAVAEAVGKLLRELGQRHQVLCVTHLPQVAACAHAQYRVSKVESGGSTRSRIAELDAEARVEEVARMLGGIKITATTRDHAREMLGGHTAPAA
>CP024175.1|AZW33519.1|4123963_4124383_-|transcriptional-repressor
MSDQSELKNMGLKATFPRLKILDIFRKSDLRHLSAEDVYRALIAENVEIGLATVYRVLTQFEQAGILTRSQFDTGKAVFELNDGDHHDHLICTNCGTVFEFSDPDIEKRQYKVAKDNGFVLESHAMVLYGICGNCQKGR

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Crispr_ID: CP024175_4

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

CP024175_4

4322783-4322992

Orphan

Consensus_repeat	Method
GTGCCTGTCCCCGCTGGGACAGGCAC	CRISPRCasFinder
GTGCCTGTCCCCGCTGGGACAGGCAC	PILER-CR

3 spacers

The CRISPR arrays of CP024175_4

>merge|CP024175|4|4322783-4322992|CRISPRCasFinder,PILER-CR
GTGCCTGTCCCCGCAGGGGGACTGGCACCCACAAATTCCTGGGGTGCCTGTCCCCGCAGGGGGACTGGCACCTGCAAGATTTCATGGCGTCTGCCCGTGCGTGTGCCTGTCCCCGCTGGGACAGGCACACTACCGTACGCCATCGACGCGACGGCCAAGACGGTATCTGCCCCGCGGGAATCCGGTGCCTGTCCCCGCTGGGACAGGCAC

>CP024175|4|4|4322783-4322992|CRISPRCasFinder
GTGCCTGTCCCCGCAGGGGGACTGGC	ACCCACAAATTCCTGGG
GTGCCTGTCCCCGCAGGGGGACTGGC	ACCTGCAAGATTTCATGGCGTCTGCCCGTGCGT
GTGCCTGTCCCCGCTGGGACAGGCAC	ACTACCGTACGCCATCGACGCGACGGCCAAGACGGTATCTGCCCCGCGGGAATCCG
GTGCCTGTCCCCGCTGGGACAGGCAC

>CP024175|4|1|4322826-4322992|PILER-CR
GTGCCTGTCCCCGCAGGGGGACTGGC	ACCTGCAAGATTTCATGGCGTCTGCCCGTGCGTGTGCCTGT
CCCCGCTGGGACAGGCACACTACCGT	ACGCCATCGACGCGACGGCCAAGACGGTATCTGCCCCGCGGGAATCCGGTGCCTGT
CCCCGCTGGGACAGGCAC

Protein	Signature genes	Signature genes Name	Protein_function
CP024175.1\|AZW32467.1\|4316131_4317046_+\|NAD(P)-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|224995
CP024175.1\|AZW32479.1\|4328610_4329126_+\|3-isopropylmalate-dehydratase	unknown	unknown	gnl\|CDD\|234762
CP024175.1\|AZW32476.1\|4325562_4326528_+\|tripartite-tricarboxylate-transporter-substrate-binding-protein	unknown	unknown	gnl\|CDD\|270296
CP024175.1\|AZW32473.1\|4321844_4322675_-\|itaconyl-CoA-hydratase	unknown	unknown	gnl\|CDD\|226300
CP024175.1\|AZW32468.1\|4317042_4317843_+\|NAD(P)-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|212491
CP024175.1\|AZW32483.1\|4332328_4334467_+\|glycine--tRNA-ligase-subunit-beta	unknown	unknown	gnl\|CDD\|234925
CP024175.1\|AZW32481.1\|4329985_4331176_-\|MFS-transporter	unknown	unknown	gnl\|CDD\|340883
CP024175.1\|AZW32464.1\|4313919_4314330_-\|4-carboxymuconolactone-decarboxylase	unknown	unknown	gnl\|CDD\|131478
CP024175.1\|AZW32482.1\|4331352_4332327_+\|glycine--tRNA-ligase-subunit-alpha	unknown	unknown	gnl\|CDD\|236473
CP024175.1\|AZW32475.1\|4324612_4325380_-\|enoyl-CoA-hydratase	unknown	unknown	gnl\|CDD\|181325
CP024175.1\|AZW32472.1\|4320651_4321848_-\|CoA-transferase	unknown	unknown	gnl\|CDD\|224717
CP024175.1\|AZW32466.1\|4315281_4316079_+\|beta-D-hydroxybutyrate-dehydrogenase	unknown	unknown	gnl\|CDD\|187644
CP024175.1\|AZW32471.1\|4319815_4320655_-\|CoA-ester-lyase	unknown	unknown	gnl\|CDD\|225184
CP024175.1\|AZW32477.1\|4326549_4327329_+\|GntR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|225099
CP024175.1\|AZW32478.1\|4327351_4328614_+\|3-isopropylmalate-dehydratase-large-subunit	unknown	unknown	gnl\|CDD\|234748
CP024175.1\|AZW32474.1\|4323020_4324544_-\|fumarate-hydratase	unknown	unknown	gnl\|CDD\|224862
CP024175.1\|AZW32465.1\|4314457_4315285_+\|N-acyl-homoserine-lactonase-family-protein	unknown	unknown	gnl\|CDD\|293815
CP024175.1\|AZW32470.1\|4318897_4319812_-\|sugar-kinase	unknown	unknown	gnl\|CDD\|238920
CP024175.1\|AZW32469.1\|4317877_4318864_+\|tripartite-tricarboxylate-transporter-substrate-binding-protein	unknown	unknown	gnl\|CDD\|270296
CP024175.1\|AZW32480.1\|4329125_4329989_+\|carboxyvinyl-carboxyphosphonate-phosphorylmutase	unknown	unknown	gnl\|CDD\|225311

Protein	Function_ID	Function_description	E-value
CP024175.1\|AZW32467.1\|4316131_4317046_+\|NAD(P)-dependent-oxidoreductase	gnl\|CDD\|224995	COG2084, MmsB, 3-hydroxyisobutyrate dehydrogenase and related beta-hydroxyacid dehydrogenases [Lipid metabolism].	3.88012e-72
CP024175.1\|AZW32479.1\|4328610_4329126_+\|3-isopropylmalate-dehydratase	gnl\|CDD\|234762	PRK00439, leuD, 3-isopropylmalate dehydratase small subunit; Reviewed.	1.24963e-57
CP024175.1\|AZW32476.1\|4325562_4326528_+\|tripartite-tricarboxylate-transporter-substrate-binding-protein	gnl\|CDD\|270296	cd13578, PBP2_Bug27, Aromatic solutes transporter of Bug (Bordetella uptake gene) protein family; contains the type 2 periplasmic binding fold. Bug27 binds non-carboxylated solute nicotinamide, in contrast to BugD (aspartic acid transporter) and BugE (glutamate transporter) which both bind aliphatic carboxylated ligands. The Bug (Bordetella uptake gene) protein family is a large family of periplasmic solute-binding (PBP) receptors present in a number of bacterial species, but mainly in proteobacteria. Bug proteins are the PBP components of the tripartite carboxylate transporters (TTT). Their expansive expansion in proteobacteria indicates a large functional diversity.	5.10374e-127
CP024175.1\|AZW32473.1\|4321844_4322675_-\|itaconyl-CoA-hydratase	gnl\|CDD\|226300	COG3777, COG3777, Uncharacterized conserved protein [Function unknown].	3.36813e-95
CP024175.1\|AZW32468.1\|4317042_4317843_+\|NAD(P)-dependent-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.	3.62974e-56
CP024175.1\|AZW32483.1\|4332328_4334467_+\|glycine--tRNA-ligase-subunit-beta	gnl\|CDD\|234925	PRK01233, glyS, glycyl-tRNA synthetase subunit beta; Validated.	0
CP024175.1\|AZW32481.1\|4329985_4331176_-\|MFS-transporter	gnl\|CDD\|340883	cd17325, MFS_MdtG_SLC18_like, bacterial MdtG-like and eukaryotic solute carrier 18 (SLC18) family of the Major Facilitator Superfamily of transporters. This family is composed of eukaryotic solute carrier 18 (SLC18) family transporters and related bacterial multidrug resistance (MDR) transporters including several proteins from Escherichia coli such as multidrug resistance protein MdtG, from Bacillus subtilis such as multidrug resistance proteins 1 (Bmr1) and 2 (Bmr2), and from Staphylococcus aureus such as quinolone resistance protein NorA. The family also includes Escherichia coli arabinose efflux transporters YfcJ and YhhS. MDR transporters are drug/H+ antiporters (DHA) that mediate the efflux of a variety of drugs and toxic compounds, and confer resistance to these compounds. The SLC18 transporter family includes vesicular monoamine transporters (VAT1 and VAT2), vesicular acetylcholine transporter (VAChT), and SLC18B1, which is proposed to be a vesicular polyamine transporter (VPAT). The MdtG/SLC18 family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	1.45801e-43
CP024175.1\|AZW32464.1\|4313919_4314330_-\|4-carboxymuconolactone-decarboxylase	gnl\|CDD\|131478	TIGR02425, putative_gamma-carboxymuconolactone_decarboxylase, 4-carboxymuconolactone decarboxylase. Members of this family are 4-carboxymuconolactone decarboxylase, which catalyzes the third step in the catabolism of protocatechuate (and therefore the fourth step in the catabolism of para-hydroxybenzoate, of 3-hydroxybenzoate, of vanillate, etc.). Most members of this family are encoded within protocatechuate catabolism operons. This protein is sometimes found as a fusion protein with other enzymes of the pathway, as in Rhodococcus opacus, Streptomyces avermitilis, and Caulobacter crescentus. [Energy metabolism, Other].	2.57263e-46
CP024175.1\|AZW32482.1\|4331352_4332327_+\|glycine--tRNA-ligase-subunit-alpha	gnl\|CDD\|236473	PRK09348, glyQ, glycyl-tRNA synthetase subunit alpha; Validated.	0
CP024175.1\|AZW32475.1\|4324612_4325380_-\|enoyl-CoA-hydratase	gnl\|CDD\|181325	PRK08252, PRK08252, crotonase/enoyl-CoA hydratase family protein.	4.12983e-154
CP024175.1\|AZW32472.1\|4320651_4321848_-\|CoA-transferase	gnl\|CDD\|224717	COG1804, CaiB, Predicted acyl-CoA transferases/carnitine dehydratase [Energy production and conversion].	3.36283e-152
CP024175.1\|AZW32466.1\|4315281_4316079_+\|beta-D-hydroxybutyrate-dehydrogenase	gnl\|CDD\|187644	cd08940, HBDH_SDR_c, d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs. DHBDH, an NAD+ -dependent enzyme, catalyzes the interconversion of D-3-hydroxybutyrate and acetoacetate. It is a classical SDR, with the canonical NAD-binding motif and active site tetrad. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.	1.95026e-85
CP024175.1\|AZW32471.1\|4319815_4320655_-\|CoA-ester-lyase	gnl\|CDD\|225184	COG2301, CitE, Citrate lyase beta subunit [Carbohydrate transport and metabolism].	2.12464e-69
CP024175.1\|AZW32477.1\|4326549_4327329_+\|GntR-family-transcriptional-regulator	gnl\|CDD\|225099	COG2188, PhnF, Transcriptional regulators [Transcription].	2.01574e-61
CP024175.1\|AZW32478.1\|4327351_4328614_+\|3-isopropylmalate-dehydratase-large-subunit	gnl\|CDD\|234748	PRK00402, PRK00402, 3-isopropylmalate dehydratase large subunit; Reviewed.	0
CP024175.1\|AZW32474.1\|4323020_4324544_-\|fumarate-hydratase	gnl\|CDD\|224862	COG1951, TtdA, Tartrate dehydratase alpha subunit/Fumarate hydratase class I, N-terminal domain [Energy production and conversion].	1.20835e-140
CP024175.1\|AZW32465.1\|4314457_4315285_+\|N-acyl-homoserine-lactonase-family-protein	gnl\|CDD\|293815	cd07729, AHL_lactonase_MBL-fold, quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain. Acyl Homoserine Lactones (also known as AHLs) are signal molecules which coordinate gene expression in quorum sensing, in many Gram-negative bacteria. Quorum-quenching N-acyl-homoserine lactonase (also known as AHL lactonase, N-acyl-L-homoserine lactone hydrolase, EC 3.1.1.81) catalyzes the hydrolysis and opening of the homoserine lactone rings of AHLs, a reaction that can block quorum sensing. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.	1.25412e-68
CP024175.1\|AZW32470.1\|4318897_4319812_-\|sugar-kinase	gnl\|CDD\|238920	cd01945, ribokinase_group_B, Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time. .	7.74279e-101
CP024175.1\|AZW32469.1\|4317877_4318864_+\|tripartite-tricarboxylate-transporter-substrate-binding-protein	gnl\|CDD\|270296	cd13578, PBP2_Bug27, Aromatic solutes transporter of Bug (Bordetella uptake gene) protein family; contains the type 2 periplasmic binding fold. Bug27 binds non-carboxylated solute nicotinamide, in contrast to BugD (aspartic acid transporter) and BugE (glutamate transporter) which both bind aliphatic carboxylated ligands. The Bug (Bordetella uptake gene) protein family is a large family of periplasmic solute-binding (PBP) receptors present in a number of bacterial species, but mainly in proteobacteria. Bug proteins are the PBP components of the tripartite carboxylate transporters (TTT). Their expansive expansion in proteobacteria indicates a large functional diversity.	9.50228e-138
CP024175.1\|AZW32480.1\|4329125_4329989_+\|carboxyvinyl-carboxyphosphonate-phosphorylmutase	gnl\|CDD\|225311	COG2513, PrpB, PEP phosphonomutase and related enzymes [Carbohydrate transport and metabolism].	4.31561e-89

>CP024175.1|AZW32473.1|4321844_4322675_-|itaconyl-CoA-hydratase
MTATSLAAWIGSSERVQDSLDPIAVGRVAATLGEPAPGAGQPLPPLWQWAFFIGTVGLDGLGRDGHPARGGFLPPADDRNRMWAGGRVEFRQPLRVGVPAERLSTVASIQEKTGRTGALLFVTVRHEYRQEGELAILEEQDIVYRQPSPPKLAGTEPAPAAQWRETMTPSEVLLFRYSAVTFNGHRIHYDYPYVTGVEGYPGLVVHGPMIATMMVAAFRRAHPGARLDHLSYRGLRPLIAPRPFEVAGAVAEPGLARLWAQQDDTLAHQGELRFTA
>CP024175.1|AZW32472.1|4320651_4321848_-|CoA-transferase
MSDVPAIRPLDGITVVSLEHAIAAPFCTRQLADMGARVIKIERPGSGDFARGYDERVRGLSSHFVWTNRSKESLTLDLKRPGADEVLERLLASADVLVQNLAPGAAARLGLSFEQLHARFSRLIVCDISGYGQGGPYQDKKAYDLLIQSESGFVSVTGTPDEPVKAGCSISDIAAGMYAYSGILNALLLRGKTGVGSRIDVSMLESTVEWMGYPMYYAFDDAPPPPRAGAAHATIYPYGPFPVGDGATIMLGLQNEREWRAFCERVLRQPELADDERYASNSRRAANRDALRALIVAAFARLDIGEVTARLEQAQIANARVNQMRDVWKHPQLQARQRWREVDSPAGTLPALLPPATSNAFAARMDAVPAVGENTAAVLASLGYAPDEVARLRAAEVV
>CP024175.1|AZW32471.1|4319815_4320655_-|CoA-ester-lyase
MMQTVVRTALFVPASRPERIPKALASGADAVIVDLEDAVEHLAKDSAREALCDFLGTHPDARLWVRINDASTAWHDDDLKACRGRPGVRGILLPKAESLMQVRHAAQSGIPIVPIIETARGVLNAADVAGTPGVARLAFGSLDYALDLGLTPDTEAAGVVLDQARVQVLLHSRAAGLAQPLDGVHPGVQDTAGLRAAATRARDMGFAGMLCIHPTQVPIVHEALLPPLAELDWARRVVAAHRDSGAGTFMLDGKMVDAPVIARARQLLARAGEPAGQEA
>CP024175.1|AZW32470.1|4318897_4319812_-|sugar-kinase
MAAPGPAPAALFVGHAYIDVTLLADEWPSGDEKRVARDYAVSFGGNAVTAAFACARLGLAPDLICPQAPDWLGHMFADMAASHGVRVHPRPVRRSSLSFIMPRDGKRAILRARDTDYLQSFPLLEVGGYRVLHLDGHQPDAALHYARACRAAGVLTSLDGGGLRSNTAELMRHIDVAVCAERLCEQMGLSAEALLEWLRDCGCRIGAVTQGERGMLWYDEAGVVSRLPALDIPASAVVDTSGAGDVFHGAYVWSYAARPQLPWREHFRFARAAAAYKIQHLGNEAGLPGQDDVAAVMARWPEKA
>CP024175.1|AZW32469.1|4317877_4318864_+|tripartite-tricarboxylate-transporter-substrate-binding-protein
MSGSFLKALRRAPLLALCLTLLPAAAARAAYPERPVRVIVPFAAGGGADIVARLVFKGVSEQLGQPFIIDNRGGAGGIIGTDAVAKAEADGYTLLLGQSGPNAINPSVYSKLPYDARKDFAPVTQLTSYPYVVAVKNGLAPNNLRELIELARREPGTLTLSTAGQGSSAHLAVELFMRQAGIVVIPVPYKGAGPALLDVVGGVVDMTFGDAASASKQAQAGKIKALAVTGARRSPLIPDVPTVQEAGVPGYEASAWHAVLAPRGTPQPVIQTLYTAIGKVLADPQLKARLAQDGIEAVGSEPQAFGQALNAEIDKWQKVVEDAGIRLE
>CP024175.1|AZW32468.1|4317042_4317843_+|NAD(P)-dependent-oxidoreductase
MSTAGVAVITGGASGIGAACARRFAAQGMAVAILDVAREAGEALAAELGAQGAPARFYACDVADAAAVQACADAVSAELGETALLVTSAALIPNTESVLDMDLAEHDRMWRVNYHGTVHACRSFGRILRARRAGHIVTLGSINSRNALPLPAYNPGKAALARLTELLAQELGRHGVRVNSVAPTYVMTPALQARIDAGQRDLAAMMSVHALDALPTPADIADAVAFLCSPQARLITGVLLPVDAGWASGISYRTYAGGMPPQSHGA
>CP024175.1|AZW32467.1|4316131_4317046_+|NAD(P)-dependent-oxidoreductase
MTTEKHLGFVGIGRMGTPIAERLLEAGYTLTVYDTQAPALQALAAKGAHIADSPKAVADRAETVLVSLPTPDIVLAVALGENGLARGGAVRTVIDLSTSGSQAARTLADGLAAQNIASIDCPVSGGVTGAKRGTLALMVSGPRDRYDALHDMFGVIGKPVYVGERAGMAQTMKVINNLISVTALSITSELMVMGVKAGLDPDIMLQVINSGSGRTNASEDKIPRFVLTRSFDFGFAIGLSAKDVRLCLEESEQLGVPLRVGDAARRLLNDARDKFGNDADLTEIIRYVEDNAGVQVRGKAADAA
>CP024175.1|AZW32466.1|4315281_4316079_+|beta-D-hydroxybutyrate-dehydrogenase
MNPARPLHGRCALVTGAEAGLGLAIADTLARAGADIVMHCLQANESARQAQAALAREHGVRVLLLQADLRDVDQIEAMAAQALAELPRLDILVNNAVVRHFEPAHELPRAHWDESLAVNLSAAFHLARLALPGMLAQGWGRIINLSSVYGAGGAANRVGYVTTKTALLGLTRALAVETAASGITCNAVAPGTAPTPAIVGRIADIARRDGVAQEQAEREYLAARQPTGRFVAMENVAALVAFLCSDAGRDITGATLPIDGGWTAA
>CP024175.1|AZW32465.1|4314457_4315285_+|N-acyl-homoserine-lactonase-family-protein
MNCAPFDVYAIRYARHSGRIAADNYLGKVDFHDAESDLDYYVWALRRGDEVYVVDTGFAEDAARQRGRELLMRPAQGLALIGIDAAQVRDVILTHLHYDHAGTLGDFPAATFHVQDAEPAYATGRCMCHGPLRHPYDVEDVVGFVRKVYAGRVSFHNGQTELAPGLSLHLVGGHTGGLQIVRVWTQRGWVVLASDASHLYGNIGHDAPFPAVYHVGDMLEGYRTVRRLADSEAHIVPGHDPQVMQRYPAPTPELQGKVVRLDVAPTPDSLVPEAA
>CP024175.1|AZW32464.1|4313919_4314330_-|4-carboxymuconolactone-decarboxylase
MALRPEFQTEQFQKGLAVRRAVVGDAYVDKSLNSADDLTASLQKLVTEYCWGEVWTRPGLERKTRSFLNLAMLIALNRPNELRLHLRGAINNGVTKEEIVEVVLQAAIYCGVPAGLDAMKAVREVVETMEKEGAFA
>CP024175.1|AZW32474.1|4323020_4324544_-|fumarate-hydratase
MTVLIKEEDFIQSIADGIQFISYYHPVDYIRHLARAYEREESPAARDAMAQILTNSRMCAEGKRPLCQDTGIVNVFLKVGMNVRFDTQRTLQELCDEGVRRGYLNPDNPLRASVLDDPLFARKNTRDNTPCILHVELVPGDTVDVQVASKGGGSENKSKFVMLNPSDSLVDWVLKTVPTMGAGWCPPGMLGIGVGGTAEKAMLMAKQSLMEDIDMYELLARGPQNKLEELRIELYEKVNALGIGAQGLGGLTTVLDVKISTFPTHAASKPVAMIPNCAATRHAHFVLDGSGPARLDPPSLSEWPEVHWAPDYNKSRQVDLDTLTKEEVASWKPGQTLLLSGKMLTGRDAAHKRIQDMLSKGESLPVDFTNRVIYYVGPVDPVRDEVVGPAGPTTATRMDKFTDMMLAQTGLISMIGKSERGPVAIESIRKHGSAYLMAVGGAAYLVSKAIRNAKVLAFEDLGMEAIYEFDVKDMPVTVAVDSQGTSVHTTGPKEWQARIGKIPVAVA
>CP024175.1|AZW32475.1|4324612_4325380_-|enoyl-CoA-hydratase
MSELVKVEIADGIQIITVNRPEARNAINFETAQAMAAALDQLDERDDVRIGILTGAGGTFSAGMDLKAFARTGQRPSLPERGFAALTERPPKKPLIAAVEGYALAGGCEMALSCDLLVAADNAKFGLPEVKRGLVPGAGGMLRLPRRLPYHIAMEIILTGDFLDASRAHALGLVNRLTAAGGALEGALALARVIVENGPLAVQVAKSIVAQSGDWDQETMFDRQRPQVTEIFTSADAKEGATAFAEKRKPVWQGK
>CP024175.1|AZW32476.1|4325562_4326528_+|tripartite-tricarboxylate-transporter-substrate-binding-protein
MQGLQRLAAGCALFGALALPLAPASAQNNAIKLVVGAPPGGTTDTVARSIAQHMAQDLKRTVLVENKPGAGGNIAADYVAKGKADGSTLLVTFTSFSINASLYRNLPFDPVRDFTPISMLANVPSVLVTRKDFPARTMPEFVSLVQASPGKYTMALGAIGSSLHMAGERMKMMAGLDILNVPYKGTSPAITDLLGGQVDMMVASSLNALPHIKSGALKALGVTSPQPLPQFPGVPPIGDTIKGFESNAWFALFGPAGLPPETVAALNAAARKAVDTPEFRKLLEGEAATAVSSSPQELDEFVRKDIERYAELVKFTGATVD
>CP024175.1|AZW32477.1|4326549_4327329_+|GntR-family-transcriptional-regulator
MPDSPLPLYHKVYLLLKQRLQSGGFALNAAMPGENALAAEYGVSRLTIRRSLEALESEGLIERRQGRGTFAAEGAILSAPQHSADIDTLMAHLARMGMHTQVNLLELDTVPATPQVAAQLELPAGAPVQRAVRVRSHQGLPFSYLVTYVPGEIGQRIRREDLGAKPLLAIFRDLGVRVARAQQSISAVLAEPGTAGALDVPVGSALLSLQRLVRDDAGRPVEWLHALYRPDRYEYRLDMQAHDTPGQPTWLPAGAPRRA
>CP024175.1|AZW32478.1|4327351_4328614_+|3-isopropylmalate-dehydratase-large-subunit
MPAQTLAQKLLAAAAGRDAVRVGEIVTCKVDLAMFHDSSGPRRLQPMLEELGTGLWDRSRIVLVMDHYVPESDEESRRIVRIARDWAREQALPHVYDSLGICHVVVPEHGHVRPGMFCVGGDSHSPTGGAFGAYMFGVGSTEMLGVVSSGEIWMRVPDTLMMHWRGRLRPGVMAKDMMLHMIGLHGMNGGRYQAVEFCGEAVRALSMQERMTLSNMSAELGAQAGLIAPDRTTAQYLRQAGAPEPDTARWQSDPDAPAQWHEYDADSLPPYVAAPHSPANAAPVQAYADTAVQVAYIGACTGAKLDDLRAAAQVLRGRRVAPGVSLLVAPASQRDQARAQDEGVLPALVEAGATVLPTTCGACSGYGGSIPDGANVISTTARNFKGRMGAASARVYLASPYTVAASALAGRIADPREVLS
>CP024175.1|AZW32479.1|4328610_4329126_+|3-isopropylmalate-dehydratase
MSETHQAWRVGDDVDTDQLAPGAYMKLGIADIARHCLEGVRPDFAGGVRPGDVLVAGRNFGIGSSREQAAAALVQLGLRAVVAPSYSGLYFRNAFNVGLLLLTCERAGEIAEGERIRIDLPNQRVLRADGTPLPCEPVPAFLLDMVQAGGLLMQLKRRLADGSLPRYPMKA
>CP024175.1|AZW32480.1|4329125_4329989_+|carboxyvinyl-carboxyphosphonate-phosphorylmutase
MTPASLKHKLAAGQALLAPGVYDALSALIAEQAGFDAVYLSGASIAYTRLGRSDVGLTTYSEVEDVLARITERVRCPVIVDADTGFGNALNVQRTVRGFERAGAAMIQLEDQDFPKRCGHLAGKSLVPADEMCGKLRAALDARASDGTLILARTDAVAVEGIDAAFERAERYLECGVDALFIEALRSPQQLDAACARFAARVPLLANMVEGGQTPVESAQALAERGFRIVIFPGGTARAVSHALQDYYGSLREHGTTAPWRARMLDFDQLNALIGTPALLETAERYR
>CP024175.1|AZW32481.1|4329985_4331176_-|MFS-transporter
MSDHDASFSLKDIAVPAFGPSILYGVSNGAILPVVALTARELGASLATSGLIVGLVGIGSLVSNIPAAMFTSRHGERRSMVGAAALSVVALLLCIFAGTLWMLATGVFMVGMASSVFLLARQGYMIDAVPAYMRARALSTLAGTMRIGVFAGPFAGAALIHFMGLQGAYWVAAVAMTGAGLIAWFAPDMAPPRRRGEAAVARPRLLDVARAHRQVYLTLGLGILLVSAVRASRQVVIPLWADHLGVNPATTSLIYGLVAAIDMSVFYPAGMLMDRRGRLWVAVPSTLLMGCALIGTSLTSGVAGFVIVAMMLGMGNGIGSGIVMTLGADAAPASGRTEFLGLWRLMSDLGGSLGPVALSGITALVSLAAGVAAMGGVGLAAAAVFWHWLPRGQAPR
>CP024175.1|AZW32482.1|4331352_4332327_+|glycine--tRNA-ligase-subunit-alpha
MAGFPRCRLARGLPRPDFLTPMLTFQQIILTLQDYWDKQGCALLQPYDMEVGAGTSHTATFLRAIGPEPWRAAYVQPSRRPKDGRYGENPNRLQHYYQYQVVLKPAPPEILDLYIGSLKALGIDPTQHDIRFVEDDWENPTLGAWGLGWEVWLNGMEVTQFTYFQQVGGLDCTPTTGEITYGLERLAMYLQDVESVYDLVWTEGANGNRVYYRDVFHQNEVEQSTYNFEHASADMLFAHFNDYEAEAKRLMDVPLALPAYEAALKAAHTFNMLDARGAISVTERAAYIGRIRNLSRAVAQAYYESRERLGFPMLAGRKAAGEAA
>CP024175.1|AZW32483.1|4332328_4334467_+|glycine--tRNA-ligase-subunit-beta
MTTDIRPLLVELFTEELPPKALQKLGQAFAEGVRATLARHHLLADGCAVEPFATPRRLAVRLSAVLAQAPEQAYAEKLMPVKVGLDANGQPTAALAKKLAAKGLEGLDPATLERESDGKQEYLVARGTAAGAQLAAGLQEGLDAAIDGLPIPKVMRYQLADGQTTVKFVRPAHGLVALFGADIVPVAALGLQAGRATQGHRFQSNGAIELATAQGYEADLAERGRVIASFEARRAEISRLLDEHAQRLGATLGDDPEVTALLDEVTALVEHPTVYVGQFEEQFLQVPQECLILTMRLNQKYFPLFDPASGKLTHRFLIVSNMQVADPANIVEGNQRVVRPRLADAQFFFETDRKTPLAARVEQLGSIVYHNKLGTQLERVERVRAIARGIATALGGDAAHCDRAALLAKADLGSNMVGEFPELQGIMGAYYAQGDGEPADVVTALRTQYRNRYDAPVDAATLTAATLFIAERIETLVGIWSIGLAPTGERDPFGLRRAALGLISAFEQLAAGGWLKVSEDGPLSLDGLLALAAQAFPDGKIGADTLAEVRAFIYERYRNQLIGEHDRNAVEAVIALAPPLHQVAARVRAVAAFAQLPAAASLAAANKRIGNLLKKAEGEIGAVDAALLQDPAEKALAEAVAQLRPQARAQLQAGDFAASLATLAQAREPVDAFFADVMVMADDAALRANRLALLGQLHGLMNQVADISRLAQ

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Crispr_ID: CP024175_5

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

CP024175_5

4511711-4511804

Orphan

Consensus_repeat	Method
GTGCCTGTCCCCGCCGGGACAGGCAC	CRISPRCasFinder

1 spacers

The CRISPR arrays of CP024175_5

>merge|CP024175|5|4511711-4511804|CRISPRCasFinder
GTGCCTGTCCCCGCCGGGACAGGCACCCGGGCCCAGGAACCCCCCCACGCTGCGCCCGCTGTGCGGGCGTGCCTGTCCCCACCGGGACAGGCAC

>CP024175|5|5|4511711-4511804|CRISPRCasFinder
GTGCCTGTCCCCGCCGGGACAGGCAC	CCGGGCCCAGGAACCCCCCCACGCTGCGCCCGCTGTGCGGGC
GTGCCTGTCCCCACCGGGACAGGCAC

Protein	Signature genes	Signature genes Name	Protein_function
CP024175.1\|AZW32635.1\|4517509_4518613_-\|ChbG/HpnK-family-deacetylase	unknown	unknown	gnl\|CDD\|212118
CP024175.1\|AZW33535.1\|4514468_4515383_+\|EamA/RhaT-family-transporter	unknown	unknown	gnl\|CDD\|223769
CP024175.1\|AZW32627.1\|4508846_4509365_+\|methyltransferase	unknown	unknown	gnl\|CDD\|224204
CP024175.1\|AZW32636.1\|4518800_4520420_-\|dolichyl-phosphate-mannose--protein-mannosyltransferase	unknown	unknown	gnl\|CDD\|224720
CP024175.1\|AZW32630.1\|4512435_4512780_-\|TIGR01244-family-phosphatase	unknown	unknown	gnl\|CDD\|225984
CP024175.1\|AZW32633.1\|4516128_4517052_+\|alpha/beta-hydrolase	unknown	unknown	gnl\|CDD\|378820
CP024175.1\|AZW32621.1\|4502449_4503610_-\|acyl-CoA-dehydrogenase	unknown	unknown	gnl\|CDD\|173841
CP024175.1\|AZW32619.1\|4500134_4501328_-\|acetyl-CoA-C-acyltransferase	unknown	unknown	gnl\|CDD\|180775
CP024175.1\|AZW32623.1\|4504735_4505707_-\|tripartite-tricarboxylate-transporter-substrate-binding-protein	unknown	unknown	gnl\|CDD\|270234
CP024175.1\|AZW32622.1\|4503747_4504725_+\|LysR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|176106
CP024175.1\|AZW33536.1\|4518532_4518841_+\|GtrA-family-protein	unknown	unknown	gnl\|CDD\|377229
CP024175.1\|AZW32626.1\|4507980_4508736_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|223930
CP024175.1\|AZW32632.1\|4515379_4516039_+\|LysE-family-translocator	unknown	unknown	gnl\|CDD\|224199
CP024175.1\|AZW32620.1\|4501394_4502423_-\|acyl-CoA-dehydrogenase	unknown	unknown	gnl\|CDD\|366103
CP024175.1\|AZW32634.1\|4517057_4517513_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|226610
CP024175.1\|AZW32631.1\|4512879_4514280_-\|PLP-dependent-aminotransferase-family-protein	unknown	unknown	gnl\|CDD\|224089
CP024175.1\|AZW32629.1\|4511876_4512347_-\|universal-stress-protein	unknown	unknown	gnl\|CDD\|366180
CP024175.1\|AZW32628.1\|4509361_4511485_-\|elongation-factor-G	unknown	unknown	gnl\|CDD\|234569
CP024175.1\|AZW32624.1\|4505773_4506559_-\|enoyl-CoA-hydratase	unknown	unknown	gnl\|CDD\|181723
CP024175.1\|AZW32625.1\|4506551_4507784_-\|CoA-transferase	unknown	unknown	gnl\|CDD\|367110

Protein	Function_ID	Function_description	E-value
CP024175.1\|AZW32635.1\|4517509_4518613_-\|ChbG/HpnK-family-deacetylase	gnl\|CDD\|212118	cd10807, YdjC_like_3, uncharacterized YdjC-like family proteins from bacteria. This subfamily contains many hypothetical proteins, and belongs to the YdjC-like family of uncharacterized proteins from bacteria. The YdjC-family is represented by an uncharacterised protein YdjC (also known as ChbG) encoded by the chb (N,N'-diacetylchitobiose, also called [GlcNAc]2) or cel operon in Escherichia coli, which encodes enzymes involved in growth on an N,N'-diacetylchitobiose carbon source. The molecular function of this subfamily is unclear.	3.026e-93
CP024175.1\|AZW33535.1\|4514468_4515383_+\|EamA/RhaT-family-transporter	gnl\|CDD\|223769	COG0697, RhaT, Permeases of the drug/metabolite transporter (DMT) superfamily [Carbohydrate transport and metabolism / Amino acid transport and metabolism / General function prediction only].	1.28877e-09
CP024175.1\|AZW32627.1\|4508846_4509365_+\|methyltransferase	gnl\|CDD\|224204	COG1285, SapB, Uncharacterized membrane protein [Function unknown].	1.24362e-44
CP024175.1\|AZW32636.1\|4518800_4520420_-\|dolichyl-phosphate-mannose--protein-mannosyltransferase	gnl\|CDD\|224720	COG1807, ArnT, 4-amino-4-deoxy-L-arabinose transferase and related glycosyltransferases of PMT family [Cell envelope biogenesis, outer membrane].	1.98065e-51
CP024175.1\|AZW32630.1\|4512435_4512780_-\|TIGR01244-family-phosphatase	gnl\|CDD\|225984	COG3453, COG3453, Uncharacterized protein conserved in bacteria [Function unknown].	1.33393e-34
CP024175.1\|AZW32633.1\|4516128_4517052_+\|alpha/beta-hydrolase	gnl\|CDD\|378820	pfam12146, Hydrolase_4, Serine aminopeptidase, S33. This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2.	2.97616e-21
CP024175.1\|AZW32621.1\|4502449_4503610_-\|acyl-CoA-dehydrogenase	gnl\|CDD\|173841	cd01152, ACAD_fadE6_17_26, Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26. Putative acyl-CoA dehydrogenases (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position.	4.43018e-83
CP024175.1\|AZW32619.1\|4500134_4501328_-\|acetyl-CoA-C-acyltransferase	gnl\|CDD\|180775	PRK06954, PRK06954, acetyl-CoA C-acetyltransferase.	2.70376e-175
CP024175.1\|AZW32623.1\|4504735_4505707_-\|tripartite-tricarboxylate-transporter-substrate-binding-protein	gnl\|CDD\|270234	cd07012, PBP2_Bug_TTT, Bug (Bordetella uptake gene) protein family of periplasmic solute-binding receptors; contains the type 2 periplasmic binding fold. The Bug (Bordetella uptake gene) protein family is a large family of periplasmic solute-binding (PBP) proteins present in a number of bacterial species, but mainly in proteobacteria. In eubacteria, at least three families of periplasmic binding-protein dependent transporters are known: the ATP-binding cassette (ABC) transporters, the tripartite ATP-independent periplasmic transporters, and the tripartite tricarboxylate transporters (TTT). Bug proteins are the PBP components of the TTT. Their expansive expansion in proteobacteria indicates a large functional diversity. The best studied examples are Bordetella pertussis BugD, which is an aspartic acid transporter, and BugE, which is glutamate transporter.	1.39784e-117
CP024175.1\|AZW32622.1\|4503747_4504725_+\|LysR-family-transcriptional-regulator	gnl\|CDD\|176106	cd08414, PBP2_LTTR_aromatics_like, The C-terminal substrate binding domain of LysR-type transcriptional regulators involved in the catabolism of aromatic compounds and that of other related regulators, contains type 2 periplasmic binding fold. This CD includes the C-terminal substrate binding domain of LTTRs involved in degradation of aromatic compounds, such as CbnR, BenM, CatM, ClcR and TfdR, as well as that of other transcriptional regulators clustered together in phylogenetic trees, including XapR, HcaR, MprR, IlvR, BudR, AlsR, LysR, and OccR. The structural topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the substrate-binding domains from ionotropic glutamate receptors, LysR-like transcriptional regulators, and unorthodox sensor proteins involved in signal transduction.	3.89179e-59
CP024175.1\|AZW33536.1\|4518532_4518841_+\|GtrA-family-protein	gnl\|CDD\|377229	pfam04138, GtrA, GtrA-like protein. Members of this family are predicted to be integral membrane proteins with three or four transmembrane spans. They are involved in the synthesis of cell surface polysaccharides. The GtrA family are a subset of this family. GtrA is predicted to be an integral membrane protein with 4 transmembrane spans. It is involved is in O antigen modification by Shigella flexneri bacteriophage X (SfX), but does not determine the specificity of glucosylation. Its function remains unknown, but it may play a role in translocation of undecaprenyl phosphate linked glucose (UndP-Glc) across the cytoplasmic membrane. Another member of this family is a DTDP-glucose-4-keto-6-deoxy-D-glucose reductase, which catalyzes the conversion of dTDP-4-keto-6-deoxy-D-glucose to dTDP-D-fucose, which is involved in the biosynthesis of the serotype-specific polysaccharide antigen of Actinobacillus actinomycetemcomitans Y4 (serotype b). This family also includes the teichoic acid glycosylation protein, GtcA, which is a serotype-specific protein in some Listeria innocua and monocytogenes strains. Its exact function is not known, but it is essential for decoration of cell wall teichoic acids with glucose and galactose.	1.61408e-10
CP024175.1\|AZW32626.1\|4507980_4508736_-\|hypothetical-protein	gnl\|CDD\|223930	COG0861, TerC, Membrane protein TerC, possibly involved in tellurium resistance [Inorganic ion transport and metabolism].	1.14565e-78
CP024175.1\|AZW32632.1\|4515379_4516039_+\|LysE-family-translocator	gnl\|CDD\|224199	COG1280, RhtB, Putative threonine efflux protein [Amino acid transport and metabolism].	8.41728e-32
CP024175.1\|AZW32620.1\|4501394_4502423_-\|acyl-CoA-dehydrogenase	gnl\|CDD\|366103	pfam00441, Acyl-CoA_dh_1, Acyl-CoA dehydrogenase, C-terminal domain. C-terminal domain of Acyl-CoA dehydrogenase is an all-alpha, four helical up-and-down bundle.	5.75066e-13
CP024175.1\|AZW32634.1\|4517057_4517513_-\|hypothetical-protein	gnl\|CDD\|226610	COG4125, COG4125, Predicted membrane protein [Function unknown].	2.35069e-54
CP024175.1\|AZW32631.1\|4512879_4514280_-\|PLP-dependent-aminotransferase-family-protein	gnl\|CDD\|224089	COG1167, ARO8, Transcriptional regulators containing a DNA-binding HTH domain and an aminotransferase domain (MocR family) and their eukaryotic orthologs [Transcription / Amino acid transport and metabolism].	1.52472e-110
CP024175.1\|AZW32629.1\|4511876_4512347_-\|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.	9.38587e-30
CP024175.1\|AZW32628.1\|4509361_4511485_-\|elongation-factor-G	gnl\|CDD\|234569	PRK00007, PRK00007, elongation factor G; Reviewed.	0
CP024175.1\|AZW32624.1\|4505773_4506559_-\|enoyl-CoA-hydratase	gnl\|CDD\|181723	PRK09245, PRK09245, crotonase/enoyl-CoA hydratase family protein.	7.88581e-157
CP024175.1\|AZW32625.1\|4506551_4507784_-\|CoA-transferase	gnl\|CDD\|367110	pfam02515, CoA_transf_3, CoA-transferase family III. CoA-transferases are found in organisms from all lines of descent. Most of these enzymes belong to two well-known enzyme families, but recent work on unusual biochemical pathways of anaerobic bacteria has revealed the existence of a third family of CoA-transferases. The members of this enzyme family differ in sequence and reaction mechanism from CoA-transferases of the other families. Currently known enzymes of the new family are a formyl-CoA: oxalate CoA-transferase, a succinyl-CoA: (R)-benzylsuccinate CoA-transferase, an (E)-cinnamoyl-CoA: (R)-phenyllactate CoA-transferase, and a butyrobetainyl-CoA: (R)-carnitine CoA-transferase. In addition, a large number of proteins of unknown or differently annotated function from Bacteria, Archaea and Eukarya apparently belong to this enzyme family. Properties and reaction mechanisms of the CoA-transferases of family III are described and compared to those of the previously known CoA-transferases.	1.64046e-118

>CP024175.1|AZW32628.1|4509361_4511485_-|elongation-factor-G
MTRRTSIERYRNIGISAHIDAGKTTTTERILFYTGITHKLGEVHEGAATMDWMEQEQERGITITSAATTAFWRGMAGNYPEHRINIIDTPGHVDFTIEVERSMRVLDGACMVYDSVGGVQPQSETVWRQANKYGVPRIAFVNKMDRVGADFFRVQRQIVERLKGDAVPIQIPVGAEDHFEGVVDLVKMKAIIWDDASQGVRFEYRDIPPELQAQAEQWREKMIEKAAEASEALLEKYLSGQPLSEDEIKSGLRARTVANEIVPMLCGSAFKNKGVQAMLDAVIDYLPSPADVPAIIGHDERDREIERHPADDEPFSALAFKIMTDPFVGQLVFFRVYSGVVKSGDSVLNPLKSKKERLGRILQMHANERREISEVYAGDIAAAVGIKEITTGDTLTDPAHVIILERMTFPEPVISQAVEPRTKADQEKMGIALNRLAQEDPSFRVRTDEESGQTIISGMGELHLEILVDRMKREFGVEANVGKPQVAYRETIRSTVTDVEGKFVKQSGGRGQYGHVVLKLEPQEQGKGYEFVDAIKGGVVPREFIPAVDRGVRETLNTGVLAGYPVVDVKVTLVFGSYHDVDSNENAFRMAASMAFKEGMRRAKPVLLEPMMHVEVETPEDFTGNVMGDLSSRRGMVQGMEDIAGGGGKLVRAEVPLAEMFGYSTSLRSLTQGRATYSMEFKHYAEAPRQVAEQIIAARGSGAAARG
>CP024175.1|AZW32627.1|4508846_4509365_+|methyltransferase
MDTVWTEIWTTVRNEFADIPDVAEATRIVLRLGMAVALGGLLGYERERSGKAAGLRTHMLVALGAALFVLVPLQGGMEVGDLSRVLQGVIAGIGFLGAGAIIKLGNEGEIRGLTTSAGIWLTAAIGVAAGMGREATALASTLIALFVLAALRRLEKRIAARDDKRVVAQPPP
>CP024175.1|AZW32626.1|4507980_4508736_-|hypothetical-protein
MDYLVSLAQQPAAWAALATLIAMEVVLGIDNLIFISILTNKLPPQHQTKARRIGIGMALILRLALLGTVAFIVQLTQPVFELFGHGFSWRDVILVAGGLFLVWKATKEIHHHVDPNPGDDMFGGKAATLGFAAAVAQILMLDLVFSIDSIITAVGMTEHIPIMFVAVIVAVAVMLLAAEPLARFIERNPTVVMLALAFLMMIGMTLIAEGFGAHVPKGYIYAAMAFSALVEGLNMMARRAREGRGAGAAGG
>CP024175.1|AZW32625.1|4506551_4507784_-|CoA-transferase
MSGPLEGVRILDVTTVLMGPYATQILGDLGADVIKVEPPAGDNVRGIGPGRHADMGGIFLHANRSKRSIALDLKKPAGREALLKVAATCDVLVYNVRPQAMARLGLSYAEVAQANPSILYVGMYGYDQRGPYAARAAYDDLIQGAVGIPSLSVEAGSDIPRYAPSAMVDRIVGISAANAVTAGLYHRARTGQGQAIDVPMFETMAHLILGDHMMGQTFEPPLGPPGYPRILNADRRPYATRNGHICVLLYADKHWKAFFELIGQPGRDAADPRFRDIGTRTQHIHAIYRLVSDAIASRTTEEWLAAFEAADIPAMPVHTMASLLRDPHLEAIGFFGTVDHPSEGAVRMMAVPSRWSGTPPQPRGHAPRLGEHSVDVLKEAGYDDEAIAALVRDGAAIAAARQRPEGTDHD
>CP024175.1|AZW32624.1|4505773_4506559_-|enoyl-CoA-hydratase
MTDFLRHERHGGVLLLTMDRERTRNALSDADAVEALVQACARIGADLSVRAVVLTGSHGVFSSGGNLKTLSDTVGAGLGEPVHSRQAYRSGIQRIPLALYNLEVPTIAAVNGPAIGAGCDLACMCDIRLAARQASFAESFVKLGLTPGDGGAWLLPRIVGMSRACELAFTGRSIDAARARELGLVSEVFDADALLPAALALAQEIAQHSGHALRLTKRLLREGQHTRLDTLLELSAGFQALAHHTQEHAGALDAYLSRKRG
>CP024175.1|AZW32623.1|4504735_4505707_-|tripartite-tricarboxylate-transporter-substrate-binding-protein
MHPRTLALAVLSVAALAQGGSARAASDYPAHPVKIIVSLPPGSGADTTARFLSKHLAERFKQPFVVENRPGANSFIAAQAVATAPPDGYTLFVASNSPMTTNAAVFKNLPYDALKDFAPVAPIARFPMALVVPANSPYRSVADLVAAARAAPGQLNFASGTATYQVVLELFHEQNGIKATHVPYKGTSAALADVAGGVVQYSVADVSAALPLIRGGKLRPLAVTSTRRIKDLPDVPTMQESGNKGFEAYAWTAAFFPAKVDPAIVARVSDAVQALVRSEEGKAFMEQLGGEPFVGGPATLAAFQRDELASMRRIAKLANIQQE
>CP024175.1|AZW32622.1|4503747_4504725_+|LysR-family-transcriptional-regulator
MWTGQYIVHIASPAHHWRRAVELRQLKQLLVLSETLNFHRAAERLHMAQPPLSTAIKKLEQELGVQLFERLPAGLQPTPAAEVVLRYARATLFYADEIQRAAQEGASGKQGMLKVGFVGSSVYSLMPQLLSAFRKDYPRVDLVIEESTTVDLLRRLDAHTLDVALVRFPVLEPSTARVTLLQADHLMLAVPAGSRYAQRDDVALDELADEPFIGYSRTHVPGMHALVMYAFQQYGVVPHITQEAIQVQTILSLVESGLGLAIVPKVAGRQAGSGVRLVNVPQLAETIKVGIALAVHPDNATPTTANFVDMACRLMQTEPAAGQAR
>CP024175.1|AZW32621.1|4502449_4503610_-|acyl-CoA-dehydrogenase
MGTIIEALQLAAIPAHDEALRPAVRAFLDEALREMPADRRARSWMGHDAEFSRALARQGWLGLTLPVEYGGAGRSNFARFVLSEELLAAGAPVSAHWIADRQTAPLILRFGSPAQRAFYLPRIIRGEAFFAIGMSEPDTGSDLASVRTRATPVADGWLLNGRKIWTTNAHRSHYMCALVRTSGAPEDRHRGLSQMIFDLALPGIEIRPIRDMAGDAHFCEVLFDNVLLPHDALVGEEGSGWRQVMAELALERSGPERIYSSMVLLDGWLAHLRRDAAPQRAQVCLAGRLAARLAVLRSMSLAVSQRLEQGADASLAAVLVKDLGTEFEQAVPELIGQALRASPQPAPDDVLMRTLAYLTLINPTFSLRGGTRHILRGIIARELGLR
>CP024175.1|AZW32620.1|4501394_4502423_-|acyl-CoA-dehydrogenase
MVSTMQQDLYETFAQALAGLCPLERVRELEAAADPRVGAARTWNEVDALGYGDALSPAEHGGAGLSLADAEGLLRAAGAMALPFPFADTLLARALLRAAGQAVPDGPIALGVALPHGADWRCAPIAGVALAQAVAVEHDGCLALWPAPDVVQPGLFRPRASGAPAWRGMPAQAGRAGAPAGAVQAWRNAADAAGMAGAMQAVLDRCVAYVQERQQFGRALGRFQAIQQDISMLAEQVAAVAMAARLACASGALFPDPALAACARLRACEAVPVVCALAHAVHGAIGITEELPLGLYTARLHEWRATGMSEDDCAELLGRRVLADGERTLLDVVRGMVSAAQA
>CP024175.1|AZW32619.1|4500134_4501328_-|acetyl-CoA-C-acyltransferase
MSVHPDPVVIVAARRTPIGAFQGALAHYSAPQLGAHALAAAVRQAGLQPDAAQEALMGCCLFAGLGQAPARQAVLGAGLPTDVQATTLSKMCGSGMKAAMLAHDMLRAGSADVVLAGGMESMSNAPHLIPKARQGYRLGDGQLLDHMYRDGLQDAYEGRLMGHYADLAAREYGFSREQQDAYAHESVLRAQRSVAEGEFAEEIAPMAGLARRGAPAAMVAVDETPGLCDVSRLASLKPVFNADGTVTAGNASSISDGAAALVLTRQAHAERLGLAPQARIVGHATAALPPGQFPAAPVRAIARLFERVGWNRDSVDLFEINEAFAVVTMIALRELGLPAERVNVNGGACALGHPVGATGARLIVTLMHALRRRGLRRGVACLCLGGGEATAIAIERA
>CP024175.1|AZW32629.1|4511876_4512347_-|universal-stress-protein
MFKKILIPTDGSPLSAQAANAGICFARSTGAEVVALHVTQPFAATIGFDGMAAAYAITDEDYEKASAEQAEKYLKLILDRAETAGVKAESRAVSNFNVADGIVQAAGEAGCDLIFIGSHGRSGLSRLLLGSVTAKVLSLAHTAVLVYRVKEDKDKK
>CP024175.1|AZW32630.1|4512435_4512780_-|TIGR01244-family-phosphatase
MSAAIKPLTENFAVAPQLAPADMADVAAAGYKSVIINRPDFEGGPDQPTAADVSQAALALGLQVEYQPVVGSAMTAADVARFAELLRTMPGPVLAYCRTGTRCTNLFAAAQQLG
>CP024175.1|AZW32631.1|4512879_4514280_-|PLP-dependent-aminotransferase-family-protein
MRQADATLVTQLADDLARRIDEHGLRPGTRLPSIRRMAEQSGVSRFTVVEAYDRLVARGLVQSRRGAGFFVRARSASLTALASARVPQAAPETPVRVDVSWLLRNMFRETAAGMPGGAGLLPPEWLDPDMVAAAVRAVGRTVRGNLVSYGSPQGYAPLRQQLASMLQADGVPAHPERNLLTTNGVTHGLDIVARHLIKPGDTVLVEDPAWFVIFGRLAAFGARPVGVPRGPDGPDLAMLDRLAAEHKPRLYIINGAVHNPTGHTLSAGAAYDILRLAERHDFMVVEDDTYADLHPGGAMKLAALDRLERVILVGGFSKMLAASLRVGYIAAGAETLQRLTDLKMLAGLTSPELGERVVHRVLVEGQYRRHIERVRARVNEARLRSIQALQQLGLSVPHEPHAGMFVWADCGRDSEPVARNAAERGMLLAPGTLFSPSGAPSTMLRFSVAMVDTPGIWQSIAAVMAQ
>CP024175.1|AZW33535.1|4514468_4515383_+|EamA/RhaT-family-transporter
MSPPSAQASAPSASSHAPSWEGYGYGLIGVLVFALTLPMTRLAVGELSPLLVGLGRALLAAVPAAALLWLTRSRRPDRAEWSGIVLAAVGIVVGWPVASTLAMASVPAAHGAVFNGLLPLSTAVFAAWRSGERPSPAFWSFAVLGAVLVAGYALRQGHGALQPGDLWLLLAVVLGGMGYAEGARASRTLGGWRTICWALVVSVPALLPAVLWLAHDAAWPSLPVAGAFAYLAFGSMFLGFFAWYRGLAIGGIARVGQIQLLQPFLTVVAAALLFNEQVEPITYVFAVAVVLVIAGGRRAMVRKA
>CP024175.1|AZW32632.1|4515379_4516039_+|LysE-family-translocator
MIGSDLSSLDQAPLASLSVLMPLVLFTLVNSLTPGPNNVMLASSGLTFGFRRTIPHLLGISVGFSIMLLMVGLGLGATLERLPWLYSTLKYGGAAYLLYLAWKIATSGPMESGAERGKPLTFIQAALFQWVNPKAWVMIVSVVATYTPQHGYFANLIIATLVCGVVNLPSVGVWAAFGMALRRWLHRPAAVRAFNVGMAALLVVSLYPVGLDLLALYTG
>CP024175.1|AZW32633.1|4516128_4517052_+|alpha/beta-hydrolase
MVSLPFRLSWRRMAAVLLLAAGALGFNQLDAWQRQAIFSPQTDQQRWWREPPAGTEVFDLALPNGDKVHAWYWQSPRRDAPTVLYLHGARWNLNGSAFRMEGWTRMGYSMLAIDYRGFGQSTPLLPSEQSASQDAAAALQELARRQPDPARRFIYGHSLGGAIAIDLAARPDLPPFAGLIVESSFTSIGAMLGTMKWGWVPGATLLVTQPFASVDKLAALTTPMLLLHGTADRVVPHTMSDELYRAAQQVPADLKRLVKIEGASHSGAIRSGRIYEDAVADFVRDAGRGYAGRQGAPTPLTASRPGT
>CP024175.1|AZW32634.1|4517057_4517513_-|hypothetical-protein
MSSSSKQTPKTIKERFLHAFFFEIIAIGLSAPVAAWAMDQPLFDMGVLTAVIAWIALLWNMVYNAGFERLERRFGVVRTMPVRVAHAVGFELGLVLIIVPLAAWWLAISFWEAFMLDIGLLMFYLPYAFFYNLAYDKLRARWWGRIEPAGA
>CP024175.1|AZW32635.1|4517509_4518613_-|ChbG/HpnK-family-deacetylase
MTSERYDEGQQPAHDVGPQRGQAGPFHAGDRDGPMGGGRGASDGNEPGNLSQQAAHVEEVSPLRNQAGDVRCRRIAVCGDDFGMNEAIDGALIELAGAGRLSAVSCMPLAPAFAADAPALARLDVDLGVHVDFTEAFAGAAPAAPGLAALLWRAYAGQLDPDWIDARLASQFDAFERAFGRAPDYVDGHQHVHQLPGILPRLRALLKRRYAGQRIWLRHTAPGLQFGLPLAQAAKARLIGALGAGALARAAGQEGWQTNRRMLGVYDFTGGPRRYAGLLHHWLMNARDGDLLMCHPGWPQVHGAAHASQRAAEYEVLAHPELGTWLARNGLRIVRLSQVRGRQASQESGKVRNVPHSGSFRRLASRL
>CP024175.1|AZW33536.1|4518532_4518841_+|GtrA-family-protein
MEWAGLPPLGANVVGWLLAFVVSFTGHFRLTFRHLAASWTIAARRFFLVSALGFAINELSYAWLLHATSLPYDVLLALVLIGLAFLTFVASRLWAFRHRHAP
>CP024175.1|AZW32636.1|4518800_4520420_-|dolichyl-phosphate-mannose--protein-mannosyltransferase
MTLATRSMQPHAVSPGQARSWPLPAAGWLLLAVGVWLAFLSWMRPLALPDEGRYAGVAWDMLRNGSFAVPLIDGMPYFHKPPLYYWLAELSFRLFGVNEWAARLPSALAAWASAVALYLFVRRHRDAASATLCVLVLATLPLFFGGAQYANMDMLVAGMITLCVLAGADTALRARAGQAWRAMALATGVCAALAMLAKGLIGLVLPGAVLLAWLAWRRDWRGLRVLLWPPAILAFAVVAVPWFWLMQVRYPGFFEYFFVHQHFERFAQTGFNNVQPFWFYLPVIAGLALPWSLWAGGLLRKQFWAADADPDGLRRLALVWLAVIVAFFSMPQSKLVGYIMPVLPPLAFLLAEVVMGALRDAAVARATRRMARVSALVAVAICVTAVFVASFNARGSSRELALSLRGELRPDDTLVALHTYPFDLQLYAHAARPMWVVDDWSNPEIPKRDNWRRELYDAVQFEPALGERLLVSADTFQQRLCQAPEGSRYWVWGTAADEEAYAPLRGQAARFADARRSLWLVLVDEAFKGRVCDGTPTGG

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Crispr_ID: CP024175_6

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

CP024175_6

4559675-4559823

Orphan

Consensus_repeat	Method
CGTACGCCATGAACGCTGGCCGGCCAAGACGGCATCTATCCCGCACGG	CRISPRCasFinder

1 spacers

The CRISPR arrays of CP024175_6

>merge|CP024175|6|4559675-4559823|CRISPRCasFinder
CGTACGCCATGAACGCTGGCCGGCCAAGACGGCATCTATCCCGCACGGCAGCCGACATCCACGGCAGGGTGTGCCTGTCCCCGCCGGGACAGGCACGCCGCCGTACGCCATGAACGCTGGCCGGCCAAGACGGTATCTATCCCGCACGG

>CP024175|6|6|4559675-4559823|CRISPRCasFinder
CGTACGCCATGAACGCTGGCCGGCCAAGACGGCATCTATCCCGCACGG	CAGCCGACATCCACGGCAGGGTGTGCCTGTCCCCGCCGGGACAGGCACGCCGC
CGTACGCCATGAACGCTGGCCGGCCAAGACGGTATCTATCCCGCACGG

Protein	Signature genes	Signature genes Name	Protein_function
CP024175.1\|AZW32670.1\|4557847_4558813_+\|tripartite-tricarboxylate-transporter-substrate-binding-protein	unknown	unknown	gnl\|CDD\|270234
CP024175.1\|AZW32675.1\|4562838_4563630_+\|GntR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|225099
CP024175.1\|AZW33538.1\|4553843_4554578_+\|NADH-pyrophosphatase	unknown	unknown	gnl\|CDD\|234699
CP024175.1\|AZW32664.1\|4550681_4551488_+\|zinc-binding-dehydrogenase	unknown	unknown	gnl\|CDD\|176203
CP024175.1\|AZW32678.1\|4565812_4566643_-\|GntR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|225099
CP024175.1\|AZW32681.1\|4569352_4570954_-\|choline-dehydrogenase	unknown	unknown	gnl\|CDD\|235000
CP024175.1\|AZW32666.1\|4552785_4553730_+\|oxidoreductase	unknown	unknown	gnl\|CDD\|99782
CP024175.1\|AZW32677.1\|4564810_4565800_+\|tripartite-tricarboxylate-transporter-substrate-binding-protein	unknown	unknown	gnl\|CDD\|270234
CP024175.1\|AZW32673.1\|4560930_4561983_+\|taurine-ABC-transporter-substrate-binding-protein	unknown	unknown	gnl\|CDD\|270279
CP024175.1\|AZW32672.1\|4560004_4560904_+\|ABC-transporter-ATP-binding-protein	unknown	unknown	gnl\|CDD\|213260
CP024175.1\|AZW32665.1\|4551484_4552789_+\|amidase	unknown	unknown	gnl\|CDD\|223232
CP024175.1\|AZW32663.1\|4549644_4550559_-\|LysR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|176104
CP024175.1\|AZW32674.1\|4561979_4562777_+\|ABC-transporter-permease	unknown	unknown	gnl\|CDD\|223673
CP024175.1\|AZW32679.1\|4566696_4567758_-\|C4-dicarboxylate-ABC-transporter	unknown	unknown	gnl\|CDD\|187763
CP024175.1\|AZW32676.1\|4563682_4564732_+\|taurine-ABC-transporter-substrate-binding-protein	unknown	unknown	gnl\|CDD\|270279
CP024175.1\|AZW32671.1\|4558814_4559588_+\|enoyl-CoA-hydratase	unknown	unknown	gnl\|CDD\|180591
CP024175.1\|AZW32668.1\|4555600_4556794_+\|CoA-transferase	unknown	unknown	gnl\|CDD\|367110
CP024175.1\|AZW32680.1\|4567754_4569212_-\|sulfatase	unknown	unknown	gnl\|CDD\|293760
CP024175.1\|AZW32667.1\|4554605_4555274_-\|TetR/AcrR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|380061
CP024175.1\|AZW32669.1\|4556790_4557795_+\|NADPH:quinone-reductase	unknown	unknown	gnl\|CDD\|176203

Protein	Function_ID	Function_description	E-value
CP024175.1\|AZW32670.1\|4557847_4558813_+\|tripartite-tricarboxylate-transporter-substrate-binding-protein	gnl\|CDD\|270234	cd07012, PBP2_Bug_TTT, Bug (Bordetella uptake gene) protein family of periplasmic solute-binding receptors; contains the type 2 periplasmic binding fold. The Bug (Bordetella uptake gene) protein family is a large family of periplasmic solute-binding (PBP) proteins present in a number of bacterial species, but mainly in proteobacteria. In eubacteria, at least three families of periplasmic binding-protein dependent transporters are known: the ATP-binding cassette (ABC) transporters, the tripartite ATP-independent periplasmic transporters, and the tripartite tricarboxylate transporters (TTT). Bug proteins are the PBP components of the TTT. Their expansive expansion in proteobacteria indicates a large functional diversity. The best studied examples are Bordetella pertussis BugD, which is an aspartic acid transporter, and BugE, which is glutamate transporter.	5.02031e-115
CP024175.1\|AZW32675.1\|4562838_4563630_+\|GntR-family-transcriptional-regulator	gnl\|CDD\|225099	COG2188, PhnF, Transcriptional regulators [Transcription].	1.18037e-24
CP024175.1\|AZW33538.1\|4553843_4554578_+\|NADH-pyrophosphatase	gnl\|CDD\|234699	PRK00241, nudC, NAD(+) diphosphatase.	3.83191e-86
CP024175.1\|AZW32664.1\|4550681_4551488_+\|zinc-binding-dehydrogenase	gnl\|CDD\|176203	cd08241, QOR1, Quinone oxidoreductase (QOR). QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR acts in the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.	7.45947e-22
CP024175.1\|AZW32678.1\|4565812_4566643_-\|GntR-family-transcriptional-regulator	gnl\|CDD\|225099	COG2188, PhnF, Transcriptional regulators [Transcription].	7.39747e-26
CP024175.1\|AZW32681.1\|4569352_4570954_-\|choline-dehydrogenase	gnl\|CDD\|235000	PRK02106, PRK02106, choline dehydrogenase; Validated.	0
CP024175.1\|AZW32666.1\|4552785_4553730_+\|oxidoreductase	gnl\|CDD\|99782	cd06185, PDR_like, Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron transfer from NADH to FMN to an iron sulfur cluster. PDR has an an N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding domain and a C-terminal iron-sulfur [2Fe-2S] cluster domain. Although structurally homologous to FNR, PDR binds FMN rather than FAD in it's FNR-like domain. Electron transfer between pyrimidines and iron-sulfur clusters (Rieske center [2Fe-2S]) or heme groups is mediated by flavins in respiration, photosynthesis, and oxygenase systems. Type I dioxygenase systems, including the hydroxylate phthalate system, have 2 components, a monomeric reductase consisting of a flavin and a 2Fe-2S center and a multimeric oxygenase. In contrast to other Rieske dioxygenases the ferredoxin like domain is C-, not N-terminal.	2.05797e-81
CP024175.1\|AZW32677.1\|4564810_4565800_+\|tripartite-tricarboxylate-transporter-substrate-binding-protein	gnl\|CDD\|270234	cd07012, PBP2_Bug_TTT, Bug (Bordetella uptake gene) protein family of periplasmic solute-binding receptors; contains the type 2 periplasmic binding fold. The Bug (Bordetella uptake gene) protein family is a large family of periplasmic solute-binding (PBP) proteins present in a number of bacterial species, but mainly in proteobacteria. In eubacteria, at least three families of periplasmic binding-protein dependent transporters are known: the ATP-binding cassette (ABC) transporters, the tripartite ATP-independent periplasmic transporters, and the tripartite tricarboxylate transporters (TTT). Bug proteins are the PBP components of the TTT. Their expansive expansion in proteobacteria indicates a large functional diversity. The best studied examples are Bordetella pertussis BugD, which is an aspartic acid transporter, and BugE, which is glutamate transporter.	1.11409e-116
CP024175.1\|AZW32673.1\|4560930_4561983_+\|taurine-ABC-transporter-substrate-binding-protein	gnl\|CDD\|270279	cd13561, PBP2_SsuA_like_4, Putative substrate binding domain of sulfonate binding protein-like, the type 2 periplasmic binding protein fold. This subfamily includes the periplasmic component of putative ABC-type sulfonate transport system similar to SsuA. These domains are found in eubacterial SsuA proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding the ligand, SsuA 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 SsuA 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.	2.67352e-49
CP024175.1\|AZW32672.1\|4560004_4560904_+\|ABC-transporter-ATP-binding-protein	gnl\|CDD\|213260	cd03293, ABC_NrtD_SsuB_transporters, ATP-binding cassette domain of the nitrate and sulfonate transporters. NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. 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.	9.97351e-123
CP024175.1\|AZW32665.1\|4551484_4552789_+\|amidase	gnl\|CDD\|223232	COG0154, GatA, Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit and related amidases [Translation, ribosomal structure and biogenesis].	3.44874e-92
CP024175.1\|AZW32663.1\|4549644_4550559_-\|LysR-family-transcriptional-regulator	gnl\|CDD\|176104	cd08412, PBP2_PAO1_like, The C-terminal substrate-binding domain of putative LysR-type transcriptional regulator PAO1-like, a member of the type 2 periplasmic binding fold protein superfamily. This family includes the C-terminal substrate domain of a putative LysR-type transcriptional regulator from the plant pathogen Pseudomonas aeruginosa PAO1and its closely related homologs. The LysR-type transcriptional regulators (LTTRs) are composed of two functional domains joined by a linker helix involved in oligomerization: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal substrate-binding domain, which is structurally homologous to the type 2 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcriptional repressor undergoes a conformational change upon substrate binding which in turn changes the DNA binding affinity of the repressor. The genes controlled by the LTTRs have diverse functional roles including amino acid biosynthesis, CO2 fixation, antibiotic resistance, degradation of aromatic compounds, nodule formation of N2 fixing bacteria, and synthesis of virulence factors, to a name a few. The structural topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the substrate-binding domains from ionotropic glutamate receptors, LysR-like transcriptional regulators, and unorthodox sensor proteins involved in signal transduction.	3.30463e-74
CP024175.1\|AZW32674.1\|4561979_4562777_+\|ABC-transporter-permease	gnl\|CDD\|223673	COG0600, TauC, ABC-type nitrate/sulfonate/bicarbonate transport system, permease component [Inorganic ion transport and metabolism].	6.50972e-66
CP024175.1\|AZW32679.1\|4566696_4567758_-\|C4-dicarboxylate-ABC-transporter	gnl\|CDD\|187763	cd09323, TDT_SLAC1_like, Tellurite-resistance/Dicarboxylate Transporter (TDT) family includes SLAC1 (Slow Anion Channel-Associated 1). SLAC1 (Slow Anion Channel-Associated 1) is a plasma membrane protein, preferentially expressed in guard cells, which encodes a distant homolog of fungal and bacterial dicarboxylate/malic acid transport proteins. It is essential for stomatal closure in response to carbon dioxide, abscisic acid, ozone, light/dark transitions, humidity change, calcium ions, hydrogen peroxide and nitric oxide. In the Arabidopsis genome, SLAC1 is part of a gene family with five members and encodes a membrane protein that has ten putative transmembrane domains flanked by large N- and C-terminal domains. Mutations in SLAC1 impair slow (S-type) anion channel currents that are activated by cytosolic calcium ions and abscisic acid, but do not affect rapid (R-type) anion channel currents or calcium ion channel function.	5.7586e-111
CP024175.1\|AZW32676.1\|4563682_4564732_+\|taurine-ABC-transporter-substrate-binding-protein	gnl\|CDD\|270279	cd13561, PBP2_SsuA_like_4, Putative substrate binding domain of sulfonate binding protein-like, the type 2 periplasmic binding protein fold. This subfamily includes the periplasmic component of putative ABC-type sulfonate transport system similar to SsuA. These domains are found in eubacterial SsuA proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding the ligand, SsuA 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 SsuA 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.	4.57061e-85
CP024175.1\|AZW32671.1\|4558814_4559588_+\|enoyl-CoA-hydratase	gnl\|CDD\|180591	PRK06494, PRK06494, enoyl-CoA hydratase; Provisional.	1.03822e-61
CP024175.1\|AZW32668.1\|4555600_4556794_+\|CoA-transferase	gnl\|CDD\|367110	pfam02515, CoA_transf_3, CoA-transferase family III. CoA-transferases are found in organisms from all lines of descent. Most of these enzymes belong to two well-known enzyme families, but recent work on unusual biochemical pathways of anaerobic bacteria has revealed the existence of a third family of CoA-transferases. The members of this enzyme family differ in sequence and reaction mechanism from CoA-transferases of the other families. Currently known enzymes of the new family are a formyl-CoA: oxalate CoA-transferase, a succinyl-CoA: (R)-benzylsuccinate CoA-transferase, an (E)-cinnamoyl-CoA: (R)-phenyllactate CoA-transferase, and a butyrobetainyl-CoA: (R)-carnitine CoA-transferase. In addition, a large number of proteins of unknown or differently annotated function from Bacteria, Archaea and Eukarya apparently belong to this enzyme family. Properties and reaction mechanisms of the CoA-transferases of family III are described and compared to those of the previously known CoA-transferases.	2.23734e-123
CP024175.1\|AZW32680.1\|4567754_4569212_-\|sulfatase	gnl\|CDD\|293760	cd16037, sulfatase_like, uncharacterized sulfatase 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.	4.32173e-176
CP024175.1\|AZW32667.1\|4554605_4555274_-\|TetR/AcrR-family-transcriptional-regulator	gnl\|CDD\|380061	pfam17932, TetR_C_24, Tetracyclin repressor-like, C-terminal domain. TetR family regulators are involved in the transcriptional control of multidrug efflux pumps, pathways for the biosynthesis of antibiotics, response to osmotic stress and toxic chemicals, control of catabolic pathways, differentiation processes, and pathogenicity. The TetR proteins identified in overm ultiple genera of bacteria and archaea share a common helix-turn-helix (HTH) structure in their DNA-binding domain. However, TetR proteins can work in different ways: they can bind a target operator directly to exert their effect (e.g. TetR binds Tet(A) gene to repress it in the absence of tetracycline), or they can be involved in complex regulatory cascades in which the TetR protein can either be modulated by another regulator or TetR can trigger the cellular response. TetR regulates the expression of the membrane-associated tetracycline resistance protein, TetA, which exports the tetracycline antibiotic out of the cell before it can attach to the ribosomes and inhibit protein synthesis. TetR blocks transcription from the genes encoding both TetA and TetR in the absence of antibiotic. The C-terminal domain is multi-helical and is interlocked in the homodimer with the helix-turn-helix (HTH) DNA-binding domain. This entry represents the C-terminal domain present in family members such as HTH-type transcriptional repressor KstR2 as well as fatty acid metabolism regulator proteins. In Mycobacterium smegmatis, KstR2 is involved in involved in cholesterol catabolism, while YsiA in Bacillus subtilis is involved in fatty acid degradation.	2.22179e-19
CP024175.1\|AZW32669.1\|4556790_4557795_+\|NADPH:quinone-reductase	gnl\|CDD\|176203	cd08241, QOR1, Quinone oxidoreductase (QOR). QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR acts in the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.	6.06081e-154

>CP024175.1|AZW32671.1|4558814_4559588_+|enoyl-CoA-hydratase
MAQADDIEVRVADQVAWVTINRPQRMNALARATFARLVEVSLELDQDPGVKVVVYTGAGERAFSAGVDLKELDAAGRMTHPMGGPARNLNEVVLEMATPTIAAINGVAAGGGCELALACDIRVAASTARIGLPEARVGMGANFGSVVLPQLIPRGVALELLYTGELIDMALAHRLGLVNHVFEPAELMAQTAGLARRIADNAPLSVQRMKAVAFKSIGLPTAAALRLSVGPDPYNSEDRLEGARAFVEKRKPRFQGR
>CP024175.1|AZW32670.1|4557847_4558813_+|tripartite-tricarboxylate-transporter-substrate-binding-protein
MFKRIALMGAAAMLAAAPAAHAQDKYPSRPITLVSPYQAGGTTETFARLIIDDVAAILGQPIVVEQKPGAAGTIGARFVATSKGDGYTLLANTSQHVMYEGMFKNLPFRPMEDFRPVGVLGSAPIIVVTGENSPYKTFKDVLEAARTRNLTFASGAQGSLPHLTGERVAVQGKLNMTHVPFSGTAPALTNVMGGHVDLLYSTAASVMSQIRAGKLRALAVSTKERMPELPDVPSIAEMGMPGFDVTAWYAVWAPKDTRPEVVDAINQAMREASARPEAKKRMAALSVTPSTLTAAQFAAFAESERKTWLDVMRRANMQPAN
>CP024175.1|AZW32669.1|4556790_4557795_+|NADPH:quinone-reductase
MKAVVCREYGGPDVAAYEEVPAPALAPGAVRIQVQACSASFASLLVMEGKHQNRAPLPLIPGTEVAGVVTELGAGATRFRVGDRVIAGVQSGGYAQEVVAPEATVFELPADVPFETGAQFPTIYGTAYGALQWRAQVEPGEVVLVHGAAGGSGLAAVEVAKALGATVIATVGSDAKQAIVREHGADHAINYRTQDWRAEVLRLTGQRGADVIYDPVGGETFDASLRCIAPDGRIIPMGFASGAIPTVPANIVLVKNISILGVYWGYYFGWGRHPVKPGNDARMRAAYARLFEWTRQGRIRPRAHAVMPLADFRTALRMIASREAIGRIVMQPQQ
>CP024175.1|AZW32668.1|4555600_4556794_+|CoA-transferase
MDGPLSGVRVLDMTAALSGPVATQILGDMGAEVIKIEPPEGDSIRDLGPARHRGMGAMFLHTNRSKRSIVLDLKLEGGREAFRRLAGTADVFVCNTRPKAMARLGLAYADIAALNPALVYLNIVGYGSAGTHADKPAYDDLIQAAAGIASLRADGDPARYAPIALADRVTGILAANAVLGALYHRARTGAGQHIEVPMFESIASLVLSDHMAGLSFEPPIGPPVFDRYASIRRPFQTRDGFLCMMVLTDRQWREFFRAVGRPEVMDDDRFGTMAQRTRNLEALYAIVSAIMATRDTDAWVAHLEAADIPVARIESVASLTAHPHLAQAGFFQTVEHPTEGPIRSMACASTWSATQPAATRPAPRLGEHSLEILREAGFSEEETQAMFASGAARGYES
>CP024175.1|AZW32667.1|4554605_4555274_-|TetR/AcrR-family-transcriptional-regulator
MILTPELENWVGIDYDDMPAVQRKLLDAAAKAFTTYGFAATSIDVIASQIGATKGSVYYHYRSKTDLFFAVHKCAMVMNLKAQVPVAFDASLDPRAKLYRMAYLHAMLMMDSLYYQRVTVQGVELHQSVSTTPMEREALAEVIAMRDVYEGLFSQVVRDGMASGHFAEADHSIAAKGILGILNWITVWYRPRETESSGFRQRVATQLATQAIQGIARADTRG
>CP024175.1|AZW33538.1|4553843_4554578_+|NADH-pyrophosphatase
MRDSGVDLPDGDTCAQVGVRFELMQQIWLTHDPQLRTTHVARDTVAPPGYAFRKLRALLSELGERAPLAGRAFQIAEWVRTHRYCGVCATPMQHARHELCLQCPACGLHAYPRVSPAMMVLIKRGEHILLARHARYATARYTALAGFVEAGESIEDAVHREVAEEVGLRVRDLRYFGSQSWPFPHSLMIAFTAEYAGGELRVQEDEITEARWFGPGEPLPDIPMRESIAGRLVRANLPPGMASD
>CP024175.1|AZW32666.1|4552785_4553730_+|oxidoreductase
MKLVVRAVTPLTAEIRHFELAAPDGAALPAYTPGAHLSVHVVLPDGTPARREYSLLGDGSATASYEIAVQCREPAAGSAWMHRLAPGDRIDAEAPVNAFALAADAAEHVLIAGGIGITPILSMARHLRGVGAAFTLHYAGRARAAMAFAEEAAAMGAACRLYHDDGAPLQDALPGILAAPAAGRHLYVCGPRALIADTVDGAAAAGWPSASVHYELFQGALALRGDQPFDLVLRQSGITVSVPAGQTMLDALLQAGVEPLYDCRRGECGMCLTPVLEGKPDHRDHYLSPREREAGDAVCVCVSRACGASLTLDL
>CP024175.1|AZW32665.1|4551484_4552789_+|amidase
MTSLHRAPPLSAHTTRAAVLDGHASAELLEPCLAAIRAHEPVVRAWRELDVDAARAQARRLDAHAARGLLAGVPIAVKDIFLTEQFPTRYGSPIYEHGIAGTDADCVARARAAGALVLGKTVTTEFAYFTPGPTANPRDPSRTPGGSSSGSAAAVAAGMVPLAFGSQTAGSLIRPASYCGVFALKPTHGLHSLAGAKAMAPSLDTLGWLARDAGDLELMRCALAGEDYRPLPDARPDALRLGVCLTHEWHAIEPDGAQAFAHAQVLCTAAGAQVAPLVLPDALQGLMQAQQTIMAYEAARSLAAEWRDARARLSPAMQALIEAGLDCDAQSYAQALALAARGRAHLEHAMRDLDAVIAPAAPGEAPPGLARTGDPIFSRVWTLLGLPCVNVPGLAGPHGMPIGVQLVGRPGDERRLLAVAAALHRVFHPTGAPQ
>CP024175.1|AZW32664.1|4550681_4551488_+|zinc-binding-dehydrogenase
MTIGIAPMPSPRRPAPRLRVRVQACLGDAGGLRLPGVAFIGSAGPGRRVAALATQAAAPGADIEIDAGQAWTVADGLDEQSALLLAVLWPSAWIALVEIGGLRAGQQVLVHEADTPLGLLATVLARQADASVIAAARTAGGIAAALRAGAAEGVLYGDPWPELAREHGGADLVFDPGAGRYAVASLPCARRRARMLALGMHDGPAGPPIGAAQLLRRQTSLAAAGWDLVRDAPALQRACRALPPHWPRIAALLPLRPLSLSTSQEALP
>CP024175.1|AZW32663.1|4549644_4550559_-|LysR-family-transcriptional-regulator
MRAPDFSLRQLSYFLAAAECESVQQAAQALHVSAPAVSTAIAHLEALLGVQLFRRRHARGLILTEQGSAFAVQCRGILQEAWGLGSLQGRGELHGQVRVGCLTTFAPFVIPPLLTRVQQHLPGVRLAWFEGHHEYLLEGLRTGTLDIAVLYDFEIPSGIKLVALRAAPLQVVLPASHPLAAKETLATSDLNTEPLILLDLPRTREYMLTAFSSNGAIPRIAHSVLSINMLLGMVAAGHGFSLLNFCPPNALPGMGGIVSRAFESHVRQPNIVAAYSFRYHYPRAAAAIVEHISELVDELVIQAH
>CP024175.1|AZW32672.1|4560004_4560904_+|ABC-transporter-ATP-binding-protein
MNAQVNTFTPLPCSEPGKPGAPPRPGASQDNQVKISFQGVSKTYGGRGRSGNRTLALDRMDVDIKAAEIVTVLGPTGCGKSSTLNLIAGFEQTSTGSLLIDGKPIDGPGPDRAVVFQQPSLFPWLTVMENVTLGVKCRGVPKDTYEPRAQMLLREVGLSGFEKHYPYQLSGGMQQRVQIARALISEPKVLLLDEPFGALDYQTRILMQELLLQLWQEHKPTIFFITHDVSEAIFVADRVLVMSHRPGRIKLAVNVDADKPRNADFLSTPEFISLQRDLLHAVQEEVHANKNRPPMAKAA
>CP024175.1|AZW32673.1|4560930_4561983_+|taurine-ABC-transporter-substrate-binding-protein
MQSCLRLAASLLSAALLCLPAPGAAQTASPAKKELLKFNWGAPTADYYALYVAKDQKLFEEVGLEPNFYFFPSGAPLLAGLKSKSLDVITTGLATVFALGQNVPLKLIYWELDHAAAEGLVVDPAAGIKSYKDIAKAKAIGAPSGTCAQVSLVLMAKELNLKYSDLNIINIAPPLYGNAFKSKSIQAAVAWSPYSSILNADQLPVVNWASDYTPDQGVCPGLTGVRTEFMQQHPDIGLKLVQVQAKAMDMIRKDPELGIGVLMKYLSVSREVAKHIYDREFSRIPSYAQQIDPASPYSLAAKDAGLARKLLIASQALAEVGTIPAPLTPQAINEAIDPSAIQRYMKGERK
>CP024175.1|AZW32674.1|4561979_4562777_+|ABC-transporter-permease
MSERVAVEGRQPAISPTVFSVASVVGLLVIWTLVTNLGVVGPGYLPSPQAMFAQLVTLFEQGYGGKPLWDHVGASLFRALAGFAIGVLAGVPFGLFSGYHKAVGAMMSPIMAFIRPIPPIAFIPMAVLYFGLGEMGKVVLIVFTAFNYSFVSAQAGALSVPMSYYRAAESIGMTKLQIFWRVVFPSSIPHIFTGLKVAMALSWAVVVAAELVGAQKGLGFMISDAAQLFQIPVVFIGIALIGLIGLVLNVMLTVAEEKIVHWKGR
>CP024175.1|AZW32675.1|4562838_4563630_+|GntR-family-transcriptional-regulator
MDTDAIRSEIFGQLARPDNSGIPKYRRLSNILVEAIRRGVWQPGDRLPAEEQLTEMTPFSLGTVQRALRALTDEGLVIRMQGHGNFVADQQRQMADPWHCRFLDDDSDGIVPIYSKAVQRAVVTPSETGPWQRYLHSGSVMRLDRIINVNDEFRIFSRFYADRELLQPLWHVPLEELDGANFKDIIMRQVGLPITEIDRSVRIRRIDAQAARLIGVAPEATVLFMQAVARAGRDACIYYQEFYIPETGRALQLPEQRPRVHGR
>CP024175.1|AZW32676.1|4563682_4564732_+|taurine-ABC-transporter-substrate-binding-protein
MTPKQGRHTAFLTKAAAAAVLAAGSAASLAADPPKLLKINYGAPTADYYTLYVAKDHGLFEKHGLEPNFFWFASGAPLLAGLKSESLDVFTTGLASAFALGQNLPVKLLFWQLDDAPGQGLVVSKDSGIDSYRDLKKAKAIGTPSGTCAQVALGLMARKAGIAMKELNVVNIAPPLYANAFTSNSIDAGVTWAPYLQSVAERGYKIVNYDTDYDGICPVMTGARTKFLQEHPDVGLKLVQISAEAQRLVADNPQLAIDVLEKYLKVSPAVAKATYERLCCGNFPTFKQQADPESPYSLVSDKGIVAKLHTATQILAEAGTIPQAISRETVAASIDASYVRKYLATQPGQ
>CP024175.1|AZW32677.1|4564810_4565800_+|tripartite-tricarboxylate-transporter-substrate-binding-protein
MRSISLHLRRALAVLGLAGIAAAPLHAAETWPDRPVRLIVPYPAGGGVDFAARLIASDLSKQTGQNFIVENRTGAAGTIGAQAVVQSTADGNTVLFASPAEVLVSRIAGQKTSYDAGKDLQPVTLAGETPLAVVVNPAVPARTLAELVALARKDPSAISYGTPGTGSTMQFAGEALNLAAGIKMLHVPYRGAAPAIADLLGNQIPVAIVGVPPLVAHHKGGKLRILAVTGSQRIAALPDVPTVAEELGVADYRYTNWFGVYVPGNTPVAVGDRLAALIHASVHRDAIKAQLAEQGVEPIGNSTPEFVRFLAGEKARYETVQRKSGIQMD
>CP024175.1|AZW32678.1|4565812_4566643_-|GntR-family-transcriptional-regulator
MLMNTSLRRSTPAGGQIVVNAERPAVFDQLHRPNYSGIPKYRLVLNAIAEGIESGHWKPGERLPTEDDLVQMTSYSLGTVQRALRILVDQGLVVREHGLGTFVAQQQLRIQDPWHCRFLADDGVGFLPVYSTIISRDYASGEGEWQRYFDTAAGAQVILIERTINVGNEFEVFTRFYVDRNVFPSLWDTPMEKLNGLNFKKQITQELNVPVTKIDHFVAMEPFDPTVAGYTKTPPYAAGIALQVVACMGQERCIYYQKFFIPPTKRVLSIPDQLTD
>CP024175.1|AZW32679.1|4566696_4567758_-|C4-dicarboxylate-ABC-transporter
MTASTARPRSRVAAPIRHAMQTQTGLPAALRPAGATFLAGFPVSMFASVLGLSGLGMAWRKAHQVWGLPLQVALAIQVAVAAVYGVLLALFLLRLLRHPDEIAREWNHPVQLAFFSAISLGVVLIGTAWADDAPRAAAALWWLGATVHLGFTLVIVRSWIFHTHYQLDHVNPSWFVPVVGNIVIPIAGVRFAPAECAWFFFSLGIVFWIVLKAIILYRLMFGAPLARALTPTLFIMIAPPAVAFLAYMALTGSLDGFARVLYYISLFWTLLLFSAAPRFARLPFSLAAWSYSFPLAAITLATFSFAEHSGHALVFHTLAGFLVAVLSTVLVLLTGATVRGLLNGALADARGGA
>CP024175.1|AZW32680.1|4567754_4569212_-|sulfatase
MKVTPQNMIVIMSDEHQSRALGCYGHEFVHTPNLDALAARGTRFASAYCASPVCIPARASFATGKYINQIGFWDNADAYDGSVPSWHHMLRDRDHQVVSIGKLHFRDYGGDHGFSEEIIPMHIVGGKGDLMGLVRSDLPVRKGAYKMAQMAGPGESQYTFYDREIVSRAQIWLREQAPRHADKPWVLFVSFVSPHFPLTAPPEHYYRYYNRDLPLPKLYDKSQRPDHPYQQDYRGSFNYDDYFDPGLVKKAQAGYYGLCSFLDENIGKLLGTLDDLDILDSTRVVYTSDHGDNLGARGMWGKSNMFEEAAAVPLIIAGKDIPSGVTVNTPVSHVDVAPFIYDAVGETSPGLKEGLPGVSLFQLARGETPQRNVMAEYHGMGSATGAFMIREGRYKYIFYVHYPHQLFDLEADPEELEDLAGRPDYADVVALCKQKLWQLCDPVEVDRRARARQAELLEHNGGREAVIARGDLGFSPAPGAVHKFD
>CP024175.1|AZW32681.1|4569352_4570954_-|choline-dehydrogenase
MDMRTFDYIVVGAGSAGCALAARLVERKAGSVLLLEAGPPDRNMWIHIPIGYGKTMFDPRNNWQFYSEPEPELNGRKIYQPRGKTLGGSSSINGLVYIRGQAEDFDDWARLGNPGWAWQDVLPLFKRAERNERGDSEFHGGAGRLGVSDIRGRHELVEAFIQAGQENGIARTNDFNGASQEGVGYFQLTTRGGLRCSAAKGYLGPLKGDANLTIETDAQATGVIFEGRRAIGVRYRQRGAAFEARAAKEVILAAGAFQSPQLLMLAGIGDGAQLQAHGIPVLHHLPEVGMNLQDHLQVRLIYKCTRPITTNDQLRTLWGRAAIGMRWIFRRAGPVAAGIQLGAMFARACPGATRPDVQFHFGTISADMAAGKPHDFSGFTISMCQLRPRSRGQVSLKSANPLEAPRIQPNYFSAQEDRDTMVAGLRLTRRLTRSRPLAAYIAEEYHPGPRMETEEDMVRFVRESGTTIFHPVGTCRMGGDEASVVDPSLRVRGVQGLRVADASIMPLLLSGNTNAGAIMIGEKAADLITQARP

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Crispr_ID: CP024175_7

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

CP024175_7

4785847-4785931

Orphan

Consensus_repeat	Method
GGGTGCCTGTCCCCGCGGGGACAG	CRISPRCasFinder

1 spacers

The CRISPR arrays of CP024175_7

>merge|CP024175|7|4785847-4785931|CRISPRCasFinder
GGGTGCCTGTCCCCGCGGGGACAGATGCCCTCTTGGCCGTCAAGCGTTCTGGCGTATGACGGGGTGCCTGTCCCCGCGGGGACAG

>CP024175|7|7|4785847-4785931|CRISPRCasFinder
GGGTGCCTGTCCCCGCGGGGACAG	ATGCCCTCTTGGCCGTCAAGCGTTCTGGCGTATGACG
GGGTGCCTGTCCCCGCGGGGACAG

Protein	Signature genes	Signature genes Name	Protein_function
CP024175.1\|AZW32872.1\|4783465_4783999_+\|YraN-family-protein	unknown	unknown	gnl\|CDD\|173148
CP024175.1\|AZW32870.1\|4781891_4782464_-\|methylated-DNA--[protein]-cysteine-S-methyltransferase	unknown	unknown	gnl\|CDD\|223427
CP024175.1\|AZW32880.1\|4789566_4791060_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|279307
CP024175.1\|AZW32884.1\|4795250_4795814_-\|rod-shape-determining-protein-MreD	unknown	unknown	gnl\|CDD\|274574
CP024175.1\|AZW32879.1\|4788778_4789354_+\|nucleoid-occlusion-factor-SlmA	unknown	unknown	gnl\|CDD\|181894
CP024175.1\|AZW32882.1\|4792151_4793288_-\|rod-shape-determining-protein-RodA	unknown	unknown	gnl\|CDD\|274033
CP024175.1\|AZW32877.1\|4787080_4787983_+\|acetylglutamate-kinase	unknown	unknown	gnl\|CDD\|234869
CP024175.1\|AZW32883.1\|4793284_4795237_-\|penicillin-binding-protein-2	unknown	unknown	gnl\|CDD\|274573
CP024175.1\|AZW32878.1\|4787982_4788729_+\|pyrimidine-5'-nucleotidase	unknown	unknown	gnl\|CDD\|319791
CP024175.1\|AZW33541.1\|4779151_4779904_-\|cytochrome-c	unknown	unknown	gnl\|CDD\|225418
CP024175.1\|AZW32885.1\|4795800_4796685_-\|rod-shape-determining-protein-MreC	unknown	unknown	gnl\|CDD\|237560
CP024175.1\|AZW32869.1\|4780944_4781895_+\|septal-ring-lytic-transglycosylase-RlpA-family-protein	unknown	unknown	gnl\|CDD\|223868
CP024175.1\|AZW32867.1\|4777854_4779141_-\|alcohol-dehydrogenase	unknown	unknown	gnl\|CDD\|365823
CP024175.1\|AZW32881.1\|4791070_4792126_+\|lactate-dehydrogenase	unknown	unknown	gnl\|CDD\|376860
CP024175.1\|AZW32875.1\|4785337_4785829_+\|TlpA-family-protein-disulfide-reductase	unknown	unknown	gnl\|CDD\|239264
CP024175.1\|AZW32868.1\|4780075_4780948_+\|RNase-adaptor-protein-RapZ	unknown	unknown	gnl\|CDD\|235450
CP024175.1\|AZW32874.1\|4784597_4785341_+\|phospholipid-binding-protein	unknown	unknown	gnl\|CDD\|182907
CP024175.1\|AZW32873.1\|4783998_4784601_+\|phosphoheptose-isomerase	unknown	unknown	gnl\|CDD\|237567
CP024175.1\|AZW32871.1\|4782460_4783399_-\|16S-rRNA-(cytidine(1402)-2'-O)-methyltransferase	unknown	unknown	gnl\|CDD\|223390
CP024175.1\|AZW32876.1\|4786030_4786819_-\|MetQ/NlpA-family-lipoprotein	unknown	unknown	gnl\|CDD\|224381

Protein	Function_ID	Function_description	E-value
CP024175.1\|AZW32872.1\|4783465_4783999_+\|YraN-family-protein	gnl\|CDD\|173148	PRK14685, PRK14685, hypothetical protein; Provisional.	1.91773e-89
CP024175.1\|AZW32870.1\|4781891_4782464_-\|methylated-DNA--[protein]-cysteine-S-methyltransferase	gnl\|CDD\|223427	COG0350, Ada, Methylated DNA-protein cysteine methyltransferase [DNA replication, recombination, and repair].	9.34456e-53
CP024175.1\|AZW32880.1\|4789566_4791060_+\|hypothetical-protein	gnl\|CDD\|279307	pfam00939, Na_sulph_symp, Sodium:sulfate symporter transmembrane region. There are also some members in this family that do not match the Prosite motif, and belong to the subfamily SODIT1.	2.68833e-115
CP024175.1\|AZW32884.1\|4795250_4795814_-\|rod-shape-determining-protein-MreD	gnl\|CDD\|274574	TIGR03426, shape_MreD, rod shape-determining protein MreD. Members of this protein family are the MreD protein of bacterial cell shape determination. Most rod-shaped bacteria depend on MreB and RodA to achieve either a rod shape or some other non-spherical morphology such as coil or stalk formation. MreD is encoded in an operon with MreB, and often with RodA and PBP-2 as well. It is highly hydrophobic (therefore somewhat low-complexity) and highly divergent, and therefore sometimes tricky to discover by homology, but this model finds most examples. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan].	7.62373e-19
CP024175.1\|AZW32879.1\|4788778_4789354_+\|nucleoid-occlusion-factor-SlmA	gnl\|CDD\|181894	PRK09480, slmA, division inhibitor protein; Provisional.	1.59741e-107
CP024175.1\|AZW32882.1\|4792151_4793288_-\|rod-shape-determining-protein-RodA	gnl\|CDD\|274033	TIGR02210, Rod_shape-determining_protein_RodA, rod shape-determining protein RodA. This protein is a member of the FtsW/RodA/SpoVE family (pfam01098). It is found only in species with rod (or spiral) shapes. In many species, mutation of rodA has been shown to correlate with loss of the normal rod shape. Note that RodA homologs are found, scoring below the cutoffs for this model, in a number of both rod-shaped and coccoid bacteria, including four proteins in Bacillus anthracis, for example. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Cellular processes, Cell division].	3.23854e-160
CP024175.1\|AZW32877.1\|4787080_4787983_+\|acetylglutamate-kinase	gnl\|CDD\|234869	PRK00942, PRK00942, acetylglutamate kinase; Provisional.	1.71108e-158
CP024175.1\|AZW32883.1\|4793284_4795237_-\|penicillin-binding-protein-2	gnl\|CDD\|274573	TIGR03423, pbp2_mrdA, penicillin-binding protein 2. Members of this protein family are penicillin-binding protein 2 (PBP-2), a protein whose gene (designated pbpA or mrdA) generally is found next to the gene for RodA, a protein required for rod (bacillus) shape in many bacteria. PBP-2 acts as a transpeptidase for cell elongation (hence, rod-shape). [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan].	0
CP024175.1\|AZW32878.1\|4787982_4788729_+\|pyrimidine-5'-nucleotidase	gnl\|CDD\|319791	cd02604, HAD_5NT, haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p and Sdt1p. This family includes Saccharomyces cerevisiae Phm8p (phosphate metabolism protein 8) and Sdt1p (Suppressor of disruption of TFIIS). Phm8p participates in the ribose salvage pathway, it catalyzes the dephosphorylation of nucleotide monophosphates to nucleosides, its preferred substrates are nucleotide monophosphates AMP, GMP, CMP, and UMP. Phm8p is also a lysophosphatidic acid phosphatase, dephosphorylating lysophosphatidic acids (LPAs) to monoacylglycerol in response to phosphate starvation. Sdt1p is a pyrimidine and pyridine-specific 5'-nucleotidase; it is an NMN/NaMN 5'-nucleotidases involved in the production of nicotinamide riboside and nicotinic acid riboside, and is a pyrimidine 5'-nucleotidase with high specificity for UMP and CMP. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.	1.14842e-46
CP024175.1\|AZW33541.1\|4779151_4779904_-\|cytochrome-c	gnl\|CDD\|225418	COG2863, COG2863, Cytochrome c553 [Energy production and conversion].	1.67273e-12
CP024175.1\|AZW32885.1\|4795800_4796685_-\|rod-shape-determining-protein-MreC	gnl\|CDD\|237560	PRK13922, PRK13922, rod shape-determining protein MreC; Provisional.	9.0892e-90
CP024175.1\|AZW32869.1\|4780944_4781895_+\|septal-ring-lytic-transglycosylase-RlpA-family-protein	gnl\|CDD\|223868	COG0797, RlpA, Lipoproteins [Cell envelope biogenesis, outer membrane].	5.60479e-55
CP024175.1\|AZW32867.1\|4777854_4779141_-\|alcohol-dehydrogenase	gnl\|CDD\|365823	pfam00034, Cytochrom_C, Cytochrome c. The Pfam entry does not include all Prosite members. The cytochrome 556 and cytochrome c' families are not included. All these are now in a new clan together. The C-terminus of DUF989, pfam06181, has now been merged into this family.	1.87506e-10
CP024175.1\|AZW32881.1\|4791070_4792126_+\|lactate-dehydrogenase	gnl\|CDD\|376860	pfam02615, Ldh_2, Malate/L-lactate dehydrogenase. This family consists of bacterial and archaeal Malate/L-lactate dehydrogenase. L-lactate dehydrogenase, EC:1.1.1.27, catalyzes the reaction (S)-lactate + NAD(+) <=> pyruvate + NADH. Malate dehydrogenase, EC:1.1.1.37 and EC:1.1.1.82, catalyzes the reactions: (S)-malate + NAD(+) <=> oxaloacetate + NADH, and (S)-malate + NADP(+) <=> oxaloacetate + NADPH respectively.	9.5787e-126
CP024175.1\|AZW32875.1\|4785337_4785829_+\|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.	1.58284e-41
CP024175.1\|AZW32868.1\|4780075_4780948_+\|RNase-adaptor-protein-RapZ	gnl\|CDD\|235450	PRK05416, PRK05416, RNase adapter RapZ.	1.18739e-149
CP024175.1\|AZW32874.1\|4784597_4785341_+\|phospholipid-binding-protein	gnl\|CDD\|182907	PRK11023, PRK11023, divisome-associated lipoprotein YraP.	1.20064e-42
CP024175.1\|AZW32873.1\|4783998_4784601_+\|phosphoheptose-isomerase	gnl\|CDD\|237567	PRK13936, PRK13936, phosphoheptose isomerase; Provisional.	1.25469e-125
CP024175.1\|AZW32871.1\|4782460_4783399_-\|16S-rRNA-(cytidine(1402)-2'-O)-methyltransferase	gnl\|CDD\|223390	COG0313, COG0313, Predicted methyltransferases [General function prediction only].	9.54075e-109
CP024175.1\|AZW32876.1\|4786030_4786819_-\|MetQ/NlpA-family-lipoprotein	gnl\|CDD\|224381	COG1464, NlpA, ABC-type metal ion transport system, periplasmic component/surface antigen [Inorganic ion transport and metabolism].	1.17353e-136

>CP024175.1|AZW32875.1|4785337_4785829_+|TlpA-family-protein-disulfide-reductase
MKKIALVLIIAVAAGIGGWFMWRPAQTAPDVAFTTLEGQKITMQDLRGKVVLVKFWATSCVTCVKQMPDNIANYNQYHPQGYETIAVAMNYDPPNYVLNFAQTRKLPFPVALDTSGELAQAFGNVRLTPTAFLIDKQGQIIKRYLGEYDKAEFQATVQKALAG
>CP024175.1|AZW32874.1|4784597_4785341_+|phospholipid-binding-protein
MMPDAKTAARPLLLAAALSAAALTLSACAPLVIGGAAATTAVVVTDRRTSGVQLEDQNIAFKAESQIAQKLGNTARVNAMVYGGHVLLTGDAPTEEAKAQATAIAQSIENVKAVTNQLTVGPAADFSTRSNDTWLTSKVKTALINTKYVPSGTISVTTSRGVVYLMGKVTQAEGDYAANAAAGVGGVARVVKLFETISREEAIRLSGSGTKSGEGSSDGTAAQKAPIESGAAPAGSGSNGVEAIPIK
>CP024175.1|AZW32873.1|4783998_4784601_+|phosphoheptose-isomerase
MRAMDMTSRMTSHFRDAMALCEQSADALAAPLAAAVDLLFAALANNGRILACGNGGSAADAQHFIAELVGRFERERLPLAGIALNTDTSIMTAVGNDYGFDEIFERQVHALGQPGDVLVAISTSGNSPNVVRAMETAREREMHVIALTGKGGGVMGELITPHDVHLCVPHDRTMRIQEVHIILLHALCDGIDALLLGDTE
>CP024175.1|AZW32872.1|4783465_4783999_+|YraN-family-protein
MTDTATRLAFARAAQAQRRLHRRPPASPRASPGARDGGSPTQRRGQAYESAALRWLARQGLRPLARNLRCRAGEIDLAMRDGEVLVLVEVRARAHAGYGGAAASIGASKQGRLARAAALLLPVLLRRHWPGAPPPVRFDVVAFEAGRPHWLRGAFWLAEHAPAQGRRGQDAQGWRVR
>CP024175.1|AZW32871.1|4782460_4783399_-|16S-rRNA-(cytidine(1402)-2'-O)-methyltransferase
MNQDVLSPAPGDAWSRVADRVAAQHWPAATLYVIATPIGNLGDLGLRAWQALVRADVIAAEDTRASRTLLDAWGVSTPLMAAHRHNEASAAQAICERLAQGQRVALVSDAGAPAVSDPGARIVRAVREAGYAVVPVPGPSAVIAALMGSGATSDENPAFAFAGFPPAKAVARQRWLRQWCALPAPVVMFESPHRLAATLADLREAGGPARLLTVARELTKRFEEIATMPLGEAADWLAADAHRGQGEFVLIVHQAPGAQDDEADPADPRTDALLDALLESLSVRDAARVAAKVTGLARDVLYARALARKEQP
>CP024175.1|AZW32870.1|4781891_4782464_-|methylated-DNA--[protein]-cysteine-S-methyltransferase
MNPPSAQATDILYCDTDTPLGPMRLAARGQALCGAWFVDQRDCPAAAGWTLDAAHPALRQAAAELEQWFAGRRRAFEVAMQPEGTPFQRQVWQALLELPFGATISYGELARRVGRPKAARAVAGAVGRNPISILIPCHRIIGHDTSLTGFGGGLPRKQALLAHEGHRYLSRAARARRVSTTQMELPLGAA
>CP024175.1|AZW32869.1|4780944_4781895_+|septal-ring-lytic-transglycosylase-RlpA-family-protein
MIRSRPLALLSTLLLALAIAGCSTPGKKRGGYYKDDGPDANPPSNLDNVPDATPRLEPLASGPNRPYVVFGKRYVPDTSERPFRQQGLASWYGKKFHGNSTSNGESYDMYAMTAAHPTMPIPSYARVTSKINGRTVIVRVNDRGPFHSDRIMDLSYVAAHKLGIIGPGSGPVTVERILPAEILAMNGGAAAPRPGPASATGPLPVAAPSAAAAVELHPATQLASNAPTPPRPAAGAGSGIYLQLGAFSQPANAESLVSRINGQLDPASGIPPAVVEQANNLYRVRIGPYATREAALGAVQPVADRTGILPSLSATP
>CP024175.1|AZW32868.1|4780075_4780948_+|RNase-adaptor-protein-RapZ
MLRVVLITGISGSGKSVALRLLEDAGFTCIDNLPVRFLAEFIANARDDAMERVAVAIDVRSPGELAELPDVITASRAMGTSLSVIFLDANTDTLVQRYSESRRRHPLTDRLARGGKTPSLAECIALERELMAPLRDQEHVIDTSDLTPGQLRAWIRDLIQADRPPLVLTFESFAYKRGVPSDADLMFDVRCLPNPYYDRTLRPLTGRDEPVATWLGGFDIVTQMIDDIAAFIRRWLPQYTQDTRNYLTVAIGCTGGQHRSVYVVEQLARRFSDHDPLLVRHRTQLPDDPA
>CP024175.1|AZW33541.1|4779151_4779904_-|cytochrome-c
MLAFKSDLRIAMRAWRAACGVLAAAAGMLAMSQAVAQGEAALRPDTMAARVAACTACHGEQGRAGPDGYYPRLAGKPQDYLYHQLLNFRDARRQYPPMAHLLNGLPDAYLREMAAYFAGQDVPYPPPARIEASAALVERGRLLVREGDPARAIPSCASCHGASLAGVAPAIPGLLGLPRDYLVAQIGSWQNGLRRAAEPDCMAQVSLKLTPEDIGAVSAWLAGQPVGHPYTPQPAGSLTLPLECGSQAGH
>CP024175.1|AZW32867.1|4777854_4779141_-|alcohol-dehydrogenase
MKIIKRVLVVVILALLAAVATLYWLGTRDHVPAGPQAAPATGSADELVEQGRYLARAGNCMACHTARGGQAYAGGTPIPTPFGTLYGPNITPDAETGIGGWSADDFWQALHNGKGPGGRLLYPAFPYTEYTRMTRADADALYAFLRSVEPVRQASRPHELASPYDQRLLLAAWRALYFEPGGPQADPGQSLQWNRGRYLTEGLGHCAACHTPRNSLGATRAAEALGGGMIDGLGWYAPPLTGQPGTGLGDWSAQDIAALLTTGIAPHSTVAGPMAEVVLGSTQYLSGEDALAIGTYLKSLPAAAPPPARRGAPSATVMELGGKLYSQNCAQCHQADGKGSFPAWPALAGNPSVIAAEPANVIRMVLDGGFAPATAANPRPHGMPPFAQALPDNDIAMLVSYVRNSWGNQAGAVTPLDVKRTRESGAGR
>CP024175.1|AZW32876.1|4786030_4786819_-|MetQ/NlpA-family-lipoprotein
MRMNFVRSALLASAFLLAGGAAQAEKLVVGATQVPHAEILEVVKPALAKEGVELDIKVFTDYVQPNLQLADKQLDANFFQHQPYLDTFNKDRKTNLVSVGLVHVEPFGGYSKKIKSLAELKDGATIAIPNDPSNSGRALLLLQKQGLLKLKDPSNIVATPIDIAENPKKLKFRELEAAMLPRSLDDLDLALINTNYALEAGLVPTRDALFIEGADSPYANLVAARPDNKDAPAVKKLVNALHSEAVRKFIIEKYKGAVVPAF
>CP024175.1|AZW32877.1|4787080_4787983_+|acetylglutamate-kinase
MTDTPDPAAVLSPAVKAAVLSEALPYIRRFHGKTIVVKYGGNAMTEERLQRSFAHDVVLLKLVGLNPVVVHGGGPQIDDALRRIGKQGTFVQGMRVTDAETMEVVEWVLGGQVQQDIVMMINEVGGKAVGLTGKDGMLIQATKKLMVNKDDPSQPLDIGFVGDITRVEPAVVKALQDDQFIPVISPIGYGEDGTAYNINADVVAGKMAEVLGAEKLLMMTNTPGVLDKGGKLLRSLSAQTIDELFADGTISGGMLPKISSSLDAAKNGVNSVHIVDGRVPHCLLLEILTDQGVGTMISSH
>CP024175.1|AZW32878.1|4787982_4788729_+|pyrimidine-5'-nucleotidase
MQARRYLLRPAARLRRSRRIATAAPERLWLFDLDNTLHDTSHAIFPLIDRGMTEAVAETLAVDEATANRLRAEYWRRYGATVIGLVRHHGVDADAFLHRSHNFEVAPLVRAETALADKLRRLPGRKVLLTNAPLHYARAVLRHLGLLRQFDSIWAIEQMRMHGQFRPKPSDALLRYVLAREGVPAARAVLIEDTLDNLRSARRVGLRTVHVFHPGTPFARGHRQRPGYVDLRVNSVSDLLLRRRPLRG
>CP024175.1|AZW32879.1|4788778_4789354_+|nucleoid-occlusion-factor-SlmA
MASKPGERKTQILHTLAEMLEQPHAARITTSALAARMQVSEAALYRHFASKAQMFEGLIEFIETSIFTVVNQIAVSEPYGMGQARKTVAMLLAFAERNRGITRVLTGDALVTEDNRLQERINHINDRIEASLKQCLRVAVSDGALPADANIAAHASLLTHLVLGRWLRYAQSGWRVAPTTHLEEHLRLALG
>CP024175.1|AZW32880.1|4789566_4791060_+|hypothetical-protein
MTAPAAVPAPQSPPKVKIPIGLIAGIIAMVVVLLLPLPAELPPAGHRMLAILAFAVVVWITEAVSYEASAIMITTLMAFLLGTAPNVKNPDVLYGTSAAISMALTGFSNSALALVTGALFIAAAMTFTGLDKRIALVTLARVGTSTRRILLGAIAVTIVLSLVVPSATARSAAVVPIMLGVIAAFGVDKRSNIAAGIMIIVAQATSIWNVGIQTAAAQNLLTVGFMDKMLGERVAWSDWLIAGVPWSLLMSAVLIFVVLRLLPPESDAIAGGKEAVEASLRELGPMTSAQKRLMLVSIMLLLFWSTEGKLHKFDTTSTTYFGLVLLMLPRFGVMTWKDVQTRIPWGTVIVFGVGISLGTALLTTQAGQWLGAQVVAHTGLDHLGPLGIFAILSAFLILIHLGFASATALTSAMLPILIAVLQTLPGDFNRLGMTMLLGFVVSYGFILPINAPQNMVALGTETFTAKQFAKVGIVLTIVGYLLMLLMSVTYWRWLGWM
>CP024175.1|AZW32881.1|4791070_4792126_+|lactate-dehydrogenase
MKLSIAQAIAFGQRLLAAQGVPDDIARDVAEHLVESDRVGYTSHGLSILPNYRRVLAEGFVKADGRAKLLNDRGAMLAFDGDNGFGQHVGKAVMQQAIERARQYGQCIVTLRRTHHLGRMGYYGEMAAEAGLILLAFTNVVNRPPTVAPYGGAQACLTTNPLCFAGPLPGGRPPFLVDMATSSIAVNKARVLAARGEPAPDGALIDAQGNPTNDPNALFADPPGALLPFGGHKGYAMGLVAELLAGVLSGGGTIQPEHPRNGVATNNMFAILLDPQVDFNADWRTQEVGAFIDYLHACPPQPGVDRVQYPGEYEAMNRARHAEAIEFEGAIWDSLAKLAQDLGAADALPRA
>CP024175.1|AZW32882.1|4792151_4793288_-|rod-shape-determining-protein-RodA
MKRLGLILLRVFTAFDWPLLLILILFTLLGLTVMHSAVGSTDWRFAEQSRNFLIAFAAMWAMALVPPNTLMKLALPFYVLGVILLLGVEFFGETSKGATRWLNLGVTRIQPSEMMKIAVPMMLAWYFQRHDGAVRIRDFFVAAAMLAAPFVLIVLQPDLGTALLVFGAGFFVIYFAGLSFKLLVPCLLAGIIAIGTLIYYEDQLCEPEVDWVVLHDYQKHRVCTLLNPSSDPLGKGFHTIQSMIAVGSGGLYGKGYMQGTQTHLDFIPERTTDFIFAVYAEEFGLYGGVALLVLYGLFMARGLAIASRASSQFGRLLAGAITMMMFIYVFVNVGMVTGILPVVGVPLPFMSYGGTALLTMGIACGILMSISRRRPAPA
>CP024175.1|AZW32883.1|4793284_4795237_-|penicillin-binding-protein-2
MFEFKKTGQQQKQRFRLRAWVGGLFALACFGVLAGRFWYLQVDRYEGFSERADRNRIAVVPIPPRRGEILDRNGEVLARNYRTYTLEVVPAQAGNLDQLFDRLARVVYISPSDQRRFKRRVGESSRYASLQLRNNLNDTEAAWFSAHSFEFPGVELRARWVREYPQGEAAAHVVGFIGRIAENDIEELDKAGQLGNYRGTDVIGKKGIEKTWEAALHGRTGLEEVEVTAGGRPMRTLRRIDPVPGSDIMLSIDLELQKLAEQAFEGRRGALVALDPDTGEVLAFVSQPSFDPNLFVDGIDVENWRRLNESPDHPLINRPLYGTYPIGSTYKPFVALAALELGKRRATDRMPDPGYFEFGGQKFRNAGGAAYGMTDMHRAIVVSSDTYFYSLGPEIGVNALHDFSKQFGFGQITGIDLEGEKAGVLPSTEWKRKAYKDRDRQRWYAGETISVAVGQGYNSFTLLQLAQATSTLANSGLYRRPHLVHAIRDSRSGSVNPTEIAPDYRIPLKQENVDVIKRAMADVVRAGTARRAFAGAPYQAAGKTGTAQVFSLRGGQYRASAIDERLRDHALFMGFAPVEQPRIAVALIVENAGWGASAAAPIARTLFDNWLGRADAPSVVRAGAKPVAAEPEAAALELGATDGPMQERRQ
>CP024175.1|AZW32884.1|4795250_4795814_-|rod-shape-determining-protein-MreD
MERTKVSVPARRKLGTPSNVEPERLARPAHGVFVWGTVLLVWLLSLLPWRQWPGSPDVLVLVIAFWCVHEPRRVGLLTAFVFGLLLDVHDAGLLGGHALSYTLTAYGAIALHRRLQRFDLWSQAMHMLPVFFLAQLVTQIILAWLAGKWPGWQWAVSVGLTVAIWPLAGWVLHMPQRRYDDVESSAV
>CP024175.1|AZW32885.1|4795800_4796685_-|rod-shape-determining-protein-MreC
MQRQATPPLFRRGPPAEVRLAVLVILALALLIVDSQLRVLEPVRRAVSVALYPFQRAVMAPRDLVQQVDEWINAASLIRSENEALQRQRIELAQVATHAAQLAAENAQLRRLLGVTDTVAQSAVVVEVLYEPPNAFHQRLVFNKGAKSGLAPGMPVIDEGGVVGQIVRVTPMTAEAALVTDERVSIPVQVLRNGLRLIAFGANTPGVIEVRYLAANADIKVGDTIVTSGVGGLFPAGLPVAKVASVERDTASGFARALGEPLAHPERYRHFLVLQVDVDQAESNRQEADVDGAD

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Crispr_ID: CP024175_8

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

CP024175_8

4801359-4801433

Orphan

Consensus_repeat	Method
CGGGAGCCAGTCCCCGCGGGGAC	CRISPRCasFinder

1 spacers

The CRISPR arrays of CP024175_8

>merge|CP024175|8|4801359-4801433|CRISPRCasFinder
CGGGAGCCAGTCCCCGCGGGGACTGGCTCCTGGAGTCTGCGTGTGCCGCCAGCGGGAGCCTGTCCCCGCGGGGAC

>CP024175|8|8|4801359-4801433|CRISPRCasFinder
CGGGAGCCAGTCCCCGCGGGGAC	TGGCTCCTGGAGTCTGCGTGTGCCGCCAG
CGGGAGCCTGTCCCCGCGGGGAC

Protein	Signature genes	Signature genes Name	Protein_function
CP024175.1\|AZW32896.1\|4807716_4808808_+\|tartrate-dehydrogenase	unknown	unknown	gnl\|CDD\|273963
CP024175.1\|AZW32897.1\|4808850_4810242_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|274824
CP024175.1\|AZW33542.1\|4810314_4810761_-\|DUF305-domain-containing-protein	unknown	unknown	gnl\|CDD\|367619
CP024175.1\|AZW32886.1\|4796773_4797817_-\|rod-shape-determining-protein	unknown	unknown	gnl\|CDD\|237562
CP024175.1\|AZW32885.1\|4795800_4796685_-\|rod-shape-determining-protein-MreC	unknown	unknown	gnl\|CDD\|237560
CP024175.1\|AZW32890.1\|4801450_4802158_-\|orotate-phosphoribosyltransferase	unknown	unknown	gnl\|CDD\|234771
CP024175.1\|AZW32882.1\|4792151_4793288_-\|rod-shape-determining-protein-RodA	unknown	unknown	gnl\|CDD\|274033
CP024175.1\|AZW32891.1\|4802262_4803051_+\|exodeoxyribonuclease-III	unknown	unknown	gnl\|CDD\|197336
CP024175.1\|AZW32889.1\|4799898_4801353_+\|Asp-tRNA(Asn)/Glu-tRNA(Gln)-amidotransferase-GatCAB-subunit-B	unknown	unknown	gnl\|CDD\|235489
CP024175.1\|AZW32883.1\|4793284_4795237_-\|penicillin-binding-protein-2	unknown	unknown	gnl\|CDD\|274573
CP024175.1\|AZW32881.1\|4791070_4792126_+\|lactate-dehydrogenase	unknown	unknown	gnl\|CDD\|376860
CP024175.1\|AZW32892.1\|4803423_4804818_+\|NADP-specific-glutamate-dehydrogenase	unknown	unknown	gnl\|CDD\|181834
CP024175.1\|AZW32887.1\|4798046_4798355_+\|Asp-tRNA(Asn)/Glu-tRNA(Gln)-amidotransferase-GatCAB-subunit-C	unknown	unknown	gnl\|CDD\|178810
CP024175.1\|AZW32895.1\|4806705_4807620_-\|LysR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|176168
CP024175.1\|AZW32888.1\|4798357_4799896_+\|Asp-tRNA(Asn)/Glu-tRNA(Gln)-amidotransferase-GatCAB-subunit-A	unknown	unknown	gnl\|CDD\|234572
CP024175.1\|AZW32898.1\|4810937_4811609_+\|DNA-binding-response-regulator	unknown	unknown	gnl\|CDD\|130454
CP024175.1\|AZW32880.1\|4789566_4791060_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|279307
CP024175.1\|AZW32884.1\|4795250_4795814_-\|rod-shape-determining-protein-MreD	unknown	unknown	gnl\|CDD\|274574
CP024175.1\|AZW32893.1\|4804854_4805493_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|225415
CP024175.1\|AZW32894.1\|4805680_4806547_+\|universal-stress-protein	unknown	unknown	gnl\|CDD\|238182

Protein	Function_ID	Function_description	E-value
CP024175.1\|AZW32896.1\|4807716_4808808_+\|tartrate-dehydrogenase	gnl\|CDD\|273963	TIGR02089, Probable_tartrate_dehydrogenase/decarboxylase, tartrate dehydrogenase. Tartrate dehydrogenase catalyzes the oxidation of both meso- and (+)-tartrate as well as a D-malate. These enzymes are closely related to the 3-isopropylmalate and isohomocitrate dehydrogenases found in TIGR00169 and TIGR02088, respectively. [Energy metabolism, Other].	3.45189e-178
CP024175.1\|AZW32897.1\|4808850_4810242_-\|hypothetical-protein	gnl\|CDD\|274824	TIGR03866, PQQ_ABC_repeats, PQQ-dependent catabolism-associated beta-propeller protein. Members of this protein family consist of seven repeats each of the YVTN family beta-propeller repeat (see TIGR02276). Members occur invariably as part of a transport operon that is associated with PQQ-dependent catabolism of alcohols such as phenylethanol.	1.14159e-21
CP024175.1\|AZW33542.1\|4810314_4810761_-\|DUF305-domain-containing-protein	gnl\|CDD\|367619	pfam03713, DUF305, Domain of unknown function (DUF305). Domain found in small family of bacterial secreted proteins with no known function. Also found in Paramecium bursaria chlorella virus 1. This domain is short and found in one or two copies. The domain has a conserved HH motif that may be functionally important. This domain belongs to the ferritin superfamily. It contains two sequence similar repeats each of which is composed of two alpha helices.	9.52115e-16
CP024175.1\|AZW32886.1\|4796773_4797817_-\|rod-shape-determining-protein	gnl\|CDD\|237562	PRK13927, PRK13927, rod shape-determining protein MreB; Provisional.	0
CP024175.1\|AZW32885.1\|4795800_4796685_-\|rod-shape-determining-protein-MreC	gnl\|CDD\|237560	PRK13922, PRK13922, rod shape-determining protein MreC; Provisional.	9.0892e-90
CP024175.1\|AZW32890.1\|4801450_4802158_-\|orotate-phosphoribosyltransferase	gnl\|CDD\|234771	PRK00455, pyrE, orotate phosphoribosyltransferase; Validated.	4.57247e-80
CP024175.1\|AZW32882.1\|4792151_4793288_-\|rod-shape-determining-protein-RodA	gnl\|CDD\|274033	TIGR02210, Rod_shape-determining_protein_RodA, rod shape-determining protein RodA. This protein is a member of the FtsW/RodA/SpoVE family (pfam01098). It is found only in species with rod (or spiral) shapes. In many species, mutation of rodA has been shown to correlate with loss of the normal rod shape. Note that RodA homologs are found, scoring below the cutoffs for this model, in a number of both rod-shaped and coccoid bacteria, including four proteins in Bacillus anthracis, for example. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Cellular processes, Cell division].	3.23854e-160
CP024175.1\|AZW32891.1\|4802262_4803051_+\|exodeoxyribonuclease-III	gnl\|CDD\|197336	cd10281, Nape_like_AP-endo, Neisseria meningitides Nape-like subfamily of the ExoIII family purinic/apyrimidinic (AP) endonucleases. This subfamily includes Neisseria meningitides Nape and related proteins. These are Escherichia coli exonuclease III (ExoIII)-like AP endonucleases and belong to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. AP endonucleases participate in the DNA base excision repair (BER) pathway. AP sites are one of the most common lesions in cellular DNA. During BER the damaged DNA is first recognized by DNA glycosylase. AP endonucleases then catalyze the hydrolytic cleavage of the phosphodiester bond 5' to the AP site, and this is followed by the coordinated actions of DNA polymerase, deoxyribose phosphatase, and DNA ligase. If left unrepaired, AP sites block DNA replication, and have both mutagenic and cytotoxic effects. AP endonucleases can carry out a variety of excision and incision reactions on DNA, including 3'-5' exonuclease, 3'-deoxyribose phosphodiesterase, 3'-phosphatase, and occasionally, nonspecific DNase activities. Different AP endonuclease enzymes catalyze the different reactions with different efficiences. Many organisms have two AP endonucleases, usually one is the dominant AP endonuclease, the other has weak AP endonuclease activity; for example, Neisseria meningitides Nape and NExo. Nape, found in this subfamily, is the dominant AP endonuclease. It exhibits strong AP endonuclease activity, and also exhibits 3'-5'exonuclease and 3'-deoxyribose phosphodiesterase activities.	1.64731e-140
CP024175.1\|AZW32889.1\|4799898_4801353_+\|Asp-tRNA(Asn)/Glu-tRNA(Gln)-amidotransferase-GatCAB-subunit-B	gnl\|CDD\|235489	PRK05477, gatB, Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase subunit GatB.	0
CP024175.1\|AZW32883.1\|4793284_4795237_-\|penicillin-binding-protein-2	gnl\|CDD\|274573	TIGR03423, pbp2_mrdA, penicillin-binding protein 2. Members of this protein family are penicillin-binding protein 2 (PBP-2), a protein whose gene (designated pbpA or mrdA) generally is found next to the gene for RodA, a protein required for rod (bacillus) shape in many bacteria. PBP-2 acts as a transpeptidase for cell elongation (hence, rod-shape). [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan].	0
CP024175.1\|AZW32881.1\|4791070_4792126_+\|lactate-dehydrogenase	gnl\|CDD\|376860	pfam02615, Ldh_2, Malate/L-lactate dehydrogenase. This family consists of bacterial and archaeal Malate/L-lactate dehydrogenase. L-lactate dehydrogenase, EC:1.1.1.27, catalyzes the reaction (S)-lactate + NAD(+) <=> pyruvate + NADH. Malate dehydrogenase, EC:1.1.1.37 and EC:1.1.1.82, catalyzes the reactions: (S)-malate + NAD(+) <=> oxaloacetate + NADH, and (S)-malate + NADP(+) <=> oxaloacetate + NADPH respectively.	9.5787e-126
CP024175.1\|AZW32892.1\|4803423_4804818_+\|NADP-specific-glutamate-dehydrogenase	gnl\|CDD\|181834	PRK09414, PRK09414, NADP-specific glutamate dehydrogenase.	0
CP024175.1\|AZW32887.1\|4798046_4798355_+\|Asp-tRNA(Asn)/Glu-tRNA(Gln)-amidotransferase-GatCAB-subunit-C	gnl\|CDD\|178810	PRK00034, gatC, Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase subunit GatC.	1.84578e-32
CP024175.1\|AZW32895.1\|4806705_4807620_-\|LysR-family-transcriptional-regulator	gnl\|CDD\|176168	cd08479, PBP2_CrgA_like_9, The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional regulator CrgA-like, contains the type 2 periplasmic binding fold. This CD represents the substrate binding domain of an uncharacterized LysR-type transcriptional regulator (LTTR) CrgA-like 9. The LTTRs are acting as both auto-repressors and activators of target promoters, controlling operons involved in a wide variety of cellular processes such as amino acid biosynthesis, CO2 fixation, antibiotic resistance, degradation of aromatic compounds, nodule formation of nitrogen-fixing bacteria, and synthesis of virulence factors, to name a few. In contrast to the tetrameric form of other LTTRs, CrgA from Neisseria meningitides assembles into an octameric ring, which can bind up to four 63-bp DNA oligonucleotides. Phylogenetic cluster analysis showed that the CrgA-like regulators form a subclass of the LTTRs that function as octamers. The CrgA is an auto-repressor of its own gene and activates the expression of the mdaB gene which coding for an NADPH-quinone reductase and that its action is increased by MBL (alpha-methylene-gamma-butyrolactone), an inducer of NADPH-quinone oxidoreductase. The structural topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.	5.26972e-105
CP024175.1\|AZW32888.1\|4798357_4799896_+\|Asp-tRNA(Asn)/Glu-tRNA(Gln)-amidotransferase-GatCAB-subunit-A	gnl\|CDD\|234572	PRK00012, gatA, Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase subunit GatA.	0
CP024175.1\|AZW32898.1\|4810937_4811609_+\|DNA-binding-response-regulator	gnl\|CDD\|130454	TIGR01387, Transcriptional_regulatory_protein_PcoR, heavy metal response regulator. Members of this family contain a response regulator receiver domain (pfam00072) and an associated transcriptional regulatory region (pfam00486). This group is separated phylogenetically from related proteins with similar architecture and contains a number of proteins associated with heavy metal resistance efflux systems for copper, silver, cadmium, and/or zinc. Most members encoded by genes adjacent to genes for encoding a member of the heavy metal sensor histidine kinase family (TIGRFAMs:TIGR01386), its partner in the two-component response regulator system. [Regulatory functions, DNA interactions].	6.44921e-106
CP024175.1\|AZW32880.1\|4789566_4791060_+\|hypothetical-protein	gnl\|CDD\|279307	pfam00939, Na_sulph_symp, Sodium:sulfate symporter transmembrane region. There are also some members in this family that do not match the Prosite motif, and belong to the subfamily SODIT1.	2.68833e-115
CP024175.1\|AZW32884.1\|4795250_4795814_-\|rod-shape-determining-protein-MreD	gnl\|CDD\|274574	TIGR03426, shape_MreD, rod shape-determining protein MreD. Members of this protein family are the MreD protein of bacterial cell shape determination. Most rod-shaped bacteria depend on MreB and RodA to achieve either a rod shape or some other non-spherical morphology such as coil or stalk formation. MreD is encoded in an operon with MreB, and often with RodA and PBP-2 as well. It is highly hydrophobic (therefore somewhat low-complexity) and highly divergent, and therefore sometimes tricky to discover by homology, but this model finds most examples. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan].	7.62373e-19
CP024175.1\|AZW32893.1\|4804854_4805493_-\|hypothetical-protein	gnl\|CDD\|225415	COG2860, COG2860, Predicted membrane protein [Function unknown].	5.30548e-72
CP024175.1\|AZW32894.1\|4805680_4806547_+\|universal-stress-protein	gnl\|CDD\|238182	cd00293, USP_Like, Usp: Universal stress protein family. The universal stress protein Usp is a small cytoplasmic bacterial protein whose expression is enhanced when the cell is exposed to stress agents. Usp 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 Usp reveals an alpha/beta fold similar to that of the Methanococcus jannaschii MJ0577 protein, which binds ATP, athough Usp lacks ATP-binding activity.	7.81466e-22

>CP024175.1|AZW32889.1|4799898_4801353_+|Asp-tRNA(Asn)/Glu-tRNA(Gln)-amidotransferase-GatCAB-subunit-B
MNWEIVIGLETHTQLSTDSKIFSGSSTRFGAAPNTQANAVDLALPGSLPVMNRGAAERAILFGLAVGGKVAPRSVFARKNYFYPDLPKGYQISQYELPVVEGGTLSFFVGEEEKTVNLTRAHLEEDAGKSLHDEFSLASGAPASGIDLNRAGTPLLEIVTEPEMRSAAEAVAYARALHSLVVWLGICDGNMQEGSFRCDANVSVRPVGQKEFGTRTEIKNVNSFRFLERAILFEARRQIELIEDGGTVVQETRLYDADRDETRSMRSKEDAHDYRYFPDPDLPPLVIGQDWVDAVRAGMPELPAAQRARFEADYGLPAYDAAQLTVSRAMADYFEAVARALPAGQAKLAANWIMGEVAATLNREEKDIDAAPVSAAALAALINRIIDGTISNKIARDVFAAMWAGENGGDADAIIEARGLKQISDSGAIGAMIDDVLAANPAIVEEYRAGKQKAFNSLVGQIMKAAKGKANPQQVNELLKEKLG
>CP024175.1|AZW32888.1|4798357_4799896_+|Asp-tRNA(Asn)/Glu-tRNA(Gln)-amidotransferase-GatCAB-subunit-A
MTQSALHTEFGGIAALRDALARRQVSAVELAQSGLDAAQAASGLNAFLHIDPDLTLAQARAADAALAAGTAGPLAGIPIAHKDAFVTRGWRTTAGSKMLAGYASPFDATVVERLAEAGAVSLGKLNCDEFAMGSGNENSAYGPVRNPWDTQAVPGGSSGGSAAAVAARLVAAATGTDTGGSVRQPAALCGVSGIKPTYGTVSRYGMIAFGSSLDQAGPLAPSSRDLLELLDVMTGFDPRDATSLQACDGQANESGRVRRGHDAAQAGYDAAGSQPLKGLRIGVPQEYFGAGLAPDVAAAVEAALAQFEQLGAVRVPVSLPRTELAIPAYYVIAPAEASSNLARYDGVRYGHRAAQYGDLNEMISRSRAEGFGDEVKRRILIGTYVLSHGYYDAYYLQAQRLRRLIAQDFQRAFADQCDVIMGPVSPTVAKNIGDNRDDPTADWLADVYTLGVSLAGLPAMSVPCGFGGQDGRRPVGLQIIGNYFDEGRLLALADRYQQVTDWHQRAPVSQDA
>CP024175.1|AZW32887.1|4798046_4798355_+|Asp-tRNA(Asn)/Glu-tRNA(Gln)-amidotransferase-GatCAB-subunit-C
MALNEQDVARIARLARIELTPDQRGRAQAELNGILHLIERLQAVDTQGVEPLAHPLSAHEDITLRLREDAVSEQATEARRAELLANAPESADGLFLVPKVIE
>CP024175.1|AZW32886.1|4796773_4797817_-|rod-shape-determining-protein
MFGFLRSYFSSDMAIDLGTANTLIYVRGKGIVLDEPSVVAIRHEGGPNGKKIIQAVGHEAKQMLGRVPGNIEAIRPMKDGVIADFTVTEQMLKQFIRMVHPRNMLAPSPRIIVCVPCGSTQVERRAIRESALGAGASHVYLIEEPMAAAIGAGLAVSDASGSMVVDIGGGTTEVAVISLGGMVYKGSVRVGGDKFDEAIVNYIRRNYGMLIGEPTAELIKKEIGSAFPGSEVREIEVKGRNLAEGVPRSFTVSSNEILESLTDPLNQIVSAVKIALEQTPPELGADITDKGIALTGGGALLRDLDRLLQEETGLPVVVADDPLTCVVRGCGEALEHLEKLGAIFIND
>CP024175.1|AZW32885.1|4795800_4796685_-|rod-shape-determining-protein-MreC
MQRQATPPLFRRGPPAEVRLAVLVILALALLIVDSQLRVLEPVRRAVSVALYPFQRAVMAPRDLVQQVDEWINAASLIRSENEALQRQRIELAQVATHAAQLAAENAQLRRLLGVTDTVAQSAVVVEVLYEPPNAFHQRLVFNKGAKSGLAPGMPVIDEGGVVGQIVRVTPMTAEAALVTDERVSIPVQVLRNGLRLIAFGANTPGVIEVRYLAANADIKVGDTIVTSGVGGLFPAGLPVAKVASVERDTASGFARALGEPLAHPERYRHFLVLQVDVDQAESNRQEADVDGAD
>CP024175.1|AZW32884.1|4795250_4795814_-|rod-shape-determining-protein-MreD
MERTKVSVPARRKLGTPSNVEPERLARPAHGVFVWGTVLLVWLLSLLPWRQWPGSPDVLVLVIAFWCVHEPRRVGLLTAFVFGLLLDVHDAGLLGGHALSYTLTAYGAIALHRRLQRFDLWSQAMHMLPVFFLAQLVTQIILAWLAGKWPGWQWAVSVGLTVAIWPLAGWVLHMPQRRYDDVESSAV
>CP024175.1|AZW32883.1|4793284_4795237_-|penicillin-binding-protein-2
MFEFKKTGQQQKQRFRLRAWVGGLFALACFGVLAGRFWYLQVDRYEGFSERADRNRIAVVPIPPRRGEILDRNGEVLARNYRTYTLEVVPAQAGNLDQLFDRLARVVYISPSDQRRFKRRVGESSRYASLQLRNNLNDTEAAWFSAHSFEFPGVELRARWVREYPQGEAAAHVVGFIGRIAENDIEELDKAGQLGNYRGTDVIGKKGIEKTWEAALHGRTGLEEVEVTAGGRPMRTLRRIDPVPGSDIMLSIDLELQKLAEQAFEGRRGALVALDPDTGEVLAFVSQPSFDPNLFVDGIDVENWRRLNESPDHPLINRPLYGTYPIGSTYKPFVALAALELGKRRATDRMPDPGYFEFGGQKFRNAGGAAYGMTDMHRAIVVSSDTYFYSLGPEIGVNALHDFSKQFGFGQITGIDLEGEKAGVLPSTEWKRKAYKDRDRQRWYAGETISVAVGQGYNSFTLLQLAQATSTLANSGLYRRPHLVHAIRDSRSGSVNPTEIAPDYRIPLKQENVDVIKRAMADVVRAGTARRAFAGAPYQAAGKTGTAQVFSLRGGQYRASAIDERLRDHALFMGFAPVEQPRIAVALIVENAGWGASAAAPIARTLFDNWLGRADAPSVVRAGAKPVAAEPEAAALELGATDGPMQERRQ
>CP024175.1|AZW32882.1|4792151_4793288_-|rod-shape-determining-protein-RodA
MKRLGLILLRVFTAFDWPLLLILILFTLLGLTVMHSAVGSTDWRFAEQSRNFLIAFAAMWAMALVPPNTLMKLALPFYVLGVILLLGVEFFGETSKGATRWLNLGVTRIQPSEMMKIAVPMMLAWYFQRHDGAVRIRDFFVAAAMLAAPFVLIVLQPDLGTALLVFGAGFFVIYFAGLSFKLLVPCLLAGIIAIGTLIYYEDQLCEPEVDWVVLHDYQKHRVCTLLNPSSDPLGKGFHTIQSMIAVGSGGLYGKGYMQGTQTHLDFIPERTTDFIFAVYAEEFGLYGGVALLVLYGLFMARGLAIASRASSQFGRLLAGAITMMMFIYVFVNVGMVTGILPVVGVPLPFMSYGGTALLTMGIACGILMSISRRRPAPA
>CP024175.1|AZW32881.1|4791070_4792126_+|lactate-dehydrogenase
MKLSIAQAIAFGQRLLAAQGVPDDIARDVAEHLVESDRVGYTSHGLSILPNYRRVLAEGFVKADGRAKLLNDRGAMLAFDGDNGFGQHVGKAVMQQAIERARQYGQCIVTLRRTHHLGRMGYYGEMAAEAGLILLAFTNVVNRPPTVAPYGGAQACLTTNPLCFAGPLPGGRPPFLVDMATSSIAVNKARVLAARGEPAPDGALIDAQGNPTNDPNALFADPPGALLPFGGHKGYAMGLVAELLAGVLSGGGTIQPEHPRNGVATNNMFAILLDPQVDFNADWRTQEVGAFIDYLHACPPQPGVDRVQYPGEYEAMNRARHAEAIEFEGAIWDSLAKLAQDLGAADALPRA
>CP024175.1|AZW32880.1|4789566_4791060_+|hypothetical-protein
MTAPAAVPAPQSPPKVKIPIGLIAGIIAMVVVLLLPLPAELPPAGHRMLAILAFAVVVWITEAVSYEASAIMITTLMAFLLGTAPNVKNPDVLYGTSAAISMALTGFSNSALALVTGALFIAAAMTFTGLDKRIALVTLARVGTSTRRILLGAIAVTIVLSLVVPSATARSAAVVPIMLGVIAAFGVDKRSNIAAGIMIIVAQATSIWNVGIQTAAAQNLLTVGFMDKMLGERVAWSDWLIAGVPWSLLMSAVLIFVVLRLLPPESDAIAGGKEAVEASLRELGPMTSAQKRLMLVSIMLLLFWSTEGKLHKFDTTSTTYFGLVLLMLPRFGVMTWKDVQTRIPWGTVIVFGVGISLGTALLTTQAGQWLGAQVVAHTGLDHLGPLGIFAILSAFLILIHLGFASATALTSAMLPILIAVLQTLPGDFNRLGMTMLLGFVVSYGFILPINAPQNMVALGTETFTAKQFAKVGIVLTIVGYLLMLLMSVTYWRWLGWM
>CP024175.1|AZW32890.1|4801450_4802158_-|orotate-phosphoribosyltransferase
MAGFAISPIARMSASASTAADFVRFALDEGVLRFGSFKVKSGRISPYFFNAGLFNSGRSVGTLAGFYAQALIDSGVAFDMLFGPAYKGIPLATATSVALAGHGAMAGRDVPFAFNRKEAKDHGEGGTLVGAPLTGKVVIIDDVITAGTSVRESVEIIRAAGAEPAAVLIALDRMERAGPDDALSPHSAVQDVARTYGIPVVSIASLADIMTLLQDDAQFAEHRAAVQAYRSKYGV
>CP024175.1|AZW32891.1|4802262_4803051_+|exodeoxyribonuclease-III
MLRITSLNLNGIRSAFRKGLQPWMTAHNADVLCLQEIKVSHDDLTDELRHPPGYTGHFHHAEKKGYSGVGMYLRAGAERVVAGFDCEEFDAEGRILRADWKDLSVISAYLPSGSSGDERQQAKYRFLDQFGPWLDGLMAEHRKTGREFVICGDWNIAHKEIDLKNWKGNQKNSGFLPEERAWLTEVFDRRGFVDVFRKLDERADQYTWWSNRGQAWAKNVGWRIDYQIATPGIAERARATSIYKDERFSDHAPLTVDYDIAL
>CP024175.1|AZW32892.1|4803423_4804818_+|NADP-specific-glutamate-dehydrogenase
MHRNTTRCTIALPGGSILKLQSLDDFLRRVAARDPQQAEFMQAVQEVMLSLWPFIEKHPHYAEHALLERLVEPERVIQFRVCWTDDQGQAQVNRAFRIQHSSAIGPFKGGMRFHPTVNLSVLKFLAFEQTLKNALTTLPMGGGKGGSDFDPKGKSDAEVMRFCQALMLELHRHLGPDTDVPAGDIGVGAREVGFMAGMMKKLSNSAASVFTGKGLCFGGSLIRPEATGYGTVYFAQEMLQRAGLSFDGMRVSVSGSGNVAQYAIEKAMALGAKVVTISDSCGTVIDEAGFTHEKLLALMHIKNDLRGRLDTYASQFGLRYEAGVRPWHVPVDVALPCATQNELDENDARTLIRNGVKCVAEGANMPATLDAAKAFIAAEVLYAPGKASNAGGVAVSGLEMSQNSARLPWTREQVDARLHAIMRDIHENCVRHGHGAGNYVNYVDGANIAGFVKVADAMRQQGLY
>CP024175.1|AZW32893.1|4804854_4805493_-|hypothetical-protein
MPPDPSVLLLYTLYLVAIVAEAMTAALAAGRRDMDWVGVCVIACVTALGGGSLRDVLLGHYPLSWVAHPEYLWMTAGAALLTALGARALRRLRSLFLLLDAIGLVAFTIIGCQVAQQMEMPLTIVLVSGMITGCAGGVLRDVLCNDIPLLFRSELYASVSAVTGGLYLAMYGQGVSASVSVPVALAVGLAFRLLALRFNWQMPKFVYRGDWH
>CP024175.1|AZW32894.1|4805680_4806547_+|universal-stress-protein
MQAQTAPILLATDLSARSDRALDRALMLAAQAQTSLVALHIMEPTNAPLTTPVWRRLSADHKQLAERRLAEDLADAPVPTSAVVRSGETVPLIRETADHFGCSLIVTGIARESTLSRLLLGTTVERLARQASQPVLVVKARPRKPYRDVVVATDFSEGSRQALVAALRVAGDAPLTLFHAYDVPFGKDAPEDAVVRSFYNDAAQKARAFLDGTPELAGRPAPELVLESGQPETLLSEYVFNRRCDLVVTGTHGLTGILRTAIGSVAEKLLEALPCDVLIVRQTGTAGD
>CP024175.1|AZW32895.1|4806705_4807620_-|LysR-family-transcriptional-regulator
MSNIPANEDLRVFLHVARLSSFAAAAEELRVSTAYVSKRLRVLEGVLGVRLLHRTTRRVSVTREGERVFLWAQRVLDNVDQLMQEVAATRAVPRGLLRVSCSFGFGRNVVGPMLSRLVERFPALQVRLEVFDRLVDVASEGFDLDVRVGDDIAPHLIARRLADNHRLLCAAPDYLARRGTPRTPEELAGHDCLVIKERDHPFGVWTLRAGAENRTIKVTGPLSANNGEIAVRWAVDGRGIVLRSHWDVAPLLRDGLLVPLLAPWRQDANIWAVYPSRLENSAKVRVAVEFLQEEFRRFAAQAGG
>CP024175.1|AZW32896.1|4807716_4808808_+|tartrate-dehydrogenase
MSSPRTYRIAAIAGDGIGREVMPEGLRVVRAAARRFGLDLDIVTFDWAHCDYYREHGQMMPDDWKAQLAGMDAIYFGAVGWPATVPDHVSLWGSLLKFRREFDQYINLRPVRLFEGVPCPLAGRQPGDIDYLVVRENTEGEYTSAGGVIYEGTEREIVIQESVYSRYGADRVLHYAYALADSRPRRRLTVATKSNGIAISMPWWDKRADAVGQQYPGVAVDKQHIDILSARFVLQPDRFDVVVASNLFGDILSDLGPATTGTIGLAPSANLNPEREFPSLFEPVHGSAPDIYGQNIANPVAMIWSGALMLDFLTEGAGAGRAAHDAIVAAIEHVLAHGPRTRDLGGSAATDAMGEAIAARLAA
>CP024175.1|AZW32897.1|4808850_4810242_-|hypothetical-protein
MKKTYSFCALAALALHAGAAWSLPSAHDRVYTADQNSNTVSVVDPSTNTLLGQIRLGNARPDLLSPLYKGQINVHGMGFSPDHKTLLVVSNGSNSATFIDTATNKVKGITYLGRSPHEGFFTMDGKQAWVVVRGEDYISVIDPQTFKETDRIQTNLGPGMVIFHPDGKLAFVVSSFTPSVDVIDVKSHKIVKKIDVVSPFSPFLQITPDNSEIWMTHKDVGKVTRIDTKSLQVTGVMDTGFITNHIAFAPVAGKTYAYVTIGGENAVKVYTTDKPAKLVATIPTGALPHGIWTSDDGSRVYVGLENGDALDVIDTASNKVVKRVPVGQAPQALAFVSGVVAQGRGDQNLVPRVNGDPVNIALKPVGKQGRGFVVLRNLGVVDALEVNLFGLKAETVYNVYLNGVKAPVASFRTGADGKAAGTMIAPLRQPAEPHATAAAGQGGIVIMEGDAPVDAARAVLVGA
>CP024175.1|AZW33542.1|4810314_4810761_-|DUF305-domain-containing-protein
MQLLLKGPFHAGAGRSVAALLLCLAGGYASAHGGHHGADPSAPAAGAAKAPPVFVASTAKPFSALMDDAMAVMDEGMLRAPMNGQSNHDFMTMMMPHHQGAVDMAKAVLLYTEDPEVRNLALGIITEQQNEIRVMQAWLDRHAAAAGK
>CP024175.1|AZW32898.1|4810937_4811609_+|DNA-binding-response-regulator
MAILVIEDDLKTGDYLKKGLLESGYSVDLARNGIDGLHRLREQRYDVLVLDVMLPGKDGWQVIEEVRQDSDVPVIFLTARDHVADRIRGLRLGADDYLVKPFSFAELVLRIQTMLRRGAARAAETLQVADLRLDPVRRKVTRGGASIVLTNKEFMLLHLLVRRQGEALSRTIIASEVWDMNFDSDTNVVDVAIKRLRAKVDAPFPLKLIQTVRGIGYALAEQP

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Self-targeting detection

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_ID	Protospacer_location	Mismatch	Identity
CP024175_4	4.1\|4322809\|17\|CP024175\|CRISPRCasFinder	4322809-4322825	17	CP024175.1	3027692-3027708	1	0.941
CP024175_4	4.2\|4322852\|33\|CP024175\|CRISPRCasFinder	4322852-4322884	33	CP024175.1	916551-916583	1	0.97
CP024175_4	4.4\|4322852\|41\|CP024175\|PILER-CR	4322852-4322892	41	CP024175.1	916543-916583	1	0.976
CP024175_4	4.4\|4322852\|41\|CP024175\|PILER-CR	4322852-4322892	41	CP024175.1	4740117-4740157	1	0.976
CP024175_4	4.4\|4322852\|41\|CP024175\|PILER-CR	4322852-4322892	41	CP024175.1	4032005-4032045	2	0.951

1. spacer 4.1|4322809|17|CP024175|CRISPRCasFinder matches to position: 3027692-3027708, mismatch: 1, identity: 0.941

acccacaaattcctggg	CRISPR spacer
acccgcaaattcctggg	Protospacer
****.************

2. spacer 4.2|4322852|33|CP024175|CRISPRCasFinder matches to position: 916551-916583, mismatch: 1, identity: 0.97

acctgcaagatttcatggcgtctgcccgtgcgt	CRISPR spacer
acctgcaagatttcatggcgtctgccggtgcgt	Protospacer
************************** ******

3. spacer 4.4|4322852|41|CP024175|PILER-CR matches to position: 916543-916583, mismatch: 1, identity: 0.976

ggactggcacctgcaagatttcatggcgtctgcccgtgcgt	CRISPR spacer
ggactggcacctgcaagatttcatggcgtctgccggtgcgt	Protospacer
********************************** ******

4. spacer 4.4|4322852|41|CP024175|PILER-CR matches to position: 4740117-4740157, mismatch: 1, identity: 0.976

ggactggcacctgcaagatttcatggcgtctgcccgtgcgt	CRISPR spacer
ggactggcgcctgcaagatttcatggcgtctgcccgtgcgt	Protospacer
********.********************************

5. spacer 4.4|4322852|41|CP024175|PILER-CR matches to position: 4032005-4032045, mismatch: 2, identity: 0.951

ggactggcacctgcaagatttcatggcgtctgcccgtgcgt	CRISPR spacer
ggactggcgcctgcaagattccatggcgtctgcccgtgcgt	Protospacer
********.***********.********************

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity

Prophage detection

Region

Region Position

Protein_number

Hit_taxonomy

Key_proteins

Att_site

Prophage annotation

DBSCAN-SWA_1

2375194 : 2383384

Moraxella_phage(28.57%)

tRNA

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

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
AZW30754.1\|2375194_2375782_+	thymidylate synthase	A0A1X9I5T8	Streptococcus_phage	2.8e-16	35.8
AZW30755.1\|2375799_2376183_-	thioredoxin	V9SJ74	Achromobacter_phage	8.1e-09	25.8
AZW30756.1\|2376318_2377344_-	LLM class flavin-dependent oxidoreductase	NA	NA	NA	NA
AZW30757.1\|2377549_2378842_-	NCS2 family permease	A0A0R6PHV4	Moraxella_phage	1.7e-66	36.0
AZW30758.1\|2378976_2380017_+\|tRNA	tRNA (adenosine(37)-N6)-threonylcarbamoyltransferase complex transferase subunit TsaD	A0A0R6PI74	Moraxella_phage	9.3e-92	51.6
AZW30759.1\|2380186_2380834_-	glycerol-3-phosphate acyltransferase	NA	NA	NA	NA
AZW30760.1\|2380959_2381718_+	5'-nucleotidase SurE	A0A1B1ITZ2	uncultured_Mediterranean_phage	8.1e-69	51.2
AZW33458.1\|2381792_2382482_+	protein-L-isoaspartate(D-aspartate) O-methyltransferase	A0A1B1IU40	uncultured_Mediterranean_phage	3.2e-32	46.9
AZW30761.1\|2382499_2383384_+	peptidase	A0A292GJG6	Xanthomonas_phage	4.6e-15	49.5

DBSCAN-SWA_2

3211111 : 3259887

Pseudomonas_phage(24.24%)

head,integrase,capsid,tail,terminase,portal,protease

attL 3206574:3206592|attR 3263808:3263826

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
3206574:3206592	attL	NA	NA	NA	NA
AZW31478.1\|3211111_3212416_-\|protease	ATP-dependent Clp protease ATP-binding subunit ClpX	G3M9Z9	Bacillus_virus	5.4e-129	53.8
AZW31479.1\|3212520_3213174_-\|protease	ATP-dependent Clp protease proteolytic subunit	A0A223W000	Agrobacterium_phage	6.8e-56	57.5
AZW31480.1\|3213176_3214487_-	trigger factor	NA	NA	NA	NA
AZW31481.1\|3214665_3215244_+	TIGR00645 family protein	K4K6D8	Caulobacter_phage	6.0e-24	33.7
AZW31482.1\|3215341_3215548_-	cold-shock protein	A0A2H4N7Y6	Lake_Baikal_phage	8.1e-16	62.1
AZW31483.1\|3215893_3216460_-	DUF924 domain-containing protein	NA	NA	NA	NA
AZW31484.1\|3216543_3216747_-	cold-shock protein CspA	A0A2H4N7Y6	Lake_Baikal_phage	1.6e-16	62.1
AZW31485.1\|3217053_3217374_-	hypothetical protein	NA	NA	NA	NA
AZW31486.1\|3217415_3217697_-	hypothetical protein	NA	NA	NA	NA
AZW31487.1\|3217771_3219019_-	autotransporter Phg	NA	NA	NA	NA
AZW31488.1\|3219401_3219731_+	DUF4148 domain-containing protein	NA	NA	NA	NA
AZW31489.1\|3220096_3220768_+	SOS response-associated peptidase	Q5QF62	Pseudomonas_virus	2.7e-36	40.3
AZW31490.1\|3220815_3221109_+	hypothetical protein	NA	NA	NA	NA
AZW33491.1\|3221466_3221721_+	transcriptional regulator	NA	NA	NA	NA
AZW31491.1\|3222208_3222706_+	helix-turn-helix domain-containing protein	NA	NA	NA	NA
AZW31492.1\|3222987_3223188_+	hypothetical protein	NA	NA	NA	NA
AZW31493.1\|3223379_3223646_-	hypothetical protein	NA	NA	NA	NA
AZW31494.1\|3223645_3224194_-	hypothetical protein	I6NSS1	Burkholderia_phage	7.7e-29	52.7
AZW31495.1\|3224190_3224664_-	hypothetical protein	A0A075CF93	Pseudomonas_phage	2.7e-14	38.5
AZW31496.1\|3224723_3225113_-	hypothetical protein	NA	NA	NA	NA
AZW31497.1\|3225109_3225838_-	hypothetical protein	NA	NA	NA	NA
AZW33492.1\|3225890_3229664_-	hypothetical protein	I7HDJ4	Xanthomonas_virus	1.6e-61	27.1
AZW31498.1\|3229702_3230089_-	hypothetical protein	NA	NA	NA	NA
AZW31499.1\|3230088_3230565_-	DUF1833 domain-containing protein	I7GYA2	Xanthomonas_virus	3.1e-10	25.2
AZW31500.1\|3230566_3230914_-	hypothetical protein	NA	NA	NA	NA
AZW31501.1\|3230915_3233054_-	hypothetical protein	A0A088FB58	Idiomarinaceae_phage	2.6e-32	27.9
AZW31502.1\|3233054_3233279_-	hypothetical protein	NA	NA	NA	NA
AZW31503.1\|3233359_3233692_-	hypothetical protein	NA	NA	NA	NA
AZW31504.1\|3233695_3234172_-\|tail	phage tail protein	NA	NA	NA	NA
AZW31505.1\|3234231_3234603_-	DUF3168 domain-containing protein	NA	NA	NA	NA
AZW31506.1\|3235347_3235710_-\|head,tail	head-tail adaptor protein	Q9XJT0	Pseudomonas_phage	9.9e-33	58.7
AZW31507.1\|3235710_3236055_-\|head,tail	phage gp6-like head-tail connector protein	H2BDB3	Pseudomonas_virus	1.4e-23	54.0
AZW31508.1\|3236045_3236699_-	methyltransferase domain-containing protein	H2BDB7	Pseudomonas_virus	2.5e-50	49.5
AZW33493.1\|3236622_3237507_-	hypothetical protein	B5WZS7	Pseudomonas_phage	8.3e-73	53.4
AZW33494.1\|3237518_3237761_-	hypothetical protein	H2BDB2	Pseudomonas_virus	2.1e-23	60.0
AZW31509.1\|3238272_3239478_-\|capsid	phage major capsid protein	A0A2H4PI18	Pseudomonas_phage	3.6e-119	57.1
AZW31510.1\|3239480_3240356_-	peptidase	A0A0U4B0F3	Pseudomonas_phage	2.5e-82	54.5
AZW31511.1\|3240373_3241744_-\|portal	phage portal protein	G0ZT36	Aeromonas_phage	1.6e-144	60.7
AZW31512.1\|3241740_3243414_-\|terminase	terminase large subunit	A0A1W6JP18	Morganella_phage	5.9e-104	39.2
AZW31513.1\|3243410_3243917_-	hypothetical protein	C7BGG6	Burkholderia_phage	5.1e-19	37.3
AZW31514.1\|3243998_3244376_-	HNH endonuclease	A0A218MNA6	uncultured_virus	4.4e-07	33.3
AZW31515.1\|3244663_3244915_-	hypothetical protein	NA	NA	NA	NA
AZW31516.1\|3245045_3245273_-	hypothetical protein	NA	NA	NA	NA
AZW31517.1\|3245609_3248021_-	hypothetical protein	A0A2D1GN57	Marinobacter_phage	1.3e-80	45.0
AZW31518.1\|3248302_3248857_-	hypothetical protein	B7SYH6	Stenotrophomonas_phage	6.0e-21	36.4
AZW31519.1\|3248946_3249237_-	transcriptional regulator	D0UIL8	Aggregatibacter_phage	1.2e-12	59.0
AZW31520.1\|3250150_3250447_+	hypothetical protein	NA	NA	NA	NA
AZW31521.1\|3250597_3250885_+	hypothetical protein	NA	NA	NA	NA
AZW31522.1\|3250933_3251125_+	hypothetical protein	NA	NA	NA	NA
AZW31523.1\|3251175_3251817_+	hypothetical protein	A0A248SKG7	Salicola_phage	1.1e-10	29.8
AZW31524.1\|3251794_3251980_+	hypothetical protein	NA	NA	NA	NA
AZW33495.1\|3252781_3253111_+	DUF550 domain-containing protein	A0A2K8HR09	Pseudomonas_phage	6.7e-28	65.2
AZW31525.1\|3253237_3254095_+	Band 7 protein	A0A2C9D0H9	Yersinia_phage	1.2e-49	52.5
AZW31526.1\|3254207_3254561_+	hypothetical protein	NA	NA	NA	NA
AZW31527.1\|3254542_3255424_+	hypothetical protein	U6C6B8	Ralstonia_phage	4.7e-12	51.4
AZW31528.1\|3255420_3255648_+	hypothetical protein	A0A125RNQ4	Pseudomonas_phage	2.2e-14	50.8
AZW31529.1\|3255647_3255899_+	hypothetical protein	NA	NA	NA	NA
AZW31530.1\|3256028_3257600_+	hypothetical protein	A0A291L9X3	Bordetella_phage	4.9e-28	32.3
AZW31531.1\|3257776_3257989_+	hypothetical protein	NA	NA	NA	NA
AZW31532.1\|3257978_3258347_+	hypothetical protein	W6MWX0	Pseudomonas_phage	2.8e-06	41.1
AZW31533.1\|3258336_3258588_+	hypothetical protein	NA	NA	NA	NA
AZW31534.1\|3258580_3258700_+	hypothetical protein	NA	NA	NA	NA
AZW31535.1\|3258700_3258901_+	helix-turn-helix domain-containing protein	NA	NA	NA	NA
AZW31536.1\|3258897_3259887_-\|integrase	site-specific integrase	A0A1B1P9F9	Acinetobacter_phage	2.9e-74	44.1
3263808:3263826	attR	NA	NA	NA	NA

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. CP024175

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CRISPR-Cas detection and classification

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Click the colored protein region to show detailed information

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Click the colored protein region to show detailed information

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Self-targeting detection

MGE targeting detection<

Prophage detection

Anti-CRISPR protein detection