CRISPRimmunity

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Overview of predicted results

Overview of the results

Contig_ID	Contig_def	CRISPR array number	Contig Signature genes	Self targeting spacer number	Target MGE spacer number	Prophage number	Anti-CRISPR protein number
NZ_CP040710	Flavobacteriaceae bacterium F202Z8 chromosome, complete genome	4 crisprs	RT,DEDDh,WYL,csa3,cas3	0	2	1	0

Results visualization

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CRISPR-Cas detection and classification

Crispr_ID: NZ_CP040710_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP040710_1

118906-119004

Orphan

Consensus_repeat	Method
TTCGAACATCGATTCCATACTTAC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP040710_1

>merge|NZ_CP040710|1|118906-119004|CRISPRCasFinder
TTCGAACATCGATTCCATACTTACAACGGAATTCACTTCCCAGTCCCGAAGGGGCTGATTGAATGCCGTTGCCCGTTCGAACATCGATTCCATACTCAC

>NZ_CP040710|1|1|118906-119004|CRISPRCasFinder
TTCGAACATCGATTCCATACTTAC	AACGGAATTCACTTCCCAGTCCCGAAGGGGCTGATTGAATGCCGTTGCCCG
TTCGAACATCGATTCCATACTCAC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP040710.1\|WP_138851028.1\|132428_133229_-\|pyrroline-5-carboxylate-reductase	unknown	unknown	gnl\|CDD\|223422
NZ_CP040710.1\|WP_138851012.1\|108503_109454_+\|carbon-nitrogen-hydrolase-family-protein	unknown	unknown	gnl\|CDD\|143588
NZ_CP040710.1\|WP_138851025.1\|129144_129909_-\|glutamate-5-kinase	unknown	unknown	gnl\|CDD\|239775
NZ_CP040710.1\|WP_138851026.1\|129999_131199_-\|glutamate-5-semialdehyde-dehydrogenase	unknown	unknown	gnl\|CDD\|143398
NZ_CP040710.1\|WP_138851016.1\|111533_113363_-\|WG-repeat-containing-protein	unknown	unknown	gnl\|CDD\|379719
NZ_CP040710.1\|WP_138851011.1\|107481_108387_+\|UbiA-family-prenyltransferase	unknown	unknown	gnl\|CDD\|260124
NZ_CP040710.1\|WP_138851020.1\|124142_124685_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP040710.1\|WP_138851010.1\|106532_107471_+\|mevalonate-kinase	unknown	unknown	gnl\|CDD\|224493
NZ_CP040710.1\|WP_138851019.1\|122781_124101_+\|serine-hydrolase	unknown	unknown	gnl\|CDD\|365903
NZ_CP040710.1\|WP_138851014.1\|110325_110793_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|133649
NZ_CP040710.1\|WP_138851022.1\|126183_127251_-\|M20/M25/M40-family-metallo-hydrolase	unknown	unknown	gnl\|CDD\|349902
NZ_CP040710.1\|WP_138851015.1\|110837_111530_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP040710.1\|WP_138851017.1\|113540_114470_-\|type-IX-secretion-system-membrane-protein-PorP/SprF	unknown	unknown	gnl\|CDD\|371704
NZ_CP040710.1\|WP_138851027.1\|131195_132341_-\|aminotransferase-class-III-fold-pyridoxal-phosphate-dependent-enzyme	unknown	unknown	gnl\|CDD\|227325
NZ_CP040710.1\|WP_138851013.1\|109481_110324_+\|pseudouridine-synthase	unknown	unknown	gnl\|CDD\|224108
NZ_CP040710.1\|WP_138851024.1\|128200_129148_-\|acetylornithine-carbamoyltransferase	unknown	unknown	gnl\|CDD\|235304
NZ_CP040710.1\|WP_138851009.1\|106148_106496_+\|four-helix-bundle-protein	unknown	unknown	gnl\|CDD\|183395
NZ_CP040710.1\|WP_138851023.1\|127252_128029_-\|acetylglutamate-kinase	unknown	unknown	gnl\|CDD\|239771
NZ_CP040710.1\|WP_138851008.1\|105024_106119_+\|diphosphomevalonate-decarboxylase	unknown	unknown	gnl\|CDD\|225941
NZ_CP040710.1\|WP_138851021.1\|124759_126040_-\|argininosuccinate-lyase	unknown	unknown	gnl\|CDD\|179143

Protein	Function_ID	Function_description	E-value
NZ_CP040710.1\|WP_138851028.1\|132428_133229_-\|pyrroline-5-carboxylate-reductase	gnl\|CDD\|223422	COG0345, ProC, Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism].	6.39124e-63
NZ_CP040710.1\|WP_138851012.1\|108503_109454_+\|carbon-nitrogen-hydrolase-family-protein	gnl\|CDD\|143588	cd07564, nitrilases_CHs, Nitrilases, cyanide hydratase (CH)s, and similar proteins (class 1 nitrilases). Nitrilases (nitrile aminohydrolases, EC:3.5.5.1) hydrolyze nitriles (RCN) to ammonia and the corresponding carboxylic acid. Most nitrilases prefer aromatic nitriles, some prefer arylacetonitriles and others aliphatic nitriles. This group includes the nitrilase cyanide dihydratase (CDH), which hydrolyzes inorganic cyanide (HCN) to produce formate. It also includes cyanide hydratase (CH), which hydrolyzes HCN to formamide. This group includes four Arabidopsis thaliana nitrilases (Ath)NIT1-4. AthNIT1-3 have a strong substrate preference for phenylpropionitrile (PPN) and other nitriles which may originate from the breakdown of glucosinolates. The product of PPN hydrolysis, phenylacetic acid has auxin activity. AthNIT1-3 can also convert indoacetonitrile to indole-3-acetic acid (IAA, auxin), but with a lower affinity and velocity. From their expression patterns, it has been speculated that NIT3 may produce IAA during the early stages of germination, and that NIT3 may produce IAA during embryo development and maturation. AthNIT4 has a strong substrate specificity for the nitrile, beta-cyano-L-alanine (Ala(CN)), an intermediate of cyanide detoxification. AthNIT4 has both a nitrilase activity and a nitrile hydratase (NHase) activity, which generate aspartic acid and asparagine respectively from Ala(CN). NHase catalyzes the hydration of nitriles to their corresponding amides. This subgroup belongs to a larger nitrilase superfamily comprised of belong to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 1.	7.37104e-137
NZ_CP040710.1\|WP_138851025.1\|129144_129909_-\|glutamate-5-kinase	gnl\|CDD\|239775	cd04242, AAK_G5K_ProB, AAK_G5K_ProB: Glutamate-5-kinase (G5K) catalyzes glutamate-dependent ATP cleavage; G5K transfers the terminal phosphoryl group of ATP to the gamma-carboxyl group of glutamate, in the first and controlling step of proline (and, in mammals, ornithine) biosynthesis. G5K is subject to feedback allosteric inhibition by proline or ornithine. In microorganisms and plants, proline plays an important role as an osmoprotectant and, in mammals, ornithine biosynthesis is crucial for proper ammonia detoxification, since a G5K mutation has been shown to cause human hyperammonaemia. Microbial G5K generally consists of two domains: a catalytic G5K domain and one PUA (pseudo uridine synthases and archaeosine-specific transglycosylases) domain, and some lack the PUA domain. G5K requires free Mg for activity, it is tetrameric, and it aggregates to higher forms in a proline-dependent way. G5K lacking the PUA domain remains tetrameric, active, and proline-inhibitable, but the Mg requirement and the proline-triggered aggregation are greatly diminished and abolished, respectively, and more proline is needed for inhibition. Although plant and animal G5Ks are part of a bifunctional polypeptide, delta 1-pyrroline-5-carboxylate synthetase (P5CS), composed of an N-terminal G5K (ProB) and a C-terminal glutamyl 5- phosphate reductase (G5PR; ProA); bacterial and yeast G5Ks are monofunctional single-polypeptide enzymes. In this CD, all three domain architectures are present: G5K, G5K+PUA, and G5K+G5PR.	3.95429e-94
NZ_CP040710.1\|WP_138851026.1\|129999_131199_-\|glutamate-5-semialdehyde-dehydrogenase	gnl\|CDD\|143398	cd07079, ALDH_F18-19_ProA-GPR, Gamma-glutamyl phosphate reductase (GPR), aldehyde dehydrogenase families 18 and 19. Gamma-glutamyl phosphate reductase (GPR), a L-proline biosynthetic pathway (PBP) enzyme that catalyzes the NADPH dependent reduction of L-gamma-glutamyl 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The glutamate route of the PBP involves two enzymatic steps catalyzed by gamma-glutamyl kinase (GK, EC 2.7.2.11) and GPR (EC 1.2.1.41). These enzymes are fused into the bifunctional enzyme, ProA or delta(1)-pyrroline-5-carboxylate synthetase (P5CS) in plants and animals, whereas they are separate enzymes in bacteria and yeast. In humans, the P5CS (ALDH18A1), an inner mitochondrial membrane enzyme, is essential to the de novo synthesis of the amino acids proline and arginine. Tomato (Lycopersicon esculentum) has both the prokaryotic-like polycistronic operons encoding GK and GPR (PRO1, ALDH19) and the full-length, bifunctional P5CS (PRO2, ALDH18B1).	1.35057e-156
NZ_CP040710.1\|WP_138851021.1\|124759_126040_-\|argininosuccinate-lyase	gnl\|CDD\|179143	PRK00855, PRK00855, argininosuccinate lyase; Provisional.	0
NZ_CP040710.1\|WP_138851011.1\|107481_108387_+\|UbiA-family-prenyltransferase	gnl\|CDD\|260124	cd13961, PT_UbiA_DGGGPS, Geranylgeranylglycerol-phosphate geranylgeranyltransferase. Digeranylgeranylglyceryl phosphate synthase (DGGGPS) transfers a geranylgeranyl group from geranylgeranyl diphosphate to (S)-3-O-geranylgeranylglyceryl phosphate to form (S)-2,3-di-O-geranylgeranylglyceryl phosphate, as part of the isoprenoid ether lipid biosynthesis. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways.	7.95762e-65
NZ_CP040710.1\|WP_138851010.1\|106532_107471_+\|mevalonate-kinase	gnl\|CDD\|224493	COG1577, ERG12, Mevalonate kinase [Lipid metabolism].	1.06301e-14
NZ_CP040710.1\|WP_138851019.1\|122781_124101_+\|serine-hydrolase	gnl\|CDD\|365903	pfam00144, Beta-lactamase, Beta-lactamase. This family appears to be distantly related to pfam00905 and PF00768 D-alanyl-D-alanine carboxypeptidase.	1.98498e-48
NZ_CP040710.1\|WP_138851014.1\|110325_110793_+\|hypothetical-protein	gnl\|CDD\|133649	MTH00007, COX1, cytochrome c oxidase subunit I; Validated.	0.000471116
NZ_CP040710.1\|WP_138851022.1\|126183_127251_-\|M20/M25/M40-family-metallo-hydrolase	gnl\|CDD\|349902	cd05651, M20_ArgE_DapE-like, M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases. Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are bacterial, and have been inferred by homology as being related to both ArgE and DapE.	0
NZ_CP040710.1\|WP_138851027.1\|131195_132341_-\|aminotransferase-class-III-fold-pyridoxal-phosphate-dependent-enzyme	gnl\|CDD\|227325	COG4992, ArgD, Ornithine/acetylornithine aminotransferase [Amino acid transport and metabolism].	8.935e-127
NZ_CP040710.1\|WP_138851017.1\|113540_114470_-\|type-IX-secretion-system-membrane-protein-PorP/SprF	gnl\|CDD\|371704	pfam11751, PorP_SprF, Type IX secretion system membrane protein PorP/SprF. This entry describes a protein family unique to, and greatly expanded in, the Bacteriodetes. Species in this lineage include several, such as Cytophaga hutchinsonii and Cytophaga johnsonae (Flavobacterium johnsoniae), that exhibit a poorly understood rapid gliding phenotype. Several members of this protein family are found in operons with other genes whose loss leads to a loss of the rapid gliding phenotype.	4.34318e-52
NZ_CP040710.1\|WP_138851013.1\|109481_110324_+\|pseudouridine-synthase	gnl\|CDD\|224108	COG1187, RsuA, 16S rRNA uridine-516 pseudouridylate synthase and related pseudouridylate synthases [Translation, ribosomal structure and biogenesis].	6.40239e-59
NZ_CP040710.1\|WP_138851024.1\|128200_129148_-\|acetylornithine-carbamoyltransferase	gnl\|CDD\|235304	PRK04523, PRK04523, N-acetylornithine carbamoyltransferase; Reviewed.	1.77547e-90
NZ_CP040710.1\|WP_138851009.1\|106148_106496_+\|four-helix-bundle-protein	gnl\|CDD\|183395	PRK12275, PRK12275, hypothetical protein; Reviewed.	1.4346e-32
NZ_CP040710.1\|WP_138851023.1\|127252_128029_-\|acetylglutamate-kinase	gnl\|CDD\|239771	cd04238, AAK_NAGK-like, AAK_NAGK-like: N-Acetyl-L-glutamate kinase (NAGK)-like . Included in this CD are the Escherichia coli and Pseudomonas aeruginosa type NAGKs which catalyze the phosphorylation of N-acetyl-L-glutamate (NAG) by ATP in the second step of arginine biosynthesis found in bacteria and photosynthetic organisms using either the acetylated, noncyclic (NC), or non-acetylated, cyclic (C) route of ornithine biosynthesis. Also included in this CD is a distinct group of uncharacterized (UC) bacterial and archeal NAGKs. Members of this CD belong to the Amino Acid Kinase Superfamily (AAK).	3.06941e-70
NZ_CP040710.1\|WP_138851008.1\|105024_106119_+\|diphosphomevalonate-decarboxylase	gnl\|CDD\|225941	COG3407, MVD1, Mevalonate pyrophosphate decarboxylase [Lipid metabolism].	1.38347e-61
NZ_CP040710.1\|WP_138851016.1\|111533_113363_-\|WG-repeat-containing-protein	gnl\|CDD\|379719	pfam14903, WG_beta_rep, WG containing repeat. This repeat contains an N-terminal WG repeat motif. The extent of the repeat is poorly defined. This repeat may form a beta solenoid structure (Bateman A pers. obs.).	2.50331e-05

>NZ_CP040710.1|WP_138851017.1|113540_114470_-|type-IX-secretion-system-membrane-protein-PorP/SprF
MKATHKFGTLALGVFLSFLSLQTVSAQQTAVFSEYNFNPFIINSAYAGLLPSTEATATNTGFSTFEGSPRNFSLSFHSPVSDGKIGLGAGIIRDQIGVTTSTSAFAAYSYKIFFDFKDDRPYWQIYQPGTLSFGITAGVQQYQDNLLALGIVDDPNFSQNINATIPTIGVGFLFNHARFYAGVSTPNVLGDALASDDNLQLESPVYGYFGYRFYNNLFEDFILKPSVLLKYEHGAPFQADLNLSVSYRNRFEIGGGFRTSSSANLLAGIYLLNNFRMVYHYNLALKDSPLGNTHGIMLSYRFGRGYSRS
>NZ_CP040710.1|WP_138851016.1|111533_113363_-|WG-repeat-containing-protein
MNKAVLLFFAFILLCANTLTAQELTPEMESFIANIDGTSLADIEAELDEGLRGLKAFMGFFDGGDSEGIKDYAGEEENFEEPFAIDTAVVAKAVLQFEDIGFQQNFRNGKSQLKFEKIGDNYWNTVWMEEGMAESFMPKTIYFKDGTKVTEGISDNEISFHFENPWGPIAIIDSVAVDYTVYFTAKYDSLMLTKKSKKIKYKEGLIKVKQFENNFLYVTVSDAYADGFYVNALNADGKVLNQNSSSFSPTTDDQAGDGIAEIVSLLEEIQVKLKNKDFKDTEAFKSYFLKEVSKLETAKDTDGVYHKKYYFEGNIDTVKLFIETEEKSKTVSFTAINNSGFGNIILMQDKKHNIFLDANAKELFRSEYRPIQSLGSRYYQSDSLYYHLDLEAKQLRAIDAFRVWEAPNGLAFVQATEESNFLMYDAEFKLLSDFAFEGLYTIDDTYVQGITGTDNFILDSKGTIKKLDGISDIRDPYYGRMAAKSNGKYGYLAGSGEVAIPFVYIDAGNFQDGLAIVAKETNKYGLIDTNGKVVIPLKYFGIQSFENGIVWVSTGDGHELLDKTGKVLVTAEGSSYSVSGSGLDKTYQFGDDTYDAFGRLLPKKEEIKD
>NZ_CP040710.1|WP_138851015.1|110837_111530_-|hypothetical-protein
MQKIYDYIFELSPKKLAIYLVLGPLLLFLLHTIFTIGIRNLSNNSPTQENLIRIIIIILALCLAIFVLLWLCWLRSVVYSVGDMQLGLPRKWFEIAYVALWIYIIYTVTVSIIEPLMDTHFSGADYRYLIYASKEFMSFGGIMIAYPIVCHYAARAVTAKRNNSPATFVQAIPLTLLLIFGTVLGIPFLHPHFSSRSSKNSRILTVYAIAFGLLVFIVIIGFVAAVTGLL
>NZ_CP040710.1|WP_138851014.1|110325_110793_+|hypothetical-protein
MVAGLLLREKPFVGLTVFSGLLFVLSYLRFFFFEGSTLDINIHDTYYVFSQHHLLNFTAIWIGLCAFGYWVLFKKGIRTIYGLTIAHLLFSILAIVGLIFDLGFISPDDTPNRDYQNTVYPKGMDFLVYILLFSIGQLLYFINITASTIRRERIR
>NZ_CP040710.1|WP_138851013.1|109481_110324_+|pseudouridine-synthase
MGRSESNEKGRKSGREGGNFRKKSYARGNAPIKKKQQPQKPSDPNVIRLNRYVANSGVCSRRDADIYIAAGNITVNGKPVTEMGHKVKLTDTVKFDGRLLNPVKREYVLLNKPKDFVTSGRDEHGKRTAVGLISNASKTELKPVGKLDKDTTGLILFTNDGEMTKRLNSPKNGLRKIYHIELTKPLRSADLKKIQDGLPVDEKVVKVQEVSFVDNAPKNQVGMEIYSSRNNIVRRIFEELDYEIVKLDRVVYAGLTKKDLPRGHWRYLTEQEVINLGMIQ
>NZ_CP040710.1|WP_138851012.1|108503_109454_+|carbon-nitrogen-hydrolase-family-protein
MENTLKVALAQIAPVWLNKSGTIQKIETTIQDAGKEKAELIIFGEALLPGYPFWLALTDGAAWDTKVNKELHAHYTRNSIQIEAGELDSIRQLAKEHRMAVYLGVMERAKNRGGHSLYASLVYINAEGEIQSVHRKLQPTYDERLTWAPGDGNGLRVHCLKQFTVGGLNCWENWMPLPRAALYGQGENLHIAVWPGSDHNTKDITRFIARESRSYVISVSSLMKKSDFPEDTPHVEAILKKAPETLANGGSCIAGPDGKWILEPVLHQEGIIYKTLDFNRIYEERQNFDPVGHYSRPDVTKLSVNRERQSTVEFKD
>NZ_CP040710.1|WP_138851011.1|107481_108387_+|UbiA-family-prenyltransferase
MLSRKNKLLLLKLLSLFSVVRGYNILMIALAQYLASIYILSPNLPLRQVIFDLNLFFIVLASGLVIASGYIINNFYDAEKDLINKPKKSMLDRLVGQRFKLTTYFLLNFLAVFAASYVSFRAVLFFSAYIFGIWLYSHKLKKVPFIGNFVSAILAISPFFAVFVYYKNFETVIFVHAVFLFLLILAREMIKDLENMTGDIAQNYRTIPILYGARVSKLGIAALVLLTLVPSLLLIAKFDIGHMNLYFMACVAFLLLFLVLLARSSTKAHYVWLHNILKLIIVVGVFSILLIDVNLVLNRIF
>NZ_CP040710.1|WP_138851010.1|106532_107471_+|mevalonate-kinase
MKGPLFYSKILLFGEYGIIKDSKGLSIPYNFFKGALKNDDVDSEAAKKSNSGLREFAGYLEIVQKNSPDLVSFDIAALKRDVDAGMYFDSSIPQGYGVGSSGALVAAIYDKYAKEKITVLENLTREKLLKLKMIFGKMESFFHGKSSGLDPLNSYLSLPILINSKDNIESASIPSQNTEGKGAVFLLDSGITGETAPMVQIFMEKMKNEGFRNMLKDQFIKHTDACVEDFVDGNIKSLFGNLKQLSHVVLDNFKPMIPKKFHQLWKQGIDTNEYYLKLCGSGGGGYILGFTEDIDKAKSALKDYNLEVVYNF
>NZ_CP040710.1|WP_138851009.1|106148_106496_+|four-helix-bundle-protein
MRDNVIKSKSFDFAVYIVYLYKKLVAEHKEYVMSRQLLKSGTSIGANVREAEFAVSKPDFINKMTISLKEANETDYWLDLLHKTGYLVDETHLNAKHKIEEILKLLVSIVKSSKQ
>NZ_CP040710.1|WP_138851008.1|105024_106119_+|diphosphomevalonate-decarboxylase
MREQDFEPANYVGQVDEGKVTYRSPSNIALVKYWGKKEHQIPANPSISFTLESCATTTTVSFTKLKSKAKDYSFELSFEGKPKEDFKPKIEVFFNRIEPYLPFLKEYHFIIETSNSFPHSSGIASSASGMSALALCLMHLEMELQPDLTIEYFNQKASFLARLGSGSACRSIEGPLVQWGKHETVGSTDLFGIRYPYKVHPVFQEYHDTILLVDKGQKQVSSTVGHDLMHNHPFAEQRFAQAHENLTKLRTVFENGDVETFIQIVESEALTLHAMMMTSLPYFILMKSNTLEIINTIWAFRKKTGTPVCFTLDAGANVHVLFPKAEKEKVDRFIADELVVFCENGQYICDSVGYGAKKLIDKNE
>NZ_CP040710.1|WP_138851019.1|122781_124101_+|serine-hydrolase
MQRFKILGGAALFLLTLFILMPLSENTATSIPGPEALVSKSALQETAIDQEEVRRYQLRQQQLKSTLTDYFNKAIASGEIVGAGVSIVKGDSILLSDGFGKRKINDAATVNGQTIFRLGSLSKGFAGILAASLEDEGKLDWEDKVIDYLPEFQLGDRQNTAQITLANILSHTAGTPYHSFTNLVEAGLSVKEIATHFKEVAPISEPGSLYSYQNAMFSLCQEMMHKATGKKITTSLNNRFFKPLGMHSATMDHQTISDADNVAMPHSKWRKSFRSRPLTNRYYNAVAAGGINASALDMAKWMRFLLGYRPEVMQKSVIKEAFNPIIEHKGKSKYYQRWPGHLKSYYGFGWRIHKMAASDGSDQEQTIWHHGGSVNSYRNEIAVYPEVDLGICVLLNSNSKLARRVIPDLYEIVQEVYKASPRKKAQKDDTKILAGSNFE
>NZ_CP040710.1|WP_138851020.1|124142_124685_-|hypothetical-protein
MRSILIVSILVFCFLNCKDTTKKISDKKTTGNEIVCSDSACEGIYEGPEFVNGSDVAHQFSNAMSAKVGDQLKDLFIKGAYSQVDFSKIRMSTKGMGSGQVVYQLFIPFVSVTKKCDAFTSFDHVGGWNHAPALSARKAQLGPALMPDDSLHISALKTTPEGLQEYWIQWRNKITQALCD
>NZ_CP040710.1|WP_138851021.1|124759_126040_-|argininosuccinate-lyase
MRLWDKGFSTDKKIDHFTVGDDRELDLHLAKYDVIASKAHAKMLGKIGLLTGEETDDLVRELDHIADTVEKGKFVIEDAFEDMHSKIEYVLTEKLGDTGKKIHTARSRNDQILVAMHLYLKDELTEIKSQTKVLFDLLLRLAETHKEVLLPGYTHLQIAMPSSFGLWFSAYAESLIDDLYFIDAAFKIADQNPLGSAAGYGSSFPIDRTYTTEEMDFETMKYNVVAAQMGRGKVEKATAFGMANIAATLSKLAMDICLYMSQNFNFISFPDELTTGSSIMPHKKNPDVFELVRGKCNKLQAVPNQLTLVINNLPSGYHRDLQLVKEIIVPAIQDMKACLEILTFSLEKISVNDTILDDPKYDYLFSVDTLNELVQQGIPFRDAYKKMGMEIQKGTFIPKRDITHTHEGSLGDLCLDGIRKKMHKIT
>NZ_CP040710.1|WP_138851022.1|126183_127251_-|M20/M25/M40-family-metallo-hydrolase
MTQEQLTIKALDLLKQLISIQSFSSEEDQTADAIQNWLKALDIPFERIHNNVFAKNKFWDEGKPTLLLNSHHDTVKPNKAYTKDPFHPHIEDGKLYGLGSNDAGGCLVSLLATFAHFYATENLNHNMLMVASMEEENAGEHSLRGLLPSLPKIDVAIVGEPTLMDLAIAEKGLVVFDAVVKGTPSHAAHPNDNNAIYNTIEVLEWFKNYKFKKSSEALGDVKMTVTQINAGSQHNVVPSQVDLVVDVRVNDAYTNKEIADLLKAEAPCKLQERGLKLNSSKIDKNHPLVQSGIALGRKTYGSPTLSDQAALNCQSLKLGPGDSTRSHSADEYIYVREIEEGIDLYIKILNGFLFA
>NZ_CP040710.1|WP_138851023.1|127252_128029_-|acetylglutamate-kinase
MDKVSIVKIGGNVIEDEVALGKFLDLFASLDGLKILVHGGGKMATQLASKLGIESKMVGGRRITDAETLQVITMVYAGLTNKNIVAQLQARRCNALGLSGADGDTIQAHKRPVESIDYGFAGDVDGINSTLVTKFLETGLTPVFCAMTHDGNGQLLNTNADTIAAELAIGLSNVFETILYYCFEKKGVLKNVEDDNSLVEHLNSATYRQLLADGVIADGMLPKLENCFRVLNKNVGKVCIGHPSMLASENELFTTITL
>NZ_CP040710.1|WP_138851024.1|128200_129148_-|acetylornithine-carbamoyltransferase
MKHYLSLKDIDSLPDWVSEARQLKEKPTAYKNLGSGKILCLLFFNNSLRTRLSTQKAAMNLGMDVMVMNFGSEGWQLEFEDGKVMDQGKSEHIKEAAQVVSQYCDIVAIRAFAGLKDKLTDEAEMVLNGFKKYASVPVVNMESSVGHPLQALADAITLAEQNSKPRPKIVLSWAPHPKALPHAVANSFVAMMRLQDAEFVITHPIGYELNPELTKGIPLEYDQERALENADFVYVKNWSSYTDYGKVLHQDPDWMMTSKKLGKAKFMHCLPVRRNVVVADAVLDGGQSLVIEQANNRTYAVQVVLKKILEGSNQK
>NZ_CP040710.1|WP_138851025.1|129144_129909_-|glutamate-5-kinase
MNKKRILLKIGTNTLTKETDQISRGKIEDIGRQIAKLKDDHEFIIVSSGAIAAAKQFVKLEHNGEEINVKQALAAIGQPHLMRIFQENFRELGLFTAQCLLSYSDFEKIESQENIKSTINVLVANNFIPIINENDTVSTDEIQFGDNDKLAALTAALLQVDLLLIATNTDGIYTKTSIANGMRSTILEVSDIADIKKEISSKKSSHGTGGMQSKIEAATIAQHASIETWIVNGLKDNFITDALNNISNHTKIKA
>NZ_CP040710.1|WP_138851026.1|129999_131199_-|glutamate-5-semialdehyde-dehydrogenase
MSKQLNITQRNSVLNTMAKSIATSRETLLNANQIDLESYTGEDIAMLDRLKVDQGKIDGMIISLEQLASEPDPLGIERFATTHENGMHISNKTAPFGTILIIYESRPDVTIEAAGIAFKSGNKILLKGGKESLNSNLVLVDLWHKALQENGCATDWVNYLKFDRNETQAFLERPSQKLDLIVPRGGERLIAFVKKHATCPVIVSGRGNNFVFVDSEADLQMAVDIIINAKTTKISACNALDKVLVASDLARKHHFLQHLILELQKSEVMILTDKAFASLEGTHPIADENIWHEEFLDHKIVIGQASDLEDAIAKINTYGGGHSASIITANTEKADAFMEAVDSAAVYHNASTRFTDGGQFGLGGELAISTDKLHQRGPIGLQHLVTNKWYVKGNGQLRN
>NZ_CP040710.1|WP_138851027.1|131195_132341_-|aminotransferase-class-III-fold-pyridoxal-phosphate-dependent-enzyme
MNLFDVYPLYDVTPVSAEGIVVTDDKGQEYLDFYGGHAVISIGHSHPHYVKRLKDQLDKIGFYSNAVQNPLQLELANKLGQLSDCGDYNLFLCNSGAEANENALKMASFHTGKTRVIAFKNGFHGRTSAAVAATDNEKINAPLNKQQKVTILPLNDSVAFEQEISKGDVCGVIIEAIQGVGGLDEPTTAFYQEIAKLCRQNAVVLIADEVQSGFGRSGKFFGFQHHDISPARSVRPDIISIAKGMGNGFPVGGILIHESIKASYGLLGTTFGGNHLACVATLAVLEVLEKENLMENATALGIYFSEKAAEIPQVKRVKGRGLMLGLEFDFEVAELRKKLIYDRHLFTGGAKDKHVLRILPALNITKEHIDIFFNALKAELQ
>NZ_CP040710.1|WP_138851028.1|132428_133229_-|pyrroline-5-carboxylate-reductase
MKIAIIGAGNLGLSIAKGILNSNGATTMYLTKRKPAEISEFEKYGDVSVTADNRVAVKNSDILIFAVQPSQFEAILRDTKDLLTDNHVVISTITGFSIANIEGIIGKDNHIIRSMPNTAISVGKSMTCICANGKGKSRIDLAKAIFNRMGHTLEIPEEQMQAATVICASGIAFWMRLIRATTQGAIQLGFDAKEAQELAMHTCNGAAGLLIASGSHPEAEIDRVTTPKGCTIQGLNEMEHQGLSSSLIQGIVASFEKISRIKEGQL

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Crispr_ID: NZ_CP040710_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP040710_2

578425-579020

Orphan

Consensus_repeat	Method
CTTCANACTTCACACTTCNNAC	CRT

9 spacers

The CRISPR arrays of NZ_CP040710_2

>merge|NZ_CP040710|2|578425-579020|CRT
CCTCAAACCTCAAACCTCAAACCTCAAACCTCAAACCTCAAACCTCAAACCTCAAACCTCAAACCTCAAACTTCAAACTTCAAACTTCGCGCTTCAAACTTCACACTTCAAACTTCACGCTTCAAACTTCTCACCTTGCACTTCGAACCTCGTACTTCGCACTTCAAACTTCACGCTTCACACTCCGCACTTCAAACTTCCCACCTCGCACCACAAACTTCAAATTTTGCGCTTCGCACATAACACTTCGAGCTTCAAACTTCACGCTTCAAACTTCTCACCTCGCACCTCGCACTTTGAGCCTCGTACTTCAAACTTCACACCTAAAATATCACACTTCCCGCTTCGCGCTTCGTGCTTCAAACTTCTCACTTCGCACATCGCACTTCGAGCTTCTCACCTCGCACCTCGCACTTCAAACTTCACACTTCAAGCTTCAAACTTCAGACATCACATATCACACTTCCCACTTCCCACTTCCCACTTCGCGCTTCGCGCTTCGTGCTTCGTGCTTCAAACTTCTCACCTCGCACTTCAAACTTCGCGCTTCAAACTTCTCACCTCGCACTTCGAGCCTCGTACTTCAAACTTCTCAC

>NZ_CP040710|2|1|578425-579020|CRT
CCTCAAACCTCAAACCTCAAAC	CTCAAACCTCAAACCTCAAACCTCAAACCTCAAACCTCAAACCTCAAACTTCAAACTTCAAACTTCGCG
CTTCAAACTTCACACTTCAAAC	TTCACGCTTCAAACTTCTCACCTTGCACTTCGAACCTCGTACTTCGCACTTCAAACTTCACG
CTTCACACTCCGCACTTCAAAC	TTCCCACCTCGCACCACAAACTTCAAATTTTGCGCTTCGCACATAACACTTCGAG
CTTCAAACTTCACGCTTCAAAC	TTCTCACCTCGCACCTCGCACTTTGAGCCTCGTA
CTTCAAACTTCACACCTAAAAT	ATCACACTTCCCGCTTCGCGCTTCGTG
CTTCAAACTTCTCACTTCGCAC	ATCGCACTTCGAGCTTCTCACCTCGCACCTCGCA
CTTCAAACTTCACACTTCAAGC	TTCAAACTTCAGACATCACATATCACACTTCCCA
CTTCCCACTTCCCACTTCGCGC	TTCGCGCTTCGTGCTTCGTGCTTCAAACTTCTCA
CCTCGCACTTCAAACTTCGCGC	TTCAAACTTCTCACCTCGCACTTCGAG
CCTCGTACTTCAAACTTCTCAC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP040710.1\|WP_138851366.1\|586954_587416_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP040710.1\|WP_138851363.1\|582306_583467_+\|serine-hydrolase	unknown	unknown	gnl\|CDD\|365903
NZ_CP040710.1\|WP_138851367.1\|587538_589041_+\|M20/M25/M40-family-metallo-hydrolase	unknown	unknown	gnl\|CDD\|349927
NZ_CP040710.1\|WP_138851369.1\|590517_591366_+\|prephenate-dehydratase	unknown	unknown	gnl\|CDD\|270349
NZ_CP040710.1\|WP_138851357.1\|570706_571537_-\|IS3-family-transposase	unknown	unknown	gnl\|CDD\|222853
NZ_CP040710.1\|WP_138851364.1\|583473_584466_+\|helix-turn-helix-transcriptional-regulator	unknown	unknown	gnl\|CDD\|197715
NZ_CP040710.1\|WP_138851361.1\|577087_578041_+\|methylenetetrahydrofolate-reductase-[NAD(P)H]	unknown	unknown	gnl\|CDD\|273212
NZ_CP040710.1\|WP_138851355.1\|568982_569543_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP040710.1\|WP_138851370.1\|591362_592514_+\|aminotransferase-class-I/II-fold-pyridoxal-phosphate-dependent-enzyme	unknown	unknown	gnl\|CDD\|181749
NZ_CP040710.1\|WP_138851360.1\|573599_576818_+\|dihydropteroate-synthase	unknown	unknown	gnl\|CDD\|236539
NZ_CP040710.1\|WP_138851368.1\|589293_590187_-\|gliding-motility-associated-ABC-transporter-ATP-binding-subunit-GldA	unknown	unknown	gnl\|CDD\|132561
NZ_CP040710.1\|WP_138851352.1\|566371_567235_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP040710.1\|WP_138851359.1\|572548_573580_+\|5-methyltetrahydrofolate--homocysteine-methyltransferase	unknown	unknown	gnl\|CDD\|236539
NZ_CP040710.1\|WP_138851356.1\|569665_570637_-\|RNA-directed-DNA-polymerase	RT	pfam00078_RT_CAS-I:CAS-III	gnl\|CDD\|239569
NZ_CP040710.1\|WP_138851353.1\|567231_567645_-\|MarR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224759
NZ_CP040710.1\|WP_138854590.1\|580378_581143_+\|DUF2807-domain-containing-protein	unknown	unknown	gnl\|CDD\|371327
NZ_CP040710.1\|WP_138851365.1\|584546_586874_+\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|379720
NZ_CP040710.1\|WP_138851358.1\|571560_571836_-\|transposase	unknown	unknown	gnl\|CDD\|366690
NZ_CP040710.1\|WP_138851354.1\|568057_568996_-\|TIR-domain-containing-protein	unknown	unknown	gnl\|CDD\|379328
NZ_CP040710.1\|WP_138851362.1\|579172_580267_+\|acyloxyacyl-hydrolase	unknown	unknown	gnl\|CDD\|378181

Protein	Function_ID	Function_description	E-value
NZ_CP040710.1\|WP_138851363.1\|582306_583467_+\|serine-hydrolase	gnl\|CDD\|365903	pfam00144, Beta-lactamase, Beta-lactamase. This family appears to be distantly related to pfam00905 and PF00768 D-alanyl-D-alanine carboxypeptidase.	4.85202e-61
NZ_CP040710.1\|WP_138851369.1\|590517_591366_+\|prephenate-dehydratase	gnl\|CDD\|270349	cd13631, PBP2_Ct-PDT_like, Catalytic domain of prephenate dehydratase from Chlorobium tepidum and similar proteins, subgroup 2; the type 2 periplasmic binding protein fold. Prephenate dehydratase (PDT, EC:4.2.1.51) converts prephenate to phenylpyruvate through dehydration and decarboxylation reactions. PDT plays a key role in the biosynthesis of L-Phe in organisms that utilize the shikimate pathway. PDT is allosterically regulated by L-Phe and other amino acids. The catalytic PDT domain consists of two similar subdomains with a cleft in between, which hosts the highly conserved active site. In gram-postive bacteria and archaea, PDT is a monofunctional enzyme, consisting of a catalytic domain (PDT domain) and a regulatory domain (ACT) (aspartokinase, chorismate mustase domain). In gram-negative bacteria, PDT exists as fusion protein with chorismate mutase (CM), forming a bifunctional enzyme, P-protein (PheA). The CM in the P-protein catalyzes the pericycle isomerization of chorismate to prephenate that serves as a substrate for PDT. The CM and PDT are essentail enzymes for the biosynthesis of aromatic amino acids in microorganisms but are not found in humans. Thus, both CM and PDT can potentially serve as drug targets against microbial pathogens. The PDT domain has the same structural fold as the type 2 periplasmic binding proteins (PBP2), many of which 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.	4.83157e-91
NZ_CP040710.1\|WP_138851357.1\|570706_571537_-\|IS3-family-transposase	gnl\|CDD\|222853	PHA02517, PHA02517, putative transposase OrfB; Reviewed.	1.06123e-36
NZ_CP040710.1\|WP_138851364.1\|583473_584466_+\|helix-turn-helix-transcriptional-regulator	gnl\|CDD\|197715	smart00421, HTH_LUXR, helix_turn_helix, Lux Regulon. lux regulon (activates the bioluminescence operon.	5.55217e-18
NZ_CP040710.1\|WP_138851361.1\|577087_578041_+\|methylenetetrahydrofolate-reductase-[NAD(P)H]	gnl\|CDD\|273212	TIGR00676, 510-methylenetetrahydrofolate_reductase., 5,10-methylenetetrahydrofolate reductase, prokaryotic form. The enzyme activities methylenetetrahydrofolate reductase (EC 1.5.1.20) and 5,10-methylenetetrahydrofolate reductase (FADH) (EC 1.7.99.5) differ in that 1.5.1.20 (assigned in many eukaryotes) is defined to use NADP+ as an acceptor, while 1.7.99.5 (assigned in many bacteria) is flexible with respect to the acceptor; both convert 5-methyltetrahydrofolate to 5,10-methylenetetrahydrofolate. From a larger set of proteins assigned as 1.5.1.20 and 1.7.99.5, this model describes the subset of proteins found in bacteria, and currently designated 1.7.99.5. This protein is an FAD-containing flavoprotein. [Amino acid biosynthesis, Aspartate family].	1.8434e-103
NZ_CP040710.1\|WP_138851370.1\|591362_592514_+\|aminotransferase-class-I/II-fold-pyridoxal-phosphate-dependent-enzyme	gnl\|CDD\|181749	PRK09276, PRK09276, LL-diaminopimelate aminotransferase; Provisional.	2.20565e-147
NZ_CP040710.1\|WP_138851360.1\|573599_576818_+\|dihydropteroate-synthase	gnl\|CDD\|236539	PRK09490, metH, B12-dependent methionine synthase; Provisional.	0
NZ_CP040710.1\|WP_138851368.1\|589293_590187_-\|gliding-motility-associated-ABC-transporter-ATP-binding-subunit-GldA	gnl\|CDD\|132561	TIGR03522, GldA_ABC_ATP, gliding motility-associated ABC transporter ATP-binding subunit GldA. Members of this protein family are exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides). GldA is an ABC transporter ATP-binding protein (pfam00005) linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Flavobacterium johnsoniae and Cytophaga hutchinsonii. Knockouts of GldA abolish the gliding phenotype. Gliding motility appears closely linked to chitin utilization in the model species Flavobacterium johnsoniae. Bacteroidetes with members of this protein family appear to have all of the genes associated with gliding motility.	1.63072e-153
NZ_CP040710.1\|WP_138851353.1\|567231_567645_-\|MarR-family-transcriptional-regulator	gnl\|CDD\|224759	COG1846, MarR, Transcriptional regulators [Transcription].	9.37213e-13
NZ_CP040710.1\|WP_138851359.1\|572548_573580_+\|5-methyltetrahydrofolate--homocysteine-methyltransferase	gnl\|CDD\|236539	PRK09490, metH, B12-dependent methionine synthase; Provisional.	0
NZ_CP040710.1\|WP_138851356.1\|569665_570637_-\|RNA-directed-DNA-polymerase	gnl\|CDD\|239569	cd03487, RT_Bac_retron_II, RT_Bac_retron_II: Reverse transcriptases (RTs) in bacterial retrotransposons or retrons. The polymerase reaction of this enzyme leads to the production of a unique RNA-DNA complex called msDNA (multicopy single-stranded (ss)DNA) in which a small ssDNA branches out from a small ssRNA molecule via a 2'-5'phosphodiester linkage. Bacterial retron RTs produce cDNA corresponding to only a small portion of the retron genome.	5.25747e-74
NZ_CP040710.1\|WP_138851365.1\|584546_586874_+\|TonB-dependent-receptor	gnl\|CDD\|379720	pfam14905, OMP_b-brl_3, Outer membrane protein beta-barrel family. This family includes proteins annotated as TonB dependent receptors. But it is also likely to contain other membrane beta barrel proteins of other functions.	2.99161e-37
NZ_CP040710.1\|WP_138854590.1\|580378_581143_+\|DUF2807-domain-containing-protein	gnl\|CDD\|371327	pfam10988, DUF2807, Putative auto-transporter adhesin, head GIN domain. This bacterial family of proteins shows structural similarity to other pectin lyase families. Although structures from this family align with acetyl-transferases, there is no conservation of catalytic residues found. It is likely that the function is one of cell-adhesion. In Structure 3jx8, it is interesting to note that the sequence of contains several well defined sequence repeats, centred around GSG motifs defining the tight beta turn between the two sheets of the super-helix; there are 8 such repeats in the C-terminal half of the protein, which could be grouped into 4 repeats of two. It seems likely that this family belongs to the superfamily of trimeric auto-transporter adhesins (TAAs), which are important virulence factors in Gram-negative pathogens. In the case of Parabacteroides distasonis, which is a component of the normal distal human gut microbiota, TAA-like complexes probably modulate adherence to the host (information derived from TOPSAN).	3.02932e-43
NZ_CP040710.1\|WP_138851367.1\|587538_589041_+\|M20/M25/M40-family-metallo-hydrolase	gnl\|CDD\|349927	cd05678, M20_dipept_like, uncharacterized M20 dipeptidase. Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.	0
NZ_CP040710.1\|WP_138851358.1\|571560_571836_-\|transposase	gnl\|CDD\|366690	pfam01527, HTH_Tnp_1, Transposase. Transposase proteins are necessary for efficient DNA transposition. This family consists of various E. coli insertion elements and other bacterial transposases some of which are members of the IS3 family.	0.000976401
NZ_CP040710.1\|WP_138851354.1\|568057_568996_-\|TIR-domain-containing-protein	gnl\|CDD\|379328	pfam13676, TIR_2, TIR domain. This is a family of bacterial Toll-like receptors.	3.24716e-20
NZ_CP040710.1\|WP_138851362.1\|579172_580267_+\|acyloxyacyl-hydrolase	gnl\|CDD\|378181	pfam09411, PagL, Lipid A 3-O-deacylase (PagL). PagL is an outer membrane protein with lipid A 3-O-deacylase activity. It forms an 8 stranded beta barrel structure.	1.42789e-17

>NZ_CP040710.1|WP_138851361.1|577087_578041_+|methylenetetrahydrofolate-reductase-[NAD(P)H]
MKITDHIKEAKGETLFSFEIIPPVKGHKIQELYDNIDPLMEFKPPFIDVTTSREEYVYIDRNGLLDKKLTRMRPGTVGICASIKHKYDVDTVPHVLCGGFTKEETEYVLVDCQYLGIDNVMALRGDAMREEKYFQPAEGGHEYAIGLVEQLNDLNCGNYLHDTMEGTNCADFCIGVAGYPEKHLEAPSLQSDLKRLKEKVDAGAHYIVTQMFFDNKKYFEFVDAAKAMGIDVPIIPGIKPIAVKRHLNLLPQVFRIDIPQDLIDAVDGCENNKAVRQVGIEWAIQQSKELKEAGVPVLHYYSMGKSDNIHAIASALF
>NZ_CP040710.1|WP_138851360.1|573599_576818_+|dihydropteroate-synthase
MKEDLNISKEAFTAPPSGAGGARYLKLSGLEPLVVTPETNFVNVGERTNVAGSKKFLRLIKERKFEEALDVARDQVEGGAQIIDINMDDGLIDGKEAMVKFLNLVIAEPDIARVPIMIDSSKWEIIEAGLQVVQGKCVVNSISLKEGEKEFIHHAKLIKRYGAAVIVMAFDEVGQADNYDRRIEIAKRSYDILVDEVGFPPEDIIFDLNIFPVATGMDEHKLNAIDFIKATKWVRENLPHCSVSGGVSNVSFSFRGNNPVREAMHSVFLYHAIKAGMNMGIVNPTMLEVYDDIPKDLLEHVEDVMLNRRDDATERLLDFAESVVGTAKESKVDLSWREEPLQDRITRALVKGIDQYIVEDVEEARQAADKPIEVIEGNLMTGMNVVGDLFGSGKMFLPQVVKSARVMKKAVAHLLPYIEEEKLKSAPQPPKGEQHWETANPVLYGLLKEHAKRMRNEPTPAETMLWNALSGKNLGGYKFRRQHIIGEYIADFICLKHNLIVEVDGLIHQLPENKKSDTERTEWLENLGYRVIRFTNNQVLTNLENVLEEIHQALSAPPSGAGGAAGKILMATVKGDVHDIGKNIVSVVLACNNYEIVDLGVMVPPEKIIAAAIEHNVDVIGLSGLITPSLDEMVHLAKEMERKNFSVPLLIGGATTSKAHTAVKIDPQYSQAVVHVNDASRAVTVVGDLLQKETSDTYKEKIKEDYDVFREKFLKRAVQKDYKTLAEARKNKFQIDWDTTKIVKPNELGIQVIEDMDLEKLVPFIDWTPFFRSWELHGKYPDILTDDVVGTQATELFADAQKMLKEIVAEKKLKAKGIFGLFPANTVNEDDIEVDLSPYLGEMPKGQAGPLKDNNSGDNSTSLGGGREGAIFRTLRQQLQRREGVPDYALADFIAPKASGKEDYIGCFCVSTGFGTAELAAQYEKELDDYSSILIKALADRLAEAFAEYLHKEVRMNHWGYAADEDLSSEELINESYKGIRPAPGYPACPDHLEKLTIWEMLQVEEKIGVKLTESLAMWPAASVSGYYFGNPEARYFGLGKIKEDQVADFAKRKGIPVEEATKWLAPNIADD
>NZ_CP040710.1|WP_138851359.1|572548_573580_+|5-methyltetrahydrofolate--homocysteine-methyltransferase
MRAIREVLKERILVLDGAMGTMLQRYKFQEEDFRGERFKDWEHPLQGNNDLLSLTQPEAIAEVHAKYFAAGADIVETNTFSGTTIAMADYHMEDLVYELNYESAKIAKRVADEFTAKEPHKPRFVAGSIGPTNKTASMSPDVNDPGYRAVSFDELRIAYKQQAEALLDGGSDLLLVETIFDTLNAKAALFAIEEVKEERGIDVPIMVSGTITDASGRTLSGQTAEAFLISISHIPILSVGFNCALGANQLVPHLEVISKRSEHAVSAHPNAGLPNAFGEYDETPEQMAAQIKEYVEKGLVNIVGGCCGTTPPHISAIAELVKDYKPRSFGPMAPTGEMNSLVE
>NZ_CP040710.1|WP_138851358.1|571560_571836_-|transposase
MTRRKFTPKFKTKVVLEALKERETAQELAQRFEISPQQVNLWKREFLAQAESVFIKGPKSAKSEAEEKEDHLLKVIGKQKVELDFLKNALR
>NZ_CP040710.1|WP_138851357.1|570706_571537_-|IS3-family-transposase
MISKDHSNLSIAKQSELLKLHRSGLYYKPKGESELNLELMRLMDEHYADHYFKGAKRMHTWLTMDKGYKVNQKRIDRLYYRVMGLSAIMPGKHTSRRNKAHKVYPYLLRNLKVYRPNQVWATDITYIPMRKGFMYLVAIIDLHSRYVLNWSVSNTMDAQWCKETLEVAMTKHGKPEIVNTDQGSQFTSEVFTHLVLSNDIKLSMDGKGRAIDNVFIERLWRSVKYESIYLNPPDSGIDLYEQLNGYFDYYNNRRRHQGIDNQIPFKRYLKQQQKAA
>NZ_CP040710.1|WP_138851356.1|569665_570637_-|RNA-directed-DNA-polymerase
MIKNENIRLNMLGLPIIQSINDFSHITHLSKYTLYQLSEKSDFHYKKFPLKKKAGGTRTICQPSKNLKGLQSWILVNILNKLKVSDSCKGFEKGSSIGDNARPHINANCILTLDLSDFFGTVSDIQVYNVFKSIGYNNLISTMMTNICTSDGSLPQGSPSSPKLANLVSWKLDKRIQGFVGKRGITYTRYADDLSFSGLHPANTVQVLPVVKSIIQDEGFRINPRKTRVSGASRAKIITGLVISNNRFGIGQTKYRILRAKIFHLTKPKEQNNIDLLNEVNGWIAYLKSVDKLRFNKVFKYVSKLKKEHPKTLINQMTIANIV
>NZ_CP040710.1|WP_138851355.1|568982_569543_-|hypothetical-protein
MTQETKDYIETWTKKISSHTGNDLATLFDKYTALFTLYNRLYNESFKQMRDNNQLSKTRYSDFEKATNLVVDFNSANEIIDRLKKRDNFDDIATIADLIRKDIFHINLANGMSQKDIDLELMQNLENKEPIIKAQGAVSTIYNVRCNMQHGEKHFEEHQRMLLEPLIRILDSIVELQIEKLTNEKS
>NZ_CP040710.1|WP_138851354.1|568057_568996_-|TIR-domain-containing-protein
MKNPKAFISYAWESDEIKLWVKHLATELRTDGIDAKLDQWEIVPGDQMPHFMEKSVRENDYVLIVCTPKYKSKSENRVGGVGYEGDIMTAEVLQSSNHRKFIPILKEGTKDNAIPSWLQGKYYVNLTNEKHYVNNYSDLTTTLLNTRETAPALSPTTRREVVKNTYIPKDKKINSKDEPIRIKGILISEITQPKNDGTKGSALYKIPFELNRTPSYEWADLFVNAWNRPSKFTSMHRSGIASTYGNKVILDGTTIEEVEKYHKDTLKLAVHTANQQLKRINLQKEQEAERERLERERHTKNIEDIGGRISFD
>NZ_CP040710.1|WP_138851353.1|567231_567645_-|MarR-family-transcriptional-regulator
MQNNGSYHPKECISSKVMRLNRIIANIFRKYLKPFGITNSQLSILFVLNYRNDLNQRKLSDLTILEKSSLNRNLTRLQQSDLISKAKFPYIRITEKGRQLVNNIIPEWEKAMAECNLLIEKEGINALNLLMDKVLKK
>NZ_CP040710.1|WP_138851352.1|566371_567235_-|hypothetical-protein
MNPQENIQLTLEYLSIIVLGGLVIFQLLHFIIGSWRFWKNDKFRIFKTISVGIFWVIYGSFFVTIVTDMTSYYHAVPYVLCGLYLPSIIALFLIAVSKKFKDFVDQTSLRWTIQSVGGPARMIVGIIFLFWFFAGRLPGVVAWVAGPGDWISGYITFYAVKRLRIFKKTADLKTKHWSISDLKKNLGERMPIIPIYKLNRNLNIAIAFVAFGILDFILAPASTALSIFNGNIPEEMGRVPLTLIPLVLVPQVLLLEIFAMRQLIGLKKIIRNKKKPVPNIGNRCARP
>NZ_CP040710.1|WP_138851362.1|579172_580267_+|acyloxyacyl-hydrolase
MSQKVFFLFLFVVGFCFSQEEKAKRHYAFDANAYFGSIILHNPDISHLINEHPAGFMLGYNRKTFGEQEWQQGYNYPDLGASFIYHNPNNATLGENYGLYAHFNFYFLKRNLQFRIGQGIAYATNPYDRDTNFRNNAYGSTFLSSTFLMLNYHKERIFRRLGFRAGISLVHYSNANVRAPNTSTNTLALNLGLTYSLSEETPEYIEREKQKVTEPIRYNLAFRTGINESDNVGAGQFPFYIFSGYTDKRLSRKSAIQLGTDVFFSNFLKELIRYQSISFPENNVAADTDFKRVGVFVGHELFINKLSIGTQLGYYVYYPFDFEGRVYNRFSLKRYFGDKVFGVISLKSHGAAAEAVEFGVGVRL
>NZ_CP040710.1|WP_138854590.1|580378_581143_+|DUF2807-domain-containing-protein
MCSHFWKVLLALPILLVQTACSSESAPDCFQRAGEIERQEIALPDFSKITVFENVSLVLQQGDVQKVEIETGENLRNEVTATVEGDRLLLRDTNDCNFVRSYGTTIIYVTSPAINEIRSSTGRRISSEGVLAYPNLTLFSESFLNPESETTDGLFDLAVDTENLTVIVNGITYFKLRGNTENLNLTIAAGDSRIEAENLSAESVTLNHRGSNDMFVNPQEAINGVIRGTGDVISSNRPDLVEVEELYKGKLVFK
>NZ_CP040710.1|WP_138851363.1|582306_583467_+|serine-hydrolase
MNPITKYLKNLFASKRVLGEDANLKGLAKAEALLQNLVNDNKVPGISISVLKKGETLLQKGYGYADMEAKIPVDIQKTIFRIASVSKPIAATALAHMVAEGRIDLDASFYDYVPYYPKKKWDFTIRQLASHTAGIRGYQGTEYGLNIPYSIKESIEIFKDDELLFEPGTDYLYNSYDWVLISLAMQEASGIPFEAYVKQKVLQPLGMEATFAPVCPAEPVEALSKVANSQLNVQQDKIKHRLTSFYSKNRSGFRKAIPVNNYYKLAGGGYLSTSADIARFGQAFLDGRILNEGLFEQFLTATTVNGKSTYYGLGWQVSEDKNGRPFYGHVGNGVGGYSNFFVYPEQQMVFAILVNCTNPDVQDTLDALVDCLLKTVENNYLGTSTT
>NZ_CP040710.1|WP_138851364.1|583473_584466_+|helix-turn-helix-transcriptional-regulator
MLRTIIFLTLVFFGGQLYGQSAISGYVPQEDGLPTPQEIYLSQIDLEDLPEYSKAKKVSKTTIAENGFFQFNKESISDTDAIYRLHYMQIGNSKDDSLVVDHLFMLSNRDSIHFKKSVVPFSNYTTTNLGDKEWQRLRQFEHRIREGYYKKEDSLSYAYVGSMKTYAKDSLRILMVKLIGIKQLDHKRLLEKDIAKNPEYYVALLKELKESDIERADYLFLENKLAFLTTEAAERKYATSTIINWLLGFGVVALLFLLFRRRRTNSTAALSDLSRQERNIQGIILEGKSNKEIANELFISLSTVKTHITNIYGKLQVSNRQELLRKMQNS
>NZ_CP040710.1|WP_138851365.1|584546_586874_+|TonB-dependent-receptor
MRGLWFSLCSLVGTLVCAQNTYDISGNITDDQNQLVSIGDALLFPIANDTLVAYTSIIDGAFLMPNIPEGSYRLRVSCLGFEDVEQNLVVTGNLVVSIQLVAHTTNLEAVEVVAARPVTTNENGNLKIDVTNPVFSAIPDPMELLSRLPNLQVSPDWASVTILGKGTPLVYLGNQRISMEEFNALTVDDISTIEIIRNPSAKYEANGRAVLLITRKSNLSEGFRLNLSETLSFKRNFNNYSNINGSYHSGKVTLKANFAYNDLLQWESHQFEFGIPDADIFSDYLILVDRNDRIELNGGGGLFYQINDTDYFSANTTFRSQTNDVIIATDTFLRQGSEQDDILTETNNQNNKRFGSANLNYARKLNTKTNVFAGIQYSSYEQRLDTEIANNYNTTAFDISQLREQRYRINVLTYRMDFDKKLTNDLKWEFGANNSIARANAQTNIQFLETASNLEIDYDYSESTIAAYTTLSGELGEKVQFNGGLRVENNTVKGEEEAENIPLVNRRSTNLFPKANLTVELDSTKHLTFNYGKSIDRPNYSSASSIQIFFNPFLEGEGNVNLLPTVTEDLSAVFQFGNNSLSIEYFKRKNPIYYTIGYTIGEERAVFSLKNLERESGLDINFNFPITKGIWTSTNAVSLSRRRIQDATASGKPVKPYVYFYTDHQFKIGKETTVSFGAWGLTKRSEGIFERNAMVVWNAALTKTFFKNWNCALRFNDITRAMNYEESYAINGVVADGVYFVDAQEVALSIKYTFGNSKDHDYNNKEVDENLDRIK
>NZ_CP040710.1|WP_138851366.1|586954_587416_+|hypothetical-protein
MRKLFFGIVLFSLCVSSLEAQEITMFPGSFGYEFYQDKDKLTYKEINKIMNESTVAEMHWQKSKKQLIGGMIAGAANFGSAIWFLVEDRDGNNVVAPAITFLGTGLVSSIFYKCAMKNKKKAILEYNDALGSKTGFRLEPTSNQYGVGLALKF
>NZ_CP040710.1|WP_138851367.1|587538_589041_+|M20/M25/M40-family-metallo-hydrolase
MKYFPYFLFTCIPMLLIGQQVQKLDELSSAYAKQSFPMLQELLSIPNDAFFPKDIEKNISWCESNFRARGFTLERLATETVPLLLAERKHPKAKQTVLIYLQLDGQPVDSTRWFQGNPYTPVLKEKVADAWQELPWDNIADYDDDWRVFARSASDAKGPVAMFLTALDAIAAEGIVPNFNIKVIMDFEEELGSPQLPKAVLENQEALKADMLIIFDGPRHISNKPTLTFGARGIATITLTTYGPVVPQHSGHFGNYAPNPALRLAKLLASMKDEGGRVTIPGFYDGISIDTDTEKILKSVPDNESEIKNRLQIAATDEVGRYYQEAIQYPSLNIRGMQSGWIDEKVRTIIPGWARAEIDVRLVLESDPERLINLIRDHIENEGYLVIDREPTKEERLAHAKIASFTSEISYQSFRTDFDSEVGIWLTNALENAFGEEPIRIRMSGGSIPISPFVNTLGIPAVTVPTVNRDNNQHSPNENLRLGNYREGIKTMIAILGEKL
>NZ_CP040710.1|WP_138851368.1|589293_590187_-|gliding-motility-associated-ABC-transporter-ATP-binding-subunit-GldA
MSITVKNITKTFGTQKALDNVSFALHKGEIVGFLGPNGAGKSTMMKILTTYHQADVGEAHVNSFDVRNDIKNVQKSIGYLPEHNPLYLDMYVKEYLGFNADVYKTERSRIPEVIEQTGLTPEAHKKIGQLSKGYRQRVGLAAALLHDPEVLILDEPTTGLDPNQLLEIRKLIREIGKEKTILLSTHIMKEVEAVCDRVLIINKGILVADRKLADLREADEQIIEVEFDYRVEEAFLYKLPHVTHVKNVAGFVYEITFNTSKDMRSSVFDFAHDNQLKTLQLSSKNKNLESLFSELTQ
>NZ_CP040710.1|WP_138851369.1|590517_591366_+|prephenate-dehydratase
MRLKVAIQGIKGSNHHQVAREYFDDDTELLECMSFDALVESLLNGTADKGVMAIENSIAGSIIPNYNLIYHNKLHVIGEHYLHINHNLMVLKGSAIADLSEVRSHPMALLQCKEFFRNYPQIKLVEDADTAEPAKRIQEEQLAHVAAIAPQVAAELYGLDIVAPNIQTIQNNATRFIIVQTKNKLVAQMDEKFSEDGVNKASVRFITDHKRGSLAAMLNVMSDCNLNLTKIQSLPIIETPWKYAFFVDITFEGFANFEKAKSLLNIMSEDFKVLGEYKNARL
>NZ_CP040710.1|WP_138851370.1|591362_592514_+|aminotransferase-class-I/II-fold-pyridoxal-phosphate-dependent-enzyme
MIRTADRLHTVEEYYFSKKLREVRGLLADGRPIINMGIGSPDLAPSTAIIESIQNAVTDTGAHQYQSYQGLPQLRQAIADFYSLRFGVTADPNTEILPLMGSKEGIMHISMAFLNQGDVVLIPNPGYPTYSAVTKLVGAVPKFYNLSSDNDWFPDLEALQLKDLSKVKIMWVGYPHMPTGATADEAQFERLIAFAEENDILLVNDNPYSFVLNERPKSILVVPGAKKNVLELNSLSKTFNMAGWRVGMVLGSSEHINAILKVKSNMDSGMFYGIQKGAITALKSSQQWFADLNKVYSSRRELIFKLADKLNCTYDKNAVGLFVWAKLPEGSKSAEDVIDEVLYDKNIFITPGTIFGSNGEGYIRFSLCVPEEKIKEAIGRFEK

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Crispr_ID: NZ_CP040710_3

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP040710_3

2594845-2594965

Orphan

Consensus_repeat	Method
GTCGTCGTCGGAGACGAGGCGGGCACCTCCCC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP040710_3

>merge|NZ_CP040710|3|2594845-2594965|CRISPRCasFinder
GTCGTCGTCGGAGACGAGGCGGGCACCTCCCCACAAGGGGAGGGTTTTCGAATTCCTTTTCAAATCTTTCTGGCTTCCTCTCCTCCAAAGTCGTCGTCGGAGACAAGGCGGGCACCTCCCC

>NZ_CP040710|3|2|2594845-2594965|CRISPRCasFinder
GTCGTCGTCGGAGACGAGGCGGGCACCTCCCC	ACAAGGGGAGGGTTTTCGAATTCCTTTTCAAATCTTTCTGGCTTCCTCTCCTCCAAA
GTCGTCGTCGGAGACAAGGCGGGCACCTCCCC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP040710.1\|WP_138852903.1\|2581892_2582525_-\|hemolysin-III-family-protein	unknown	unknown	gnl\|CDD\|185044
NZ_CP040710.1\|WP_138852907.1\|2593749_2594094_+\|50S-ribosomal-protein-L20	unknown	unknown	gnl\|CDD\|179959
NZ_CP040710.1\|WP_138852908.1\|2594356_2594779_-\|YjbQ-family-protein	unknown	unknown	gnl\|CDD\|376651
NZ_CP040710.1\|WP_138852917.1\|2606118_2606718_+\|outer-membrane-beta-barrel-protein	unknown	unknown	gnl\|CDD\|372635
NZ_CP040710.1\|WP_138852910.1\|2596136_2597393_-\|asparagine-synthetase-B	unknown	unknown	unknown
NZ_CP040710.1\|WP_138854688.1\|2599474_2600428_-\|acetyl-CoA-carboxylase-carboxyltransferase-subunit-alpha	unknown	unknown	gnl\|CDD\|235580
NZ_CP040710.1\|WP_138852914.1\|2602465_2603596_-\|tRNA-guanosine(34)-transglycosylase-Tgt	unknown	unknown	gnl\|CDD\|376596
NZ_CP040710.1\|WP_138852904.1\|2582651_2583992_-\|amidohydrolase-family-protein	unknown	unknown	gnl\|CDD\|238624
NZ_CP040710.1\|WP_138852901.1\|2580231_2580657_+\|DUF4268-domain-containing-protein	unknown	unknown	gnl\|CDD\|379461
NZ_CP040710.1\|WP_138854687.1\|2590697_2592635_+\|threonine--tRNA-ligase	unknown	unknown	gnl\|CDD\|234752
NZ_CP040710.1\|WP_138852915.1\|2604135_2604981_+\|transketolase	unknown	unknown	gnl\|CDD\|238970
NZ_CP040710.1\|WP_138852902.1\|2580967_2581888_+\|ThuA-domain-containing-protein	unknown	unknown	gnl\|CDD\|377643
NZ_CP040710.1\|WP_138852906.1\|2593429_2593627_+\|50S-ribosomal-protein-L35	unknown	unknown	gnl\|CDD\|234676
NZ_CP040710.1\|WP_138852911.1\|2597759_2599307_-\|replicative-DNA-helicase	unknown	unknown	gnl\|CDD\|273206
NZ_CP040710.1\|WP_138852912.1\|2600470_2601376_-\|EamA-family-transporter	unknown	unknown	gnl\|CDD\|273359
NZ_CP040710.1\|WP_138852900.1\|2579560_2580232_+\|ZIP-family-metal-transporter	unknown	unknown	gnl\|CDD\|308248
NZ_CP040710.1\|WP_138852916.1\|2605116_2606070_+\|transketolase-family-protein	unknown	unknown	gnl\|CDD\|226467
NZ_CP040710.1\|WP_138852913.1\|2601383_2602466_-\|LptF/LptG-family-permease	unknown	unknown	gnl\|CDD\|367632
NZ_CP040710.1\|WP_138852909.1\|2595054_2595858_+\|Cof-type-HAD-IIB-family-hydrolase	unknown	unknown	gnl\|CDD\|223635
NZ_CP040710.1\|WP_138852905.1\|2592737_2593292_+\|translation-initiation-factor-IF-3	unknown	unknown	gnl\|CDD\|234582

Protein	Function_ID	Function_description	E-value
NZ_CP040710.1\|WP_138852903.1\|2581892_2582525_-\|hemolysin-III-family-protein	gnl\|CDD\|185044	PRK15087, PRK15087, hemolysin; Provisional.	1.98157e-55
NZ_CP040710.1\|WP_138852907.1\|2593749_2594094_+\|50S-ribosomal-protein-L20	gnl\|CDD\|179959	PRK05185, rplT, 50S ribosomal protein L20; Provisional.	9.9104e-61
NZ_CP040710.1\|WP_138852908.1\|2594356_2594779_-\|YjbQ-family-protein	gnl\|CDD\|376651	pfam01894, UPF0047, Uncharacterized protein family UPF0047. This family has no known function. The alignment contains a conserved aspartate and histidine that may be functionally important.	1.74365e-55
NZ_CP040710.1\|WP_138852917.1\|2606118_2606718_+\|outer-membrane-beta-barrel-protein	gnl\|CDD\|372635	pfam13568, OMP_b-brl_2, Outer membrane protein beta-barrel domain. This domain is found in a wide range of outer membrane proteins. This domain assumes a membrane bound beta-barrel fold.	7.68048e-09
NZ_CP040710.1\|WP_138854688.1\|2599474_2600428_-\|acetyl-CoA-carboxylase-carboxyltransferase-subunit-alpha	gnl\|CDD\|235580	PRK05724, PRK05724, acetyl-CoA carboxylase carboxyltransferase subunit alpha; Validated.	0
NZ_CP040710.1\|WP_138852914.1\|2602465_2603596_-\|tRNA-guanosine(34)-transglycosylase-Tgt	gnl\|CDD\|376596	pfam01702, TGT, Queuine tRNA-ribosyltransferase. This is a family of queuine tRNA-ribosyltransferases EC:2.4.2.29, also known as tRNA-guanine transglycosylase and guanine insertion enzyme. Queuine tRNA-ribosyltransferase modifies tRNAs for asparagine, aspartic acid, histidine and tyrosine with queuine. It catalyzes the exchange of guanine-34 at the wobble position with 7-aminomethyl-7-deazaguanine, and the addition of a cyclopentenediol moiety to 7-aminomethyl-7-deazaguanine-34 tRNA; giving a hypermodified base queuine in the wobble position. The aligned region contains a zinc binding motif C-x-C-x2-C-x29-H, and important tRNA and 7-aminomethyl-7deazaguanine binding residues.	0
NZ_CP040710.1\|WP_138852904.1\|2582651_2583992_-\|amidohydrolase-family-protein	gnl\|CDD\|238624	cd01299, Met_dep_hydrolase_A, Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.	9.66988e-59
NZ_CP040710.1\|WP_138852901.1\|2580231_2580657_+\|DUF4268-domain-containing-protein	gnl\|CDD\|379461	pfam14088, DUF4268, Domain of unknown function (DUF4268). This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria and archaea. Proteins in this family are typically between 151 and 387 amino acids in length.	5.91878e-27
NZ_CP040710.1\|WP_138854687.1\|2590697_2592635_+\|threonine--tRNA-ligase	gnl\|CDD\|234752	PRK00413, thrS, threonyl-tRNA synthetase; Reviewed.	0
NZ_CP040710.1\|WP_138852915.1\|2604135_2604981_+\|transketolase	gnl\|CDD\|238970	cd02012, TPP_TK, Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK catalyzes the transfer of a two-carbon unit from ketose phosphates to aldose phosphates. In heterotrophic organisms, TK provides a link between glycolysis and the pentose phosphate pathway and provides precursors for nucleotide, aromatic amino acid and vitamin biosynthesis. In addition, the enzyme plays a central role in the Calvin cycle in plants. Typically, TKs are homodimers. They require TPP and divalent cations, such as magnesium ions, for activity.	1.65269e-119
NZ_CP040710.1\|WP_138852902.1\|2580967_2581888_+\|ThuA-domain-containing-protein	gnl\|CDD\|377643	pfam06283, ThuA, Trehalose utilisation. This family consists of several bacterial ThuA like proteins. ThuA appears to be involved in utilisation of trehalose. The thuA and thuB genes form part of the trehalose/sucrose transport operon thuEFGKAB, which is located on the pSymB megaplasmid. The thuA and thuB genes are induced in vitro by trehalose but not by sucrose and the extent of its induction depends on the concentration of trehalose available in the medium.	7.23942e-33
NZ_CP040710.1\|WP_138852906.1\|2593429_2593627_+\|50S-ribosomal-protein-L35	gnl\|CDD\|234676	PRK00172, rpmI, 50S ribosomal protein L35; Reviewed.	1.22944e-18
NZ_CP040710.1\|WP_138852911.1\|2597759_2599307_-\|replicative-DNA-helicase	gnl\|CDD\|273206	TIGR00665, DnaB, replicative DNA helicase. This model describes the helicase DnaB, a homohexameric protein required for DNA replication. The homohexamer can form a ring around a single strand of DNA near a replication fork. An intein of > 400 residues is found at a conserved location in DnaB of Synechocystis PCC6803, Rhodothermus marinus (both experimentally confirmed), and Mycobacterium tuberculosis. The intein removes itself by a self-splicing reaction. The seed alignment contains inteins so that the model built from the seed alignment will model a low cost at common intein insertion sites. [DNA metabolism, DNA replication, recombination, and repair].	0
NZ_CP040710.1\|WP_138852912.1\|2600470_2601376_-\|EamA-family-transporter	gnl\|CDD\|273359	TIGR00950, Uncharacterized_inner_membrane_transporter_YicL, Carboxylate/Amino Acid/Amine Transporter. [Transport and binding proteins, Amino acids, peptides and amines].	9.23186e-12
NZ_CP040710.1\|WP_138852900.1\|2579560_2580232_+\|ZIP-family-metal-transporter	gnl\|CDD\|308248	pfam02535, Zip, ZIP Zinc transporter. The ZIP family consists of zinc transport proteins and many putative metal transporters. The main contribution to this family is from the Arabidopsis thaliana ZIP protein family these proteins are responsible for zinc uptake in the plant. Also found within this family are C. elegans proteins of unknown function which are annotated as being similar to human growth arrest inducible gene product, although this protein in not found within this family.	4.22882e-06
NZ_CP040710.1\|WP_138852916.1\|2605116_2606070_+\|transketolase-family-protein	gnl\|CDD\|226467	COG3958, COG3958, Transketolase, C-terminal subunit [Carbohydrate transport and metabolism].	1.08679e-132
NZ_CP040710.1\|WP_138852913.1\|2601383_2602466_-\|LptF/LptG-family-permease	gnl\|CDD\|367632	pfam03739, YjgP_YjgQ, Predicted permease YjgP/YjgQ family. Members of this family are predicted integral membrane proteins of unknown function. They are about 350 amino acids long and contain about 6 transmembrane regions. They are predicted to be permeases although there is no verification of this.	2.93541e-56
NZ_CP040710.1\|WP_138852909.1\|2595054_2595858_+\|Cof-type-HAD-IIB-family-hydrolase	gnl\|CDD\|223635	COG0561, Cof, Predicted hydrolases of the HAD superfamily [General function prediction only].	6.10827e-60
NZ_CP040710.1\|WP_138852905.1\|2592737_2593292_+\|translation-initiation-factor-IF-3	gnl\|CDD\|234582	PRK00028, infC, translation initiation factor IF-3; Reviewed.	3.3793e-79

>NZ_CP040710.1|WP_138852908.1|2594356_2594779_-|YjbQ-family-protein
MIFHQKELRLKAYARGFHLITETVLESFPEIAQIQSGMLQVFIKHTSASLTINENADPTVRQDFESHMNVMVPENAKYYIHNYEGPDDMPAHIKASLMGASVQIPITDGMLNLGIWQGIYLCEHRDHASGRNIVISAYGT
>NZ_CP040710.1|WP_138852907.1|2593749_2594094_+|50S-ribosomal-protein-L20
MPRSVNAVASRARRKKVMKQAKGYFGRRKNVWTVAKNAVEKAMLYAYRDRKNKKRTFRALWITRINAGARMHGMSYSQFMGKVKASGIELNRKVLADLAMNHPAAFKAIVEKVK
>NZ_CP040710.1|WP_138852906.1|2593429_2593627_+|50S-ribosomal-protein-L35
MPKQKTKSSAKKRFKLTGTGKIKRKHAFKSHILTKKSKKRKLALTHDTLVHPADVNSIKEQLRLK
>NZ_CP040710.1|WP_138852905.1|2592737_2593292_+|translation-initiation-factor-IF-3
MAIRKRFRPQPRRENKNPHKINKKILAPEVRLVGDNVEVGVYPIRVALDKADEAGLDLVEISPNAAPPVCKIIDYKKFLYEQKKREKAMKAKASKVVVKEIRFGPNTDDHDYEFKKKHAEKFLKDGAKLKAYVFFKGRSIVYKDQGEILLLRLASELEELGKVEQMPRLEGKRMTMFIAPKTKK
>NZ_CP040710.1|WP_138854687.1|2590697_2592635_+|threonine--tRNA-ligase
MINITLPDGSVKAHENGSTPMDVAKDISEGLARNVISAKFNDTIVETSTPLHEDGAITLYTWNSPEGKMAFWHSSAHILAQALEALYPNIKLWVGPAIENGFYYDVDLGDESISDKDFKAIEDKMLEIARGKYDFKMREVSKAEALNYYKGKNEYKVDLIEKLEDGTITFCDHDSFTDLCRGGHIPNTGIVKAFKILSVAGAYYKGDENNKMLTRVYGISFPKQKELTEYLALLEEAKKRDHRKLGRELELFTFSTKVGQGLPLWLPKGAALRERLEQFLKKAQKKAGYEMVMTPHIGQKELYVTSGHYEKYGADSFQPIKTPKEDEEFLLKPMNCPHHCEIYNARPFSYKELPKRYAEFGTVYRYEQSGELHGLTRVRGFTQDDAHIFCTPDQVDQEFKNVIDLSLYVLESLGFDNFTAQVSVRDLDTPEKYIGTVENWEKAENAIINAAKEKGLDYIIESGEAAFYGPKLDFMIKDALGRNWQLGTIQVDYTLPERFDLTYKGSDNELHRPIMIHRAPFGSMERFIALLLEHTGGNFPLWLTPEQAIILSVSEKHEKYAQKVSDYLENNEIRALVDNRNETVGKKIREAEMNKIPFMLIMGENEEANETVSVRKHGGEDLGSISLKEFRDLVNTEINSTLKSF
>NZ_CP040710.1|WP_138852904.1|2582651_2583992_-|amidohydrolase-family-protein
MTRIFAVCLLSFLSFQLITAQDTKIKALVGGTLIDGFGSDPIRNSVIIIEGEKIKAVGTISDTPIPPNAEIISTEGMSVLPGLWDMHVHTMITGHADYNYWDKTYPPLFEDVIMPASAQQLLLAGVTSARDLGGPLAESIAVRDAINSGKIPGATLYVSGPFIQHEPYPGTEDFRWGVKGAEDGRKKIRTLAKAGVDCIKIVDQDQMTKEEFKAVVDEAHKNNLKVVAHSHRPEEIRMGLEVGVDCFEHTGLSSAPKYPDDVMIMIKERTANMSKGPLFWCPTVEGLYNYEYVRDNPEKLDNDSWHLGLPDSVITDIKNSIAHPDRLPYFQLTPSRRPTLKTKINQLLDAGVVLMVGTDSGIPMKFHSQSTWNELDVWVNEFDIDPMYAIRAATYWPSLWMGVAEEVGTITPGKYADIIAVDGDVLRYISLLQDVDMVIKHGKRYK
>NZ_CP040710.1|WP_138852903.1|2581892_2582525_-|hemolysin-III-family-protein
MGNESTYRTEERLNVVSHAIGILLGIVGLVLLLRQDSHKTAFAGFSIIVYSLSFILLFSASTAYHAVSSPILKRRLRVLDHIGIYILIAGTYTPLALITLFHASGWTLFYIVWGIAALGTVLKIFFTGKYELISLILYLAMGWLVVFDYENVLDYVPSIGINLLFLGGAFYTIGTLFYAIKKIPYNHFIWHVFVLAGAVSHWFFIYYGVV
>NZ_CP040710.1|WP_138852902.1|2580967_2581888_+|ThuA-domain-containing-protein
MRNSILTSSALFFLLHLSAQRLEPVEINNTWLASIEKLASSETRIPTENKRKILVFSKATGFDHWTIPHNNEMLKILAKKTDAFEIHIGYDVTNFSASYLDGFDAVVLNNSNPKGPKRDLFYDLLKANSSMSEEAITEAAAGYEDNLMEYVKNGGGLMLLHGAITVQNNSEKFSEMTGGSFDYHPKQQKMHVKEVDPEHPLVEAFKGDGFEHVDEPYLFKNAYFDYNFRPLLYVDTTKLEGLKKEVKNTTNYVSWIKKYGEGRVFYTSASHNAQSLENSEFLQYLLDGMQYVVGDLECDDSPIDQP
>NZ_CP040710.1|WP_138852901.1|2580231_2580657_+|DUF4268-domain-containing-protein
MFSKDESKQLRQEFWTSFGKSYPRKWILYDTKIKGLVLKFHFDVKKAMVAMTVEGDLAQRIAIWENLLSLQSILKEEYLPEAVLEDSYLLKNHKEISIIFVEKEGVSIHDKNTWRETMIFLNEKMTSLEAFFVTYREIIES
>NZ_CP040710.1|WP_138852900.1|2579560_2580232_+|ZIP-family-metal-transporter
MIYLLPILGVLLSFGFVFIAKPKNKENFKLLLAFSGAFLLALSLFELFPEVYAHSEPKTIGVFVMLGILLQIFLEFFSKGAEHGHVHIDREKSDFPWLLFISLSIHSLLEGFPMESNSTIIYGILIHKIPIAIILSIFLLNSKIKLVKAIFFILLFSIMTPVGSYMAANFNLPPNYIANINALVIGVFLHISTVILFESSEGHKFNLRKVLVIMAGITIAYFL
>NZ_CP040710.1|WP_138852909.1|2595054_2595858_+|Cof-type-HAD-IIB-family-hydrolase
MDLSNIKMVVSDMDGTLLNSNHEVSHRFFELFEKLKKRDILFVAASGRQYNSILDKLQDIKNEIVIVAENGGYVMRKDEELLSTLLPKYQQDIILKTLSEIANINTVLCGKEHAYLTGESDAFANMLRQYYSAFEIVEDLRQVETDILKIAIYHYESSEAHIYPSVQHLEGDLKVKISGPNWVDISSPNAHKGFALQKLQERYDITPAETMVFGDYNNDLEMLALADFSFAMANAHPNVKQVAKFQTASNDNFGVERILEQLVLASS
>NZ_CP040710.1|WP_138852910.1|2596136_2597393_-|asparagine-synthetase-B
MRSFFPLICILFSVHMSASSILIPMDAEGQKNHLKAYGITYWVLSKQQKVQWLLNYRGGSFLLPDGDAIRKECQIRGVSFEILSDGQAQGILDDISSPSMNQEAVILEKAPRIAVYSPKGNQPWDDAVTMVLTYAEIPYETVYDEEVLEDKLVLYDWLHLHHEDFTGQYGKFYGSYRAAPWYIEQKQNAEALANKLGFSKVSEEKRAVALKIRNYVIGGGFMFAMCSATDSFDIALAADGVDICEPMFDGDPSEANYQSKLDFKKTFAFQDFVLERSPLQYEFSSIDMTAKRRIPKESDYFSLMDFSAKWDPVPTMLCQNHTALVKGFMGQTTSFDRKGIKPTVMVLGENKINQEARYIHGIKGKGFFTFYGGHDPEDYQHRVGDPKTELELHPTSPGYRLILNNVLFPAAQKKKQKT
>NZ_CP040710.1|WP_138852911.1|2597759_2599307_-|replicative-DNA-helicase
MERTEPLIARKIDKSTIINLERGKIPPQAVDLEEVVLGAMMIDKKGVDEVIDILHPEVFYKDAHRHIYEAIFKLFETSEPVDLLTVSSQLKKDGNLEVIGGDFYLIKLTQKVASSAHIEFHARIILQKYIQRSLIKISNEIIEEAYDEGTDVFDLLDAAESKLYDVTQGNLKRSAETAQNLVIQAKKRIEEIANKEGLSGIPSGFDKVDKLTSGWQPSDLIIVAARPGMGKTALTLSMAKNMAVNHGIPVAFFSCEMSSVQLITRLISSETGLSSEKLRTGKLEKHEWEQLNVKVKALETAPLFIDDTPSLSIFDLRAKARRLASQHGIKLVIIDYLQLMTAGGTQKGGNREQEISTISRNLKALAKELNVPVIALSQLSRAVETRGGSKRPLLSDLRESGAIEQDADIVSFIYRPEYYKIDEWDDEERTPTQGQAEFIVAKHRNGGLENIRLKFIGNLGKFDNLDDFDSPFEFQSKMNANEDNPFITKNLPDANEAFGSSLNDGLPDEDNDVPF
>NZ_CP040710.1|WP_138854688.1|2599474_2600428_-|acetyl-CoA-carboxylase-carboxyltransferase-subunit-alpha
MEYLDFELPIKELEEQLDKCMIIGEESDVDVTETCKQIEKKLADTRKDIYKNLTAWQRVQLSRHPNRPYTLDYINAICKDTFLELHGDRSVKDDKAMIGGLGKIGDQSYMFIGQQKGYNTKTRQYRNFGMANPEGYRKALRLMKSAEKFNLPVVCFVDTPGAYPGIEAEERGQGEAIARNIMEMTRLKVPIIVVIIGEGASGGALGIGVGDVVLMLENTWYSVISPESCSSILWRSWEYKELAAEALKLTATDMKKLKLIDEIVREPAGGAHANREKTFEIVRNKISTHFEQLEKLSPKELVDKRMDKYAKMGVFNG
>NZ_CP040710.1|WP_138852912.1|2600470_2601376_-|EamA-family-transporter
MNTKPNDYVHLHFIVFIWGFTAVLGKLITIAALPLVWYRMLIAVVLVFGFIAFKRFPLRTNRKTMLWMLTGGVLIALHWVTFFLAIKVSTVSIALATMSTGAFFTAILEPIVYKRKIIFYEILFGVLVIAGLLIIFKVETEYAYGIGIALMSSFLAAVFSLINGKLVHKARPAVISFYELGAGVLFLSIYLMATGAFDSAFFQLSNNDWMYIFILASVCTAYAFIASVKVMRHLSPYTVMLTINLEPVYGIILAFFLLGEEEKMSPLFYLGATIILVTVVANGIAKNKVKLKNHRSDSDSS
>NZ_CP040710.1|WP_138852913.1|2601383_2602466_-|LptF/LptG-family-permease
MLTILDKYILKRYLVTFFVMILLFIPIGIMANLAEQISKMIDNEAPLNEILMYYGNFTLYIGSLLFPIFLFLSILFFTSKMASNTEIVAILSSGVSFGRFLRPYFIGASIIALLMFLMGMFIVPKASAGFNEFKFKYLKKGRQDRVTNNIFTQLNEHDFLYVSSFDPARQIGYNFTFERFDDNDQLDFKISAANIRWMEKDTLYRLTSYAKRRVRGETEIMETKRRLDTLFTFDISDLTPVSYVAETKNFFELNQFIEDQKQKGASNINAYLLVKYRRWALPVTAFILTIIAVAVSSIKRRGGMGLNLAFGIFVAFIFIFFDKVFGTLAEQAGFSPLLAVVIPNVMFGLTAFYLLQKAKR
>NZ_CP040710.1|WP_138852914.1|2602465_2603596_-|tRNA-guanosine(34)-transglycosylase-Tgt
MKFTIQHKDPQSKARAATMVTDHGTIETPIFMPVGTVASVKGVHQKELREEVNPDIILGNTYHLFLRPKIDILKKAGGLHKFMGWDRNILTDSGGYQVYSLSANRKIKEEGVKFKSHIDGSMHWFTPENVMEIQRVIGADIIMAFDECTPYPCEYDYAKRSMHMTHRWLDRCIAHLEKTPYEYDYAQTFFPIVQGSTYTDLRKQSAEYIAGVGAEGNAIGGLSVGEPAEEMYAMTEVVCDILPEDKPRYLMGVGTPINLLENIALGVDMFDCVMPTRNARNGMLFTAHGTMNMRNKKWEDDFSALDEMGTTFVDREYSKAYVRHLFAANEYLAKQIATIHNLGFYLWLVREARKHILAGDFADWKTVMVKQMDKRL
>NZ_CP040710.1|WP_138852915.1|2604135_2604981_+|transketolase
MPKLEDLQDIVQQTRRDILRMVHKVNSGHPGGSLGCTEFFVALYHEIMELKQDFDMDGDGEDLFFLSNGHISPVWYSILARKGFFPVSELSTFRELDSRLQGHPTTHEGLPGVRVASGSLGQGMSVAIGAALAKKLNGDQHIVYSLHGDGELQEGQNWEAIMYASGNNVDNLIATIDRNGQQIDGPTEEVLPLGNLREKFEAFGWDVLEVKDGNNLEAVIKGLKEAKVRTGKGKPVCMILDTVMGNGVDFMMHTHAWHGKAPNDEQLQDALAQNPETLGDY
>NZ_CP040710.1|WP_138852916.1|2605116_2606070_+|transketolase-family-protein
MKQYTDQGKKDTRSGYGAGMTELGRSHPNVVALCADLVGSLKIEDFIAENPDRFFQTGIAEANMMGIAAGLTIGGKIPFASTFANFATGRVYDQIRQSIAYSGKNVKICASHAGLTLGEDGATHQILEDIGMMKMLPGMTVINPCDFNQTKAATLAIADHEGPVYLRFGRPKVPNFTPADQKFEIGKALLLQEGTDVTIIATGHLVWPALTAAENLEKQGISAEVINIHTIKPLDEEAILKSVEKTGCVVSAEEHNFLGGLGESIARTLALHLPSPQEFVATQDTFGESGTADQLMDKYGLNNKSIEDAVHRVTNRK
>NZ_CP040710.1|WP_138852917.1|2606118_2606718_+|outer-membrane-beta-barrel-protein
MKVTKSILLCAVFALIGATAFSQSDSGFGIKGGLNYNGNGDYFESIGDAAREPDRNLGFHIGLYGKLELGRLYVRPEVFYTKTKSDYDDDTFDMSKIDLPVLLGAKIIGPVHIFAGPSFQYIINTEYDGITIEDIENDFSVGLHFGGGVNLGKLGIDLRYERGFGDNEGRFINTNITSLPQSRIDTRPEQLILSLSYRL

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Crispr_ID: NZ_CP040710_4

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP040710_4

2964824-2965023

Orphan

Consensus_repeat	Method
GCGCTTCGACGGGCTCAGCGTGACAG	PILER-CR

2 spacers

The CRISPR arrays of NZ_CP040710_4

>merge|NZ_CP040710|4|2964824-2965023|PILER-CR
GCGCTTCGACGGGCTCAGCGTGACAGTTCGCTTTTGATTTGTCCGTTTGTTTTAGAAGCTCATCTAGACCGTGGTTTGCTTTCACTAGCGCTTCGACGGGCTCAGCGTGACAAATGCAATTGATTTGACCTTTATTTGCTCGGAGTTCATATTGACTCCTATATTCTTTCATCTGCGCTTCGACAGGCTCAGCGTGACAG

>NZ_CP040710|4|1|2964824-2965023|PILER-CR
GCGCTTCGACGGGCTCAGCGTGACAG	TTCGCTTTTGATTTGTCCGTTTGTTTTAGAAGCTCATCTAGACCGTGGTTTGCTTTCACTA
GCGCTTCGACGGGCTCAGCGTGACAA	ATGCAATTGATTTGACCTTTATTTGCTCGGAGTTCATATTGACTCCTATATTCTTTCATCT
GCGCTTCGACAGGCTCAGCGTGACAG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP040710.1\|WP_138853227.1\|2970913_2971753_-\|50S-ribosomal-protein-L11-methyltransferase	unknown	unknown	gnl\|CDD\|234786
NZ_CP040710.1\|WP_138853213.1\|2956386_2956851_-\|MaoC-family-dehydratase	unknown	unknown	gnl\|CDD\|239534
NZ_CP040710.1\|WP_138853218.1\|2960838_2961594_-\|glucose-1-dehydrogenase	unknown	unknown	gnl\|CDD\|235546
NZ_CP040710.1\|WP_138853224.1\|2968732_2969332_-\|cyclic-nucleotide-binding-domain-containing-protein	unknown	unknown	gnl\|CDD\|223736
NZ_CP040710.1\|WP_138853229.1\|2972785_2973883_-\|DoxX-family-membrane-protein	unknown	unknown	gnl\|CDD\|225168
NZ_CP040710.1\|WP_138853231.1\|2974571_2975396_+\|dihydropteroate-synthase	unknown	unknown	gnl\|CDD\|273657
NZ_CP040710.1\|WP_138853221.1\|2963490_2964708_-\|acyl-CoA-dehydrogenase	unknown	unknown	gnl\|CDD\|173844
NZ_CP040710.1\|WP_138853225.1\|2969471_2969747_-\|ATP-dependent-Clp-protease-adaptor-ClpS	unknown	unknown	gnl\|CDD\|376861
NZ_CP040710.1\|WP_138853220.1\|2962199_2963267_-\|phosphotransferase	unknown	unknown	gnl\|CDD\|270703
NZ_CP040710.1\|WP_138853212.1\|2954489_2956316_-\|AMP-binding-protein	unknown	unknown	gnl\|CDD\|341233
NZ_CP040710.1\|WP_138853223.1\|2966104_2967919_-\|acyl-CoA-dehydrogenase	unknown	unknown	gnl\|CDD\|173842
NZ_CP040710.1\|WP_138853214.1\|2956860_2957598_-\|glucose-1-dehydrogenase	unknown	unknown	gnl\|CDD\|187594
NZ_CP040710.1\|WP_138853217.1\|2960060_2960837_-\|enoyl-CoA-hydratase/isomerase-family-protein	unknown	unknown	gnl\|CDD\|119339
NZ_CP040710.1\|WP_138853219.1\|2961815_2962196_-\|DUF1330-domain-containing-protein	unknown	unknown	unknown
NZ_CP040710.1\|WP_138853215.1\|2957753_2958728_-\|zinc-binding-dehydrogenase	unknown	unknown	gnl\|CDD\|176203
NZ_CP040710.1\|WP_138853216.1\|2958857_2959862_-\|zinc-binding-dehydrogenase	unknown	unknown	gnl\|CDD\|176190
NZ_CP040710.1\|WP_138853228.1\|2971906_2972656_-\|triose-phosphate-isomerase	unknown	unknown	gnl\|CDD\|234589
NZ_CP040710.1\|WP_138853226.1\|2969872_2970736_-\|peptidase	unknown	unknown	gnl\|CDD\|372084
NZ_CP040710.1\|WP_138853222.1\|2965130_2965907_-\|glucose-1-dehydrogenase	unknown	unknown	gnl\|CDD\|180802
NZ_CP040710.1\|WP_138853230.1\|2973915_2974467_-\|DUF1599-domain-containing-protein	unknown	unknown	gnl\|CDD\|377892

Protein	Function_ID	Function_description	E-value
NZ_CP040710.1\|WP_138853227.1\|2970913_2971753_-\|50S-ribosomal-protein-L11-methyltransferase	gnl\|CDD\|234786	PRK00517, prmA, 50S ribosomal protein L11 methyltransferase.	1.30657e-83
NZ_CP040710.1\|WP_138853213.1\|2956386_2956851_-\|MaoC-family-dehydratase	gnl\|CDD\|239534	cd03450, NodN, NodN (nodulation factor N) contains a single hot dog fold similar to those of the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit. Rhizobium and related species form nodules on the roots of their legume hosts, a symbiotic process that requires production of Nod factors, which are signal molecules involved in root hair deformation and meristematic cell division. The nodulation gene products, including NodN, are involved in producing the Nod factors, however the role played by NodN is unclear.	3.97028e-71
NZ_CP040710.1\|WP_138853218.1\|2960838_2961594_-\|glucose-1-dehydrogenase	gnl\|CDD\|235546	PRK05653, fabG, 3-oxoacyl-ACP reductase FabG.	4.56037e-85
NZ_CP040710.1\|WP_138853224.1\|2968732_2969332_-\|cyclic-nucleotide-binding-domain-containing-protein	gnl\|CDD\|223736	COG0664, Crp, cAMP-binding proteins - catabolite gene activator and regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms].	1.7275e-18
NZ_CP040710.1\|WP_138853229.1\|2972785_2973883_-\|DoxX-family-membrane-protein	gnl\|CDD\|225168	COG2259, COG2259, Predicted membrane protein [Function unknown].	9.79738e-06
NZ_CP040710.1\|WP_138853231.1\|2974571_2975396_+\|dihydropteroate-synthase	gnl\|CDD\|273657	TIGR01496, Dihydropteroate_synthase, dihydropteroate synthase. This model represents dihydropteroate synthase, the enzyme that catalyzes the second to last step in folic acid biosynthesis. The gene is usually designated folP (folic acid biosynthsis) or sul (sulfanilamide resistance). This model represents one branch of the family of pterin-binding enzymes (pfam00809) and of a cluster of dihydropteroate synthase and related enzymes (COG0294). Other members of pfam00809 and COG0294 are represented by model TIGR00284. [Biosynthesis of cofactors, prosthetic groups, and carriers, Folic acid].	1.56862e-106
NZ_CP040710.1\|WP_138853221.1\|2963490_2964708_-\|acyl-CoA-dehydrogenase	gnl\|CDD\|173844	cd01155, ACAD_FadE2, Acyl-CoA dehydrogenases similar to fadE2. FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA dehydrogenases (ACAD) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACAD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. ACAD's are generally homotetramers and have an active site glutamate at a conserved position.	0
NZ_CP040710.1\|WP_138853225.1\|2969471_2969747_-\|ATP-dependent-Clp-protease-adaptor-ClpS	gnl\|CDD\|376861	pfam02617, ClpS, ATP-dependent Clp protease adaptor protein ClpS. In the bacterial cytosol, ATP-dependent protein degradation is performed by several different chaperone-protease pairs, including ClpAP. ClpS directly influences the ClpAP machine by binding to the N-terminal domain of the chaperone ClpA. The degradation of ClpAP substrates, both SsrA-tagged proteins and ClpA itself, is specifically inhibited by ClpS. ClpS modifies ClpA substrate specificity, potentially redirecting degradation by ClpAP toward aggregated proteins.	1.16062e-21
NZ_CP040710.1\|WP_138853220.1\|2962199_2963267_-\|phosphotransferase	gnl\|CDD\|270703	cd05154, ACAD10_11_N-like, N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins. This subfamily is composed of the N-terminal domains of vertebrate ACAD10 and ACAD11, and similar uncharacterized bacterial and eukaryotic proteins. ACADs are a family of flavoproteins that are involved in the beta-oxidation of fatty acyl-CoA derivatives. ACAD deficiency can cause metabolic disorders including muscle fatigue, hypoglycemia, and hepatic lipidosis. There are at least 11 distinct ACADs, some of which show distinct substrate specificities to either straight-chain or branched-chain fatty acids. ACAD10 is widely expressed in human tissues and highly expressed in liver, kidney, pancreas, and spleen. ACAD10 and ACAD11 are both significantly expressed in human brain tissues. They contain a long N-terminal domain with similarity to phosphotransferases with a Protein Kinase fold, which is absent in other ACADs. They may exhibit multiple functions in acyl-CoA oxidation pathways. ACAD11 utilizes substrates with carbon chain lengths of 20 to 26, with optimal activity towards C22CoA. ACAD10 may be associated with an increased risk in type II diabetes. The ACAD10/11-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).	1.63818e-85
NZ_CP040710.1\|WP_138853212.1\|2954489_2956316_-\|AMP-binding-protein	gnl\|CDD\|341233	cd05907, VL_LC_FACS_like, Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases. This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.	3.77306e-166
NZ_CP040710.1\|WP_138853223.1\|2966104_2967919_-\|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.	1.72721e-125
NZ_CP040710.1\|WP_138853214.1\|2956860_2957598_-\|glucose-1-dehydrogenase	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.	2.40572e-102
NZ_CP040710.1\|WP_138853217.1\|2960060_2960837_-\|enoyl-CoA-hydratase/isomerase-family-protein	gnl\|CDD\|119339	cd06558, crotonase-like, Crotonase/Enoyl-Coenzyme A (CoA) hydratase superfamily. This superfamily contains a diverse set of enzymes including enoyl-CoA hydratase, napthoate synthase, methylmalonyl-CoA decarboxylase, 3-hydoxybutyryl-CoA dehydratase, and dienoyl-CoA isomerase. Many of these play important roles in fatty acid metabolism. In addition to a conserved structural core and the formation of trimers (or dimers of trimers), a common feature in this superfamily is the stabilization of an enolate anion intermediate derived from an acyl-CoA substrate. This is accomplished by two conserved backbone NH groups in active sites that form an oxyanion hole.	4.78908e-48
NZ_CP040710.1\|WP_138853215.1\|2957753_2958728_-\|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.	9.15304e-174
NZ_CP040710.1\|WP_138853216.1\|2958857_2959862_-\|zinc-binding-dehydrogenase	gnl\|CDD\|176190	cd05288, PGDH, Prostaglandin dehydrogenases. Prostaglandins and related eicosanoids are metabolized by the oxidation of the 15(S)-hydroxyl group of the NAD+-dependent (type I 15-PGDH) 15-prostaglandin dehydrogenase (15-PGDH) followed by reduction by NADPH/NADH-dependent (type II 15-PGDH) delta-13 15-prostaglandin reductase (13-PGR) to 15-keto-13,14,-dihydroprostaglandins. 13-PGR is a bifunctional enzyme, since it also has leukotriene B(4) 12-hydroxydehydrogenase activity. These 15-PGDH and related enzymes are members of the medium chain dehydrogenase/reductase family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.	5.00574e-179
NZ_CP040710.1\|WP_138853228.1\|2971906_2972656_-\|triose-phosphate-isomerase	gnl\|CDD\|234589	PRK00042, tpiA, triosephosphate isomerase; Provisional.	2.02705e-136
NZ_CP040710.1\|WP_138853226.1\|2969872_2970736_-\|peptidase	gnl\|CDD\|372084	pfam12388, Peptidase_M57, Dual-action HEIGH metallo-peptidase. The catalytic triad for this family of proteases is HE-H-H, which in many members is in the sequence motif HEIGH.	8.72319e-93
NZ_CP040710.1\|WP_138853222.1\|2965130_2965907_-\|glucose-1-dehydrogenase	gnl\|CDD\|180802	PRK07035, PRK07035, SDR family oxidoreductase.	7.46928e-97
NZ_CP040710.1\|WP_138853230.1\|2973915_2974467_-\|DUF1599-domain-containing-protein	gnl\|CDD\|377892	pfam07659, DUF1599, Domain of Unknown Function (DUF1599).	1.19584e-33

>NZ_CP040710.1|WP_138853221.1|2963490_2964708_-|acyl-CoA-dehydrogenase
MNFEYTDKSKTLQEKLKQFIAKNVTPVENEVAAFHRDPANVWKKWPGLEALKQKAKDEGLWNLFLPIGYGDLSPGLTNLEYAPLAEIMGRILWSSEIFNCSAPDTGNMEVLAKYGTPEQQEKWLKPLMNGEIRSAFLMTEPDVASSDATNIETSIVADGNEYVINGTKWWSSGAMDPNCKITIVMGKTDFDAPRHLQQSMILVPMDTPGLQIVRPLSVFGYNDSPEGHAEIILDKVRVPKENLLVGEGQGFAIAQGRLGPGRIHHCMRLIGMAQRALEMMCERTTQRKPFGRTLDTYSSIRQDVANSVCEIEQTRLLVLSAADKMDRMGNKEAKDLIAMIKIVTPNMTLRVVDRAMQIMGGKGVSSDTPLAHFFAAARMLRLADGPDEVHMSQLGKNTIKKYTKE
>NZ_CP040710.1|WP_138853220.1|2962199_2963267_-|phosphotransferase
MNTKPVREGEELNQDDLKKFLLEHNLIADSNSELQVSQFSNGFSNLTYLLNIEERAYVLRRPPFAAPKRGHDMGREFKVIRNLNTVFDKTPKAFAYSEDTTILGAPFYVMSKVEGEILTAKEAHKRQVTPDEFRTISNTWLDTFVAFHNIDYNAAGLEDLGRPEGYIERQVTNWSKQYLAAATDDVPTAKKVMVWMQENQPKHYDHTIIHNDFKYDNVVFKDDSWKDIAAVLDWEMCTLGDPLMDLGTSLGYWTTAADPDFMKQGLQSPTVMPGNPIRTELVQQYATKSGRNIDNLIFYYAYGLFKIAVIAQQIYYRYKNGHTNDPKFAFLNKASELCCNTAWQAIQKKQIDNLF
>NZ_CP040710.1|WP_138853219.1|2961815_2962196_-|DUF1330-domain-containing-protein
MNENSYLEINIEQFNAFKQLPVNTPVVMLNLLKFKDVVTETGLSGEASYKEYMRQAAPFFAKANGEVLFLGKPRAMLIGPEDEYLWDKVLLIRYNTIVDFLAMVQAEGYPSHLRKQALEDSRLIHC
>NZ_CP040710.1|WP_138853218.1|2960838_2961594_-|glucose-1-dehydrogenase
MNLKNKIVIITGAGSGIGAATAKLFGTHGAVVVASDINLNNAQKIAGDITEAGGIASAIKTDVTQYQEVEALIANTIEKHDRLDVIVNNAGIGGKEQLKTAEHTHDDWHNVIAVNQTGVFYCMKVALQHMMRQGHGNIVNVASLAGLKASGHNLSYSASKFAVVGMTKSAALEYARKNIRINAVCPGFTHSALLDQLLAVSPDMGEKLKRFIPMGRFGEADEIAEAICWLASENSKFITGQTITLDGGTSL
>NZ_CP040710.1|WP_138853217.1|2960060_2960837_-|enoyl-CoA-hydratase/isomerase-family-protein
MEFKTLEITHKTNYAIVQMNRGKVNAINHEMVMELRAVFKALGEHEQVYGVVLTGQPHYFSAGLDLIELYQYDKDQITDFFGAFGALYLEMVQFKKPLISAITGHSPAGGCVLAVTCDNRYMAEGDKYVIGLNEVAVNIQISQNLTEIYAFWMGDGRASRYILEGKLLSGQEALEAGLVDELLPLANVLQRAEKQMQLYMKADQEILRNTKAKLREHLWNKLDLNAENSLKEASELWWKPEIRAKMKMYVESFSSKKK
>NZ_CP040710.1|WP_138853216.1|2958857_2959862_-|zinc-binding-dehydrogenase
MNKQLLFVKRPDGEADASTWSLKTNPIPEIKDGEVLVQQHYISLDPAMRGWMNEGKSYIEPMEIGSVMRAGSVGQVIEAKNHPHFKKGDYVSGYAGVQQYIATEGKGYFKVDPNLVPLPTYIGTLGMPGMTAYFGITEVGKIKEGDVVLVSGAAGAVGSIVGQVAKIKGSRVVGIAGGPEKCKYVVDELGFDACIDYKNENVKERLKQECPKGLDVYFDNVGGEILDIALGRLRMHARIVICGAISQYNNKEGMKGPSNYLSLLVNRATMQGMVVFDYADRYAEGAKILGEWMAQGKIKSREDIYEGIENFPETYNRLFTGDKMGKLVLKVIEE
>NZ_CP040710.1|WP_138853215.1|2957753_2958728_-|zinc-binding-dehydrogenase
MKAIRCKAYGPPSSLVLEEVDNLKPKAKEVLVSVKACGLNFPDTLIIQGLYQFKPDLPFTPGSDVAGIVKEVGEEVTHLKVGQEVFGFVAYGALAEEVVVPANACFPKPPQMDFPTAASFLMAYGTSYHALKDRAHLAEGETLLVLGASGGVGIAAVELGKLMGAKVIAAASTEEKLALCKEYGADETINYVAQDLKATIKELTEGKGVDVVYDPVGGTFSEPALRGTAWNGRFLVVGFAAGDIPKIPLNLPLLKGASIVGVFWGAFAMKNPKANMQNSMQLMQWHAEGKLKPHIHAIYDLADTAKALEEMTNRKVKGKLIVKV
>NZ_CP040710.1|WP_138853214.1|2956860_2957598_-|glucose-1-dehydrogenase
MRLKNKIAVVTGGSRGIGQAISELFAKEGATVIIVDLLPQGQKVADDINANGGKAEFHSVSVTDKMAIESLFAATNEKHGSLDILVNNAGITRDRTLEKMSEDEWDAVIDVNLKGVFLCTQAAAPYMKANKYGRIVSAASNVGLRGNFGQTNYAATKAGVIAMSKTWTMELGKHGITANAIAPGFTMTDMVDKIPQEHFAAIKESIPLKTVAQPIDIAYGYLYLASDEARFVSGICLTIDGGTSR
>NZ_CP040710.1|WP_138853213.1|2956386_2956851_-|MaoC-family-dehydratase
MAKLEPDSFQEFRELEGKELPTGDWLSVTQDMINDFAKATMDFQWIHVDVEKAEKYSPFKKPVAHGFMSVSLLAKMLGDVIKVKSVQMGVNYGLNKVRFPAPVLVDSRLRLVSRISNIEEYGDTGLKITWNCTVEMEGSEKPACAAEFLSLMFE
>NZ_CP040710.1|WP_138853212.1|2954489_2956316_-|AMP-binding-protein
MTMTRLFDLLYHQLNDNPIDKSLNVRDANGQWQSYSTAAFVETVEQAASGLLELGLEPGDKVALVVYKNRPEFVIMDFALQLVGMVSVPLYPTISVGEYEYILKEAEVKAAFCGGDDLFYKLSETQKKVPSLKQIFTFDQEPKASFWKTICNSTNSAAVESIKEGILADDLATIIYTSGTTGNPKGVMLTHGNVMHVVRETEPHMAAKAGDPVLSFLPLCHIFERAVSMVYIFKGTRVYFAGTDNLSGPDGDLAAVKPVTFATVPRLLEKIYEAIYNKGLSLEGAKKKIFFWALALTDSWEPNQKISFGQKLKWKIADKLIFSKWREALGGQVNAIVTGAAPCPVKIMRVFCAAGIPIREGYGLTETSPTLTVNTMEQDGVMLGTAGPAIAGVEIKIYASEGDYNEDEGEILAHGPNVMLGYYKKPEVNAQVFREIDKKRWFCTGDIGKLVKGPTGREFLKITDRKKELLKTSGGKYVAPAPIENRVKEEFLVEQMMVIGDKQKFVSALILPAEEALKSYCAKKEIPWTTMAEVIKHKKVIRRYQKIIDKYNPEFGHVEQIKKFRLLSSPWLPVHDNGAEAELTPTLKLKRRVIREKFQKEIASIYTD
>NZ_CP040710.1|WP_138853222.1|2965130_2965907_-|glucose-1-dehydrogenase
MKSIKQKFDLKGKVAIVTGSSKGIGLSIAKGLAENGAKLVISSRKQAAVDMVAEEFKKAGLEAIGLACHIGDAEQRKVLVAKTMEQYGRIDILVNNAAINPFYGPLETSGEEVFDKIMNVNVKAPWLLSNLVQPHMKAQGSGSIINISSVEGIHPGFRLGLYSMTKSALIMLTKNQAKEWGRYGIRSNVVCPGLIKTKFSESLWSDEKLAAGYNQMVPLKRMAEPDEMAGVVMLLASDAGSYMTGGVYAADGGYLISG
>NZ_CP040710.1|WP_138853223.1|2966104_2967919_-|acyl-CoA-dehydrogenase
MANQYVDLDTLKFLLYKVHDLQSVLDQDRYADYDKESIDMMLNSVKDFSDKELFPFFREMDEHPAHFKDGEIVVHPQVNKYMKAGGEMGFISGPFPYEDGGMQMPAMALNASAYIQEAANNHLPGYIGLTVGAAELITHFANQELKDTYVPNMLEGKWGGTMCLTEPQAGSSLSDIVTSATPDGDMYKIHGQKIFISGGDYQGAENIVHLVLARIKGAPAGTKGISLFVVPKNRPAADGSLSPNDVQTVADFKKMGQKGYCTTHLFFGDKEDCRGWLVGEANQGLKYMFLMMNGARIGVGRGAAAIATAAYHASLNYAHERPQGRQLTSTGKKDANQEQTLIINHPDVRRMLLLQKVVSEGSLSLIFLAAKYQDLSMSSADADEREKYRLLLEILTPVVKTYPSEMGKVAVDNGVQVLGGYGFCSDYILQQYLRDIRIFAIYEGTTGIQSQDLLGRKVTMNNGKALQLLSEEIMNSIKASMAHESLAPYAKKLGAKLELTQQVLQSLMGFAMKGDYQRFLADATPFMEFFSNILIGWLWLDMAREAQNALVTGNTENSTDFYESKIHAMQFYFKYELPKTSALAEILMDNEQALTIGTDKKVFA
>NZ_CP040710.1|WP_138853224.1|2968732_2969332_-|cyclic-nucleotide-binding-domain-containing-protein
MKLAVEVDHLKHLRNKILSYTQVDEELLDRELRYYKRIELQKGEALVTAGQIVEHFYYVAEGCIYYYKVEEGQIQVLEFYTDDVFFTDLTAYVKATPAQHNLCATEDTIVFAVKKSDAERSFNQSHQLERFGRLSMQEAFMKSFNRIERLNSRSNEKRYLRLLEKRPDLLQRVPQYLIASYLGLTPVGLSKIRKRLAKV
>NZ_CP040710.1|WP_138853225.1|2969471_2969747_-|ATP-dependent-Clp-protease-adaptor-ClpS
MGTIEKLQEDLLLAEETVKQSEIVLFNDEVNTFDHVIETLIAVCEHTPEQAEQCSIIVHHNGKCTVKTGEYDELKPRCSKLLQAGLSAEII
>NZ_CP040710.1|WP_138853226.1|2969872_2970736_-|peptidase
MRKFRLPFLLIAFLFILNACQKENTPIVEEQDSATAEKVQEPELEITDAVVQTLKSNFYNTSDIKVVNFMLPDGTFEARYQVEDDITFSVESLEALPEVKKGSDAERNYHTNNLVSSRTLTIIGFTGGNNALTSKEQTALQYAVNNYNRLNLSIRFSLTFGTNYQNKDMVVYYNPNESGSGGSAGFPSNGNPNKFVQIYGLDNSSVDVIEHVITHEIGHSVGFRHTDWFSRQSCGQNVNEGAGGIGANPIPGTPSGYDPTSIMLACFSSNEDGEFNNNDIIALNYLY
>NZ_CP040710.1|WP_138853227.1|2970913_2971753_-|50S-ribosomal-protein-L11-methyltransferase
MSNTTYIEYAFKVNPLQPASDILIAELGEVGFESFVENDEGLLAYIQQEDWTDGILALVQVLRNDLFEIHFDYKTIEQENWNATWEENFEPILVDDKCMVRAPFHKKEEVEYDIVIMPKMSFGTGHHETTHMMLRHVLNHDFNGKSVLDMGSGTGVLAILAALKGAATVDAIDIDHWCFLNAKENVDRNGCGHIHVYEGDVSLLNSQKYHVILANINRNILLNDIPVYASCLHEKGILFLSGFYETDVKVISEKCAEIGLNFQEKSKKGEWVSLKFIKP
>NZ_CP040710.1|WP_138853228.1|2971906_2972656_-|triose-phosphate-isomerase
MRSKIVAGNWKMNKNLEQTEALLAELAGKLPDTDAEVMVAPTYVNLAAAVRALGNSTIEVIAQNMHFAESGAYTGEISADMLLNIGIHTAIIGHSERRAYFGETDEILAKKVKAALGKNIRVMFCFGEELEQRKSGDHFNLVESQLRNALFSLNASDWSNIVLAYEPVWAIGTGETASPEQAQEMHAFIRKTITEAYDAEIAANVSILYGGSVKSGNAAEIFSKPDVDGGLIGGASLVADDFVAIIKAI
>NZ_CP040710.1|WP_138853229.1|2972785_2973883_-|DoxX-family-membrane-protein
MKYLVGFSRIIVGILFIISGFIKLNDPVGFSFKLEEYFSQGVLNLPFFEPYALYISVFVVIVEVLLGVMLLVGFRVKFTVWSLLLMIIGFTFLTFYSAYFNKVTDCGCFGDALKLTPWQSFTKDIVLLLLIIILFVGRRFIQPIVGDNAKRIITVVALVICGLYANHVLKHLPVIDFRPYNIGANIEEGMGIPEDAPKAIYDYAWKFNVNGEEQTIVTQGDYPTVDGEYVSVETTEVQAGYEPPIHDFTIEQNGEDFAASLLQEPKLVMVVAYDLQKTNTNVYSELKKVTDRAIKNGYKVIGMSASNNEQSSELVKRYSLGFEFYFTDETALKTIVRSNPGLLVLEKGTIKQKVHYNDMDELKFE
>NZ_CP040710.1|WP_138853230.1|2973915_2974467_-|DUF1599-domain-containing-protein
MQHTSEQYDAVIKTCRDLFEKKMKDYGSAWRILRLPSLTDQIFIKAQRIRGLQENAVRKVDEGEIPEFMGIINYCIMALVQLEKGIAVQPDLNAKEALSLFDRHTSETKSLMENKNHDYGEAWRDMRVSSLTDLILQKLLRVKQIENNKGKTLVSEGIDANYQDMVNYAVFALIHLKKKAPTD
>NZ_CP040710.1|WP_138853231.1|2974571_2975396_+|dihydropteroate-synthase
MTLNCNGKLIDLKVPKVMGILNITPDSFYDGGKFKEEAAVLKQVDKMLNEGATFVDVGAYSSRPGADFVSEAIELRRILPIVKLLLAEFPNIILSIDTFRSGVAHACLSEGAAIINDISAGIQDEKIFAVVSEHQAPLVMMHMRGTPKNMQQQTQYDNLSVAILKYFSERIAIARTYGIYDLIIDPGFGFAKTLEQNYELLSQLDLFKNLRHPILVGLSRKSMIYRLLDTDAENALNGTTALHSIALSKGAQILRAHDVKEAMECIRLVQQLNR

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Self-targeting detection

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_ID	Protospacer_location	Mismatch	Identity

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity
NZ_CP040710_2	2.9\|578972\|27\|NZ_CP040710\|CRT	578972-578998	27	MH153807	Rhodococcus phage Peregrin, complete genome	89969-89995	4	0.852
NZ_CP040710_2	2.8\|578916\|34\|NZ_CP040710\|CRT	578916-578949	34	NZ_CP020399	Burkholderia multivorans strain FDAARGOS_246 plasmid unnamed, complete sequence	247653-247686	8	0.765

1. spacer 2.9|578972|27|NZ_CP040710|CRT matches to MH153807 (Rhodococcus phage Peregrin, complete genome) position: , mismatch: 4, identity: 0.852

ttcaaacttctcacctcgcacttcgag	CRISPR spacer
ttcaaacttcactcctcgcacttcacg	Protospacer
********** * ***********. *

2. spacer 2.8|578916|34|NZ_CP040710|CRT matches to NZ_CP020399 (Burkholderia multivorans strain FDAARGOS_246 plasmid unnamed, complete sequence) position: , mismatch: 8, identity: 0.765

ttcgcgcttcgtgcttcgtgcttcaaacttctca	CRISPR spacer
ttcgtgcttcgtgcttcgtgcttcgtgctgcgtg	Protospacer
****.*******************. .** * ..

Prophage detection

Region

Region Position

Protein_number

Hit_taxonomy

Key_proteins

Att_site

Prophage annotation

DBSCAN-SWA_1

664467 : 730720

Thermus_phage(25.0%)

integrase,transposase,tRNA,protease

attL 660803:660819|attR 708423:708439

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
660803:660819	attL	NA	NA	NA	NA
WP_138851432.1\|664467_664920_-\|tRNA	tRNA (cytidine(34)-2'-O)-methyltransferase	NA	NA	NA	NA
WP_138851433.1\|665018_665258_-	DNA-binding protein VF530	NA	NA	NA	NA
WP_138851434.1\|665502_666366_-	sigma-70 family RNA polymerase sigma factor	M4SMP8	Cyanophage	1.2e-36	33.4
WP_138851435.1\|666542_667793_+	acyloxyacyl hydrolase	NA	NA	NA	NA
WP_138851436.1\|667907_670133_-	polyribonucleotide nucleotidyltransferase	NA	NA	NA	NA
WP_138851437.1\|670347_670617_-	30S ribosomal protein S15	NA	NA	NA	NA
WP_138851438.1\|670744_671242_-	hypothetical protein	NA	NA	NA	NA
WP_138854594.1\|671253_672114_-	acetyl-CoA carboxylase, carboxyltransferase subunit beta	NA	NA	NA	NA
WP_138851439.1\|672147_673215_-	class II fructose-bisphosphate aldolase	NA	NA	NA	NA
WP_138851440.1\|673510_676114_-	BamA/TamA family outer membrane protein	NA	NA	NA	NA
WP_138851441.1\|676148_676892_+	RNA methyltransferase	NA	NA	NA	NA
WP_138851442.1\|677058_677523_+	hypothetical protein	NA	NA	NA	NA
WP_138851443.1\|677626_678337_-	outer membrane beta-barrel protein	NA	NA	NA	NA
WP_138851444.1\|678341_679070_-	bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE	NA	NA	NA	NA
WP_138851445.1\|679456_680806_+	Trk system potassium transporter TrkA	NA	NA	NA	NA
WP_138851446.1\|680806_682297_+	TrkH family potassium uptake protein	NA	NA	NA	NA
WP_138851447.1\|682267_682714_-	DUF1801 domain-containing protein	NA	NA	NA	NA
WP_138851448.1\|682922_683765_-	hypothetical protein	NA	NA	NA	NA
WP_138854595.1\|684400_684925_-	hypothetical protein	NA	NA	NA	NA
WP_138851449.1\|685055_685340_-	putative addiction module antidote protein	NA	NA	NA	NA
WP_138851450.1\|686463_687459_-\|transposase	IS110 family transposase	NA	NA	NA	NA
WP_138851451.1\|688053_688353_-	type II toxin-antitoxin system RelE/ParE family toxin	NA	NA	NA	NA
WP_138851452.1\|688345_688597_-	type II toxin-antitoxin system ParD family antitoxin	NA	NA	NA	NA
WP_138851453.1\|689254_689791_-	DUF2199 domain-containing protein	NA	NA	NA	NA
WP_138851454.1\|692088_692568_-	hypothetical protein	NA	NA	NA	NA
WP_138851455.1\|692898_693675_-	hypothetical protein	NA	NA	NA	NA
WP_138851456.1\|693671_694151_-	hypothetical protein	NA	NA	NA	NA
WP_138851450.1\|694557_695553_+\|transposase	IS110 family transposase	NA	NA	NA	NA
WP_138851457.1\|696015_697071_+\|transposase	IS110 family transposase	A0A1S7J231	Thermus_phage	1.1e-12	27.1
WP_138851458.1\|697352_697655_-	HigA family addiction module antidote protein	M9MUN2	Rhodococcus_phage	1.6e-12	48.2
WP_138851459.1\|697665_697947_-	plasmid maintenance system killer family protein	A0A222YWE2	Escherichia_phage	7.0e-10	44.1
WP_138851460.1\|700218_700662_-	hypothetical protein	NA	NA	NA	NA
WP_138851461.1\|701247_702432_-	hypothetical protein	NA	NA	NA	NA
WP_138851457.1\|702538_703594_+\|transposase	IS110 family transposase	A0A1S7J231	Thermus_phage	1.1e-12	27.1
WP_138851462.1\|703890_704280_-	hypothetical protein	NA	NA	NA	NA
WP_138851463.1\|704443_705526_+\|integrase	tyrosine-type recombinase/integrase	S5W9T9	Leptospira_phage	6.4e-27	31.1
WP_138851464.1\|705560_706754_-	aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme	NA	NA	NA	NA
WP_138851465.1\|707008_708109_-	acyl-CoA desaturase	A6N231	Microbacterium_phage	2.4e-05	36.6
WP_138851466.1\|708253_708889_+	16S rRNA (guanine(527)-N(7))-methyltransferase RsmG	NA	NA	NA	NA
708423:708439	attR	NA	NA	NA	NA
WP_138851467.1\|709173_709545_-	hypothetical protein	NA	NA	NA	NA
WP_138851468.1\|709766_710285_-	DinB family protein	NA	NA	NA	NA
WP_138851469.1\|710407_711382_-	hypothetical protein	NA	NA	NA	NA
WP_138851470.1\|711648_713277_-	L-glutamate gamma-semialdehyde dehydrogenase	NA	NA	NA	NA
WP_138851471.1\|713779_714166_-	Co2+/Mg2+ efflux protein ApaG	NA	NA	NA	NA
WP_138854596.1\|714174_715212_-	DUF3667 domain-containing protein	NA	NA	NA	NA
WP_138851472.1\|715611_716859_-	DUF5103 domain-containing protein	NA	NA	NA	NA
WP_138851473.1\|717011_718361_+	Na(+)-translocating NADH-quinone reductase subunit A	NA	NA	NA	NA
WP_138854597.1\|718379_719645_+	NADH:ubiquinone reductase (Na(+)-transporting) subunit B	NA	NA	NA	NA
WP_138851474.1\|719648_720404_+	Na(+)-translocating NADH-quinone reductase subunit C	NA	NA	NA	NA
WP_138851475.1\|720403_721051_+	NADH:ubiquinone reductase (Na(+)-transporting) subunit D	NA	NA	NA	NA
WP_138851476.1\|721235_721997_+	NADH:ubiquinone reductase (Na(+)-transporting) subunit E	NA	NA	NA	NA
WP_138851477.1\|721999_723307_+	NADH:ubiquinone reductase (Na(+)-transporting) subunit F	NA	NA	NA	NA
WP_138851478.1\|723589_723952_+	Na(+)-translocating NADH-quinone reductase subunit F	NA	NA	NA	NA
WP_138851479.1\|724021_725029_+	FAD:protein FMN transferase	NA	NA	NA	NA
WP_138851480.1\|725032_725797_-	methyltransferase domain-containing protein	NA	NA	NA	NA
WP_138851481.1\|725837_726218_-	GxxExxY protein	E5ESB4	Bathycoccus_sp._RCC1105_virus	4.0e-08	37.0
WP_138851482.1\|726276_727080_-	type I methionyl aminopeptidase	NA	NA	NA	NA
WP_138851483.1\|727276_728794_-	2,3-bisphosphoglycerate-independent phosphoglycerate mutase	NA	NA	NA	NA
WP_138851484.1\|729124_729511_+	ankyrin repeat domain-containing protein	NA	NA	NA	NA
WP_138851485.1\|729949_730720_-\|protease	M48 family metalloprotease	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. NZ_CP040710

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CRISPR-Cas detection and classification

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Self-targeting detection

MGE targeting detection<

Prophage detection

Anti-CRISPR protein detection