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_CP016907	Flavobacterium anhuiense strain GSE09 chromosome, complete genome	6 crisprs	RT,DEDDh,cas3,csa3,WYL	0	3	2	0

Results visualization

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CRISPR-Cas detection and classification

Crispr_ID: NZ_CP016907_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP016907_1

265334-265407

Orphan

Consensus_repeat	Method
GGCGGTTTCAGAAGCGACAGAAG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP016907_1

>merge|NZ_CP016907|1|265334-265407|CRISPRCasFinder
GGCGGTTTCAGAAGCGACAGAAGTTCTTCTAGAGATGGAGGTTCACGTGATGGAGGTTTCAGAAGCGACAGAAG

>NZ_CP016907|1|1|265334-265407|CRISPRCasFinder
GGCGGTTTCAGAAGCGACAGAAG	TTCTTCTAGAGATGGAGGTTCACGTGAT
GGAGGTTTCAGAAGCGACAGAAG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP016907.1\|WP_008462511.1\|257514_258297_+\|NYN-domain-containing-protein	unknown	unknown	gnl\|CDD\|350237
NZ_CP016907.1\|WP_123906980.1\|253988_256226_-\|nitric-oxide-reductase-large-subunit	unknown	unknown	gnl\|CDD\|225795
NZ_CP016907.1\|WP_008462506.1\|262480_262885_+\|DUF2809-domain-containing-protein	unknown	unknown	gnl\|CDD\|378530
NZ_CP016907.1\|WP_066032290.1\|273590_274535_-\|2-nitropropane-dioxygenase	unknown	unknown	gnl\|CDD\|132195
NZ_CP016907.1\|WP_066032289.1\|273159_273570_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP016907.1\|WP_008462499.1\|270032_270665_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP016907.1\|WP_066032287.1\|271845_272490_-\|CoA-pyrophosphatase	unknown	unknown	gnl\|CDD\|239518
NZ_CP016907.1\|WP_008462500.1\|269530_270025_+\|sigma-70-family-RNA-polymerase-sigma-factor	unknown	unknown	gnl\|CDD\|274357
NZ_CP016907.1\|WP_066032282.1\|261008_262187_-\|glucuronyl-hydrolase	unknown	unknown	gnl\|CDD\|369381
NZ_CP016907.1\|WP_066032286.1\|268315_269377_+\|DUF3810-domain-containing-protein	unknown	unknown	gnl\|CDD\|378933
NZ_CP016907.1\|WP_066032285.1\|266676_268137_-\|aminoacyl-histidine-dipeptidase	unknown	unknown	gnl\|CDD\|349885
NZ_CP016907.1\|WP_066032280.1\|259900_260329_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP016907.1\|WP_008462503.1\|265782_266562_+\|carboxypeptidase-like-regulatory-domain-containing-protein	unknown	unknown	gnl\|CDD\|372685
NZ_CP016907.1\|WP_066032279.1\|258332_259847_+\|FMN-binding-glutamate-synthase-family-protein	unknown	unknown	gnl\|CDD\|239202
NZ_CP016907.1\|WP_008462498.1\|270903_271713_-\|1-acyl-sn-glycerol-3-phosphate-acyltransferase	unknown	unknown	gnl\|CDD\|153251
NZ_CP016907.1\|WP_066032278.1\|256864_257314_-\|Rrf2-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|273242
NZ_CP016907.1\|WP_066032281.1\|260594_261002_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP016907.1\|WP_066032283.1\|262850_263429_+\|non-canonical-purine-NTP-diphosphatase	unknown	unknown	gnl\|CDD\|237823
NZ_CP016907.1\|WP_066032277.1\|256315_256843_-\|azurin	unknown	unknown	gnl\|CDD\|259989
NZ_CP016907.1\|WP_066032288.1\|272581_273019_+\|DUF4268-domain-containing-protein	unknown	unknown	gnl\|CDD\|379461

Protein	Function_ID	Function_description	E-value
NZ_CP016907.1\|WP_008462511.1\|257514_258297_+\|NYN-domain-containing-protein	gnl\|CDD\|350237	cd11297, PIN_LabA-like_N_1, uncharacterized subfamily of N-terminal LabA-like PIN domains. This N-terminal LabA-like PIN domain is found in a well conserved group of mainly bacterial proteins with no defined function, which contain a C-terminal LabA_like_C domain. LabA from Synechococcus elongatus PCC 7942, (which does not contain this C-terminal domain), has been shown to play a role in cyanobacterial circadian timing. The LabA-like C-terminal domains characteristic of this subfamily may be related to the LOTUS domain family (which also co-occurs with LabA-like N-terminal domains). The function of the N-terminal domain is unknown. The LabA-like PIN domain family also includes the N-terminal domain of limkain b1, a human autoantigen localized to a subset of ABCD3 and PXF marked peroxisomes. Other members are the LabA-like PIN domains of human ZNF451, uncharacterized Bacillus subtilis YqxD and Escherichia coli YaiI. Curiously, a gene labeled NicB from Pseudomonas putida S16, which is described as a putative NADH-dependent hydroxylase involved in the microbial degradation of nicotine also falls into the LabA-like PIN family. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons.	4.3735e-65
NZ_CP016907.1\|WP_123906980.1\|253988_256226_-\|nitric-oxide-reductase-large-subunit	gnl\|CDD\|225795	COG3256, NorB, Nitric oxide reductase large subunit [Inorganic ion transport and metabolism].	0
NZ_CP016907.1\|WP_008462506.1\|262480_262885_+\|DUF2809-domain-containing-protein	gnl\|CDD\|378530	pfam10990, DUF2809, Protein of unknown function (DUF2809). Some members in this family of proteins are annotated as yjgA however currently no function for the protein is known.	1.31275e-27
NZ_CP016907.1\|WP_066032290.1\|273590_274535_-\|2-nitropropane-dioxygenase	gnl\|CDD\|132195	TIGR03151, enACPred_II, putative enoyl-[acyl-carrier-protein] reductase II. This oxidoreductase of the 2-nitropropane dioxygenase family (pfam03060) is commonly found in apparent operons with genes involved in fatty acid biosynthesis. Furthermore, this genomic context generally includes the fabG 3-oxoacyl-[ACP] reductase and lacks the fabI enoyl-[ACP] reductase.	1.82718e-101
NZ_CP016907.1\|WP_066032287.1\|271845_272490_-\|CoA-pyrophosphatase	gnl\|CDD\|239518	cd03426, CoAse, Coenzyme A pyrophosphatase (CoAse), a member of the Nudix hydrolase superfamily, functions to catalyze the elimination of oxidized inactive CoA, which can inhibit CoA-utilizing enzymes. The need of CoAses mainly arises under conditions of oxidative stress. CoAse has a conserved Nudix fold and requires a single divalent cation for catalysis. In addition to a signature Nudix motif G[X5]E[X7]REUXEEXGU, where U is Ile, Leu, or Val, CoAse contains an additional motif upstream called the NuCoA motif (LLTXT(SA)X3RX3GX3FPGG) which is postulated to be involved in CoA recognition. CoA plays a central role in lipid metabolism. It is involved in the initial steps of fatty acid sythesis in the cytosol, in the oxidation of fatty acids and the citric acid cycle in the mitochondria, and in the oxidation of long-chain fatty acids in peroxisomes. CoA has the important role of activating fatty acids for further modification into key biological signalling molecules.	5.13097e-51
NZ_CP016907.1\|WP_008462500.1\|269530_270025_+\|sigma-70-family-RNA-polymerase-sigma-factor	gnl\|CDD\|274357	TIGR02937, RNA_polymerase_sigma_factor, RNA polymerase sigma factor, sigma-70 family. This model encompasses all varieties of the sigma-70 type sigma factors including the ECF subfamily. A number of sigma factors have names with a different number than 70 (i.e. sigma-38), but in fact, all except for the Sigma-54 family (TIGR02395) are included within this family. Several Pfam models hit segments of these sequences including Sigma-70 region 2 (pfam04542) and Sigma-70, region 4 (pfam04545), but not always above their respective trusted cutoffs.	2.05308e-26
NZ_CP016907.1\|WP_066032282.1\|261008_262187_-\|glucuronyl-hydrolase	gnl\|CDD\|369381	pfam07470, Glyco_hydro_88, Glycosyl Hydrolase Family 88. Unsaturated glucuronyl hydrolase catalyzes the hydrolytic release of unsaturated glucuronic acids from oligosaccharides (EC:3.2.1.-) produced by the reactions of polysaccharide lyases.	3.46762e-16
NZ_CP016907.1\|WP_066032286.1\|268315_269377_+\|DUF3810-domain-containing-protein	gnl\|CDD\|378933	pfam12725, DUF3810, Protein of unknown function (DUF3810). This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 333 and 377 amino acids in length. There is a conserved HEXXH sequence motif that is characteristic of metallopeptidases. This family may therefore belong to an as yet uncharacterized family of peptidase enzymes.	4.63927e-124
NZ_CP016907.1\|WP_066032285.1\|266676_268137_-\|aminoacyl-histidine-dipeptidase	gnl\|CDD\|349885	cd03890, M20_pepD, M20 Peptidase D has specificity for beta-alanyl-L-histidine dipeptide. Peptidase M20 family, Peptidase D (PepD, Xaa-His dipeptidase; X-His dipeptidase; aminoacylhistidine dipeptidase; dipeptidase D; Beta-alanyl-histidine dipeptidase; pepD g.p. (Escherichia coli); EC 3.4.13.3) subfamily. PepD is a cytoplasmic enzyme family characterized by its unusual specificity for the dipeptides beta-alanyl-L-histidine (L-carnosine or beta-Ala-His) and gamma-aminobutyryl histidine (L-homocarnosine or gamma-amino-butyl-His). Homocarnosine has been suggested as a precursor for the neurotransmitter gamma-aminobutyric acid (GABA), acting as a GABA reservoir, and may mediate anti-seizure effects of GABAergic therapies. It has also been reported that glucose metabolism could be influenced by L-carnosine. PepD also includes a lid domain that forms a homodimer; however, the physiological function of this extra domain remains unclear.	0
NZ_CP016907.1\|WP_066032283.1\|262850_263429_+\|non-canonical-purine-NTP-diphosphatase	gnl\|CDD\|237823	PRK14823, PRK14823, putative deoxyribonucleoside-triphosphatase; Provisional.	1.26861e-123
NZ_CP016907.1\|WP_008462503.1\|265782_266562_+\|carboxypeptidase-like-regulatory-domain-containing-protein	gnl\|CDD\|372685	pfam13715, CarbopepD_reg_2, CarboxypepD_reg-like domain. This domain family is found in bacteria, archaea and eukaryotes, and is approximately 90 amino acids in length. The family is found in association with pfam07715 and pfam00593.	1.12485e-16
NZ_CP016907.1\|WP_066032279.1\|258332_259847_+\|FMN-binding-glutamate-synthase-family-protein	gnl\|CDD\|239202	cd02808, GltS_FMN, Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that catalyzes the reductive synthesis of L-glutamate from 2-oxoglutarate and L-glutamine via intramolecular channelling of ammonia, a reaction in the plant, yeast and bacterial pathway for ammonia assimilation. It is a multifunctional enzyme that functions through three distinct active centers, carrying out L-glutamine hydrolysis, conversion of 2-oxoglutarate into L-glutamate, and electron uptake from an electron donor.	2.34821e-173
NZ_CP016907.1\|WP_008462498.1\|270903_271713_-\|1-acyl-sn-glycerol-3-phosphate-acyltransferase	gnl\|CDD\|153251	cd07989, LPLAT_AGPAT-like, Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: AGPAT-like. Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are such LPLATs as 1-acyl-sn-glycerol-3-phosphate acyltransferase (AGPAT, PlsC), Tafazzin (product of Barth syndrome gene), and similar proteins.	2.08814e-19
NZ_CP016907.1\|WP_066032278.1\|256864_257314_-\|Rrf2-family-transcriptional-regulator	gnl\|CDD\|273242	TIGR00738, Putative_HTH-type_transcriptional_regulator, Rrf2 family protein. This model represents a superfamily of probable transcriptional regulators. One member, RRF2 of Desulfovibrio vulgaris is an apparent regulatory protein experimentally (MEDLINE:97293189). The N-terminal region appears related to the DNA-binding biotin repressor region of the BirA bifunctional according to results after three rounds of PSI-BLAST with a fairly high stringency. [Unknown function, General].	3.25472e-22
NZ_CP016907.1\|WP_066032277.1\|256315_256843_-\|azurin	gnl\|CDD\|259989	cd13922, Azurin, Azurin is a redox partner for enzymes such as nitrite reductase or arsenite oxidase. Azurin is a bacterial blue copper-binding protein. It serves as a redox partner to enzymes such as nitrite reductase or arsenite oxidase. The copper of Azurin is tetrahedrally coordinated by a cysteine, 2 histidines, and a methionine residue. The electron transfer reactions are carried out with the Cu center transitioning between the oxidized Cu(II) form and the reduced Cu(I) form. Azurin can function as a tumor suppressor; it forms a complex with p53 that triggers apoptosis in various human cancer cells.	1.20908e-59
NZ_CP016907.1\|WP_066032288.1\|272581_273019_+\|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.	2.13308e-32

>NZ_CP016907.1|WP_066032283.1|262850_263429_+|non-canonical-purine-NTP-diphosphatase
MNLVFASNNKNKIAEIQSMLPESIKILSLEDINCFEDIPETADTIEGNAILKADYVTQKYGYDCFADDTGLEVDALNGEPGVYSARYAGEQKNADDNMNKLLEALKNKENRSAQFKTVITLNLKGKQYLFTGIAKGEITFTKTGTNGFGYDPIFKPENFNETFAELPLATKNTIGHRGKAVKQLIDFLNTTK
>NZ_CP016907.1|WP_008462506.1|262480_262885_+|DUF2809-domain-containing-protein
MNKTRINYFLIFLTIIFLGVLSRKIPFIPLWIGDFLYAVMIYFLVRIFFPSKKFWLVILLSLFICYGIEFLQLYQGNWIVELRKTLFGRYVLGQGFLWSDILAYTFGISLTFIIEKSFLKYYHNESRFRIKQQK
>NZ_CP016907.1|WP_066032282.1|261008_262187_-|glucuronyl-hydrolase
MKAKFFTLIAALFLLGNQGYSQKNNSFNIKKQLDYCAEQASKTLKVIPNDGTSPRTVPNGSNEWKFVGYKDWTSGFWPGELWFLYEATKDKKWEKEADKFSRFLTPLSTSKAGDHDLGFQIFNSFGNGYRLTKNPEYKQIILRTADTLATLFNPKVGTIQSWPHNKMGGHNTIIDNMMNLELLFWASKNGGSKKLYDIAVKHAETTMANHFRPDNTSYHVIIYDYETGKKIKGRTAQGYSDDSMWARGQAWAIYGFTMTYRETKDAKFLDFAHKLARVYLDKLTTEDLVPYWDFNAPNIPNEPRDASAAAIVSSALLELSSYTKDKSLKAEYLTKAKKMIVSLSNNYQSHDVNSAFLLHSTGHKPANSEIDCSINYADYYYLEALLRLQKLK
>NZ_CP016907.1|WP_066032281.1|260594_261002_-|hypothetical-protein
MLKKISQIAFAIMIVLTLLSCKNTKQKLQEYVVTYNKTIAPSFRADNVTLTTARGYINDNKIELRFETDLEQNEANKSASIISFPKLIKVMIDKDEIPRQLIEEGVQFDVYFLADDNTVLDKETLTGESLKDFLK
>NZ_CP016907.1|WP_066032280.1|259900_260329_-|hypothetical-protein
MKKITQIAFALAFALFLVSCKNTKQKIQEHVSNYNNLSSIKGSGITSTTAKAFLDDNKIEIRIETNLEENDANKLAYKESFPDLLKEMIKNDQISPSLIAEGVKFDVYFLAYNNAILAQELVDQDELAVLEGTAKSKETAKL
>NZ_CP016907.1|WP_066032279.1|258332_259847_+|FMN-binding-glutamate-synthase-family-protein
MRKKFFIYGFLLFIIVAAIYYYTGRGYLLVIILPILLIVGIYNASQEKHAILRNFPVLGYFRYLFEMIAPEIQQYFIERSTDGKPFSRNQRSLVYQRAKNIDSSTPFGTQLNLNTENYEGIKHSIFPAKVNEELPRVLVGGKDCKQPYSASLFNVSAMSFGSLSEHAVRAINIGAKKGNFYQNTGEGGLTDYHLEGGGDITWQIGTGYFGCRDAEGNFSPENFSAKANLPNVKMIEIKLSQGAKPGHGGVLPAKKNTEQIAKIRGVVPHTMILSPPGHHAFSDSKGLILFIKQLRDLSNGKPIGFKLCIGNTAEFEAICQEMINEDTYPDFITVDGAEGGTGAAPLEFADGVGMPFEPALIFVNKTLVRLGIRDKMRIIGSGKIISGYSILHAIALGADMCNSARGFMFSLGCIQALRCHNNECPTGVATQNKMLMKGLVVTDKSERVYHFHKNTLHAANELLAAAGKTSFADVDINIFMRGDEFTNLSELYFPDNLKNVTQFS
>NZ_CP016907.1|WP_008462511.1|257514_258297_+|NYN-domain-containing-protein
MPLSNSKDLKLAVLIDADNVPYSNVKGMMEEIAKLGTPTTKRIYADWTKPNANGWKGVLLEHAITPIQQYSYTVGKNSSDSALIIDAMDLLYSGKLDGFCIVSSDSDFTRLAVRLRESGMKVIGIGEKKTPNSFIVACDRFIYIEVLDGATQKKKPKEVVAADTKKIVEKPAEKALHKVDKQTIELIESTIEDIEDDDGWAFLGDVGNLIVKKKPEFDPRNYGYSKLTPMLKSLTDILEIDERESDKKGIKHVYVRLRFN
>NZ_CP016907.1|WP_066032278.1|256864_257314_-|Rrf2-family-transcriptional-regulator
MFSKACEYGIRASIFIATKSSKGIRVGIKDVAKEIDSPEPFTAKIMQILTKNGIIHSAKGVGGGFEVSPEASKSVKLIQIVDAIDGNKIYSGCGIGLKECSEEHPCPVHHEFKKIRGLLLEMLTKTTLEQLASDVKSGDFFLKTLNINE
>NZ_CP016907.1|WP_066032277.1|256315_256843_-|azurin
MNTKTKISVLILMGFLAVTSCGKKETAPAESTETTEASTEGEQAPTVAPAEENVLVIEGNDQMQFNTNELKAVAGKPIKLTLKHVGKIPKEAMGHNLVILQEGTDQAAFALKANDAKATDYIPESEKASIIAHTKLIGGGEEDTIEFTIDKKGSYPFICSFPGHVAMMKGVLIVE
>NZ_CP016907.1|WP_123906980.1|253988_256226_-|nitric-oxide-reductase-large-subunit
MMKREKKLWLVFALVMSVSFAVLGYYGYEIYQQAPPVPKEIVTDSGKVVFSESEIKDGQNIWQSIGGQEVGSIWGHGAYVAPDWTADWLHREAVFILDIYAKKDFNKKYEELDAEKQSSLKIRLQKDLRTNRYNADTGVLTISENRLAAIEHLSEYYKGLFTNDPQFDKLREEYAIPKNSITDVERMHKMNAFFFWATWATVTNRPDGDISYTHNWPSDELVGNKATTELLAWSGVSIILLILSVGILVFYHAKSGEEEGFPLPKEDPLIKQGKTKSMGLVTKYFWIVSLLMVLQMVFGIITAHYGVEGNGLYGIPIDKILPYAVTRTWHTQLAIFWIATAWLATGLYIAPAVSGKDPKFQCFGINFLFIALLIIVLGSMAGQWFGVMQKLNLVQNFWFGHQGYEYVDLGRFWQIFLLVGLFLWLALMIRPLLPVLKKKTEEKNLIILFLVSCTAIAMFYGAGLMWGRQTNLAIAEYWRWWVVHLWVEGFFEVFATVVIAFLFVRLGLLKTKTATLNVLFATIIFMSGGILGTFHHLYFSGTPTAIMALGATFSALEVVPLTLIGFEAYQNYKISKSTQWIADYKWPIYFMISVAFWNFLGAGIFGFIINPPIALYYVQGLNTTPLHGHTALFGVYGMLGIGLVLFVLRSLYRNVSWNTKLLKITFWSLNIGLFLMAILSLLPIGVWQAIESINHGMWYARSSELMQQPTMITLKWLRAIGDSIFGIGFITMAWFVFELTLKNKK
>NZ_CP016907.1|WP_008462503.1|265782_266562_+|carboxypeptidase-like-regulatory-domain-containing-protein
MKYFAIFFFTLFASIGFAQDTQQQPTVPQRVSGYVINDDSKQPLAGVNIINTNKVRGAKSDEKGYFEIDVQVNDTLHFSILGFQSLRIRVTNDWIKNKVTRIQLTEKAIALEEVVIAPFSLTGYLEIDSKLIPTKENYRYSISGLTQGYEAGEYAPNAFGKVLGSIFNPADMLYNFFGKNGKELKKLKEMKKDDTVRTLLESKYDRETVAVLLGVSKDEIPEIMHRCNYSDSFIQTANDLQIMDAISACYEQYKVLKRN
>NZ_CP016907.1|WP_066032285.1|266676_268137_-|aminoacyl-histidine-dipeptidase
MSQEVRNLEPKALWNKFADLNEVPRPSKKEERVIEFMKNFGNSLGLETFEDEIRNVIIRKPATPGMENRKPIVMQGHLDMVHQKNADTVFDFDTQGIDMYVDGDWVRARGTTLGADNGLGVATIMAILESKDIPHPAIEALFTVDEETGMTGALNLKGGILQGQILLNLDTEEDDEIDIGCAGGIDVTATRTYHEEEVPEGSVGYTITVKGLNGGHSGMDIHKGLGNANKIMNRLLFDGFENFGLQIAEINGGSLRNAIPRESFAKVIISQMFDEAYVYDMQEIISDIKAEYKTTEPNLTIEIVKSELSEKVMDLGVQEGIIRAIYAAQNGVYKMSADMADLVETSNNIARVVIKDGEILVGCLTRSSVESSKFDLANSLRSAFELVGCEVELSGSYPGWTPNVNSEILEVLKGIYEKQNGEQPKVVACHAGLECGILGTNYPDMDMISFGPTIHGAHSPDERASISSAQKYWKFVLEILENIPVK
>NZ_CP016907.1|WP_066032286.1|268315_269377_+|DUF3810-domain-containing-protein
MKSKYILPLFLIVQIIFYKILVYFPDFVEGFYSKNLYIRISHFSRMLLGKIPFSVGDFFYGLLIISMISWFWRIRKTWKTDWKDHLLKIVGKISIYYFLFHLLWAFNYYREPLSQKMNIKREYSDADLLAFTKKLIIKTNEIQFKITKDKNEKIQLPYSQEEVFKMNINGYDNLAREHSYFKYETLSVKKSLFSLPLTYMGFGGYLNPFTNEAQVNNLLPMYSFPLTSSHEMAHQIGFASENECNFIGVLASVKNDNLYFQYSGYSFALRYCLGIWKFKNEKIFEILKKQVNTGILKNYQESQDFWKKYDTFIDKGFHFLYDNFLKSNNQKDGMESYSRFIDLMINYYKTREL
>NZ_CP016907.1|WP_008462500.1|269530_270025_+|sigma-70-family-RNA-polymerase-sigma-factor
MSENLEQSFVAQLQANQNIIHKICRLYTAGEDAHKDLFQEITIQLWKAYPKFRGDSKFSTWTYRVALNTAITLYRKTKRTISTVDYENHQHFVKDVDYNYEEEEQIKLMYKAVYQLNDIEKALVFMYLEDKDYQEIAETLGISEVNARVKMNRIKGKLKKILNP
>NZ_CP016907.1|WP_008462499.1|270032_270665_+|hypothetical-protein
MKELDLLKKDWQKNSDSFQQISENEIYKMIHRKSSSIVKWILIISILEISFWTFSNLFINTDDVLHKMNHPEIVTALEFLTYFNYVVVLIFVYIFYKNYKTISTTIATKSLMSAILRTRKTVQYYVWYNLGMIVITAILSFFIAFVYNPDMEFLREKLAMNGKAMFVTIGILFLVILGFFGLFWCFYRIIYGTLLRRLYANYKELKKIDF
>NZ_CP016907.1|WP_008462498.1|270903_271713_-|1-acyl-sn-glycerol-3-phosphate-acyltransferase
MGLFKRNPFGHILFIKKWLIRVLGAMTHKRYRGFNELQIEGSEIIKTLPDTNVLFISNHQTYFADVVAMFHVFNASLSGRQDTIKNIGYLWQPKMNIYYVAAKETMQAGLLPRILAYVGAITVERTWRSKGVDVTEKREVNPNDTENIRIALEDGWVITFPQGTTKSFKPVRKGTAHIIKQHKPIVIPIVIDGFRRSFDKKGLRMKKKGILQSFIIKEPLDIDYENDTIEQIVEKVEYAIEQHPSFLKVIPAEEIKAQEELNKMRQWDY
>NZ_CP016907.1|WP_066032287.1|271845_272490_-|CoA-pyrophosphatase
MNFQDFLKYVPNIIPVELPAVTSHLKMAPKERIEGLKNLDIEALNARMAGVMMLFYPKQGKTHLVLIVRNAYDGVHSAQIAFPGGKYEKEDLNFETTALRETHEEVGITSDKIDIVKHFSPMYIPPSNFLVHPFLGIAKEELSFYPDIREVAGIIELPLSVFLNDDIIIEARLSTSYGANILVPAFNIQNHVVWGATAMILSELRDVLKEAMVK
>NZ_CP016907.1|WP_066032288.1|272581_273019_+|DUF4268-domain-containing-protein
MYSKEESQRIKREFWVTFAEKYPRKWVLYDTKIKDFSFKFYVDNKKAQVLIDIEHRSDEKRIAYFEKLEALKNILEEEFIKDLVFEKNYTLENGKTISRIWVEKTGVGFSNKNTWDAIFDFFNENMHALEMFYLEYDEFIKDVEN
>NZ_CP016907.1|WP_066032289.1|273159_273570_-|hypothetical-protein
MNSIRPYILLLFLTFGLQELQSQSYHFKTSGFSVLEKNERGKWGEWSNLDLVNLSVVLDTNKHRIVVYSQEIQLYNILDYIEREENDTDIVYSFICKDNDGKECKLSIITRKKQDYRKQLYINYDDHIIVYNIITV
>NZ_CP016907.1|WP_066032290.1|273590_274535_-|2-nitropropane-dioxygenase
MNKITQLFNIKYPIIQGGMIWNSGYKLASAVSNAGGLGLIGAGSMYPEVLREHIQKCKKATDKPFGVNIPMLYPNIEEIMNIVVEEGVKIVFTSAGNPKTWTSFLKERGVTVVHVVSSSVFALKAQDACVDAVVAEGFEAGGHNGREETTTLTLIPMVKEKIKIPLIAAGGIATGRGMLAAMILGADGVQVGSRFAASIESSSHNNFKETIVNTLEGGTQLTLKELAPVRLIKNKFYQDVQDLYQKCPSKEELVQLLGRARAKKGMFEGDLEEGELEIGQVAGLIHEILPVEEIIQQMIAEFETASKEKTTFEF

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Crispr_ID: NZ_CP016907_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP016907_2

1644268-1644605

Unclear

Consensus_repeat	Method
ATGTTTCTAAAAATATAGCTTTA	CRISPRCasFinder

5 spacers

cas3

The CRISPR arrays of NZ_CP016907_2

>merge|NZ_CP016907|2|1644268-1644605|CRISPRCasFinder
ATCTTTCTAATAATATTGCTTTAGAAGATTTATCTATAGGCGATAATCAGTTAACAGCTTTAGATGTTTCTAAAAATATAGCTTTAAAAAGTCTCTACTTTCACAACAACCAACTAGACAGTATAAATGTTTCTAAAAATACAGCTTTACGATGGTTATATATGACTGGAAATAAGGTAAAAGATTTAAACGTTTCAAAAAATACTGCTTTAGTGCACTTAACCTGTAGTTCCAATTTATTAACTACCCTTGATCTTTCTCAAAATAAAGCTCTTGAAGATTTAATCTGCGATCATAATCAATTGACAGAATTAGATATTTCTAAAAATATTTTACTA

>NZ_CP016907|2|2|1644268-1644605|CRISPRCasFinder
ATCTTTCTAATAATATTGCTTTA	GAAGATTTATCTATAGGCGATAATCAGTTAACAGCTTTAG
ATGTTTCTAAAAATATAGCTTTA	AAAAGTCTCTACTTTCACAACAACCAACTAGACAGTATAA
ATGTTTCTAAAAATACAGCTTTA	CGATGGTTATATATGACTGGAAATAAGGTAAAAGATTTAA
ACGTTTCAAAAAATACTGCTTTA	GTGCACTTAACCTGTAGTTCCAATTTATTAACTACCCTTG
ATCTTTCTCAAAATAAAGCTCTT	GAAGATTTAATCTGCGATCATAATCAATTGACAGAATTAG
ATATTTCTAAAAATATTTTACTA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP016907.1\|WP_066033084.1\|1645861_1646719_-\|MBL-fold-metallo-hydrolase	unknown	unknown	gnl\|CDD\|293839
NZ_CP016907.1\|WP_008466068.1\|1650843_1652160_+\|Fe-S-cluster-assembly-protein-SufD	unknown	unknown	gnl\|CDD\|376550
NZ_CP016907.1\|WP_008466089.1\|1628872_1629244_+\|YraN-family-protein	unknown	unknown	gnl\|CDD\|184791
NZ_CP016907.1\|WP_066033083.1\|1638508_1640143_-\|S8-family-serine-peptidase	unknown	unknown	gnl\|CDD\|173809
NZ_CP016907.1\|WP_066033080.1\|1631260_1634626_-\|transcription-repair-coupling-factor	cas3	cd09639_cas3_CAS-I	gnl\|CDD\|224118
NZ_CP016907.1\|WP_008466070.1\|1650030_1650777_+\|Fe-S-cluster-assembly-ATPase-SufC	unknown	unknown	gnl\|CDD\|273907
NZ_CP016907.1\|WP_008466087.1\|1629368_1630025_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP016907.1\|WP_035691498.1\|1655235_1655661_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP016907.1\|WP_066033087.1\|1655663_1656089_+\|SufE-family-protein	unknown	unknown	gnl\|CDD\|376883
NZ_CP016907.1\|WP_008466071.1\|1648461_1649910_+\|Fe-S-cluster-assembly-protein-SufB	unknown	unknown	gnl\|CDD\|236990
NZ_CP016907.1\|WP_066033078.1\|1626533_1627625_-\|endonuclease	unknown	unknown	gnl\|CDD\|197338
NZ_CP016907.1\|WP_066033085.1\|1652438_1653788_-\|serine-hydrolase	unknown	unknown	gnl\|CDD\|224594
NZ_CP016907.1\|WP_066033081.1\|1634618_1635227_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|235549
NZ_CP016907.1\|WP_008466073.1\|1648046_1648376_+\|iron-sulfur-cluster-assembly-accessory-protein	unknown	unknown	gnl\|CDD\|223393
NZ_CP016907.1\|WP_008466080.1\|1635549_1636488_+\|L-threonine-3-dehydrogenase	unknown	unknown	gnl\|CDD\|187580
NZ_CP016907.1\|WP_008466074.1\|1646793_1647714_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|274008
NZ_CP016907.1\|WP_066033082.1\|1636563_1638444_-\|M1-family-metallopeptidase	unknown	unknown	gnl\|CDD\|341067
NZ_CP016907.1\|WP_066033079.1\|1630530_1631085_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP016907.1\|WP_066033086.1\|1654006_1655221_+\|cysteine-desulfurase	unknown	unknown	gnl\|CDD\|99746
NZ_CP016907.1\|WP_066035114.1\|1627854_1628754_+\|LD-carboxypeptidase	unknown	unknown	gnl\|CDD\|132882

Protein	Function_ID	Function_description	E-value
NZ_CP016907.1\|WP_066033084.1\|1645861_1646719_-\|MBL-fold-metallo-hydrolase	gnl\|CDD\|293839	cd16281, metallo-hydrolase-like_MBL-fold, uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain. Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.	5.0418e-152
NZ_CP016907.1\|WP_008466068.1\|1650843_1652160_+\|Fe-S-cluster-assembly-protein-SufD	gnl\|CDD\|376550	pfam01458, UPF0051, Uncharacterized protein family (UPF0051).	1.88262e-95
NZ_CP016907.1\|WP_008466089.1\|1628872_1629244_+\|YraN-family-protein	gnl\|CDD\|184791	PRK14686, PRK14686, hypothetical protein; Provisional.	2.15594e-60
NZ_CP016907.1\|WP_066033083.1\|1638508_1640143_-\|S8-family-serine-peptidase	gnl\|CDD\|173809	cd07483, Peptidases_S8_Subtilisin_Novo-like, Peptidase S8 family domain in Subtilisin_Novo-like proteins. Subtilisins are a group of alkaline proteinases originating from different strains of Bacillus subtilis. Novo is one of the strains that produced enzymes belonging to this group. The enzymes obtained from the Novo and BPN' strains are identical. The Carlsburg and Novo subtilisins are thought to have arisen from a common ancestral protein. They have similar peptidase and esterase activities, pH profiles, catalyze transesterification reactions, and are both inhibited by diispropyl fluorophosphate, though they differ in 85 positions in the amino acid sequence. Members of the peptidases S8 and S35 clan include endopeptidases, exopeptidases and also a tripeptidyl-peptidase. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin.. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.	7.83637e-121
NZ_CP016907.1\|WP_008466070.1\|1650030_1650777_+\|Fe-S-cluster-assembly-ATPase-SufC	gnl\|CDD\|273907	TIGR01978, Probable_ATP-dependent_transporter_SufC, FeS assembly ATPase SufC. SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other].	6.00273e-143
NZ_CP016907.1\|WP_066033087.1\|1655663_1656089_+\|SufE-family-protein	gnl\|CDD\|376883	pfam02657, SufE, Fe-S metabolism associated domain. This family consists of the SufE-related proteins. These have been implicated in Fe-S metabolism and export).	1.62387e-65
NZ_CP016907.1\|WP_008466071.1\|1648461_1649910_+\|Fe-S-cluster-assembly-protein-SufB	gnl\|CDD\|236990	PRK11814, PRK11814, cysteine desulfurase activator complex subunit SufB; Provisional.	0
NZ_CP016907.1\|WP_066033078.1\|1626533_1627625_-\|endonuclease	gnl\|CDD\|197338	cd10283, MnuA_DNase1-like, Mycoplasma pulmonis MnuA nuclease-like. This subfamily includes Mycoplasma pulmonis MnuA, a membrane-associated nuclease related to Deoxyribonuclease 1 (DNase1 or DNase I, EC 3.1.21.1). The in vivo role of MnuA is as yet undetermined. This subfamily belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds.	1.13047e-06
NZ_CP016907.1\|WP_066033085.1\|1652438_1653788_-\|serine-hydrolase	gnl\|CDD\|224594	COG1680, AmpC, Beta-lactamase class C and other penicillin binding proteins [Defense mechanisms].	8.82527e-34
NZ_CP016907.1\|WP_066033081.1\|1634618_1635227_-\|hypothetical-protein	gnl\|CDD\|235549	PRK05658, PRK05658, RNA polymerase sigma factor RpoD; Validated.	0.00869795
NZ_CP016907.1\|WP_008466073.1\|1648046_1648376_+\|iron-sulfur-cluster-assembly-accessory-protein	gnl\|CDD\|223393	COG0316, sufA, Fe-S cluster assembly scaffold protein [Posttranslational modification, protein turnover, chaperones].	9.50704e-34
NZ_CP016907.1\|WP_008466080.1\|1635549_1636488_+\|L-threonine-3-dehydrogenase	gnl\|CDD\|187580	cd05272, TDH_SDR_e, L-threonine dehydrogenase, extended (e) SDRs. This subgroup contains members identified as L-threonine dehydrogenase (TDH). TDH catalyzes the zinc-dependent formation of 2-amino-3-ketobutyrate from L-threonine via NAD(H)-dependent oxidation. This group is distinct from TDHs that are members of the medium chain dehydrogenase/reductase family. This group has the NAD-binding motif and active site tetrad of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.	0
NZ_CP016907.1\|WP_008466074.1\|1646793_1647714_-\|hypothetical-protein	gnl\|CDD\|274008	TIGR02168, Chromosome_partition_protein_Smc, chromosome segregation protein SMC, common bacterial type. SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins].	6.4123e-05
NZ_CP016907.1\|WP_066033082.1\|1636563_1638444_-\|M1-family-metallopeptidase	gnl\|CDD\|341067	cd09604, M1_APN_like, Peptidase M1 family similar to aminopeptidase N catalytic domain. This family contains bacterial M1 peptidases with smilarity to the catalytic domain of aminopeptidase N (APN; CD13; alanyl aminopeptidase; EC 3.4.11.2), a type II integral membrane protease belonging to the M1 gluzincin family. APN preferentially cleaves neutral amino acids from the N-terminus of oligopeptides and, in higher eukaryotes, is present in a variety of human tissues and cell types (leukocyte, fibroblast, endothelial and epithelial cells). APN expression is dysregulated in inflammatory diseases such as chronic pain, rheumatoid arthritis, multiple sclerosis, systemic sclerosis, systemic lupus erythematosus, polymyositis/dermatomyosytis and pulmonary sarcoidosis, and is enhanced in tumor cells such as melanoma, renal, prostate, pancreas, colon, gastric and thyroid cancers. It is predominantly expressed on stem cells and on cells of the granulocytic and monocytic lineages at distinct stages of differentiation, thus considered a marker of differentiation. Thus, APN inhibition may lead to the development of anti-cancer and anti-inflammatory drugs. APNs are also present in many pathogenic bacteria and represent potential drug targets. Some APNs have been used commercially, such as one from Lactococcus lactis used in the food industry. APN also serves as a receptor for coronaviruses, although the virus receptor interaction site seems to be distinct from the enzymatic site and aminopeptidase activity is not necessary for viral infection. APNs have also been extensively studied as putative Cry toxin receptors. Cry1 proteins are pore-forming toxins that bind to the midgut epithelial cell membrane of susceptible insect larvae, causing extensive damage. Several different toxins, including Cry1Aa, Cry1Ab, Cry1Ac, Cry1Ba, Cry1Ca and Cry1Fa, have been shown to bind to APNs; however, a direct role of APN in cytotoxicity has been yet to be firmly established.	5.97326e-146
NZ_CP016907.1\|WP_066033080.1\|1631260_1634626_-\|transcription-repair-coupling-factor	gnl\|CDD\|224118	COG1197, Mfd, Transcription-repair coupling factor (superfamily II helicase) [DNA replication, recombination, and repair / Transcription].	0
NZ_CP016907.1\|WP_066033086.1\|1654006_1655221_+\|cysteine-desulfurase	gnl\|CDD\|99746	cd06453, SufS_like, Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to cysteine desulfurase (SufS) and selenocysteine lyase. SufS catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine; and selenocysteine lyase catalyzes the decomposition of L-selenocysteine.	0
NZ_CP016907.1\|WP_066035114.1\|1627854_1628754_+\|LD-carboxypeptidase	gnl\|CDD\|132882	cd07025, Peptidase_S66, LD-Carboxypeptidase, a serine protease, includes microcin C7 self immunity protein. LD-carboxypeptidase (Muramoyltetrapeptide carboxypeptidase; EC 3.4.17.13; Merops family S66; initially described as Carboxypeptidase II) family also includes the microcin c7 self-immunity protein (MccF) as well as uncharacterized proteins including hypothetical proteins. LD-carboxypeptidase hydrolyzes the amide bond that links the dibasic amino acids to C-terminal D-amino acids. The physiological substrates of LD-carboxypeptidase are tetrapeptide fragments (such as UDP-MurNAc-tetrapeptides) that are produced when bacterial cell walls are degraded; they contain an L-configured residue (L-lysine or meso-diaminopimelic acid residue) as the penultimate residue and D-alanine as the ultimate residue. A possible role of LD-carboxypeptidase is in peptidoglycan recycling whereby the resulting tripeptide (precursor for murein synthesis) can be reconverted into peptidoglycan by attachment of preformed D-Ala-D-Ala dipeptides. Some enzymes possessing LD-carboxypeptidase activity also act as LD-transpeptidase by replacing the terminal D-Ala with another D-amino acid. MccF contributes to self-immunity towards microcin C7 (MccC7), a ribosomally encoded peptide antibiotic that contains a phosphoramidate linkage to adenosine monophosphate at its C-terminus. Its possible biological role is to defend producer cells against exogenous microcin from re-entering after having been exported. It is suggested that MccF is involved in microcin degradation or sequestration in the periplasm.	1.04857e-107

>NZ_CP016907.1|WP_066033083.1|1638508_1640143_-|S8-family-serine-peptidase
MSHIKPLKLSAFALLVLAGCSATVQAQVSTSKEFITAPAAVVKKAPLSENELKRWSHLDLIKDSIPGMSVDKAYAELLQGKKGQKVIVGVVDSGVDIEHEDLQGMIWTNKKEIPGNGIDDDKNGFIDDIHGWNFLGDAVHENLEMTRIVKKADDGSPEYKAALAQYTEKYEKALKDKQQVDFLLEVHNTIKKELNKSTYKIEDLSAITSTDPKVARSKAIMTQIFTNAGPTFDPEADFGEYKEQVDDQLNYNLNKEYDGRKIVGDNPEDIKNNRYGNNVVFGPDKEKALHGTHVAGIIAQVRGNNLGGDGVANNVEILTVRAVPDGDEYDKDIALAIRYAVDNGAKVINGSFGKSFSPHKQWVYDAIAYAAKKDVLIVHAAGNDGYNIDEAKNINYPNDSKDNVKEFADNLITIGAINKSYGENVVAPFSNFGKINVDVFAPGEEIYATVPNNKYKYLQGTSMASPNAAGVAALIRSYYPKLKAAQVKKILMDSGVALPSMVVLGESENPGESPKAVSSVESSKTAKMVNAYNALLMAEKMSKK
>NZ_CP016907.1|WP_066033082.1|1636563_1638444_-|M1-family-metallopeptidase
MRKIILLSFLSLGFNSAFAQSAPYWQQHADYKMEVSMDVKNYQYKGKQELVYTNNSSDTLKKVFYHLYPNAFQPGSEMDARLHFIKDPDGRMVNKVKQADGKEVKQSRIETLKPNEVGYLKIANFKQDGVTAQTRVSGTILEVTLAKPILPNSKTTFTLDFDGQVPVQIRRSGRNNSEGVELSMSQWYPKLAEFDFEGWHADPYIAREFHGVWGNFDVKITIDKDYTIGGSGYLQDKNSIGHGYQDAGVTVAYPKKAKTLTWHFIAPNVHDFTWAADKEYTHDIVKGPNDVDLHFFYKNNEKTTANWKQLEPLMVKVMEYYNQRVGAYPYKQYSFIQGGDGGMEYAMCTLMLGNGTLEGILGTATHELGHSWFQHILASNESKHPWMDEGFTTYIEDSALNELKGDKKEVNPFVGNYKAYYSLVNSGKEQPQTTHGDRYDENRPYSISSYIKGSLFLSQLEYVIGKENVDATLKRYFNDFKFKHPTPNDIKRTAERVSGAELDWYLIDWTQTTNTIDYGIKDVADNAGKTTISLERIGRMPMPIDLKVEYTDGTSETFYIPLRMMNFVKPNPNPNEKRTVLEDWAWAQQNYSFTIDKNKTSIKKITIDPSGLMADVKQTNNVFEVK
>NZ_CP016907.1|WP_008466080.1|1635549_1636488_+|L-threonine-3-dehydrogenase
MNPKILIIGACGQIGTELTQKLRKLYGTDNVIASDIRKLNTDVVNSGPFEVVNALDFNQIEHLVEVHKITDVYLMAALLSATAEKNPAFAWDLNMNSLFHVLNLAKAKKIQKIFWPSSIAVFGPTTPKENTPQYTIMEPSTVYGISKQSGERWCEYYHNVYGVDVRSIRYPGLISWSTPPGGGTTDYAVDIFYKAIADKKYECFLSSETKMPMMYMDDAIDATINIMKAPAEEIKIHSSYNLAAMSFTPTEIAAEIKKHIPEFEITYNPDFRQKIADSWPASIDDAEARKDWGWNHKFDLETMTKDMLEHLS
>NZ_CP016907.1|WP_066033081.1|1634618_1635227_-|hypothetical-protein
MKYQISLFLLLTTVLFSCQNENEKRLAENAKEAKKKEAIFNNINKGWTFLDEPINEISESQLNSWTEWREFIKEIGEKPRKTIGAFQKKSAAISKKAMALNNNIPAQFNQPQIKSRISILITKIRMLDLFIHLNNIPDDKVVFLIQEINKELISLERQMDKIVEKAKIPKEEGEEDFLRMLDTTRAIPNSAPPIDPNIPKVE
>NZ_CP016907.1|WP_066033080.1|1631260_1634626_-|transcription-repair-coupling-factor
MSKNALYTTYDNLPKAEQIAKSLLEGNQVKMNISGLLGSAVSFIIRSVFRKTELPFLIVLDNKEEAAYYLNDLEQMIGEQDVLFYPASFRRPYQIDETDNANVLLRAEVLNRINSRKKPAVIVTYPEALFEKVVTRRELDKNTLKVALNDKISIDFINEVLFEYEFKRVDFITEPGEFSVRGGIVDVFSFSNDHPYRIEFFGNEVDSIRTFDVETQLSVETHKKITIIPNVENKLFQENRESFLDYIAEKTVLFIQNTEGLFSQLDKQFARAEEAFEKLSKEIKHATPEQLFLNQASFIKRALDFSVVELASRPVFKTTKKFEFHIQPQPSFNKQFDLLLNNLSDNHFNGYVNYLFCSNETQAKRFHDIFESLDEANSENIRKQYHTIVLPLYQGFIDEENQITAYTDHQIFERYHKFNIKNGYSKKQNITLKELTALSVGDYVTHIDHGIGKFGGLQKIQVEGKTQEAIKLVYADNDIVYVSIHSLHKISKYNGKDGTPPKIYKLGSNAWKVLKQKTKARVKHIAFNLIQLYAKRRLEKGFQFAPDSYLQNELESSFIYEDTPDQMKSTAEVKADMESDRPMDRLVCGDVGFGKTEVAIRAAFKAVDNSKQVAVLVPTTILAYQHYRTFSERLKDMPVSIGYLNRFRTAKQKAQTLKDLAEGKLDIVIGTHQLVNKNVVFKDLGLLIVDEEQKFGVNVKDKLKTIAANVDTLTLTATPIPRTLQFSLMAARDLSVITTPPPNRYPIETNVVGFNEEIIRDAISYEIQRNGQVFFINNRIENIKEVAGMIQRLVPNARVGIGHGQMDGAKLEELMLGFMNGDFDVLVATTIIESGLDVPNANTIFINNANNFGLSDLHQMRGRVGRSNKKAFCYFICPPYSSMTEDARKRIQALEQFSELGSGFNIAMKDLEIRGAGDLLGGEQSGFINEIGFDTYQKIMNEAIEELKENEFKELYPEENDIDTKEYVKDIQIDADFELLFPDEYINNVSERLVLYNELGAIKDEAGLQEFEKKLIDRFGPLPKQAVALLNSIRIKWIATKVGIEKLVLKQGKMIGYFVSDQQSDYYQSVKFRNVLNFVQKHATLCKMKEKQTVNGLRLLLTFENVKSIKRAFELMELFEE
>NZ_CP016907.1|WP_066033079.1|1630530_1631085_-|hypothetical-protein
MQNQLILLFLFLGFTTIFAQGKDKIVLKDSLKSETIDPLRPAKAAFYSAVLPGLGQIYNKKYWKIPLVYGAIGTCTYFYIDNQKKYNLYRDEYKNRLEGKKSDSEFLARLSESQLTTAQKEYQRYRDLSALFIVGFYVLNIIDANIDAALSQFNVDERLAFKPAVIKNDITLNTNFGFALNYSF
>NZ_CP016907.1|WP_008466087.1|1629368_1630025_+|hypothetical-protein
MKTVSSIVENYIKTKPFLLNALSLGIINLTSLSRNIMTELESEFGKEVKQGAVVMSLKRLTEELDFKLNHKINKVIKNIGEITVRSELTDYTFAASETVLNKQADLISDINALSDIFYTSSRGVNETNIVVSSSVNHLVEKHFMREKLIQKLDNLASITVKLPKENIVVPGIYYFIFQRLAWEGIIINEVISTSNEFTILVGEDQVDVAFKVIKDLKN
>NZ_CP016907.1|WP_008466089.1|1628872_1629244_+|YraN-family-protein
MAEHNDLGKLGEDLAAAYLEENGYSIVERNFVIQKAEIDIIAQKDSILAIIEVKTRSSLDFGSPQDFVKQKKIQLLIKAVNAYINDREKDFQEDLEIRFDIIAVHKNGESFAIEHLTDAFYHF
>NZ_CP016907.1|WP_066035114.1|1627854_1628754_+|LD-carboxypeptidase
MITPPYLQKGDTVALLATARKNIDDNLKPTIDLLHSWGLEAVIGSTIGLDYHQLAGTDEQRAADFQKQLDNPNIKAIWCVRGGYGTVRMLDLLDFTKFKQHPKWVIGFSDVTVLHNHLNTMGYKSIHGIMPVTVPRATPDAVSSLKSALFNEPISYSISPSPMNRLGSATGELVGGNLSILYSLLGSPSAIDCKDKILFIEDLDEYLYHIDRMMMNLKRNGCIENLKGIIIGGMTSMKDNEVPWGKNALEIIDDVTKKYNIPVIFNFPAGHIRDNRALIMGNIVTMEVTASGSTVTFKK
>NZ_CP016907.1|WP_066033078.1|1626533_1627625_-|endonuclease
MHFFRAFLIVLFFSIQTQSQSKKYKIHTVAFYNFENLYDTVDDIFTNDDEWTPNGAQHWTTEKYQQKLKNLARVLSEIGAPENSNAPTLIGGAEIENRGVLEDLIKEPKLQSLDLGIIHFDSPDKRGIDVALLYQKKYFRPTSYSNIPLIIYKKEIPQKEETEVVDDEIEAKKESKNRVFTRDQLLVSGFLENEEIHIIVNHWPSRSGGEKATSLFREAAGKLNRKIIDSLQRINPQAKVLTMGDFNDGPFNKSIKVGLGAKSLKTEVAEFDVFNPFEELANKGLGTIAYRDSWNIFDQIIMTASLVKSDFSSFNFWKAGIFSRPYLIQNSGAYKGYPLRNTLSEAGFSDHLPVYVYLIKEFK
>NZ_CP016907.1|WP_066033084.1|1645861_1646719_-|MBL-fold-metallo-hydrolase
MKLYPIESGNFKLDGGAMFGVVPKTIWNKTNPADANNLIDIAARCLLIEDGNRLILIDTGMGDKQSEKFFGYYSLWGSHSLDKSLAKYGFNRDDITDVFMTHLHFDHCGGSVQWNADRTGYEPAFKNAKFWTNENHWEWATKPNAREKASFLSENILPMQESGQLHFIERPESDFGFSKELNFDIYYVDGHTEKQMIPYIKYQDKTIVFCADLLATAGHIPLPYVMGYDTRPLLTMPEKSKFLNLAADQNHYLFLEHDAHNQIITVEHTEKGVRLKDVFTCEEIL
>NZ_CP016907.1|WP_008466074.1|1646793_1647714_-|hypothetical-protein
MKKQNEIKWFKPMFAIIFVLGVGAVVWVFSSEPDKNNSEVKEESIANTISFESKETSEQKNILDSLNTLKNAYDQAILEKTALSKELELERKNVENLVAIIKASNNPSAEQIRVYRNQLSDLNASLENRVQEIKKLKSQNKNLLTEIETQNVVMYKQKLENDTLVSKQKKLESTLKDASKLYLSNFKAVALREKSSGAELETTKAKNTKKLKISFTVNGNAVAKTGKRVFYVQVLDQKNTVLGDNKLIEFGNDKALVYSFIVSTDFQGKSVNAYGILNADQFKKGTYFVNYFDKQEIMGSTSVTLE
>NZ_CP016907.1|WP_008466073.1|1648046_1648376_+|iron-sulfur-cluster-assembly-accessory-protein
MIKVSDTAKKKIIDLMKDDGFDAAHDYVRVGVKSGGCSGLSYELKFDKTKNDDDKIFVDNDISIAVEKKSFLYLAGTILEFSGGLNGKGFVFNNPNASRTCGCGESFSL
>NZ_CP016907.1|WP_008466071.1|1648461_1649910_+|Fe-S-cluster-assembly-protein-SufB
MSKYTEDDLKIELETKEYEYGFYTNIESETFPIGLNEEIVRAISLKKEEPEWMTEWRIEAFRAWKEMIEPEWANVSYEKPDFQAISYYSAPKQVDPNKTLDDVDPELLEMYKKLGISIDEQKKMNNIAMDIVVDSVSVATTFKKTLAEKGIIFCPISEAIKEHPELVKKYLGTVVPQKDNFYAALNSAVFSDGSFCYIPKGVKCPMELSTYFRINQAGTGQFERTLVIADEGSYVSYLEGCTAPSRDENQLHAAVVELIALDDAEIKYSTVQNWFPGNKEGKGGVYNFVTKRGLCETNAKISWTQVETGSAVTWKYPSCVLKGDNSVGEFYSIAVTNNFQQADTGTKMIHLGKNTKSTIISKGISAGKSQNSYRGLVQISPRAENARNFSQCDSLLMGNNCGAHTFPYIESKNPTAKIEHEATTSKIGEDQVFYCNQRGIPTEKAIALIVNGFSKDVLNKLPMEFAVEAQKLLEISLEGSVG
>NZ_CP016907.1|WP_008466070.1|1650030_1650777_+|Fe-S-cluster-assembly-ATPase-SufC
MLSIKNLHAAIGDKEILKGINIEVKAGEVHAIMGPNGSGKSTLSAVIAGNENYEVTDGEVILDGEDLADLAPEERAHKGVFLSFQYPVEIPGVSVTNFMKTAINETRKANGQEEMPANEMLKVIREKSELLEIDRKFLSRSLNEGFSGGEKKRNEIFQMAMLEPKLAILDETDSGLDIDALRIVANGVNKLKSDKNAIIVITHYQRLLDYIVPDFVHVLYNGRIVKSGGKELAYELEEKGYDWIKAEN
>NZ_CP016907.1|WP_008466068.1|1650843_1652160_+|Fe-S-cluster-assembly-protein-SufD
MDLKEKLVSSFMAFEERVDVHSDLHDIRTNALKNFENKGFPTKKEEAWKYTSLNAILKNDFTVFPKQENAIEFNQVKKYFLHEIDTYKLVFIDGVFSSHLSSTTHDGIDVCLMSSALTKPKYKMVIDTYFNQIASKDDSLTSLNTAFAIEGAFINIPKKKVADKPIEIMYFSTGNEAALMVQPRNLVIVGENSHVQIIERHQSLNENPVLTNSVTEIFAQKRAIVDYYKIQNDNNEANLIDNTYVSQQQESHASVHTFSFGGNLTRNNLNFYHFGERLTSTLNGISILNDKQHVDHYTLVNHATPNCESFQDYKGIFSDRSTGVFNGKVLVEKEAQKTNAFQKSNNILLSDKATINAKPQLEIFADDVKCSHGCTVGQLDETAMFYMQSRGIPKKEAKALLMYAFSNAVIESIKIPELKQRITKIIAMKLGVNLGFDL
>NZ_CP016907.1|WP_066033085.1|1652438_1653788_-|serine-hydrolase
MKKFLKVLLLVLVLAFLYFGFTTYPKLDLISGFSAKSVASGHFIDNRPLDLIQKTDNDINLVDLAKNSIDDAGKFAISSVYGLKERKAIYREGLGATLINDDFDITKPYLLPKRTKLENNLPFPYGNNEPKDSTFANIDYSKLKKAVDDAFDKTGGRIKRTRAVVVLYKDYLIAEKYDTGFNKDSKILGWSMTKSITSSAFGVLAKQGKIDIYKPAPVVEWQNDERKNITLNDLLHMNSGLEWEENYSTICDATKMLFQAEDMGKVQLEKPAQFKPNTHWNYSSGTTNLLSLILRRHFKTQQEYLDFWYSAVIDKIGMNSMIVEQDMSGTFVGSSYGWATPRDWSKFGLLYLRKGNWNGEQILDESWVKYTATPTNTSEGKYGAQFWLNAGGKFPDVPRDMFYCSGYQGQMVAIIPSKDMVIVRMGVREEEPGFDFNGFLKGIISSVKK
>NZ_CP016907.1|WP_066033086.1|1654006_1655221_+|cysteine-desulfurase
MLDIQKIRADFPILSQTVNGKPLVYFDNGATSQKPQVVIDAEVKYYNEINANIHRGVHTLSQLATDAYEVARGKVKDHINAKHAHEVLFTSGTTHGINLVANGFASILKPGDEVVVSSLEHHSNIVPWQMLCEKTGAILKVIPIDENGELIIEEFDKLLSDKTKIVTVNHISNALGVINPIKYIIDKAHAIGAAVLIDGAQAVPHLKPDVQELDCDFYAFSGHKMCGPTGTGILYGKEAWLNKLPPYQGGGEMIKEVTFEKTTYADLPHKFEAGTPNIAGGIVLGTAIDYLNSVGFENIQAYEHELLEHATKRLNEIEGIRIYGNTKNKASVVSFNIDGIHPYDVGSIIDKLGIAVRTGHHCAQPIMNFFCIPGTIRASFSFYNTKEEIDQMVGAVKKAQTMLS
>NZ_CP016907.1|WP_035691498.1|1655235_1655661_+|hypothetical-protein
MRIVSLLLLTLFIATGCCSQKKADMKSTQIEYSAMSRGYYKSIVVQNKSVSVVKERNAEAVKSNIDDAKWNKIVDAYSKVNLESLSSLKAPTDKRTYDGAAIGNLKITKDGKTYETAGFDNGFPPKEIEKLVNLLVDFAKE
>NZ_CP016907.1|WP_066033087.1|1655663_1656089_+|SufE-family-protein
MTIKEIQDEIIDEFSMFDDWMQRYEYIIELGKSLPLIKEEYKTDNNLIKGCQSKVWLQGEEQDDKIVFTADSDAILTKGIIAILIRAFSNQKAKDILEADTDFIDEIGLKEHLSATRANGLVSMIKNIKMYALAFDAKNKN

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Crispr_ID: NZ_CP016907_3

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP016907_3

1782441-1782559

Orphan

Consensus_repeat	Method
AAGGGATTGATTCAGCTGTATTGTAACCCT	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP016907_3

>merge|NZ_CP016907|3|1782441-1782559|CRISPRCasFinder
AAGGGATTGATTCAGCTGTATTGTAACCCTAATAAAAACAGAGCACTGGGACTAATAAAGCTTGTTTGTTCCCATAAAAGACAAAGCACAAGGGATTGATTCTGCTGTATTGTAACCCT

>NZ_CP016907|3|3|1782441-1782559|CRISPRCasFinder
AAGGGATTGATTCAGCTGTATTGTAACCCT	AATAAAAACAGAGCACTGGGACTAATAAAGCTTGTTTGTTCCCATAAAAGACAAAGCAC
AAGGGATTGATTCTGCTGTATTGTAACCCT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP016907.1\|WP_008465829.1\|1788655_1789054_-\|polymer-forming-cytoskeletal-protein	unknown	unknown	gnl\|CDD\|377376
NZ_CP016907.1\|WP_008465841.1\|1781669_1782116_-\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|366181
NZ_CP016907.1\|WP_008465834.1\|1786703_1787879_-\|F0F1-ATP-synthase-subunit-A	unknown	unknown	gnl\|CDD\|237381
NZ_CP016907.1\|WP_066033160.1\|1777170_1778529_-\|tetratricopeptide-repeat-protein	unknown	unknown	gnl\|CDD\|274350
NZ_CP016907.1\|WP_008465838.1\|1783727_1785305_-\|F0F1-ATP-synthase-subunit-alpha	unknown	unknown	gnl\|CDD\|236448
NZ_CP016907.1\|WP_008465839.1\|1782781_1783642_-\|ATP-synthase-F1-subunit-gamma	unknown	unknown	gnl\|CDD\|376304
NZ_CP016907.1\|WP_066033164.1\|1791769_1792465_-\|ABC-transporter-ATP-binding-protein	unknown	unknown	gnl\|CDD\|224054
NZ_CP016907.1\|WP_008465852.1\|1774146_1774539_-\|30S-ribosome-binding-factor-RbfA	unknown	unknown	gnl\|CDD\|376719
NZ_CP016907.1\|WP_008465836.1\|1785880_1786381_-\|F0F1-ATP-synthase-subunit-B	unknown	unknown	gnl\|CDD\|184695
NZ_CP016907.1\|WP_066033159.1\|1772945_1774145_-\|ABC-transporter-permease	unknown	unknown	gnl\|CDD\|226957
NZ_CP016907.1\|WP_008465831.1\|1788447_1788675_-\|AtpZ/AtpI-family-protein	unknown	unknown	gnl\|CDD\|378198
NZ_CP016907.1\|WP_008465851.1\|1774663_1775083_+\|CBS-domain-containing-protein	unknown	unknown	gnl\|CDD\|341361
NZ_CP016907.1\|WP_008465848.1\|1776390_1777170_-\|DUF4292-domain-containing-protein	unknown	unknown	gnl\|CDD\|372917
NZ_CP016907.1\|WP_066033161.1\|1778577_1779594_-\|nucleotidyltransferase	unknown	unknown	gnl\|CDD\|133024
NZ_CP016907.1\|WP_008465837.1\|1785342_1785876_-\|ATP-synthase-F1-subunit-delta	unknown	unknown	gnl\|CDD\|365949
NZ_CP016907.1\|WP_008465844.1\|1780112_1781573_-\|oligosaccharide-flippase-family-protein	unknown	unknown	gnl\|CDD\|240533
NZ_CP016907.1\|WP_008465850.1\|1775112_1776366_-\|peptidoglycan-DD-metalloendopeptidase-family-protein	unknown	unknown	gnl\|CDD\|227278
NZ_CP016907.1\|WP_008465835.1\|1786471_1786669_-\|ATP-synthase-F0-subunit-C	unknown	unknown	gnl\|CDD\|349414
NZ_CP016907.1\|WP_008465845.1\|1779650_1780085_-\|dUTP-diphosphatase	unknown	unknown	gnl\|CDD\|234802
NZ_CP016907.1\|WP_066033163.1\|1789066_1791679_-\|gliding-motility-protein	unknown	unknown	gnl\|CDD\|276809

Protein	Function_ID	Function_description	E-value
NZ_CP016907.1\|WP_008465829.1\|1788655_1789054_-\|polymer-forming-cytoskeletal-protein	gnl\|CDD\|377376	pfam04519, Bactofilin, Polymer-forming cytoskeletal. This is a family of bactofilins, a functionally diverse class of cytoskeletal, polymer-forming, proteins that is widely conserved among bacteria. In the example species C. crescentus, two bactofilins assemble into a membrane-associated laminar structure that shows cell-cycle-dependent polar localization and acts as a platform for the recruitment of a cell wall biosynthetic enzyme involved in polar morphogenesis. Bactofilins display distinct subcellular distributions and dynamics in different bacterial species, suggesting that they are versatile structural elements that have adopted a range of different cellular functions.	1.73393e-25
NZ_CP016907.1\|WP_008465841.1\|1781669_1782116_-\|GNAT-family-N-acetyltransferase	gnl\|CDD\|366181	pfam00583, Acetyltransf_1, Acetyltransferase (GNAT) family. This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.	3.08662e-14
NZ_CP016907.1\|WP_008465834.1\|1786703_1787879_-\|F0F1-ATP-synthase-subunit-A	gnl\|CDD\|237381	PRK13419, PRK13419, F0F1 ATP synthase subunit A; Provisional.	3.6851e-73
NZ_CP016907.1\|WP_066033160.1\|1777170_1778529_-\|tetratricopeptide-repeat-protein	gnl\|CDD\|274350	TIGR02917, TPR_domain_protein, putative PEP-CTERM system TPR-repeat lipoprotein. This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.	2.0945e-14
NZ_CP016907.1\|WP_008465838.1\|1783727_1785305_-\|F0F1-ATP-synthase-subunit-alpha	gnl\|CDD\|236448	PRK09281, PRK09281, F0F1 ATP synthase subunit alpha; Validated.	0
NZ_CP016907.1\|WP_008465839.1\|1782781_1783642_-\|ATP-synthase-F1-subunit-gamma	gnl\|CDD\|376304	pfam00231, ATP-synt, ATP synthase.	4.60203e-130
NZ_CP016907.1\|WP_066033164.1\|1791769_1792465_-\|ABC-transporter-ATP-binding-protein	gnl\|CDD\|224054	COG1131, CcmA, ABC-type multidrug transport system, ATPase component [Defense mechanisms].	1.27738e-56
NZ_CP016907.1\|WP_008465852.1\|1774146_1774539_-\|30S-ribosome-binding-factor-RbfA	gnl\|CDD\|376719	pfam02033, RBFA, Ribosome-binding factor A.	6.72625e-30
NZ_CP016907.1\|WP_008465836.1\|1785880_1786381_-\|F0F1-ATP-synthase-subunit-B	gnl\|CDD\|184695	PRK14471, PRK14471, F0F1 ATP synthase subunit B; Provisional.	2.84234e-74
NZ_CP016907.1\|WP_066033159.1\|1772945_1774145_-\|ABC-transporter-permease	gnl\|CDD\|226957	COG4591, LolE, ABC-type transport system, involved in lipoprotein release, permease component [Cell envelope biogenesis, outer membrane].	1.05292e-42
NZ_CP016907.1\|WP_008465831.1\|1788447_1788675_-\|AtpZ/AtpI-family-protein	gnl\|CDD\|378198	pfam09527, ATPase_gene1, Putative F0F1-ATPase subunit Ca2+/Mg2+ transporter. This model represents a protein found encoded in F1F0-ATPase operons in several genomes, including Methanosarcina barkeri (archaeal) and Chlorobium tepidum (bacterial). It is a small protein (about 100 amino acids) with long hydrophobic stretches and is presumed to be a subunit of the enzyme. It carries two transmembrane helices and is a magnesium or calcium uniporter. The atp operon of alkaliphilic Bacillus pseudofirmus OF4, as in most prokaryotes, contains the eight structural genes for the F-ATPase (ATP synthase), which are preceded by an atpI gene that encodes a membrane protein with 2 TMSs. A tenth gene, atpZ, has been found in this operon, which is upstream of and overlapping with atpI.	2.00978e-10
NZ_CP016907.1\|WP_008465851.1\|1774663_1775083_+\|CBS-domain-containing-protein	gnl\|CDD\|341361	cd04584, CBS_pair_AcuB_like, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ACT domain. The putative Acetoin Utilization Protein (Acub) from Vibrio Cholerae contains a CBS pair domain. The acetoin utilization protein plays a role in growth and sporulation on acetoin or butanediol for use as a carbon source. Acetoin is an important physiological metabolite excreted by many microorganisms. It is used as an external energy store by a number of fermentive bacteria. Acetoin is produced by the decarboxylation of alpha-acetolactate. Once superior carbon sources are exhausted, and the culture enters stationary phase, acetoin can be utilised in order to maintain the culture density. The conversion of acetoin into acetyl-CoA or 2,3-butanediol is catalysed by the acetoin dehydrogenase complex and acetoin reductase/2,3-butanediol dehydrogenase, respectively. Acetoin utilization proteins, acetylpolyamine amidohydrolases, and histone deacetylases are members of an ancient protein superfamily.This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the acetoin utilization proteins in bacteria. Acetoin is a product of fermentative metabolism in many prokaryotic and eukaryotic microorganisms. They produce acetoin as an external carbon storage compound and then later reuse it as a carbon and energy source during their stationary phase and sporulation. In addition these CBS domains are associated with a downstream ACT (aspartate kinase/chorismate mutase/TyrA) domain, which is linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).	2.31267e-30
NZ_CP016907.1\|WP_008465848.1\|1776390_1777170_-\|DUF4292-domain-containing-protein	gnl\|CDD\|372917	pfam14125, DUF4292, Domain of unknown function (DUF4292). This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 243 and 287 amino acids in length.	6.36963e-67
NZ_CP016907.1\|WP_066033161.1\|1778577_1779594_-\|nucleotidyltransferase	gnl\|CDD\|133024	cd04181, NTP_transferase, NTP_transferases catalyze the transfer of nucleotides onto phosphosugars. Nucleotidyltransferases transfer nucleotides onto phosphosugars. The enzyme family includes Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase. The products are activated sugars that are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides.	9.52282e-55
NZ_CP016907.1\|WP_008465837.1\|1785342_1785876_-\|ATP-synthase-F1-subunit-delta	gnl\|CDD\|365949	pfam00213, OSCP, ATP synthase delta (OSCP) subunit. The ATP D subunit from E. coli is the same as the OSCP subunit which is this family. The ATP D subunit from metazoa are found in family pfam00401.	5.51309e-48
NZ_CP016907.1\|WP_008465844.1\|1780112_1781573_-\|oligosaccharide-flippase-family-protein	gnl\|CDD\|240533	cd13128, MATE_Wzx_like, Wzx, a subfamily of the multidrug and toxic compound extrusion (MATE)-like proteins. Escherichia coli Wzx and related proteins from other gram-negative bacteria are thought to act as flippases, assisting in the membrane translocation of lipopolysaccharides including those containing O-antigens. Proteins from the MATE family are involved in exporting metabolites across the cell membrane and are often responsible for multidrug resistance (MDR).	2.84753e-32
NZ_CP016907.1\|WP_008465850.1\|1775112_1776366_-\|peptidoglycan-DD-metalloendopeptidase-family-protein	gnl\|CDD\|227278	COG4942, COG4942, Membrane-bound metallopeptidase [Cell division and chromosome partitioning].	1.41624e-25
NZ_CP016907.1\|WP_008465835.1\|1786471_1786669_-\|ATP-synthase-F0-subunit-C	gnl\|CDD\|349414	cd18121, ATP-synt_Fo_c, membrane-bound Fo complex of F-ATP synthase, subunit c. Subunit c (also called subunit 9, or proteolipid) of the Fo complex of F-ATP synthase. The F-ATP synthase (also called FoF1-ATPase) consists of two structural domains: the F1 (factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha, beta, gamma, delta, and epsilon subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons though the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Methanosarcina acetivorans.	2.58508e-09
NZ_CP016907.1\|WP_008465845.1\|1779650_1780085_-\|dUTP-diphosphatase	gnl\|CDD\|234802	PRK00601, dut, dUTP diphosphatase.	6.41387e-85
NZ_CP016907.1\|WP_066033163.1\|1789066_1791679_-\|gliding-motility-protein	gnl\|CDD\|276809	sd00006, TPR, Tetratricopeptide repeat. The Tetratricopeptide repeat (TPR) typically contains 34 amino acids and is found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans. It is present in a variety of proteins including those involved in chaperone, cell-cycle, transcription, and protein transport complexes. The number of TPR motifs varies among proteins. Those containing 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accommodate an alpha-helix of a target protein. It has been proposed that TPR proteins preferentially interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes.	0.000516921

>NZ_CP016907.1|WP_008465841.1|1781669_1782116_-|GNAT-family-N-acetyltransferase
MALQIKELTTIDEMAAQINTIRFLYPNISLEKYKSFLSEMLPHNYIQIAVFEDDICLGLTGCWSATKLWTGKYLEIDNFVVNPEYRSKGIGKMLTDYVDKKAIELNCSSIVLDAFTGNFGAHRFYYNQGYAPRGFHFVKILDEKKLTV
>NZ_CP016907.1|WP_008465844.1|1780112_1781573_-|oligosaccharide-flippase-family-protein
MGLYKNLFKQTAIYGLATVLPRMLSFLLVRLYTGILPTAEYGEVSIVLSWMVFFNVVLSYGMETAFFRFYSAEEDKKNVIATSTISIFWTSIIFLFAGLIFRNTLANLAEVDVQYITYTIWILVLDALVLIPFSKLRANQRPMVYAAIKIGNVVINLLLNIFFLIYLPKLAEASPNSIWDNLYVQNFQIAYIFIANLLASLATFIVLSPNYLSLGRKFDPVLWKKMMKYGLPILVAGLAFAVNEHFDKILLGYLLPENLAKSEVGAYSACYKLGLFMVLFATAFRLGIEPFFFSHAKNENAPQTYAVITKYFVILGSLILLGVIVFADVLKYLLLDNKSYWEAMKVVPLIILANFFLGIYNNLSVWYKLTDKTQIGAYISIVGAIVTLILNYLLIPKYSYYGSAIATISAYGSMMLISYVLGNKYYPIPYDMNKIGAYLGVSILFSIISFYGFREKYYVGIPLLLAFMYLVYHFEKDTIKGIMKRK
>NZ_CP016907.1|WP_008465845.1|1779650_1780085_-|dUTP-diphosphatase
MKIQIINKSQHDLPNYETIASAGMDLRANIIEPITLKPLERTIVKTGLFIELPIGYEAQVRPRSGLAAKKGVTVLNSPGTVDADYRGEIGVILVNLSNDDFVIENGERIAQLIIAKHERAEWIEVETLSETSRGEGGFGSTGVK
>NZ_CP016907.1|WP_066033161.1|1778577_1779594_-|nucleotidyltransferase
MKIIVPMAGRGSRLRPHTLTVPKPLIPVAGKSIVHRLVEDIVKILKEPIEEVAFILGDEAFFGDDVVASLEDLAKGLGAKASIYRQDQPLGTGHAIMCAKESLSGPAVIAYADTLIRADFELDPEADAVIWVKQVDQPEAFGVVKLNQNNEIIELVEKPKEFVSDLAVIGIYYFKEVGILRNELQNVLDNNIQNGGEYQINDGIKAMMANGKVFKTGSVDEWMDCGNKDVTVETNTRMLGFLHNDGEHLVDYGVTLENSTIIPPCYIGENVVLKNTTIGPNVSLGKGCHVSDSTIKNSLIQTYSQIKNAALDNAMIGNHVSYDGKFTSISIGDYAVLE
>NZ_CP016907.1|WP_066033160.1|1777170_1778529_-|tetratricopeptide-repeat-protein
MIKKRVFTILVFALLGTPFSVFAQTEPEDIAMATDEYQDSFYESLKQKGIENYDKAIVSLEKCIKLKPNDAVAYFELGKNYFALKEYQNAQTAFEKAAQLDPKNKWFWLGIYDVSYETKNYPLAIEIIQKIIVFDEEYKDDLISLYMITNQYDKALTAINEMNDKFGKSSDREIYKAQILSQGKYQNAEIDNLIQQIKKDPKEESNYLNLILLYSKNNENEKSLEVAKQLAKEIPNSEWGQVSLFKTYLDANQADKAIKSMNVILASSKIDSKIKHRTLNEFLIYVNKNPQYAADLEKAISYFDNDKEVDVAKEIGKFYHSKGQFENAIKYYEKDLKANSDTDLETNMLLLEAYAQAKQYEPMTKRAMMLIEVYPSQAQFYYYAGLGSNQQKQFKNAKTVLEMGLDYVVDDVKLESNFNIQLGEAYNGLGDAKKKEEYFLKANELLKKKNKI
>NZ_CP016907.1|WP_008465848.1|1776390_1777170_-|DUF4292-domain-containing-protein
MKKYISILVLSIAVISCKSKAVAVQGNTSQTIVEKEDKKVIEKHYNNKLDFSTLYIKASAKYADEKQSQNVTAEIRIEKDKQILISVRFLGITMAKALITPDAVSYYEKINSTYYEGDFTSLSKWLGTDLDYSKVQNLLVGEAFDDLRKGKYTQTIVENLFRLDEEKDANLKKTFFLDGEKYLIQKEEISQPSENRTLQIAYSDTKTFDQGILPTSIEINAVQPKGKTSINLNYNNISFNEELSFPYSVPSGYKKVTIK
>NZ_CP016907.1|WP_008465850.1|1775112_1776366_-|peptidoglycan-DD-metalloendopeptidase-family-protein
MPKFLLSLVLICATTFVWAQDSQQEKLEQRKAQIQQEIRDNEKMLQSVRKKEKSAVNEYLIQANKIKLKEKLINTTAKQERLISNDMYINQVQVNKLKKELKVLKEDYAEMILKSYKSRSEQSRAMFILSSESFLQAYKRAQYLKQYTAFRKNQGLEIQSKTAQLVEFNAKLDGQRQVKKKIIAENQKEKVTLEAEKKEQQKLVNALKKDKNKIAADIRSKQSEAKRIDRQIDRLIREAIAEANRKAAAERAKANPGSSEAKAPVSSSKIALTPEDKILAADFKANRGRLPWPVEKGFISLGYGDQPHPLHPSITVHNSGVEITTEDGASARAVFAGEVSKVIVLSPVNKAVVIQHGDYFTVYQNLSSVSVSQGDKVTTKQTIGRVRTSGDTGKTIIKFLILQNTSNNNPEGWLQSR
>NZ_CP016907.1|WP_008465851.1|1774663_1775083_+|CBS-domain-containing-protein
MKKREPISHIMTKTVVTANEKDDLKTVVEKLKANTIRHIPIVRGKEVIGIISRTDINRLTFGALFEGQDNADEAILEMLTVPQVMTSKPKTVSSDTIIRDLAEIFVKEDFHALPVVDNSELKGIVTTTDVVRYFLEQYD
>NZ_CP016907.1|WP_008465852.1|1774146_1774539_-|30S-ribosome-binding-factor-RbfA
METNRQKKIGGVLQKDLVDILQGEVRKNGITNLVISVSKVSVTTDLSIATVYLSIFPQEKAKETLEAIKTNSNLIKHDLAQRVRLQLRRVPNLVFFIDDSLDYIEKIDNALAGKENPIENRDLLEKRRKS
>NZ_CP016907.1|WP_066033159.1|1772945_1774145_-|ABC-transporter-permease
MNFPLYIAKRYIFSSSKNNAINIINRIASMGIIVGTMALFVVLSVFSGLKVFSLSFTNEIDPDLKLTSTYGKSFLITPDQEKQIKKIEGVASYTKIIEERVLFLFKDKQQVTYLKGVDSLYPVVNDIKKKLFNGQWLKPDSFQVVIGYGLAQNFSMGILDFENPLQIFAPKPGKGGIENPEEAFNKTDVLPVGIYSISEDLDSKYVFADLGLVQELLMYKHNQISGLEFKLKENADESAVKSKLNSIFKNKITLKNRAQLNESLYKMLNTENIAVYLIFTLVIIVALFNLIGALIMMILEKKGNLKTLFNLGSDIGDLRKIFLLQGTLLSVFGGLIGLVLGIILVILQQKFELIMITPTLAYPVVFTVENVIIVMTTIISLGFIASLIASSRVSKKLLD
>NZ_CP016907.1|WP_008465839.1|1782781_1783642_-|ATP-synthase-F1-subunit-gamma
MANLKEIRNRITSVSSTMQITSAMKMVSAAKLKKAQDAITAMRPYAEKLTELLQDLSATLEGEVGGDYTTQREVKKVLLVAVTSNRGLCGAFNSNIIKEIKNRTDFYAGKQVDVFAIGKKGSDALSKTHKVHGHHNAIFDHLTFENVAGIADDLTQKFLTGEYDRIELVYNQFKNAATQIVQVEQFLPLAPINTDKAATSGDYIFEPGKEEIVLALIPKSLKTQLYKGIRDSFASEHGARMTAMHKATDNATALRNQLKLTYNKARQAAITSEILEIVGGAEALNG
>NZ_CP016907.1|WP_008465838.1|1783727_1785305_-|F0F1-ATP-synthase-subunit-alpha
MAEIKPAEISAILRKQVEGFESGATLEEVGSVLQVGDGIARVYGLSNVQYGELVEFDNGMEGIVLNLEEDNVGVVLLGPSTGIKEGSTAKRTQRIASLKVGEQMVGRVVNTLGFPIDGKGPIGGDLYEMPLERKAPGVIFRQPVTEPLQTGVKAVDAMIPVGRGQRELVIGDRQTGKSTVCIDTILNQKEFYDAGKPVFCIYVAIGQKASTVAGIAKMLEEKGAMAYTVIVAANASDPAPMQVYAPFAGAAIGEYFRDSGRPALIVYDDLSKQAVAYREVSLLLRRPPGREAYPGDVFYLHSRLLERACKVIADDGIAKNMNDLPDSIKSIVKGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLDGDLFNSGVRPAINVGISVSRVGGNAQIKSMKKVSGTLKLDQAQFRELEAFAKFGSDLDSVTLNVIEKGKRNVEILKQGLNDPYTVENQVAIIYAGSKNLLRNVPVNKVKEFEADFLAYLNSKHKDTLNALKAGKLDDAITDVIEKAAKEISAKYN
>NZ_CP016907.1|WP_008465837.1|1785342_1785876_-|ATP-synthase-F1-subunit-delta
MASTRAAIRYAKAILDLANSKGVAEAVNNDMKSIATAIETNQELSTFIQNPTTTVEVKEGALLEVFANVNGVTKGLFRLLFENKRFEILDAIAVEYNKLFDENNGVQVAKVTTAIPMDAALEAKVLAKIATLSDKKITIENIVDPSIIGGFILRIGDNQYNASVAYRLQVLKRELSN
>NZ_CP016907.1|WP_008465836.1|1785880_1786381_-|F0F1-ATP-synthase-subunit-B
MDKLINDFSFGLFFWQALILVILILLLVKFAWKPIMESITAREEGIKNALLSAENAKREMENLQADNQRILNEARAERDAMLKEAREMKEKMIADSKNEAQEAGQKMIDQAKAAIESEKNAAMAELKSQVSSLSLSIAEKLLKEELSNKESQTKLVEKMLGDVKLN
>NZ_CP016907.1|WP_008465835.1|1786471_1786669_-|ATP-synthase-F0-subunit-C
MGTIPTLVGAGLVVIGAGLGLGKIGGSAMDAIARQPEAAGKIQTAMIIIAALLEGLAFAALILGK
>NZ_CP016907.1|WP_008465834.1|1786703_1787879_-|F0F1-ATP-synthase-subunit-A
MVISNKPLSFILAAFVASLPIMGFANPENDSTHVQTETAHEEKVVSHNAHQEGEHVALDPKAKVDAFIDHHLQDSHDFVFFSDEKENKHYGFSLPVILIDGGLKVFSSSKLHHGEEVAEVDGSYYKLVHGKIYKTDAAGTINFDEHGHPSNEKPLDFSITKNVVSMLFVSVLLFFMFTGLAKSYKKGPIPTGFGRVLEPLVIFIRDEIAVPNIGEKKYRKYMGYLLTVFFFVWVLNLLGMTPLGINVTGNIAITVCLAAFTFIITQFSANKDYWGHIFWMPGVPVPMKIILAPIEVLGTLTKPFALLIRLYANITAGHVVIMSLIAMIFVGKNLAADLPISLGLTLFISVIEVLVAFLQAFIFTMLSSLFIGMAVQDHDHAHHHEDETAII
>NZ_CP016907.1|WP_008465831.1|1788447_1788675_-|AtpZ/AtpI-family-protein
MEKEPNNNRRNKWLAFINIPFQMGVIIFVFSYFGTWLDEEHPSPKVYYNTIFVLVGVGVALYNVIRQVNDINKTK
>NZ_CP016907.1|WP_008465829.1|1788655_1789054_-|polymer-forming-cytoskeletal-protein
MFEKVKKNGTEQLGRTNRIVEGTSIVGDIVSKADFRLDGELIGNFTSQGKIVIGAKGAVKGEIICNNADIEGEFHGKIKVLETLNIKSTAQIHGEVAVGKLSIEPGADFTATCTMLAHSNPVIMLEDGKGAE
>NZ_CP016907.1|WP_066033163.1|1789066_1791679_-|gliding-motility-protein
MKKNTLKYSFIPIFLFFLIACSTKKNTFLARSSHSIGTKYNILYNGGIGLDKGLKSIQANNEDNFWKQLPIEKMQFDENFSEGEKAKNPDFEKAETKATKAIQKHSMNIGGRERNWQMDEAYLMLGKARYYDQRFIPAIEAFNYILYKYPESNNIYTAKIWREKTNMRLGNDAIALKNIKILLKKTDLDKQTYADANALLAEAFLNLEQKDSAVSRLRVAEQFTKSNEERARYRFILGQMYQAEGKRDSAIYFYDAVIDLNRKADRKYMMHAYAKKAQMFDYGKDNDTIFLKTFNKLVTDRENRPYYDVLFYEMGVYYDKKKDQENALKFYNKSLGRKSKDPYLMASAYRNIGNMYFKDTDYSMAAKYYDSTLVKLDPKTREFAFIEKNRKNLDDVIKYEAIAKRNDSIIKVFNLPPNEKKDYFENYIAELKKKDEAKRLLEEKEKERLANIDRNSQADFSGNGAVNPNSLGKPVEPEGIGMPPGGNDNASTFYFYNPTTVAYGKLQFKKMWGSRTLGGNWRLAGVKSANDAAMNDTINTKEVANALKDTIVPEKYTVAYYVEQLPTSQAAMDSIGKERNFSYYQLGLIYKEKFKEYNLASDKLEQLLKNNPEEKYVLPSMYNLYKIYQITNPAKAEAIKAEISTKYPDSRYAHILNNKEDDPNSSPDKEYQKWYKLFEEEKFDEVLANIDNLINQYSGDDIVSKYELLKANTLGKVNGLEAYKKGLENVADNYPNSEEGKNAREILEKQVPVLEKLSFTTTDTKNWKILYRVANNDTKTVKRIEEAIRVFLLVENYERLTTSLDKYNKTESFVVIHGLKSEAYANDIAGVFREDKKYKIPDQAIIISNDNYKIVQIKKNLDAYLTPKTP
>NZ_CP016907.1|WP_066033164.1|1791769_1792465_-|ABC-transporter-ATP-binding-protein
MIRVNQLSKKYNGTTVLNISNLEIPKGQSFGLVGNNGAGKTTFFSLLLDLIQPSTGYIKSNNIQVNTSENWKSFTGSFLDENFLIGYLTPEEYFYFIGDLRNQNKADIDALLAKHEEFFNGEILKNKKYLRDLSKGNQKKVGIIATLIGNPEVVILDEPFANLDPTTVSRLKKIIKELADDPNVTVLVSSHDLQHTVEVCDRIVALNKGEIVKDIQTSKETLQELELFFAV

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Crispr_ID: NZ_CP016907_4

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP016907_4

2387780-2387868

Orphan

Consensus_repeat	Method
AGTTTTCAGTCTCAGTCTCAGTTTTCAGT	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP016907_4

>merge|NZ_CP016907|4|2387780-2387868|CRISPRCasFinder
AGTTTTCAGTCTCAGTCTCAGTTTTCAGTATGAAATTGAGACTAAAGAGTTTATTTTTTGAGTTTTCAGTCGCAGTCTCAGTTTTCAGT

>NZ_CP016907|4|4|2387780-2387868|CRISPRCasFinder
AGTTTTCAGTCTCAGTCTCAGTTTTCAGT	ATGAAATTGAGACTAAAGAGTTTATTTTTTG
AGTTTTCAGTCGCAGTCTCAGTTTTCAGT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP016907.1\|WP_066033504.1\|2380849_2381755_-\|TIGR01777-family-protein	unknown	unknown	gnl\|CDD\|187553
NZ_CP016907.1\|WP_083219824.1\|2395819_2397094_+\|HlyC/CorC-family-transporter	unknown	unknown	gnl\|CDD\|224173
NZ_CP016907.1\|WP_066033511.1\|2388732_2389884_-\|5-(carboxyamino)imidazole-ribonucleotide-synthase	unknown	unknown	gnl\|CDD\|235674
NZ_CP016907.1\|WP_066033503.1\|2380253_2380709_-\|SRPBCC-family-protein	unknown	unknown	gnl\|CDD\|176862
NZ_CP016907.1\|WP_066033509.1\|2385745_2387773_-\|M3-family-metallopeptidase	unknown	unknown	gnl\|CDD\|341051
NZ_CP016907.1\|WP_008464249.1\|2397181_2398183_+\|GTPase-ObgE	unknown	unknown	gnl\|CDD\|237048
NZ_CP016907.1\|WP_008464247.1\|2395044_2395617_+\|adenylate-kinase	unknown	unknown	gnl\|CDD\|234711
NZ_CP016907.1\|WP_066033513.1\|2390667_2392770_-\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|238657
NZ_CP016907.1\|WP_066033502.1\|2379248_2380061_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|260130
NZ_CP016907.1\|WP_066033508.1\|2382899_2383403_-\|ArsR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224427
NZ_CP016907.1\|WP_066033507.1\|2382561_2382843_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP016907.1\|WP_066033506.1\|2382211_2382565_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP016907.1\|WP_066035133.1\|2376203_2379053_-\|aminomethyl-transferring-glycine-dehydrogenase	unknown	unknown	gnl\|CDD\|235432
NZ_CP016907.1\|WP_066033512.1\|2390092_2390644_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP016907.1\|WP_066033514.1\|2392989_2394261_-\|sorbosone-dehydrogenase-family-protein	unknown	unknown	gnl\|CDD\|225044
NZ_CP016907.1\|WP_066033515.1\|2394447_2394978_+\|hypoxanthine-phosphoribosyltransferase	unknown	unknown	gnl\|CDD\|223707
NZ_CP016907.1\|WP_083219823.1\|2383541_2384804_+\|sodium:proton-antiporter	unknown	unknown	gnl\|CDD\|223104
NZ_CP016907.1\|WP_066033505.1\|2381812_2382199_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP016907.1\|WP_066033510.1\|2387899_2388382_-\|5-(carboxyamino)imidazole-ribonucleotide-mutase	unknown	unknown	gnl\|CDD\|376377
NZ_CP016907.1\|WP_008464250.1\|2398416_2400561_+\|S46-family-peptidase	unknown	unknown	gnl\|CDD\|371067

Protein	Function_ID	Function_description	E-value
NZ_CP016907.1\|WP_066033504.1\|2380849_2381755_-\|TIGR01777-family-protein	gnl\|CDD\|187553	cd05242, SDR_a8, atypical (a) SDRs, subgroup 8. This subgroup contains atypical SDRs of unknown function. Proteins in this subgroup have a glycine-rich NAD(P)-binding motif consensus that resembles that of the extended SDRs, (GXXGXXG or GGXGXXG), but lacks the characteristic active site residues of the SDRs. A Cys often replaces the usual Lys of the YXXXK active site motif, while the upstream Ser is generally present and Arg replaces the usual Asn. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.	1.71971e-114
NZ_CP016907.1\|WP_083219824.1\|2395819_2397094_+\|HlyC/CorC-family-transporter	gnl\|CDD\|224173	COG1253, TlyC, Hemolysins and related proteins containing CBS domains [General function prediction only].	9.0884e-115
NZ_CP016907.1\|WP_066033511.1\|2388732_2389884_-\|5-(carboxyamino)imidazole-ribonucleotide-synthase	gnl\|CDD\|235674	PRK06019, PRK06019, phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed.	1.30561e-141
NZ_CP016907.1\|WP_066033503.1\|2380253_2380709_-\|SRPBCC-family-protein	gnl\|CDD\|176862	cd07820, SRPBCC_3, Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins. Uncharacterized group of the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands. SRPBCC domains include the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), Class I and II phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of the superfamily include PYR/PYL/RCAR plant proteins, the aromatase/cyclase (ARO/CYC) domains of proteins such as Streptomyces glaucescens tetracenomycin, and the SRPBCC domains of Streptococcus mutans Smu.440 and related proteins.	3.7579e-47
NZ_CP016907.1\|WP_066033514.1\|2392989_2394261_-\|sorbosone-dehydrogenase-family-protein	gnl\|CDD\|225044	COG2133, COG2133, Glucose/sorbosone dehydrogenases [Carbohydrate transport and metabolism].	1.88899e-94
NZ_CP016907.1\|WP_008464249.1\|2397181_2398183_+\|GTPase-ObgE	gnl\|CDD\|237048	PRK12299, obgE, GTPase CgtA; Reviewed.	0
NZ_CP016907.1\|WP_066033513.1\|2390667_2392770_-\|TonB-dependent-receptor	gnl\|CDD\|238657	cd01347, ligand_gated_channel, TonB dependent/Ligand-Gated channels are created by a monomeric 22 strand (22,24) anti-parallel beta-barrel. Ligands apparently bind to the large extracellular loops. The N-terminal 150-200 residues form a plug from the periplasmic end of barrel. Energy (proton-motive force) and TonB-dependent conformational alteration of channel (parts of plug, and loops 7 and 8) allow passage of ligand. FepA residues 12-18 form the TonB box, which mediates the interaction with the TonB-containing inner membrane complex. TonB preferentially interacts with ligand-bound receptors. Transport thru the channel may resemble passage thru an air lock. In this model, ligand binding leads to closure of the extracellular end of pore, then a TonB-mediated signal facillitates opening of the interior side of pore, deforming the N-terminal plug and allowing passage of the ligand to the periplasm. Such a mechanism would prevent the free diffusion of small molecules thru the pore.	5.23699e-38
NZ_CP016907.1\|WP_066033502.1\|2379248_2380061_+\|hypothetical-protein	gnl\|CDD\|260130	cd13967, PT_UbiA_5, UbiA family of prenyltransferases (PTases), Unknown subgroup. Many characterized members of the UbiA prenyltransferase family are aromatic prenyltransferases and play an important role in the biosynthesis of heme, chlorophyll, vitamin E, and vitamin K. They contain two copies of a motif similar to the active site DxxD motif of trans-prenyltransferases and are potentially related. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways. The function of this subgroup is unknown.	0.000514908
NZ_CP016907.1\|WP_066033508.1\|2382899_2383403_-\|ArsR-family-transcriptional-regulator	gnl\|CDD\|224427	COG1510, COG1510, Predicted transcriptional regulators [Transcription].	2.53822e-26
NZ_CP016907.1\|WP_066035133.1\|2376203_2379053_-\|aminomethyl-transferring-glycine-dehydrogenase	gnl\|CDD\|235432	PRK05367, PRK05367, aminomethyl-transferring glycine dehydrogenase.	0
NZ_CP016907.1\|WP_008464247.1\|2395044_2395617_+\|adenylate-kinase	gnl\|CDD\|234711	PRK00279, adk, adenylate kinase; Reviewed.	4.04985e-76
NZ_CP016907.1\|WP_066033515.1\|2394447_2394978_+\|hypoxanthine-phosphoribosyltransferase	gnl\|CDD\|223707	COG0634, Hpt, Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism].	2.58044e-52
NZ_CP016907.1\|WP_083219823.1\|2383541_2384804_+\|sodium:proton-antiporter	gnl\|CDD\|223104	COG0025, NhaP, NhaP-type Na+/H+ and K+/H+ antiporters [Inorganic ion transport and metabolism].	1.89816e-53
NZ_CP016907.1\|WP_066033509.1\|2385745_2387773_-\|M3-family-metallopeptidase	gnl\|CDD\|341051	cd06456, M3A_DCP, Peptidase family M3, dipeptidyl carboxypeptidase (DCP). Peptidase family M3 dipeptidyl carboxypeptidase (DCP; Dcp II; peptidyl dipeptidase; EC 3.4.15.5). This metal-binding M3A family also includes oligopeptidase A (OpdA; EC 3.4.24.70). DCP cleaves dipeptides off the C-termini of various peptides and proteins, the smallest substrate being N-blocked tripeptides and unblocked tetrapeptides. DCP from Escherichia coli is inhibited by the anti-hypertensive drug captopril, an inhibitor of the mammalian angiotensin converting enzyme (ACE, also called peptidyl dipeptidase A). OpdA may play a specific role in the degradation of signal peptides after they are released from precursor forms of secreted proteins. It can also cleave N-acetyl-L-Ala. This family also includes Arabidopsis thaliana organellar oligopeptidase OOP (At5g65620), which plays a role in targeting peptide degradation in mitochondria and chloroplasts; it degrades peptide substrates that are between 8 to 23 amino acid residues, and shows a weak preference for hydrophobic residues (F/L) at the P1 position.	0
NZ_CP016907.1\|WP_066033510.1\|2387899_2388382_-\|5-(carboxyamino)imidazole-ribonucleotide-mutase	gnl\|CDD\|376377	pfam00731, AIRC, AIR carboxylase. Members of this family catalyze the decarboxylation of 1-(5-phosphoribosyl)-5-amino-4-imidazole-carboxylate (AIR). This family catalyze the sixth step of de novo purine biosynthesis. Some members of this family contain two copies of this domain.	4.38014e-83
NZ_CP016907.1\|WP_008464250.1\|2398416_2400561_+\|S46-family-peptidase	gnl\|CDD\|371067	pfam10459, Peptidase_S46, Peptidase S46. Dipeptidyl-peptidase 7 (DPP-7) is the best characterized member of this family. It is a serine peptidase that is located on the cell surface and is predicted to have two N-terminal transmembrane domains.	0

>NZ_CP016907.1|WP_066033509.1|2385745_2387773_-|M3-family-metallopeptidase
MSVLTQYFNTKHNTAPFSQIKIEDYVPAFQEGIALAKAEIDAIVNNPDEPTFENTIVAMDFSGDILDRLSSIFFNLNSAETNDEMQKIAQEVSPWLSEFGNDIRLNAELFARVKTVYDQKENLNLNPEQTTLLDKKYKSFSRNGANLPEDKKNQLREIDKELSKLSLQFGENVLAETNNFELHLTDEKDLSGLPEGAIEAARLLAKNQEKEGWIFTLDHPSYVPFLTYANNRELRKKMAIAFGAKGFQKNEFNNEEIVLKIAKLRHERANLLGYKTHAHFVLEERMAESPEKVFSFLNDLLAKAKPAAQKEFAELTAFAKELDGIEQLEKWDGAYYSEKLKQQLFNLDDEKLKPYFQLEKVLDGAFTVAKKLYGLTFTEVFDIDKYHEEVTTYEVKDADGNLVSIFYADFFPRKGKRNGAWMTSFKSQYVKDGVNERPHISNVCNFTKPTETKPSLLTFNEVTTLFHEFGHGLHGMLANTVYPSLSGTSVYWDFVELPSQIMENWCYEPEALALFANHYETGEIIPIEYVQKIKESASFQEGLATLRQLSFGLLDMAWHGQDPTNITDLKAFETEQFANTQLYPDVKENAMSTAFSHIFQGGYSSGYYSYKWAEVLDADAFEYFHENGIFNEDIAKKFKDNVLSKGGTEHPMILYKRFRGQEPKPEALLKRAGLL
>NZ_CP016907.1|WP_083219823.1|2383541_2384804_+|sodium:proton-antiporter
MELYYTFSVLIVLASFFAYLNLRFLKLPGTIGIMIIAMLVSVGIRLLGDSYFPATTKHFFDLIKEFDFNEILMGAMLNFLLFAGALHVNMFDLKEQKVPIMIYSTVSVVLSALIISVLLYYIAPFFGITIPYIFCLVFGTLISPTDPIVVLGVLKEAKVPKRIETKIVGESLFNDGVAVVMFAVVLKMATDPTFDATFGSISWLFIKEGIGGLLLGAAFGFTASKVMKKIDDYKVSVLITLSIVMGGFLIAQSLHVSSPLAMVVAGLIIGNYGKKVAMSEVTKDYLGKFWELIDEILNAVLFLFIGFELLLLPDLNKQLLTGFIAIFIVLFSRLTSIVLPWKFFDIFKFFGIKSAYNKGSLMVLVWGGIRGGVSIALVLSMPESEYKNLLLEVTYIVVLFSIVVQGLTVGKLANRVLEKE
>NZ_CP016907.1|WP_066033508.1|2382899_2383403_-|ArsR-family-transcriptional-regulator
MEFKEAKNKFVQTWGALGSQWGINKTMAQIHALLMVSNEPVSMEDIMEELQISRGNASMNLRALMDWGIVYKEFKAGERKEFFTAEKDLDELAAKISRERSKREIKPALKILKEVSTIEAKDSAEEKHFVDQTTKLYDFVLKADNMLDKMTEFNDNWLGKLFIKMMK
>NZ_CP016907.1|WP_066033507.1|2382561_2382843_-|hypothetical-protein
MKTTFKIMEIINICALTFLLAGAYGIAITGALQVLAAFLFLILFPKNKFIYIYFSLVIFFFLIWDGEFTWLFLLPVALIFFLTFIIYNQKKKL
>NZ_CP016907.1|WP_066033506.1|2382211_2382565_-|hypothetical-protein
MNFNIIGYLIYLGITTFIILKVGKICYKNGNIYVADLIPNHADICQRINQVLLLAYYLLNIGYCAMTLISWKKIISSTQVIETICTKTAVIIFIISILHYLNILIITKYVEKLIHNN
>NZ_CP016907.1|WP_066033505.1|2381812_2382199_-|hypothetical-protein
METTKILIGYGIYLPVALFLTYYVSKTLFKNGKIFMLDIFKGREEIAEATNKLFETGFYLLNIGFALMILELQLNQDSYQELIERLSYKIGGFSIYLGIMLFFNLYFFFRGKRKAKEAQREERLVFKA
>NZ_CP016907.1|WP_066033504.1|2380849_2381755_-|TIGR01777-family-protein
MKKLLIAAGTGFLGKVLANHFKNKFDEIVILTRGKSQTIDGIKYVNWNARTFTGWEKELENATVLINLAGKSVDCRYTKGNKKEILWSRIESTKILNKAVLKCQNPPKHWLNSSTATIYRFSLDKQMDEVDGEIGNDFSINVALSWEKAFFKTETPNTLKTTLRTSIVLGKNGGAFIPLKTLAKIGFGGKQGKGNQFVSWIHEDDFAHAVDFIIEQEMSGMINIVSPTPIRNVDFMQKLRKAIGFPFGIPLNTFFLKIGSFLIRTETELVLKSRNVIPKRLLENGFEFKFGEIDKAFRDLI
>NZ_CP016907.1|WP_066033503.1|2380253_2380709_-|SRPBCC-family-protein
MTTINLTTKIKAPKQIVFDASRNINIHQQSASFSKEKAIAGVTSGLINLDETVTWRGKHFGFYLTHKSRITAMNLYDYFVDEMEKGKFKSFKHEHFFEEENGFIIMKDKLQYETPFGIFGKLFDVLFLKRHLINFLLERNKVLKEISENNN
>NZ_CP016907.1|WP_066033502.1|2379248_2380061_+|hypothetical-protein
MIVSKRFLDFYLNSSIHVALSCYALVRITFHVFHIQYDEPMALFVFFGTIVGYNFVKYDALVRVKKNPIGTQLKIIAILSFISVVLVGYYFFHLKRITQIVSVGIFAITALYTLPFFPNRKNARNWAGVKIYIVALCWVGATLVLPLINAEIPFTTDFFIKCIQRFILVFVLILVFEILDLANDDPHLQTVPQTIGVKRTKILGLSLLVPFWFLEILVSTFNYHDAFINLIMVIMLMLFIIFANPNRSKYYTSFWVEAVPIFWWLMVVFL
>NZ_CP016907.1|WP_066035133.1|2376203_2379053_-|aminomethyl-transferring-glycine-dehydrogenase
MKTDAFALRHIGPRETDLQHMLKTIGVDSIEQLVYETLPDDIRLKAPLNLDPAMTEYEFANHIQELGKKNKVFKSYIGLGYHPTIVPAPIQRNIFENPGWYTAYTPYQAEIAQGRLEAILNFQTTVIELTGMEIANASLLDEGTAAAEAMALLFDVRTRDQKKNNTHKFFVSEEILPQTLSVLQTRSTPIGIELVVGNHETFDFSNEFFGAILQYPGKYGQVNDYSAFVAKAKENEIKVAFAADILSLATLTSPGEMGAAVVVGTTQRFGVPMGYGGPHAAYFATKEEYKRSMPGRIIGVSIDANGNRALRMALGTREQHIKREKATSNICTAQVLLAVMAGMYAVYHGPEGLKYIANKVHASAVTTAEALNKLGVYQTNSAYFDTILVKADAQKVKAVAEKNEVNFFYPDAESVSISFNETTSISDINQIIAIFAEALGKETVSVSELSEASQLPASLERTSSFLTHDVFNNHHSESQLMRYIKKLERKDLSLNHSMISLGSCTMKLNAASEMLPLSMPNWNSIHPFAPVEQAEGYITMLKKLEQQLNVITGFAGTTLQPNSGAQGEYAGLMAIRAYHMSRNEGHRNVCLIPSSAHGTNPASAAMAGMKIIVTKTTPEGNIDVEDLRAKAIEHKDDLSCLMVTYPSTHGVYESSIIEITKLIHENGGLVYMDGANMNAQVGLTNPATIGADVCHLNLHKTFAIPHGGGGPGVGPICVNEKLVPFLPTNPILKVGGENAITAISSAPYGSALVCLISYGYITMMGAEGLKSATEHAILNANYMKARFEGHYPILYTGECGRAAHEMILDCRAFKENGIEVGDIAKRLMDYGFHAPTVSFPVAGTLMIEPTESEDLAELDRFCDALISIRKEIEAATAEDTNNVLKNAPHTLAMLTNDAWDFPYSREKAAYPLDYIADNKFWPSVRRVDDAYGDRNLVCSCAPIEAYMES
>NZ_CP016907.1|WP_066033510.1|2387899_2388382_-|5-(carboxyamino)imidazole-ribonucleotide-mutase
MSKVAIIMGSISDMPVMQDAIDILKQFNVEVELDIVSAHRTPEKLFDFSKNAHNRGISVIIAGAGGAAHLPGMVASMSPLPVIGVPVKSSNSIDGWDSVLSILQMPGGVPVATVALNGAKNAGILAAQIIGSHDKKVLDTIISYKEELKAAVNKAAESLK
>NZ_CP016907.1|WP_066033511.1|2388732_2389884_-|5-(carboxyamino)imidazole-ribonucleotide-synthase
MNYFSSDFKLGILGGGQLGKMLLFDTRKFDIQTYVLDPSDEAPSKIACNKFFQGDLMDYDTVYNFGKQVDVLTFEIELVNLEALTQLENEGLKVYPSPKTLKGIQNKGVQKEFYAKNNIPTAPFERFENLENLKSKISDLKLPFVWKCTEFGYDGNGVKIVRQASDLDTLPNVECIAETMVPFKNELAVIVVRNASGEMKTYPVVEMEFHPEANQVEYVICPARIDDKVAEKARAIALQVSENFNHVGLLAVEMFQTQDDEILVNEVAPRPHNSGHYSIEASYTSQFENHLRAILDLPLGNTDSKVAGIMVNLVGAEGHSGNVVYENIETILGWNGVTPHIYGKKQTRPFRKMGHVTIVNENMAEARRIAQEVKNTIKVISDQ
>NZ_CP016907.1|WP_066033512.1|2390092_2390644_-|hypothetical-protein
MLSELQKKLDYVNAYRENRLKTAQDVLENPSLFSALVSICFSPEDKNNHKACWILEFVSYEELLWLQPHLDFFCSNLKVLKDESAMRPIAKIVQLLVKSHYKKSENSIKLSEENLQDCIEASFDWLINDTKVATKAYSIRTLYILGNYYDWIHPELKVTIDKDFGDHSAAYKAVAKEVLKKIK
>NZ_CP016907.1|WP_066033513.1|2390667_2392770_-|TonB-dependent-receptor
MPFKKYFLLLFVLFISKNSSAQEKEVQNIDSVKTQKLNEILISPLHINRNLQNSPASIGILSEKELLRNNTTDISNVINTIPGVFMQSSNITTTRISIRGIGARTPYGTNNIRAFYGSIPLTSGNSETVIDDIDLQNINQIEVIKGPLSSIYGAGLGGAILISPETFNKSNYQTEVSSVFGSFGLLKNRVGFNLNEKSASLNLSYHNLKTDGWRENSAYNREGITLSGELFRKKNSRLTYFSNYTYLKAYIPSSINKTTFENNPQAGAPTWVASKGFKEYKSTLAGLAYDFKLNDHLNNSTSVFINYKDSNEPRPFDILRQYTFASGARTQFSGDFSIGKIKNQFIAGLEYFRDNYSGNTFENLYQQNNGNGSLQGDQLTATDQKRHFYNIFSQIRTLLSDRFEIQAGLNYNKTKFELQNDFPASANNPKEEYSYDGIFSPQLSFLFKPNEIRTFYFSASRGFSLPATEETLTSTGNINSDIKPETGYNFELGGKLHFFNKKLYTQIAIYRMEIKDLLVAKRIGDDQYEGVNAGKTFHEGIEISLNHNWTINRIFNLHSYVGASIGNYEFKDFVDNGNDYSGNKLTGVPANTASAGFNFNTNSGFYFSADFQFTDKIPMNDSNADFSDSYSLLNLKTGYQFEILSGLKAHLDAGINNVTNEKYASMILTNATGVGNAQPRFYYPGLPINYYGIISLNYLF
>NZ_CP016907.1|WP_066033514.1|2392989_2394261_-|sorbosone-dehydrogenase-family-protein
MKKTTTLLSIPLLALMTACNGQVKKEEKEALANQPGNVVKTAIGDITLPPPYATESKTNNSKVIGWPAGKTPKAPEGFTVTKFADGFENPRWTYIAPNQDIFVVESGTRSSKNQITVLRDKDKDGKFETREVFISGLNKPFGMLVLKDFFYIANTDGLYRYPYKNNPLKLESKGEKILELPAGGYNNHWTRNLLASPDGSKIYVSVGSGSNNGENGMDKEIRRAAILEINPDGTGEKIFASGLRNPVGMDWNPVNKELWTAVNERDELGDDLVPDYITSVKRDGFYGWPYSYFGSIPDPRMKGQRKDLVEKAIVPDVPVGSHTASLGLAFYTKEKFPAKYKNGAFVGQHGSWNRSKISGYKVLFVPFKDGKPSGKPEDFLTGFISDENKAEVYGRPVAVTVMNDGSLLVNDDSGNTIWKVTAK
>NZ_CP016907.1|WP_066033515.1|2394447_2394978_+|hypoxanthine-phosphoribosyltransferase
MIQLHDKQFVPFISAKEIDFALTKLVAQVEDDFGDDTPIFIGVLNGAFMVVSDFLKKYKKPCEVSFIKMASYEGTQSSESVKELIGINHDLTGRTVIVIEDIVDTGNTIEELKHLFKAQNVKHFKIATLFFKPEAYKKDIKIDYIGIRIPNKFIVGYGLDYDGLGRNLTEVYKLAE
>NZ_CP016907.1|WP_008464247.1|2395044_2395617_+|adenylate-kinase
MINIVLFGKPGAGKGTQAEFLKEKYNLTHLSTGDIFRFNLKNDTELGKQARVFMDNGELVPCEVTTAMLIDEVKKHPDTAGFLFDGYPRTINQAEALDKFLPTIGSSVTATIALEADDEILVKRLLERGKTSGRVDDQDEEKIRVRYQEYNEKTAPLIGYYKEQGKFHAVDGIGTIEQITERLTSVIDNL
>NZ_CP016907.1|WP_083219824.1|2395819_2397094_+|HlyC/CorC-family-transporter
MEILIIFFLILLNGVFSMSEIALISARKNRLETAAKKGNKSAKTALDLANSPNKFLSTVQIGITLIGILTGIYSGDKITADVELFVAGIAVLKPYAHSIAVGIVVVVLTFFSLVLGELLPKRIGLNYPEAIAKMVAMPMKVISIITAPFIWLLTSSTDFLLNVLQIKPTADGKVTEEEIKAIIKEGTEVGEVQEIEQDIVERVFHIGDRKVNSLMTHRKSVDMLPLKADKEKIKELVVQDLHAVYPVYNDNYDDIVGVATLKNIFANIENDNFDFSSIITEAPYLMEQTTAYKALENFKKTGVHYALVSDEYGVFQGMITLNDILEALVGDASEFYKDEFQLIEREDGSWLVDGHYSLHDFLTYFELDELTNDYEVNTVSGMIMTELSHIPKEGEKLIWQKFILEVVDMDGVKIDKVLVKALKE
>NZ_CP016907.1|WP_008464249.1|2397181_2398183_+|GTPase-ObgE
MTEGNFVDYVKIYVSSGKGGKGSTHLHREKFIEKGGPDGGDGGRGGHVYLVGNKGLWTLFHLKFARHIKAGHGGDGGSDRSTGADGEDKIIEVPLGTVVKDKETGETLFEITEHGEKQILARGGKGGLGNWHFRSSTNQTPRYAQPGLLGVEMDVILELKVLADVGLVGFPNAGKSTLLSVLTSAKPKIADYPFTTLKPNLGIVAYRDFQSFVIADIPGIIEGAAEGKGLGHYFLRHIERNSTLLFLIPVDTADIKAEYDILVNELTKYNPEMLDKERLVVISKCDMLDDELKAELKAELDVSFKDVPYMFISSVAQQGLTDLKDRLWKMLNE
>NZ_CP016907.1|WP_008464250.1|2398416_2400561_+|S46-family-peptidase
MKKVILFLTMCLMAFPMRADEGMWFLMFIERLNHRDMEKMGLQLTAEEIYSINHHSLKDAIVQFNGGCTAEIVSNTGLVLTNHHCGYGAIAELSTAEQNHLKDGFWAKSRSEELKPKSLFVRFFVRMDDVSKRILSKVNDTMTETERNKIIQQEIALIEKENSENGKYTVSVRPFFQGNEYYYFVYQDYTDVRLVGTPPESVGKFGGDTDNWEWPRQTGDFSMFRVYADKDGNPAAYSKDNVPLKPKHYLPVSLKGVKENDFAMILGYPGRTNRWMPAGGIEQNIKYAYPAWVEGAKTGMDVMKKYMDKDATVRLQYASKYASTANYWKNRQGMIDALTKAGTVDTKAEQEDKFYEWASKPANKEKYENVIPTINDYYRETNLKARHDNYLTQLLRTSAYATGPANLGNALIAYYKENDAKKAEMLPKINAMVESIYGDFYAPLEKDVLTAQLNLYASKAAEYGLAPEIAKMKTANNGDFTADVAKATEISYFSTKEKVLAFLADPKPLAIVHDPLYIISNDLLTKYRSKTDDQAKADDGFATAYRKLVEGLRESKLNAIKYPDANSTLRLTYGKVRALPADPRNDAKINNYTTMESMVKKYKAGDQEFDLPARLLELNKKKDYGQYADKAGYMPVNFLTDNDITGGNSGSPVLNGKGELIGIAFDGNIEAMAGDVIFDSKLQRTINVDIRYVLWIIDKYAGAKNIIDELTIAK

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Crispr_ID: NZ_CP016907_5

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP016907_5

2626570-2626646

Orphan

Consensus_repeat	Method
TTCCTCCGCTAGAAGCATCTGCT	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP016907_5

>merge|NZ_CP016907|5|2626570-2626646|CRISPRCasFinder
TTCCTCCGCTAGAAGCATCTGCTTTTAGACTTAAGATTGGACGTACAGAAACGGTTCCTCCGCTAGAAGCATCTGCA

>NZ_CP016907|5|5|2626570-2626646|CRISPRCasFinder
TTCCTCCGCTAGAAGCATCTGCT	TTTAGACTTAAGATTGGACGTACAGAAACGG
TTCCTCCGCTAGAAGCATCTGCA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP016907.1\|WP_164085586.1\|2630732_2630894_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP016907.1\|WP_008464568.1\|2619151_2620054_-\|ParB/RepB/Spo0J-family-partition-protein	unknown	unknown	gnl\|CDD\|275105
NZ_CP016907.1\|WP_066033662.1\|2637685_2638018_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP016907.1\|WP_008464565.1\|2617850_2618552_-\|4-hydroxy-tetrahydrodipicolinate-reductase	unknown	unknown	gnl\|CDD\|234595
NZ_CP016907.1\|WP_008464669.1\|2624472_2625420_+\|thioredoxin-disulfide-reductase	unknown	unknown	gnl\|CDD\|273540
NZ_CP016907.1\|WP_066033660.1\|2633497_2636044_-\|copper-translocating-P-type-ATPase	unknown	unknown	gnl\|CDD\|319783
NZ_CP016907.1\|WP_066033658.1\|2627233_2628982_-\|PspC-domain-containing-protein	unknown	unknown	gnl\|CDD\|377200
NZ_CP016907.1\|WP_008464563.1\|2616240_2617794_-\|signal-peptidase-I	unknown	unknown	gnl\|CDD\|182787
NZ_CP016907.1\|WP_008464569.1\|2620059_2620827_-\|ParA-family-protein	unknown	unknown	gnl\|CDD\|379293
NZ_CP016907.1\|WP_066033654.1\|2621047_2621452_-\|septal-ring-lytic-transglycosylase-RlpA-family-protein	unknown	unknown	gnl\|CDD\|223868
NZ_CP016907.1\|WP_066035144.1\|2621680_2623852_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|378931
NZ_CP016907.1\|WP_083219833.1\|2625551_2626451_-\|DUF2807-domain-containing-protein	unknown	unknown	gnl\|CDD\|371327
NZ_CP016907.1\|WP_123907025.1\|2631067_2633308_-\|multicopper-oxidase-domain-containing-protein	unknown	unknown	gnl\|CDD\|273649
NZ_CP016907.1\|WP_066035145.1\|2637060_2637588_-\|DUF3347-domain-containing-protein	unknown	unknown	gnl\|CDD\|378730
NZ_CP016907.1\|WP_052017591.1\|2618591_2619152_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP016907.1\|WP_119792881.1\|2629466_2629946_-\|DUF4870-domain-containing-protein	unknown	unknown	gnl\|CDD\|378240
NZ_CP016907.1\|WP_066033661.1\|2636497_2637058_-\|helix-turn-helix-transcriptional-regulator	unknown	unknown	gnl\|CDD\|225117
NZ_CP016907.1\|WP_008464693.1\|2630175_2630628_+\|DUF4442-domain-containing-protein	unknown	unknown	gnl\|CDD\|373120
NZ_CP016907.1\|WP_008464689.1\|2628985_2629318_-\|PadR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224609
NZ_CP016907.1\|WP_066033653.1\|2615533_2616148_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|378083

Protein	Function_ID	Function_description	E-value
NZ_CP016907.1\|WP_008464568.1\|2619151_2620054_-\|ParB/RepB/Spo0J-family-partition-protein	gnl\|CDD\|275105	TIGR04285, parB-like_partition_protein, nucleoid occlusion protein. This model describes nucleoid occlusion protein, a close homolog to ParB chromosome partitioning proteins including Spo0J in Bacillus subtilis. Its gene often is located near the gene for the Spo0J ortholog. This protein bind a specific DNA sequence and blocks cytokinesis from happening until chromosome segregation is complete.	2.92645e-82
NZ_CP016907.1\|WP_008464565.1\|2617850_2618552_-\|4-hydroxy-tetrahydrodipicolinate-reductase	gnl\|CDD\|234595	PRK00048, PRK00048, dihydrodipicolinate reductase; Provisional.	1.67355e-57
NZ_CP016907.1\|WP_008464669.1\|2624472_2625420_+\|thioredoxin-disulfide-reductase	gnl\|CDD\|273540	TIGR01292, Thioredoxin_reductase, thioredoxin-disulfide reductase. This model describes thioredoxin-disulfide reductase, a member of the pyridine nucleotide-disulphide oxidoreductases (pfam00070). [Energy metabolism, Electron transport].	7.30022e-143
NZ_CP016907.1\|WP_066033660.1\|2633497_2636044_-\|copper-translocating-P-type-ATPase	gnl\|CDD\|319783	cd02094, P-type_ATPase_Cu-like, P-type heavy metal-transporting ATPase, similar to human copper-transporting ATPases, ATP7A and ATP7B. The mammalian copper-transporting P-type ATPases, ATP7A and ATP7B are key molecules required for the regulation and maintenance of copper homeostasis. Menkes and Wilson diseases are caused by mutation in ATP7A and ATP7B respectively. This subfamily includes other copper-transporting ATPases such as: Bacillus subtilis CopA , Archeaoglobus fulgidus CopA, and Saccharomyces cerevisiae Ccc2p. This subclass of P-type ATPase is also referred to as CPx-type ATPases because their amino acid sequences contain a characteristic CPC or CPH motif associated with a stretch of hydrophobic amino acids and N-terminal ion-binding sequences. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.	0
NZ_CP016907.1\|WP_066033658.1\|2627233_2628982_-\|PspC-domain-containing-protein	gnl\|CDD\|377200	pfam04024, PspC, PspC domain. This family includes Phage shock protein C (PspC) that is thought to be a transcriptional regulator. The presumed domain is 60 amino acid residues in length.	6.89777e-23
NZ_CP016907.1\|WP_008464563.1\|2616240_2617794_-\|signal-peptidase-I	gnl\|CDD\|182787	PRK10861, PRK10861, signal peptidase I.	8.82741e-16
NZ_CP016907.1\|WP_008464569.1\|2620059_2620827_-\|ParA-family-protein	gnl\|CDD\|379293	pfam13614, AAA_31, AAA domain. This family includes a wide variety of AAA domains including some that have lost essential nucleotide binding residues in the P-loop.	8.84891e-93
NZ_CP016907.1\|WP_066033654.1\|2621047_2621452_-\|septal-ring-lytic-transglycosylase-RlpA-family-protein	gnl\|CDD\|223868	COG0797, RlpA, Lipoproteins [Cell envelope biogenesis, outer membrane].	3.9801e-38
NZ_CP016907.1\|WP_066035144.1\|2621680_2623852_+\|hypothetical-protein	gnl\|CDD\|378931	pfam12708, Pectate_lyase_3, Pectate lyase superfamily protein. This family of proteins possesses a beta helical structure like Pectate lyase. This family is most closely related to glycosyl hydrolase family 28.	0.00826335
NZ_CP016907.1\|WP_083219833.1\|2625551_2626451_-\|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).	5.44759e-15
NZ_CP016907.1\|WP_123907025.1\|2631067_2633308_-\|multicopper-oxidase-domain-containing-protein	gnl\|CDD\|273649	TIGR01480, unnamed_protein_product, copper-resistance protein, CopA family. This model represents the CopA copper resistance protein family. CopA is related to laccase (benzenediol:oxygen oxidoreductase) and L-ascorbate oxidase, both copper-containing enzymes. Most members have a typical TAT (twin-arginine translocation) signal sequence with an Arg-Arg pair. Twin-arginine translocation is observed for a large number of periplasmic proteins that cross the inner membrane with metal-containing cofactors already bound. The combination of copper-binding sites and TAT translocation motif suggests a mechansism of resistance by packaging and export. [Cellular processes, Detoxification, Transport and binding proteins, Cations and iron carrying compounds].	3.04031e-106
NZ_CP016907.1\|WP_066035145.1\|2637060_2637588_-\|DUF3347-domain-containing-protein	gnl\|CDD\|378730	pfam11827, DUF3347, Protein of unknown function (DUF3347). This family of proteins are functionally uncharacterized. This protein is found in bacteria. Proteins in this family are typically between 169 to 570 amino acids in length.	1.78725e-50
NZ_CP016907.1\|WP_119792881.1\|2629466_2629946_-\|DUF4870-domain-containing-protein	gnl\|CDD\|378240	pfam09685, DUF4870, Domain of unknown function (DUF4870).	4.86634e-28
NZ_CP016907.1\|WP_066033661.1\|2636497_2637058_-\|helix-turn-helix-transcriptional-regulator	gnl\|CDD\|225117	COG2207, AraC, AraC-type DNA-binding domain-containing proteins [Transcription].	2.29255e-15
NZ_CP016907.1\|WP_008464693.1\|2630175_2630628_+\|DUF4442-domain-containing-protein	gnl\|CDD\|373120	pfam14539, DUF4442, Domain of unknown function (DUF4442). This family of proteins is found in bacteria, archaea and eukaryotes. Proteins in this family are typically between 139 and 165 amino acids in length. There is a conserved PYF sequence motif. There is a single completely conserved residue N that may be functionally important.	1.0886e-08
NZ_CP016907.1\|WP_008464689.1\|2628985_2629318_-\|PadR-family-transcriptional-regulator	gnl\|CDD\|224609	COG1695, COG1695, Predicted transcriptional regulators [Transcription].	2.67693e-22
NZ_CP016907.1\|WP_066033653.1\|2615533_2616148_-\|hypothetical-protein	gnl\|CDD\|378083	pfam08889, WbqC, WbqC-like protein family. This family of proteins are functionally uncharacterized. However it is found in an O-antigen gene cluster in E. coli and other bacteria suggesting a role in O-antigen production. Feng et al. suggest that wbnG may code for a glycine transferase.	1.08065e-33

>NZ_CP016907.1|WP_083219833.1|2625551_2626451_-|DUF2807-domain-containing-protein
MIFLYLSKSNLELMKKSTALLLLLLVTTLTFAQKREKIKGSKIVTTSIKEVGSFDALEVDDNIEVYLEQGEKNEIKIEADDNLHDIVGMDLREKTLRLYTNKESTIFKKLSVKVTYTKSLNKVITKNEAIVYAIQELQLDDITMNCLDFSKLYLNVNSKKFTLIADDKSRTELNLKAEDGSLQLSKYAGVKTLVSAIKFKCDLYQKATAAIEGIAEKATIRLDNNSVFTGTKFTLKDANVTAEGSAVATILAENTVAIAAGDKSEISLYGDPKIDLTRFSEEAKLIKKPGATKPKATTL
>NZ_CP016907.1|WP_008464669.1|2624472_2625420_+|thioredoxin-disulfide-reductase
MSNTIEKIKCLIIGSGPAGYTAAIYAARANMNPVLYQGMQPGGQLTTTNEVENFPGYVDGVTGPEMMIQLQEQAKRFGADIRDGWATKVDFSGDIHKVWINDTIELHCETVIISTGASAKYLGLPSEQHYLNMGGGVSACAVCDGFFYRNQDVVIVGAGDSACEEAHYLSKLCKKVTMLVRSDKFRASKIMEERVRKTENIEILMNHDTVEVLGDNNVVHAIKALNKTTGETIEIPATGFFVAIGHKPNTDIFKDYITLDETGYIVNTPGTSKTNVEGVFVAGDAADHVYRQAITAAGTGCMAALDAERYLASKE
>NZ_CP016907.1|WP_066035144.1|2621680_2623852_+|hypothetical-protein
MSKKVISLLTVFTFMMLLCSFVSPNSTNEKIKGNKNIERKIVYNKKKHSITLSWSAFGSSGNYTITRGGSRLASDFMSVGSTSKLSFIDNKPNTSKYENYYKVRRNDITIIISLENQIFGDNMYFYDRKHEKAETARNEINSQFSSIGLGGANGEWTTKRQAYYFKPNVNGQTYDVGGSGSASSAEANSIELGFYSHIGGLGKVPSDVKLGAIFTRPHLSGGANATCTFWRSVENVEVMRDFSWTVSQSTSARRLLIESTSKYISDIGNTNFWGSGGFIADAHYTTSRPNWGGQQQWYTRNTVFPSGSGVMGGSYNMVWQGCVNSPQANEANSPITTTPIIREKPFLFIGDDGEYKVFVPAWQKDRVGVSWSATDMGKGEIQDLIASWYVAKEGDTDVEINAALKAGKNIFFTPGHYALNAPIQVNRKDAILLGAGIASVTLEPTEKNIWGCIYADDKDGIIIAGLLMDSFNSTTYQVRIGNEGANADHSTDPILLSDITCRVGGVQSKNIQIQASMQINSNNVVGDHFWLWRADHGSQKGGDARWKRDRCKNGLIVAGNDVTLYALFVEHYQEYEVLWLGERGRTFFFQNEPPYDAPNQASWSSQGGRVDGYAAFKVANSVKEHHTIGMGSYAVFTGTDGNVNKKNGFEIPNSPNVKLEKMCITRFAGSGNIQNVINGTGGSTATGVKRVASYNNGEGTQPFDEEFTLPNKESYPSYISMEK
>NZ_CP016907.1|WP_066033654.1|2621047_2621452_-|septal-ring-lytic-transglycosylase-RlpA-family-protein
MREIILFITLFFSAVAIAQQKNITPIDSCASVRESVLYKQNAHASYYHDKFNGRKTASGRRFNNNDFTAAHKKFPFGTMLKVTNEVNNKFVIVEITDRGPFVKGREIDLSKRAFMDIATNKKSGLVFVTIEILK
>NZ_CP016907.1|WP_008464569.1|2620059_2620827_-|ParA-family-protein
MGKIIAIANQKGGVGKTTTSVNLAASLGVLEKKVLLIDADPQANATSGLGIDVETVETGTYQILEHTVTPKEAVLKCTAPNVDVIPAHIDLVAIEIELVDKENREYMLKKALEEAKEEYDYIIIDCAPSLGLLTLNALTAADSVVIPIQCEYFALEGLGKLLNTIKSIQKIHNPDLDIEGLLLTMYDSRLRLSNQVVEEVQKHFNDMVFDTVIQRNVKLSEAPSFGESIINYDATSKGAVNYIHLAQEIIKKNSK
>NZ_CP016907.1|WP_008464568.1|2619151_2620054_-|ParB/RepB/Spo0J-family-partition-protein
MTKVIKKQALGRGLSALLKDPENDIKSVEDKNADKVVGNIIELEISAIEINPFQPRSNFNEESLRELATSIKELGVIQPITVRKLDFNKYQLISGERRLRASKLVGLTHVPAYIRIANDNESLVMALVENIQRHDLDPIEIALSYQRLIDEIQLTQEQMSERVGKKRSTIANYLRLLKLDPIIQTGIRDGFISMGHGRAIINIEDLDVQTDIYQKIVSQNLSVRETEALVKNYHEGQQPKADGKPKADAAFIVRETQKNTFNDYFGSKVDIKVAGNGKGKITIPFNSEADFNRIIKLING
>NZ_CP016907.1|WP_052017591.1|2618591_2619152_-|hypothetical-protein
MNKIVPIGLLFFLTGTVSLFAQVKKDTVLVVKDTTALQEIDPLTPAKAAFYSAILPGLGQAYNKKYWKIPLVYGAIGTSLYFYIDNNKKYHDYRDAYKRRLEGYNDDKYQFLDDSRLVDGQKFYQRNRDLSALFVVGFYVLNIIDANVDAALIQFNVNERLSMRPEIYPDDVTFKPNVGLTFNYKF
>NZ_CP016907.1|WP_008464565.1|2617850_2618552_-|4-hydroxy-tetrahydrodipicolinate-reductase
MKIALLGYGKMGKVIERIALERGHEIVLKKDEFNTYDGLSTADVAIDFSVPSAAVSNISASFNANVPVVSGTTGWLEHYDEMIALCNEKKGGFISSSNFSLGVNIFFGLNEYLAKIMNQFDSYKVSMEEIHHIHKLDAPSGTAISLAQGVIQNSNYANWTLEEAKANEIHIEAKRIGEVPGTHTVTYDSPIDSIEIKHTAHNREGFALGAVIAAEWLAGKQGIYSMKDVLNLQ
>NZ_CP016907.1|WP_008464563.1|2616240_2617794_-|signal-peptidase-I
MTLYSWFVFFLAVQIIHFLGTWKLYQAAGRKSWEAAIPVYNSIVLMKIIGRPTWWTLLLFIPIINLIMFPVVWVETLRTFGKKSTLDTILGLFTLGFYIYVVNYTQKLEYHKDRKLTPDNKAADTVSSLLFAIIVATLVHTYVVQPYTIPTSSLEKSLLIGDFLFVSKLNYGPRVPMTTVALPMVHDSIPLTKSKSYLSWPQLPYFRLPAIQKINRCDIVVFNWPVDTVHYFFEPKGRPGVIKPIDKKSNYVKRCVGIPGDSLSIKDGYVFINGKKLVLPERAKPQYSYAVALDGKTPIDFETIFKELDITDPAGFRTEKRDTLYLGALTEAGAERFKNTPGVTAVIRKVDHGDDNAIFPHINKWNQDNMGPIYIPEAGKTVALTNESLPFYKEIITNYEGNTLELQGSKFLINGKPATTYTFKQNYYWMMGDNRHNSEDSRYWGYVPENHIVGKPVFIWMSWDTNGKGINKIRWNRVFTTVDGEGQPHSYFKYFLILLAIYFVGDFIWKKRRENKA
>NZ_CP016907.1|WP_066033653.1|2615533_2616148_-|hypothetical-protein
MNSLILPTYFPSISHFAVIAQSDSITFEMEDNFQKQTNRNRTYIYSPNGIQLLNIPVKHSKTAHQKTKDILIENEFDWQKQHFKSLEAAYRSSPFFEYFEDDIVPIFEKKHEFLMDLNFEVLDVVTKCLRMKLEFGKTTEYFHEVTDFADFRYLANGKKDANSFEKYTQVFDDKHGFINNLSVLDLLFNEGKFAMDYLKTQKII
>NZ_CP016907.1|WP_066033658.1|2627233_2628982_-|PspC-domain-containing-protein
MNKTVNINLGGMFFHIDEDAYLKLTRYFDAIKRSLNNSSGQDEIIKDIEMRVSELLTEKQKSEKHVVGLKDVDEVIAVMGQPEDYRIEDEENPNQSYNNYGPRKHKKLYRDKEKGMIGGVATGLGHYFGIDAVWIKIIFLIFVFAGFGTGILAYFVLWIVTPEAVTTSEKLEMTGEPVTISNIEKKVREEIDSLSEKFKNADYDKMGNQVKSGAERISSSFGDFIMTIFKIFAKFLGVILIISGISTLIMLLIGVFTLGTNIFIDFPWQNFIEAGNFTEYPLWSFGLLMFFAVGIPFFFLTLLGFKLLSPNLKSIGNITKYTLLALWIISIAILTSIGIKQATEISYDNKVVEKKVLAIKPTDTLYIKFKYNDYYTKSLNHYREFEFVQDSANNELIYSNDVRLHVLHTDESTPFIQIEKSARGNSFTNAKKRAEKINYKFQVNGNQLLLDNYFLTDVKNKFRGQEVDIYLYVPEGQLIKPDSSVRDYYNSDDNFFELNYNGDYNYKVIGTKVKCLNCPADEDNDNNYESDYENDQNDSDTNTTNDTIKEVSVKINGKEVLNGKKTKGKLTTDKNGVIIKIN
>NZ_CP016907.1|WP_008464689.1|2628985_2629318_-|PadR-family-transcriptional-regulator
MNIENTKAQMRKGVLEFCILSVLKEKDAYTSEILDTLKNAKLLVVEGTVYPLLTRLKNDGLLNYRWEESTSGPPRKYYGLTEIGQTFLNELSGTWTELSDAVNLITNQNQ
>NZ_CP016907.1|WP_119792881.1|2629466_2629946_-|DUF4870-domain-containing-protein
METTTPLIMEKTSEKNTAAFTHLSTLSQYIIPFGNYIFPLIIWTNYKDKSEFADHHGKQALNFQLSILLYSLILALIAIPIFVTVFLQNLPLEAVFNDDDFVIRNFNIQANIGILSVGITAVILFGLLKFVEFFLVIYASIKASNGELYKYPITIPFIK
>NZ_CP016907.1|WP_008464693.1|2630175_2630628_+|DUF4442-domain-containing-protein
MAVSVSKLNKFVLFKLPSAYFCGVRVKAIDKDSCIVSVKHRWINQNPFNSMYFAVQAMAAELTTGALVISQIQESGRKISMLVANNKGNFTKKATGRITFVCNDGHLIAEAIQKTIETGEGQTFWMKSIGTNEEGVQVSEMDFEWSVRLK
>NZ_CP016907.1|WP_164085586.1|2630732_2630894_-|hypothetical-protein
MTKVITIATAALFSIGIMAQETKPVTKDKEKKESCCKKTSTDKKDKKSCCVKK
>NZ_CP016907.1|WP_123907025.1|2631067_2633308_-|multicopper-oxidase-domain-containing-protein
MKIKYILIFFLIAFQLKAQKVVRYDLHVRDTIVNFSGKEKRAIAVNGQIPMPTLTFTEGDIAEIYVHNELKKESTSMHWHGLFLPNKEDGVPYLTQMPIEPGTTHKYTFPIIQNGTYWYHSHSGLQEQIGLYGLFIINKKKDDSTIRKGIDDLPTIPVILSEWSDLKPENIQRMLHNANDWFAVKKGTTQSYAEAIKQGHFSTKVTNEWKRMNAMDVSDVYYEKFLINGKNEQQFSDLKPGSKVRLRIANGGASSYFWLTYGGGKITVVASDGNDVEPVEVDRLITAVSETYDVVVTIPENNKSFAFLATAEDRTGSATLFLGNGEKQPVHHLSKLKYFEGMKMMNDMMKMNGEMNDMGMNMSLNKMDMNAVMYPEISGEDENAKPAMDHSNHNMENMKMQSDSTETSEIVTLNYGMLKSPFKTNLPKDAPVKELRFTLSGNMNRYVWSLDNKVVSETDKILIKKGENVRIVLYNGSMMRHPMHLHGHDFRILNEHGDYSPLKNVIDIMPMETDTIEFQANADGDWFFHCHILYHMMAGMGRIFSYENSAPNPLIHHPEMAFKMLKMDDRMFHFMAENDFATNGNDGEAMFSNTRWSIGTEWRLGYNDKHGYETETHIGRYIGKNQWLMPFIGFDWRYRKMGMDEQEQNLFGQKNTKDNRSVFSAGLEYTLPMLIKAQIEVYTDGNVRVQFERKDIPLSQRLRMNLMWNTDKEYMAGLKYIVGRNFGITTHYDSDMGIGFGVNLNY
>NZ_CP016907.1|WP_066033660.1|2633497_2636044_-|copper-translocating-P-type-ATPase
MTHQYIISGMSCDGCRKKVEKTLNEVQGVHAEVSLNPPIATITMDKHVPTEKFQKVLAAAGNYTIEMDSPKNHGEVAVKSCCSSHKKEHHGHNHDHHKTETKKVHQHSANGVYYCPMHCEGDKTYNKPGDCPVCGMDLVPQVAITATQFTCPMHPEVVSNEPGDCPICGMDLVPMQASESEENKTYTDLLKKMKIAILFTLPIFIISMSEMIPNNPLYNIMSIEKWNWVQLLFSIPVLFYAGWMFFVRAYKSIVTWNLNMFTLIGIGTSVAFLFSIVGMFFPDIFPSEFKSHHGTIHLYFEAATVIITLVLLGQLLEAKAHGQTNGAIKELLKLAPTEATLVENGLDKVISIHNIKKGDLLRVKPGEKIPVDGKITTGESNIDESMITGEPIPVDKKTGNAVISGTINGAKSFVMIAEKVGSETMLSQIIQMVNDASRSRAPIQKLVDRVSKYFVPTVVIISIITFFVWAKFGPEPAYVYGLINAIAVLIIACPCALGLATPMSVMVGVGKGAQNGILIKNAEALENMNKIDVLITDKTGTITEGKPSVEKIYAINNDEDFLLQNIASLNQHSEHPLAQAVVNFAKAKNSSLKEVHGFETIAGKGVLGTIENISVALGNKKLMDEIGASVSNDLEQKVISEQNLGKTISYIAIEKSVLGFVAITDAIKENSAKAIKELISQGVEVIMMTGDNHNTAKAVAEHLHLSSFKADCLPQDKLKEIERLQAQGKIVAMAGDGINDAPALAQSNIGIAMGTGTDVAIESAKITLVKGDLNGIVKAKNLSHAVMSNIKQNLFFAFIYNTLGVPIAAGILYPVFGILLSPMLAAVAMSLSSVSVIVNALRLRNLKL
>NZ_CP016907.1|WP_066033661.1|2636497_2637058_-|helix-turn-helix-transcriptional-regulator
MKLYIKNMVCSRCKMVVKSEFEKLGLQTTAVELGEVELNEEISDSQKEILLENLQALGFDLIDDKKTKTVERIKNLIVDLVHHKNNDLKINLSEYLAENLNQDYNSLSNLFSEIENTTIEKYFISQKIEKVKELLIYNELSLSEIADILNYSNVAHLSNQFKKITGFTPTSFKQSKDKMRIQIENI
>NZ_CP016907.1|WP_066035145.1|2637060_2637588_-|DUF3347-domain-containing-protein
MKKSIIALATTLTIVFNANTIQAKTNTTELTAIEMADSQLQSVYDAYFTVKDALIKSDSKLTSAKAKDLLTAITAVKMDKLKNNEHTVWMKVVKKLTADAKSISATTDLKKQRETFKSLSKSTYDLIKVSNPEQPIYKQYCPMADADWLSKEKAVKNPYYGSSMLTCGNVVETIK
>NZ_CP016907.1|WP_066033662.1|2637685_2638018_-|hypothetical-protein
MLFITLSFFLNPSYTFACHTGHSKEITAKEENSCSKKCCEKKTSKQEKHNCDGKCRHSGCNTSTLNIFLTSNDFDLQNDVFNFSLKNTISSYSNSTISSGFTSIWLKPKI

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Crispr_ID: NZ_CP016907_6

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP016907_6

3611092-3611315

Orphan

Consensus_repeat	Method
ATTAAATTATCTAACGTTGTTAAGTAAA	CRISPRCasFinder

3 spacers

The CRISPR arrays of NZ_CP016907_6

>merge|NZ_CP016907|6|3611092-3611315|CRISPRCasFinder
ATTAAATTATCTAACGTTGTTAAGTAAATGTGCGCAAATTTCCATACAGTAAGCCTTTCCAATTCTATTTTAAATCAGTATTAAATTATCTAACGTTGTTAAGTAAAAGTCTAAAAAAAGAGCTTTTATTACCTTTATTAAATTTTCTAACAGTGTTAAGCGAAAGTTATAAAAAAAAGGATTTTATGTTATCCCGTTTAAATCATTTTACACTGTTAAGTAAA

>NZ_CP016907|6|6|3611092-3611315|CRISPRCasFinder
ATTAAATTATCTAACGTTGTTAAGTAAA	TGTGCGCAAATTTCCATACAGTAAGCCTTTCCAATTCTATTTTAAATCAGT
ATTAAATTATCTAACGTTGTTAAGTAAA	AGTCTAAAAAAAGAGCTTTTATTACCTTT
ATTAAATTTTCTAACAGTGTTAAGCGAA	AGTTATAAAAAAAAGGATTTTATGTTATCCCG
TTTAAATCATTTTACACTGTTAAGTAAA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP016907.1\|WP_066034214.1\|3618766_3619855_-\|efflux-RND-transporter-periplasmic-adaptor-subunit	unknown	unknown	gnl\|CDD\|273776
NZ_CP016907.1\|WP_066034201.1\|3600744_3601254_-\|DinB-family-protein	unknown	unknown	gnl\|CDD\|378981
NZ_CP016907.1\|WP_066034203.1\|3602371_3603103_-\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|366181
NZ_CP016907.1\|WP_123906998.1\|3613727_3614063_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP016907.1\|WP_066034212.1\|3616879_3617500_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP016907.1\|WP_123907029.1\|3612171_3613074_-\|SMP-30/gluconolactonase/LRE-family-protein	unknown	unknown	gnl\|CDD\|225921
NZ_CP016907.1\|WP_066034210.1\|3615535_3615769_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP016907.1\|WP_066034205.1\|3603997_3604615_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP016907.1\|WP_066035191.1\|3613231_3613660_+\|cupin-domain-containing-protein	unknown	unknown	gnl\|CDD\|380344
NZ_CP016907.1\|WP_066034211.1\|3615836_3616808_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP016907.1\|WP_008467738.1\|3601431_3601641_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP016907.1\|WP_008467744.1\|3599993_3600155_+\|DUF1328-domain-containing-protein	unknown	unknown	gnl\|CDD\|227774
NZ_CP016907.1\|WP_066034206.1\|3606687_3609852_-\|efflux-RND-transporter-permease-subunit	unknown	unknown	gnl\|CDD\|223911
NZ_CP016907.1\|WP_123906999.1\|3617560_3618493_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP016907.1\|WP_066034209.1\|3614429_3614978_+\|type-1-glutamine-amidotransferase	unknown	unknown	gnl\|CDD\|153228
NZ_CP016907.1\|WP_066035190.1\|3604941_3606360_-\|TolC-family-protein	unknown	unknown	gnl\|CDD\|224455
NZ_CP016907.1\|WP_066034202.1\|3601654_3602035_-\|DoxX-family-protein	unknown	unknown	gnl\|CDD\|379266
NZ_CP016907.1\|WP_066034204.1\|3603174_3603780_-\|Crp/Fnr-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|223736
NZ_CP016907.1\|WP_008467741.1\|3600249_3600717_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|369297
NZ_CP016907.1\|WP_008467721.1\|3611329_3611923_-\|TetR/AcrR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224228

Protein	Function_ID	Function_description	E-value
NZ_CP016907.1\|WP_008467744.1\|3599993_3600155_+\|DUF1328-domain-containing-protein	gnl\|CDD\|227774	COG5487, COG5487, Small integral membrane protein [Function unknown].	0.000143084
NZ_CP016907.1\|WP_066034201.1\|3600744_3601254_-\|DinB-family-protein	gnl\|CDD\|378981	pfam12867, DinB_2, DinB superfamily. The DinB family are an uncharacterized family of potential enzymes. The structure of these proteins is composed of a four helix bundle.	4.06586e-11
NZ_CP016907.1\|WP_066034203.1\|3602371_3603103_-\|GNAT-family-N-acetyltransferase	gnl\|CDD\|366181	pfam00583, Acetyltransf_1, Acetyltransferase (GNAT) family. This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.	3.15313e-08
NZ_CP016907.1\|WP_066034214.1\|3618766_3619855_-\|efflux-RND-transporter-periplasmic-adaptor-subunit	gnl\|CDD\|273776	TIGR01730, COG0845:_Membrane-fusion_protein, RND family efflux transporter, MFP subunit. This model represents the MFP (membrane fusion protein) component of the RND family of transporters. RND refers to Resistance, Nodulation, and cell Division. It is, in part, a subfamily of pfam00529 (Pfam release 7.5) but hits substantial numbers of proteins missed by that model. The related HlyD secretion protein, for which pfam00529 is named, is outside the scope of this model. Attributed functions imply outward transport. These functions include nodulation, acriflavin resistance, heavy metal efflux, and multidrug resistance proteins. Most members of this family are found in Gram-negative bacteria. The proposed function of MFP proteins is to bring the inner and outer membranes together and enable transport to the outside of the outer membrane. Note, however, that a few members of this family are found in Gram-positive bacteria, where there is no outer membrane. [Transport and binding proteins, Unknown substrate].	5.34756e-49
NZ_CP016907.1\|WP_066034204.1\|3603174_3603780_-\|Crp/Fnr-family-transcriptional-regulator	gnl\|CDD\|223736	COG0664, Crp, cAMP-binding proteins - catabolite gene activator and regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms].	2.57524e-16
NZ_CP016907.1\|WP_123907029.1\|3612171_3613074_-\|SMP-30/gluconolactonase/LRE-family-protein	gnl\|CDD\|225921	COG3386, COG3386, Gluconolactonase [Carbohydrate transport and metabolism].	8.69528e-56
NZ_CP016907.1\|WP_066034206.1\|3606687_3609852_-\|efflux-RND-transporter-permease-subunit	gnl\|CDD\|223911	COG0841, AcrB, Cation/multidrug efflux pump [Defense mechanisms].	0
NZ_CP016907.1\|WP_066034209.1\|3614429_3614978_+\|type-1-glutamine-amidotransferase	gnl\|CDD\|153228	cd03134, GATase1_PfpI_like, A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus furiosus. A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus furiosus. This group includes proteins similar to PfpI from P. furiosus. and PH1704 from Pyrococcus horikoshii. These enzymes are ATP-independent intracellular proteases and may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For PH1704, it is believed that this Cys together with a different His in one monomer and Glu (from an adjacent monomer) forms a different catalytic triad from the typical GATase1domain. PfpI is homooligomeric. Protease activity is only found for oligomeric forms of PH1704.	2.66395e-79
NZ_CP016907.1\|WP_066035190.1\|3604941_3606360_-\|TolC-family-protein	gnl\|CDD\|224455	COG1538, TolC, Outer membrane protein [Cell envelope biogenesis, outer membrane / Intracellular trafficking and secretion].	1.30126e-66
NZ_CP016907.1\|WP_066034202.1\|3601654_3602035_-\|DoxX-family-protein	gnl\|CDD\|379266	pfam13564, DoxX_2, DoxX-like family. This family of uncharacterized proteins are related to DoxX pfam07681.	1.64896e-15
NZ_CP016907.1\|WP_066035191.1\|3613231_3613660_+\|cupin-domain-containing-protein	gnl\|CDD\|380344	cd02214, cupin_MJ1618, Methanocaldococcus jannaschii MJ1618 and related proteins, cupin domain. This family includes bacterial and archaeal proteins homologous to MJ1618, a Methanocaldococcus jannaschii protein of unknown function with a cupin beta barrel domain. The active site of members of the cupin superfamily is generally located at the center of a conserved barrel and usually includes a metal ion.	7.43751e-19
NZ_CP016907.1\|WP_008467741.1\|3600249_3600717_-\|hypothetical-protein	gnl\|CDD\|369297	pfam07274, DUF1440, Protein of unknown function (DUF1440). This family contains a number of bacterial proteins of unknown function approximately 180 residues long. These are possibly integral membrane proteins.	0.00015875
NZ_CP016907.1\|WP_008467721.1\|3611329_3611923_-\|TetR/AcrR-family-transcriptional-regulator	gnl\|CDD\|224228	COG1309, AcrR, Transcriptional regulator [Transcription].	9.4633e-12

>NZ_CP016907.1|WP_066034206.1|3606687_3609852_-|efflux-RND-transporter-permease-subunit
MFKIFIQRPVLATVISILLVILGVLGLTKLPLQQFPDIAPPSVLVTAVYPGANAETVLRSVAPSLEESINGVENMTYMSSTASNDGTLAITVFFKLGTDADQAAVNVQNRVAQATSQLPAEVVQQGIITAKQQNSFIMAIGMYTDDEAKYDQTFVANYAQINIIPELKRIPGVGSASIFGGVKDYSMRVWLNPTQMSAYKVTPSEVMGAIQDKSLEAAPGKFGERSKEVFEYVIKYKGKLTKPEDYENIAIRSNADGSVLRLKDVARVELGAYSYNSLTRLNGKKGIVIGVIQLAGSNSNDIQIAINKMMEKASKDFPKGIKHNIFYSTKVSLDQSIEQVEHTLIEAFILVFIVVFIFLQDFRSTLIPAIAVPVAILGTFFFMQLFGFSINLLTLFALILAIGIVVDDAIVVVEAVHAKMEHKRLSPKIATHEAMHEITGAIISITLVMAAVFLPVGFMEGSTGVFYRQFAFTMAIAIVISAVNALTLSPALAALFLKDNHRAHDHNEPYQKKGFKEKFFSAFNSSFESLTNRYVGGIKFLIRRKWLSLGGLALITLATVVMVKTTPSGFIPTEDQGFIAIAVNTPSGTSLDGTQKVMTEAENTLKALDASRFVTAISGFNLLTNSTSPSSAVVFVLLKPNEERGEIKNIDEIMNQVRGKLGSISGGSFFVFSFPTVPGFSNVEALDLVLQDKTGGKLDKFSGVSQNFIGELMKRPEIAVAFTSFKADYPQLQLEVNDEKANQLGVNVKDILQTMQAYFGSAQASDFNRFGKYYRVVVQADIEDRADPTSIDRVFVKNKTGEMVPINTLVKLTRIYGSETASRYNLFNSISINAIPKPGFSSGDAIKAIEEVAAQQLPAGYGFEFSGQTREEISSGGQSATIFLLCLIFVYFLLAAQYESYILPLAVILSIPAGIFGVFAAIGLTGIQNNIYVQVALVMLIGLLAKNAILIVEFAAQRRRSGQGLVAASIMAAKLRLRPIIMTSLAFVVGLIPMMSAKGPSAQGNHSISIGAAGGMLSGVVLGLFIIPVLFIIFQHLQEKVSGKPIAVIHNEEK
>NZ_CP016907.1|WP_066035190.1|3604941_3606360_-|TolC-family-protein
MKNHITKIVTFAILITTLISCKVSKDIETPKDAFPDNFRNASVSSDTTSIADVEWKNFFTEKDIIKLIDSAVARNNDLQIAEKNIEIAQYRFTQSKWGNVPQVNLFVNASTSNPSDNSFTGLNLNQAIGAKHIDDYSAGASLSWEADIWGKIRNQKKGAYAGYLQSEEVKKALQTNIVANVSRGYYNLLMLDAQLDIARQNLRLNDSTTNIIKLKYDAGQVTNLAIQQSEAQKLNSAQLIPLLEQNIAIQENVLSVLTGSFPNSKERSVKLSALEVKHNTAIGIPSALVSRRPDVKSAELALKVANANVGITKADLYPALRITAQGGVNSFETSNWFNIPASLFGTVAGGLTQPLLNNKRLKTQYNIALAEREKAVLAFRQSVLVAVSEVSDALVKVEKLQQQETFLKEKVKTLQQAIKNANLLFKNGLAEYLEVLTAQANLLQSELELADIKRQQLTANTDLYRALGGGWK
>NZ_CP016907.1|WP_066034205.1|3603997_3604615_-|hypothetical-protein
MKKYYFALFVFFFLIISCKKNIEVSNVSTLDTTKIVKPLPPLDYEQYLKNVPKTDSLCNGEIERAKKDLSKYDGVYVQTICFGCDFKPYEEEIKEVLKKRKFKLGIQDIGCVRYEGQTVGCYIEYIDLKMKEKYGENYKSEIENDAIKILIKNININNKIVSIYDLEPNEKPKILDPKIAIENDYYVTIKTDLPINKTGTRYFMY
>NZ_CP016907.1|WP_066034204.1|3603174_3603780_-|Crp/Fnr-family-transcriptional-regulator
MTFNKETYLNNLKLYFESYTPISEKSWKSIENLTHFQTVKKGEIVLENGEICKNLYFIAKGILRTFITDEQGNFYNKNLFLENKLACSKVSSILQTPSSFTIEALEDCILIRLNYKKYIQLISENDDLKTFYIAYLEKNWIIEKEQREVALVMQNATERYLNLLETHPTIADRVPLLHIASHLGITPTQLSRIRKSLEKDL
>NZ_CP016907.1|WP_066034203.1|3602371_3603103_-|GNAT-family-N-acetyltransferase
MDHINLIKDNIDNLTTLWKTVATPLLSYHKNDPFEFSQIKNSGWPNRLWSREDITEENFLQIQETMEKNPGLVIPYWDIFGSNSKEIFEKNGFHIRIQLVAMALKLGEKFPLQNNLTFKRVLNEEDAKTWSDIYPMSFSYVISKETLIANYENAKFYLVHFEGKAIGTLTLFQTYKTMGIHGVGVIPEMRKRGFAEEIMKFAINEAIDANCEYAQLQASALGKGIYTRLGFEDLFTITNYQLS
>NZ_CP016907.1|WP_066034202.1|3601654_3602035_-|DoxX-family-protein
MKTTKIIFWTTTILIFLFEGVMPALTSQTELAKEGIKHLGYPEYFGNALVVFKILGVLALIIPQVPGRIKEWAYAGFAFDFIFASISHFAVDGIGFQGFFPLIVFAVLIISYVTYHRIQRYKNIAL
>NZ_CP016907.1|WP_008467738.1|3601431_3601641_-|hypothetical-protein
MIEVFKTNVQEESQCNIIIEKLLEHYPNGSINFDLEDCDKILRIHAPAISNTKIIDILNSHGYFCEVLP
>NZ_CP016907.1|WP_066034201.1|3600744_3601254_-|DinB-family-protein
MKSAIQNTILETYSKLGDLLSSFSKEEINVVPFEGSWTAGQTAQHSILACSGLTMLFAGKTEKTNREPDENVKGLDSIFLDYTTKYQSPENIKPPAIEYEKGTLLASVKKIQNDLFEAAETYDLTLTCLDAKVPGFEYFTIYEWLHFAIVHTQRHTQQLKSIYEHIKKQ
>NZ_CP016907.1|WP_008467741.1|3600249_3600717_-|hypothetical-protein
MRSKVRTIVSSGLVAGTLDITAAILIYAGILHKTTAEKILQSIASGIFKKEAYTAGTEMTFVGLGLHFLIAFIFAWFYFKIFPYIPFFKINTLLSGVSYGFFIWVVMNLVVLPIVFPVLPEKKLDFPLLLSILIVIFCVGIPIAFITRKYYAKWY
>NZ_CP016907.1|WP_008467744.1|3599993_3600155_+|DUF1328-domain-containing-protein
MLRWTVIFIILAIIAGIFGFGGIAAGAASIAKVLFFIFLVLFIISLITGRRKV
>NZ_CP016907.1|WP_008467721.1|3611329_3611923_-|TetR/AcrR-family-transcriptional-regulator
MASKDRILRQKEETRNNILGAAYDIVKDEGWNGLSMRKIADRIEYTAPIIYEYFSNKEAILEELTGKGFIKLAKELQTAKDKFEKPEDQLEAMWMTYWDFAFTNTEMYQLMFGVQMTCCAQRCSAQEAPYKLFTGVIAEIMKDSNPSEDIIKQKYFTFFSVIHGLIAINIINKSDILETINAQILKDAITGIIKSIQ
>NZ_CP016907.1|WP_123907029.1|3612171_3613074_-|SMP-30/gluconolactonase/LRE-family-protein
MKSHFLFLITLTFTNFIYAQSLKEKSHSIIAKGAVLTKLSDQFSFTEGPASDKKGNIYFTDQPNNRIMKWSVNGQLSVFMENAGRANGLYFDHTGNLLACADEKNELWKIDENKKYTVILNNFEGKRLNGPNDLWVDTKGGIYFTDPFYQRDYWKHTSKEIEKECVYYLSPDKSKIINVESDLVKPNGIIGTSNGKTLYVADIAGNKTYSYTIESNGSLSKKTLFTESGSDGMTIDESGNIYLCGKGVTIFNPKGEKIAHIDVPEPWTANVCFGGKKFKTLFITASKSVYTIEMNVRGMK
>NZ_CP016907.1|WP_066035191.1|3613231_3613660_+|cupin-domain-containing-protein
MKTLTILQTTIAVLFFQKTFCQETKKETPQYTIENCVNHFDINKATKTKVGYQYWFANKDFTQENTLKMSIVEPGKSTHAPHHHPEEEFFYILEGTAEFFLDGKTVTAGPNTSFYCPPNAEHGISNAGKTDLKYLVIKKDLR
>NZ_CP016907.1|WP_123906998.1|3613727_3614063_-|hypothetical-protein
MPLTKKIAELMSKKYNTNITILGDYEGSNHTSILDNDNGTILVVSDRNQFYFKDRHRNLWLSVLDPFQIDGKKHFPELGDSYTLNHGVQYSFTTQEAIVEMASLYFAKHAD
>NZ_CP016907.1|WP_066034209.1|3614429_3614978_+|type-1-glutamine-amidotransferase
MKKNIAILATNGFEESELASSKAYLEEQGWNADIVSLKSGTIKAWKDGNWSNEYNVDVVLDQANEADYDALVLPGGVINPDSLRREEAAVNFVRSFFESKKPVAAICHGPQILVDADVLDGRKVTSFFSVKNDLKNAGAQWEDSEVVVDNGLVTSRNPNDLPAFNKKMVEEIKEGIHERQRA
>NZ_CP016907.1|WP_066034210.1|3615535_3615769_+|hypothetical-protein
MNSNTLSKEAETRLIDFFNHIIDPEDMAKILRQVNCILALGVMRQHETLQIGLTNFEDNYYWLNELAEILNPYLSEE
>NZ_CP016907.1|WP_066034211.1|3615836_3616808_-|hypothetical-protein
MKHQTLSQKLDQIERKVKNKVYKCIYEDCNEIAIKSHVLQKNGILNSISYNNHLYQVIGNSPFEEQTKGKFQFQKIGINNIYTFPGFCKNHDASIFSSIENTKKMDLKSEKNLCLFAYRSLCQEIRRKEMAFDIASGYLDISTGIKSVVFLSNYKKGILNSLNNLLFFKKEFENELKNNKNRFIYKVCEINRLEICISSPINIIDSENSLSRTNLNGERINPFTTSIINIFPYKDKSYVLIAFHADYICKWSEILFEKIINSDDAQIKKIISDLISTRIEFWCISPELYNTLDEKKKKELFTIWEKEAFNHSWNIENTFNLFQ
>NZ_CP016907.1|WP_066034212.1|3616879_3617500_+|hypothetical-protein
MDINFYNKISRSYQILSDRFTNFSKSYQNGYIIYDKNMFQVRDDQFKFLKQFENIPFGTFFNDDFIKKNDTGGDYYKSSSIIETEKTMNIHSEFYMILFYYLINEFKQDLQNLLDLLESDIFKEKYRGFYKVDEFKFKYYLSEHESIFKFIMDRIQNFGLIYHLFHRTNSGFIYATESEMVFRVQAIKDLLEANSRIYNFQKFRIV
>NZ_CP016907.1|WP_123906999.1|3617560_3618493_+|hypothetical-protein
METNIVDIQDRVLDYGDIRKQSIRAEHGIRSLCVMYDDHSTDVNSKENIFILKENVHYRVFSLVHQYQIFLSQLDFHEHNLNQLYKANPHYLSAFPFGNPHFKQVDLEMSSVFDNVIFQISSVYDYLSHLICYICKINKSDTLYWTKLAKAAAGQNNEFSNLEIRNTIADLNREFVARLYDYRSRLLHNKKDDHIFNGEIKLEGFNFNLKILASDTAIRHFKGIRKIYESEQITLAFLTSWMIKKTFIDIETILDALREEILKKSNFENNLRNPKNKNNAMFFYMEPGTNEVRPASEGLWNEYKNWDKHN
>NZ_CP016907.1|WP_066034214.1|3618766_3619855_-|efflux-RND-transporter-periplasmic-adaptor-subunit
MNTKIIKYSPLFLVAVFFMNSCNSKKEEPVKAEIEPKVETFLLAKEKLTTELRLPAELTGFQQVDLYAKVSSFVKTLKVDIGSKVKKGQLLIVLEAPEISSQLAAAESRLKSMEAIYATSKSTYNRLYETSKVEGTISKNDLEMASGKKNSDYAQYQAAIAAHKEISIMRGYLEIRAPFDGVVAARNVNLGTFVGPQGKGSDLPLLTIQEQSKLRLAVSVPELYTGYLHPGDEMSFNVKSLPETFTAKITRMSGALDLKLRSERVEMDVHNTKGNLLPGMVAEVLLPLNAKDSTFVVPKSAVVNSAEGLYVVKVVNHKATRVDIKKGREIEDKIEIFGDLTPNDKLVKIASEETKEGDVINE

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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_CP016907_6	6.2\|3611199\|29\|NZ_CP016907\|CRISPRCasFinder	3611199-3611227	29	NZ_CP033935	Chryseobacterium balustinum strain KC_1863 plasmid unnamed, complete sequence	17201-17229	6	0.793
NZ_CP016907_6	6.2\|3611199\|29\|NZ_CP016907\|CRISPRCasFinder	3611199-3611227	29	NC_014533	Gloeothece verrucosa PCC 7822 plasmid Cy782201, complete sequence	490517-490545	7	0.759
NZ_CP016907_6	6.2\|3611199\|29\|NZ_CP016907\|CRISPRCasFinder	3611199-3611227	29	KT895374	Bacillus phage vB_BpuM-BpSp, complete genome	103359-103387	7	0.759
NZ_CP016907_6	6.3\|3611256\|32\|NZ_CP016907\|CRISPRCasFinder	3611256-3611287	32	NC_018510	Bacillus thuringiensis HD-789 plasmid pBTHD789-3, complete sequence	203311-203342	7	0.781
NZ_CP016907_6	6.3\|3611256\|32\|NZ_CP016907\|CRISPRCasFinder	3611256-3611287	32	NZ_CP013280	Bacillus thuringiensis serovar israelensis strain AM65-52 plasmid pAM65-52-5-100K, complete sequence	63517-63548	7	0.781
NZ_CP016907_6	6.3\|3611256\|32\|NZ_CP016907\|CRISPRCasFinder	3611256-3611287	32	NZ_CP039726	Bacillus thuringiensis strain BT-59 plasmid p5, complete sequence	72563-72594	7	0.781
NZ_CP016907_6	6.3\|3611256\|32\|NZ_CP016907\|CRISPRCasFinder	3611256-3611287	32	NZ_CP009350	Bacillus thuringiensis HD1002 plasmid 4, complete sequence	92347-92378	7	0.781
NZ_CP016907_6	6.3\|3611256\|32\|NZ_CP016907\|CRISPRCasFinder	3611256-3611287	32	NC_014533	Gloeothece verrucosa PCC 7822 plasmid Cy782201, complete sequence	479559-479590	7	0.781
NZ_CP016907_4	4.1\|2387809\|31\|NZ_CP016907\|CRISPRCasFinder	2387809-2387839	31	NZ_CP046704	Nostoc sp. ATCC 53789 plasmid pNsp_a, complete sequence	51510-51540	8	0.742
NZ_CP016907_6	6.3\|3611256\|32\|NZ_CP016907\|CRISPRCasFinder	3611256-3611287	32	NZ_CP017573	Bacillus thuringiensis strain SCG04-02 plasmid PSCG61, complete sequence	54767-54798	8	0.75
NZ_CP016907_6	6.3\|3611256\|32\|NZ_CP016907\|CRISPRCasFinder	3611256-3611287	32	MN855778	Myoviridae sp. isolate 416, complete genome	10860-10891	8	0.75
NZ_CP016907_6	6.3\|3611256\|32\|NZ_CP016907\|CRISPRCasFinder	3611256-3611287	32	NC_014533	Gloeothece verrucosa PCC 7822 plasmid Cy782201, complete sequence	59532-59563	9	0.719
NZ_CP016907_6	6.3\|3611256\|32\|NZ_CP016907\|CRISPRCasFinder	3611256-3611287	32	MN693753	Marine virus AFVG_250M679, complete genome	6054-6085	9	0.719
NZ_CP016907_6	6.3\|3611256\|32\|NZ_CP016907\|CRISPRCasFinder	3611256-3611287	32	NZ_CP032531	Bacillus megaterium NCT-2 plasmid pNCT2_3, complete sequence	1036-1067	10	0.688
NZ_CP016907_6	6.3\|3611256\|32\|NZ_CP016907\|CRISPRCasFinder	3611256-3611287	32	KT995479	Bacillus phage BM5, complete genome	25703-25734	10	0.688

1. spacer 6.2|3611199|29|NZ_CP016907|CRISPRCasFinder matches to NZ_CP033935 (Chryseobacterium balustinum strain KC_1863 plasmid unnamed, complete sequence) position: , mismatch: 6, identity: 0.793

agtctaaaaaaagagcttttattaccttt	CRISPR spacer
tgtttaaaaaaagagcttttataagttct	Protospacer
 **.****************** * .*.*

2. spacer 6.2|3611199|29|NZ_CP016907|CRISPRCasFinder matches to NC_014533 (Gloeothece verrucosa PCC 7822 plasmid Cy782201, complete sequence) position: , mismatch: 7, identity: 0.759

agtctaaaaaaagagcttttattaccttt	CRISPR spacer
tgtctaaaacaagagcttttattggttaa	Protospacer
 ******** *************. .*

3. spacer 6.2|3611199|29|NZ_CP016907|CRISPRCasFinder matches to KT895374 (Bacillus phage vB_BpuM-BpSp, complete genome) position: , mismatch: 7, identity: 0.759

agtctaaaaaaagagcttttattaccttt	CRISPR spacer
agtctaaaaaaagatctttttttaatcga	Protospacer
************** ***** *** ..

4. spacer 6.3|3611256|32|NZ_CP016907|CRISPRCasFinder matches to NC_018510 (Bacillus thuringiensis HD-789 plasmid pBTHD789-3, complete sequence) position: , mismatch: 7, identity: 0.781

agttataaaaaaaaggattttatgttatcccg	CRISPR spacer
atctataaaaataaggattttatgttatttta	Protospacer
* .******** ****************....

5. spacer 6.3|3611256|32|NZ_CP016907|CRISPRCasFinder matches to NZ_CP013280 (Bacillus thuringiensis serovar israelensis strain AM65-52 plasmid pAM65-52-5-100K, complete sequence) position: , mismatch: 7, identity: 0.781

agttataaaaaaaaggattttatgttatcccg	CRISPR spacer
atctataaaaataaggattttatgttatttta	Protospacer
* .******** ****************....

6. spacer 6.3|3611256|32|NZ_CP016907|CRISPRCasFinder matches to NZ_CP039726 (Bacillus thuringiensis strain BT-59 plasmid p5, complete sequence) position: , mismatch: 7, identity: 0.781

agttataaaaaaaaggattttatgttatcccg	CRISPR spacer
atctataaaaataaggattttatgttatttta	Protospacer
* .******** ****************....

7. spacer 6.3|3611256|32|NZ_CP016907|CRISPRCasFinder matches to NZ_CP009350 (Bacillus thuringiensis HD1002 plasmid 4, complete sequence) position: , mismatch: 7, identity: 0.781

agttataaaaaaaaggattttatgttatcccg	CRISPR spacer
atctataaaaataaggattttatgttatttta	Protospacer
* .******** ****************....

8. spacer 6.3|3611256|32|NZ_CP016907|CRISPRCasFinder matches to NC_014533 (Gloeothece verrucosa PCC 7822 plasmid Cy782201, complete sequence) position: , mismatch: 7, identity: 0.781

--agttataaaaaaaaggattttatgttatcccg	CRISPR spacer
ccaat--taaaaaaaacgattttatgtcatccac	Protospacer
  *.*  ********* **********.****

9. spacer 4.1|2387809|31|NZ_CP016907|CRISPRCasFinder matches to NZ_CP046704 (Nostoc sp. ATCC 53789 plasmid pNsp_a, complete sequence) position: , mismatch: 8, identity: 0.742

atgaaattgagactaaagagtttattttttg	CRISPR spacer
atgaaaatgcgactaaagagtttttatcagc	Protospacer
****** ** ************* * *.

10. spacer 6.3|3611256|32|NZ_CP016907|CRISPRCasFinder matches to NZ_CP017573 (Bacillus thuringiensis strain SCG04-02 plasmid PSCG61, complete sequence) position: , mismatch: 8, identity: 0.75

agttataaaaaaaaggattttatgttatcccg	CRISPR spacer
atctataaaaataaggtttttatgttattttt	Protospacer
* .******** **** ***********...

11. spacer 6.3|3611256|32|NZ_CP016907|CRISPRCasFinder matches to MN855778 (Myoviridae sp. isolate 416, complete genome) position: , mismatch: 8, identity: 0.75

agttataaaaaaaaggattttatgttatcccg	CRISPR spacer
tgcaagaaaaaaacggattttattttatcgct	Protospacer
 *. * ******* ********* ***** *

12. spacer 6.3|3611256|32|NZ_CP016907|CRISPRCasFinder matches to NC_014533 (Gloeothece verrucosa PCC 7822 plasmid Cy782201, complete sequence) position: , mismatch: 9, identity: 0.719

agttataaaaaaaaggattttatgttatcccg	CRISPR spacer
tcgattaaaaataaggattttatgtcatccgc	Protospacer
     ****** *************.****

13. spacer 6.3|3611256|32|NZ_CP016907|CRISPRCasFinder matches to MN693753 (Marine virus AFVG_250M679, complete genome) position: , mismatch: 9, identity: 0.719

agttataaaaaaaaggattttatgttatcccg	CRISPR spacer
agttattaaaaaaaggattttttgcagacata	Protospacer
****** ************** **. . * ..

14. spacer 6.3|3611256|32|NZ_CP016907|CRISPRCasFinder matches to NZ_CP032531 (Bacillus megaterium NCT-2 plasmid pNCT2_3, complete sequence) position: , mismatch: 10, identity: 0.688

agttataaaaaaaaggattttatgttatcccg	CRISPR spacer
ttgtataaaaaccaggattttatgtttttaaa	Protospacer
   ********  ************* *.  .

15. spacer 6.3|3611256|32|NZ_CP016907|CRISPRCasFinder matches to KT995479 (Bacillus phage BM5, complete genome) position: , mismatch: 10, identity: 0.688

agttataaaaaaaaggattttatgttatcccg	CRISPR spacer
agttataataaaaaggaatttattaaaagaga	Protospacer
******** ******** *****   *    .

Prophage detection

Region

Region Position

Protein_number

Hit_taxonomy

Key_proteins

Att_site

Prophage annotation

DBSCAN-SWA_1

2097008 : 2106936

Klosneuvirus(11.11%)

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

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_066033331.1\|2097008_2097701_+	NUDIX hydrolase	A0A1V0SIB1	Klosneuvirus	1.3e-09	35.1
WP_066033332.1\|2097775_2098609_+	ribose-phosphate pyrophosphokinase	A0A0S1RV70	Klebsiella_phage	1.2e-41	42.4
WP_066033333.1\|2098728_2099256_+	NADAR family protein	A0A1S6UAJ7	Serratia_phage	1.1e-37	50.0
WP_066033334.1\|2099266_2099773_+	O-acetyl-ADP-ribose deacetylase	A0A0K1L687	Scale_drop_disease_virus	3.1e-32	43.7
WP_066033335.1\|2099900_2100548_+	DUF4291 domain-containing protein	NA	NA	NA	NA
WP_066033336.1\|2100540_2101089_+	RNA 2'-phosphotransferase	A0A2R2ZGT8	Clostridioides_phage	2.2e-52	53.8
WP_066033337.1\|2101085_2101817_+	serine/threonine protein phosphatase	S0A0Y6	Cellulophaga_phage	7.6e-40	33.6
WP_066033338.1\|2101819_2102755_+	hypothetical protein	G3M9X5	Bacillus_virus	2.3e-33	30.7
WP_066033339.1\|2102766_2104236_+	nicotinate phosphoribosyltransferase	A0A218KC49	Bacillus_phage	1.1e-154	57.8
WP_008465373.1\|2104287_2104884_+	rhodanese-like domain-containing protein	NA	NA	NA	NA
WP_066033340.1\|2104942_2105644_-	hypothetical protein	NA	NA	NA	NA
WP_066033341.1\|2105644_2106256_-	nicotinate-nucleotide adenylyltransferase	NA	NA	NA	NA
WP_008465369.1\|2106363_2106936_-	guanylate kinase	A0A1W6JK60	Lactococcus_phage	1.1e-12	34.3

DBSCAN-SWA_2

2475870 : 2487190

Enterobacteria_phage(25.0%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_066033558.1\|2475870_2476989_+	GDP-mannose 4,6-dehydratase	M4QRT5	Synechococcus_phage	3.2e-122	62.5
WP_066033559.1\|2477033_2477966_+	GDP-L-fucose synthase	M1HKX0	Paramecium_bursaria_Chlorella_virus	1.7e-108	61.3
WP_066033560.1\|2477975_2478947_+	glycosyltransferase family 4 protein	NA	NA	NA	NA
WP_066033561.1\|2478936_2479359_+	hypothetical protein	NA	NA	NA	NA
WP_066033562.1\|2479358_2480492_+	aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme	A0A0P0YLZ6	Yellowstone_lake_phycodnavirus	7.0e-16	26.7
WP_066033563.1\|2480501_2481050_+	dTDP-4-dehydrorhamnose 3,5-epimerase	I7HJC4	Enterobacteria_phage	1.3e-39	47.7
WP_066033564.1\|2481049_2481895_+	dTDP-4-dehydrorhamnose reductase	I7HXC9	Enterobacteria_phage	4.7e-41	37.5
WP_066033565.1\|2481955_2482840_+	glucose-1-phosphate thymidylyltransferase RfbA	H9NC64	Sphingomonas_phage	1.4e-99	63.1
WP_066033566.1\|2482925_2484893_+	polysaccharide biosynthesis protein	L7Y3T9	Megavirus	5.1e-30	32.2
WP_066033567.1\|2485042_2485909_+	ABC transporter permease	NA	NA	NA	NA
WP_066033568.1\|2485909_2487190_+	ABC transporter ATP-binding protein	W6JKT0	Anomala_cuprea_entomopoxvirus	4.9e-10	23.5

Anti-CRISPR protein detection

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

Overview of predicted results

Overview of the results

Cas Category Instructions

Results visualization

1. NZ_CP016907

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CRISPR-Cas detection and classification

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Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Self-targeting detection

MGE targeting detection<

Prophage detection

Anti-CRISPR protein detection