CRISPRimmunity

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_CP046316	Capnocytophaga sp. FDAARGOS_737 chromosome, complete genome	7 crisprs	cas9,cas2,PrimPol,RT,DEDDh,WYL,csa3,cas3,PD-DExK	0	7	0	0

1. NZ_CP046316

CRISPR-Cas detection and classification

Crispr_ID: NZ_CP046316_1

• CRISPR_ID: NZ_CP046316_1
• CRISPR_location: 131913-131999
• CRISPR_type: Orphan
• Repeat_type: NA
• Spacer_info: 1 spacers

Consensus repeat of NZ_CP046316_1

Consensus_repeat	Method
AAAGTGAACAGGCTCTACAGGTGC	CRISPRCasFinder

spacers of NZ_CP046316_1

>1.1|131937|39|NZ_CP046316|CRISPRCasFinder
CGGTTCAGCTGCTGGAGTAGGTTCTGCAGGAGGAGTAGT

CRISPR arrays and Neighbor proteins around NZ_CP046316_1

CRISPR arrays

The CRISPR arrays of NZ_CP046316_1

>merge|NZ_CP046316|1|131913-131999|CRISPRCasFinder
AAAGTGAACAGGCTCTACAGGTGCCGGTTCAGCTGCTGGAGTAGGTTCTGCAGGAGGAGTAGTAAAGTGAACAGGCTCTACAGGTAC

>NZ_CP046316|1|1|131913-131999|CRISPRCasFinder
AAAGTGAACAGGCTCTACAGGTGC	CGGTTCAGCTGCTGGAGTAGGTTCTGCAGGAGGAGTAGT
AAAGTGAACAGGCTCTACAGGTAC

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP046316.1|WP_009390874.1|124152_126177_+|tetratricopeptide-repeat-protein	unknown	unknown	gnl|CDD|276809
NZ_CP046316.1|WP_009390872.1|123305_123902_-|AhpC/TSA-family-protein	unknown	unknown	gnl|CDD|239268
NZ_CP046316.1|WP_034539967.1|122852_123236_-|SRPBCC-superfamily-protein	unknown	unknown	gnl|CDD|176856
NZ_CP046316.1|WP_009390882.1|132596_133631_-|virulence-RhuM-family-protein	unknown	unknown	gnl|CDD|379118
NZ_CP046316.1|WP_009390878.1|128800_129520_+|3'-5'-exonuclease	unknown	unknown	gnl|CDD|99825
NZ_CP046316.1|WP_009390887.1|137196_137763_-|aminoacyl-tRNA-hydrolase	unknown	unknown	gnl|CDD|235457
NZ_CP046316.1|WP_009390885.1|136741_137197_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP046316.1|WP_009390899.1|140711_141767_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP046316.1|WP_009390884.1|134659_136720_-|sialate-O-acetylesterase	unknown	unknown	gnl|CDD|238865
NZ_CP046316.1|WP_009390897.1|140109_140715_-|NADAR-family-protein	unknown	unknown	gnl|CDD|271319
NZ_CP046316.1|WP_009390889.1|137812_139117_-|30S-ribosomal-protein-S12-methylthiotransferase-RimO	unknown	unknown	gnl|CDD|273453
NZ_CP046316.1|WP_009390879.1|129536_130172_-|tRNA-(adenosine(37)-N6)-threonylcarbamoyltransferase-complex-dimerization-subunit-type-1-TsaB	unknown	unknown	gnl|CDD|274750
NZ_CP046316.1|WP_009390857.1|120641_121946_-|tRNA-lysidine(34)-synthetase-TilS	unknown	unknown	gnl|CDD|238950
NZ_CP046316.1|WP_009390895.1|139651_140029_-|glyoxalase	unknown	unknown	gnl|CDD|319947
NZ_CP046316.1|WP_009390893.1|139260_139605_+|hypothetical-protein	unknown	unknown	unknown
NZ_CP046316.1|WP_009390859.1|121958_122813_-|aminotransferase-class-IV	unknown	unknown	gnl|CDD|238254
NZ_CP046316.1|WP_009390875.1|126217_127546_+|hypothetical-protein	unknown	unknown	gnl|CDD|372583
NZ_CP046316.1|WP_009390877.1|127621_128776_+|serine-hydrolase	unknown	unknown	gnl|CDD|224594
NZ_CP046316.1|WP_009390883.1|133724_134615_-|fructose-bisphosphate-aldolase	unknown	unknown	gnl|CDD|180045
NZ_CP046316.1|WP_009390880.1|130185_130857_-|16S-rRNA-(cytidine(1402)-2'-O)-methyltransferase	unknown	unknown	gnl|CDD|381175

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
NZ_CP046316.1|WP_009390874.1|124152_126177_+|tetratricopeptide-repeat-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.	2.99316e-16
NZ_CP046316.1|WP_009390872.1|123305_123902_-|AhpC/TSA-family-protein	gnl|CDD|239268	cd02970, PRX_like2, Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. Members of this group contain a CXXC motif, similar to TRX. The second cysteine in the motif corresponds to the peroxidatic cysteine of PRX, however, these proteins do not contain the other two residues of the catalytic triad of PRX. PRXs confer a protective antioxidant role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either thioredoxin, glutathione, trypanothione and AhpF. TRXs alter the redox state of target proteins by catalyzing the reduction of their disulfide bonds via the CXXC motif using reducing equivalents derived from either NADPH or ferredoxins.	3.81086e-35
NZ_CP046316.1|WP_034539967.1|122852_123236_-|SRPBCC-superfamily-protein	gnl|CDD|176856	cd07814, SRPBCC_CalC_Aha1-like, Putative hydrophobic ligand-binding SRPBCC domain of Micromonospora echinospora CalC, human Aha1, and related proteins. This family includes the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of Micromonospora echinospora CalC, human Aha1, and related proteins. Proteins in this group belong to the SRPBCC domain superfamily of proteins, which bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. MeCalC confers resistance to the enediyne, calicheamicin gamma 1 (CLM), by a self sacrificing mechanism which results in inactivation of both CalC and the highly reactive diradical enediyne species. MeCalC can also inactivate two other enediynes, shishijimicin and namenamicin. A crucial Gly of the MeCalC CLM resistance mechanism is not conserved in this subgroup. This family also includes the C-terminal, Bet v1-like domain of Aha1, one of several co-chaperones, which regulate the dimeric chaperone Hsp90. Aha1 promotes dimerization of the N-terminal domains of Hsp90, and stimulates its low intrinsic ATPase activity, and may regulate the dwell time of Hsp90 with client proteins. Aha1 can act as either a positive or negative regulator of chaperone-dependent activation, depending on the client protein, but the mechanisms by which these opposing functions are achieved are unclear. Aha1 is upregulated in a number of tumor lines co-incident with the activation of several signaling kinases.	0.000400258
NZ_CP046316.1|WP_009390882.1|132596_133631_-|virulence-RhuM-family-protein	gnl|CDD|379118	pfam13310, Virulence_RhuM, Virulence protein RhuM family. There are currently no experimental data for members of this group or their homologs. However, these proteins are implicated in virulence/pathogenicity because RhuM is encoded in the SPI-3 pathogenicity island in Salmonella typhimurium.	7.35136e-144
NZ_CP046316.1|WP_009390878.1|128800_129520_+|3'-5'-exonuclease	gnl|CDD|99825	cd05782, DNA_polB_like1_exo, Uncharacterized bacterial subgroup of the DEDDy 3'-5' exonuclease domain of family-B DNA polymerases. A subfamily of the 3'-5' exonuclease domain of family-B DNA polymerases. This subfamily is composed of uncharacterized bacterial family-B DNA polymerases. Family-B DNA polymerases contain an N-terminal DEDDy DnaQ-like exonuclease domain in the same polypeptide chain as the polymerase domain, similar to family-A DNA polymerases. This exonuclease domain contains three sequence motifs termed ExoI, ExoII and ExoIII, with a specific YX(3)D pattern at ExoIII. These motifs are involved in metal binding and catalysis. The exonuclease domain of family-B DNA polymerases has a fundamental role in proofreading activity. It contains a beta hairpin structure that plays an important role in active site switching in the event of a nucleotide misincorporation. Family-B DNA polymerases are predominantly involved in DNA replication and DNA repair.	3.84292e-58
NZ_CP046316.1|WP_009390887.1|137196_137763_-|aminoacyl-tRNA-hydrolase	gnl|CDD|235457	PRK05426, PRK05426, peptidyl-tRNA hydrolase; Provisional.	1.55557e-88
NZ_CP046316.1|WP_009390884.1|134659_136720_-|sialate-O-acetylesterase	gnl|CDD|238865	cd01827, sialate_O-acetylesterase_like1, sialate O-acetylesterase_like family of the SGNH hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.	2.11811e-81
NZ_CP046316.1|WP_009390897.1|140109_140715_-|NADAR-family-protein	gnl|CDD|271319	cd15457, NADAR, Escherichia coli swarming motility protein YbiA and related proteins. This family of uncharacterized domains was initially classified as Domain of Unknown Function (DUF1768). It contains members such as the E. coli swarming motility protein YbiA. Mutations in YbiA cause defects in Escherichia coli swarming, but not necessarily in motility. More recently, this family has been predicted to be involved in NAD-utilizing pathways, likely to act on ADP-ribose derivatives, and has been named the NADAR (NAD and ADP-ribose) superfamily.	1.02507e-42
NZ_CP046316.1|WP_009390889.1|137812_139117_-|30S-ribosomal-protein-S12-methylthiotransferase-RimO	gnl|CDD|273453	TIGR01125, Ribosomal_protein_S12_methylthiotransferase_RimO, ribosomal protein S12 methylthiotransferase RimO. Members of this protein are the methylthiotransferase RimO, which modifies a conserved Asp residue in ribosomal protein S12. This clade of radical SAM family proteins is closely related to the tRNA modification bifunctional enzyme MiaB (see TIGR01574), and it catalyzes the same two types of reactions: a radical-mechanism sulfur insertion, and a methylation of the inserted sulfur. This clade spans alpha and gamma proteobacteria, cyano bacteria, Deinococcus, Porphyromonas, Aquifex, Helicobacter, Campylobacter, Thermotoga, Chlamydia, Streptococcus coelicolor and Clostridium, but does not include most other gram positive bacteria, archaea or eukaryotes. [Protein synthesis, Ribosomal proteins: synthesis and modification].	2.54042e-161
NZ_CP046316.1|WP_009390879.1|129536_130172_-|tRNA-(adenosine(37)-N6)-threonylcarbamoyltransferase-complex-dimerization-subunit-type-1-TsaB	gnl|CDD|274750	TIGR03725, T6A_YeaZ, tRNA threonylcarbamoyl adenosine modification protein YeaZ. This family describes a protein family, YeaZ, now associated with the threonylcarbamoyl adenosine (t6A) tRNA modification. Members of this family may occur as fusions with ygjD (previously gcp) or the ribosomal protein N-acetyltransferase rimI, and is frequently encoded next to rimI. [Protein synthesis, tRNA and rRNA base modification].	1.63727e-58
NZ_CP046316.1|WP_009390857.1|120641_121946_-|tRNA-lysidine(34)-synthetase-TilS	gnl|CDD|238950	cd01992, PP-ATPase, N-terminal domain of predicted ATPase of the PP-loop faimly implicated in cell cycle control [Cell division and chromosome partitioning]. This is a subfamily of Adenine nucleotide alpha hydrolases superfamily.Adeninosine nucleotide alpha hydrolases superfamily includes N type ATP PPases and ATP sulphurylases. It forms a apha/beta/apha fold which binds to Adenosine group. This domain has a strongly conserved motif SGGXD at the N terminus.	5.77841e-71
NZ_CP046316.1|WP_009390895.1|139651_140029_-|glyoxalase	gnl|CDD|319947	cd08359, VOC_like, uncharacterized subfamily of vicinal oxygen chelate (VOC) family. The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.	3.0818e-28
NZ_CP046316.1|WP_009390859.1|121958_122813_-|aminotransferase-class-IV	gnl|CDD|238254	cd00449, PLPDE_IV, PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, one of five classes of PLPDE, consists of branched-chain amino acid aminotransferases (BCAT), D-amino acid transferases (DAAT), and 4-amino-4-deoxychorismate lyases (ADCL). BCAT catalyzes the reversible transamination reaction between the L-branched-chain amino and alpha-keto acids. DAAT catalyzes the synthesis of D-glutamic acid and D-alanine, and ADCL converts 4-amino-4-deoxychorismate to p-aminobenzoate and pyruvate. Except for a few enzymes, i. e., Escherichia coli and Salmonella BCATs, which are homohexamers arranged as a double trimer, the class IV PLPDEs are homodimers. Homodimer formation is required for catalytic activity.	9.20267e-43
NZ_CP046316.1|WP_009390875.1|126217_127546_+|hypothetical-protein	gnl|CDD|372583	pfam13372, Alginate_exp, Alginate export. This domain forms an 18-stranded beta-barrel pore which is likely to act as an alginate export channel.	9.78354e-14
NZ_CP046316.1|WP_009390877.1|127621_128776_+|serine-hydrolase	gnl|CDD|224594	COG1680, AmpC, Beta-lactamase class C and other penicillin binding proteins [Defense mechanisms].	2.31806e-34
NZ_CP046316.1|WP_009390883.1|133724_134615_-|fructose-bisphosphate-aldolase	gnl|CDD|180045	PRK05377, PRK05377, fructose-1,6-bisphosphate aldolase; Reviewed.	0
NZ_CP046316.1|WP_009390880.1|130185_130857_-|16S-rRNA-(cytidine(1402)-2'-O)-methyltransferase	gnl|CDD|381175	cd11648, RsmI, Ribosomal RNA small subunit methyltransferase I (RsmI), also known as rRNA (cytidine-2'-O-)-methyltransferase. RsmI is an S-AdoMet (S-adenosyl-L-methionine or SAM)-dependent methyltransferase responsible for the 2'-O-methylation of cytidine 1402 (C1402) at the P site of bacterial 16S rRNA. Another S-AdoMet-dependent methyltransferase, RsmH (not included in this family), is responsible for N4-methylation at C1402. These methylation reactions may occur at a late step during 30S assembly in the cell. The dimethyl modification is believed to be conserved in bacteria, may play a role in fine-tuning the shape and functions of the P-site to increase the translation fidelity, and has been shown for Staphylococcus aureus, to contribute to virulence in host animals by conferring resistance to oxidative stress.	1.85597e-120

Protein sequences

>NZ_CP046316.1|WP_009390880.1|130185_130857_-|16S-rRNA-(cytidine(1402)-2'-O)-methyltransferase
MSKLYLIPTPIGNLEDITLRALRLLKEVEVILAEDTRTSSKLLKHYDIHTPMQSYHLFNEHKVVDTWVQRIKGGTTVGLITDAGTPAISDPGFLLARACIAEGIAVECLPGATAFVPALVSSGLPNARFTFEGFLPDKKGRQTRLQLLAQETKTMIFYVSPHKLLKTLTDFITTFGADRQASISRELTKVHEETQRGTLQELLEYYKDKNIKGEIVFVLSGNR
>NZ_CP046316.1|WP_009390879.1|129536_130172_-|tRNA-(adenosine(37)-N6)-threonylcarbamoyltransferase-complex-dimerization-subunit-type-1-TsaB
MKLLHIETSGVNCSVALTDNDTILATKAQNAGHFTHSENLHLFIETVMTTAGVPLSSLDAIAVSAGAGSYTGLRIGVATAKGLCFALGKPLIGIPTLQILAHQVAADCIIPMLDARRMEVYSAVFDSEYRFVSPTEAKILDADSYKEYLDKGKVTFLGDGSTKFATICQHPNATFIAGAFPEAKDMIPFAIEKYKAANFEDIAYFEPTYLK
>NZ_CP046316.1|WP_009390878.1|128800_129520_+|3'-5'-exonuclease
MLHKINLEDILFLDIETVPQYPDYSCVPAAAQALWEEKTQYLRKDEHTAEEYYNRAGIWAEFGKIVCISVGYFSFRHEQRTFRVTSFTGEEDSLLRDFVRLVEEHFSRPNKLFCAHNGKEFDFPYLSRRMIINGIRIPNKLQLFGKKPWEVPHLDTLDLWKFGDYKHYTSLTLLAHTLGIPSPKDDINGSQVRDVFYEENDIHRIATYCEKDTITVAQILLHLRYEPLLTDDEILIIPR
>NZ_CP046316.1|WP_009390877.1|127621_128776_+|serine-hydrolase
MKKFTISLFLLLLIVVGGVYLLGYGYLFKAVRVVYATGHSTTFLDDYTYFDNRTISRSTTPQAWALAAEYNQVAETPELQNAHHKYGTVAFLIIKGDSIWHERYFDNYNSKSKSNSFSMAKSYVSALLGRAITDGYIKSLDQPVSDFFPQYKEGLAAKLTVGDLSSMASGLDWDEAYYDPFSITTRAYFDEHFREKMLQLKITSEPGKAFKYLSGNTFLLGMVIEKATGKTLSEYLAEALWQPMGCEGEALWQLDSEESGLEKAYCCIASNARDFARLGKLYRDHGKWDGKQLLDSAFVAKSVQPRFADHPEYGYGWWLLDYKGIHFFMMRGHLGQYVIVNPTDKVIIVRLGHSLSDEAPEGSTFPSDIYTYIDETYKMINGNS
>NZ_CP046316.1|WP_009390875.1|126217_127546_+|hypothetical-protein
MNKKLMTLGVLATLLAAPNYLAAQEADEMAPKNSIDITAQIRPRFEYRNGAYLPLQDGDAPAILVNNRTRLNFEYNNADRLKVYVSLQNVNIWGQAPQIQATDKTGGMSVFEAYAAFPLAEQVNIKLGRQVIALDDDRIFGSLDWHPAGRSHDAVNINWAPNEDFTLRGFIAYNQSAASPLNVNFPKGQYFSGGQPYQHLEALHAHYHIAPTQQLSFLFANLGYKTDAAKANNMQTFGAHYAGKSDEVTYGATAYLQTGKNAAGVSKSAYMFALNAGYRFSPIFALTAGLDYLSGNATDDTSGKDKAFDPFSGTNHKFYGLMDYYFVGAPGSNNAPAQGLLNPYLTANVRTGEKSNLSATYHFFGPAAKYQVGTKKHSSYGSEIDLVYSLKVQPFVGLQLGYSTYLVNDGTKALKGTPNPRAYQDWLWCSLNINPKIFSAKF
>NZ_CP046316.1|WP_009390874.1|124152_126177_+|tetratricopeptide-repeat-protein
MKKYHTKTFLFALLLILLISAGAVVFFFTHKEDYTSVEAVDTVGHNSYVGAASCRECHSAEHQQWQLSDHFKAMQIANDSTVLGDFNTSYTADGITSRFFKRDGKFFINTQNEKGDYQDYEVLYTFGYYPLQQYITDFPNGKKQVFRQSWDSRKKQWFHQYAGEVIPPDDYLHWTQAGQNWNLMCASCHSTNLQKNLDPYTDSYHTTYSELTVGCESCHGAAGAHVQSKGKAPLVPMQQQGQELTACMPCHTRRGEVSQHHGFSAEVMDNYIPEVPVTDLYFADGQVMGENYKYSSFLQSKMYQQGVRCTSCHSPHTGKLKAEGSKVCLQCHAPNYATTAHTFHKGNDAETDCRVCHMPTRTYMGNDVRHDHNFYVPRPDLSAKYGTPNACNACHSDKSAQWAAKAVVQWYGKERKPHFAENLIIGSKQTAESLPRLQSLLQTPNTPDIIRAAALHYLGGQPSEARFPLIVKELTAADAQTRYRAVIALSEYPLSRYEAQLLPLLTDKVKAVRMVVANVILTQKGWDNARAMSPHFEKAHQEYRDFVLSQADFPLGSATAGDYFVKINQPVEAIRFYERALQKDKNLNYLRLNLATLYNGEGQNDKAAAVLHTALQYEPKNAEIYYFLALLYSEEKRYTEAKNAFEKAMQLGMKDENIQRNYRNLLQLLVGIKK
>NZ_CP046316.1|WP_009390872.1|123305_123902_-|AhpC/TSA-family-protein
MKIFKTLLFAVLLAVAPIYGQDTSKALKVGDKAPQFTLKNALGKKVKLSTLLKNGNVVLTWYRGGWCPYCNRALQGWQEVLPEIKAQGATFVALTPELPDYSLSTKEKHQLAFEILTDLNNEVASRYGLVFTLDENTAVRYEKGFGLSAYNGNHLNQLPMPATYIINQKGVIVYAFVNADYTQRANTEEVIKKLKEIK
>NZ_CP046316.1|WP_034539967.1|122852_123236_-|SRPBCC-superfamily-protein
MNTKEKYQLEVGINASPQLLYQYISTPAGLASWYADDVRADADVYLFFWNKSPEKAILMRTKLDEYIRFHWVDDDPANTFFEIRINVDELTQEVSLVIVDFAYPDEIEEAKQMWRLQIADLKARIGG
>NZ_CP046316.1|WP_009390859.1|121958_122813_-|aminotransferase-class-IV
MNINYNGVLIGAEGNILALHNRAFAYGDAVTDVSKYSYQQLLFWEEHYLRLMAGMRVLRMNIPMSFSMEYIEEEILKTIRSNALESQPVRVRISIFRKSGNTYTPTNNDIEYLIETQPLSSAFYVLNEEPYEVELFKDFYIQPDLLANIKHTNRIVNVLGSIFAQENDYQNCILLNSQKNIAGALDGNIFLVNGNTLKTPALTDGAVNGITRKMLIKSLQKVGDYQVEETSISPFELQKADELFITNSLIGIQPVSQYRKKTYTHTATKSLIGKLNTIARFGIV
>NZ_CP046316.1|WP_009390857.1|120641_121946_-|tRNA-lysidine(34)-synthetase-TilS
MKTNLLEALKHQRVLVAISGGIDSVVLAHLLYSHGAEVILAHCNFSLRGEESDGDEAFVRSFAERLGVQLLVERFDTHAYAKEHQLNTQLAARELRYEWFDRMAQAYACAYIATAHHANDNLETFLINLSRGSGLDGLLGIPQQNGKLIRPLLSFSRQQIYQYAQAKQLSWREDSSNASNKYVRNVIRHEIIPQLRYVHPNYLENFNQTQEYLHQSARFIDYYIEKIRNECFQGDPIRISPSPLLQVPELPLVLHRLFYPYGFNNVKDLQQLLFTAEAGKMLCSPSHQLIKDKEWVWLLPIEDEEEAPFLIAEGTREVTTPIRLVFEEVPPTAAISEDPNTISVDADKLEFPLALRHKREGDIFYPIGLGSAKKLSKYFIDEKYSQIARQQQWLLCSGDRIVWVVGKRLDHRFRVTPKTKRVLQISVVGNSQIC
>NZ_CP046316.1|WP_009390882.1|132596_133631_-|virulence-RhuM-family-protein
MEAQKGEIILYQREDGSVQIDVKIENETVWLTQEQMATLFGKGRSTITEHISHIFEEGELDEKVVCRSFRQTYKHGAIESKTQEREVKHYNLDVVISVGYRVRSVQGTRFRQWATERLKEYVIKGFTMDDERLKGNAGGNYWKELLNRIRDIRSSEKALYRQVLDLYATSLDYDPKSETTIAFFKVVQNKLHYASSEQTSAELIYHKADSSKDFMGLTTFKGALPTLNEAKIAKNYLTEEELFRLNRLVSAFFDLAELKAEMQTPMYMKDWIEELDKFSANYGKGVLKGAGNISHEQAIQKATQEYRTYEAKTLSPVEQSYLESLKVLEKSTAKLLKHKKKREL
>NZ_CP046316.1|WP_009390883.1|133724_134615_-|fructose-bisphosphate-aldolase
MKKEQLEQMKNGKGFIAALDQSGGSTPKALKLYGIDESQYTNDAEMFALIHQMRTRIIKSPAFNSEKILGAILFEQTMDNLIDGKYTADYLWEEKHIIPFLKVDKGLLDIDSDGVQLMKPIDGLPDLLKRANERHIFGTKMRSVIKEASPRGIAQVVAQQFEVAQVIIDAGLVPIIEPEVDITIPDKSRAEAILRDEIRKHLDRLRDTSDVMLKLSLPTIDNFYKEFTKHPRVVRVVALSGGYPREKANEILAKNKGVIASFSRALTQGLSAQQTDTEFNQMLAETIEGIYEASVK
>NZ_CP046316.1|WP_009390884.1|134659_136720_-|sialate-O-acetylesterase
MKKILLTMLLLLSLGAGAQKKLTKVACVGNSITYGYLLENRTQDAYPSVLQRALGKAYLVGNFGKSGATLLNKGHRPYTQQDEYKQALAFAADIVVIHLGINDTDPRNWPNYRDNFVSDYLQLIASFKEVNPQARILLAQMSPISHRHPRFESGTRDWHAEIQEAITMVAREAQAQLIDFHAPLYPYPQLLPDGLHPNAEGAARLAKVVYSAITGDYGGLQLPAIYTDNMVLQHGQPLPIKGTANTGTKVMVSIGKQKYSAVADENGNWQVVLDPLKAKEVYTLSIVAGKQKRILKNVVAGEVWLCSGQSNMEFMLKQIITGATDIPRATNPNIRFYDMKARWRTDAVEWNATVLDSLNHLQYYRDTQWQECTPKTAAEFSAVGYYFGRWLQKDLDMPIGLICNAVGGSPTEAWVGRNTLENNFPRILYDWRNNDFIMQWVRERASQNIKKSTDKLQRHPYEPAYLYEAAILPLKDFPIKGVIWYQGESNAHNKDAHSKLFKLLVKSWRETFQNPKLPFYYVQLSSINRPSWGWFRDSQRRLLSEVPYSGMAVSYDYGHRTDVHPKNKQPIGERLARWALNRTYDKQHITPSGPLLRSVHFAEGAAFVSFNYAKGLHTSDNKPIRGFELSDGNGIFYPATAEIVGDEVKVSCEQVRIPKSVRYAWSPVTDANLVNEEELPTSTFVF
>NZ_CP046316.1|WP_009390885.1|136741_137197_-|hypothetical-protein
MYTHHILLILHLVAATIWVGGHLVLAIGYLPKALKHNDFSYIGNFEKTYEPIGMPSLLVLVITGILMAYDYGVSFSTWLHFDFSIEKVVSLKLLCLLTSVCFAISAQTRVLPQLRKGNIKKLPEMAVHIICVTLLGVTMVVLGSLVRIGGL
>NZ_CP046316.1|WP_009390887.1|137196_137763_-|aminoacyl-tRNA-hydrolase
MKKYLIACLGNIGAEYANTRHNIGFLVADKLAKDHNASFTTQKLGDLAEIKVKGRTFILLKPSTYMNLSGKAVRYWLEKERLTAENLLVVCDDLNIKFGTLRIKGKGSDGGHNGLKDIQYQLGTQEYARLRFGISSNFESGKQIDYVLGEWAPEEQTLLPERVAKCAEAVLSYGLAGLAITMNTFNNK
>NZ_CP046316.1|WP_009390889.1|137812_139117_-|30S-ribosomal-protein-S12-methylthiotransferase-RimO
MRTRSIKKNTINVVTLGCSKNVYDSEVLMGQLKAGGKNVVHEQEGNIVVINTCGFINNAKEESINTILDYVQQKEAGLIDKVFVMGCLSERYKPDLEKEIPDVDQYFGTSELPALLKVLGADYKHELIGERLTTTPKNYAYLKISEGCDRPCSFCAIPLMRGAHISTPIEALVTEAEKLAAKGVKELILIAQDITYYGLDLYKKRALADLLRALVKVEGIEWIRIHYAFPTGFPMDVIEVMKEEPKICNYLDIPLQHISDPILASMKRGTTQEKTTKLLKKFREAMPEMAIRTTLIVGYPGETQADFEALKFFVKEMRFDRLGCFTYSHEENTTAYDLEDDVPEEVKLARANEIMEIQSQISWELNQQKVGKTFRCLIDRKEGNYFVGRTEYDSPDVDNEVLIDAKKHYVKTGDFVEVKIIDATDYDLYGEPVV
>NZ_CP046316.1|WP_009390893.1|139260_139605_+|hypothetical-protein
MKKRFLIAAFFALFLGGIAVAQSQEQASTLTELQAEKEKLEAKLAKVLEEKENAENSLIGKYKDVAFAFNNHISKKQKKFAKIVLRGAKRKEKRIKKELKRLNKRIEKISKLEN
>NZ_CP046316.1|WP_009390895.1|139651_140029_-|glyoxalase
MKLNAGIITEKLAESKAFYTQVLQFGITFENDFYLLLHTPNHEAEISFLLPNHPSQQPLFQKPFTQQGVYLTIEVENVDEYYHSLKEQGVPIAIELREEPWGDRHFAIIDPNGIGIDIVTYSAPE
>NZ_CP046316.1|WP_009390897.1|140109_140715_-|NADAR-family-protein
MNTNERTYKKEEVITFRSTKESFGALSNMASGFSILVNNVIIPSSEALYQACRYPLFPAIQEEIINQNSPMTAKMISKKHYKYTRQDWEQKKYDIMYWVLKIKLLHNYHRLSELLRKTEEKPIVELSNKDRDWGAKEENGFLVGKNALGRLLMQLRKEFILEEQTLDKVYPPKVSGFLLYNTEISIIYKTDLEMLFDIDLD
>NZ_CP046316.1|WP_009390899.1|140711_141767_-|hypothetical-protein
MQELAEKIFEILKDYHCDYPDTKHKMSVEHILKWAEQFGGDGEFILTELLHFLPNIYVSKEKAISILKEHLESFRIRYKYSSMNDFIKNAYFIDLQKEEKSQREILVLVKEILQKEYGIDYNFLIQISSKKHYIYFDDILATGGTISRDLKSIIEKERDSFINKQKTIALSLFCYHTLGYGNILWGLGKDIGVPLKDILDIEANYIIENKLKPEWIAQKQKINCTYPIDKQSSKISEYIGKLNVNNPYSPPTFRPEQLPLEETFFSSKENRNKFEKIILDKGLELLQKVKKENPDPRKRPLGDTVKSHKTLGTGTLFFTWRNISNTCPIVFWWDVFGHNWTPLFSLKNRGI

Crispr_ID: NZ_CP046316_2

• CRISPR_ID: NZ_CP046316_2
• CRISPR_location: 327184-327267
• CRISPR_type: TypeII
• Repeat_type: NA
• Spacer_info: 1 spacers
• Cas_protein_info: cas9,cas2

Consensus repeat of NZ_CP046316_2

Consensus_repeat	Method
TTGCCCGTCACATCTCCCCCTTTGAAGG	CRISPRCasFinder

spacers of NZ_CP046316_2

>2.1|327212|28|NZ_CP046316|CRISPRCasFinder
GGGCTGGGGGGGATGTTAATACCCCCGT

CRISPR arrays and Neighbor proteins around NZ_CP046316_2

CRISPR arrays

The CRISPR arrays of NZ_CP046316_2

>merge|NZ_CP046316|2|327184-327267|CRISPRCasFinder
TTGCCCGTCACATCTCCCCCTTTGAAGGGGGCTGGGGGGGATGTTAATACCCCCGTTTGCCCGTCACATCTCCCCCTTTGAAGG

>NZ_CP046316|2|2|327184-327267|CRISPRCasFinder
TTGCCCGTCACATCTCCCCCTTTGAAGG	GGGCTGGGGGGGATGTTAATACCCCCGT
TTGCCCGTCACATCTCCCCCTTTGAAGG

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP046316.1|WP_009392478.1|328031_329222_+|6-bladed-beta-propeller	unknown	unknown	gnl|CDD|375027
NZ_CP046316.1|WP_009392525.1|342263_342515_+|GlsB/YeaQ/YmgE-family-stress-response-membrane-protein	unknown	unknown	gnl|CDD|225170
NZ_CP046316.1|WP_009392516.1|335889_340197_+|type-II-CRISPR-RNA-guided-endonuclease-Cas9	cas9	cd09643_cas9_CAS-II-A:CAS-II-B:CAS-II-C	gnl|CDD|375967
NZ_CP046316.1|WP_009392515.1|335255_335708_+|D-tyrosyl-tRNA(Tyr)-deacylase	unknown	unknown	gnl|CDD|376833
NZ_CP046316.1|WP_009392526.1|342589_342970_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP046316.1|WP_009392528.1|343320_343701_-|phage-holin-family-protein	unknown	unknown	gnl|CDD|377816
NZ_CP046316.1|WP_009392464.1|314207_315281_+|hypothetical-protein	unknown	unknown	unknown
NZ_CP046316.1|WP_009392529.1|343705_344032_-|YtxH-domain-containing-protein	unknown	unknown	gnl|CDD|378938
NZ_CP046316.1|WP_009392472.1|320716_321859_+|lactonase-family-protein	unknown	unknown	gnl|CDD|378416
NZ_CP046316.1|WP_009392517.1|340314_340656_+|CRISPR-associated-endonuclease-Cas2	cas2	COG3512_cas2_CAS-II-A:CAS-II-B:CAS-II-C	gnl|CDD|226043
NZ_CP046316.1|WP_009392470.1|319328_320711_+|aromatic-amino-acid-lyase	unknown	unknown	gnl|CDD|376303
NZ_CP046316.1|WP_009392465.1|315536_316337_+|hypothetical-protein	unknown	unknown	unknown
NZ_CP046316.1|WP_009392527.1|343085_343331_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP046316.1|WP_009392473.1|321903_323571_+|formate--tetrahydrofolate-ligase	unknown	unknown	gnl|CDD|376511
NZ_CP046316.1|WP_034540508.1|327373_327976_+|CDP-alcohol-phosphatidyltransferase	unknown	unknown	gnl|CDD|223632
NZ_CP046316.1|WP_009392476.1|326255_326984_+|RNA-methyltransferase	unknown	unknown	gnl|CDD|349982
NZ_CP046316.1|WP_034540502.1|316341_317574_+|leucine-rich-repeat-domain-containing-protein	unknown	unknown	gnl|CDD|372554
NZ_CP046316.1|WP_009392460.1|312277_313504_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP046316.1|WP_009392468.1|317707_319312_+|apolipoprotein-N-acyltransferase	unknown	unknown	gnl|CDD|143595
NZ_CP046316.1|WP_034540504.1|323641_326215_-|BamA/TamA-family-outer-membrane-protein	unknown	unknown	gnl|CDD|366466

HMMScan for Signature genes

Protein	Cas_name	Cas_description	E-value	Identity	Coverage
NZ_CP046316.1|WP_009392516.1|335889_340197_+|type-II-CRISPR-RNA-guided-endonuclease-Cas9	cas9	cd09643_cas9_CAS-II-A:CAS-II-B:CAS-II-C	9.5e-63	207.5	57.7
NZ_CP046316.1|WP_009392517.1|340314_340656_+|CRISPR-associated-endonuclease-Cas2	cas2	COG3512_cas2_CAS-II-A:CAS-II-B:CAS-II-C	8.2e-29	94.9	0.2

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
NZ_CP046316.1|WP_009392478.1|328031_329222_+|6-bladed-beta-propeller	gnl|CDD|375027	pfam17170, DUF5128, 6-bladed beta-propeller. This family is a 6-bladed beta-propeller structure of unknown function. There is a highly conserved FDxxG motif which might be important.	1.03638e-10
NZ_CP046316.1|WP_009392525.1|342263_342515_+|GlsB/YeaQ/YmgE-family-stress-response-membrane-protein	gnl|CDD|225170	COG2261, COG2261, Predicted membrane protein [Function unknown].	2.07502e-05
NZ_CP046316.1|WP_009392516.1|335889_340197_+|type-II-CRISPR-RNA-guided-endonuclease-Cas9	gnl|CDD|375967	pfam18541, RuvC_III, RuvC endonuclease subdomain 3. Cas9 proteins are abundant across the bacterial kingdom, but vary widely in both sequence and size. All known Cas9 enzymes contain an HNH domain that cleaves the DNA strand complementary to the guide RNA sequence (target strand), and a RuvC nuclease domain required for cleaving the noncomplementary strand (non-target strand), yielding double-strand DNA breaks (DSBs). The crystal structures of type II-A and II-C Cas9 proteins highlight the features in Cas9 enzymes that support their function as RNA-guided endonucleases. Cas9 enzymes adopt a bilobed architecture composed of a nuclease lobe containing juxtaposed RuvC and HNH nuclease domains and a variable alpha-helical lobe likely to be involved in nucleic acid binding. The RuvC domain forms the structural core of the nuclease lobe, a six-stranded beta sheet surrounded by four alpha helices, with all three conserved subdomains (I, II, III) contributing catalytic residues to the active site.	3.40614e-58
NZ_CP046316.1|WP_009392515.1|335255_335708_+|D-tyrosyl-tRNA(Tyr)-deacylase	gnl|CDD|376833	pfam02580, Tyr_Deacylase, D-Tyr-tRNA(Tyr) deacylase. This family comprises of several D-Tyr-tRNA(Tyr) deacylase proteins. Cell growth inhibition by several d-amino acids can be explained by an in vivo production of d-aminoacyl-tRNA molecules. Escherichia coli and yeast cells express an enzyme, d-Tyr-tRNA(Tyr) deacylase, capable of recycling such d-aminoacyl-tRNA molecules into free tRNA and d-amino acid. Accordingly, upon inactivation of the genes of the above deacylases, the toxicity of d-amino acids increases. Orthologues of the deacylase are found in many cells.	9.06637e-86
NZ_CP046316.1|WP_009392528.1|343320_343701_-|phage-holin-family-protein	gnl|CDD|377816	pfam07332, Phage_holin_3_6, Putative Actinobacterial Holin-X, holin superfamily III. Phage_holin_3_6 is a family of small hydrophobic proteins with two or three transmembrane domains of the Hol-X family. Holin proteins are produced by double-stranded DNA bacteriophages that use an endolysin-holin strategy to achieve lysis of their hosts. The endolysins are peptidoglycan-degrading enzymes that are usually accumulated in the cytosol until access to the cell wall substrate is provided by the holin membrane lesion.	0.00728175
NZ_CP046316.1|WP_009392472.1|320716_321859_+|lactonase-family-protein	gnl|CDD|378416	pfam10282, Lactonase, Lactonase, 7-bladed beta-propeller. This entry contains bacterial 6-phosphogluconolactonases (6PGL)YbhE-type (EC:3.1.1.31) which hydrolyze 6-phosphogluconolactone to 6-phosphogluconate. The entry also contains the fungal muconate lactonising enzyme carboxy-cis,cis-muconate cyclase (EC:5.5.1.5) and muconate cycloisomerase (EC:5.5.1.1), which convert cis,cis-muconates to muconolactones and vice versa as part of the microbial beta-ketoadipate pathway. Structures of proteins in this family have revealed a 7-bladed beta-propeller fold.	5.40541e-113
NZ_CP046316.1|WP_009392517.1|340314_340656_+|CRISPR-associated-endonuclease-Cas2	gnl|CDD|226043	COG3512, COG3512, CRISPR-associated protein, Cas2 homolog [Defense mechanisms].	9.60297e-25
NZ_CP046316.1|WP_009392470.1|319328_320711_+|aromatic-amino-acid-lyase	gnl|CDD|376303	pfam00221, Lyase_aromatic, Aromatic amino acid lyase. This family includes proteins with phenylalanine ammonia-lyase, EC:4.3.1.24, histidine ammonia-lyase, EC:4.3.1.3, and tyrosine aminomutase, EC:5.4.3.6, activities.	7.64565e-119
NZ_CP046316.1|WP_009392473.1|321903_323571_+|formate--tetrahydrofolate-ligase	gnl|CDD|376511	pfam01268, FTHFS, Formate--tetrahydrofolate ligase.	0
NZ_CP046316.1|WP_034540508.1|327373_327976_+|CDP-alcohol-phosphatidyltransferase	gnl|CDD|223632	COG0558, PgsA, Phosphatidylglycerophosphate synthase [Lipid metabolism].	0.000879264
NZ_CP046316.1|WP_009392476.1|326255_326984_+|RNA-methyltransferase	gnl|CDD|349982	cd18109, SpoU-like_RNA-MTase, SAM-dependent RNA methylase related to SpoU-TrmH. RNA 2'-O ribose methyltransferase catalyzes the methyltransfer from S-adenosyl-L-methionine (AdoMet) to the 2'-OH group of ribose in tRNA or rRNA. It is part of the SpoU family of MTases, a subfamily of the SPOUT methyltransferase superfamily. The SPOUT methyltransferase superfamily is a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot.	1.0382e-74
NZ_CP046316.1|WP_034540502.1|316341_317574_+|leucine-rich-repeat-domain-containing-protein	gnl|CDD|372554	pfam13306, LRR_5, Leucine rich repeats (6 copies). This family includes a number of leucine rich repeats. This family contains a large number of BSPA-like surface antigens from Trichomonas vaginalis.	2.3906e-31
NZ_CP046316.1|WP_009392529.1|343705_344032_-|YtxH-domain-containing-protein	gnl|CDD|378938	pfam12732, YtxH, YtxH-like protein. This family of proteins is found in bacteria. Proteins in this family are typically between 100 and 143 amino acids in length. The N-terminal region is the most conserved. Proteins is this family are functionally uncharacterized.	1.07736e-12
NZ_CP046316.1|WP_009392468.1|317707_319312_+|apolipoprotein-N-acyltransferase	gnl|CDD|143595	cd07571, ALP_N-acyl_transferase, Apolipoprotein N-acyl transferase (class 9 nitrilases). ALP N-acyl transferase (Lnt), is an essential membrane-bound enzyme in gram-negative bacteria, which catalyzes the N-acylation of apolipoproteins, the final step in lipoprotein maturation. This is a reverse amidase (i.e. condensation) reaction. This subgroup belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 9.	9.79035e-70
NZ_CP046316.1|WP_034540504.1|323641_326215_-|BamA/TamA-family-outer-membrane-protein	gnl|CDD|366466	pfam01103, Bac_surface_Ag, Surface antigen. This entry includes the following surface antigens; D15 antigen from H.influenzae, OMA87 from P.multocida, OMP85 from N.meningitidis and N.gonorrhoeae. The family also includes a number of eukaryotic proteins that are members of the UPF0140 family. There also appears to be a relationship to pfam03865 (personal obs: C Yeats). In eukaryotes, it appears that these proteins are not surface antigens; S. cerevisiae YNL026W (SAM50) is an essential component of the Sorting and Assembly Machinery (SAM) of the mitochondrial outer membrane. The protein was localized to the mitochondria.	5.02861e-19

Protein sequences

>NZ_CP046316.1|WP_009392476.1|326255_326984_+|RNA-methyltransferase
MLSKNQVKLIQKLHHKKYRNELNLFIVEGKKSINEFLQAGYTPQLLIATEAFTTSVPQHLITPVSKDELRKVSTLQNPDEGLAVFQQPKHKGILQEGVIVALDNVQDPGNLGTIIRLCDWFGVETLLCNTQTVDCYNPKVVQATMGSLTRVAVHYLDLAAFLTTTALPVYTMDLEGENLYTATFPKDCILILGNEANGISSEVRALSNEVITIPRFSQHQRTESLNVAMAGAIILSEVMGHH
>NZ_CP046316.1|WP_034540504.1|323641_326215_-|BamA/TamA-family-outer-membrane-protein
MKKAFFRYSFISGLCVLLCYLSACEATKRVAADDYLLRENKVYVNDALTDDAKVNNFIFQKPNSYILGLPVSLYIYNWANPHSEEEFVQWLDNHPRWHRFLNGFLSKKQVGRLQESFLVSGIDHQLQKIGEAPVILDTAQVRRSTKQLAAYYRSIGYFNAKVGDSIRKLTKTEKRTAIVDYYIQTGDRYYIDSLKTAITSPEIDSVYRLHLDKTLLKQGAPYQLADFAGERTRLYTLFRNKGFYTFQQSSINFEIVRDTVHKQKDRNLQVSTNIGDLIERDGDVVTTKKYKVHHINKIRMYTDYDSQTDKSALDSITYRDLIIYYKDKLHYRPRVLWRASGLRQGQLYSDTDRGNTYKQLNNLRVFRYPNMEFKYPAKDTLMNKLDANIYLSPLDKFSLRLTNEIKRSEIEAIGFGVGTAFSARNVFRGAETLELNLQGTFASQPSLNDSHFFNTSEISGDVRFIFPTILFPLNTRKLIPYYMTPQTILQAGMSYQTNIGIDKRTTSGLLRYVWNPREQKNKVIFDLINVQYVNNINPRNFFSIYQSTYERLNDISRKYHLGTAYVDSRGNLTPREGTFRFLGDIFNRTIPVQAEDVVPLLGILERYNRITNNDFIVSSSYTYIFNSKSQFFERDFSQFRIKVEAAGGLLNTLASTYNVVKTDNNKNKIFGVEYAQFAKGELDFIKHFPIGKQNSLAFRSFFGIAVPYGNSDNIPFSQSYFAGGTTDNRGFKAYRLGPGASQSVFDYNEANMKLTLNLEYRFQMLGAFKGALFTDVGNIWNVADNTPIADNKFVNFSSLKDVGVSTGFGLRYDFNFFVIRLDMGVPTYDPAYEVGDRWIKKFKMKDVVFNFGINYPF
>NZ_CP046316.1|WP_009392473.1|321903_323571_+|formate--tetrahydrofolate-ligase
MTDLEIAQKAQMLPIREVAKKLNISEDNLDPYGKYKAKLPLHLINPEKMKNSKLVLVTAITPTPAGEGKTTVSIGLTEGLNKIGKKAIAVLREPSLGPVFGIKGGAAGGGYSQVVPMEDINLHFTGDFSAIEKANNLLSAVIDNNIQSKTHSIGIDPRTVVWKRVMDMNDRALRHIVVGLGGSTHGTPREDGFNITPASEIMAILCLSESFSDLKRRIGNIYVGKKFDGTPVFARDLNVVGAMALLLKEAIKPNLVQTLENNPAILHGGPFASIAQGTNTVLATKMGLSLGDYVVTEAGFGADLGAEKFLNIKCVSAGLAPDAVVVVATIRALRHHGGAKKEEYNTPDLQKVKLGIANLEKHIENVQHFGLKAVVAINYFPHDSEEEIAYVKEVCAKKGVEAVVSKGFSEGGKGTEELARAVVAIAESGESHFAPLYSHQASIEDKITTVATKIYGANKVNYSSKALSQLKQINKLGFDKLPVCIVKTPKSLSDDEKKLARPTDFEVTVREFEFASGAGFVIPILGDTVRMPGLPSVPAAEGMDIDDEGIISGLS
>NZ_CP046316.1|WP_009392472.1|320716_321859_+|lactonase-family-protein
MKKLQILLVLLGAIVSLHSFAQGGKVNNLTMYVGTYTEGGNSKGIYTYNFNQENGTFELLNTATAANPSFVTLSPEGKRLYAVSEYNDGRQGAYSFDLSENKAKLSNPVFRPTASKDALPRAGADPCHIVSDGNYVITANYTGGDTSVFSLDTEGRLQAEVQHIAFAGRTPERVAHIHCIIPTPDKKYILATDLGNDRVYRFRYNKKASKKAEVLTAQQVAYQVSDGQGPRHLTFSKDGHFAYLINELGGECVVLSYRKGKLKEVQRLIADEGGGCGSADIHISPDGRFLYTSHRLKKDGIAIFAINPKKGTLTKVGYQLTGVHPRNFAITPNGKYLLVACRDNNKIQVFQRNETTGELTETSQEIEVDKPTCILFAKSN
>NZ_CP046316.1|WP_009392470.1|319328_320711_+|aromatic-amino-acid-lyase
MVHYISNEVLLLEQLDTIINTDVKLKLSEEAVLNIEKCHTFFTEKVKDTSLSEATEQHYTQLRHYACGIGERLPCKLVRIMLFLKIQSFSYGFSGVRLALVQRLIDFFNNGVYPVVYSKDIPDERIALAHLSLPLIGEGEVCIQNKIYSAQELASKYGWEPLPLSQREVDALLNGTQLTTAYSAHNLIESLKLIEWADFVASVSTQVFGGNLSAFSELMQVVRPHKGLVETAQHLRTLLKDSTLVDSPEDFQSMPEAFCSIPQIHGAVREAIAAIRKVVKTEINSVTDNPILFPEQGEIIFGGNSHTLPLSLSMDFLSITLTSLGNISERRVFYLLSNVGKDIETEIDYPIFQRIIEGILNENRRLSTPSSIESPILFEKTIDIKGMGGSSAIKCSQIVKNVMQIIAIELILATSLWKKKPLRYHSSIFKDYLDFIAEEEATTLKKQIEHTIQFFNSTQN
>NZ_CP046316.1|WP_009392468.1|317707_319312_+|apolipoprotein-N-acyltransferase
MKKNILLALLSGGLLAGAWVTYGFTALIFIALVPLLLMESRVRTRYQHTKRKVFALSYLAFLVWNIPTTWWIWYSTQIGAVFAILANTLLMTITFLLYHLVAKRLSTKVSLVFLVCIWLSFEKFHLWWDVSWPWLNLGNVFSEQITWIQWYEYTGAFGGTLWVWLVNIALFIGVKDYLSDKNRPLLAKRVGGAMLLFAVPVLISYFQYQNYSEEGKKTIKAIALQPNIDPYQEKYDFSNAKVAQLLVQLAEVKMDKEVNFIVTPETVFADNVKLHELPYTQEVAILRTLVDRYPQLNWVGGTAMIEFITDKAHTTSQSNYLPQYNIWYNDYNTAFLLNSRPEVPLYHKSKLVVAVENFPYQQVLKPILGETLINLGGTVALKTTQPERTAFAGVGTEGKAAPIICYETIYGEFVTDYIKKGANFLAILTNDAWWRNTQGHKQLLSYTRLRAIETRRSVVRSANTGISAFINGRGEVLQTLPYGVQGSLKGTIALNEEVTFYVRMGDYIARIAYFLAFFIFLSAVVKRRGLLSKN
>NZ_CP046316.1|WP_034540502.1|316341_317574_+|leucine-rich-repeat-domain-containing-protein
MKNFIYIAMAIAAPIALVNCTKEKTIVEVQKGNTILSGTETPTATLGSVGDYYLRLPVYDFYGPKTAEGWGTPVSLKGAPAGQSGSKIHSGSGAPDADKGNEGDWYIDTVNKRLYGPKTATSWPTTYIGLGADDEDDEEPDQPITAADYELSPDGKTLIKWKNNKTKNLNMQADPVLKNVTAIGNYAFEDKKKLITVVLPDNLLTIGDRAFANDFFTVESTMYEIRINIPNKVTHIGKEAFKYRGLSSIIIPNNVVSIGEGAFSFNNSNSVVISNSITVIPKNAFQANVFTTVTIPNSVVTIEDEAFFVGKLTSISIPNSVQVIGKNAFGNNQLATLTIPATVKEVKENAFQNNRLTTITFEGTTPPLKSNKDNNTIFAENRIQHIYVPASSVAAYKALLPTYQSYITAK
>NZ_CP046316.1|WP_009392465.1|315536_316337_+|hypothetical-protein
MASLIANIKGAKNVPVIERLKNESPDFNCVSGGYTQVFNGVEEEMKKSLSNFIMDICDLLKKSIEIADQYNEPDIFETSPYTFTPPQTLIEYYVAKYLRGRLDKERWNLLFKKPINGVVHDIRLVEKELPQTGEKTPKRKQKLRTIIIDLFAELWLFPLSNSDFIQNRKAEFPAITLDELVAKIKAKMEASGVTPENYFVALIVLPATNGGEGIDLDELAKRLGIPRKKLFICSKVIDIVKLFEELIEMIWSLKVLFESEEENIKH
>NZ_CP046316.1|WP_009392464.1|314207_315281_+|hypothetical-protein
MKTIVLISCVSQKENTAVVAEGMYKSPLFRKSLAYAKKLVTDDAIYILSAKHHLLPLDKVIDPYNETLNRMRKEDRTAWGAKVIEQLREVADLQEDKFIILAGEKYIEPIKDCLTNIELPLKGMRIGQRLQYLTFENHNLNSMQKSLTLRLHELFNSLERFSYPFEAEKQQIPANGIYVMFEEGETFEGLDRIVRVGTHNGDNNLFKRLEEHYVNENKNRSIFLQRVGDALLNKENNPYFEVWNVNATAKEAQERVAGKVDSVLEAQITEEAVAHIREKITFVVFAVEEEKDRKKWEKKLIGTLSNAAKAGEIKVSDGWLGNFSTEPKVKESGLWQTQGLYSESLTEEEFAALQKIV
>NZ_CP046316.1|WP_009392460.1|312277_313504_-|hypothetical-protein
MNYQEHIIRLQTEVNRTFGRTVTSMFDFELLAEKIHLSTQTLRRFYGKIDKDKQLSAASLNLICQYIGFADWESFCVQPDTPKVNVHELINAFYDTVAYSGATFFDPKLRDTHEAYAELIIKDLPYAYTFLERYKAYPVITQSLYPWFPYYDQMAQRSYVQLIEAYLATEPLKHLRVCQNSFLAYGAFCAANGGRKQVLTEVEKYVKNADKHIDSIYRDYPDSFFHYPETRYTIAKVAQAYLQGNEQEATRVAEAALIRNSHTEPLYVFGEYFQTPDILVSKLCNALIWMGKIDFAIEIYSTYSEKLFSTEDPVEHQSKNFVYERDTNFAAQTVEMMHLFDERIPLLESKRQPHWKTQHYEEIQQWLIALKRTEKQKFSERRAIKEHLYSLGKKLNYGIVESLIERFS
>NZ_CP046316.1|WP_034540508.1|327373_327976_+|CDP-alcohol-phosphatidyltransferase
MPLPYILILFRFLLAPTIFWIAYATPESVARPAIVIAIVVGLLSDIFDGIIARHRGISTVKMRRLDSQTDLVFWLSVGVACYWLNPALITAYRYQIITLFVMEALCYGLSFLRFGKETCTHAFLSKIWGLTLLIAFVSLIGFGYGGFPLQLAIYWGLLSQTDVILIILLLPRWQNDIPSAYHAYLIRKGKTIKKNKWLNS
>NZ_CP046316.1|WP_009392478.1|328031_329222_+|6-bladed-beta-propeller
MKLPIILGLLTASITASFAQPFRDTTVLQLADTKVLTAETSQAQHLNLNPFLVKDKEFDFGALLKEINFVPLETTAQSRLGQIRKVVTTAEHIYIMDDLDESGIVIFTRQGKFVKRIPNGKKPEQLYRLYDIDFNTQTNELIAYKRSFLLIFDKEGNFLRFKYLPIGFLNMAATPDGYVLKSLVGQNKNLGDKSNYRLQFINKDLKLNAVALPDKESKAFSAKSYLYRVADLVKITAEISDTIYQYNPKDNKLAAEFILDYDHKLPRSYIYGKDFSVFENAIRDHNYNYCIGDYIETTHHNVFFISNKTANVVVYRDKHSGNMVGGGIAQSKQGLPFLAFPDSFYDDQLIKYYYPGENDYEVLKEMPFLSEANKKKSESFKKGDNPILIYYTLNKF
>NZ_CP046316.1|WP_009392515.1|335255_335708_+|D-tyrosyl-tRNA(Tyr)-deacylase
MRVVIQKVTQASVSIENQIVASIDKGLFVLVGIEDTDTNDDIAWLSAKIVNLRVFDDDNGVMNLSVKEVEGEVLIVSQFTLHASTKKGNRPSYIKAARPEVAIPIYEAFIKQVESLLGKRVPTGQFGVMMQVSLCNDGPVTILIDTKNKE
>NZ_CP046316.1|WP_009392516.1|335889_340197_+|type-II-CRISPR-RNA-guided-endonuclease-Cas9
MKNILGLDLGTTSIGFAHIVEDENKEKSEIKELGVRIVSLATDEQSDFEKGKSISTNANRTLKHGARLNLDRYQQRRKFLIDLLQKANLITSASILAENGKNTTHSTWQLRAKAVTERIEKEEFARVLLAINKKRGYKNSRKTKTEDEGQAIDGMAIAKCLYDENLTPGQLSLQLLQQNKKLLPDFYRSDLQKEFDLVWNLQKQFYPDILTDSFYKELQGKGKDATSKAFSKRYHFDTAENKGSKESVRLQAYQWRAEAISKQLSKEEVAYVLTEINNNLNNSSGYLGAISDRSKELYFNRQTVGQYLYAQLQENRHNSLKNKVFYRQDYLDEFERIWETQASFHKELTDELKKQIRDVVIFYQRKLKSQKGLVSFCEFESKEIEIEKDGKAITKSIGARVVPKSSPLFQEFKIWQILNNVTCKRKGIRKKKSSAKSTELDLFNEPSQSIFSLDMECKQLLFDELNLKGDLKSDKVLKLLGYSPQEWEINYNQLEGNRTQKSLYEAYLKIIEIEGYEVKDILQIKSTKDDWSLDESPLSASEIRERVKVIFQTLGICTKILYFDPLLPVKEFEQQYSYQLWHLLYSYESDDSTSGNETLYRILEKKYAFKREHATILANVALQDDYGSLSTKAIRKIYPYIKENQYSTACELAGYKHSKLSLTTEELEARELKNIIPLLKKNALRNPVVEKILNQMINVVNALIEKNSERDAEGKITKYFHFDEIRIELARELKKNAQERYEMTQNINKAKLEHQKISEKLQKQFGIKNPTKSDIIRYRLYQELEHNGYKELYTNTYIAPDVLFSKNIDIEHIVPKARVFDDSFSNKTLAFKEFNIKKGESTAFDYITSLNCEGELNQYLTRVENAYKTKSISLTKYKNLLKKASEIGDGFINRDLRDTQYIAKKAKEILFQVTKNVLSTSGSITDRLREDWGLVDVMKELNMPKYQSLGLTEVEERKDGNKVTVIKDWTKRNDHRHHAMDALTVAFTKPSYIQYLNHLNARKDENNKNYSVILAIEKKETIKVPINNGKNKRVFIEPILNFRQVAKKHLEEIFISHKAKNKVVTKNINKPAGTDKQQITLTPRGQLHKETIYGKYQYYVNKEEKVGVKFDERTITKVSNPLYREALLKRLQANDNDPKKAFAGKNALSKNPIYLDEAKTKTLPEKVNLTYLEEDFSIRKDISPDNFKDLKSIEKVIDQGVKRILIKRLQAYDNDPKKAFVDLEKNPIWLNKEKGIAIKRVTISGVSNAQPLHIGKDHLGKTTLNKEGKEVPVDYVSTGNNHHVAIYRDKEGNLQEQIVSFFEAVVRAQQGLPIIDKNYKQAEGWQFMFTMKQNEMFVFPNEATGFNPAEIDLLDPKNKKLISPNLFRVQTISIVKYGNSVVRDFKFRHHLETTLQDDKILQGITFQQIKSLEPLRNIVKVRINHLGDIVNIGEY
>NZ_CP046316.1|WP_009392517.1|340314_340656_+|CRISPR-associated-endonuclease-Cas2
MIIAERYNAYRIMWVLVLYDLPTETKKMRREAQVFRDKLIKDGFTLFQFSMYIRHCPSRENAQVHINRVKQNLPQYGNIAIMCLTDKQFGDMEFFYCQKETTAPETYVQLELF
>NZ_CP046316.1|WP_009392525.1|342263_342515_+|GlsB/YeaQ/YmgE-family-stress-response-membrane-protein
MGIIATLIIGAIAGWLGGTIYKGSGLGLIGNIIIGVLGSSVGYWLLGSVLHISLGEGLIGSILTGAIGAIVILFLINLIFKKK
>NZ_CP046316.1|WP_009392526.1|342589_342970_-|hypothetical-protein
MKKIIALASVICLSLVFFASCSKNDDPADNDLFVGTYKGEISFLKGKEKKSVDNGSVTVVKTGNDYYFRFSDGIEDLKGVSFKKEGDNTLVNVDLQDGLKVIRINASSLYILYTTDGKTWIANAKR
>NZ_CP046316.1|WP_009392527.1|343085_343331_-|hypothetical-protein
MNNKTYSSFEEIDNEIRLLRLEKEIDRLSLTQQVSASAESLSPKNLLANTLGSLFNNKRWLNIALGYGMQLLAKRYLNKNK
>NZ_CP046316.1|WP_009392528.1|343320_343701_-|phage-holin-family-protein
MAIYSIKETFVEVPTKANTAFNSQFAYYKMIVFRFIAKSSYGLITFFVYAFACLLILFFLSLAAAYAIGEALGSNGLGFAIVGAFYILLSLVVLLFRRKLIEKSLLQKLSEIYFKSDPEDEEENEQ
>NZ_CP046316.1|WP_009392529.1|343705_344032_-|YtxH-domain-containing-protein
MSKTANAVLGLAVGTAIGVGLGILFAPDEGKNTRKKIKDSLRDKSDEFKEQLDNLTESVREKSLELKGSLEEKVDRLFSKSSNKAEDVISLLEKKLASLKEEAAKIKK

Crispr_ID: NZ_CP046316_3

• CRISPR_ID: NZ_CP046316_3
• CRISPR_location: 340776-342183
• CRISPR_type: TypeII
• Repeat_type: NA
• Spacer_info: 18 spacers
• Cas_protein_info: cas2,cas9

Consensus repeat of NZ_CP046316_3

Consensus_repeat	Method
TGTTATCAATCACAAAACTACAAAATTTGAAAGCAATTCACAAC	PILER-CR
TGTTATCAATCACAAAACTACAAAATTTGAAAGCAATTCACAAC	CRISPRCasFinder
TGTTATCAATCACAAAACTACAAAATTTGAAAGCAATTCACAAC	CRT

spacers of NZ_CP046316_3

>3.1|340820|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT
AAAGACTTCCCTATTTTGAATAACCTGATAGT
>3.2|340896|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT
CAGTCCTTAATGTGTAGAGGGAACTGCCATGT
>3.3|340972|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT
GAGCTATGTAGCTATACACAATGAGGGAGGGA
>3.4|341048|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT
TGCCAGCCTTGTAGCATATAGATAGCGTTAGA
>3.5|341124|29|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT
AAACCGCTTACTCCAATAATCGCGTTTGT
>3.6|341197|31|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT
AGGCTTTTTTGAAGGGGTTTTTGCTTGAGGT
>3.7|341272|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT
CAACAAATGAATGAAACAGCAAAACAAAGTGT
>3.8|341348|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT
AACTACATCTTACAAGGCTTTGGATTTAGGGT
>3.9|341424|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT
AAAAGCTGGAACGCCCTTTTGACGAGTATAGT
>3.10|341500|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT
TACGTTAGGCATTATAACCTTTGCCGATGAGA
>3.11|341576|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT
CTCTCGCCCTCCCTCCCGTTGGTCGGTTGGGA
>3.12|341652|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT
AAAGCATTAAACAAACAACAAGAGATACAAGT
>3.13|341728|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT
GTTTTCTAACTTTATGAAACCCGGACAAGAGT
>3.14|341804|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT
CTGTCACCTATTTGGTATTGATTTGAAAAAGA
>3.15|341880|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT
TACCCAGTGGAGGACCCTCAAGCACACTTTGA
>3.16|341956|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT
CAACAAATGAATGAGATGAGCAAACAAAGTGA
>3.17|342032|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT
CAACAAATGAATGAGATGAGCAAACAAAGAGA
>3.18|342108|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT
TTTTAGCACAAACAAGAACGTACGAAAGTTGT

CRISPR arrays and Neighbor proteins around NZ_CP046316_3

CRISPR arrays

The CRISPR arrays of NZ_CP046316_3

>merge|NZ_CP046316|3|340776-342183|PILER-CR,CRISPRCasFinder,CRT
TGTTATCAATCACAAAACTACAAAATTTGAAAGCAATTCACAACAAAGACTTCCCTATTTTGAATAACCTGATAGTTGTTATCAATCACAAAACTACAAAATTTGAAAGCAATTCACAACCAGTCCTTAATGTGTAGAGGGAACTGCCATGTTGTTATCAATCACAAAACTACAAAATTTGAAAGCAATTCACAACGAGCTATGTAGCTATACACAATGAGGGAGGGATGTTATCAATCACAAAACTACAAAATTTGAAAGCAATTCACAACTGCCAGCCTTGTAGCATATAGATAGCGTTAGATGTTATCAATCATTAAACTACAAAATTTGAAAGCAATTCACAACAAACCGCTTACTCCAATAATCGCGTTTGTTGTTATCAATCACAAAATTACAAAATTTGAAAGCAATTCACAACAGGCTTTTTTGAAGGGGTTTTTGCTTGAGGTTGTTATCAATCGCAAAACTATAAAATTTGAAAGCAATTCACAACCAACAAATGAATGAAACAGCAAAACAAAGTGTTGTTATCAATCGCAAAACTACAAAATTTGAAAGCAATTCACAACAACTACATCTTACAAGGCTTTGGATTTAGGGTTGTTATCAATCACAAAACTACAAAATTTGAAAGCAATTCACAACAAAAGCTGGAACGCCCTTTTGACGAGTATAGTTATTATCAATCGCAAAACTACAAAATTTGAAAGCAATTCACAACTACGTTAGGCATTATAACCTTTGCCGATGAGATGTTATCAATCGCAAAACTACAAAATTTGAAAGCAATTCACAACCTCTCGCCCTCCCTCCCGTTGGTCGGTTGGGATGTTATCAATCACAAAATTACAAAATTTGAAAGCAATTCACAACAAAGCATTAAACAAACAACAAGAGATACAAGTTGTTATCAATCACAAGACTACAAAATTTGAAAGTAATTCACAACGTTTTCTAACTTTATGAAACCCGGACAAGAGTTGTTATCAATCGCAAAACCACAAAATCTGAAAGCAATTCACAACCTGTCACCTATTTGGTATTGATTTGAAAAAGATGTTATCAATCACAAAACTACAAAATTTGAAAGCAATTCACAACTACCCAGTGGAGGACCCTCAAGCACACTTTGATGTTATCAATCACAAAACTACAAAATTTGAAAGCAATTCACAACCAACAAATGAATGAGATGAGCAAACAAAGTGATGTTATCAATCACAAAACTACAAAATTTGAAAGCAATTCACAACCAACAAATGAATGAGATGAGCAAACAAAGAGATGTTATCAATCACAAAACTACAAAATTTGAAAGCAATTCACAACTTTTAGCACAAACAAGAACGTACGAAAGTTGTTGTTATCAATCACAAAACTACAAAATTTGAAAGCAATTCACAAC

>NZ_CP046316|3|1|340776-342183|PILER-CR
TGTTATCAATCACAAAACTACAAAATTTGAAAGCAATTCACAAC	AAAGACTTCCCTATTTTGAATAACCTGATAGT
TGTTATCAATCACAAAACTACAAAATTTGAAAGCAATTCACAAC	CAGTCCTTAATGTGTAGAGGGAACTGCCATGT
TGTTATCAATCACAAAACTACAAAATTTGAAAGCAATTCACAAC	GAGCTATGTAGCTATACACAATGAGGGAGGGA
TGTTATCAATCACAAAACTACAAAATTTGAAAGCAATTCACAAC	TGCCAGCCTTGTAGCATATAGATAGCGTTAGA
TGTTATCAATCATTAAACTACAAAATTTGAAAGCAATTCACAAC	AAACCGCTTACTCCAATAATCGCGTTTGT
TGTTATCAATCACAAAATTACAAAATTTGAAAGCAATTCACAAC	AGGCTTTTTTGAAGGGGTTTTTGCTTGAGGT
TGTTATCAATCGCAAAACTATAAAATTTGAAAGCAATTCACAAC	CAACAAATGAATGAAACAGCAAAACAAAGTGT
TGTTATCAATCGCAAAACTACAAAATTTGAAAGCAATTCACAAC	AACTACATCTTACAAGGCTTTGGATTTAGGGT
TGTTATCAATCACAAAACTACAAAATTTGAAAGCAATTCACAAC	AAAAGCTGGAACGCCCTTTTGACGAGTATAGT
TATTATCAATCGCAAAACTACAAAATTTGAAAGCAATTCACAAC	TACGTTAGGCATTATAACCTTTGCCGATGAGA
TGTTATCAATCGCAAAACTACAAAATTTGAAAGCAATTCACAAC	CTCTCGCCCTCCCTCCCGTTGGTCGGTTGGGA
TGTTATCAATCACAAAATTACAAAATTTGAAAGCAATTCACAAC	AAAGCATTAAACAAACAACAAGAGATACAAGT
TGTTATCAATCACAAGACTACAAAATTTGAAAGTAATTCACAAC	GTTTTCTAACTTTATGAAACCCGGACAAGAGT
TGTTATCAATCGCAAAACCACAAAATCTGAAAGCAATTCACAAC	CTGTCACCTATTTGGTATTGATTTGAAAAAGA
TGTTATCAATCACAAAACTACAAAATTTGAAAGCAATTCACAAC	TACCCAGTGGAGGACCCTCAAGCACACTTTGA
TGTTATCAATCACAAAACTACAAAATTTGAAAGCAATTCACAAC	CAACAAATGAATGAGATGAGCAAACAAAGTGA
TGTTATCAATCACAAAACTACAAAATTTGAAAGCAATTCACAAC	CAACAAATGAATGAGATGAGCAAACAAAGAGA
TGTTATCAATCACAAAACTACAAAATTTGAAAGCAATTCACAAC	TTTTAGCACAAACAAGAACGTACGAAAGTTGT
TGTTATCAATCACAAAACTACAAAATTTGAAAGCAATTCACAAC

>NZ_CP046316|3|3|340776-342183|CRISPRCasFinder
TGTTATCAATCACAAAACTACAAAATTTGAAAGCAATTCACAAC	AAAGACTTCCCTATTTTGAATAACCTGATAGT
TGTTATCAATCACAAAACTACAAAATTTGAAAGCAATTCACAAC	CAGTCCTTAATGTGTAGAGGGAACTGCCATGT
TGTTATCAATCACAAAACTACAAAATTTGAAAGCAATTCACAAC	GAGCTATGTAGCTATACACAATGAGGGAGGGA
TGTTATCAATCACAAAACTACAAAATTTGAAAGCAATTCACAAC	TGCCAGCCTTGTAGCATATAGATAGCGTTAGA
TGTTATCAATCATTAAACTACAAAATTTGAAAGCAATTCACAAC	AAACCGCTTACTCCAATAATCGCGTTTGT
TGTTATCAATCACAAAATTACAAAATTTGAAAGCAATTCACAAC	AGGCTTTTTTGAAGGGGTTTTTGCTTGAGGT
TGTTATCAATCGCAAAACTATAAAATTTGAAAGCAATTCACAAC	CAACAAATGAATGAAACAGCAAAACAAAGTGT
TGTTATCAATCGCAAAACTACAAAATTTGAAAGCAATTCACAAC	AACTACATCTTACAAGGCTTTGGATTTAGGGT
TGTTATCAATCACAAAACTACAAAATTTGAAAGCAATTCACAAC	AAAAGCTGGAACGCCCTTTTGACGAGTATAGT
TATTATCAATCGCAAAACTACAAAATTTGAAAGCAATTCACAAC	TACGTTAGGCATTATAACCTTTGCCGATGAGA
TGTTATCAATCGCAAAACTACAAAATTTGAAAGCAATTCACAAC	CTCTCGCCCTCCCTCCCGTTGGTCGGTTGGGA
TGTTATCAATCACAAAATTACAAAATTTGAAAGCAATTCACAAC	AAAGCATTAAACAAACAACAAGAGATACAAGT
TGTTATCAATCACAAGACTACAAAATTTGAAAGTAATTCACAAC	GTTTTCTAACTTTATGAAACCCGGACAAGAGT
TGTTATCAATCGCAAAACCACAAAATCTGAAAGCAATTCACAAC	CTGTCACCTATTTGGTATTGATTTGAAAAAGA
TGTTATCAATCACAAAACTACAAAATTTGAAAGCAATTCACAAC	TACCCAGTGGAGGACCCTCAAGCACACTTTGA
TGTTATCAATCACAAAACTACAAAATTTGAAAGCAATTCACAAC	CAACAAATGAATGAGATGAGCAAACAAAGTGA
TGTTATCAATCACAAAACTACAAAATTTGAAAGCAATTCACAAC	CAACAAATGAATGAGATGAGCAAACAAAGAGA
TGTTATCAATCACAAAACTACAAAATTTGAAAGCAATTCACAAC	TTTTAGCACAAACAAGAACGTACGAAAGTTGT
TGTTATCAATCACAAAACTACAAAATTTGAAAGCAATTCACAAC

>NZ_CP046316|3|1|340776-342183|CRT
TGTTATCAATCACAAAACTACAAAATTTGAAAGCAATTCACAAC	AAAGACTTCCCTATTTTGAATAACCTGATAGT
TGTTATCAATCACAAAACTACAAAATTTGAAAGCAATTCACAAC	CAGTCCTTAATGTGTAGAGGGAACTGCCATGT
TGTTATCAATCACAAAACTACAAAATTTGAAAGCAATTCACAAC	GAGCTATGTAGCTATACACAATGAGGGAGGGA
TGTTATCAATCACAAAACTACAAAATTTGAAAGCAATTCACAAC	TGCCAGCCTTGTAGCATATAGATAGCGTTAGA
TGTTATCAATCATTAAACTACAAAATTTGAAAGCAATTCACAAC	AAACCGCTTACTCCAATAATCGCGTTTGT
TGTTATCAATCACAAAATTACAAAATTTGAAAGCAATTCACAAC	AGGCTTTTTTGAAGGGGTTTTTGCTTGAGGT
TGTTATCAATCGCAAAACTATAAAATTTGAAAGCAATTCACAAC	CAACAAATGAATGAAACAGCAAAACAAAGTGT
TGTTATCAATCGCAAAACTACAAAATTTGAAAGCAATTCACAAC	AACTACATCTTACAAGGCTTTGGATTTAGGGT
TGTTATCAATCACAAAACTACAAAATTTGAAAGCAATTCACAAC	AAAAGCTGGAACGCCCTTTTGACGAGTATAGT
TATTATCAATCGCAAAACTACAAAATTTGAAAGCAATTCACAAC	TACGTTAGGCATTATAACCTTTGCCGATGAGA
TGTTATCAATCGCAAAACTACAAAATTTGAAAGCAATTCACAAC	CTCTCGCCCTCCCTCCCGTTGGTCGGTTGGGA
TGTTATCAATCACAAAATTACAAAATTTGAAAGCAATTCACAAC	AAAGCATTAAACAAACAACAAGAGATACAAGT
TGTTATCAATCACAAGACTACAAAATTTGAAAGTAATTCACAAC	GTTTTCTAACTTTATGAAACCCGGACAAGAGT
TGTTATCAATCGCAAAACCACAAAATCTGAAAGCAATTCACAAC	CTGTCACCTATTTGGTATTGATTTGAAAAAGA
TGTTATCAATCACAAAACTACAAAATTTGAAAGCAATTCACAAC	TACCCAGTGGAGGACCCTCAAGCACACTTTGA
TGTTATCAATCACAAAACTACAAAATTTGAAAGCAATTCACAAC	CAACAAATGAATGAGATGAGCAAACAAAGTGA
TGTTATCAATCACAAAACTACAAAATTTGAAAGCAATTCACAAC	CAACAAATGAATGAGATGAGCAAACAAAGAGA
TGTTATCAATCACAAAACTACAAAATTTGAAAGCAATTCACAAC	TTTTAGCACAAACAAGAACGTACGAAAGTTGT
TGTTATCAATCACAAAACTACAAAATTTGAAAGCAATTCACAAC

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP046316.1|WP_009392478.1|328031_329222_+|6-bladed-beta-propeller	unknown	unknown	gnl|CDD|375027
NZ_CP046316.1|WP_009392525.1|342263_342515_+|GlsB/YeaQ/YmgE-family-stress-response-membrane-protein	unknown	unknown	gnl|CDD|225170
NZ_CP046316.1|WP_009392517.1|340314_340656_+|CRISPR-associated-endonuclease-Cas2	cas2	COG3512_cas2_CAS-II-A:CAS-II-B:CAS-II-C	gnl|CDD|226043
NZ_CP046316.1|WP_009392537.1|349364_349916_+|transcription-termination/antitermination-factor-NusG	unknown	unknown	gnl|CDD|180161
NZ_CP046316.1|WP_009392526.1|342589_342970_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP046316.1|WP_009392528.1|343320_343701_-|phage-holin-family-protein	unknown	unknown	gnl|CDD|377816
NZ_CP046316.1|WP_009392535.1|347673_349059_+|leucine-rich-repeat-domain-containing-protein	unknown	unknown	gnl|CDD|275383
NZ_CP046316.1|WP_009392472.1|320716_321859_+|lactonase-family-protein	unknown	unknown	gnl|CDD|378416
NZ_CP046316.1|WP_009392530.1|344371_345013_-|pyridoxamine-5'-phosphate-oxidase	unknown	unknown	gnl|CDD|273138
NZ_CP046316.1|WP_009392516.1|335889_340197_+|type-II-CRISPR-RNA-guided-endonuclease-Cas9	cas9	cd09643_cas9_CAS-II-A:CAS-II-B:CAS-II-C	gnl|CDD|375967
NZ_CP046316.1|WP_009392531.1|345129_347247_-|peptidyl-prolyl-cis-trans-isomerase	unknown	unknown	gnl|CDD|372650
NZ_CP046316.1|WP_009392536.1|349166_349352_+|preprotein-translocase-subunit-SecE	unknown	unknown	gnl|CDD|376355
NZ_CP046316.1|WP_009392470.1|319328_320711_+|aromatic-amino-acid-lyase	unknown	unknown	gnl|CDD|376303
NZ_CP046316.1|WP_009392527.1|343085_343331_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP046316.1|WP_034540508.1|327373_327976_+|CDP-alcohol-phosphatidyltransferase	unknown	unknown	gnl|CDD|223632
NZ_CP046316.1|WP_009392473.1|321903_323571_+|formate--tetrahydrofolate-ligase	unknown	unknown	gnl|CDD|376511
NZ_CP046316.1|WP_009392476.1|326255_326984_+|RNA-methyltransferase	unknown	unknown	gnl|CDD|349982
NZ_CP046316.1|WP_009392515.1|335255_335708_+|D-tyrosyl-tRNA(Tyr)-deacylase	unknown	unknown	gnl|CDD|376833
NZ_CP046316.1|WP_009392529.1|343705_344032_-|YtxH-domain-containing-protein	unknown	unknown	gnl|CDD|378938
NZ_CP046316.1|WP_034540504.1|323641_326215_-|BamA/TamA-family-outer-membrane-protein	unknown	unknown	gnl|CDD|366466

HMMScan for Signature genes

Protein	Cas_name	Cas_description	E-value	Identity	Coverage
NZ_CP046316.1|WP_009392517.1|340314_340656_+|CRISPR-associated-endonuclease-Cas2	cas2	COG3512_cas2_CAS-II-A:CAS-II-B:CAS-II-C	8.2e-29	94.9	0.2
NZ_CP046316.1|WP_009392516.1|335889_340197_+|type-II-CRISPR-RNA-guided-endonuclease-Cas9	cas9	cd09643_cas9_CAS-II-A:CAS-II-B:CAS-II-C	9.5e-63	207.5	57.7

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
NZ_CP046316.1|WP_009392478.1|328031_329222_+|6-bladed-beta-propeller	gnl|CDD|375027	pfam17170, DUF5128, 6-bladed beta-propeller. This family is a 6-bladed beta-propeller structure of unknown function. There is a highly conserved FDxxG motif which might be important.	1.03638e-10
NZ_CP046316.1|WP_009392525.1|342263_342515_+|GlsB/YeaQ/YmgE-family-stress-response-membrane-protein	gnl|CDD|225170	COG2261, COG2261, Predicted membrane protein [Function unknown].	2.07502e-05
NZ_CP046316.1|WP_009392517.1|340314_340656_+|CRISPR-associated-endonuclease-Cas2	gnl|CDD|226043	COG3512, COG3512, CRISPR-associated protein, Cas2 homolog [Defense mechanisms].	9.60297e-25
NZ_CP046316.1|WP_009392537.1|349364_349916_+|transcription-termination/antitermination-factor-NusG	gnl|CDD|180161	PRK05609, nusG, transcription antitermination protein NusG; Validated.	3.01229e-57
NZ_CP046316.1|WP_009392528.1|343320_343701_-|phage-holin-family-protein	gnl|CDD|377816	pfam07332, Phage_holin_3_6, Putative Actinobacterial Holin-X, holin superfamily III. Phage_holin_3_6 is a family of small hydrophobic proteins with two or three transmembrane domains of the Hol-X family. Holin proteins are produced by double-stranded DNA bacteriophages that use an endolysin-holin strategy to achieve lysis of their hosts. The endolysins are peptidoglycan-degrading enzymes that are usually accumulated in the cytosol until access to the cell wall substrate is provided by the holin membrane lesion.	0.00728175
NZ_CP046316.1|WP_009392535.1|347673_349059_+|leucine-rich-repeat-domain-containing-protein	gnl|CDD|275383	sd00036, LRR_3, leucine-rich repeats. A leucine-rich repeat (LRR) is a structural protein motif of 20-30 amino acids that is unusually rich in the hydrophobic amino acid leucine. The conserved eleven-residue sequence motif (LxxLxLxxN/CxL) within the LRRs corresponds to the beta-strand and adjacent loop regions, whereas the remaining parts of the repeats are variable. LRRs fold together to form a solenoid protein domain, termed leucine-rich repeat domain. Leucine-rich repeats are usually involved in protein-protein interactions.	8.24002e-40
NZ_CP046316.1|WP_009392472.1|320716_321859_+|lactonase-family-protein	gnl|CDD|378416	pfam10282, Lactonase, Lactonase, 7-bladed beta-propeller. This entry contains bacterial 6-phosphogluconolactonases (6PGL)YbhE-type (EC:3.1.1.31) which hydrolyze 6-phosphogluconolactone to 6-phosphogluconate. The entry also contains the fungal muconate lactonising enzyme carboxy-cis,cis-muconate cyclase (EC:5.5.1.5) and muconate cycloisomerase (EC:5.5.1.1), which convert cis,cis-muconates to muconolactones and vice versa as part of the microbial beta-ketoadipate pathway. Structures of proteins in this family have revealed a 7-bladed beta-propeller fold.	5.40541e-113
NZ_CP046316.1|WP_009392516.1|335889_340197_+|type-II-CRISPR-RNA-guided-endonuclease-Cas9	gnl|CDD|375967	pfam18541, RuvC_III, RuvC endonuclease subdomain 3. Cas9 proteins are abundant across the bacterial kingdom, but vary widely in both sequence and size. All known Cas9 enzymes contain an HNH domain that cleaves the DNA strand complementary to the guide RNA sequence (target strand), and a RuvC nuclease domain required for cleaving the noncomplementary strand (non-target strand), yielding double-strand DNA breaks (DSBs). The crystal structures of type II-A and II-C Cas9 proteins highlight the features in Cas9 enzymes that support their function as RNA-guided endonucleases. Cas9 enzymes adopt a bilobed architecture composed of a nuclease lobe containing juxtaposed RuvC and HNH nuclease domains and a variable alpha-helical lobe likely to be involved in nucleic acid binding. The RuvC domain forms the structural core of the nuclease lobe, a six-stranded beta sheet surrounded by four alpha helices, with all three conserved subdomains (I, II, III) contributing catalytic residues to the active site.	3.40614e-58
NZ_CP046316.1|WP_009392531.1|345129_347247_-|peptidyl-prolyl-cis-trans-isomerase	gnl|CDD|372650	pfam13616, Rotamase_3, PPIC-type PPIASE domain. Rotamases increase the rate of protein folding by catalyzing the interconversion of cis-proline and trans-proline.	2.32091e-39
NZ_CP046316.1|WP_009392536.1|349166_349352_+|preprotein-translocase-subunit-SecE	gnl|CDD|376355	pfam00584, SecE, SecE/Sec61-gamma subunits of protein translocation complex. SecE is part of the SecYEG complex in bacteria which translocates proteins from the cytoplasm. In eukaryotes the complex, made from Sec61-gamma and Sec61-alpha translocates protein from the cytoplasm to the ER. Archaea have a similar complex.	3.09425e-09
NZ_CP046316.1|WP_009392470.1|319328_320711_+|aromatic-amino-acid-lyase	gnl|CDD|376303	pfam00221, Lyase_aromatic, Aromatic amino acid lyase. This family includes proteins with phenylalanine ammonia-lyase, EC:4.3.1.24, histidine ammonia-lyase, EC:4.3.1.3, and tyrosine aminomutase, EC:5.4.3.6, activities.	7.64565e-119
NZ_CP046316.1|WP_009392530.1|344371_345013_-|pyridoxamine-5'-phosphate-oxidase	gnl|CDD|273138	TIGR00558, Pyridoxine/pyridoxamine_5'-phosphate_oxidase, pyridoxamine-phosphate oxidase. This model is similar to Pyridox_oxidase from Pfam but is designed to find only true pyridoxamine-phosphate oxidase and to ignore the related protein PhzG involved in phenazine biosynthesis. This protein from E. coli was characterized as a homodimer with two FMN per dimer. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine].	2.73039e-112
NZ_CP046316.1|WP_034540508.1|327373_327976_+|CDP-alcohol-phosphatidyltransferase	gnl|CDD|223632	COG0558, PgsA, Phosphatidylglycerophosphate synthase [Lipid metabolism].	0.000879264
NZ_CP046316.1|WP_009392473.1|321903_323571_+|formate--tetrahydrofolate-ligase	gnl|CDD|376511	pfam01268, FTHFS, Formate--tetrahydrofolate ligase.	0
NZ_CP046316.1|WP_009392476.1|326255_326984_+|RNA-methyltransferase	gnl|CDD|349982	cd18109, SpoU-like_RNA-MTase, SAM-dependent RNA methylase related to SpoU-TrmH. RNA 2'-O ribose methyltransferase catalyzes the methyltransfer from S-adenosyl-L-methionine (AdoMet) to the 2'-OH group of ribose in tRNA or rRNA. It is part of the SpoU family of MTases, a subfamily of the SPOUT methyltransferase superfamily. The SPOUT methyltransferase superfamily is a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot.	1.0382e-74
NZ_CP046316.1|WP_009392515.1|335255_335708_+|D-tyrosyl-tRNA(Tyr)-deacylase	gnl|CDD|376833	pfam02580, Tyr_Deacylase, D-Tyr-tRNA(Tyr) deacylase. This family comprises of several D-Tyr-tRNA(Tyr) deacylase proteins. Cell growth inhibition by several d-amino acids can be explained by an in vivo production of d-aminoacyl-tRNA molecules. Escherichia coli and yeast cells express an enzyme, d-Tyr-tRNA(Tyr) deacylase, capable of recycling such d-aminoacyl-tRNA molecules into free tRNA and d-amino acid. Accordingly, upon inactivation of the genes of the above deacylases, the toxicity of d-amino acids increases. Orthologues of the deacylase are found in many cells.	9.06637e-86
NZ_CP046316.1|WP_009392529.1|343705_344032_-|YtxH-domain-containing-protein	gnl|CDD|378938	pfam12732, YtxH, YtxH-like protein. This family of proteins is found in bacteria. Proteins in this family are typically between 100 and 143 amino acids in length. The N-terminal region is the most conserved. Proteins is this family are functionally uncharacterized.	1.07736e-12
NZ_CP046316.1|WP_034540504.1|323641_326215_-|BamA/TamA-family-outer-membrane-protein	gnl|CDD|366466	pfam01103, Bac_surface_Ag, Surface antigen. This entry includes the following surface antigens; D15 antigen from H.influenzae, OMA87 from P.multocida, OMP85 from N.meningitidis and N.gonorrhoeae. The family also includes a number of eukaryotic proteins that are members of the UPF0140 family. There also appears to be a relationship to pfam03865 (personal obs: C Yeats). In eukaryotes, it appears that these proteins are not surface antigens; S. cerevisiae YNL026W (SAM50) is an essential component of the Sorting and Assembly Machinery (SAM) of the mitochondrial outer membrane. The protein was localized to the mitochondria.	5.02861e-19

Protein sequences

>NZ_CP046316.1|WP_009392517.1|340314_340656_+|CRISPR-associated-endonuclease-Cas2
MIIAERYNAYRIMWVLVLYDLPTETKKMRREAQVFRDKLIKDGFTLFQFSMYIRHCPSRENAQVHINRVKQNLPQYGNIAIMCLTDKQFGDMEFFYCQKETTAPETYVQLELF
>NZ_CP046316.1|WP_009392516.1|335889_340197_+|type-II-CRISPR-RNA-guided-endonuclease-Cas9
MKNILGLDLGTTSIGFAHIVEDENKEKSEIKELGVRIVSLATDEQSDFEKGKSISTNANRTLKHGARLNLDRYQQRRKFLIDLLQKANLITSASILAENGKNTTHSTWQLRAKAVTERIEKEEFARVLLAINKKRGYKNSRKTKTEDEGQAIDGMAIAKCLYDENLTPGQLSLQLLQQNKKLLPDFYRSDLQKEFDLVWNLQKQFYPDILTDSFYKELQGKGKDATSKAFSKRYHFDTAENKGSKESVRLQAYQWRAEAISKQLSKEEVAYVLTEINNNLNNSSGYLGAISDRSKELYFNRQTVGQYLYAQLQENRHNSLKNKVFYRQDYLDEFERIWETQASFHKELTDELKKQIRDVVIFYQRKLKSQKGLVSFCEFESKEIEIEKDGKAITKSIGARVVPKSSPLFQEFKIWQILNNVTCKRKGIRKKKSSAKSTELDLFNEPSQSIFSLDMECKQLLFDELNLKGDLKSDKVLKLLGYSPQEWEINYNQLEGNRTQKSLYEAYLKIIEIEGYEVKDILQIKSTKDDWSLDESPLSASEIRERVKVIFQTLGICTKILYFDPLLPVKEFEQQYSYQLWHLLYSYESDDSTSGNETLYRILEKKYAFKREHATILANVALQDDYGSLSTKAIRKIYPYIKENQYSTACELAGYKHSKLSLTTEELEARELKNIIPLLKKNALRNPVVEKILNQMINVVNALIEKNSERDAEGKITKYFHFDEIRIELARELKKNAQERYEMTQNINKAKLEHQKISEKLQKQFGIKNPTKSDIIRYRLYQELEHNGYKELYTNTYIAPDVLFSKNIDIEHIVPKARVFDDSFSNKTLAFKEFNIKKGESTAFDYITSLNCEGELNQYLTRVENAYKTKSISLTKYKNLLKKASEIGDGFINRDLRDTQYIAKKAKEILFQVTKNVLSTSGSITDRLREDWGLVDVMKELNMPKYQSLGLTEVEERKDGNKVTVIKDWTKRNDHRHHAMDALTVAFTKPSYIQYLNHLNARKDENNKNYSVILAIEKKETIKVPINNGKNKRVFIEPILNFRQVAKKHLEEIFISHKAKNKVVTKNINKPAGTDKQQITLTPRGQLHKETIYGKYQYYVNKEEKVGVKFDERTITKVSNPLYREALLKRLQANDNDPKKAFAGKNALSKNPIYLDEAKTKTLPEKVNLTYLEEDFSIRKDISPDNFKDLKSIEKVIDQGVKRILIKRLQAYDNDPKKAFVDLEKNPIWLNKEKGIAIKRVTISGVSNAQPLHIGKDHLGKTTLNKEGKEVPVDYVSTGNNHHVAIYRDKEGNLQEQIVSFFEAVVRAQQGLPIIDKNYKQAEGWQFMFTMKQNEMFVFPNEATGFNPAEIDLLDPKNKKLISPNLFRVQTISIVKYGNSVVRDFKFRHHLETTLQDDKILQGITFQQIKSLEPLRNIVKVRINHLGDIVNIGEY
>NZ_CP046316.1|WP_009392515.1|335255_335708_+|D-tyrosyl-tRNA(Tyr)-deacylase
MRVVIQKVTQASVSIENQIVASIDKGLFVLVGIEDTDTNDDIAWLSAKIVNLRVFDDDNGVMNLSVKEVEGEVLIVSQFTLHASTKKGNRPSYIKAARPEVAIPIYEAFIKQVESLLGKRVPTGQFGVMMQVSLCNDGPVTILIDTKNKE
>NZ_CP046316.1|WP_009392478.1|328031_329222_+|6-bladed-beta-propeller
MKLPIILGLLTASITASFAQPFRDTTVLQLADTKVLTAETSQAQHLNLNPFLVKDKEFDFGALLKEINFVPLETTAQSRLGQIRKVVTTAEHIYIMDDLDESGIVIFTRQGKFVKRIPNGKKPEQLYRLYDIDFNTQTNELIAYKRSFLLIFDKEGNFLRFKYLPIGFLNMAATPDGYVLKSLVGQNKNLGDKSNYRLQFINKDLKLNAVALPDKESKAFSAKSYLYRVADLVKITAEISDTIYQYNPKDNKLAAEFILDYDHKLPRSYIYGKDFSVFENAIRDHNYNYCIGDYIETTHHNVFFISNKTANVVVYRDKHSGNMVGGGIAQSKQGLPFLAFPDSFYDDQLIKYYYPGENDYEVLKEMPFLSEANKKKSESFKKGDNPILIYYTLNKF
>NZ_CP046316.1|WP_034540508.1|327373_327976_+|CDP-alcohol-phosphatidyltransferase
MPLPYILILFRFLLAPTIFWIAYATPESVARPAIVIAIVVGLLSDIFDGIIARHRGISTVKMRRLDSQTDLVFWLSVGVACYWLNPALITAYRYQIITLFVMEALCYGLSFLRFGKETCTHAFLSKIWGLTLLIAFVSLIGFGYGGFPLQLAIYWGLLSQTDVILIILLLPRWQNDIPSAYHAYLIRKGKTIKKNKWLNS
>NZ_CP046316.1|WP_009392476.1|326255_326984_+|RNA-methyltransferase
MLSKNQVKLIQKLHHKKYRNELNLFIVEGKKSINEFLQAGYTPQLLIATEAFTTSVPQHLITPVSKDELRKVSTLQNPDEGLAVFQQPKHKGILQEGVIVALDNVQDPGNLGTIIRLCDWFGVETLLCNTQTVDCYNPKVVQATMGSLTRVAVHYLDLAAFLTTTALPVYTMDLEGENLYTATFPKDCILILGNEANGISSEVRALSNEVITIPRFSQHQRTESLNVAMAGAIILSEVMGHH
>NZ_CP046316.1|WP_034540504.1|323641_326215_-|BamA/TamA-family-outer-membrane-protein
MKKAFFRYSFISGLCVLLCYLSACEATKRVAADDYLLRENKVYVNDALTDDAKVNNFIFQKPNSYILGLPVSLYIYNWANPHSEEEFVQWLDNHPRWHRFLNGFLSKKQVGRLQESFLVSGIDHQLQKIGEAPVILDTAQVRRSTKQLAAYYRSIGYFNAKVGDSIRKLTKTEKRTAIVDYYIQTGDRYYIDSLKTAITSPEIDSVYRLHLDKTLLKQGAPYQLADFAGERTRLYTLFRNKGFYTFQQSSINFEIVRDTVHKQKDRNLQVSTNIGDLIERDGDVVTTKKYKVHHINKIRMYTDYDSQTDKSALDSITYRDLIIYYKDKLHYRPRVLWRASGLRQGQLYSDTDRGNTYKQLNNLRVFRYPNMEFKYPAKDTLMNKLDANIYLSPLDKFSLRLTNEIKRSEIEAIGFGVGTAFSARNVFRGAETLELNLQGTFASQPSLNDSHFFNTSEISGDVRFIFPTILFPLNTRKLIPYYMTPQTILQAGMSYQTNIGIDKRTTSGLLRYVWNPREQKNKVIFDLINVQYVNNINPRNFFSIYQSTYERLNDISRKYHLGTAYVDSRGNLTPREGTFRFLGDIFNRTIPVQAEDVVPLLGILERYNRITNNDFIVSSSYTYIFNSKSQFFERDFSQFRIKVEAAGGLLNTLASTYNVVKTDNNKNKIFGVEYAQFAKGELDFIKHFPIGKQNSLAFRSFFGIAVPYGNSDNIPFSQSYFAGGTTDNRGFKAYRLGPGASQSVFDYNEANMKLTLNLEYRFQMLGAFKGALFTDVGNIWNVADNTPIADNKFVNFSSLKDVGVSTGFGLRYDFNFFVIRLDMGVPTYDPAYEVGDRWIKKFKMKDVVFNFGINYPF
>NZ_CP046316.1|WP_009392473.1|321903_323571_+|formate--tetrahydrofolate-ligase
MTDLEIAQKAQMLPIREVAKKLNISEDNLDPYGKYKAKLPLHLINPEKMKNSKLVLVTAITPTPAGEGKTTVSIGLTEGLNKIGKKAIAVLREPSLGPVFGIKGGAAGGGYSQVVPMEDINLHFTGDFSAIEKANNLLSAVIDNNIQSKTHSIGIDPRTVVWKRVMDMNDRALRHIVVGLGGSTHGTPREDGFNITPASEIMAILCLSESFSDLKRRIGNIYVGKKFDGTPVFARDLNVVGAMALLLKEAIKPNLVQTLENNPAILHGGPFASIAQGTNTVLATKMGLSLGDYVVTEAGFGADLGAEKFLNIKCVSAGLAPDAVVVVATIRALRHHGGAKKEEYNTPDLQKVKLGIANLEKHIENVQHFGLKAVVAINYFPHDSEEEIAYVKEVCAKKGVEAVVSKGFSEGGKGTEELARAVVAIAESGESHFAPLYSHQASIEDKITTVATKIYGANKVNYSSKALSQLKQINKLGFDKLPVCIVKTPKSLSDDEKKLARPTDFEVTVREFEFASGAGFVIPILGDTVRMPGLPSVPAAEGMDIDDEGIISGLS
>NZ_CP046316.1|WP_009392472.1|320716_321859_+|lactonase-family-protein
MKKLQILLVLLGAIVSLHSFAQGGKVNNLTMYVGTYTEGGNSKGIYTYNFNQENGTFELLNTATAANPSFVTLSPEGKRLYAVSEYNDGRQGAYSFDLSENKAKLSNPVFRPTASKDALPRAGADPCHIVSDGNYVITANYTGGDTSVFSLDTEGRLQAEVQHIAFAGRTPERVAHIHCIIPTPDKKYILATDLGNDRVYRFRYNKKASKKAEVLTAQQVAYQVSDGQGPRHLTFSKDGHFAYLINELGGECVVLSYRKGKLKEVQRLIADEGGGCGSADIHISPDGRFLYTSHRLKKDGIAIFAINPKKGTLTKVGYQLTGVHPRNFAITPNGKYLLVACRDNNKIQVFQRNETTGELTETSQEIEVDKPTCILFAKSN
>NZ_CP046316.1|WP_009392470.1|319328_320711_+|aromatic-amino-acid-lyase
MVHYISNEVLLLEQLDTIINTDVKLKLSEEAVLNIEKCHTFFTEKVKDTSLSEATEQHYTQLRHYACGIGERLPCKLVRIMLFLKIQSFSYGFSGVRLALVQRLIDFFNNGVYPVVYSKDIPDERIALAHLSLPLIGEGEVCIQNKIYSAQELASKYGWEPLPLSQREVDALLNGTQLTTAYSAHNLIESLKLIEWADFVASVSTQVFGGNLSAFSELMQVVRPHKGLVETAQHLRTLLKDSTLVDSPEDFQSMPEAFCSIPQIHGAVREAIAAIRKVVKTEINSVTDNPILFPEQGEIIFGGNSHTLPLSLSMDFLSITLTSLGNISERRVFYLLSNVGKDIETEIDYPIFQRIIEGILNENRRLSTPSSIESPILFEKTIDIKGMGGSSAIKCSQIVKNVMQIIAIELILATSLWKKKPLRYHSSIFKDYLDFIAEEEATTLKKQIEHTIQFFNSTQN
>NZ_CP046316.1|WP_009392525.1|342263_342515_+|GlsB/YeaQ/YmgE-family-stress-response-membrane-protein
MGIIATLIIGAIAGWLGGTIYKGSGLGLIGNIIIGVLGSSVGYWLLGSVLHISLGEGLIGSILTGAIGAIVILFLINLIFKKK
>NZ_CP046316.1|WP_009392526.1|342589_342970_-|hypothetical-protein
MKKIIALASVICLSLVFFASCSKNDDPADNDLFVGTYKGEISFLKGKEKKSVDNGSVTVVKTGNDYYFRFSDGIEDLKGVSFKKEGDNTLVNVDLQDGLKVIRINASSLYILYTTDGKTWIANAKR
>NZ_CP046316.1|WP_009392527.1|343085_343331_-|hypothetical-protein
MNNKTYSSFEEIDNEIRLLRLEKEIDRLSLTQQVSASAESLSPKNLLANTLGSLFNNKRWLNIALGYGMQLLAKRYLNKNK
>NZ_CP046316.1|WP_009392528.1|343320_343701_-|phage-holin-family-protein
MAIYSIKETFVEVPTKANTAFNSQFAYYKMIVFRFIAKSSYGLITFFVYAFACLLILFFLSLAAAYAIGEALGSNGLGFAIVGAFYILLSLVVLLFRRKLIEKSLLQKLSEIYFKSDPEDEEENEQ
>NZ_CP046316.1|WP_009392529.1|343705_344032_-|YtxH-domain-containing-protein
MSKTANAVLGLAVGTAIGVGLGILFAPDEGKNTRKKIKDSLRDKSDEFKEQLDNLTESVREKSLELKGSLEEKVDRLFSKSSNKAEDVISLLEKKLASLKEEAAKIKK
>NZ_CP046316.1|WP_009392530.1|344371_345013_-|pyridoxamine-5'-phosphate-oxidase
MDLSNYRKTYNKRELLEKDAPENPMQLFQTWFYEADETDSIDEANAMSVSTIGLDGFPKTRVVLLKQYTYEGFIFYTNYHSEKGKAIEANPHLCLSFFWPSIERQVIIKGIAERVPANTSDGYFESRPLGSRLGAIVSPQSEVIPTREYLEEQLHALEMQYEGKEVPRPAHWGGYLVRPQSIEFWQGRPNRLHDRLRYTLTEDYDWKIERLAP
>NZ_CP046316.1|WP_009392531.1|345129_347247_-|peptidyl-prolyl-cis-trans-isomerase
MAVLEKIRSKTVFLIAIIGLALFAFIISDFIGKGRFSNHQPTEIGTVNGEDVPIDAFRLQVENAVHQANGQASSIEAAKYVWEQNVQQILLNQQIEKLGLSVEKDQIISILAKTPLAQNPQFVNEYGVFDPSKFTAYLNTLKSNNPQAYAQWKMQEDAIIEGAKQQMYFSLIRAGLGVTNAEAEIAYHQEKDMADISYVALQYSSIDDKNINVSDSEIKDYIKKHEKQFKQEAYRNIQYIVVNEKPSAADTQAEKEAINKLLQPEIVFNNQTHANDTIAGFAQTKNVKEFVDRHSDTPYDTLFVSKEDLRSAYADTLFALPVGKVFGPYEEDGNLKLSRMIAKDPNGAVKASHILIAYKGSQAATPNTTRTKEEAKAKAESLLAEAKAAGADFAALASENSDEPGANYRGGDLGFFKRGAMVKPFEQFVFANPVGTIGIVETDFGYHVVKVTDKAPTVQLATITRKVEPSEATLNELFSKVSNFEMKASQNPKDFSNIAKSSDLTVLRADNLHKNDDQIIGLGANRQIVQWLFNKETKVGDLKKFTNGGNYIVAQLVKQGEEGLSDVQDVAPFVKPILIREKKAAILKEKAKGNSLAAIASANKTEVKTATGLTMNNPILIGEGREPKVIGAAFGLKQGAISKPIDGENAVYVIQVSSVSVAPATNDYKTYAETIEKLRTERAGQGILKSLENSATIKENISAFY
>NZ_CP046316.1|WP_009392535.1|347673_349059_+|leucine-rich-repeat-domain-containing-protein
MPTTIYKTYVCILFFALQLCFSQKGEEALFIKEGTLLKCENNRIPADGRIELPRTVKAIAPEAFKDCSRLKSINIGGSVTLIGDRAFYGCNTLTKAEFLPNTVTAIGEQAFAFCGKLSSANLPNSVATIGTEAFRACFALTAITIPESTTNIGDNAFLDCSSLQQVTFLTNQLPILPSGIFYQCKQLKEALLPASVRRIKSSAFAYCENLSRVVLPEQLEAIGDDSFEYCKSLRAIDIPDSVVFIGASAFHSCSLLTDVKLPYGLRHLLNDTFLDCTSLKAILIPDTVEKIDMQVFRNCSSLEAVQFPLALTDILYAAFYGCKKLQEVTLPDEVKYIGMFAFAECESLAYIELPRAVVDIAAKVFYNCTSLSEVKLSKFTATIGVQAFYGCTNLKDLRLPPSVEKIDLGAFENTGLTELHCKAIAPPEVNRSFGYKGKVLVPFRSLDAYKAAIGWQDCALE
>NZ_CP046316.1|WP_009392536.1|349166_349352_+|preprotein-translocase-subunit-SecE
MVQYVKESYEELKNHVTWPTLADSQREMVVVVVFSILFSLVIWGMDSFFEWIIAEYFKFMQ
>NZ_CP046316.1|WP_009392537.1|349364_349916_+|transcription-termination/antitermination-factor-NusG
MSGLLEKKWYVIKTVTGQENKIKNYVETESARLGYADYVEEVLVPTEKVVQVRNGKKTTKDRVHMPGYVMVKAHLAGEVVHIIKSIPGVVGFLSETKGGDPLPLRKADVNRMLGQVDELSETVETVAIPFEVGEVVKLIEGPFNGFNGTIERVNEEKRKLEVMVKIFGRKTPLELNYTQVEKL

Crispr_ID: NZ_CP046316_4

• CRISPR_ID: NZ_CP046316_4
• CRISPR_location: 2041742-2042004
• CRISPR_type: Orphan
• Repeat_type: NA
• Spacer_info: 2 spacers

Consensus repeat of NZ_CP046316_4

Consensus_repeat	Method
ATATGGTTTTATAGATAAAACAGGTAAAGAAGTGATTCCTATAAAGTATGATGATG	PILER-CR

spacers of NZ_CP046316_4

>4.1|2041798|46|NZ_CP046316|PILER-CR
CGAGCAGTTTTTCAGAAGGATTAGCAAGCGTGAGTTTGAATTATAG
>4.2|2041900|49|NZ_CP046316|PILER-CR
ATGTTTGGGATTTTTCAGAAGGATTAGCAAAGGTTAGCCTAAATAACAA

CRISPR arrays and Neighbor proteins around NZ_CP046316_4

CRISPR arrays

The CRISPR arrays of NZ_CP046316_4

>merge|NZ_CP046316|4|2041742-2042004|PILER-CR
ATATGGTTTTATAGATAAAACAGGTAAAGAAGTGATTCCTATAAAGTATGATGATGCGAGCAGTTTTTCAGAAGGATTAGCAAGCGTGAGTTTGAATTATAGATATGGTTTTATAGATAAAACAGGTAAAGAAGTGATTCCTATAAAGTATAATTATGATGTTTGGGATTTTTCAGAAGGATTAGCAAAGGTTAGCCTAAATAACAAATATGGTTTTATAGATAAAACAGGTAAAGAAGTGATTCCTATAAAGTATGTTGATA

>NZ_CP046316|4|2|2041742-2042004|PILER-CR
ATATGGTTTTATAGATAAAACAGGTAAAGAAGTGATTCCTATAAAGTATGATGATG	CGAGCAGTTTTTCAGAAGGATTAGCAAGCGTGAGTTTGAATTATAG
ATATGGTTTTATAGATAAAACAGGTAAAGAAGTGATTCCTATAAAGTATAATTATG	ATGTTTGGGATTTTTCAGAAGGATTAGCAAAGGTTAGCCTAAATAACAA
ATATGGTTTTATAGATAAAACAGGTAAAGAAGTGATTCCTATAAAGTATGTTGATA

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP046316.1|WP_009391872.1|2036976_2037474_+|thiol-peroxidase	unknown	unknown	gnl|CDD|179055
NZ_CP046316.1|WP_009390446.1|2049436_2051326_+|ABC-F-family-ATP-binding-cassette-domain-containing-protein	unknown	unknown	gnl|CDD|223562
NZ_CP046316.1|WP_009390438.1|2044101_2045274_+|nicotinate-phosphoribosyltransferase	unknown	unknown	gnl|CDD|235406
NZ_CP046316.1|WP_034540060.1|2045444_2045990_+|Smr/MutS-family-protein	unknown	unknown	gnl|CDD|376599
NZ_CP046316.1|WP_009391871.1|2037609_2040048_+|DNA-translocase-FtsK	unknown	unknown	gnl|CDD|224588
NZ_CP046316.1|WP_009391874.1|2035257_2036592_-|TolC-family-protein	unknown	unknown	gnl|CDD|224455
NZ_CP046316.1|WP_009390441.1|2045989_2046664_+|ABC-transporter-ATP-binding-protein	unknown	unknown	gnl|CDD|213222
NZ_CP046316.1|WP_009390443.1|2047141_2047588_+|hypothetical-protein	unknown	unknown	gnl|CDD|371505
NZ_CP046316.1|WP_034540048.1|2040069_2040846_+|DUF2807-domain-containing-protein	unknown	unknown	gnl|CDD|371327
NZ_CP046316.1|WP_009390437.1|2042793_2043987_+|aspartate-aminotransferase-family-protein	unknown	unknown	gnl|CDD|99735
NZ_CP046316.1|WP_009391869.1|2040996_2041236_+|WG-repeat-containing-protein	unknown	unknown	gnl|CDD|379719
NZ_CP046316.1|WP_034540051.1|2031974_2032280_-|KilA-N-domain-containing-protein	unknown	unknown	gnl|CDD|367917
NZ_CP046316.1|WP_009390445.1|2048112_2049339_+|NAD(P)/FAD-dependent-oxidoreductase	unknown	unknown	gnl|CDD|272992
NZ_CP046316.1|WP_009391876.1|2033064_2033811_-|ABC-transporter-ATP-binding-protein	unknown	unknown	gnl|CDD|213222
NZ_CP046316.1|WP_009390447.1|2051330_2052788_+|lipase	unknown	unknown	gnl|CDD|238863
NZ_CP046316.1|WP_155846659.1|2031190_2031892_-|SH3-domain-containing-protein	unknown	unknown	gnl|CDD|274349
NZ_CP046316.1|WP_155846660.1|2032315_2033005_-|SH3-domain-containing-protein	unknown	unknown	unknown
NZ_CP046316.1|WP_009390444.1|2047589_2048024_+|hypothetical-protein	unknown	unknown	gnl|CDD|371505
NZ_CP046316.1|WP_009391875.1|2033811_2035041_-|efflux-RND-transporter-periplasmic-adaptor-subunit	unknown	unknown	gnl|CDD|273776
NZ_CP046316.1|WP_009390442.1|2046690_2047086_+|hypothetical-protein	unknown	unknown	gnl|CDD|371505

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
NZ_CP046316.1|WP_009391872.1|2036976_2037474_+|thiol-peroxidase	gnl|CDD|179055	PRK00522, tpx, thiol peroxidase.	7.40517e-89
NZ_CP046316.1|WP_009390446.1|2049436_2051326_+|ABC-F-family-ATP-binding-cassette-domain-containing-protein	gnl|CDD|223562	COG0488, Uup, ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only].	0
NZ_CP046316.1|WP_009390447.1|2051330_2052788_+|lipase	gnl|CDD|238863	cd01825, SGNH_hydrolase_peri1, SGNH_peri1; putative periplasmic member of the SGNH-family of hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.	5.41199e-28
NZ_CP046316.1|WP_034540060.1|2045444_2045990_+|Smr/MutS-family-protein	gnl|CDD|376599	pfam01713, Smr, Smr domain. This family includes the Smr (Small MutS Related) proteins, and the C-terminal region of the MutS2 protein. It has been suggested that this domain interacts with the MutS1 protein in the case of Smr proteins and with the N-terminal MutS related region of MutS2. This domain exhibits nicking endonuclease activity that might have a role in mismatch repair or genetic recombination. It shows no significant double strand cleavage or exonuclease activity. The full-length human NEDD4-binding protein 2 also has the polynucleotide kinase activity.	4.90009e-07
NZ_CP046316.1|WP_009391871.1|2037609_2040048_+|DNA-translocase-FtsK	gnl|CDD|224588	COG1674, FtsK, DNA segregation ATPase FtsK/SpoIIIE and related proteins [Cell division and chromosome partitioning].	1.87095e-127
NZ_CP046316.1|WP_009391874.1|2035257_2036592_-|TolC-family-protein	gnl|CDD|224455	COG1538, TolC, Outer membrane protein [Cell envelope biogenesis, outer membrane / Intracellular trafficking and secretion].	3.01375e-43
NZ_CP046316.1|WP_009390441.1|2045989_2046664_+|ABC-transporter-ATP-binding-protein	gnl|CDD|213222	cd03255, ABC_MJ0796_LolCDE_FtsE, ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and cell division protein. This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. An FtsE null mutants showed filamentous growth and appeared viable on high salt medium only, indicating a role for FtsE in cell division and/or salt transport. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.	5.37372e-108
NZ_CP046316.1|WP_009390443.1|2047141_2047588_+|hypothetical-protein	gnl|CDD|371505	pfam11396, PepSY_like, Putative beta-lactamase-inhibitor-like, PepSY-like. This family of bacterial proteins is probably periplasmic. Members are found predominantly in microbes of the human gut and oral cavity. Structurally, one member of this family is found to show similarity to the beta-lactamase-inhibitor PepSY proteins, so the overall function may be inhibitory. There are tandem repeats of the domain on many family members.	9.3242e-25
NZ_CP046316.1|WP_034540048.1|2040069_2040846_+|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).	2.05504e-14
NZ_CP046316.1|WP_009390438.1|2044101_2045274_+|nicotinate-phosphoribosyltransferase	gnl|CDD|235406	PRK05321, PRK05321, nicotinate phosphoribosyltransferase; Provisional.	0
NZ_CP046316.1|WP_009391869.1|2040996_2041236_+|WG-repeat-containing-protein	gnl|CDD|379719	pfam14903, WG_beta_rep, WG containing repeat. This repeat contains an N-terminal WG repeat motif. The extent of the repeat is poorly defined. This repeat may form a beta solenoid structure (Bateman A pers. obs.).	0.000104043
NZ_CP046316.1|WP_034540051.1|2031974_2032280_-|KilA-N-domain-containing-protein	gnl|CDD|367917	pfam04383, KilA-N, KilA-N domain. The amino-terminal module of the D6R/N1R proteins defines a novel, conserved DNA-binding domain (the KilA-N domain) that is found in a wide range of proteins of large bacterial and eukaryotic DNA viruses. The KilA-N domain family also includes the previously defined APSES domain. The KilA-N and APSES domains may also share a common fold with the nucleic acid-binding modules of the LAGLIDADG nucleases and the amino-terminal domains of the tRNA endonuclease.	1.61509e-06
NZ_CP046316.1|WP_009390445.1|2048112_2049339_+|NAD(P)/FAD-dependent-oxidoreductase	gnl|CDD|272992	TIGR00275, TIGR00275, flavoprotein, HI0933 family. The model when searched with a partial length search brings in proteins with a dinucleotide-binding motif (Rossman fold) over the initial 40 residues of the model, including oxidoreductases and dehydrogenases. Partially characterized members include an FAD-binding protein from Bacillus cereus and flavoprotein HI0933 from Haemophilus influenzae. [Unknown function, Enzymes of unknown specificity].	5.3394e-152
NZ_CP046316.1|WP_009391876.1|2033064_2033811_-|ABC-transporter-ATP-binding-protein	gnl|CDD|213222	cd03255, ABC_MJ0796_LolCDE_FtsE, ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and cell division protein. This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. An FtsE null mutants showed filamentous growth and appeared viable on high salt medium only, indicating a role for FtsE in cell division and/or salt transport. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.	7.52306e-109
NZ_CP046316.1|WP_155846659.1|2031190_2031892_-|SH3-domain-containing-protein	gnl|CDD|274349	TIGR02916, sensor_histidine_kinase, putative PEP-CTERM system histidine kinase. Members of this protein family have a novel N-terminal domain, a single predicted membrane-spanning helix, and a predicted cystosolic histidine kinase domain. We designate this protein PrsK, and its companion DNA-binding response regulator protein (TIGR02915) PrsR. These predicted signal-transducing proteins appear to enable enhancer-dependent transcriptional activation. The prsK gene is often associated with exopolysaccharide biosynthesis genes. [Protein fate, Protein and peptide secretion and trafficking, Signal transduction, Two-component systems].	0.0020681
NZ_CP046316.1|WP_009390437.1|2042793_2043987_+|aspartate-aminotransferase-family-protein	gnl|CDD|99735	cd00610, OAT_like, Acetyl ornithine aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to ornithine aminotransferase, acetylornithine aminotransferase, alanine-glyoxylate aminotransferase, dialkylglycine decarboxylase, 4-aminobutyrate aminotransferase, beta-alanine-pyruvate aminotransferase, adenosylmethionine-8-amino-7-oxononanoate aminotransferase, and glutamate-1-semialdehyde 2,1-aminomutase. All the enzymes belonging to this family act on basic amino acids and their derivatives are involved in transamination or decarboxylation.	4.53901e-134
NZ_CP046316.1|WP_009390444.1|2047589_2048024_+|hypothetical-protein	gnl|CDD|371505	pfam11396, PepSY_like, Putative beta-lactamase-inhibitor-like, PepSY-like. This family of bacterial proteins is probably periplasmic. Members are found predominantly in microbes of the human gut and oral cavity. Structurally, one member of this family is found to show similarity to the beta-lactamase-inhibitor PepSY proteins, so the overall function may be inhibitory. There are tandem repeats of the domain on many family members.	2.85763e-18
NZ_CP046316.1|WP_009391875.1|2033811_2035041_-|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].	3.71576e-58
NZ_CP046316.1|WP_009390442.1|2046690_2047086_+|hypothetical-protein	gnl|CDD|371505	pfam11396, PepSY_like, Putative beta-lactamase-inhibitor-like, PepSY-like. This family of bacterial proteins is probably periplasmic. Members are found predominantly in microbes of the human gut and oral cavity. Structurally, one member of this family is found to show similarity to the beta-lactamase-inhibitor PepSY proteins, so the overall function may be inhibitory. There are tandem repeats of the domain on many family members.	9.4675e-09

Protein sequences

>NZ_CP046316.1|WP_009391869.1|2040996_2041236_+|WG-repeat-containing-protein
MDWNAFIRVYLQVPKKSLNTFIDKIGREVIPTRYFDAKSFSGGVALVRPTELDRWFEINKKGECAEFCDEAPAGHPITK
>NZ_CP046316.1|WP_034540048.1|2040069_2040846_+|DUF2807-domain-containing-protein
MKNIILSIGFILISTVLSAQNVFEASGERSTQKISVAKYTKIAIDEMLDVALVNEKNDHIYIDADNAIHPIIKTTVEEGTLKVALKLPKGVNMVQTGGITVKIPVKGTEELQMKMGKLSSDEPIKLASYKIKLDYVSELNLDLNIQELDLKISSCRKGDLKLNCKNLTFEAGSLSGLAISGKAENATFVSNGIANIEAYDLKIQDATFDNSSILKAKLYINGTIQGKTNGIFELRYKGNAISRIEPSPMVKIIKEEKE
>NZ_CP046316.1|WP_009391871.1|2037609_2040048_+|DNA-translocase-FtsK
MAKKKQQQTDDKKEDKKDDKKPKKNNAAKVRQRRIAVGLFLIFLAFFLLFTYFSFFFSWQTDQSIWSDLSARDEVAENWMSKIGAYLGHILIYKGFGVACIIAFWLILITGLKVLLNIKMPLLNRWYWGTLQMVYVSTAFGFFSGKATVLAGAAGYELNQWLQDYLGKIGTVLLLILGALLYAVFKWQLTPERVIDFSKGIADKVKQAIPEEEEKPVVSEVTSEVQTEEEEEDEAPEEADNKPLEIIIPQGENTPVDPFTHQREIPPLHPESPLEITNTKEEEPAFTITPTVPPAMVDPEELAQQLVQNYGEYDPRLDLSDYRFPTVELLDEPKDKSIIINEEELKENNDKIIKTLADYKIEISKIKATVGPTVTLYEIVPVAGTRIAQIKRLEDDIALSLAALGIRIIAPIPGKGTIGIEVPNKKPTTVYMRTMITAQKFQNAEMELPIAFGKTISNEPFITDLAKMPHLLMAGATGQGKSVGINVVLTSLLYKKHPAEVKFVLVDPKKVELSIFETIERHYLAKLPDSEDAIITDTKKVVNTLNSLCIEMDNRYELLKNAQVRNIKEYNTKFKARQLNPNEGHRFLPYIVLVVDEFADLIMTAGKEVELPIARIAQLARAIGIHLIIATQRPSVNVITGVIKANFPARIAFKVAQKIDSKTILDGSGAEQLIGRGDMLYSQGNEPVRIQCAFIDTPEVKRITEYIGAQRAYANAYLLPEYVGPDSEPTDLSDFDPSERDSMFREAAEIVVNAQQGSASLLQRKLKLGYNRAGRLIDQLEYAGIVGPFEGSKARQVLVQDIVSLDRLLGGE
>NZ_CP046316.1|WP_009391872.1|2036976_2037474_+|thiol-peroxidase
MANITFHNEPAHTAGDLPKVGTVAPDFSAVKNDLAEVKLSDFKGKKVILNIFPSVDTGVCAASVRKFHVEASKLNNVAILCISKDLPFALTRFCAAEGIDNLVMLSDFRGGFEQHYPIAFTDSPLKGLLSRSVVVVDENGKVVYTEQVAETTEEPNYAKALEAIK
>NZ_CP046316.1|WP_009391874.1|2035257_2036592_-|TolC-family-protein
MKKNFYILSMCLLPLGVWAQSKQWSLTDCINYAVQHNISVKKTELNQQTAEINLSQAKDNRLPTVSGSASANLNNGSAINQISNERVSRRTFSNNFGVSASMPLYQGNKLNLQIDRSQLLLEQNELYVQEAKNNITLSVLEAYLQALYSYEGIAVAKNAARSSAEELKQAQTKFANGSIAKLSLAEIETRNANNEYAIIQAENQYAKRVLTLKQLLELPPNSDFAIALDLQEDDYVAIIPNKDEVFAQAKQALPNLKIYQSQQKIAEKDIKIAKAGALPSVSLQAGVNTGYSNLNSLSYATQLDSNFGQTIGASLNIPIFSQNKNKNNVKLAKLTQQQSVLEEQQAEKDLYAKIETAWQNATTHQAQQAASRTARDNAKLAYDLAVKKHEFGGLTNTELLVSENAYLTAEQTYLQNKYMLALYVQLLKFYMGVLPLAPSQGGGM
>NZ_CP046316.1|WP_009391875.1|2033811_2035041_-|efflux-RND-transporter-periplasmic-adaptor-subunit
MKKKIKKIIIIALLAVVAFVGYQFFMKEKPTPIILQTDEVTQGDVTTEVTATGSVQPVDEVEVGTQVSGLVSKIYVDYNSQVKKGQLLAELDKTNLQENVINATANYNSALNELNYYQQNYDRQKKMYNAQVISQQDYEQALYQLNNAKASVAQRLTTLNQAKTNLGYANIYSPIDGIILSKEVEEGQTVAASMSAPTLFKIAKDIKRMQVEVNVDEADIGQVKVGQRVSFTVDAYPQEEFVGRVTQVRLSPTTSSNVVTYTVIVEAENPDEKLKPGLTATIAIYTNELKGVTIVPAKAINFTPDTDVLLQYYAQKGITAEAPKVQHGRRKNKYVWVVNADGTLAQKAVTIGSNDGINVQIVSGLNVGEKVATSLQGNTPQVAGGDSKSSDSSSPFMPKRPKRNNSKAK
>NZ_CP046316.1|WP_009391876.1|2033064_2033811_-|ABC-transporter-ATP-binding-protein
MKKAIIDIRDMKRNFLMGNEMVHALKGINLTIREGEFVTIMGPSGSGKSTLLNILGCLDRPSSGDYILDGISVKDMSKNDLAHIRNTKIGFIFQSYNLLARTSAIENVELPLMYNPKVSAKERRERAIEALISVGLESRLNHLPSELSGGQQQRVAIARSLVNNPVILLADEATGNLDTKTSYEVMELFQRLNDQGSTIGFVTHEDDIAQFSKRTVVLKDGHIISDKEVTDRLNAKEQLAQLRNTSEE
>NZ_CP046316.1|WP_155846660.1|2032315_2033005_-|SH3-domain-containing-protein
MKQLFILFFLLTTNAFAQGPFGDYAVVKDKDGYVNIRAKENVKSKIVGTLPNNTLVYGFFDKEYNPTNWIEVDKGYVHQSRLKRIFDFRAIEGKVQGNSVIFDDKDVKVTITKQKFDKTKHKITKKDQGSYDQLIIDGKEIYGIEVYGGDDSLPEDHYKSIIVTMKGKNVPIPKSAYDDLYQISYFSSSIYYDEEAEALYIYADNGEAGLAYEVCWQIVKGEYKTRIIR
>NZ_CP046316.1|WP_034540051.1|2031974_2032280_-|KilA-N-domain-containing-protein
MAPTNNKLKVQDVEISLATIDNQDYISLTDMAKGKNDEARAADIIKNWIRNRSTLEFLGTWEILYNPNFKVVEFDHFKKEAGLPTFTISVSNWVENTSEIY
>NZ_CP046316.1|WP_155846659.1|2031190_2031892_-|SH3-domain-containing-protein
MKHLLILFFLLTTNAFAQGPFGDYAVVKDKDGYVNIRAKESVKSKIVGTLPANTLVNVYFLEDEPTPPNWIAVDKGYVHKSRLKMISEFPSIGKGKEQGNSITIAGKGISVTLTKQPFDKTKHKITKKKHKEYSEYIIDGKRVQGLDNDEFLPKDHYKSITVTINGKNVPIPKSAYDDLYEIGIWDTNNFAYYDEEDDILYIIAHNGDGYLAYEVCWQIVKGEYKTRIIGEPF
>NZ_CP046316.1|WP_009390437.1|2042793_2043987_+|aspartate-aminotransferase-family-protein
MNQQQDFLKYQAPTSPYPRLLEVERAEGSYIYTTDGKKYLDFVAGVSACTLGHCHPAVVKAIQEQCATYMHVMVYGEYIQKPAVDFCKLLATQLPPELNTTYLVNSGTEAIEGSVKLAKRVTGRTQLIAAKNAYHGNTQGSMSLMGYEERKRPFRPLLPDVDFIEFNNEADILKITERTAGVVLESIQGGAGFIEPQNDYLIKVKRRCEEVGALLIIDEIQPGFGRTGKLFGFQNYGITPDIIAIGKGMASGMPVGAFVSSYERMQLLANNPKMGHITTFGGNPVIAAASLATLNQLLTTDLMAQTLEKEKLFRKYLQHPLIESVNGKGLMLAVIVKSSEIADFVINYCQDRGLIVYWLLFEGRAVRLSPPLTLSEAEIKEGCDIILEALEVAKTKF
>NZ_CP046316.1|WP_009390438.1|2044101_2045274_+|nicotinate-phosphoribosyltransferase
MSKVLTSLLDNDFYKFTMQCGVVQLFPKTKARYTFINRGKHEFPKGFDKALRAAVDAMADLKLTKDEKAFLVKNCPYLSPLYLDFLEGYRYDPSEVHIAQEGSDLKVTVEGHWYRTILWEVPLLSIISELYYQLMNATAWTDAQVIANTREKELLYKELGVVFAEFGTRRRHSYHVHDIVMRTLLEGYGSTFMGSSNVHFAMKYKVKPIGTHAHEWFMFHAAEYSYKMANALSLEHWVDVYRGDLGVALSDTYTTDVFFKQFDKKFSKLFDGVRHDSGDPIVFAEKTIAHYKKMGIDPLSKYIIFSDGLNPKKVQAITEACKGKIGISFGIGTDLTNDVGLRPMNIVMKLTEVLTSDDEWVPTVKLSDEPNKHTGDPKMIALAKGILGIE
>NZ_CP046316.1|WP_034540060.1|2045444_2045990_+|Smr/MutS-family-protein
MNIGDYIEVLDDTIKGHVVRVTPQEVTMLSTEGFELSFRPDEVVAISEEVPIKSAFATIDEESLRKDVLPKRRQKAPLTKREKSIPPMEVDLHIEQLVDSTRNMTNYDMLTLQLETARRQLEFAIAQRIQRVVFIHGVGEGVLRTELEFLLGRYSNVTFYDAEYAKYGVGATEVYIYQKAK
>NZ_CP046316.1|WP_009390441.1|2045989_2046664_+|ABC-transporter-ATP-binding-protein
MIEATNIHKTYKTLEVLKGVSVEVAKAEIVSIVGASGAGKTTLLHILGTLDSPDANTEASLRINGTDILALSSKNLAKFRNEHIGFIFQFHQLLPEFTALENICIPAFIKGVGKKEAEKRAMELLDFLHLGARAHHKPNALSGGEQQRVSVARALINQPDVVFADEPSGNLDSESAEHLHQLFFQLRKEFNQTFVIVTHNEELAAMADRKLVMVDGKIISKLAD
>NZ_CP046316.1|WP_009390442.1|2046690_2047086_+|hypothetical-protein
MKKILLMTLMVCGLTACTSLPQSANNFINTYFAHTTVQEVERESDTNGYSVKLKDRTEIEFAENGDWLKVEAEDGNSIPTDFFPKKIADYAAERSFIIESISKTNIGYKVEIVGSKSALFFNKAGDPIGNY
>NZ_CP046316.1|WP_009390443.1|2047141_2047588_+|hypothetical-protein
MNTLKKLSTVAFALFAFGVANAQEDGLIPVQSLPTSAQTFINQNFSANNIVSVWQDNEKGRVEDYTVLFADGTEVEFRANGDWKEVKARNGAVPAKIVPAKISKYVHKNYPNVLIKEIQKERRKYEVSLSNGLDLDFNLNGKFLKIDD
>NZ_CP046316.1|WP_009390444.1|2047589_2048024_+|hypothetical-protein
MKKILFAILAAFSLQVATAQDRKVDFNELPADAINFVRQHFLVADINSVWKDVDYKDEEFSVIFKDGLEIEFNGEGDWKEIKVHRGKVPDHVVPEKILAHVNATFPFESIKEISHSISKKTYKVKVTDGQKLKFDDNFNFIEVK
>NZ_CP046316.1|WP_009390445.1|2048112_2049339_+|NAD(P)/FAD-dependent-oxidoreductase
MYDLLIIGGGAAGFFTAINAAEKHPDFSIAILEKSKEVLQKVRISGGGRCNLTNATFTPAELVRNYPRGYKELLSPFHRFMCGDVMEWFESHGVPLKTEDDGRVFPASDSSESIINCFLKAIAQHSIELFTQQNVQAISPAEQGWQVRTANRTFTAKRLVIATGSNPKIWQLLANLGHTIVPPVPSLFTFQTATEWAKTLSGIAVTATVQLFNQKGDFLQISERAPLLFTHKGFSGPAVLRASAWGARVLASLNYQCLMEVNFATTDDQALSYDEVLLQLQDCKQRHGRKAMQSVTLFQLPKRLWEALLESAGVAPAQQWASLNKSQLQQLAKVLTQSRFSIIGKNTFKEEFVTAGGVKLSEIDFKTYQSKLFKHLYLAGEVLDIDAVTGGFNFQNAWTGGYLISEAL
>NZ_CP046316.1|WP_009390446.1|2049436_2051326_+|ABC-F-family-ATP-binding-cassette-domain-containing-protein
MLNVHNLSVSFQGEYLFEEVAFMLNAGDRVGLIGKNGAGKSTMLKLLSRELKPDSGTIAADKDVRIGFLKQDIDFVKGRTILEEAYQAFGEIKTLEQKLDDIHHQIETRTDYESESYHNLLDMLSDYTHRFDLIGGYLYQGETEKVLLGLGFQRSDFDKLTDSFSGGWRMRIELAKLLLQNNDILLLDEPTNHLDIESIIWLEQFLTTYSGAVVIVSHDKMFLDNVTNRTIEISVGKIYDYPKPYSKFLELRQEIREQQLASQKNQEKKIQQTEKLIEKFRAKASKASMAQSLIKKLDKIDRIEVDEEDNAVMNVRFPVSVTPGKVVLEIDDVSKSYGEKEVLSHVSLLVERGSKIAFVGQNGQGKTTLAKMIIGETDYQGTIKLGHNVQLGYFAQNQADYLDGELTVLDTMYHAADDTNRMKIRDILGSFLFRGDEVDKKVKVLSGGERNRLALAKMLLSDFNVLVMDEPTNHLDIKSKNVLKKALQQFEGTLIIVSHDRDFLQGLTDKVYEFKNKNIKEYLGDIDFYLEQRAVANFREMEQQKETLSAPTKATTSAEKLSFEQQKQQKAAQNKLNKIENQIAALEEELKQMDIQMGQGVQSNDYYKEYEQKKRMLEELMTEWENLMS
>NZ_CP046316.1|WP_009390447.1|2051330_2052788_+|lipase
MHPKKILFFIIGVLVALFTMTLFSSYHITDSGTVREGISFGNTMLRYPTPDILGMLFKSKEKENNKLNELIKETNTIVDEKTDKLATNDTIANDSLHKLETNVEGKIYYPGNRIDYIKRLKNKLRQGVCQIVHYGDSQIEGDRITGYVRNRLQLAFNGGGPGFFPIKVVYNQNSIDITTSGNWVRYAFFDRKQRRKVGHDMYGLFATYSRFTNYAKDTTGLSVSKASFTIKPSAKSYARLQHYTKFGLHYGNAIGKVKIKVYENGNIIKTDSLISDGKYHNYKLNFATTPKELKIELEARVSPDFYGVTLDADTGVRMDNVAMRGEAGRIFTRMNYENYRQMSVDRQPDLFIFQYGGNTIPYMKTDQQLREYVEGLIFNMKWVKRANPNAMFMLLGPGDMTTSRNGQRLTYPFLPKLNDLMKEECMKNDVAYFSMYEAMGGENSMISWVKQGMAASDYVHFSPKGTKLISEVFYQCLHNDLASVE

Crispr_ID: NZ_CP046316_5

• CRISPR_ID: NZ_CP046316_5
• CRISPR_location: 2094270-2094374
• CRISPR_type: Orphan
• Repeat_type: NA
• Spacer_info: 1 spacers

Consensus repeat of NZ_CP046316_5

Consensus_repeat	Method
ATCGTCTTTATCAGCGATACCATC	CRISPRCasFinder

spacers of NZ_CP046316_5

>5.1|2094294|57|NZ_CP046316|CRISPRCasFinder
GTTATCAGCATCTGGGCAACCTTTAAGTTCTGGTTTACCAGCTACTTCAGGGCACTC

CRISPR arrays and Neighbor proteins around NZ_CP046316_5

CRISPR arrays

The CRISPR arrays of NZ_CP046316_5

>merge|NZ_CP046316|5|2094270-2094374|CRISPRCasFinder
ATCGTCTTTATCAGCGATACCATCGTTATCAGCATCTGGGCAACCTTTAAGTTCTGGTTTACCAGCTACTTCAGGGCACTCATCGTCTTTATCAGCGATACCGTC

>NZ_CP046316|5|4|2094270-2094374|CRISPRCasFinder
ATCGTCTTTATCAGCGATACCATC	GTTATCAGCATCTGGGCAACCTTTAAGTTCTGGTTTACCAGCTACTTCAGGGCACTC
ATCGTCTTTATCAGCGATACCGTC

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP046316.1|WP_009390533.1|2107470_2108079_+|superoxide-dismutase	unknown	unknown	gnl|CDD|223678
NZ_CP046316.1|WP_009390532.1|2105777_2107304_-|sulfatase-like-hydrolase/transferase	unknown	unknown	gnl|CDD|293750
NZ_CP046316.1|WP_009390529.1|2102277_2103114_-|hypothetical-protein	unknown	unknown	gnl|CDD|372685
NZ_CP046316.1|WP_009390518.1|2095288_2099530_-|alpha-glucan-family-phosphorylase	unknown	unknown	gnl|CDD|340852
NZ_CP046316.1|WP_034539687.1|2089586_2090906_-|hypothetical-protein	unknown	unknown	gnl|CDD|274962
NZ_CP046316.1|WP_009390510.1|2090998_2091406_+|2TM-domain-containing-protein	unknown	unknown	gnl|CDD|379083
NZ_CP046316.1|WP_009390499.1|2085503_2086511_-|nucleotidyl-transferase-AbiEii/AbiGii-toxin-family-protein	unknown	unknown	gnl|CDD|378065
NZ_CP046316.1|WP_009390502.1|2087176_2087650_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP046316.1|WP_009390505.1|2087657_2088602_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP046316.1|WP_009390495.1|2083861_2085436_+|Na+/H+-antiporter	unknown	unknown	gnl|CDD|129911
NZ_CP046316.1|WP_009390531.1|2104331_2105765_-|arylsulfatase	unknown	unknown	gnl|CDD|293764
NZ_CP046316.1|WP_009390513.1|2091893_2093675_-|excinuclease-ABC-subunit-UvrC	unknown	unknown	gnl|CDD|234792
NZ_CP046316.1|WP_009390512.1|2091402_2091897_+|dihydrofolate-reductase	unknown	unknown	gnl|CDD|365932
NZ_CP046316.1|WP_009390534.1|2108145_2110284_-|TonB-dependent-receptor	unknown	unknown	gnl|CDD|238657
NZ_CP046316.1|WP_009390508.1|2088632_2089574_-|DUF541-domain-containing-protein	unknown	unknown	gnl|CDD|377344
NZ_CP046316.1|WP_009390528.1|2101648_2102164_-|RNA-polymerase-sigma-factor	unknown	unknown	gnl|CDD|224511
NZ_CP046316.1|WP_009390520.1|2099756_2100890_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP046316.1|WP_009390527.1|2100924_2101656_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP046316.1|WP_009390530.1|2103241_2104300_-|hypothetical-protein	unknown	unknown	gnl|CDD|372635
NZ_CP046316.1|WP_009390500.1|2086497_2087109_-|hypothetical-protein	unknown	unknown	unknown

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
NZ_CP046316.1|WP_009390532.1|2105777_2107304_-|sulfatase-like-hydrolase/transferase	gnl|CDD|293750	cd16026, GALNS_like, galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS). Lysosomal galactosamine-6-sulfatase removes sulfate groups from a terminal N-acetylgalactosamine-6-sulfate (or galactose-6-sulfate) in mucopolysaccharides such as keratan sulfate and chondroitin-6-sulfate. Defects in GALNS lead to accumulation of substrates, resulting in the development of the lysosomal storage disease mucopolysaccharidosis IV A.	3.46046e-110
NZ_CP046316.1|WP_009390518.1|2095288_2099530_-|alpha-glucan-family-phosphorylase	gnl|CDD|340852	cd04299, GT35_Glycogen_Phosphorylase-like, proteins similar to glycogen phosphorylase. This family is most closely related to the oligosaccharide phosphorylase domain family and other unidentified sequences. Oligosaccharide phosphorylase catalyzes the breakdown of oligosaccharides into glucose-1-phosphate units. They are important allosteric enzymes in carbohydrate metabolism.	0
NZ_CP046316.1|WP_034539687.1|2089586_2090906_-|hypothetical-protein	gnl|CDD|274962	TIGR04074, Methyltransferase_type_12, 3' terminal RNA ribose 2'-O-methyltransferase Hen1. Members of this protein family are bacterial Hen1, a 3' terminal RNA ribose 2'-O-methyltransferase that acts in bacterial RNA repair. All members of the seed alignment belong to a cassette with the RNA repair enzyme polynucleotide kinase-phosphatase (Pnkp). Chemically similar Hen1 in eukaryotes acts instead on small regulatory RNAs. [Transcription, RNA processing, Protein synthesis, tRNA and rRNA base modification].	1.55842e-18
NZ_CP046316.1|WP_009390510.1|2090998_2091406_+|2TM-domain-containing-protein	gnl|CDD|379083	pfam13239, 2TM, 2TM domain. This short region contains two transmembrane alpha helices that are found associated with a wide range of other domains. This domain may be involved in cell lysis or peptidoglycan turnover.	8.24817e-17
NZ_CP046316.1|WP_009390499.1|2085503_2086511_-|nucleotidyl-transferase-AbiEii/AbiGii-toxin-family-protein	gnl|CDD|378065	pfam08843, AbiEii, Nucleotidyl transferase AbiEii toxin, Type IV TA system. This family was recently identified as belonging to the nucleotidyltransferase superfamily. AbiEii is the cognate toxin of the type IV toxin-antitoxin 'innate immunity' bacterial abortive infection (Abi) system that protects bacteria from the spread of a phage infection. The Abi system is activated upon infection with phage to abort the cell thus preventing the spread of phage through viral replication. There are some 20 or more Abis, and they are predominantly plasmid-encoded lactococcal systems. TA, toxin-antitoxin, systems on plasmids function by killing cells that lose the plasmid upon division. AbiE phage resistance systems function as novel Type IV TAs and are widespread in bacteria and archaea. The cognate antitoxin is pfam13338.	3.94236e-26
NZ_CP046316.1|WP_009390495.1|2083861_2085436_+|Na+/H+-antiporter	gnl|CDD|129911	TIGR00831, Putative_Na+/H+_exchanger_Rv2287/MT2345/Mb2309., Na+/H+ antiporter, bacterial form. The Monovalent Cation:Proton Antiporter-1 (CPA1) Family (TC 2.A.36) The CPA1 family is a large family of proteins derived from Gram-positive and Gram-negative bacteria, blue green bacteria, yeast, plants and animals. Transporters from eukaryotes have been functionally characterized, and all of these catalyze Na+:H+ exchange. Their primary physiological functions may be in (1) cytoplasmic pH regulation, extruding the H+ generated during metabolism, and (2) salt tolerance (in plants), due to Na+ uptake into vacuoles. This model is specific for the bacterial members of this family. [Transport and binding proteins, Cations and iron carrying compounds].	2.60441e-87
NZ_CP046316.1|WP_009390531.1|2104331_2105765_-|arylsulfatase	gnl|CDD|293764	cd16145, ARS_like, uncharacterized arylsulfatase subfamily. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.	0
NZ_CP046316.1|WP_009390513.1|2091893_2093675_-|excinuclease-ABC-subunit-UvrC	gnl|CDD|234792	PRK00558, uvrC, excinuclease ABC subunit UvrC.	0
NZ_CP046316.1|WP_009390512.1|2091402_2091897_+|dihydrofolate-reductase	gnl|CDD|365932	pfam00186, DHFR_1, Dihydrofolate reductase.	2.3929e-75
NZ_CP046316.1|WP_009390534.1|2108145_2110284_-|TonB-dependent-receptor	gnl|CDD|238657	cd01347, ligand_gated_channel, TonB dependent/Ligand-Gated channels are created by a monomeric 22 strand (22,24) anti-parallel beta-barrel. Ligands apparently bind to the large extracellular loops. The N-terminal 150-200 residues form a plug from the periplasmic end of barrel. Energy (proton-motive force) and TonB-dependent conformational alteration of channel (parts of plug, and loops 7 and 8) allow passage of ligand. FepA residues 12-18 form the TonB box, which mediates the interaction with the TonB-containing inner membrane complex. TonB preferentially interacts with ligand-bound receptors. Transport thru the channel may resemble passage thru an air lock. In this model, ligand binding leads to closure of the extracellular end of pore, then a TonB-mediated signal facillitates opening of the interior side of pore, deforming the N-terminal plug and allowing passage of the ligand to the periplasm. Such a mechanism would prevent the free diffusion of small molecules thru the pore.	3.21877e-52
NZ_CP046316.1|WP_009390508.1|2088632_2089574_-|DUF541-domain-containing-protein	gnl|CDD|377344	pfam04402, SIMPL, Protein of unknown function (DUF541). Members of this family have so far been found in bacteria and mouse SwissProt or TrEMBL entries. However possible family members have also been identified in translated rat (Genbank:AW144450) and human (Genbank:AI478629) ESTs. A mouse family member has been named SIMPL (signalling molecule that associates with mouse pelle-like kinase). SIMPL appears to facilitate and/or regulate complex formation between IRAK/mPLK (IL-1 receptor-associated kinase) and IKK (inhibitor of kappa-B kinase) containing complexes, and thus regulate NF-kappa-B activity. Separate experiments demonstrate that a mouse family member (named LaXp180) binds the Listeria monocytogenes surface protein ActA, which is a virulence factor that induces actin polymerization. It may also bind stathmin, a protein involved in signal transduction and in the regulation of microtubule dynamics. In bacteria its function is unknown, but it is thought to be located in the periplasm or outer membrane.	2.5494e-09
NZ_CP046316.1|WP_009390528.1|2101648_2102164_-|RNA-polymerase-sigma-factor	gnl|CDD|224511	COG1595, RpoE, DNA-directed RNA polymerase specialized sigma subunit, sigma24 homolog [Transcription].	2.98804e-31
NZ_CP046316.1|WP_009390533.1|2107470_2108079_+|superoxide-dismutase	gnl|CDD|223678	COG0605, SodA, Superoxide dismutase [Inorganic ion transport and metabolism].	2.92038e-108
NZ_CP046316.1|WP_009390530.1|2103241_2104300_-|hypothetical-protein	gnl|CDD|372635	pfam13568, OMP_b-brl_2, Outer membrane protein beta-barrel domain. This domain is found in a wide range of outer membrane proteins. This domain assumes a membrane bound beta-barrel fold.	0.00204026
NZ_CP046316.1|WP_009390529.1|2102277_2103114_-|hypothetical-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.	5.61134e-07

Protein sequences

>NZ_CP046316.1|WP_009390513.1|2091893_2093675_-|excinuclease-ABC-subunit-UvrC
MSIELQLQTLPTSPGIYQFYDDTDILIYVGKAINLKKRVSSYFQKTHDNAKTRVLVKKIVRIEHIVVATESDALLLENNLIKKYQPRYNVLLKDDKSYPWICVKKERFPRVFSTRRIVKDGSLYFGPYTSMKTVHTLLDLIKELFPLRNCTYDLSPQNIANHKFKVCLEYHLKNCKGPCEGLQTEEDYNNNIQQIVEILKGNFKEALTRFKEEMNVLATEMRFEEAHLIKQKITSLENYQAKSTIVSSKISNVDVFSIVSDEEYGYVNFLQVAYGAIVRAHTLEIKKKLEETDRELLEYAIIDIRERFYSTSKEIITPFEVTLSEGLQLTIPKAGEKKQLLELSVRNAKHFRQERFKQEKIVDPERHTNRILTQMQRDLHLSVPPVHIECFDNSNIQGTNPVSACVVFKNAKPSKKDYRHFNVKTVEGPNDFASMEEAVYRRYRRLLDEGQSLPQLIIIDGGKGQLSSALKALEQLELRGKIAIIGIAKRLEEIYFPEDSVPLYLDKRSETLRVIQQLRDEAHRFGITFHRQKRSKSAIVSELDSIEGIGEKTQKLLLQHFKSVKRIQEASLEDLTKVIGHRAKKVYEHFSNG
>NZ_CP046316.1|WP_009390512.1|2091402_2091897_+|dihydrofolate-reductase
MITLIAAAADDNAIGKGSNLLWHLPKDFKHFKNLTTGHCIIMGRKTFETFPKLLPQRTHIVITRQRDYTPEGVIIVGSLQEAIREALLIDPCPYIIGGGEIYAQALPLADAIELTRVHHTFAEADVFFPPIPPTHFTLVSKEHVAADEKHLYPFTFERYIKVDN
>NZ_CP046316.1|WP_009390510.1|2090998_2091406_+|2TM-domain-containing-protein
MSNTQLTPEQYELFKNAETYLKQKRLLYIHFFVFVLGCVFFFVANKILDYGVEYNWYLWLSLIWLFLWLWHAMNVFVFNRFLGKKWQEKQREQLIAAQQKKLIKMEAAVEREFELQKEQAKKELDAADTSNTRTV
>NZ_CP046316.1|WP_034539687.1|2089586_2090906_-|hypothetical-protein
MIIQIHSQNPQLLDVLNKNPETDFGIYAKALRNGQLVGNAVSAHQYDVVFQDTRYSYLPEESNQIDFQSYCSPLVILHCCNEFFKDQLQEKEAYFQQSIKWLGQPRKEVDTMPCTIEVKNLYINSSWYKNGEFLLARYFKNCHITPLIGNNVALKVEGKTIFEAINLLSFIAVITHITNEYGEYTYIDDSFAQKYARILTNIDDVPYFVFYLFIKRAVKSERQLSEIKGAFEAYFSTKGLNIDFQFTDTHGSRMAFVINEFGFETPVLDIGCGELKYYRRFMRKNYNYKQPYFATDIDPEVAAYVQTLREKMEADNLVFLKSLDDFAYTKPVNILLTEVIEHNTPEEAKALVTRCLQIPFHKMIITTPDSRFNVHYFEDPDSALRHSDHHFEWDDTQFRAFISEVTAAFPQYQVRYEGIGDRINGVCPTQAAVIENVKS
>NZ_CP046316.1|WP_009390508.1|2088632_2089574_-|DUF541-domain-containing-protein
MLKSLFLTAAVVCSSFAFSQASGNVNYKDRSRNSWNNDDTTIDFPLNYEMVVTAKGLANVKADAFVAIFSVVQVGKTAEEATQLMNQRLSSALSALKAKNFETFVDMISFVPMYEYETEKKVFSKRTYNELPVGFELKQNLHIKIKEASQLNELIILLSNSEIYDLVRMDYYASNLEAVKKELMTKVKAAFTEKQKLYETTLGESFATAEKKITDGFAQTSPSQQYKSYEAYNSASLQGKRAGNILQANKSTTQYYQPIADKDFDVVLNPIIVEPVIQLIYEMKMSINRTEKNKNKEVMFLTPAGELKKINLP
>NZ_CP046316.1|WP_009390505.1|2087657_2088602_-|hypothetical-protein
MKNSLKLLCLFLLLLCVGCASPKKIIAPEDYCVPPAYTITSDKEAPIEIDAEEFALNKTLFKGKLSDRNILIAYASHIDKPLLALIALDDNPSSEAQQKRNTLQLEIHSKITAIFSQMNAVTAELDCEEERIDQIATTISNLNDKNISRLTVASILIGAAVSVAGAYIADDGWDKGIAAGGGVIGAGLSFLTLNPKGKKVMLKHPRNLLRCFMTEKNNGEFPPFVWYMINEHRFTNSGEGSILQHMQQRWVKNLFDNDKEKALKAVLFSDGGIYYAGDLHTRAEMFDQMQSVIHSLHQNIDFFIQEVNILMLKK
>NZ_CP046316.1|WP_009390502.1|2087176_2087650_-|hypothetical-protein
MRKLFLLLLIGATLPAVAQTSKELLFVIDASYLKQGSTYGQLGLHFNCYDSYNIALSAGIAGNFRSENKQLIAIPEAQLSAWIRADNERGGFVDIPVLLLRPQLNFSPYYFAPEAGIQILILYVKAGYAFPWGKTNDNYPFQTGKFRFSVGISIPIK
>NZ_CP046316.1|WP_009390500.1|2086497_2087109_-|hypothetical-protein
MESTDDKILRKLSKCGRGNIFFPTDFVSLAEMKTILKSLERLTHIGKLIRIARGIYYYPKYDKTLGLGLLYPSYEQIAQSIAKRDKTRIAPAGAYAMNILGLTTQVPMNIVFMTDGTARKIQLFDGRQLSFKHTTPKNLSFQNKTAQLIVFALKEIGTPHITQEHIEALKKVLLNIPESKISVDYKLMPSWIRTLIKQLYELL
>NZ_CP046316.1|WP_009390499.1|2085503_2086511_-|nucleotidyl-transferase-AbiEii/AbiGii-toxin-family-protein
MNYFNLTPEQQKTVITQTAARVGLPMQAVEKDLWVTTLLQLLFTLPFASQLLFKGGTSLSKSYGLIHRFSEDIDLVIDRNYFGYKGDLTKKQIKQLRKQSSLFVEKDFTIALKQAIENFGLQKYCTIVAQPNGEGDSTYPEPRKIEVFYQSLFANIGYLQPKVVLEVGTRSLFEPTEPTQVKSLITSTFQQIETDIVSVIITTASPAKTFLEKAFLLHELFTTHKGDKAERKSRHLYDLEKMMDELFAIEAISNNELWETITHHRKLFTSVLGVDYTPDIRKRIQLIPPSNVVAIWEKDYREMQDSMIYGNSLPFNTLLERIHILQNRFHNIANL
>NZ_CP046316.1|WP_009390495.1|2083861_2085436_+|Na+/H+-antiporter
MVQYFPYLLLLMVAIMLLIMFANRLKVAYPILLVLGGLAISFIPNVPTITLNPDLVLIIFLPPLLYADVFSLSLKEMWKWRRIIFSFAFIVVFITAAAVAWVANMVFPGFSLALGFLLGGVIGSTDAVSASTIMKFVKVPKRISTIIESESLLNDASSLIVFRFAALVVTTGQLVWTDIALNFLWVVIGGTLIGLAVAWVMRKLNKFFPTDANMDIILTFIAPYIMYIVANEMGVSGVLAVVAGGMYMSFHITSILAASTYNKAVAVWDILGFVLNGLAFMLIGLALPDVLESIEAEGMSLATATNYGLLITGVVVGVRLLSSYGALLITQVMKHFITVADRRNLGFRLPLVLGWAGMRGVLSLAVALSIPLTLENGEPFPHRSLILYITFIVILATLLAQGLSLPALIRWAKFPDYEDHIPEAEAESLIRKSLAQAALDYMQKHYKEGINDSLLLQNQKDIWQYQLDLSKSNTTPEERKKYIAILHHQREILHQLNKNPRIDEEQIRNFHRQLNLEEEKWEVN
>NZ_CP046316.1|WP_009390518.1|2095288_2099530_-|alpha-glucan-family-phosphorylase
MSITKKLNPDYVFETSWEVCNKVGGIHTVIATKAASIVKQFRSKYILIGPDIWQHNENKEFVENPELFKSWRAKAASEGLRVRVGNWKIEGNPIVILVDFSHYVSSKNDVLRFYWDTYHLDSFNSPWDYVESVLFGYAVGKVIESFTKFNTASRENVICHFHEWMTGSGLLYIEERMPKIGSVFTTHATVVGRAIAGNGLPLYNTMKDYNPEEMAYKFGVQHKHFLEKETAKVADCFTTVSEITAQEALHFLARQTDIITPNGFEDKIIPAEKTFAKKRSDARKTLINVAQALTNQPISEDTKIVAISGRYEFRNKGIDAFIDALGALNRNAKNKKELVAYILIPTAHDAPNQGLLNNLKNPKQSADNEQKHLTHILPDVYHDVIMKRIYEQELFNRKEDKVKVIFCPSYLNGNDGVFNLSYYDLLIGLDGTAFPSYYEPWGYTPLESLAFKVPTITTTLAGFGKWVNDFYPEKQKAIEVVTRTDSNYGDVVASIVKNFVTLLDSKEEDLKARRDTAAKVSEIALWKNLVKYYIKCYELTLEHIEDRVEKLPPVETEGVAYLEKSKVVTPPNWRSVIIHRAIPEALQPLEELSKNLWWCWNDEAYEVFKYVDKEKWIEVRKNPIALLDSISLKRYKELEQDNVFMRNLSKVYADFQAYMAKKAEMISPSVSYFSMEYGLHSSLKIYSGGLGILAGDYLKEASDKATKITGVGLLYRYGYFTQKLSSAGNQEADYEAQDFSKIPVSPVTDETGKWVIVSIDLPGRTLYARVWRVDVGRIELYLLDTDFENNREDDRSITHHLYGGDWENRLKQEMLLGLGGIKMLRKLGIDSDIYHCNEGHAAFIGLERLSEYIQNDNLAFSEALEVVRASSLFTTHTPVPAGHDAFEEGLLHAYLAKYADKLHVNWEQILALGKIRLEDPYEKFSMSNLAANLSQEVNGVSWLHGEVSKDILKDLWPGYMPEELHISYVTNGVHQPTWTAGLWKEVENEVFGKDYKTHHYDPKSFEGIYKVSDQRVWEIKTALRSKLLRRVEQKLRLEKNTPYFSPRQLVEIKENLREDILTIGFARRFATYKRAHLLFTNIERLDRIVNNPDRPVQFIFAGKAHPADKAGQDLIKNIVEISKLPQFLGKIIFIPNYDMELARHMVQGVDVWMNTPTRPLEASGTSGEKAAMNGTMHFSVLDGWWVEGYREDAGWALPMERAYENQQYQDEMDAEMIYNIIEDEIAPIFYDKNKDGISSRWCALIKNTIAKVAVNFTTTRMLTDYENQYYFPMTERVTKLKDNRFNLAIQLSDWKRRVTQEWDNIKVVDFKVPNRNEQIISIGKTYKGEITLDVSELDPKDVGVEVVVAEQKDEKIKVLSTSEFNLVSHEGSRATYQIEIASEYPGALHLAIRIFPKNEHLPHRQDFALVKWL
>NZ_CP046316.1|WP_009390520.1|2099756_2100890_-|hypothetical-protein
MKPLQLLCMFLIVAFGGITAQDFKDKIAQTKRSIDSIVTAEKAQLKERLRTIEYRLDRKEITEIESRDLKREASKEAAEAIRIKTREQSEKLSALLHQRIAEKHLSDSITYKKEMQKVIDSVDIESRPTKTERTEVYVDRNYVHIGHNGIYIGQVPYREEDYYESDYKRTQGGGYFALAFHNLNSSEHFSNNHFRLWGSKSVEIGYIRNTRLLKNNNLLHLNYGLSWMMDKLKMKEDEHFVKNGNITEIVPYPKETIKSKFKTMYLILPISLEFDFTEPVQYKGKTYYPAQMGFHAGVGAYVGALLATKQKVKYTENGSTHKDMNRKYYNVNEWTYGVSANIGYGWFSFYARYSLVPLFTNNPINEYPFSVGIRLGH
>NZ_CP046316.1|WP_009390527.1|2100924_2101656_-|hypothetical-protein
MNNKKIEIMWKNKIKNLFQTREIPPERDLWAALEAQLDQREAKAVRPKAYFRIWHYAVAASVLLAVAVGVFYERISLPTAQEVRTTTVATEDKTPNTPLDTTPNVVAPAPAVVLPPTVADKVANTTIVPQKKSDKALDEEVEALLADVSTEALLAEVMQQVEKEQHLFKTREEQRALQRLKNLSPQELLLMATTEEMLDNYVAANYPTDKLLSEVERDLMKEKVQRFLNKIVAQWNEMRYALQ
>NZ_CP046316.1|WP_009390528.1|2101648_2102164_-|RNA-polymerase-sigma-factor
MHLLIQKAKQQDRLAQKQLYDQYAASLLSVCRLYISDAHFAEDVLLRAFFKILTHIDSYQEQEHFYAWMRHITVNECIDFLRSKTQKVALADWNDTYDSIDDTDLDSYAFEESQIQQFIDQLPAASRAVFNLYVFEDYSHKQIAAELGISEGTSKSQLAYAKKRLKQMVNE
>NZ_CP046316.1|WP_009390529.1|2102277_2103114_-|hypothetical-protein
MKHIFLIFFITVVLPIGAQQRVVSEHHTPIEYVNIGVVGTNKGIISDENGNFSLDKLRAAPTDSIYFSHISYKHKVVAYKDIKQQVVLKEANIQLPTTTLKVKKPRIRNIKDKGTSMPIDLYGGMNTYFSPYGSKGINSELGDFITLKKDAQLTEFNLEVSKSSFYLVTVRVVVYQYKKEKDKHIFTPLLEKPIYIEIYPSEKKQTFTEKLSVFAPKGDIWVGYQFVEVRGKDDAAIYFNATTDKCYIRFADNKIQQVNLGAGMPFTVKGYDYEVISK
>NZ_CP046316.1|WP_009390530.1|2103241_2104300_-|hypothetical-protein
MKKVILLIALLWGGALCAQNPFEKEILQSKYAIDSIVMSERALFRTKHNVIDSLLKEKKIDKTVYNKLYKELSTTRERNIKLKTYAEGQRLAELIRQKAPTINIDSIAAIPTDTFATKHLSQEMLQKMSTLDTIANKPKTEKASEDDKDSAKINVYGAMGFYIPSDNKPYSFLGSRTIEFGIYNTMYLQKNNEHLRLRFGLSWVHHKLRMKDNQYYVLNEGKPTLTPFPSETSKLLLRTQYLMLPLDLYWDSEPKTANKKGFHFSKERFFRGSIGLYAGYLLDSNQKVLYKANDIRYRSVMRTDLNINPWIYGLSASVGYNKIYSFYFRYQLSPLFKSGNDGAFTVGIQILK
>NZ_CP046316.1|WP_009390531.1|2104331_2105765_-|arylsulfatase
MKRIITALALLLAVPLMAQTKHPNVIFVLADDLGYGDIEPYGQQIIKTPHLSQLANEGMKFTQFYTGTAVCAPSRASFMTGQTTGETHIRGNREVREPIDGQAPILAGAPSIAQLFKQAGYRTGCFGKWGLGTPDSEGNPLKQGFDTFFGYNSQFRAHRRYPAYLWHDNEKVMIPENGNYERQEVYAEDLIQEKILDYIGKQNAQKPFFMWLTYTLPHAELVVPNDSIYQQYQHLPKRPYKGQDYSGITDKPFGWAGYMSQPDTYGTYAAMVSRLDWYVGQIRKALKAKGLEDDTIIIFASDNGAHREGGADPKFFNSSAGLRGIKRDLYEGGIRTPYIVYWKGKVKAGSVSDHVGAFWDMMPTFAEITGQKLATTPHQVSFLPTLLGKKQKAHKYLYWEFHEEGGKQAVRYKHWKGVRLQASKNPDAPIELYDLRTDPAEQHNLAEQYPKIVKKMKKIMSEAHTRSDLFPFQWERK
>NZ_CP046316.1|WP_009390532.1|2105777_2107304_-|sulfatase-like-hydrolase/transferase
MKKYVLTFLCPLWLFAQTPKPAATAEKPNVIIVIADDLGYGDLSCYGEKTIHTPAVDALAKQGLRFTNAHTTAATCTPSRYSLLTGLYNWRRNDTGIADGDAAMVIRPEQTTIADLFKTAGYTTGAIGKWHLGLGAEKGGQDWNGFITPGASDIGFDYSYLMAATADRVPCVWIENQRVANYDPSAPISVSYRAPFEGEPTGKNNPELLTKLKPSPNHGHNQAIVNGISRIGYMKGGGKALWTDEFIADTIVAKTVQYINKHKKEPFFLYVGTNDVHVPRYPNRRFAGKSGMGYRGDVILQFDWTIGEIVKALKDNKIFDNTLLIVCSDNGPVIDDGYQDQAEALLGKHRPWGKFHNHGGKYSNYEAGTRVPFIVSYPKKVKRGVSDAAFSQIDLFASLAAFIGKPVPAGAATDSADYLNTLLGKDKKGRLYIVASGGSLSITVGRWKYVAPNNYNAYHPLTRTDLGNYPEERLYDLQEDPMELANVAKDYPDVVATLKALLDKEKNK
>NZ_CP046316.1|WP_009390533.1|2107470_2108079_+|superoxide-dismutase
MAFTLPKLPYAYQALEPYIDARTMEIHHTKHHNAYTTNLNAALAPAGVEGKSIEEILQNLDMNNAALRNNAGGYYNHNLFWEVMSSNGGGKPTGELAKAIDEAFGSFEGFKEAFSKAAATRFGSGWAWLCVHKGGKVEVCSTPNQDNPLMPGTGCSGQPILGLDVWEHAYYLHYQNRRPDYIEAFFNVINWEKVAALYAAGK
>NZ_CP046316.1|WP_009390534.1|2108145_2110284_-|TonB-dependent-receptor
MKRFILPVMVLYAAISMAQNEYPTSEKDTISLDEIVITANRIKEKKTDAVANVTVIDKKKLQQFIKIAPDMSHLIGMVEPAMSLSSNTTNNRYQNLRGRALLVLIDGIPQSTPLRATDRDIRSIDPAAVERIEIIKGATSIYGNGAIGGIMNIVTKKTPENTTFGGQTSVGASARDSFKENRGFGYRFNQQFYGNYKGFSYLLDGALNQTGSAIDGTGEYISPRYGLGDVRTYNGLLKLGYQFDKDNKVEAMYNFYQSLQHTPLVASGGKYLQRPRIGVYGAKDPAAEDEGMRYNHNAYVKFNSNNIFKHTDLELSAFTQHQYTVFDFRKHNPSAPARWEETSGQATVKGAKYGIRTQLISKVLFSNDIFTQLLYGADMLIDKTSQPLVDGRYWLPELTSYNSAPFLQTKTTFYRYYVLKAGVRYDYIDVSVPNYEVLRGRRTDPRVYVKGGDLTYNNLSPNIGLAYNQYKYFQPFISYSQGFSIFDLGRTLRAAKANVLSKINTEPVKTDNYEVGAYAELTKYVHLSGSYFYTYSKLGSDLKEEGGFWVVDRSPQKVYGFEVNADIYPTKWLTLGGSFISFEGKKKTTEDGDWDGYMSGISIPAPKASAYVRVTPTESSYLQVNYLHTGSRDRFAPNNRGVYTEGEGIVFPIDLFSFSAGYTFNKHFSLGLGVENLADKVYYTPASMLVARDAEYARGNGRYFNLNLTYRY

Crispr_ID: NZ_CP046316_6

• CRISPR_ID: NZ_CP046316_6
• CRISPR_location: 2436148-2436296
• CRISPR_type: Orphan
• Repeat_type: NA
• Spacer_info: 2 spacers

Consensus repeat of NZ_CP046316_6

Consensus_repeat	Method
CAGCCTTCTCACTCCTCCCACCAGTCCCAC	CRISPRCasFinder

spacers of NZ_CP046316_6

>6.1|2436178|24|NZ_CP046316|CRISPRCasFinder
TCGTCTCACCACTCCCAGCCCTCT
>6.2|2436232|35|NZ_CP046316|CRISPRCasFinder
CAGTCCCACATCTTTGCCCGTGCGGCTCGCACTCC

CRISPR arrays and Neighbor proteins around NZ_CP046316_6

CRISPR arrays

The CRISPR arrays of NZ_CP046316_6

>merge|NZ_CP046316|6|2436148-2436296|CRISPRCasFinder
CACCAGTCCCACTCGTCCCACCTGTCCCACTCGTCTCACCACTCCCAGCCCTCTCAGCCCTCACAGCCTTCTCACTCCTCCCACCAGTCCCACATCTTTGCCCGTGCGGCTCGCACTCCCAGCCTTCCCAACCCTCTCAGCCTTCTCAT

>NZ_CP046316|6|5|2436148-2436296|CRISPRCasFinder
CACCAGTCCCACTCGTCCCACCTGTCCCAC	TCGTCTCACCACTCCCAGCCCTCT
CAGCCCTCACAGCCTTCTCACTCCTCCCAC	CAGTCCCACATCTTTGCCCGTGCGGCTCGCACTCC
CAGCCTTCCCAACCCTCTCAGCCTTCTCAT

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP046316.1|WP_009390247.1|2442743_2443106_+|dihydroneopterin-aldolase	unknown	unknown	gnl|CDD|376737
NZ_CP046316.1|WP_034540167.1|2438943_2440059_+|peptide-methionine-(R)-S-oxide-reductase-MsrB	unknown	unknown	gnl|CDD|184456
NZ_CP046316.1|WP_009390250.1|2440662_2441415_+|hypothetical-protein	unknown	unknown	unknown
NZ_CP046316.1|WP_009390274.1|2425845_2427243_-|peptide-MFS-transporter	unknown	unknown	gnl|CDD|340904
NZ_CP046316.1|WP_009390258.1|2437980_2438715_-|3-oxoacyl-ACP-reductase-FabG	unknown	unknown	gnl|CDD|187594
NZ_CP046316.1|WP_009390272.1|2429581_2430310_-|YggS-family-pyridoxal-phosphate-dependent-enzyme	unknown	unknown	gnl|CDD|143483
NZ_CP046316.1|WP_009390267.1|2433921_2434974_-|bifunctional-diaminohydroxyphosphoribosylaminopyrimidine-deaminase/5-amino-6-(5-phosphoribosylamino)uracil-reductase-RibD	unknown	unknown	gnl|CDD|273015
NZ_CP046316.1|WP_009390262.1|2436491_2436887_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP046316.1|WP_009390248.1|2441789_2442743_+|type-IX-secretion-system-membrane-protein-PorP/SprF	unknown	unknown	gnl|CDD|371704
NZ_CP046316.1|WP_009390260.1|2437048_2437420_-|DUF559-domain-containing-protein	unknown	unknown	gnl|CDD|225408
NZ_CP046316.1|WP_009390275.1|2425450_2425786_+|MerR-family-transcriptional-regulator	unknown	unknown	gnl|CDD|133393
NZ_CP046316.1|WP_009390270.1|2430891_2431662_-|threonine/serine-exporter-family-protein	unknown	unknown	gnl|CDD|377697
NZ_CP046316.1|WP_009390266.1|2434981_2435941_-|ribonucleotide-diphosphate-reductase-subunit-beta	unknown	unknown	gnl|CDD|365989
NZ_CP046316.1|WP_009390268.1|2431760_2433896_-|glycoside-hydrolase-family-92-protein	unknown	unknown	gnl|CDD|377950
NZ_CP046316.1|WP_009390254.1|2440119_2440362_+|hypothetical-protein	unknown	unknown	unknown
NZ_CP046316.1|WP_009390245.1|2443262_2443643_+|hypothetical-protein	unknown	unknown	unknown
NZ_CP046316.1|WP_009390276.1|2424469_2425444_+|M23-family-metallopeptidase	unknown	unknown	gnl|CDD|366703
NZ_CP046316.1|WP_009390271.1|2430323_2430905_-|threonine/serine-exporter	unknown	unknown	gnl|CDD|378960
NZ_CP046316.1|WP_009390273.1|2427273_2429430_-|S9-family-peptidase	unknown	unknown	gnl|CDD|366374
NZ_CP046316.1|WP_009390251.1|2440358_2440661_+|plasmid-stabilization-protein-ParE	unknown	unknown	unknown

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
NZ_CP046316.1|WP_009390247.1|2442743_2443106_+|dihydroneopterin-aldolase	gnl|CDD|376737	pfam02152, FolB, Dihydroneopterin aldolase. This enzyme EC:4.1.2.25 catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin in the biosynthetic pathway of tetrahydrofolate.	1.32806e-36
NZ_CP046316.1|WP_034540167.1|2438943_2440059_+|peptide-methionine-(R)-S-oxide-reductase-MsrB	gnl|CDD|184456	PRK14018, PRK14018, bifunctional peptide-methionine (S)-S-oxide reductase MsrA/peptide-methionine (R)-S-oxide reductase MsrB.	1.15639e-152
NZ_CP046316.1|WP_009390274.1|2425845_2427243_-|peptide-MFS-transporter	gnl|CDD|340904	cd17346, MFS_DtpA_like, Dipeptide and tripeptide permease A (DtpA)-like subfamily of the Major Facilitator Superfamily of transporters. The DtpA-like subfamily includes four Escherichia coli proteins: dipeptide and tripeptide permeases A (DtpA, TppB or YdgR), B (DtpB or YhiP), C (DtpC or YjdL), and D (DtpD or YbgH). They are proton-dependent permeases that transport di- and tripeptides. DtpA and DtpB display a preference for di- and tripeptides composed of L-amino acids. DtpC shows higher specificity for dipeptides compared to tripeptides, and prefers dipeptides containing a C-terminal lysine residue. The DtpA-like subfamily belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	1.04572e-138
NZ_CP046316.1|WP_009390258.1|2437980_2438715_-|3-oxoacyl-ACP-reductase-FabG	gnl|CDD|187594	cd05333, BKR_SDR_c, beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs. This subgroup includes the Escherichai coli K12 BKR, FabG. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.	1.99264e-101
NZ_CP046316.1|WP_009390272.1|2429581_2430310_-|YggS-family-pyridoxal-phosphate-dependent-enzyme	gnl|CDD|143483	cd00635, PLPDE_III_YBL036c_like, Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, YBL036c-like proteins. This family contains mostly uncharacterized proteins, widely distributed among eukaryotes, bacteria and archaea, that bear similarity to the yeast hypothetical protein YBL036c, which is homologous to a Pseudomonas aeruginosa gene that is co-transcribed with a known proline biosynthetic gene. YBL036c is a single domain monomeric protein with a typical TIM barrel fold. It binds the PLP cofactor and has been shown to exhibit amino acid racemase activity. The YBL036c structure is similar to the N-terminal domain of the fold type III PLP-dependent enzymes, bacterial alanine racemase and eukaryotic ornithine decarboxylase, which are two-domain dimeric proteins. The lack of a second domain in YBL036c may explain limited D- to L-alanine racemase or non-specific racemase activity.	3.4819e-110
NZ_CP046316.1|WP_009390267.1|2433921_2434974_-|bifunctional-diaminohydroxyphosphoribosylaminopyrimidine-deaminase/5-amino-6-(5-phosphoribosylamino)uracil-reductase-RibD	gnl|CDD|273015	TIGR00326, eubact_ribD, riboflavin biosynthesis protein RibD. This model describes the ribD protein as found in Escherichia coli. The N-terminal domain includes the conserved zinc-binding site region captured in the model dCMP_cyt_deam and shared by proteins such as cytosine deaminase, mammalian apolipoprotein B mRNA editing protein, blasticidin-S deaminase, and Bacillus subtilis competence protein comEB. The C-terminal domain is homologous to the full length of yeast HTP reductase, a protein required for riboflavin biosynthesis. A number of archaeal proteins believed related to riboflavin biosynthesis contain only this C-terminal domain and are not found as full-length matches to this model. [Biosynthesis of cofactors, prosthetic groups, and carriers, Riboflavin, FMN, and FAD].	1.8705e-89
NZ_CP046316.1|WP_009390270.1|2430891_2431662_-|threonine/serine-exporter-family-protein	gnl|CDD|377697	pfam06738, ThrE, Putative threonine/serine exporter. ThrE is a family of bacterial and Archaeal proteins that catalyze the export of L-threonine from the cell. UniProtKB:Q79VD1 has been characterized as being necessary for this export. The domain exhibits 10 putative TMs and catalyzes the proton-motive-force-dependent efflux of threonine and serine.	6.262e-44
NZ_CP046316.1|WP_009390248.1|2441789_2442743_+|type-IX-secretion-system-membrane-protein-PorP/SprF	gnl|CDD|371704	pfam11751, PorP_SprF, Type IX secretion system membrane protein PorP/SprF. This entry describes a protein family unique to, and greatly expanded in, the Bacteriodetes. Species in this lineage include several, such as Cytophaga hutchinsonii and Cytophaga johnsonae (Flavobacterium johnsoniae), that exhibit a poorly understood rapid gliding phenotype. Several members of this protein family are found in operons with other genes whose loss leads to a loss of the rapid gliding phenotype.	4.95335e-61
NZ_CP046316.1|WP_009390260.1|2437048_2437420_-|DUF559-domain-containing-protein	gnl|CDD|225408	COG2852, COG2852, Very-short-patch-repair endonuclease [Replication, recombination, and repair].	2.96789e-32
NZ_CP046316.1|WP_009390275.1|2425450_2425786_+|MerR-family-transcriptional-regulator	gnl|CDD|133393	cd04765, HTH_MlrA-like_sg2, Helix-Turn-Helix DNA binding domain of putative MlrA-like transcription regulators. Putative helix-turn-helix (HTH) MlrA-like transcription regulators (subgroup 2), N-terminal domain. The MlrA protein, also known as YehV, has been shown to control cell-cell aggregation by co-regulating the expression of curli and extracellular matrix production in Escherichia coli and Salmonella typhimurium. These proteins belong to the MerR superfamily of transcription regulators that promote expression of several stress regulon genes by reconfiguring the spacer between the -35 and -10 promoter elements. Their conserved N-terminal domains contain predicted HTH motifs that mediate DNA binding, while the dissimilar C-terminal domains bind specific coactivator molecules.	2.029e-34
NZ_CP046316.1|WP_009390266.1|2434981_2435941_-|ribonucleotide-diphosphate-reductase-subunit-beta	gnl|CDD|365989	pfam00268, Ribonuc_red_sm, Ribonucleotide reductase, small chain.	1.13184e-57
NZ_CP046316.1|WP_009390268.1|2431760_2433896_-|glycoside-hydrolase-family-92-protein	gnl|CDD|377950	pfam07971, Glyco_hydro_92, Glycosyl hydrolase family 92. Members of this family are alpha-1,2-mannosidases, enzymes which remove alpha-1,2-linked mannose residues from Man(9)(GlcNAc)(2) by hydrolysis. They are critical for the maturation of N-linked oligosaccharides and ER-associated degradation.	0
NZ_CP046316.1|WP_009390276.1|2424469_2425444_+|M23-family-metallopeptidase	gnl|CDD|366703	pfam01551, Peptidase_M23, Peptidase family M23. Members of this family are zinc metallopeptidases with a range of specificities. The peptidase family M23 is included in this family, these are Gly-Gly endopeptidases. Peptidase family M23 are also endopeptidases. This family also includes some bacterial lipoproteins for which no proteolytic activity has been demonstrated. This family also includes leukocyte cell-derived chemotaxin 2 (LECT2) proteins. LECT2 is a liver-specific protein which is thought to be linked to hepatocyte growth although the exact function of this protein is unknown.	1.4238e-49
NZ_CP046316.1|WP_009390271.1|2430323_2430905_-|threonine/serine-exporter	gnl|CDD|378960	pfam12821, ThrE_2, Threonine/Serine exporter, ThrE. ThrE_2 is a family of membrane proteins involved in the export of threonine and serine. L-threonine, L-serine are both substrates for the exporter. The exporter exhibits nine-ten predicted transmembrane-spanning helices with long charged C and N termini and an amphipathic helix present within the N-terminus. L-Threonine can be made by the amino acid-producing bacterium Corynebacterium glutamicum, but the potential for amino acid formation can be considerably improved by reducing its intracellular degradation into glycine and increasing its export by this exporter. Members of the family are found in Bacteria, Archaea, and the fungal kingdoms, and the family can exist either as a single long polypeptide chain or as two short polypeptides. All family members show an extended hydrophilic N-terminal domain with weak sequence similarity to portions of hydrolases (proteases, peptidases, and glycosidases); this suggests that since this region is cytoplasmic to the membrane it may be generating the transport substrate, so may imply that threonine may not be the primary substrate and the ThrE has a subsidiary function.	5.91391e-26
NZ_CP046316.1|WP_009390273.1|2427273_2429430_-|S9-family-peptidase	gnl|CDD|366374	pfam00930, DPPIV_N, Dipeptidyl peptidase IV (DPP IV) N-terminal region. This family is an alignment of the region to the N-terminal side of the active site. The Prosite motif does not correspond to this Pfam entry.	1.17342e-106

Protein sequences

>NZ_CP046316.1|WP_009390266.1|2434981_2435941_-|ribonucleotide-diphosphate-reductase-subunit-beta
MGIFDKRESYKPFEYPEVMEFVNAMHKSFWVHSEVEFTADVQDFKSNLSAVEQEAIKRALLGIAQVEVSVKTFWGDLYDLFPKPEFNGLGATFAECEFRHSEAYARLLEVLGYNNEFENLLEVPVFKERNTVLKEYLAKNRENAMERILFFTLIIENASLFSQFATVLSFARFKGYLKNVANIIAWTSVDEQLHANAGIYILKKIFEERPEMKAKAEADATDFIRNYIVLEDKMLDWIFEQGELDFFGKKDLANYMRYRLDDSLTQLGLTKPFNISADEAKPMMWFEEEVFSNELDDFFAKRPTAYTKHDKSISENDLF
>NZ_CP046316.1|WP_009390267.1|2433921_2434974_-|bifunctional-diaminohydroxyphosphoribosylaminopyrimidine-deaminase/5-amino-6-(5-phosphoribosylamino)uracil-reductase-RibD
MTDQQYIHRCIQLAQNGLGTTYPNPVVGSVIVYNDRVIGEGWHVRAGEAHAEVRAIASVKDKQLLSESTLYVSLEPCSHYGKTPPCADLIIAHRIPRVVIGCTDPFAKVAGRGIQKLREAGCEVVVGVCQEECEALNKRFFTFHQKKRPYIFLKWAETRDGLIAPLHKQEIAPQWITGAYARQYVHLLRSTEAAILVGAGTVWADNPSLSTRSWYGKSPLRVIIDPRLSTRKDFNVWNDEVPTLFIADRDYKGVRHFGQRTEVACIDFGGEVLPQLCKVLYEREVQSLIVEGGAHTLQQFIKADLWDEALVFRGDTVFTNGLKAPQLSHACLHSVASFPPDFLMTMINDK
>NZ_CP046316.1|WP_009390268.1|2431760_2433896_-|glycoside-hydrolase-family-92-protein
MQKLKLQTSKIIIVAFLALVACQTPQADKQVQHTDEQLTRYVNPFIGTDGMGNTYPGATTPFGMVQLSPDIGIPGWDRIPGYFYADSLITGFSHTHLSGTGAGDLYDILVMPTNSRFNERIKENNGKPFSYFSHQSEKATAGYYAVDLSSYGIRAELTATPRVGVQRYTFPKDDTSKITVDLGYSINWDKPTETYMKVVDDSTLEGYRYSTGWARDQKVYFVMKFSKPFAKSSLLSEKIDGKSQIGRAELLYATAEGEQIVVKTALSMHSLSGAYKNMQEEAPHFAFDTYREAARALWEKQLQKITVTSDDEQQKTIFYTMLYQTMLAPNLYSDVKEPVRYDTFSLWDTFRAAHPLYTLLQPEANADFISSFLAHYKENGTLPVWSMQGGETNMMIGYHAVPVIVDAYFKNIPMDVKLAYEACRASAMVDEREIDLYRQYGYIPYDLDKSGENWSVSKTLEYAYDDWCIAKFAAALGKGTDADYFARRAENWRNLFDPRTTFFRPRNSKGAFINPFNPKDYTPYFCESNAWQYRWFVPHNVSGLIEAMGGKEAFEQKLDSMFTFASTPDERLPIFSTGMIGQYVHGNEPSHHVAYLYNFTAHPEKASERVGEILRTQYHNTPDGHCGNEDCGQMSSWYVLSALGFYPINPADSPYYIGQPLFSKATLHLDNGKTFSIRKGSTNGQLQLNGKPLGRRYLHFKEITDGGELVY
>NZ_CP046316.1|WP_009390270.1|2430891_2431662_-|threonine/serine-exporter-family-protein
MKAIERAAKLFADINELLISSGANTRRVERNVERISNALNYHCESFYSHSAIVLTVQDKATGEKETVVRTIPHHGVNFSAISDISILSWEVLEKHLPIEQIEKHVATIKAKPHYNMYVMWFFVSIAGGSLAYVFGKENASYAEFGMSFLATFLGLAGRRILQLRKFNVYICWGWAAFVSVSVMSIFRLLGVEHYHNALAACVLWLVPGVPLINGFIDMLSGCVVPGVAKLTHAAILVFMISLGFYLALLLFGYELP
>NZ_CP046316.1|WP_009390271.1|2430323_2430905_-|threonine/serine-exporter
MSFLDVLLALSVRIFWSMWISIGFALLFNTPRRALWITGLLGGVGWGIKFVLLGTIMPEQIVITSFLGACAVGLLAVYFAHRVHTPPIVFTIPAVINMIPGKYGYEFMMKIIQIVTVETPQEETLDLLYQTFKLGLQTGFITMCLAFGVITPMLLFNTYSVKGKDLNDFIKRRLSRRKTKAELEGIIEENEPV
>NZ_CP046316.1|WP_009390272.1|2429581_2430310_-|YggS-family-pyridoxal-phosphate-dependent-enzyme
MENILQNIEIIKQRIAAACTRVGRKPEEVKLLLATKTVTPERIKIALKAGNTLIAENKIQELKEKYEALKDVPHTNHFIGHLQTNKIKEILRYEVSCVESVDRIDLAQKLHNRLASEGKELDIFIQVNTSNEESKFGADPAEVLDLVKQVAQLPTLHIKGLMTIGLFSAETEKVRACFKLLKRLQQEIIALGLPNVDPQELSMGMSGDLETAIEEGATIVRVGTAIFGQRIYPDSYYWNENK
>NZ_CP046316.1|WP_009390273.1|2427273_2429430_-|S9-family-peptidase
MRILFLLITLFTGIAWGQPAITLDKIWTQGTFYPSRMYNLKTLQHAPQYTVLEYSPADGAQEINLYDFATLTKVKTIFRAADHKQFMRLNSYTFTPNEQQLLIAVNSEYIYRHSFIADYYLYDLASGKLRKITNDKIQSPLVSPDGKKIAFARNNDLYVYDLATGKEKRITTDGAKNKIINGIADWVYEEEFSTVRFFDWNANGTQLAFVRFDEQQVPEFSMDVYGAGLYPTQQTFKYPKAGEPNSVVSLHIYDLAKAKTTPIALEAYYIPRLQWSNNPKYLTVQTLNRHQNDWQVVQVDAQTFQTRPLVIEKSKTYVEINDKITFLADNSFIYQSERDGYNHLYHCDAQGKSVRQLTFGQTEVTDLYGYDAKNKQLFYQATQADGIQRAICAVGLNGKNQRTLSAVAGTHKATFSGDFAYYIDAFSSATTPPRYTLHAANGKELKEILNNNAFAERLKGYQLPTKEYFQVKTSRATLNAYIMKPFDFNPEKKYPVLMYQYSGPGSQEVADEWWDMNDFWHAMLTQKGYIVLCVDGRGTGYRGEEFKKCTYEQLGKFEVDDQAEVATIVGNYSYVDKSRIGIWGWSFGGFMSSNCIFQKGDIFKMAIAVAPVTNWRFYDTVYTERFMRTPQENPAGYDLNSPLTHAHKLKGKYLLVHGTADDNVHVQNAMSLIEQLVTQRKDFDWLIYPDRNHGIYDNTGSTRWQLYHKMTQFIEENL
>NZ_CP046316.1|WP_009390274.1|2425845_2427243_-|peptide-MFS-transporter
MDTNVENVKKKHPKGLYLVFLTGMWERFSYYGMRGILMLYLTKTFLEGGLAFDPQTASLIYGFATGLTYFTPLIGGWIADNFLGQRKAVLLGGLIMFFGEFVLFAMHSHIGLYLGLFLLIIGNGFFKPNISALVGGLYEPGDKRLDSAFSIFYMGINLGAFLAPLLTGLLTDNIFASNVTNPETGEVVMSFGYKYGFLAAAIGMLVSEVIFLLFAQKYLGDLGLHPKGGKKKVADVEVSDAPLTKEEKERIAVIFVYFFFAIFFFAGFEQAGSSFTLYTDKFIDRVVGGFEIPTAWFQSVNPLFIVVLAPVFASFWNSKFGQTLTTPFKMGTGLILLGIGYFFMLGAVYERGGSIGNDPSDMAVKASLAWLVLTYLTHTMGELCLSPVGLSIVTKLSPPKLAGLLMGVWMTAAFFANAAGGVIASYVEKLGPSIVFTVISGFVILCGLGMVLLNKKLQRMMHGVK
>NZ_CP046316.1|WP_009390275.1|2425450_2425786_+|MerR-family-transcriptional-regulator
MDINLPDKLYYSIGEVATAFGVNSSLIRFWEKEFEIISPKKDTKGSRKFSADDVKKLQLIYHLVKEQGFTLEGARQRLKDEKQKTLSNFEIVAKLEKIKRKLVALKEAMDN
>NZ_CP046316.1|WP_009390276.1|2424469_2425444_+|M23-family-metallopeptidase
MKKVKYYYDPETLSYKRIRNKKRTKVRNALIFLLAAALFGSILSLIIINSRLFFTPREVMLAREIKAYETNYEILNRKMELVEQVLADVQERDNNMYRLYFNAPIIPDSVRKGGFDPNKYKDLEKLGSSKLVANTTKRLDKLRKQLVIQSKSLDEINKLSKEKEKFLASIPAIQPVNNKDLKRMASGYGWRSDPFTKARKFHYGMDFSSPQGTPVYATGDGVVIRADDGSSGYGNHIRIDHGYGYVTLYGHLSAYNVRAGQHVKRGDLIGKVGSTGRSEAPHLHYEVIKNGEHINPIHFYYGNLSADEYAEMLRVSTQENQSLD
>NZ_CP046316.1|WP_009390262.1|2436491_2436887_-|hypothetical-protein
MPLTKKEFRDNLISLLIENNINISSEDKFIIKPIKEKNVSYNSFDDYVRIWFLQEKNINRYFYFQEAIDFLSFSNERYPLWIKVVLFEKDHFFSIFELYISMRFRKPSELKYKELGHPPFIFEDFKNNQLE
>NZ_CP046316.1|WP_009390260.1|2437048_2437420_-|DUF559-domain-containing-protein
MSNKIIPYNPKLKDFAQYLRNHSTASEITLWNHIRRKALGVEFHRQVPILGYIVDFYCHELALAIEVDGNIHEFNFLEDCQRQEAIEKYGITFVRFSNEEINTNLFGVLLSLENTVNTLKNST
>NZ_CP046316.1|WP_009390258.1|2437980_2438715_-|3-oxoacyl-ACP-reductase-FabG
MRKFAIITGGSRGIGRAITEKLAQDTDYHLLITYQSNEIAARETLGHVKKLGREGEIIRFDVSDHQSTVKALTQWQHDNKDAVVEVIVNNAGINRDGLFMWMPPEDWSKVISTSLDGFYNVTNFFIQKMLRHRYGRIINIASVSGVKGTAGQTNYSAAKGAIIAATKALAQEVAKRHITVNAIAPGFIRTDMTSSLKEEDLVKLIPVGRFGEAEEVADLVSFLVSKKASYITGEVININGGIYS
>NZ_CP046316.1|WP_034540167.1|2438943_2440059_+|peptide-methionine-(R)-S-oxide-reductase-MsrB
MKTFVLTAVTALFALGCAHKKTNSYTSYQKTEQMAENQDKYYEVIDEEEPQSKTYIYFAGGCFWGTEHFFKQIRGVLATEVGYANGNRDKAPTYEQVCEGNTNFAETVKVIYNPQLIDLRKLIDLYFKIIDPTSLNKQGNDRGTQYRTGIYYTDATEKPLIEKAIHQLATQYTKPIVVEVLPLRNFYKAEEYHQAYLDKNPNGYCHISPAMFELARKANPVPTKYKRPAESELRKLLTPEQYAVTQESATERPFANEYWNEYREGIYVDITTGEPLFISTDKFESGCGWPSFSKPINKKLITEKTDTSHQMVRTEVRSTLGNAHLGHVFNDGPKELGGLRYCINSASLRFIPKENMEKEGYGEYLKLLEKK
>NZ_CP046316.1|WP_009390254.1|2440119_2440362_+|hypothetical-protein
MTTNTITFKEHLPFEKYQSIMKFLDDIGVEVIEPEQTTFSELTADDLKSIYLSKEQSRMGMVIDHSEVQREAMERRYCRK
>NZ_CP046316.1|WP_009390251.1|2440358_2440661_+|plasmid-stabilization-protein-ParE
MRVVWTTEAIKSYYETLDYWDEHNGSNSYSIKIMTAIDVLIKELVEDPYFLGQYDEQLNLHRRTILKGRFLIYYEIKDAESTIEIQYFRSSYQKPLSNYS
>NZ_CP046316.1|WP_009390250.1|2440662_2441415_+|hypothetical-protein
MKPLKKLLFFCIAALFFSCQHTPQRPVEMSDRQILGLTDKVQQVTLISQHIDEEKRDTTFLTFDSKGRMTEKIEHLQKAKDSILKTKYVYDDVQHTRLAQTYKSDGTLLSEELATYNAYNFVEKYTLTNGETKEVITVVFNYSADGLKAEAKATDGKGELFLTSNIEYNPRGQAVKEEVYITKDKKHSSTTYYVYDEKGALIDKKDYNIKEKNIRNYTFTHTYDNAGNKKEERIYIDGNLSIINKTEIRK
>NZ_CP046316.1|WP_009390248.1|2441789_2442743_+|type-IX-secretion-system-membrane-protein-PorP/SprF
MKRIVLLLLAVCAFEGKTLAQELNLPQQNQYLADSEFLIAPTYAGIGDFVRIRLSGITQWVGVKGAPDYQSLAGDMRLGERSGAGVMLYNDRNGHTYQRGGKVSFAHHLTLDRYDNHFVSFGISYALNTFEIDIKKFNQSIRDQAVTNDRFTVNHNFDVGVLYRYKNWFVNLSAMNILNKDIEHFYKEEPKALRNYMIFAGYRYKQDKKSNFEIEPSLLYQLYESDGRSTTDFNLKFRWMDLEDYYWVGVNYRSLNDQLFRPLNIGPMAGLKRGMLYFAYSYQLTLNEIIGYNSGTHVITLGLDLFQGVSNCKCAQR
>NZ_CP046316.1|WP_009390247.1|2442743_2443106_+|dihydroneopterin-aldolase
MEQIILKNIRSYAYHGCLSEETTIGSDYRTDLKISADLKKSMLSDALQDTVDYVHLNRIVKEEMAIPAKLLENVAARIVKRIFDELPEVQKVTLKVAKINPPIGGDVESVSVKIKQERFG
>NZ_CP046316.1|WP_009390245.1|2443262_2443643_+|hypothetical-protein
MTNVLDKFIQDMKNNIPGFIAVSVTEVRSGVSYGSDSVDPSFDPNLASAYNLEVVKAKQNALQVLGLASKERIVDILITLTDQIHIIDISSNGSYIIYLAVDSNKANLGLTRALLSKYKKDLVAIF

Crispr_ID: NZ_CP046316_7

• CRISPR_ID: NZ_CP046316_7
• CRISPR_location: 2534209-2534297
• CRISPR_type: Orphan
• Repeat_type: NA
• Spacer_info: 1 spacers

Consensus repeat of NZ_CP046316_7

Consensus_repeat	Method
AATCGCCCGTGCGGCTCGCACTCC	CRISPRCasFinder

spacers of NZ_CP046316_7

>7.1|2534233|41|NZ_CP046316|CRISPRCasFinder
CACTCGTCTCCCAATCCTCCCAGCCCTCTCAGCCGTCCCAC

CRISPR arrays and Neighbor proteins around NZ_CP046316_7

CRISPR arrays

The CRISPR arrays of NZ_CP046316_7

>merge|NZ_CP046316|7|2534209-2534297|CRISPRCasFinder
AATCGCCCGTGCGGCTCGCACTCCCACTCGTCTCCCAATCCTCCCAGCCCTCTCAGCCGTCCCACAATTGCCCGTGCGGCTCGCACTCC

>NZ_CP046316|7|6|2534209-2534297|CRISPRCasFinder
AATCGCCCGTGCGGCTCGCACTCC	CACTCGTCTCCCAATCCTCCCAGCCCTCTCAGCCGTCCCAC
AATTGCCCGTGCGGCTCGCACTCC

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP046316.1|WP_009390059.1|2528758_2530456_-|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	unknown	unknown	gnl|CDD|369630
NZ_CP046316.1|WP_009390062.1|2526998_2527835_-|glycoside-hydrolase-family-16-protein	unknown	unknown	gnl|CDD|185693
NZ_CP046316.1|WP_009390052.1|2536057_2537443_+|aspartate-ammonia-lyase	unknown	unknown	gnl|CDD|237031
NZ_CP046316.1|WP_009390072.1|2520565_2521588_-|UDP-glucose-4-epimerase-GalE	unknown	unknown	gnl|CDD|187558
NZ_CP046316.1|WP_009390069.1|2521628_2523842_-|hypothetical-protein	unknown	unknown	gnl|CDD|274350
NZ_CP046316.1|WP_155846670.1|2539156_2539378_+|twin-arginine-translocase-TatA/TatE-family-subunit	unknown	unknown	gnl|CDD|224739
NZ_CP046316.1|WP_009390051.1|2537605_2538589_+|DUF4837-family-protein	unknown	unknown	gnl|CDD|379774
NZ_CP046316.1|WP_034540125.1|2527824_2528391_-|four-helix-bundle-protein	unknown	unknown	gnl|CDD|275085
NZ_CP046316.1|WP_009390054.1|2534661_2535474_-|hypothetical-protein	unknown	unknown	gnl|CDD|119396
NZ_CP046316.1|WP_009390066.1|2524865_2525990_-|adenylate-kinase	unknown	unknown	gnl|CDD|234711
NZ_CP046316.1|WP_009390074.1|2519388_2520447_-|FAD-dependent-oxidoreductase	unknown	unknown	gnl|CDD|274478
NZ_CP046316.1|WP_008622960.1|2534391_2534613_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP046316.1|WP_009390049.1|2538721_2539102_+|DUF559-domain-containing-protein	unknown	unknown	gnl|CDD|238509
NZ_CP046316.1|WP_155846669.1|2528466_2528628_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP046316.1|WP_034540129.1|2526261_2526936_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP046316.1|WP_009390039.1|2541349_2542636_+|gliding-motility-associated-protein-GldE	unknown	unknown	gnl|CDD|274626
NZ_CP046316.1|WP_009390042.1|2540868_2541294_+|single-stranded-DNA-binding-protein	unknown	unknown	gnl|CDD|366099
NZ_CP046316.1|WP_009390047.1|2539422_2539740_+|YbjQ-family-protein	unknown	unknown	gnl|CDD|376657
NZ_CP046316.1|WP_009390046.1|2539756_2540818_+|A/G-specific-adenine-glycosylase	unknown	unknown	gnl|CDD|224115
NZ_CP046316.1|WP_009390067.1|2523867_2524866_-|GTPase-ObgE	unknown	unknown	gnl|CDD|237048

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
NZ_CP046316.1|WP_009390059.1|2528758_2530456_-|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	gnl|CDD|369630	pfam07980, SusD_RagB, SusD family. This domain is found in bacterial cell surface proteins such SusD and SusD-like proteins, as as well RagB, outer membrane surface receptor antigen. Bacteroidetes, one of the two dominant bacterial phyla in the human gut, are Gram-negative saccharolytic microorganisms that utilize a diverse array of glycans. Hence, they express starch-utilization system (Sus) for glycan uptake. SusD has 551 amino acids, and is almost entirely alpha-helical, with 22 alpha-helices, eight of which form 4 tetra-trico peptide repeats (TPRs: helix-turn-helix motifs involved in protein-protein interactions). The four TPRs pack together to create a right-handed super-helix. This is predicted to mediate the formation of SusD and SusC porin complex at the cell surface. The interaction between SusC and TPR1/TPR2 region of SusD is predicted to be of functional importance since it allows SusD to be in position for oligosaccharide capture from other Sus lipoproteins and delivery of these glycans to the SusC porin. The non-TPR containing portion of SusD is where starch binding occurs. The binding site is a shallow surface cavity located on top of TPR1. SusD homologs such as SusD-like proteins have a critical role in carbohydrate acquisition. Both SusD and its homologs, contain about 15-20 residues at the N-terminus that might be a flexible linker region, anchoring the protein to the membrane and the glycan-binding domain. Other homologs to SusD have been examined in Porphyromonas gingivalis such as RagB, an immunodominant outer-membrane surface receptor antigen. Structural characterization of RagB shows substantial similarity with Bacteroides thetaiotaomicron SusD (i.e alpha-helices and TPR regions). Based on this structural similarity, functional studies suggest that, RagB binding of glycans occurs at pockets on the molecular surface that are distinct from those of SusD.	5.18917e-41
NZ_CP046316.1|WP_009390062.1|2526998_2527835_-|glycoside-hydrolase-family-16-protein	gnl|CDD|185693	cd08023, GH16_laminarinase_like, Laminarinase, member of the glycosyl hydrolase family 16. Laminarinase, also known as glucan endo-1,3-beta-D-glucosidase, is a glycosyl hydrolase family 16 member that hydrolyzes 1,3-beta-D-glucosidic linkages in 1,3-beta-D-glucans such as laminarins, curdlans, paramylons, and pachymans, with very limited action on mixed-link (1,3-1,4-)-beta-D-glucans.	8.53002e-69
NZ_CP046316.1|WP_009390052.1|2536057_2537443_+|aspartate-ammonia-lyase	gnl|CDD|237031	PRK12273, aspA, aspartate ammonia-lyase; Provisional.	0
NZ_CP046316.1|WP_009390072.1|2520565_2521588_-|UDP-glucose-4-epimerase-GalE	gnl|CDD|187558	cd05247, UDP_G4E_1_SDR_e, UDP-glucose 4 epimerase, subgroup 1, extended (e) SDRs. UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup has the characteristic active site tetrad and NAD-binding motif 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.	4.0493e-170
NZ_CP046316.1|WP_009390069.1|2521628_2523842_-|hypothetical-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.	0.00260702
NZ_CP046316.1|WP_155846670.1|2539156_2539378_+|twin-arginine-translocase-TatA/TatE-family-subunit	gnl|CDD|224739	COG1826, TatA, Sec-independent protein secretion pathway components [Intracellular trafficking and secretion].	2.64808e-14
NZ_CP046316.1|WP_009390051.1|2537605_2538589_+|DUF4837-family-protein	gnl|CDD|379774	pfam16125, DUF4837, Domain of unknown function (DUF4837). This family consists of uncharacterized proteins around 350 residues in length and is mainly found in various Bacteroides species. The function of this family is unknown.	2.90499e-124
NZ_CP046316.1|WP_034540125.1|2527824_2528391_-|four-helix-bundle-protein	gnl|CDD|275085	TIGR04258, hypothetical_protein, four helix bundle suffix domain. This domain occurs as a suffix domain to some members of the much broader protein family TIGR02436, a few of whose other members are encoded within intervening sequences of bacterial 23S ribosomal RNA. Some proteins with this domain, in turn, are followed by a predicted DNA topoisomerase type C4 zinc finger.	4.27166e-17
NZ_CP046316.1|WP_009390054.1|2534661_2535474_-|hypothetical-protein	gnl|CDD|119396	cd06462, Peptidase_S24_S26, The S24, S26 LexA/signal peptidase superfamily contains LexA-related and type I signal peptidase families. The S24 LexA protein domains include: the lambda repressor CI/C2 family and related bacterial prophage repressor proteins; LexA (EC 3.4.21.88), the repressor of genes in the cellular SOS response to DNA damage; MucA and the related UmuD proteins, which are lesion-bypass DNA polymerases, induced in response to mitogenic DNA damage; RulA, a component of the rulAB locus that confers resistance to UV, and RuvA, which is a component of the RuvABC resolvasome that catalyzes the resolution of Holliday junctions that arise during genetic recombination and DNA repair. The S26 type I signal peptidase (SPase) family also includes mitochondrial inner membrane protease (IMP)-like members. SPases are essential membrane-bound proteases which function to cleave away the amino-terminal signal peptide from the translocated pre-protein, thus playing a crucial role in the transport of proteins across membranes in all living organisms. All members in this superfamily are unique serine proteases that carry out catalysis using a serine/lysine dyad instead of the prototypical serine/histidine/aspartic acid triad found in most serine proteases.	1.8816e-07
NZ_CP046316.1|WP_009390066.1|2524865_2525990_-|adenylate-kinase	gnl|CDD|234711	PRK00279, adk, adenylate kinase; Reviewed.	1.30674e-83
NZ_CP046316.1|WP_009390074.1|2519388_2520447_-|FAD-dependent-oxidoreductase	gnl|CDD|274478	TIGR03197, MnmC_Cterm, tRNA U-34 5-methylaminomethyl-2-thiouridine biosynthesis protein MnmC, C-terminal domain. In Escherichia coli, the protein previously designated YfcK is now identified as the bifunctional enzyme MnmC. It acts, following the action of the heterotetramer of GidA and MnmE, in the modification of U-34 of certain tRNA to 5-methylaminomethyl-2-thiouridine (mnm5s2U). In other bacterial, the corresponding proteins are usually but always found as a single polypeptide chain, but occasionally as the product of tandem genes. This model represents the C-terminal region of the multifunctional protein. [Protein synthesis, tRNA and rRNA base modification].	7.82084e-22
NZ_CP046316.1|WP_009390049.1|2538721_2539102_+|DUF559-domain-containing-protein	gnl|CDD|238509	cd01038, Endonuclease_DUF559, Domain of unknown function, appears to be related to a diverse group of endonucleases.	1.17101e-30
NZ_CP046316.1|WP_009390067.1|2523867_2524866_-|GTPase-ObgE	gnl|CDD|237048	PRK12299, obgE, GTPase CgtA; Reviewed.	0
NZ_CP046316.1|WP_009390039.1|2541349_2542636_+|gliding-motility-associated-protein-GldE	gnl|CDD|274626	TIGR03520, GldE, gliding motility-associated protein GldE. Members of this protein family are exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides). GldC is a protein linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Flavobacterium johnsoniae and Cytophaga hutchinsonii. GldE was discovered because of its adjacency to GldD in F. johnsonii. Overexpression of GldE partially supresses the effects of a GldB point mutant suggesting that GldB and GldE interact. Gliding motility appears closely linked to chitin utilization in the model species Flavobacterium johnsoniae. Not all Bacteroidetes with members of this protein family appear to have all of the genes associated with gliding motility and in fact some do not appear to express the gliding phenotype.	0
NZ_CP046316.1|WP_009390042.1|2540868_2541294_+|single-stranded-DNA-binding-protein	gnl|CDD|366099	pfam00436, SSB, Single-strand binding protein family. This family includes single stranded binding proteins and also the primosomal replication protein N (PriB). PriB forms a complex with PriA, PriC and ssDNA.	1.54018e-35
NZ_CP046316.1|WP_009390047.1|2539422_2539740_+|YbjQ-family-protein	gnl|CDD|376657	pfam01906, YbjQ_1, Putative heavy-metal-binding. From comparative structural analysis, this family is likely to be a heavy-metal binding domain. The domain oligomerizes as a pentamer. The domain is about 100 amino acids long and is found in prokaryotes.	4.11954e-46
NZ_CP046316.1|WP_009390046.1|2539756_2540818_+|A/G-specific-adenine-glycosylase	gnl|CDD|224115	COG1194, MutY, A/G-specific DNA glycosylase [DNA replication, recombination, and repair].	4.35815e-119

Protein sequences

>NZ_CP046316.1|WP_009390059.1|2528758_2530456_-|RagB/SusD-family-nutrient-uptake-outer-membrane-protein
MKNLYKHIVFAGILLATLSQTACKNDDFLDKYPPDSFNEKGYFNTDNDLKIFANRFYGSLPVQILIYNDGDSDNMVPRNVNTFLAGNYTVPASGGGWSTGDWNGIYNCNFFLDNYSRSTGLHKEQFAAEVRFFRALYYWDKVKTFGDVPLVLTKVNDASPIIYGPRVPHKQVMEKVLEDLDFAVQHLPAKASAEAGRLHKDAALALKSRIALWEGTFRKYHGLGDETSWLQAAADASQALINSGRYRVYSTGNPTKDYRNLFIQKDLSTNSEAIMARTYIQGIGTHGYTRTAGENSTGCSKDFMENYLFTDGKPISGTSFTYDDSTPAGEAANRDPRYAQTVATPGFVWTENPDPTRQQVVTLPAVGSGQTSSGYWFIKGRSSDPEQWIAQQSDLDLFIFRYAEILLNYAEAKYELGTLSQGDLDISINKLRDRVGMPHLTTTVSADANADNYGYTVTPLLYEIRRERRIELIGEGFRFDDIMRWKAGKLIENPKTIRGMKLTPALKALYPARSGVANLPVDSNNYLIMYPSLPLTGRVWNDKQYLYPLPTDQLQLVGYRQNPGW
>NZ_CP046316.1|WP_155846669.1|2528466_2528628_-|hypothetical-protein
MGVRAARAIMGQVGRVGRVRQVGQVRQVGQVRQVGQVRQVGQVRQVGQVGRVG
>NZ_CP046316.1|WP_034540125.1|2527824_2528391_-|four-helix-bundle-protein
MMTTFLKLKGGYRSLYAYQKAEVIYDITFYFTQHFLTKGDRTIDQMLQAARSGKQNIAEGSKASTTSIETEIKLTNVAKASLEELLIDYEDYLRVRNKEQWHIGHPRYDKVRTFASSKEIFELYPSLLPKYDDASLANLCITLINQTTFLLRRLIEKQQEVFLQKGGVREQMSVARRRILTNHNSNEN
>NZ_CP046316.1|WP_009390062.1|2526998_2527835_-|glycoside-hydrolase-family-16-protein
MKISFLLLSAFVLGNACYKVAQEEKKLQEPQKPKVEQSVSKQWQLVWEDNFDRDDIFATGIWSKISRNEKIDWRNTMSDDPSLYDIKEGNLILYGKMNTDLKADPSEYITGGVYTINKKYFETGRLEVRCKLESTQGAWPAIWMLPKEGKWPTGGEIDIMEHLNYDDFVYQTLHTSYTKNVSKQNPKSGSTAKINANDYNVYAVEWDAESVRLYVNGVQTLLYPYLKDQQDKGQYPFVRPYYLLIDMQLGGNWVGAVKPFDKPVAMYIDWVRYYQLAD
>NZ_CP046316.1|WP_034540129.1|2526261_2526936_-|hypothetical-protein
MKIQFFIALSAVALIGCKNNPQEITVAEDAMANTQLAEEQRDKTKDANPFDQGTALSTPATSQGGGVTLNPPHGQPGHRCDIAVGAPLPNDGNVIAQAQNVSHPVSQGEAMPVVSNGMEQPQVIQVSQPQNYVGANGEKLNPPHGQPGHRCDIPVGAPLNSKPAAATTAAPAQQPQVVQQQVVIDPQQAQQHTGTTEPGFSGKPNPPHGQPGHRCDIAVGATLP
>NZ_CP046316.1|WP_009390066.1|2524865_2525990_-|adenylate-kinase
MELIKIHDKTFEPYISAQQLDEINARMAAEVYQDLGESRPVFVAVLNGSFMFAADFVRHYKGECEISFVKMSSYEGTQSTGKVHELIGLSGSVEGRDVVILEDIVDTGNTLEEIYRIFKDKKVKSFRIATLFFKPDAYKKDFKIDYVGKPIPNRFIVGYGLDFDEVGRNLPQVYQLNTSITMTNLVLFGKPGAGKGTQAAFLKDKYNLVHISTGDIFRFNIKNETKLGKLAQSYIEKGDLVPDEVTIQMLQEEVEKNPNAEGFLFDGFPRTIAQAEALDAFLTSKGMRIHGTLALEADDEVLIKRIVERGKVSGRADDQDEEKIKNRFVEYNEKTAPLIAYYKAQGKYHAVDGIGTVEEITVRLSKAIDQIKAQ
>NZ_CP046316.1|WP_009390067.1|2523867_2524866_-|GTPase-ObgE
MTEGNFTDYVKIYAASGNGGAGSMHLHREKFVPKGGPDGGDGGRGGHIILKGNKHLWTLIHFKFQKHFRAEHGEAGGANRSFGADGKDIYLEVPLGTIVKDAETEEVLFEITEDGQEVIALRGGKGGLGNWHFRTATNQTPRYAQPGLPGEERELLLELKVLADVGLVGFPNAGKSTLLSVITSAKPKIGDYPFTTLKPNLGIVENRDFQSFVMADIPGIIEGAAEGKGLGHFFLRHIERNSLLLFLIPADANDIVAEYEILLNELKKYNPELLDKQRLVAISKSDMLDEELTAAIDKELAAKLKVPYLFISSVSGKGIQKLKDELMSRLDN
>NZ_CP046316.1|WP_009390069.1|2521628_2523842_-|hypothetical-protein
MNKILTLCALFPLVAVAQPSDLIGVYKSKEARQFQLRINADNTVDALMATGTYTAKDKNISLQFGTGNSFRVVKTQGTTDQLTLTFKEADINMFDPRFLYIGYKNSKGEIVYESAYNKLQGQDDYTIEIPRTDNLYLVNAYGVAITGDKKAAVIIEEYLVGKNTSGVEITFDTENSVRNELQATYNPEKQTLTLNDKSLSSNPIVFSKVLAVDAQALQPVATEKVKQWKHLIAFDEEKDIPEFNPEKKALSTLKQANSLSAALAAAKKNNRLVALLYQPNNKNATNEFKELFEWYEQNGETVLTDPYLFELYLATAKELKSLKAKGLTNEDQLIILTSEGEVIYHEPATIAQVLADETLEYNHTGLLRTAAKASLADRVLSNPKAPLKEVVKVLIALSNYTQDPDVQLLLAKRPKTGDVETDEDKQATIDYQLENLITYYKKPENLYRLQLTPEQLIAQWKRVVAAHKADAKLDTDFALLASLNVEINDNFFTKTFYLNYEPTTTDLEAGAYLLRFFKEIKAHNDALKDIGDYTYIQRIDRGYIAFNTAAVERTLKACYDLDKATLPEVKKAYAEGIKNGALSSLDYIDFLYNQDLTTDAAMAFDTYFKNLMATDANLIAALDNDFTNNNPENSWRYYKMLFANRANNIAWKVYEDQPNSKALMAEAYRWAKAAVQLEPKSPYYLDTLAHLMFAHGDKKEAVATEEKAVSLLSQDEDGNAEQKEEIKKNLIKMKQGL
>NZ_CP046316.1|WP_009390072.1|2520565_2521588_-|UDP-glucose-4-epimerase-GalE
MKKIVVTGGLGFIGSHTVVELQNAGFEVVIIDNLSNAQESVLEHITKITGKKPLFEKFDLRDKADVQDFFRRHTDVEGLIHFAASKAVGESVEKPLLYYNNNLTSLIYLLEELSKLKKAHFIFSSSCTVYGQADKLPITEDAPVKKAESPYGNTKQISEEIISDTCRVTPQLNAIALRYFNPIGAHPSAEIGELPLGVPQNLVPYITQTAIGLREKLSVFGDDYPTPDGTCIRDYIHVVDLAKAHVIALQRLLNDKNAENYEVFNIGTGKGSSVLEVIQSFERVSGKKLNYQIVARRAGDVTAAYANTDRANHVLGWEAKSTLDDAMLSAWKWEQKVRSK
>NZ_CP046316.1|WP_009390074.1|2519388_2520447_-|FAD-dependent-oxidoreductase
MFDFIIVGAGLAGVSFAHLLEQHGKSFCLLSDRSQVASLIAGGVYNPVVLKRFTPIWKAEEIMACANRFYDNIEATMGQPLRISLPVLRKFASVEEQNNWFAASDTPILQHYLSTTLRTTPSEALPAPYLLGEVLHTGRLDIERYIQLSLRSWQEAGVYHFHSFDYSALDIQPDFVAYQGVTAQHIVFCEGCGISKNPYFNSLPMRPCKGESLTIKAPDLQLQAIFKSDGSIISMGADIYRVGATYDPEDLTDTITEAGRAELLEKLHKMTDSPYEIISHQAAIRPTVGDRRPLVGAHPLYPHLWVLNGLGTRGVLNAPLCAQVLYKAVFEGEEIPSEMNVNRFNKRLRRKG
>NZ_CP046316.1|WP_008622960.1|2534391_2534613_-|hypothetical-protein
MQATLIFDVKILLKPLAYPTFAAPLKAKGANARRAGVLRYKMRKMKVNLNFSFKLIKILIRISKKKFLIKITY
>NZ_CP046316.1|WP_009390054.1|2534661_2535474_-|hypothetical-protein
MNVKERIKQFIEAQNLTVSAFEKEINASNGYINSISKNIGIDKLNTILEKYPKLNVEWLITGKGEMLKSGGALPLLPRVEIIKPIKVEGRSLVPKVIVVDDRDNDRIPLVPVRAQAGYLNGYDDERFIEQLPTYSLPTMQNGTYRMFQVSGLSMYPTLQDSSYVVGKFVEDWDMLSNNRVCVVVTANDGVIVKRVVNSISKYGTLYCKSDNRDYPHLSIHIEDVKEIWECKMHLSFEFLDPVTNYQKIAELEADVAHLKEELAEIRKLAN
>NZ_CP046316.1|WP_009390052.1|2536057_2537443_+|aspartate-ammonia-lyase
MTKFRTESDLIGDLQVPAEAYYGVQTQRAIENFRITGTKMGDYPEFVKAIGYVKLAAAQTNHELGLLPDNLLKPISQACEEVISGKFDHQFLVDMIQGGAGTSVNMNANEVIANRALEIMGYGRGEYQHCSPNDHVNQSQSTNDAYPTTVKLAVIKMNEKLIERLSLLIEAFRQKGKEFADVIKMGRTQLQDAVPMTLGQEFEAFAANLEEEIARLQSNAKLFLEINMGGTAIGTGLNAPKGYAQLCAQKLATLTGEKFVTAANLVEATPDTGSYVIYSSALKRMAVKLSKICNDLRLLSSGPRAGLNEINLPKMQPGSSIMPGKVNPVIPEVVNQVCFKVIGNDLTVTFAAEAGQLQLNVMEPVLCQCIIESIVFLERAIDTLRTKCIEGITANREVCLNMVKHSIGIVTALNPHIGYKNSSKIAKEALESGKSVYNLVLEHKLLSKEELDRILDPKNMI
>NZ_CP046316.1|WP_009390051.1|2537605_2538589_+|DUF4837-family-protein
MKRLLLVSLLFSILLTACSNSKGGETYLPASVGPINSLAVVIDNDLWEGSVGDTIRRYFAAPIDGLPNEEPTFSLHQVPPQVFEGNTRNSRNVLIVSRGNQPQGAIKENVYAKPQVVAVIEAKKVRDIACKIEEYHRLFINAFKENELAETRHRFQKSLNTETEYTQALGVKLQMPSFYKIVKHENNFFWIERPIKGGRASVILYEMPLKSIPTDEEGRAKAIVKMRDSIGEKYIPGPEKGMYMVTETYLAPSVSEVKIKNHFALESKGLWEVKGFALGGPYINYIIEDKAKNRLLVAEGFLYAPGVSKRDVLFELEAIIKSISFND
>NZ_CP046316.1|WP_009390049.1|2538721_2539102_+|DUF559-domain-containing-protein
MPNIIPYNPKLREFARYLRNNSTLSEVLLWKEIKNKALGVEFKRQVPILDYIVDFYCQELKLAVEVDGHIHDFRYVEDKVRQEQIEQWGITFIRFSNEDIKTNMFSVVLSLESKIDELKKTNFSEE
>NZ_CP046316.1|WP_155846670.1|2539156_2539378_+|twin-arginine-translocase-TatA/TatE-family-subunit
MKYMNIFLGMVGPWQVVIIVALILLLFGGKKIPELMRGLGTGIREFKDATKDPAKDNERIGKPEDEQINKSAN
>NZ_CP046316.1|WP_009390047.1|2539422_2539740_+|YbjQ-family-protein
MLLTTTPTIEGHPIKQYLGIVTGETIIGANAIKDFMAGLTDFFGGRSTTYEKVLIEGKETALKELQQRAAALGANAVVGIDLDYETVGANGGMLMVTASGTAVQV
>NZ_CP046316.1|WP_009390046.1|2539756_2540818_+|A/G-specific-adenine-glycosylase
MANQQIDKSANWLTSKLLSWYATAKRDLPWRGTTDPYKVWLSEIILQQTRVVQGLPYYERFITHFPTVSDLAKASEEEVLKLWQGLGYYSRAKNLHHTAQHIATVLGGVFPKSYQELVKLKGIGDYTASAIASFCYNEPCAVVDGNVYRVLSRLFGVQTPINTPAAAKEFKALANELLDKPRAGEYNQAIMEFGAIVCTPQSPDCANCVLRDNCWAWAHNQVGVLPAKLKKIKIKQRYFNYLVWLSADQQTLLQKREGKDIWHGLYEFPLIETSTPLSAAALTEQLREQHPLITPYLYNESPVVHKLTHQHIHTSFWVLTTHSPLEKGISISQLERYPVSALTANFIKNFWKL
>NZ_CP046316.1|WP_009390042.1|2540868_2541294_+|single-stranded-DNA-binding-protein
MNGYVNKVILVGRIGEAIKLTYFSEGNCVGQFRLATHEEYTNRNTNERVEHTEWHNIVVRNKLAEAIEKYTQKGDLIYLEGQLRTRSWQAEDGSPRYITEVVVSDMNLLPNMRAPKTATPPVAGTLTTQSSPELDANGVPF
>NZ_CP046316.1|WP_009390039.1|2541349_2542636_+|gliding-motility-associated-protein-GldE
MPFLTVDIALIVQFAIFCLLLLCSAIISGSEVALFSLSPTEIDELKEDHNSANNLIAKMVENPKKLLATVLIANNLVNISIVLISPELTNFAFGGIKNPILRDVMDIGLVTFVLLLCGEILPKIYANRNNLAFAKRVAYFIYILDTVFTPISLPMKSFTVWIQKRLGKTKSNISVGQLSQALELASEEDTTNEEKKLLESIVSFGNTETCEVMVPRVDIFALSEDTPFSEVLSEIVKIGYSRIPVYRENLDNITGVIYIKDLLPYIEKPDFQWTKVMRKAFFVPENKKLDDLLSEFQEKKIHLAVVVDEYGGTCGIITLEDIMEEIVGSINDEFDDDDVTYSKINDHTYIFEGKTVLKDFYRIVKMDDENILLFDEKRGEAETLAGFLLEISGNFPQKGKPIVFHNYSFTVEAFDKHRIKEIKVKINS

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity
NZ_CP046316_3	3.11|341576|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT	341576-341607	32	NZ_CP027233	Capnocytophaga sp. oral taxon 864 strain F0512 plasmid unnamed1, complete sequence	24946-24977	3	0.906
NZ_CP046316_3	3.6|341197|31|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT	341197-341227	31	NC_011723	Rippkaea orientalis PCC 8801 plasmid pP880102, complete sequence	21494-21524	7	0.774
NZ_CP046316_3	3.6|341197|31|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT	341197-341227	31	MG592478	Vibrio phage 1.106.O._10N.286.51.F7, partial genome	11156-11186	7	0.774
NZ_CP046316_3	3.7|341272|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT	341272-341303	32	CP016195	Bacillus thuringiensis serovar coreanensis strain ST7 plasmid pST7-1, complete sequence	227924-227955	7	0.781
NZ_CP046316_3	3.7|341272|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT	341272-341303	32	MN693260	Marine virus AFVG_25M320, complete genome	869-900	7	0.781
NZ_CP046316_3	3.7|341272|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT	341272-341303	32	MN693258	Marine virus AFVG_25M459, complete genome	34160-34191	7	0.781
NZ_CP046316_3	3.7|341272|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT	341272-341303	32	NZ_CP010578	Bacillus thuringiensis serovar morrisoni strain BGSC 4AA1 plasmid pBMB232, complete sequence	42007-42038	7	0.781
NZ_CP046316_3	3.7|341272|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT	341272-341303	32	NZ_CP010579	Bacillus thuringiensis serovar morrisoni strain BGSC 4AA1 plasmid pBMB92, complete sequence	72738-72769	7	0.781
NZ_CP046316_3	3.11|341576|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT	341576-341607	32	NZ_CP013915	Serratia fonticola strain GS2 plasmid pSF002, complete sequence	38192-38223	7	0.781
NZ_CP046316_3	3.1|340820|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT	340820-340851	32	NZ_CP007513	Bacillus bombysepticus plasmid pBb, complete genome	517952-517983	8	0.75
NZ_CP046316_3	3.7|341272|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT	341272-341303	32	MN693589	Marine virus AFVG_25M348, complete genome	27576-27607	8	0.75
NZ_CP046316_3	3.10|341500|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT	341500-341531	32	NZ_CP053606	Escherichia coli strain NEB_Turbo plasmid F', complete sequence	93874-93905	8	0.75
NZ_CP046316_3	3.10|341500|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT	341500-341531	32	NZ_CP053608	Escherichia coli strain NEB5-alpha_F'Iq plasmid F'Iq, complete sequence	103029-103060	8	0.75
NZ_CP046316_3	3.10|341500|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT	341500-341531	32	MK492260	Escherichia coli strain MG1655 K12 plasmid F-Tn10, complete sequence	32709-32740	8	0.75
NZ_CP046316_3	3.10|341500|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT	341500-341531	32	NZ_CP027256	Escherichia coli strain EC11 plasmid unnamed1, complete sequence	54745-54776	8	0.75
NZ_CP046316_3	3.10|341500|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT	341500-341531	32	NZ_CP009167	Escherichia coli 1303 plasmid p1303_109, complete sequence	19778-19809	8	0.75
NZ_CP046316_3	3.10|341500|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT	341500-341531	32	NZ_CP010345	Escherichia coli ECC-1470 plasmid pECC-1470_100, complete sequence	14180-14211	8	0.75
NZ_CP046316_3	3.10|341500|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT	341500-341531	32	NC_002483	Escherichia coli K-12 plasmid F DNA, complete sequence	23553-23584	8	0.75
NZ_CP046316_3	3.10|341500|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT	341500-341531	32	NZ_CP048440	Escherichia coli strain NBRC 3301 plasmid putative_pEcol1, complete sequence	13665-13696	8	0.75
NZ_CP046316_3	3.10|341500|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT	341500-341531	32	NZ_CP014271	Escherichia coli K-12 strain K-12 DHB4 plasmid F128-(DHB4), complete sequence	95204-95235	8	0.75
NZ_CP046316_3	3.10|341500|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT	341500-341531	32	NZ_CP014273	Escherichia coli K-12 strain K-12 C3026 plasmid F128-(C3026), complete sequence	76157-76188	8	0.75
NZ_CP046316_3	3.11|341576|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT	341576-341607	32	NZ_CP013915	Serratia fonticola strain GS2 plasmid pSF002, complete sequence	36073-36104	8	0.75
NZ_CP046316_3	3.11|341576|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT	341576-341607	32	NZ_CP013914	Serratia fonticola strain GS2 plasmid pSF001, complete sequence	59534-59565	8	0.75
NZ_CP046316_3	3.14|341804|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT	341804-341835	32	NZ_CP016700	Lactococcus lactis subsp. lactis strain 275 plasmid p275B, complete sequence	54263-54294	8	0.75
NZ_CP046316_3	3.7|341272|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT	341272-341303	32	CP011076	Brevibacillus laterosporus strain B9 plasmid unnamed2, complete sequence	742009-742040	9	0.719
NZ_CP046316_3	3.14|341804|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT	341804-341835	32	NZ_CP016739	Lactococcus lactis subsp. cremoris strain JM3 plasmid pJM3C, complete sequence	20244-20275	9	0.719
NZ_CP046316_3	3.14|341804|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT	341804-341835	32	NC_015902	Lactococcus lactis subsp. lactis bv. diacetylactis plasmid pVF50, complete sequence	5503-5534	9	0.719
NZ_CP046316_3	3.14|341804|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT	341804-341835	32	KU234532	Nostoc phage N1, complete genome	52215-52246	10	0.688
NZ_CP046316_3	3.12|341652|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT	341652-341683	32	MN783745	Escherichia coli plasmid pFII-FIB, complete sequence	37257-37288	11	0.656

1. spacer 3.11|341576|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT matches to NZ_CP027233 (Capnocytophaga sp. oral taxon 864 strain F0512 plasmid unnamed1, complete sequence) position: , mismatch: 3, identity: 0.906

ctctcgccctccctcccgttggtcggttggga	CRISPR spacer
ttctcgcccgccctcccgttggtcggttgggg	Protospacer
.******** *********************.

2. spacer 3.6|341197|31|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT matches to NC_011723 (Rippkaea orientalis PCC 8801 plasmid pP880102, complete sequence) position: , mismatch: 7, identity: 0.774

aggcttttttgaaggggtttttgcttgaggt	CRISPR spacer
ttgagtttttgaaggcgtttttgattgagat	Protospacer
  *  ********** ******* *****.*

3. spacer 3.6|341197|31|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT matches to MG592478 (Vibrio phage 1.106.O._10N.286.51.F7, partial genome) position: , mismatch: 7, identity: 0.774

aggcttttttgaaggggtttttgcttgaggt	CRISPR spacer
aagttattttgaaggggtttttgatggagaa	Protospacer
*.*.* ***************** * ***. 

4. spacer 3.7|341272|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT matches to CP016195 (Bacillus thuringiensis serovar coreanensis strain ST7 plasmid pST7-1, complete sequence) position: , mismatch: 7, identity: 0.781

caacaaatgaatgaaacagcaaaacaaagtgt	CRISPR spacer
acaaaaataattgaaacagcaaaacaaagtag	Protospacer
  * ****.* *******************. 

5. spacer 3.7|341272|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT matches to MN693260 (Marine virus AFVG_25M320, complete genome) position: , mismatch: 7, identity: 0.781

caacaa-atgaatgaaacagcaaaacaaagtgt	CRISPR spacer
-attaatatgaatgaaccagaaaaacaaagtca	Protospacer
 * .** ********* *** **********  

6. spacer 3.7|341272|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT matches to MN693258 (Marine virus AFVG_25M459, complete genome) position: , mismatch: 7, identity: 0.781

caacaa-atgaatgaaacagcaaaacaaagtgt	CRISPR spacer
-attaatatgaatgaaccagaaaaacaaagtca	Protospacer
 * .** ********* *** **********  

7. spacer 3.7|341272|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT matches to NZ_CP010578 (Bacillus thuringiensis serovar morrisoni strain BGSC 4AA1 plasmid pBMB232, complete sequence) position: , mismatch: 7, identity: 0.781

caacaaatgaatgaaacagcaaa----acaaagtgt	CRISPR spacer
gaacaaatgaaagaaaccgcaaaatctacaaa----	Protospacer
 ********** ***** *****    *****    

8. spacer 3.7|341272|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT matches to NZ_CP010579 (Bacillus thuringiensis serovar morrisoni strain BGSC 4AA1 plasmid pBMB92, complete sequence) position: , mismatch: 7, identity: 0.781

caacaaatgaatgaaacagcaaa----acaaagtgt	CRISPR spacer
gaacaaatgaaagaaaccgcaaaatctacaaa----	Protospacer
 ********** ***** *****    *****    

9. spacer 3.11|341576|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT matches to NZ_CP013915 (Serratia fonticola strain GS2 plasmid pSF002, complete sequence) position: , mismatch: 7, identity: 0.781

ctctcgccctccctcccgttggtcggttggga	CRISPR spacer
cgttcgcactccctcccgttggtcggtcgctt	Protospacer
* .**** *******************.*   

10. spacer 3.1|340820|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT matches to NZ_CP007513 (Bacillus bombysepticus plasmid pBb, complete genome) position: , mismatch: 8, identity: 0.75

aaagacttccctattttgaataac--ctgatagt	CRISPR spacer
caagacttccatattttaaataacagctgtcg--	Protospacer
 ********* ******.******  *** ..  

11. spacer 3.7|341272|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT matches to MN693589 (Marine virus AFVG_25M348, complete genome) position: , mismatch: 8, identity: 0.75

caacaaatgaatgaaacagcaaaacaaagtgt	CRISPR spacer
caagctggtaaagaaacagcaaaacaaggtgt	Protospacer
***   .  ** ***************.****

12. spacer 3.10|341500|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT matches to NZ_CP053606 (Escherichia coli strain NEB_Turbo plasmid F', complete sequence) position: , mismatch: 8, identity: 0.75

tacgttaggcattataacctttgccgatgaga	CRISPR spacer
tagttatggcattatcacctttaccgatgatg	Protospacer
**  *  ******** ******.******* .

13. spacer 3.10|341500|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT matches to NZ_CP053608 (Escherichia coli strain NEB5-alpha_F'Iq plasmid F'Iq, complete sequence) position: , mismatch: 8, identity: 0.75

tacgttaggcattataacctttgccgatgaga	CRISPR spacer
tagttatggcattatcacctttaccgatgatg	Protospacer
**  *  ******** ******.******* .

14. spacer 3.10|341500|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT matches to MK492260 (Escherichia coli strain MG1655 K12 plasmid F-Tn10, complete sequence) position: , mismatch: 8, identity: 0.75

tacgttaggcattataacctttgccgatgaga	CRISPR spacer
tagttatggcattatcacctttaccgatgatg	Protospacer
**  *  ******** ******.******* .

15. spacer 3.10|341500|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT matches to NZ_CP027256 (Escherichia coli strain EC11 plasmid unnamed1, complete sequence) position: , mismatch: 8, identity: 0.75

tacgttaggcattataacctttgccgatgaga	CRISPR spacer
tagttatggcattatcacctttaccgatgatg	Protospacer
**  *  ******** ******.******* .

16. spacer 3.10|341500|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT matches to NZ_CP009167 (Escherichia coli 1303 plasmid p1303_109, complete sequence) position: , mismatch: 8, identity: 0.75

tacgttaggcattataacctttgccgatgaga	CRISPR spacer
tagttatggcattatcacctttaccgatgatg	Protospacer
**  *  ******** ******.******* .

17. spacer 3.10|341500|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT matches to NZ_CP010345 (Escherichia coli ECC-1470 plasmid pECC-1470_100, complete sequence) position: , mismatch: 8, identity: 0.75

tacgttaggcattataacctttgccgatgaga	CRISPR spacer
tagttatggcattatcacctttaccgatgatg	Protospacer
**  *  ******** ******.******* .

18. spacer 3.10|341500|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT matches to NC_002483 (Escherichia coli K-12 plasmid F DNA, complete sequence) position: , mismatch: 8, identity: 0.75

tacgttaggcattataacctttgccgatgaga	CRISPR spacer
tagttatggcattatcacctttaccgatgatg	Protospacer
**  *  ******** ******.******* .

19. spacer 3.10|341500|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT matches to NZ_CP048440 (Escherichia coli strain NBRC 3301 plasmid putative_pEcol1, complete sequence) position: , mismatch: 8, identity: 0.75

tacgttaggcattataacctttgccgatgaga	CRISPR spacer
tagttatggcattatcacctttaccgatgatg	Protospacer
**  *  ******** ******.******* .

20. spacer 3.10|341500|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT matches to NZ_CP014271 (Escherichia coli K-12 strain K-12 DHB4 plasmid F128-(DHB4), complete sequence) position: , mismatch: 8, identity: 0.75

tacgttaggcattataacctttgccgatgaga	CRISPR spacer
tagttatggcattatcacctttaccgatgatg	Protospacer
**  *  ******** ******.******* .

21. spacer 3.10|341500|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT matches to NZ_CP014273 (Escherichia coli K-12 strain K-12 C3026 plasmid F128-(C3026), complete sequence) position: , mismatch: 8, identity: 0.75

tacgttaggcattataacctttgccgatgaga	CRISPR spacer
tagttatggcattatcacctttaccgatgatg	Protospacer
**  *  ******** ******.******* .

22. spacer 3.11|341576|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT matches to NZ_CP013915 (Serratia fonticola strain GS2 plasmid pSF002, complete sequence) position: , mismatch: 8, identity: 0.75

ctctcgccctccctcccgttggtcggttggga	CRISPR spacer
cgttcgcactccctcccgttggtcagtcgctt	Protospacer
* .**** ****************.**.*   

23. spacer 3.11|341576|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT matches to NZ_CP013914 (Serratia fonticola strain GS2 plasmid pSF001, complete sequence) position: , mismatch: 8, identity: 0.75

ctctcgccctccctcccgttggtcggttggga	CRISPR spacer
cgttcgcactccctcccgttggtcagtcgctt	Protospacer
* .**** ****************.**.*   

24. spacer 3.14|341804|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT matches to NZ_CP016700 (Lactococcus lactis subsp. lactis strain 275 plasmid p275B, complete sequence) position: , mismatch: 8, identity: 0.75

ctgtcacctatttggtattgatttgaaaaaga	CRISPR spacer
ttaactttgatttggaattgatttgaaaaaga	Protospacer
.*. * .. ****** ****************

25. spacer 3.7|341272|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT matches to CP011076 (Brevibacillus laterosporus strain B9 plasmid unnamed2, complete sequence) position: , mismatch: 9, identity: 0.719

caacaaatgaatgaaacagcaaaacaaagtgt	CRISPR spacer
tccaagataaatgaaacagcacaacaaagtaa	Protospacer
.   *.**.************ ********. 

26. spacer 3.14|341804|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT matches to NZ_CP016739 (Lactococcus lactis subsp. cremoris strain JM3 plasmid pJM3C, complete sequence) position: , mismatch: 9, identity: 0.719

ctgtcacctatttggtattgatttgaaaaaga	CRISPR spacer
ttaactttgatttggacttgatttgaaaaaga	Protospacer
.*. * .. ******  ***************

27. spacer 3.14|341804|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT matches to NC_015902 (Lactococcus lactis subsp. lactis bv. diacetylactis plasmid pVF50, complete sequence) position: , mismatch: 9, identity: 0.719

ctgtcacctatttggtattgatttgaaaaaga	CRISPR spacer
ttaactttgatttggacttgatttgaaaaaga	Protospacer
.*. * .. ******  ***************

28. spacer 3.14|341804|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT matches to KU234532 (Nostoc phage N1, complete genome) position: , mismatch: 10, identity: 0.688

ctgtcacctatttggtattgatttgaaaaaga	CRISPR spacer
gatggaaaaatttgatattgatttgacaaaga	Protospacer
     *   *****.*********** *****

29. spacer 3.12|341652|32|NZ_CP046316|PILER-CR,CRISPRCasFinder,CRT matches to MN783745 (Escherichia coli plasmid pFII-FIB, complete sequence) position: , mismatch: 11, identity: 0.656

aaagcattaaacaaacaacaagagatacaagt	CRISPR spacer
ttgaatttaaaaaaacaacaacagatacatta	Protospacer
  ..  ***** ********* *******