CRISPRimmunity

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Overview of predicted results

Overview of the results

Contig_ID	Contig_def	CRISPR array number	Contig Signature genes	Self targeting spacer number	Target MGE spacer number	Prophage number	Anti-CRISPR protein number
NZ_CP022163	Melittangium boletus DSM 14713 chromosome, complete genome	15 crisprs	RT,DinG,cas3,DEDDh,csa3,WYL,2OG_CAS	3	4	7	1

Results visualization

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CRISPR-Cas detection and classification

Crispr_ID: NZ_CP022163_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP022163_1

214940-215229

Orphan

Consensus_repeat	Method
GAGACGCTGGCCACCACGCGCGGCGAGCTGGACGCCACCAGCCAGACGCTCACCGAGAC	PILER-CR

2 spacers

The CRISPR arrays of NZ_CP022163_1

>merge|NZ_CP022163|1|214940-215229|PILER-CR
GAGACGCTGGCCACCACGCGCGGCGAGCTGGACGCCACCAGCCAGACGCTCACCGAGACCCAGGCCACCCTCGCCGAGACGCAGACGACGCTCGCCTCCACCGAGGCCAAGCTCTCGGCAACCGAGGAGACGCTGGCCACCACGCGCGGCGAGCTGGACGCCACCAGCCAGACGCTCACCGAGACTCAGGCCACCCTCGCCACCACGCAGGACAAGCTCGCCTCCACCGAGGAGACGCTGGCCACCACGCGCGGCGAGCTGGACGCCACCAGCCAGACGCTCACCGAGAC

>NZ_CP022163|1|1|214940-215229|PILER-CR
GAGACGCTGGCCACCACGCGCGGCGAGCTGGACGCCACCAGCCAGACGCTCACCGAGAC	CCAGGCCACCCTCGCCGAGACGCAGACGACGCTCGCCTCCACCGAGGCCAAGCTCTCGGCAACCGAG
GAGACGCTGGCCACCACGCGCGGCGAGCTGGACGCCACCAGCCAGACGCTCACCGAGAC	TCAGGCCACCCTCGCCACCACGCAGGACAAGCTCGCCTCCACCGAG
GAGACGCTGGCCACCACGCGCGGCGAGCTGGACGCCACCAGCCAGACGCTCACCGAGAC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP022163.1\|WP_095975644.1\|199657_200776_-\|DNA-processing-protein-DprA	unknown	unknown	gnl\|CDD\|376794
NZ_CP022163.1\|WP_095975659.1\|223454_224603_+\|cysteine-desulfurase	unknown	unknown	gnl\|CDD\|224029
NZ_CP022163.1\|WP_095975645.1\|200935_202162_-\|LysM-peptidoglycan-binding-domain-containing-protein	unknown	unknown	gnl\|CDD\|212030
NZ_CP022163.1\|WP_095975650.1\|207516_209106_-\|DUF1957-domain-containing-protein	unknown	unknown	gnl\|CDD\|212104
NZ_CP022163.1\|WP_095975651.1\|209116_210700_-\|DUF4912-domain-containing-protein	unknown	unknown	gnl\|CDD\|379808
NZ_CP022163.1\|WP_095975646.1\|202186_202909_-\|tetratricopeptide-repeat-protein	unknown	unknown	gnl\|CDD\|188247
NZ_CP022163.1\|WP_157774690.1\|225817_226738_-\|tetratricopeptide-repeat-protein	unknown	unknown	gnl\|CDD\|276809
NZ_CP022163.1\|WP_095975655.1\|218864_219812_+\|branched-chain-amino-acid-transaminase	unknown	unknown	gnl\|CDD\|235841
NZ_CP022163.1\|WP_095975647.1\|203076_203844_-\|peptidoglycan-editing-factor-PgeF	unknown	unknown	gnl\|CDD\|376831
NZ_CP022163.1\|WP_095975649.1\|205936_207388_-\|trypsin-like-peptidase-domain-containing-protein	unknown	unknown	gnl\|CDD\|273938
NZ_CP022163.1\|WP_095975661.1\|224879_225821_-\|serine/threonine-protein-kinase	unknown	unknown	gnl\|CDD\|270916
NZ_CP022163.1\|WP_095975654.1\|217823_218765_+\|MoxR-family-ATPase	unknown	unknown	gnl\|CDD\|223786
NZ_CP022163.1\|WP_170115419.1\|224606_224774_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095975657.1\|221351_222188_+\|Fic-family-protein	unknown	unknown	gnl\|CDD\|376885
NZ_CP022163.1\|WP_095982491.1\|217420_217639_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095975648.1\|204015_205923_+\|diguanylate-cyclase	unknown	unknown	gnl\|CDD\|143635
NZ_CP022163.1\|WP_095975656.1\|219883_221218_+\|AAA-family-ATPase	unknown	unknown	gnl\|CDD\|223679
NZ_CP022163.1\|WP_095975658.1\|222330_223458_+\|bifunctional-oligoribonuclease/PAP-phosphatase-NrnA	unknown	unknown	gnl\|CDD\|223691
NZ_CP022163.1\|WP_095975652.1\|210833_212945_+\|glycosyltransferase	unknown	unknown	gnl\|CDD\|340825
NZ_CP022163.1\|WP_095975643.1\|197027_199649_-\|type-I-DNA-topoisomerase	unknown	unknown	gnl\|CDD\|235840

Protein	Function_ID	Function_description	E-value
NZ_CP022163.1\|WP_095975644.1\|199657_200776_-\|DNA-processing-protein-DprA	gnl\|CDD\|376794	pfam02481, DNA_processg_A, DNA recombination-mediator protein A. The SMF family, of DNA processing chain A, dprA, are a group of bacterial proteins. In H. pylori, dprA is required for natural chromosomal and plasmid transformation. It has now been shown that DprA is found to bind cooperatively to single-stranded DNA (ssDNA) and to interact with RecA. In the process, DprA-RecA-ssDNA filaments are produced and these filaments catalyze the homology-dependent formation of joint molecules. While the E.coli SSB protein limits access of RecA to ssDNA, DprA alleviates this barrier. It is proposed that DprA is a new member of the recombination-mediator protein family, dedicated to natural bacterial transformation.	2.50026e-73
NZ_CP022163.1\|WP_095975659.1\|223454_224603_+\|cysteine-desulfurase	gnl\|CDD\|224029	COG1104, NifS, Cysteine sulfinate desulfinase/cysteine desulfurase and related enzymes [Amino acid transport and metabolism].	2.30741e-162
NZ_CP022163.1\|WP_095975645.1\|200935_202162_-\|LysM-peptidoglycan-binding-domain-containing-protein	gnl\|CDD\|212030	cd00118, LysM, Lysin Motif is a small domain involved in binding peptidoglycan. LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.	1.38327e-07
NZ_CP022163.1\|WP_095975650.1\|207516_209106_-\|DUF1957-domain-containing-protein	gnl\|CDD\|212104	cd10792, GH57N_AmyC_like, N-terminal catalytic domain of alpha-amylase ( AmyC ) and similar proteins. Alpha-amylases (alpha-1,4-glucan-4-glucanohydrolases, EC 3.2.1.1) play essential roles in alpha-glucan metabolism by catalyzing the hydrolysis of polysaccharides such as amylose starch, and beta-limit dextrin. This subfamily is represented by a novel alpha-amylase (AmyC) encoded by hyperthermophilic organism Thermotoga maritime ORF tm1438, and its prokaryotic homologs. AmyC functions as a homotetramer and shows thermostable amylolytic activity. It is strongly inhibited by acarbose. AmyC is composed of a N-terminal catalytic domain, containing a distorted TIM-barrel structure with a characteristic (beta/alpha)7 fold motif, and two additional less conserved domains. There are other two canonical alpha-amylases encoded from T. maritime that lack the sequence similarity to AmyC, and belong to a different superfamily.	0
NZ_CP022163.1\|WP_095975651.1\|209116_210700_-\|DUF4912-domain-containing-protein	gnl\|CDD\|379808	pfam16258, DUF4912, Domain of unknown function (DUF4912). This family consists of uncharacterized proteins around 160 residues in length and is mainly found in various Clostridium species. The function of this family is unknown.	2.33857e-23
NZ_CP022163.1\|WP_095975646.1\|202186_202909_-\|tetratricopeptide-repeat-protein	gnl\|CDD\|188247	TIGR02795, Uncharacterized_protein_in_oprL_3'region, tol-pal system protein YbgF. Members of this protein family are the product of one of seven genes regularly clustered in operons to encode the proteins of the tol-pal system, which is critical for maintaining the integrity of the bacterial outer membrane. The gene for this periplasmic protein has been designated orf2 and ybgF. All members of the seed alignment were from unique tol-pal gene regions from completed bacterial genomes. The architecture of this protein is a signal sequence, a low-complexity region usually rich in Asn and Gln, a well-conserved region with tandem repeats that resemble the tetratricopeptide (TPR) repeat, involved in protein-protein interaction.	5.97557e-21
NZ_CP022163.1\|WP_157774690.1\|225817_226738_-\|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.	1.91396e-16
NZ_CP022163.1\|WP_095975655.1\|218864_219812_+\|branched-chain-amino-acid-transaminase	gnl\|CDD\|235841	PRK06606, PRK06606, branched-chain amino acid transaminase.	5.9686e-173
NZ_CP022163.1\|WP_095975647.1\|203076_203844_-\|peptidoglycan-editing-factor-PgeF	gnl\|CDD\|376831	pfam02578, Cu-oxidase_4, Multi-copper polyphenol oxidoreductase laccase. Laccases are multi-copper oxidoreductases able to oxidize a wide variety of phenolic and non-phenolic compounds and are widely distributed among both prokaryotes and eukaryotes. There are two main active catalytic sites with conserved histidines that are capable of binding four copper atoms.	9.01772e-80
NZ_CP022163.1\|WP_095975649.1\|205936_207388_-\|trypsin-like-peptidase-domain-containing-protein	gnl\|CDD\|273938	TIGR02037, Probable_periplasmic_serine_protease_do/HhoA-like, periplasmic serine protease, Do/DeqQ family. This family consists of a set proteins various designated DegP, heat shock protein HtrA, and protease DO. The ortholog in Pseudomonas aeruginosa is designated MucD and is found in an operon that controls mucoid phenotype. This family also includes the DegQ (HhoA) paralog in E. coli which can rescue a DegP mutant, but not the smaller DegS paralog, which cannot. Members of this family are located in the periplasm and have separable functions as both protease and chaperone. Members have a trypsin domain and two copies of a PDZ domain. This protein protects bacteria from thermal and other stresses and may be important for the survival of bacterial pathogens.// The chaperone function is dominant at low temperatures, whereas the proteolytic activity is turned on at elevated temperatures. [Protein fate, Protein folding and stabilization, Protein fate, Degradation of proteins, peptides, and glycopeptides].	1.7064e-148
NZ_CP022163.1\|WP_095975661.1\|224879_225821_-\|serine/threonine-protein-kinase	gnl\|CDD\|270916	cd14014, STKc_PknB_like, Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.	3.71239e-85
NZ_CP022163.1\|WP_095975654.1\|217823_218765_+\|MoxR-family-ATPase	gnl\|CDD\|223786	COG0714, COG0714, MoxR-like ATPases [General function prediction only].	2.30526e-40
NZ_CP022163.1\|WP_095975657.1\|221351_222188_+\|Fic-family-protein	gnl\|CDD\|376885	pfam02661, Fic, Fic/DOC family. This family consists of the Fic (filamentation induced by cAMP) protein and doc (death on curing). The Fic protein is involved in cell division and is suggested to be involved in the synthesis of PAB or folate, indicating that the Fic protein and cAMP are involved in a regulatory mechanism of cell division via folate metabolism. This family contains a central conserved motif HPFXXGNG in most members. The exact molecular function of these proteins is uncertain. P1 lysogens of Escherichia coli carry the prophage as a stable low copy number plasmid. The frequency with which viable cells cured of prophage are produced is about 10(-5) per cell per generation. A significant part of this remarkable stability can be attributed to a plasmid-encoded mechanism that causes death of cells that have lost P1. In other words, the lysogenic cells appear to be addicted to the presence of the prophage. The plasmid withdrawal response depends on a gene named doc (death on curing) that is represented by this family. Doc induces a reversible growth arrest of E. coli cells by targetting the protein synthesis machinery. Doc hosts the C-terminal domain of its antitoxin partner Phd (prevents host death) through fold complementation, a domain that is intrinsically disordered in solution but that folds into an alpha-helix on binding to Doc.This domain forms complexes with Phd antitoxins containing pfam02604.	9.05063e-11
NZ_CP022163.1\|WP_095975648.1\|204015_205923_+\|diguanylate-cyclase	gnl\|CDD\|143635	cd01949, GGDEF, Diguanylate-cyclase (DGC) or GGDEF domain. Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesion in bacteria.	3.27123e-61
NZ_CP022163.1\|WP_095975656.1\|219883_221218_+\|AAA-family-ATPase	gnl\|CDD\|223679	COG0606, COG0606, Predicted ATPase with chaperone activity [Posttranslational modification, protein turnover, chaperones].	8.62136e-08
NZ_CP022163.1\|WP_095975658.1\|222330_223458_+\|bifunctional-oligoribonuclease/PAP-phosphatase-NrnA	gnl\|CDD\|223691	COG0618, COG0618, Exopolyphosphatase-related proteins [General function prediction only].	1.50034e-53
NZ_CP022163.1\|WP_095975652.1\|210833_212945_+\|glycosyltransferase	gnl\|CDD\|340825	cd03794, GT4_WbuB-like, Escherichia coli WbuB and similar proteins. This family is most closely related to the GT1 family of glycosyltransferases. WbuB in E. coli is involved in the biosynthesis of the O26 O-antigen. It has been proposed to function as an N-acetyl-L-fucosamine (L-FucNAc) transferase.	6.31926e-42
NZ_CP022163.1\|WP_095975643.1\|197027_199649_-\|type-I-DNA-topoisomerase	gnl\|CDD\|235840	PRK06599, PRK06599, DNA topoisomerase I; Validated.	0

>NZ_CP022163.1|WP_095975652.1|210833_212945_+|glycosyltransferase
MSDLPRLLLCSFDVIPGPSGSSRRVTEYLKALPDRFTVVVLSVKTPDHTHIEKYESARLLRVPVGSGDLASRIQSFERAVRRQLESEEYALAHFTDPFGGYALCELKGDYGYRLVYEAQSFPSQELRYTHPQLEGDRKFLSKVRRQELFCLMNADRVITGSATTGAYIRSLGVPDESVHVVRAPVDLTPYTPEALGVPDGSPMRLMYLGSQVAWQGLAGLLRGLALAVKEVDVRLTLVGARHPDWQPHLEDLVAELGLKQHVEFQPAVSHDDVAKVLTLADVGVLPLDDVDRNRVQGGALAKVSEYLAAGRPVLASDLPVTRELVPASAGVFYPPGDAKALAERILELARDVPRRIALGQQARAAAQKTLDAGRIRGQLLDLYDGLLGKQPVRREKSESGEIQATTIGTPTNRVLALMGNVGAAARPAEGPVEPPAPAMPDTDPGQGMPGNDEPPVVVGMALLEEGFDTRLVKTEPDSYRPEGPPVVMGLPLREPSAPPPPAAPPPAAPPPPVAPPPIPARASMSTRAISTPEPEPVRPPALPSRPSISMEVPRPSRPSIAIPPLPPRGRASSTPRPADPPAPAPAARVPVEEDEPEEISSSHAQALQDDDASLTPRNALPLEEPEEISNEELQETESAQEPPREPPASRLNPWFAQLAHGYCPPEGTRFARHTPPTTFPGRDEQPAAAADAKIQGGARGKPA
>NZ_CP022163.1|WP_095975651.1|209116_210700_-|DUF4912-domain-containing-protein
MADLKSVMVEHLRQLAHTHLERGKGRPGLLGAIVRGVSGLVRRMGLGPPEAPVAASSSDKPEDKGPPATPRRPLPGDDDEKTPVYVPPQPARVVTFPPKPKPHRPSPDEEVTLFGPQAPPASPEVTPTEPSAAEPLVEGFFVARIAGEEEASRHHLTGNSGSPPPGAGHPDSLGGLPREYGDDTLLLLPRDPHTLFVLWDFSAASRQRALAGLESPSAVLRLFNDQGRVLSTIDISLESRGYYLHGLPAAQPYRVEVHFVGRKGGSRRIGPSSNRVFLPPSGPSPDTSVRFLRVPPLTAQRPSPEQKSATPSLRVGPVEERAYITWRRVTLPGSVEAQVMARRQPTRDEPGTAPEGGAPSPEYLHAPRMEGSSERAPAIAAPEGRPWFGSSGPVGSSEQAPGALGQGGDAGQWLGSIGRAGSSEQVPGAEGHWYWSSGPVGSSEQGPGQGEIGSGWSGAAGPAGSSEQGPGAGSAGQGEGQWVWWYGAVGSSGPAGSSEQWVGSYGPAGASEQGALGRPDLPSSPVR
>NZ_CP022163.1|WP_095975650.1|207516_209106_-|DUF1957-domain-containing-protein
MTIGSLALVLHAHLPFVRHPEYEDFLEEDWLYEAISETYLPLLLMFDRLAEEEIPFRLTLTLTPTLVTMLGDELLMGRYARRLDALCELGAREVHRTRNDPIFAPIARFHRDHFESLRTAFHGRYKRDLVGAFRSLQNAGFLEIITCGATHGFLPLMQQTPEAVRAQISVAANHYRLTFGRNAPGIWLPECGYFPGVEKFLAAEHIRYFFVDTHGLTDATPRPLHGPFAPVYTEAGVAAYARDPESSQQVWSAERGYPGDPVYREFYRDIGWDLELDQVRPFVQPTGGRKNTGFKYYRITGKTQDKQPYAPDVARERAAVHAGNFLFNRQRQLEWLAGKVHGRQPVVVAPYDAELFGHWWFEGPWFLDALLRKVAREQDTFRLVTPSDDLAAFPENQVATPPLSSWGAGGYAHMWLEGANDWIYRHLHHCARLMVALAKDFPNPSTLQRRVLNQAARELLVAQSSDWAFIMKTGTMVEYAVRRTREHLEHFLSLHEQVTHGRIDEASLARLEGSLNLFPEMDYRVYRPL
>NZ_CP022163.1|WP_095975649.1|205936_207388_-|trypsin-like-peptidase-domain-containing-protein
MNKRMTLPRGAVAGALIVVLPALAPAQTAAPPASGTLQPATREAQALPSLAPLVESVKSAVVNVDVQSKSGASEEYEGMRNPSFGSEDPWSGRRREQPIRQGTGSGFIIDPKGLVLTNNHVVEGAVAIRVRLDDGRSFSAEIVGRDPLTDVALIQLKKADKLPTVKLGDSDAMRVGDWVVAIGNPFGLASSVSSGILSARARNIHAGPYDDFLQTDAAINPGNSGGPLFNLKGEVVGINTAIVGGGTGIGFSVPSNLVKALLPQLEKDGAVTRAWLGIGIQDLNAELAQALKLPVNDGAIVNLVNDDSPAGRAGVRTDDVIVAIDGQKVSSGGELTRSVALKKPGSTSTVELFRDGKKQAVKVQLGTRPDLENRGVRPRRGEESDEQSSRARVGLSLNNVDPRLTQRMGLKTSQGALITEVQPGSPAERAELEPGMVVVEADRKPVASAEALAALIRKAPSGSTVLLRVVLPNGRMLRALPIP
>NZ_CP022163.1|WP_095975648.1|204015_205923_+|diguanylate-cyclase
MASGSRTVGRKLLWSIALPGLLAALLGLGHFWREARLATRDATHDEALVLAEFLGAAFRLPTPAGAPPHSPVAALLGAPSRLIDSTAELNVLSPDGHIRWSPRPREVGQRHPAAALLTQPGPQWARSDAHQTEVLRPLGDTSCEGCHPGAGEKPVGMLHLRVAEPLVHRELTDALGGALVAVLVLGIILILAIGVSLHFFLTRPLRRLTAAMRRAEEGDLLVRAEAGGTDELARLGSAFNAMLARLTSMKVEEIDTHRDLQVTKSKLSAKEELEERMADLALLFDVAHSLNSTLELSELLTRITQLVPERLHIPDFSIMLVNADGQLEVKSTFPADPKLEGVAFQVGEGCCGRAAATQRGVYVPDVAEPSSGFTQRGLRPEPDQGAMLCVPMVHTNSVLGVLNFRRPEVASFAPEELELLTAVADQVATAVKNALLHTEAVRLTLTDPLTGVPNRRHLFSRLELEVARSQRFGTPMSILMVDIDHFKKLNDAEGHRAGDEALRRVCDTLRGRVRKVDTLARYGGEEFMLVLSNVSKEDAFDVAEKLRRAVAESPLLAAPTQPGGHITVSIGVATLPTDAPAQDTVVDCADAALYASKRGGRNRVTSYAPGMEVHPNRERGLSKPHDPSAAQVAKA
>NZ_CP022163.1|WP_095975647.1|203076_203844_-|peptidoglycan-editing-factor-PgeF
MIAPAPSFLCSALLPVPHGFTTREGGVSEGVHASLNLGFAVGDARERVEENHRRLAARVGVELGALHTVKQVHGDRVLEAEEGGGDSLRPTEGEADGVWTERPGHWVGVGTADCVPVLLVDPDRRRVAAIHSGWKGTDARIVARAVEALVARGSRADRLLAAVGPCIQRCCYVVSEDLGERFTARFGPEVIHREGAEVRLNLSLAVSRTLRDAGLVAERVDVLPECTACDAHRFFSHRRDAGRTGRHLNFVVNRF
>NZ_CP022163.1|WP_095975646.1|202186_202909_-|tetratricopeptide-repeat-protein
MVALQAEMRAMRESQSRLEKRLERMELHASVRQARASQATAESTTSPEAPPAPAFTTPELTVVKLKPRVEPAPRLPVQVAVVEPSSDDMEMFISNGSSDEPDEAVDIGPANSPDNAVLEATFEQAMAALRTGNVEGGVNNLLGFAEKNPRHARADNALYFSGLGQMGLKDHASAAKTFERLIERYPAGDAVLDGMLRLAECRLRLDQKDDARALYTRILTQFPGTAAATQAEQRLASLSH
>NZ_CP022163.1|WP_095975645.1|200935_202162_-|LysM-peptidoglycan-binding-domain-containing-protein
MRSRILSSLLFATVLAPPVWAQNADDAQQEPETTDETQGSDVVDEPSRPARSGQLTLPPGTQGRESAPGERHTVERGDTLWDLSQRYLGSPWYWPKVWSYNPEIANPHWIYPGNNVRFFPAGEEVPSRVEAGTGPVSSGNSDSDFSEVEPAVAGVEVSGDLSYKPKAARTVTTLAFVTTRELDEAGRIEGSSTGAEMLSFPDVTYVRFKRKTDAKVGEKYVVFHTAQQVMHPVTGKPVGYLTEFVGTVRVTALGDNYVKAQVMDTWDPVTRGDLVGPYGDRMSEAVVPRRNEKEIKGVVVTSLVPYQTLTAEHYFLVIDKGSADGVQPGNVFTITRQGDPARERVLKLELPGTKKNQPAPFPTENIALCLVTEVKDRASNCVLTKSIQEVGPGDEAIMRLESAPTALR
>NZ_CP022163.1|WP_095975644.1|199657_200776_-|DNA-processing-protein-DprA
MVDVTADRFTAEQRALLALWTVPGLGPRALEHLRAYAQGALARLVACPVRDWVSEAPLPPPVRRRLAELSSLESLATRVLERCARVGMGVAFVGERAYPALLADTVDAPPLLFYRGQVGPPRRRVAMVGSRQPDQGFLPFARTFARQVAEGGVGVVSGAAAGVDRACHWGAMDAGGETWAFLGSALDALDPAQAKLLPHFLARGGVFFSELPPGVRASTTTFPRRNRLIAGASDAVLVLRAGLGSGSLYTAEAGRARGRPVLALPGDVVNEGAAGCNALIRDGHARACLSVQEVWRTVGVDPQRAVPPGEGSWEELSVEARGTYEVLKRVPRSFDEVLVDSQLSPAALLSALVELELSGFVIQHPGRLFERV
>NZ_CP022163.1|WP_095975643.1|197027_199649_-|type-I-DNA-topoisomerase
MATRTKKTATAGEQEVEETATSGKAAKKPAARKKTTAKKTTAKKASAKKAAAKKTASRGKGKKGELATVEASAEEEGDEAPSRRGKGPHYLVVVESPAKAKTIKKYLGSGYTVKASVGHILDLPKSKMGVDLEKEFEPQYEVIKGKEKVLGELKKAAQGVDKVFLATDPDREGEAIAWHINQQLRHPDSYRVMFNEITKPAIQEAIANPRQLSQDNYDSQQTRRILDRLVGYQISPILWKKVRRGLSAGRVQSVAVRLICERESEIKAFVPQEYWTLDALLEGPSGPPPFKAKLSRVDGKKVDLRDAATTRGLVEELRNASFTVTKVDKRERRRNAPAPFITSKLQQEAANRLHFTAKKTMALAQRLYEGVLLGEEGQTALITYMRTDSTRLSDQAVAGVRDFILQTYGQDYLPEAPVVYRTKKGAQDAHEAIRPTSLEYPPAKVKAAFDAMNDDMAADMFRLYELIWNRFVACQTKPAVYDQTSADITSGRATFRASGSTLKFPGYLAVYGASLTPEEEAAQEKARAAGDETADDGVGDLPVLNDGDALSLQKLVDEQHFTQPPPRFSEATLVKELEERGIGRPSTYAAILSTIQDKKYAEKIEGRFRPTDLGLICNDLLVKHFPHELDVTFTASMEEKLDQISEGEANWKTVLKDFYAPFKETLEKAETEMRDVKREEVKTDVACEKCGNIMVIKWGKMGHFLACSNYPDCKNTKDFKRDAEGKIVIVEEETTDELCENCGKNMVVKRGRFGKFLACSGYPDCKTSKPISIGVTCPDCKQGYLTERRSRFGKIFFGCNRYPDCKFAAWDRPLAEACPQCQSPYLLQKFSKRDGPFVACPNKECDYRRQIEEPGAVPAASGTSPSPDASSAA
>NZ_CP022163.1|WP_095982491.1|217420_217639_-|hypothetical-protein
MSWLWRMVLVAVVTLVPGAFLLLVSYLATRTMWEHWRLAQQESLTSGVPVSFREVLATVHVKDLVQQARAAL
>NZ_CP022163.1|WP_095975654.1|217823_218765_+|MoxR-family-ATPase
MSPPSPSTAAHFLANVEDAATRLEQVGYLASPEISTASFLADRLQKPILVEGPAGVGKTELAKALAQALGRRFIRLQCYEGLDEAKALYEWEYAKQLLYTQLLKDKIGEMVHGASTLGEAADRLATSDAVFFSERFLLPRPILQSLLSDMPALLLVDEIDKADPEFEAFLLEVLSDNAVTIPELGTFSARHVPRVVLTSNNARELSDALKRRCLHLHIDFPDRERELRILRRRLPDVSRTLLEQVVEAVAAIRELDLKKSPSISETIDWAQSLALLNAETLSADLVAATLNLVLKHEGDIEKAKGQLARIAQG
>NZ_CP022163.1|WP_095975655.1|218864_219812_+|branched-chain-amino-acid-transaminase
MSSTSPNVLRSDEIWLDGKLVKWEEGQVHIMTHALHYGLGAFEGIRAYRTHDGRLAVFRLREHIDRLFDSTHICMMKMPFTREQVTEGCLELLRTQKELFANGAYLRPIAFMGDGAMGLGAINPTRVAITAWDWGAYLGDKGIREGIRAKVSSFTRMHVNVNMVRGKISGQYVNSILAKREAVLGGYDEAILLDISGFVAEASGENIFLVNKKGVIKTPPLSSPILDGITRDSVLRILRDSGREVEEVTVTRDALYISNEVFFTGTAAEITPVREVDNRTVGEGKPGPITQYVQETYFRAVRGLEPRYAHWLTYI
>NZ_CP022163.1|WP_095975656.1|219883_221218_+|AAA-family-ATPase
MRPEYVAPPNPFGLENPAILDIAPAEPKSLEETGLKMGLLSDIALRYLYYQGTATGMDIAQEMRLPWPAVIEAVVEFLTSEKLVDLRGGKGFGRASVDFVLSERGREYARGAIERSTYVGPAPIPIEQYNALITAQTEESPVISREDLVMGLSHLTVSADLMDKLGPAVNSGRSLFLYGPPGNGKTSLAEAISRMFGGEVFIPHCLEIDNQIIKVFDALNHIPVRLESERDAAGRRQTFEMDHRWQLCRRPAVVVGGELTLETLDLIYSPTARFYEAPFQVKANGGMLLIDDFGRQKVHPTDLLNRWIVPLEKRVDFLTLHTGKKFEIPFDQLLVFSTNLDPKELVDEAFLRRIKYKIEVTNPDEDVYRDIFANVCEAAGIPYVEQAVTYLFEHYYRPRNMQLRACHPRDLVQLIRDAARYRQIPPALSKDLLDQACEVFLVSL
>NZ_CP022163.1|WP_095975657.1|221351_222188_+|Fic-family-protein
MKERYQEIDEKNEALRDYLGIYKDKGREFLERFEMSWIYHDAALEGTVYSQQELVSALFPERAAMDPAMIPVVLEVRNHKAACDYLREEAAATGKKQAQITLTTIKRIHDLVCGNTPEALSARSNMERRDRSEKELAKERERSGYRKDMPLHRTYFHEIAQPAKIQPALEKFVDYTGSAEYREFHPIKQAAVAQHRFMQIFPFTENSGKVGRMLTNLVLLRNGYMPAIIHSIDRQRYYESLRGAEGVFRTLLMDAIENSLDNGIKYFKDMARRYKAIN
>NZ_CP022163.1|WP_095975658.1|222330_223458_+|bifunctional-oligoribonuclease/PAP-phosphatase-NrnA
MPATPTANSRRTPGGGESAEPPSPRLATLPARARLERLIQVAKGHKKALVLTHDNPDPDSIAAGVALAQLLKERAGVEEARVGYSGLIGRAENIAFVKVLRLPVVPIAQLDLDEYDLLALVDTQPPTGNHAVPPRLRREVDIVIDHHPLRDESLEAPFADVGGDYGATSTMVAQYLRAARLEPSTEVATALFYGVKADTRDLGRETTPTDIDTYLWLFPRADKQMLGQIEHPELPARYFQMYHTAFERAKVYGDTAIVTDLEEVYSPDMVAEVAERLMFLEGMKWSLAYASFRNQLFLSLRVKDRRMNAGRLIREICEDYGGSAGGHGSMAGARIPLSGRAHQRKALKRELVRRFLEAFGVADERPVALLSAPSP
>NZ_CP022163.1|WP_095975659.1|223454_224603_+|cysteine-desulfurase
MIYWDHNAAAPVRPEVATLLARAFSEGGFGNASSVHRGGREARGRLDGARARVARVLGCEPKEVCFVGSGSEADALALKGVWLARKEPGRRRVVSSAIEHPAVLGALKQLEALGADVVRVRPDRDGQVPLEALREALTPETLLCSLMWANNETGVVQPVEELSRECRRRGILFHTDAVQAAGKLPMTLREVDAELLSLSAHKFGGPAGAGVLVVRKGVDVQALTPGHQEAGLRGGTQNIPYAEAFALALELAHQEQPAHEERLRRLRVGFEREVRERLPDVTVNGAGAPRVPNTSNLTFHGADGEALLIALDLEGICASSGAACASGTLSPSHVLLAMGLTPAQAHGTLRFSMGPTTTPEEVERVVEALVQQVPRIRALGEG
>NZ_CP022163.1|WP_170115419.1|224606_224774_-|hypothetical-protein
MANQKDDKQPREQEEETRKAGTDSPDESHEGKQGYGQPPKEVGDKPLPDQKWGGK
>NZ_CP022163.1|WP_095975661.1|224879_225821_-|serine/threonine-protein-kinase
MNSSAPSRIPRILGNYEILSALGKGGMAEVFRARVRSGPREDWIVALKRLLPALTQDPASLALFASEARLTKLLDHPNIVQVLDVGSVADQHFIVMDLVDGRDLGHILRRCKLRGIHLPLDFAIYLCRVLLEALAYAHSRTGDQGEALGIVHCDISPSNLFISRLGDIKLGDFGVARLRVDGVLQGGEVLGKPYYLSPEALQGSISPQVDLWAATVVLYELLTLQRPFTGATPDEVFTKIIYRDYLAPSLIRPAIPEALEEIIHRGFSSDVSERFPSAESFAEALAPHYDERVGTPLAIAAVVRGLFGTTDAK
>NZ_CP022163.1|WP_157774690.1|225817_226738_-|tetratricopeptide-repeat-protein
MASVSRTIGLTALIAIVPATLRAESLPKGSYQTDVWGRVELNTEHDRVVGYAAEGAACGLAPRAKVLEGEWQGRVLVGQITVCLQGASCPAQASLPLLAFLGSEDGTFTTYVRPQAGCMAPGAGLGGLVVFSPAAPGEGTPVQSGPAVGGRVKRNPQAAKVALDRGDQLMKEKNWSAAITEFERSIALNEQSWAAFLSLGTAQLMRNEPRAAIEALDKARVINKREPLIYYHLACAYSRLGDKKQALSNLEQAVAFGLAINPEPEDDGLSKLLGSDLGSSARYTLLMQRAANNSKASAGRRQSPGP

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Crispr_ID: NZ_CP022163_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP022163_2

357298-357403

Orphan

Consensus_repeat	Method
GGCGTCGCGAAGCGCGCGGTCGACG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP022163_2

>merge|NZ_CP022163|2|357298-357403|CRISPRCasFinder
GGCGTCGCGAAGCGCGCGGTCGACGCGGGGATGTGCGTCGCGCCCAGCCCGAGGTCGTCCTCACGCTCCGTGGCGGGAGGCGGCGTCGCGAAACGCGCGGTCGACG

>NZ_CP022163|2|1|357298-357403|CRISPRCasFinder
GGCGTCGCGAAGCGCGCGGTCGACG	CGGGGATGTGCGTCGCGCCCAGCCCGAGGTCGTCCTCACGCTCCGTGGCGGGAGGC
GGCGTCGCGAAACGCGCGGTCGACG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP022163.1\|WP_095975752.1\|369353_371471_-\|serine/threonine-protein-kinase	unknown	unknown	gnl\|CDD\|270916
NZ_CP022163.1\|WP_095975751.1\|367508_369329_-\|serine/threonine-protein-kinase	unknown	unknown	gnl\|CDD\|270916
NZ_CP022163.1\|WP_179956438.1\|349897_351235_-\|undecaprenyl-phosphate-glucose-phosphotransferase	unknown	unknown	gnl\|CDD\|274396
NZ_CP022163.1\|WP_095975749.1\|365161_366706_-\|bifunctional-phosphoribosylaminoimidazolecarboxamide-formyltransferase/IMP-cyclohydrolase	unknown	unknown	gnl\|CDD\|234854
NZ_CP022163.1\|WP_095982506.1\|345864_346431_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095975744.1\|358476_359577_-\|LptF/LptG-family-permease	unknown	unknown	gnl\|CDD\|367632
NZ_CP022163.1\|WP_095975739.1\|346441_347734_-\|AHH-domain-containing-protein	unknown	unknown	gnl\|CDD\|379603
NZ_CP022163.1\|WP_095975748.1\|364912_365158_-\|zinc-ribbon-domain-containing-protein	unknown	unknown	gnl\|CDD\|372687
NZ_CP022163.1\|WP_095975747.1\|361952_364991_-\|tetratricopeptide-repeat-protein	unknown	unknown	gnl\|CDD\|274350
NZ_CP022163.1\|WP_095975750.1\|366814_367309_-\|DNA-binding-protein	unknown	unknown	gnl\|CDD\|223642
NZ_CP022163.1\|WP_095975738.1\|345626_345875_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095982509.1\|354941_355598_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_157774702.1\|353788_354874_-\|UvrB/UvrC-motif-containing-protein	unknown	unknown	gnl\|CDD\|236123
NZ_CP022163.1\|WP_095975745.1\|359573_360686_-\|LptF/LptG-family-permease	unknown	unknown	gnl\|CDD\|367632
NZ_CP022163.1\|WP_095975741.1\|351514_352636_-\|glycosyltransferase	unknown	unknown	gnl\|CDD\|340833
NZ_CP022163.1\|WP_157774701.1\|347788_349795_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|377474
NZ_CP022163.1\|WP_095982508.1\|352719_353772_+\|glycosyltransferase-family-4-protein	unknown	unknown	gnl\|CDD\|340838
NZ_CP022163.1\|WP_095975737.1\|344290_345583_-\|AHH-domain-containing-protein	unknown	unknown	gnl\|CDD\|379603
NZ_CP022163.1\|WP_095975746.1\|360682_361951_-\|phosphoribosylamine--glycine-ligase	unknown	unknown	gnl\|CDD\|234856
NZ_CP022163.1\|WP_095982510.1\|371586_371874_-\|hypothetical-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_CP022163.1\|WP_095975752.1\|369353_371471_-\|serine/threonine-protein-kinase	gnl\|CDD\|270916	cd14014, STKc_PknB_like, Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.	4.53804e-102
NZ_CP022163.1\|WP_095975751.1\|367508_369329_-\|serine/threonine-protein-kinase	gnl\|CDD\|270916	cd14014, STKc_PknB_like, Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.	5.65256e-99
NZ_CP022163.1\|WP_179956438.1\|349897_351235_-\|undecaprenyl-phosphate-glucose-phosphotransferase	gnl\|CDD\|274396	TIGR03023, Sugar_transferase., Undecaprenyl-phosphate glucose phosphotransferase. This family of proteins encompasses the E. coli WcaJ protein involved in colanic acid biosynthesis, the Methylobacillus EpsB protein involved in methanolan biosynthesis, as well as the GumD protein involved in the biosynthesis of xanthan. All of these are closely related to the well-characterized WbaP (formerly RfbP) protein, which is the first enzyme in O-antigen biosynthesis in Salmonella typhimurium. The enzyme transfers galactose from UDP-galactose (NOTE: not glucose) to a polyprenyl carrier (utilizing the highly conserved C-terminal sugar transferase domain, pfam02397) a reaction which takes place at the cytoplasmic face of the inner membrane. The N-terminal hydrophobic domain is then believed to facilitate the "flippase" function of transferring the liposaccharide unit from the cytoplasmic face to the periplasmic face of the inner membrane. Most of these genes are found within large operons dedicated to the production of complex exopolysaccharides such as the enterobacterial O-antigen. Colanic acid biosynthesis utilizes a glucose-undecaprenyl carrier, knockout of EpsB abolishes incorporation of UDP-glucose into the lipid phase, and the C-terminal portion of GumD has been shown to be responsible for the glucosyl-1-transferase activity.	0
NZ_CP022163.1\|WP_095975749.1\|365161_366706_-\|bifunctional-phosphoribosylaminoimidazolecarboxamide-formyltransferase/IMP-cyclohydrolase	gnl\|CDD\|234854	PRK00881, purH, bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; Provisional.	0
NZ_CP022163.1\|WP_095975744.1\|358476_359577_-\|LptF/LptG-family-permease	gnl\|CDD\|367632	pfam03739, YjgP_YjgQ, Predicted permease YjgP/YjgQ family. Members of this family are predicted integral membrane proteins of unknown function. They are about 350 amino acids long and contain about 6 transmembrane regions. They are predicted to be permeases although there is no verification of this.	6.40744e-60
NZ_CP022163.1\|WP_095975739.1\|346441_347734_-\|AHH-domain-containing-protein	gnl\|CDD\|379603	pfam14412, AHH, A nuclease family of the HNH/ENDO VII superfamily with conserved AHH. AHH is a predicted nuclease of the HNH/ENDO VII superfamily of the treble clef fold. The name is derived from the conserved motif, AHH. It is found in bacterial polymorphic toxin systems and functions as a toxin module. Like WHH and LHH, the AHH nuclease contains 4 conserved histidines of which, the first one is predicted to bind a metal-ion and the other three ones are involved in activation of a water molecule for hydrolysis.	1.59377e-25
NZ_CP022163.1\|WP_095975748.1\|364912_365158_-\|zinc-ribbon-domain-containing-protein	gnl\|CDD\|372687	pfam13717, zinc_ribbon_4, zinc-ribbon domain. This family consists of a single zinc ribbon domain, ie half of a pair as in family DZR, pfam12773.	3.47717e-10
NZ_CP022163.1\|WP_095975747.1\|361952_364991_-\|tetratricopeptide-repeat-protein	gnl\|CDD\|274350	TIGR02917, TPR_domain_protein, putative PEP-CTERM system TPR-repeat lipoprotein. This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.	4.16309e-19
NZ_CP022163.1\|WP_095975750.1\|366814_367309_-\|DNA-binding-protein	gnl\|CDD\|223642	COG0568, RpoD, DNA-directed RNA polymerase, sigma subunit (sigma70/sigma32) [Transcription].	3.50442e-07
NZ_CP022163.1\|WP_157774701.1\|347788_349795_-\|hypothetical-protein	gnl\|CDD\|377474	pfam05157, T2SSE_N, Type II secretion system (T2SS), protein E, N-terminal domain. This domain is found at the N-terminus of members of the Type II secretion system protein E. Proteins in this subfamily are typically involved in Type 4 pilus biogenesis, though some are involved in other processes; for instance aggregation in Myxococcus xanthus. The structure of this domain is now known.	6.44528e-16
NZ_CP022163.1\|WP_157774702.1\|353788_354874_-\|UvrB/UvrC-motif-containing-protein	gnl\|CDD\|236123	PRK07883, PRK07883, DEDD exonuclease domain-containing protein.	2.58142e-53
NZ_CP022163.1\|WP_095975745.1\|359573_360686_-\|LptF/LptG-family-permease	gnl\|CDD\|367632	pfam03739, YjgP_YjgQ, Predicted permease YjgP/YjgQ family. Members of this family are predicted integral membrane proteins of unknown function. They are about 350 amino acids long and contain about 6 transmembrane regions. They are predicted to be permeases although there is no verification of this.	6.60101e-79
NZ_CP022163.1\|WP_095975741.1\|351514_352636_-\|glycosyltransferase	gnl\|CDD\|340833	cd03804, GT4_WbaZ-like, mannosyltransferase WbaZ and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. WbaZ in Salmonella enterica has been shown to possess mannosyltransferase activity.	2.11129e-138
NZ_CP022163.1\|WP_095982508.1\|352719_353772_+\|glycosyltransferase-family-4-protein	gnl\|CDD\|340838	cd03809, GT4_MtfB-like, glycosyltransferases MtfB, WbpX, and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide.	1.08061e-84
NZ_CP022163.1\|WP_095975737.1\|344290_345583_-\|AHH-domain-containing-protein	gnl\|CDD\|379603	pfam14412, AHH, A nuclease family of the HNH/ENDO VII superfamily with conserved AHH. AHH is a predicted nuclease of the HNH/ENDO VII superfamily of the treble clef fold. The name is derived from the conserved motif, AHH. It is found in bacterial polymorphic toxin systems and functions as a toxin module. Like WHH and LHH, the AHH nuclease contains 4 conserved histidines of which, the first one is predicted to bind a metal-ion and the other three ones are involved in activation of a water molecule for hydrolysis.	2.27224e-22
NZ_CP022163.1\|WP_095975746.1\|360682_361951_-\|phosphoribosylamine--glycine-ligase	gnl\|CDD\|234856	PRK00885, PRK00885, phosphoribosylamine--glycine ligase; Provisional.	0

>NZ_CP022163.1|WP_095982509.1|354941_355598_-|hypothetical-protein
MVIRPDEKQSVQLDYGDGKRFVKVAEPPWVISGYHFLEPRFYNKSMNHSFRGLDMGLYSEVELDEEKNTCAVRCGDRSIPFSRVDAEQAEKMVAEATFEPNPQKYVPYALLRDQSGRYYLVEKGFLPEDRSYRVSIGPKGNLKQQQMKDVVSDSKGEIFSTKKGDLRLLVDREAPSSWIEKKKKIELRAVPIEENLPLIYNELGVYTGARLGTPCDDQ
>NZ_CP022163.1|WP_157774702.1|353788_354874_-|UvrB/UvrC-motif-containing-protein
MSASRVEQLREHVRARAENRPGVYRMSGPSGEVLYVGKSVRVRTRLLSYFRAPRGEKGAEIIGHAHGVEWEYTPSEFAALLQEFRSIKRWRPPFNVEHKRDNLLCFLKLTREPVPRLLVASQVINDGAEYFGPVRGRRRASEAVRAVGDLLELRDCSSDTPMRLADQIELFRVQEDPRCMRGQLGRCLSPCAGGCTRTEYEARVALARDFLNGLTDQPLVLLRERMALAARRLQFEHAAELRDRSESLERVRDALLQVGQFVERLSFVYTVPGEAGEDRVYIIRRGSVRWESAAPVSPEERHVLEAKVREVFEKPEPKMVGLRAHEAQEVLLVAKWFRLHPEELERTVPVARAEPEVLAAS
>NZ_CP022163.1|WP_095982508.1|352719_353772_+|glycosyltransferase-family-4-protein
MVRGRLHGIARYALELACRLPELAPDLRFAGLTGPEGLPTNLGTLTPRLPLHRCPVGFLSPLEQPALAASLVRLDPDLFHATSFSVPALWPGRLVATLHDANHLVLAEEYGTSRRVYYRLIVGPRAKRAQALITVSEFSRDELARELGLSPYRLQVIPNGVDARYQPQMASELKAFRERHQLPPRFLLAVGNTKPFKNLGMLADVAEELPEPLVLLAGERAAWELGFPDGTRELSNMPEEDMPRLYGAATALLLPSRYEGFGLPALEAMACGTPVVAARATSLPEVVGEAALLLPPDDASAWKDAAQRLVRDDALRRSLGEKGRERAGLFTWDDCARRTLATYRRALEAR
>NZ_CP022163.1|WP_095975741.1|351514_352636_-|glycosyltransferase
MKVALVHDWLVTQRGGEHVLEALCELFPRADIHTLVHRPGAVHPRIEARPIHTSVLQHVPRIHKLYRHFLPVLPQVIESMHLADDYDLVISSSHCVAKGIRKPPGARHLSYVHAPMRYMWDLFDDYFGPGRASLPVRMAAHAVRPMLQKWDRESTAGVDRVLVNSQHIARKVKRFWGRDATVVYPPVALERFCQHPLTGLGQGGYYLWLGAFAPYKRLDIALEAFRHLDAPLWVVGTGQEAAKLTSGPLPPHIRFLGSVSDEALTGLYRDARALIFTPEEDFGIVPLEAQASGRPVIAYGRGGALETVGPRTGVFFDAQTPEALADAVRRFEAWEPGFQPADARAQAERFSRAAFQRAVMAEVDALMGRHAAP
>NZ_CP022163.1|WP_179956438.1|349897_351235_-|undecaprenyl-phosphate-glucose-phosphotransferase
MLTGAFVLAYVTRFDGPIPVMYGMPAWEETLLSLATVLLVFPITYRQARLYATNRARTHIGEVFEVFKATIMATLIVVALTYFTRERYSRLMLAFFSVYAFVGVSSARLVLRGVLSAVRRRGYNLKSILVIGAGELGQRVIETVEGHKELGFRVVGLLSLHPDKVGQQVLGVPVVGHVKDVDTVLDARSVDQVIIAVPLEDQAAVKPLMEQLALRTVDVKVVPDLYQYVTLYGGLEEFGGLPIISLQGDPMAGWNMVAKRVFDILFALVALFVSAPFMLLVAIAVKLTSRGPLLYAQERMGMDGQTFHILKFRTMRTDAESSGALMASKDDPRRTPIGTFLRKYSLDELPQFFNVLTGDMSLVGPRPERPVFIEEFKRQIPRYHLRHKVKAGITGWAQINGLRGQTSIQKRIEYDLYYIENWSLLMDLKILVRTALGGFLSKNAY
>NZ_CP022163.1|WP_157774701.1|347788_349795_-|hypothetical-protein
MVDQLGAHLVRKGLLTQAQLDEALKSRLIYGGSLGTNLVELGMLDLATLGQALSDTYYFPLVTEAELEAVPAETVALLKPELARQHLAFPLALEGRRLRMALAEPQDPRHVDSLAFATGMRVVPSIIPEPRLLQVLEKHYGLPRPVRPARSGQPRPGAGQGNSPGVALSPSPRPAPAVQAVPPAAVARPAPAKPPPAPVAIPLAVAPRSVSAPPTGNVLVAAAPRPAPTVALAAGTAPAFSFGAAAPGRPPGLMPRTPAGASPRAARNRLVGGAPLVSSVRSMPTPLTVVQPPREPVAVPPPPPPSTPPVQEVQEVAPPSPTPPPAPPEALIPVAQVLAEPEPEPVKTPGVERLADDTPIEALTESAERDIPFEDALADILRTAEPISDAWEPEPEEEVPSALVRAAGTPPPFHIPEDSAPKEDRRGRRPRAMLELPAESASASPEALKMSSDLEYIESDSGSSSWASRCIEVDFSSQEPELVAPAPVVDFIPDWDPSTEFSEDGSPGVQWVQLPEAVEALQRAKTCGELGQALLSYAQGRFPRGFLLGETFGSVRVGQAFGPGSDKPDVVALQVNLAVPSILSQAESDGRPVVSSKPLSQTDEVLFAALGETYSNLMAAPIRVNQRAVGFLVIDGGPAPFGPGELDEMERLLAAASEAYGRLRGTSV
>NZ_CP022163.1|WP_095975739.1|346441_347734_-|AHH-domain-containing-protein
MRVFGLAALLLLASACATTRVVNLDTGQRDTIVYRPGESEPITIDEREFKSAVARLVLDMNLKVVLDESAQVGPRSLLASAGGIVDGVQGRKETASSSRYCQRQSDPSTCLSLFAGEFTLGPMERRMMALSFALDTVWEGVEDVVKDLANPEALRAMVVSIIGTSLVMLVAPEPITKFIAMGLTASLIAYLGVGPVWNLGQGFLRLMAESKNARDFAQLEESGHRFGKVLGGNGARVLVLVAMTAIGGKSAMATQGPKLPGAAQAAMRARVEGEFELSGVLAGQVRSISLPSAGVLNVALAPTAVAAVAMGTGGVIQGDPDGDIHHICTDKNEVSDASGGPWTPLFETFFEQAGMKLSDVANQVRIKGHKGPHPREYHEEVYSRIEQATLGCRSAAECRRALVDVLTKIARELTTTGTKLRKIITRNPDA
>NZ_CP022163.1|WP_095982506.1|345864_346431_-|hypothetical-protein
MRYFNLKIDVYVPGRWYMAAPTMPNGQQLDDLWVFTRGEPIEAPARLRVPLHRPGKPLDFTTAGMGSTPILSERAAAVFREMASHDTQLFPVDVEGQTEPYQLLVVARTVRCIDDAACTEARYFTPEDGRPERVGEYQVVSGLRIDKSKVGDARVFKAWGWHPALIVDEKIKSALERTGIVGGYFDEV
>NZ_CP022163.1|WP_095975738.1|345626_345875_-|hypothetical-protein
MKCELDESGRYPKEARRFTLETGRPERVGEYQVVSGLRIDKSKVEDARVFKLWGWRPALIVDGEIKLALEEAGSVGGYFEEV
>NZ_CP022163.1|WP_095975737.1|344290_345583_-|AHH-domain-containing-protein
MRLLRITALLLLTSACATTRVVTLDTGQRAPIIYRPGESAPVTIGEQEFKSAVAQLILDMDLKVVHEASEPFDSRSLLASARGIVDGARGQKASAASARHCQRRGNPAMCSSLFAGEFTLGVMERRMMALSFALDTVWEGVEEVVKDLANPEALRAMVVSIIGTSLVMLVAPEPITKFIAMGLTASLIAYLGVGPVWNLGQGFLRLMAESKNARGFAELEASGHRFGKVLGGNGARILVLVAMTAIGGKSAMAAQGPKLPGAAQAAMRARVEGGFELSGVLAGQVRSISLPAAGVLNVALAPTAVATVAMGTGGVIQGDPDGDIHHICTDKNEVSDASGGPWTPLFEPYFNRAQMKLSDVANQVRIKGHKGPHPREYHQAVLKRIEQKMEDCKGATECRAVLIETLAQIARELTTAGTELRKLVTRNPNA
>NZ_CP022163.1|WP_095975744.1|358476_359577_-|LptF/LptG-family-permease
MSGTLFRYVVRTYLGFAVGILAALVAVFLVVDFVDRARNYTGEGWVWNVLVLYANKALLAVQQLGPAALLLAAGASVSALRKRGEVTAMRALAFGPKALYLPVAACVAVACTGLIAFDEWVAVKASRTVEEITTQRFNRWGDWGLYNNPKQWFRKGDQIFYLRGGSAEEGFENVAILTVTPDFRLARRLDAKFMRPLEGTRWRLEGVVDRTFTPDGQSRVSESAEGEYDLGANAKTFRIRPGRPEQMRLAVLREQIRTRGEVGLDSRQFSLALHNRFAYPLAGFPAALLAVGLALRPSRKGHLTVAIVEGLLVCVTMWSLMVVARTLALSERLSPAVAAWLPTSLLVVGAFLLWLRGEGRLGRGGG
>NZ_CP022163.1|WP_095975745.1|359573_360686_-|LptF/LptG-family-permease
MKLLSRYLLKELVVPLVVWVAFLFLLLFVMQFLRGTDVLLGSAVTLVDMGSLLLFLAPHFLMMALPIAFLLAILLGLGRLAEDRELTALQALGIGPVQLLAGPLFVGVVLSALMVLLTSTAEPWGLTRVKEFVAEIIKKNVVGDVKPGVFYEDLSNLTLYAERVEGTDRRWTHVLLNDDRDPAAPLLMLAQTGRVNTNTSGQVLTLVLEDGEAHRSNRGTSSYSVVSFQEAEIAVGVEGSLGRRNRFRSPKEELTPRELLQAADEAERTGGDPRSFLMALHNRLGNALAPLSFALLGTPLAIGRRQGGRAWGYLLTLGGYVLFYLLMRLFEQMGQQGRMPVLLAGQLANVIFCAAGLVAMYRVNRSGTVR
>NZ_CP022163.1|WP_095975746.1|360682_361951_-|phosphoribosylamine--glycine-ligase
MKVLLLGSGAREHALAWKLAQSPRLTQLLLGPGNVGSARVGTPVALEAESPGAVVALARREAVDLVVVGPEAPLVAGVADALAEAGIPCFGPVAAAARIEGSKAFAKEIMIDAGVPTAGYRVFTDLAEAEAYAVAQGRIVVKADGLAAGKGVIVAHDAEAAREAVRSVGAMGSAGQRLVLEELLEGEEVSVIALCDGERYVLLPPAQDHKRVGEGDTGPNTGGMGAYAPAPFLSPAQLAEVGESVIAPTLKVLRARGTPFRGALYAGLMLTRNGPKVLEFNARFGDPETQVLMMQLAEDVLPLLDACARGQLEQRPLAVHPGASVGVVLAAQGYPEAPRKGARIEGVDAVPSSCPVFVAGVAERDGAWLTAGGRVLTVCARGADLAEARAQAYAAVESIRFEGMHFRRDIGAKGLRAPAVTP
>NZ_CP022163.1|WP_095975747.1|361952_364991_-|tetratricopeptide-repeat-protein
MAAKPAAPAPKPAAPAPKPAALARPLTPSASLSDELFGDLGDLAPPDSSESSPGSLLDDLASPGGAPAASKDSLFGDLADLTASSPSNPVLDTEDPRPNTPGYSLPSGDLLFDDIAQPPPPAPAPKPAAPMQARPAPQPKPAVAAFPDPSDDALFDFNAPPGYSPPPPVPDPAPAPQPKPAAAAFPDSSDDALFDFNAPPGYSPPPPVEEPAPASASAEADPLMDFFGAPPTSASPGVAAPAPAPVAPAPAPTPRGCRECGKPLVDPFDQALGACEDCRQRAQKPVPAPVPENRSVEVIDLPPMDSSMSASAAAPVAAPEGGGARAPAPALPAEPRSAARPVVARTGVAVSASSGRSKGPLVAVLVLLLLAGAGGAAYFFVPEVRALVGQPAGSGAGASGGGGASASAALPPAIEAVLPRWQLMFVDAQEGDSKQLIEQGQTLLAKDQRFAYLQAAESFQRAVLLDPRSDVAIGGYVQAISLGSGSFMDDATFQEARMLIEAAEGRAQRAPDLLVAHANLLLARSGDEQNLDQARKLAEEVLNAPAGSAAPKAEAHLLLGRTFLGSSRELATQHFESALAIAPDLQRVHYYRALADETSGDYSLAIGRLQKRLEQDPEHWETRTTLARIYMEVGEVPLARQLYEARLKSAPNDIQAQLALAVMRYQVEGGVPAALSSLRGLLRNRDKYDERDVAELLLHLSAAERLSNNLEASAKAGREALQLVKNNPPVHLQLLLVALARKDAAEASTHLATLKGHLGDLSLEKMLEGRIRLLERKPAEAIAPFTEAAKLDPRRTDALLLAGVAAAQEGRRDESFRYFAQAIQADPLRLTPRPVVTPFYLRNAEFLVGLEGAVAATSRGEDDLLPHLYEGLLRFHLGDASNAEKMFKKVAEVDATHAPSFALRALLAMGRKDMNSARTYAARAVDGGRQVAIAHLAQGLVLAESKQVEPAKRSLRDAIQLAPRLYAAEVKLDELEAASGSAPVKERLVRLLGLDPSYLPAKRVLYQLDKRG
>NZ_CP022163.1|WP_095975748.1|364912_365158_-|zinc-ribbon-domain-containing-protein
MRISCQKCAAAYAIDDRVITPKGVRAQCPRCRHLQLVKREDSPAPAAPPLRRPNPRWPPNPPPRRPSPRPPRPSPPHWRAP
>NZ_CP022163.1|WP_095975749.1|365161_366706_-|bifunctional-phosphoribosylaminoimidazolecarboxamide-formyltransferase/IMP-cyclohydrolase
MLALLSVSDKRGLVPFAQGLVRLGFELLSTGGTLAALQAAGVPARKVSEHTQSPEILGGRVKTLHPRIHGGLLGRPELESDRAEMAAHGITPISLVAVNLYPFRQTVASGASEAEVIEQIDIGGPAMVRASAKNFRHVTVVVDPEDYGAVLAELEASRATSEETRRRLMRKAFAHTAAYDASISGWLSEQAAEPFPQELTLGFQKVQSLRYGENPHQRGAFYREHAAPAEPTVAFSRVLQGKELSYNNILDLDAALGLVLEFPEQPCAVIIKHNTPCGVALDDALVKAYRTARAIDEVSAFGGIVAFNREVDPATAEALAETFLEAVIAPSYSAEAQKVLSAKKNLRLLEAGPALASPTARPRAQLEARSVSGGLVVHDKDSVEPPLDWKVVSKRAPTAEEEKALRFAWRVCKHVKSNAIVFAEGQKLLAAGGGQTSRVESAKIATARGGEALRGSAVASDAFFPFRDGLDEAARAGATCVIQPGGSVRDAELIAAADEHGMAMVLTGVRHFRH
>NZ_CP022163.1|WP_095975750.1|366814_367309_-|DNA-binding-protein
MSEVKQQRPEEEAPEEAEGGAERRRSKTMSRKEMARDLRRRRLTGQVDPEEGDLLQAVDSQRPKTRADCVNGARPCLFVSCKHNLYLDVNPETGSIKLNFPDKEIWELEHTCALDVAEKGGITLEEVGAIMNLTRERIRQVETRGLLKLREATEAEPPVSARKP
>NZ_CP022163.1|WP_095975751.1|367508_369329_-|serine/threonine-protein-kinase
MTLEAGTPIGKYVVKRKLAEGGMAEIYLATARGAEGFEKEVVIKRVRSFLSDDEGFVRMFINEARLVSRLNHANVVQIFDFDKHEDSYYLAMEYVRGSSLWELRKRCREKGIRMPPVLVAHVGAQVAAGLHYAHRTKSPEGEPLGLVHRDVTPHNVLLSFDGAVKLTDFGIAKAGNRLTQPGVLKGKFAYMSPEQARGEEVDARTDIFALGVVLWEMLTGGRLFDGDSEVAVLRAVRESLIVPPARLNPDVPEALDNVILTALEREPEARYQSAGEMERALAQCVLRSATSVDDTDVGTFVRRLFDVPLTQFMPAPALLQDRSRPRSGGVPPVGMEPTAPSPERVEAPAASTAEPPASESASVAPPLRESTAVLPGRTPALPYERVERLSVPEDSLVSASTLVLSRDGKTGEGPAAVPAEPAVERVSGNSPSPEPAPVAPVPPAPTPDSRRGRTPVWVGAGVAFLVLAGGVTAWRMSSAPASTPPAQVEARSPSVPVTPPSSTPPARPEIPPAAVAEQEVKREEAPAPAAPVVQAKGYLTVQAVPYADLYIDGKLYKRELQQPLSIELAPGTYQLTFKHPSHTRNFPVTITADSKVTKKFNVPRKK
>NZ_CP022163.1|WP_095975752.1|369353_371471_-|serine/threonine-protein-kinase
MSIENYGKYQLLKRLAMGGMAQIYLAREEGDPQLLVIKRILPHLAENEEFVQMFLDEARIAARLDHPNIVQIFDLGSQDDSFFIAMEYIHGEDLRRIWKAAERGGQLIPVPLVCRILSEACAGLDHAHKQLDASGKPLNIVHRDISPQNILLTFEGRAKVVDFGIAKAADQATETRSGVLKGKYSYMSPEQAAGQRVDRRSDIFALGVVLYELLTGVRLFKRANDIITLQAVAECDITPPSQLNARVPKDLDPIVMKALARDPAHRYSEALQFQRALEGWLDAQPQPSSTAAVSAYMKDLYAARLAEEARLGDVLVEEEGMSPPGGSKASLRAAKSSVERSLAERSLGERPGDRAPADKATVDNTMAAPRQLEAAAPPSTRTPSRPSRSESRPNGLERKRTVDLRRNPSDAVLDAPSESLSETPLLRPSLPRQRAIPPPAAELSGMSETIEDVDQSEPSVAPEPRKSNRGVLVGVVALVLLGLVLGGLWALRSEPGPPVPVASVQKEPEPKPLPPPEPEPTPTPTPTPTSTPPPPAESIVARTEIPQPVPVRVTLSAKPGQASLTVDGQLHSKSTVVLSAMPGQELVVRVEAPRHRAISRKITVGEGPTQEESLELEPLPKERPEPRPSPPPVAAVETRKGTVRFAVTPWADVSCGGRNLGSTPLPDVSLVAGVYECRFSNPEKGTRTQRIEVKPNTHTRVVVKF
>NZ_CP022163.1|WP_095982510.1|371586_371874_-|hypothetical-protein
MRVIKGGGQRRRDEPLASRDAVARVLMEAGVDLLLRRITPTRAAEIERKVDRVLELFDRVDAAPVLMPVLRRHLDDLEALMRETREVRAPVRRGG

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Crispr_ID: NZ_CP022163_3

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP022163_3

717449-717544

Orphan

Consensus_repeat	Method
GGCTGCGGCGTGGAGATGAGCGGCACCGCG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP022163_3

>merge|NZ_CP022163|3|717449-717544|CRISPRCasFinder
GACAGCGCCGTCGAGTTGAGCGGCTGCGGCGTGGAGATGAGCGGCACCGCGCCCGTGGCGTTGAGGGAGGGCGGCGTGGCGATGAGGGGCACCGGC

>NZ_CP022163|3|2|717449-717544|CRISPRCasFinder
GACAGCGCCGTCGAGTTGAGCGGCTGCGGC	GTGGAGATGAGCGGCACCGCGCCCGTGGCGTTGAGG
GAGGGCGGCGTGGCGATGAGGGGCACCGGC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP022163.1\|WP_095976013.1\|731750_734744_-\|PAS-domain-containing-protein	unknown	unknown	gnl\|CDD\|226702
NZ_CP022163.1\|WP_095976008.1\|725796_727626_+\|M4-family-metallopeptidase	unknown	unknown	gnl\|CDD\|341060
NZ_CP022163.1\|WP_170115434.1\|716932_717301_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095976001.1\|713498_714311_+\|DUF3108-domain-containing-protein	unknown	unknown	gnl\|CDD\|378635
NZ_CP022163.1\|WP_095976006.1\|721566_723732_-\|excinuclease-ABC-subunit-UvrB	unknown	unknown	gnl\|CDD\|235395
NZ_CP022163.1\|WP_095976007.1\|723791_725474_-\|M20/M25/M40-family-metallo-hydrolase	unknown	unknown	gnl\|CDD\|349910
NZ_CP022163.1\|WP_095975999.1\|712306_712972_+\|YggS-family-pyridoxal-phosphate-dependent-enzyme	unknown	unknown	gnl\|CDD\|143483
NZ_CP022163.1\|WP_095976012.1\|731272_731734_-\|response-regulator	unknown	unknown	gnl\|CDD\|381108
NZ_CP022163.1\|WP_095975996.1\|708941_710507_+\|peptidylprolyl-isomerase	unknown	unknown	gnl\|CDD\|372652
NZ_CP022163.1\|WP_095975998.1\|711710_712310_+\|septum-formation-inhibitor-Maf	unknown	unknown	gnl\|CDD\|376812
NZ_CP022163.1\|WP_095976009.1\|727626_728769_-\|bifunctional-chorismate-mutase/prephenate-dehydratase	unknown	unknown	gnl\|CDD\|223155
NZ_CP022163.1\|WP_095976004.1\|718965_719484_-\|DUF507-family-protein	unknown	unknown	gnl\|CDD\|367914
NZ_CP022163.1\|WP_095975995.1\|707852_708710_-\|rod-shape-determining-protein-MreC	unknown	unknown	gnl\|CDD\|237560
NZ_CP022163.1\|WP_095976000.1\|712978_713182_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095976005.1\|719622_721560_-\|excinuclease-ABC-subunit-UvrC	unknown	unknown	gnl\|CDD\|234792
NZ_CP022163.1\|WP_095982552.1\|714347_716027_+\|DUF4091-domain-containing-protein	unknown	unknown	gnl\|CDD\|379121
NZ_CP022163.1\|WP_095976002.1\|716055_716943_+\|DUF3108-domain-containing-protein	unknown	unknown	gnl\|CDD\|378635
NZ_CP022163.1\|WP_095976011.1\|729677_731276_-\|PAS-domain-containing-protein	unknown	unknown	gnl\|CDD\|223715
NZ_CP022163.1\|WP_095976010.1\|728775_729612_-\|prephenate-dehydratase	unknown	unknown	gnl\|CDD\|237013
NZ_CP022163.1\|WP_095975997.1\|710573_711665_-\|sensor-domain-containing-diguanylate-cyclase	unknown	unknown	gnl\|CDD\|143635

Protein	Function_ID	Function_description	E-value
NZ_CP022163.1\|WP_095976013.1\|731750_734744_-\|PAS-domain-containing-protein	gnl\|CDD\|226702	COG4251, COG4251, Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal transduction mechanisms].	9.52691e-64
NZ_CP022163.1\|WP_095976008.1\|725796_727626_+\|M4-family-metallopeptidase	gnl\|CDD\|341060	cd09597, M4_TLP, Peptidase M4 family including thermolysin, protealysin, aureolysin, and neutral protease. This peptidase M4 family includes several endopeptidases such as thermolysin (EC 3.4.24.27), aureolysin (the extracellular metalloproteinase from Staphylococcus aureus), neutral protease from Bacillus cereus, protealysin, and bacillolysin (EC 3.4.24.28). Typically, the M4 peptidases consist of a presequence (signal sequence), a propeptide sequence, and a peptidase unit. The presequence is cleaved off during export while the propeptide has inhibitory and chaperone functions and facilitates folding. The propeptide remains attached until the peptidase is secreted and can be safely activated. All peptidases in this family bind a single catalytic zinc ion which is tetrahedrally co-ordinated by three amino acid ligands and a water molecule that forms the nucleophile on activation during catalysis. The active site is found between two sub-domains; the N-terminal domain contains the HEXXH zinc-binding motif while the helical C-terminal domain, which is unique for the family, carries the third zinc ligand. These peptidases are secreted eubacterial endopeptidases from Gram-positive or Gram-negative sources that degrade extracellular proteins and peptides for bacterial nutrition. They are selectively inhibited by Steptomyces metalloproteinase inhibitor (SMPI) as well as by phosphoramidon from Streptomyces tanashiensis. A large number of these enzymes are implicated as key factors in the pathogenesis of various diseases, including gastritis, peptic ulcer, gastric carcinoma, cholera and several types of bacterial infections, and are therefore important drug targets. Some enzymes of the family can function at extremes of temperatures, while some function in organic solvents, thus rendering them novel targets for biotechnological applications. Thermolysin is widely used as a nonspecific protease to obtain fragments for peptide sequencing. It has also been used in production of the artificial sweetener aspartame.	3.12184e-124
NZ_CP022163.1\|WP_095976001.1\|713498_714311_+\|DUF3108-domain-containing-protein	gnl\|CDD\|378635	pfam11306, DUF3108, Protein of unknown function (DUF3108). This is a bacterial family of putative lipoproteins. Structure 3fzx, the first structural template for this large family including several homologs in the human gut microbiome and in metagenomic datasets, folds into a beta barrel that topologically looks like a small-scale porin (such as FepA). Bacteroides fragilis glyA is a putative exported protein, and this fold is of the YmcC-like type, with a predicted signal peptide SpI cleavage site AGAMA\|QNQDC, and a Phobius server prediction of non-cytoplasmic localization for amino acids 21-236. The possibility of it being a membrane protein can be ruled out by the hydrophilic nature of the solvent exposed surface outside the barrels. Analysis of sequence conservation suggests that an area near Glu172/Trp206 is potentially interesting. These two residues are also conserved in Dali hit Structure 2in5, a hypothetical lipoprotein classified as a new YmcC-like fold in SCOP (SCOP:159271, with a 12-stranded meander beta-sheet folded into a deformed beta-barrel) despite large structural differences between the two structures, suggesting similarity in function.	9.75456e-47
NZ_CP022163.1\|WP_095975999.1\|712306_712972_+\|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.	4.51282e-109
NZ_CP022163.1\|WP_095976007.1\|723791_725474_-\|M20/M25/M40-family-metallo-hydrolase	gnl\|CDD\|349910	cd05660, M28_like_PA, M28 Zn-peptidase containing a protease-associated (PA) domain insert. Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This subfamily is composed of uncharacterized proteins containing a protease-associated (PA) domain insert which may participate in substrate binding and/or promote conformational changes, influencing the stability and accessibility of the site to substrate.	2.05096e-85
NZ_CP022163.1\|WP_095976006.1\|721566_723732_-\|excinuclease-ABC-subunit-UvrB	gnl\|CDD\|235395	PRK05298, PRK05298, excinuclease ABC subunit UvrB.	0
NZ_CP022163.1\|WP_095976012.1\|731272_731734_-\|response-regulator	gnl\|CDD\|381108	cd17557, REC_Rcp-like, phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and similar domains. This family is composed of response regulators (RRs) that are members of phytochrome-associated, light-sensing two-component signal transduction pathways such as Synechocystis sp. Rcp1, Tolypothrix sp. RcpA, and Agrobacterium tumefaciens bacteriophytochrome response regulator AtBRR. They are stand-alone RRs containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. Also included in this family us Methanosaeta harundinacea methanogenesis regulatory protein FilR2, also a stand-alone RR. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.	9.22757e-65
NZ_CP022163.1\|WP_095975996.1\|708941_710507_+\|peptidylprolyl-isomerase	gnl\|CDD\|372652	pfam13624, SurA_N_3, SurA N-terminal domain. This domain is found at the N-terminus of the chaperone SurA. It is a helical domain of unknown function. The C-terminus of the SurA protein folds back and forms part of this domain also but is not included in the current alignment.	1.70927e-38
NZ_CP022163.1\|WP_095975998.1\|711710_712310_+\|septum-formation-inhibitor-Maf	gnl\|CDD\|376812	pfam02545, Maf, Maf-like protein. Maf is a putative inhibitor of septum formation in eukaryotes, bacteria, and archaea.	9.63113e-91
NZ_CP022163.1\|WP_095976009.1\|727626_728769_-\|bifunctional-chorismate-mutase/prephenate-dehydratase	gnl\|CDD\|223155	COG0077, PheA, Prephenate dehydratase [Amino acid transport and metabolism].	6.75875e-92
NZ_CP022163.1\|WP_095976004.1\|718965_719484_-\|DUF507-family-protein	gnl\|CDD\|367914	pfam04368, DUF507, Protein of unknown function (DUF507). Bacterial protein of unknown function.	6.68929e-42
NZ_CP022163.1\|WP_095975995.1\|707852_708710_-\|rod-shape-determining-protein-MreC	gnl\|CDD\|237560	PRK13922, PRK13922, rod shape-determining protein MreC; Provisional.	4.91626e-73
NZ_CP022163.1\|WP_095976005.1\|719622_721560_-\|excinuclease-ABC-subunit-UvrC	gnl\|CDD\|234792	PRK00558, uvrC, excinuclease ABC subunit UvrC.	0
NZ_CP022163.1\|WP_095982552.1\|714347_716027_+\|DUF4091-domain-containing-protein	gnl\|CDD\|379121	pfam13320, DUF4091, Domain of unknown function (DUF4091). This presumed domain is functionally uncharacterized. This domain family is found in bacteria, archaea and eukaryotes, and is approximately 70 amino acids in length. There is a single completely conserved residue G that may be functionally important.	1.55091e-17
NZ_CP022163.1\|WP_095976002.1\|716055_716943_+\|DUF3108-domain-containing-protein	gnl\|CDD\|378635	pfam11306, DUF3108, Protein of unknown function (DUF3108). This is a bacterial family of putative lipoproteins. Structure 3fzx, the first structural template for this large family including several homologs in the human gut microbiome and in metagenomic datasets, folds into a beta barrel that topologically looks like a small-scale porin (such as FepA). Bacteroides fragilis glyA is a putative exported protein, and this fold is of the YmcC-like type, with a predicted signal peptide SpI cleavage site AGAMA\|QNQDC, and a Phobius server prediction of non-cytoplasmic localization for amino acids 21-236. The possibility of it being a membrane protein can be ruled out by the hydrophilic nature of the solvent exposed surface outside the barrels. Analysis of sequence conservation suggests that an area near Glu172/Trp206 is potentially interesting. These two residues are also conserved in Dali hit Structure 2in5, a hypothetical lipoprotein classified as a new YmcC-like fold in SCOP (SCOP:159271, with a 12-stranded meander beta-sheet folded into a deformed beta-barrel) despite large structural differences between the two structures, suggesting similarity in function.	2.22801e-40
NZ_CP022163.1\|WP_095976011.1\|729677_731276_-\|PAS-domain-containing-protein	gnl\|CDD\|223715	COG0642, BaeS, Signal transduction histidine kinase [Signal transduction mechanisms].	2.65944e-42
NZ_CP022163.1\|WP_095976010.1\|728775_729612_-\|prephenate-dehydratase	gnl\|CDD\|237013	PRK11898, PRK11898, prephenate dehydratase; Provisional.	4.56141e-121
NZ_CP022163.1\|WP_095975997.1\|710573_711665_-\|sensor-domain-containing-diguanylate-cyclase	gnl\|CDD\|143635	cd01949, GGDEF, Diguanylate-cyclase (DGC) or GGDEF domain. Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesion in bacteria.	1.05632e-58

>NZ_CP022163.1|WP_170115434.1|716932_717301_-|hypothetical-protein
MTTLALARRAAPATLRRVSADPLRQSMEHLERRLPRRADATVLLDFLEDDLREGLDALGDVESHFTELLAALRPESLSPLALVEAGDEALVLKRLALLEDVVMRLRRRMSQAAGMMRQTPTT
>NZ_CP022163.1|WP_095976002.1|716055_716943_+|DUF3108-domain-containing-protein
MNTMRSALAPLLFCLSSTAWAQIPDTDPAEEHKAQPAAPGKTASVPVCTQTLPPLRAPLAFASGEMLEFDLDAMGATAGKMSMQVQKKQNGSLPVQVKVQTNSFFSKVRRVDATAMSYLHPKTLRSFRYTEDATENEVHRTVDVAFNPTKRSVRVDYVLRGKSGRNDYSYEHEGLDVAGSIYMMRQLPMKEGLPVCFDVYGVRRMWRMAGTVLKREHVSLPIGEFEAWHLSGTAVRLDRPSMTREVHVWISDDERRLPLAALGSIDLGTVRATLTSFSRPGEKLQQAEGKEALKW
>NZ_CP022163.1|WP_095982552.1|714347_716027_+|DUF4091-domain-containing-protein
MVAAGAVGWLLVGVLAGAPEPRVVSALEKVRPEALPKGEKQARLSLARGECEGVQVVLPPGASRVQAAPLTLSGPGKPLAAHLWREAFLDVKTASNSQGGTGLWPDPLVPVETPSGDKKAPTVLYVELCAPEAQRPGTYRGALKLKADGAAVAAVPFTAEVQPFALPATSSLPNSFGVSLYSIAKGHGVKPESPEAQGLLRDYVTALLTHRVSAHGMSMNPPPVRFDDGGAQVDFRAYDAEVSSFLEGTALPSGARFTTLDVRDSKAARTDAEKAAYYRALAAHAKEKGWRAQLFFYAKDEPKPEDVALVRTQALRVRASGKDVPVLVTAPLDESLRDSADILAPTLNCFFPRPGPQTCRNVVPLQTLRGKLAPQVKVWWYQSCNSHGCTGGAAEDASVEKAYSGWASYMVDHPAPLNRAMGPLAFLTGVDGELYFDTVFAYNTKDPWTDLFEFGGNGDGTFFYPGTPSRPGFTSHQPVLSLRLKHLRDGLEDYEYLRLLESLGEKTFAQEAVRRLVRSGYDVQRDVRQWEQVRQEMTARLRQRWEAVEEAKRSGVRSK
>NZ_CP022163.1|WP_095976001.1|713498_714311_+|DUF3108-domain-containing-protein
MHKQRKGMFTGMMLGLLGSGVALAQGETPSAFSPGEQASYRVQYLGITAGTAQVTVGAPMRQWGKDVWPIVSLARSEAVAGVWPVKDKYVSYWDFNALRVLGSDMMEDQNHKRRRVRVKLHDDGKSALVVKQKEGEAPSERQHDILEGALDVAGATFALRNRTLEVGREYAYPVFTGSKSFLMKAKVEAKETLSTRQGKQEVYRLRVYTEFSGNLASKRDLVAWLTADARHLPVRLEADLALGSLVAELTDYQQGKVLTPKPAVTAQNGF
>NZ_CP022163.1|WP_095976000.1|712978_713182_-|hypothetical-protein
MPLDYYDDDEKDSGSKASRKDFDCPECNANNPLDDALKDGQELHCNYCGCEFLVKVGDNGRFKFREI
>NZ_CP022163.1|WP_095975999.1|712306_712972_+|YggS-family-pyridoxal-phosphate-dependent-enzyme
MSGLAERLAEVRARMAAACARVGRAPESVTLVAVSKLKPGALIREAYAAGQRDFGENYAQELRDKAVELADLEGLRWHAIGPLQTNKVKYVAKVAHAYHALERLEVAQELSRRRLDAPLPCQVEVNVGGEASKSGLSPEALGPFLDAVRALPGLRVEGLMSLPPPTEDEAVARGYFRTLRELARKHGLPGLSMGTTHDFELAIEEGATLVRVGTALFGERG
>NZ_CP022163.1|WP_095975998.1|711710_712310_+|septum-formation-inhibitor-Maf
MHTPVGQTQLVLASASPRRRELLGQLGLAFEVSAADIDETPRAGETAGAYVLRLAQEKARTVATRRPGTWVLAADTTVALEDTLLGKPHDAAEARRMLGLLSGRTHEVHTGVALAGPGAEHATVVRTRVTFRSLSPEEITWYAATGEPLDKAGSYAIQGKGGFLVASVEGSPTNVIGLPLGETLELLGRAGLALPWSAR
>NZ_CP022163.1|WP_095975997.1|710573_711665_-|sensor-domain-containing-diguanylate-cyclase
MNPADLLAAMTRTVEQLAAYNDIAKALTSTLELREVLSLMMEKVRSLLRPRNWSLLLQDERTGKLYFEIAVGEGAEVLKGLQLAPGEGIAGTVFSTGTARLVADVSHDPAFAARFDAASTFRTRSIVAVPLIARGQVLGVIELVNGITDRPFTQEDLMALTAIADFAAIAIENARNFRRVQELTIKDEHTGVYNARHLRAQLEHEVRRSQRFHHPVSLVFLDLDHFKSINDAHGHLVGSAVLREVGDLLMSCCRQLDYVFRYGGDEFALLLVETGTDGAVTTATRIRDAFRSQRFQQVAELDLQVTASLGVATYPEHALSAVDLVRAADFAMYAAKARGRDDICVAVPQMERPGGRVPRLDKK
>NZ_CP022163.1|WP_095975996.1|708941_710507_+|peptidylprolyl-isomerase
MGSLDPRKVFSLLFIIAIAVVFTVQFGPGNNGFANTGTGAAPSAAAVVNGKEIPANEFLREYAGQLQYLRQQGQPITEAVARQFGLPQTVLDRLVNTELLSQAAENHGVRASDEEILKILQRSPEFQKDGQFDYATYTQVLRDYMRQSPADYEESLRKRLTAQKMLGVVQNGVVVSDDEVRARFEKEGNQARVVFARFLPSMYAGKVTEPTAADLTAFKQGHEKEIKEYYETNRFLYQQPERIRASQVLLKVAPDATPEQKAQVLARAQALLKEIEGGKDFAEVARTSSEDPGTQANGGDLGWVERGNWEPALADAAFSLEAGKVTQPVETKYGVHLVKVEEKKPVQDRSLEQVQDEIATSLYKKDKAQALARAEADKALATVKGGKSITDLFPPEKEGQPALLRFETETRPEAVQTDTFTAAATNVPHLGPAPDLVTAIFATQGPTRLEQPYAVGEGFVIAQVTERQLPDDAKFAEKKTELRQQAQQAKQYEVADSFLKSLRKSGKVETNPTVLDQAVGG
>NZ_CP022163.1|WP_095975995.1|707852_708710_-|rod-shape-determining-protein-MreC
MLSLLKRYRTLLIVGALLLYPFGSFLTTGRRGREPNVVDRAVIGLTAPVQRGLVGLIDGVKAVVYGYLDLREVRQENEQLRAENLQLRATVQALGEARVENDRLRGLLGYSEASPGPDIAARVIGVNPVSKLLSVRINRGESDGVFRGMSVVTPDGIVGQVVRTTGGWADVALVTDAQSRVGVRVQRSRSRGTAAGAGKGPLQLENMLRTEDIQEGDLIITSGTDGVYPPGLVVGKVTHLEKTEHGMFLGGDIVPAVDTTRLEEVLVRGNPFGTMAQSQGEGGTR
>NZ_CP022163.1|WP_095976004.1|718965_719484_-|DUF507-family-protein
MRLYPKVIPIISREVVQRLMQDGDVEVEQMRVADAEMDLSAIMREYLANEERVNQATREALERRGYDYSKFNQVKREMADVRGFKMGDEGIEYVINQMIEFLLISRNVEEVFAADNVLRQKIHQHMKRHLDVDEEIDKEARARLRHLQEGTSAFDIEYNKTVEQIRRARGLI
>NZ_CP022163.1|WP_095976005.1|719622_721560_-|excinuclease-ABC-subunit-UvrC
MDAKLEAKLDALPTEPGVYLMKDRRGEIIYVGKAINLRNRVRSYFTRTGDTRAFVSLLDKFLADIETVLVHNEKEALLLENELIKKHKPRFNVLLKDDKQYISLRLDKTQTYPRLEVVRRYEKDGARYFGPYSSASAIRETLRVINRYFHLRTCTDHVLANRKRPCLLHQIGRCPAPCVYPVPPEDYKKSVDEVVLFLEGKAGELVDGLRARMKQASSELKFEEAARIRDQLRAIERSLERQKVATTDFKDQDVFSFHREGDRLLVYVLYVRQGRLNGGQAFPLGSQEFPDEELLPSFVNLYYDQGNFVPEEILLPLDIEEREGLEALLSERKGDRVRVMVPKRGEKRDLVEMAQKNAEQAAIERRRTKDETESVLRRLQERLSLKRMPRRMECFDISHFQGASIVASQVAATEGEIDKSRYRRYRIKTLEKQDDFASMHEVISRRLKRGQEEGDLPDLLVIDGGKGQLASALAAAKDVGVEEVDIISLAKSRDEEVHDRDEESARSPERVFIPGRKDPIVLRQNSAELYLLARLRDEAHRFAITFQQKSMRRGSFTSVLDDVPGVGAARKKLLLRHFGSLKRVREASIEDLVEVLGPTVAERVHAALHGHPEEDDVDPIREASLADAGDLIDEKSEEGSPPGSP
>NZ_CP022163.1|WP_095976006.1|721566_723732_-|excinuclease-ABC-subunit-UvrB
MPEFQIVSDYKPQGDQPRAIGELTEGILRGDRYQTLLGVTGSGKTFTMANLIANVKRPTLLIAHNKLLAAQLYGEYKALFPHNAVEYFVSYFDYYQPEAYIPTSDTFIEKDSSVNDEIERMRHSATHSLRTRDDVLIVASVSCIYGLGTARSYVDLAVTVNVGAELGRDAFIRRLVESQYERNDLDFHRGTFRARGDTVEVFPAYEEERAVRVSFFGDEVEKITEFDPLRGVTLGALEKVVIFPASHYVTEADTRKSALQTIRDELSERLQQFQREGKLLEAQRLEQRTMYDLEMIEQIGYCNGIENYSRHFSGRRTGEPPPCLIDYFPRNMLVLIDESHQTVPQIGAMYRGDRARKETLVDHGFRLPSALDNRPLKFTEFEEMVQQAVFVSATPAEYEFQKSNGVVVEQIIRPTGLTDPEVEVRPARNQVDDVLEEVRERVTKNERVLVTTLTKRMAEDLTEYLTDVGVKVRYLHSDIGAIERTAIIRDLRKGEFDVLVGINLLREGLDIPEVSLVAIFDADKEGFLRSHVSLIQTIGRAARNMNGHVIMYADGMTDSMRLAIEETDRRRAVQKAYNAEHGITPQAVKSHILDLSEQLYDAENPNALPLAADAANDALEPKEIQRLIAETTKEMQHYADEMEFEKAARMRDQLLLLKDMDLGIKPPSRALLRAPAKTDDEPKAGTPGSRGAKGRRGGGKAKSGGGGPPHGKTGIGPRKSR
>NZ_CP022163.1|WP_095976007.1|723791_725474_-|M20/M25/M40-family-metallo-hydrolase
MKHSLVVLASAWMLLPGVALAQPSLPAEKLAAKSLEARGLRAHIDFLASDLLEGRGPGTRGDALTQLYLSTQFELLGLKPGAPGGGYLQPFELVGMTGHPDTMTFTAGAESMPLRFHEDFIASAGHQGARSELNGSELVFVGYGIQAPEYQWDDFKGVDLRGKTLLILNNDPEDDPTLFEGKARLWYGRWDYKYEQAKKQGAAGAILVHTTASAGYPWQVVQTSWTGEQFELPTPPETGALLQVKAWTTEEATHRVMTLAGHDLDALRLAARSRDFQPVALGVKVSTRFTSQVHRRATANVLGLLPGGDPTLSREVVLYTAHHDHLGMKADAKPGEDAIYNGAVDNASGVAALLEVARAFTRLPKAPPRSILFAAVAAEEQGLLGSSYLAEHLPVPAGRVAADINVDGLNIHGRTRDVTVIGLGKSSLDKPLTALVRAQGRVVKPDQLPDRGFFYRSDQFSFAKKGIPTVYFSSGMDFIDRPAGWGKARRERWERENYHQPSDELGPDADLSGAVEDTRLFFLLGAQVARTREAPRWNKGDEFEAPRLRSLETLKSEGAK
>NZ_CP022163.1|WP_095976008.1|725796_727626_+|M4-family-metallopeptidase
MQISNKQTPVSAPAVASTPATPAVPATPAAAPAAAPKATSGFAQDSSFATSAAKSPAVALSAAHVASAAKSTGPLALESKEAQSAIQKSVDFLQQNSPTQRGIVPSAPVSASVKPNQVFTDELGMTHVRLDRQSEGVKVFGEQVISHLDKDGKVADVTGTLSNVPAGLGSSPVKLTAQDALAVAQKAFGQESTRAPTSERVIVKGNDGQYHAAYHVKLDKLSDFKAGEEPRRMNYFVDAHSGELVKSFDQMGGFAHEVEAAKARASKPTTPSTPTTPNSPSQPATGKADDTSLYSGKVDLSTTKQANGTYTLEDSSRGSGVVTYDGNNKANASGKTQITDKNDVWGESSDPARSKAAVDAHYGAEMTYDFLKDVLGRNSLDGKGEKLVSYVHVDKNLVNAFWDGEKMSYGDGDGKDSGPLTTLDIAGHEIAHGLTERTAGLVYEGESGGLNESFSDIMGAGVEWYASQKNPAVKFDWKVGEDAWTPGNGTDDALRYMDDPTKDGYSVDHYKNYPKQTEVHGSSGIANNAFYLLTEGGKNRTSGLEVKDGIGMDKSLKIFGRALTTYMTPDTTFAQAREATIKAATDLHGANSVEVQKVKDAWTAVGVGR
>NZ_CP022163.1|WP_095976009.1|727626_728769_-|bifunctional-chorismate-mutase/prephenate-dehydratase
MSDVVDLQQLRVAIEQVDEELLDALRRRMDLAEDIARSKLATASPIRDQRREDLLLRRIRTAAMARNLDPHEVERLYRFIMEMSVARQHAWVTGLESTPLRVAYPGIEGSYSHQMAHKRYAGRDGGVFLSGFDTPRLAVDALRRGEMDLALLPIENTTAGAMYETYDALVEEGVTLIAEVVDQVQHRLLGLPGARLESLHTVRSHPQAITQCETFFRERLPHVRLLPDLDTGGAAQRVREANDPGVAAIASDSAAQRFGLEVLAHELQDRKGDFTRFVEVARAATPLPTDAPCKTSLVMVLENKPGTLGKALLVLAERGVNLARLESRPLPGSPWCYRFFLDLEGHAASAPIEAVLRDLQPYTQSMRLLGTYPRVELLPG
>NZ_CP022163.1|WP_095976010.1|728775_729612_-|prephenate-dehydratase
MKRISVLGPGTFSEESAHHFLGAVPHQLIPCKLIADVFQAVVSGRADLGVIPIENTLEGSVSQHLDWLVHEVDLPIQAEWVYPITMNLIGRAGPLEGIREVLSHPVALGQCREFLRARLPRAEVIPVGSTSEGARQVRERASETGLAAIGSAASAALYGLDILAGHIEDHPDNATRFVLVGPEPLVLSRPGRSKTSLLVTLPADFPGALHQVLSVFARKQVNLVRIESRPTRKRLGNYFFFIDVDSPLSAQPMPEALAELDSLGCSVRVLGSYLSHGV
>NZ_CP022163.1|WP_095976011.1|729677_731276_-|PAS-domain-containing-protein
MSERPSASIHRLMELSAQRPLSLLLLEDNALDAELILARFEEEGLSLKVERVDGEAGFTRALERSCFDIILSDYNVPGFDGLSALSTARELCPDTPFLFVSGALGEERAIEMLKRGATDYVLKEHLERLVPCVARALREAEGEARRKRTEEALRASEERYALASRATFDAIWDWDLRTDTTHWNDTLEQVVGYTPAEMGQSPSGWSERIHPEDRERVLLRFRDAIGSREERWLEEYRFLHKNGTWCDVVDRGHIVREASGRPVRMVGAMQDISERKRAEVERQRLLQEARHRAEFEQQLMGIVSHDLRNPLSAILMAGALLLRREDASPWLTKTAARIVSSAERAHRMIRDLLDFTQARMGTGIPIQPSPLDIHELAHQVVEEARTAHPARELLLSWQGDGKGVWDSDRIAQVLSNILGNALRYGREGSPVRVETEGRAESVLLRVHNEGSPISPELLPRLFEPLTRGGTRLTQSDRSIGLGLYIVRQLVLAHRGSVDVRSTEAEGTTFTVRLPRVTPSSGTQVAVLSPPGG
>NZ_CP022163.1|WP_095976012.1|731272_731734_-|response-regulator
MTGLKRILLVEDNANDVALTLAALEETRLANEVVVVRDGQQALDYLHRQGEHASRPASHPAVVLLDLKLPKVDGIQVLSQVKADPELRTIPIVMLTSSREEQDLASSYGLGVNAYVVKPVVFDDFVFTLRELGLFWAVVNQPPPGSLPPGSER
>NZ_CP022163.1|WP_095976013.1|731750_734744_-|PAS-domain-containing-protein
MPSIVETPRPCVLLVDDDHAHLAALEALLAPLGQRWVRADSGREALRCVLEEDFAVILLDVHLGDMSGLAVLESLRERERTRRTPVLLMTDADADPEEALRGYERGAVDCLTWPLVPQVVRAKVGVFVELWRAGHPSRLQEEEPREPDSLVRRREERLEAELRSRTEALNSSEERLRLAVSATALGTWDFNPVTRELRWDARCKELLGVAPDVDVTYELFISRVRPEDREASHAAVERSLDPRGTGHYDMEYRSVAEPGQEPRWLRATGRAYFEQGRAVRFIGTLRDVSVYKLAEEERSRLLAEARHRAEQLRGLTEASVALHSAEGLSPMLTLLAERARDVVGAHQCVVSLSEGAKWEQVIIAVSLSDKYAAWREYASRPDGSGIYSEVCRTNRPLRLTQAELEAHPAWKGFGAHASEHPPMRGWLAVPLVNREGHHLGLIQLSDKTRGEFSGEDEAVVVQLAQIASVAVENKRLYELARTQRRNLLAAFMQLPEPLSVMKGPDFVYEMVNTSFQRSVGERAVVGLPARQVLPELEGQRYFEPMERVYHEGVSIQLSEVALRWRTLPEPTPREGFFNISYQPLRDMDGRVEGIISVAFDVTEQVRARREVEALAERLSQSEKKLRALANSMPQLAWISDSEGQVLWYNDRWYEYTGSTPEEMLAGKWRNIYHAEELPRVWKSWSRSVARGELWEDQFRLRAADGSWRWFLTRALPLRDAEGRIIQWFGTNTDIHEERRILENLRRAEEEIRQLNSGLEARVRERTAQLQEANQELESFSYSVSHDLRAPLRHIIGFAQLLERRAGAALDDVARGHLRTITNAAQQGGMLVDDLLAFSRMGRAELRQTRVDLGALVQEVRRELEPESKGRQIEWRVGELPAVKADPSLLRQVLRNLLGNAVKYTRPRAQALIEVGARSDEAEAEVWVRDNGVGFEMQYVDKLFGVFQRLHTAEQFEGTGIGLANVRRIISRHGGRTWAEGAPEQGATFHFTLPRATT

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Crispr_ID: NZ_CP022163_4

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP022163_4

2940896-2941000

Orphan

Consensus_repeat	Method
TGGCCGCCGCCTTCTTCGTGGCCG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP022163_4

>merge|NZ_CP022163|4|2940896-2941000|CRISPRCasFinder
TGGCCGCCGCCTTCTTCGTGGCCGAGGGGGGCGCCTTGGCGGCGGGCTTCTTGCGGCCGATGGACTTGGAGGCCCCCGGCTTGGCCGCCGCCTTCTTCGCGGCCG

>NZ_CP022163|4|3|2940896-2941000|CRISPRCasFinder
TGGCCGCCGCCTTCTTCGTGGCCG	AGGGGGGCGCCTTGGCGGCGGGCTTCTTGCGGCCGATGGACTTGGAGGCCCCCGGCT
TGGCCGCCGCCTTCTTCGCGGCCG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP022163.1\|WP_095977605.1\|2948513_2949266_-\|nickel-pincer-cofactor-biosynthesis-protein-LarB	unknown	unknown	gnl\|CDD\|224605
NZ_CP022163.1\|WP_095977588.1\|2929648_2930683_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|237030
NZ_CP022163.1\|WP_095977603.1\|2946237_2947314_-\|dipeptide-epimerase	unknown	unknown	gnl\|CDD\|239435
NZ_CP022163.1\|WP_095977602.1\|2944575_2946225_-\|FAD-dependent-monooxygenase	unknown	unknown	gnl\|CDD\|235728
NZ_CP022163.1\|WP_095977604.1\|2947337_2948510_-\|nickel-pincer-cofactor-biosynthesis-protein-LarC	unknown	unknown	gnl\|CDD\|376691
NZ_CP022163.1\|WP_095977597.1\|2939896_2940778_-\|nucleotide-exchange-factor-GrpE	unknown	unknown	gnl\|CDD\|271355
NZ_CP022163.1\|WP_095977599.1\|2941455_2942946_+\|endonuclease/exonuclease/phosphatase-family-protein	unknown	unknown	gnl\|CDD\|197338
NZ_CP022163.1\|WP_095977608.1\|2956142_2957099_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|378339
NZ_CP022163.1\|WP_095977595.1\|2936505_2938011_-\|serine/threonine-protein-kinase	unknown	unknown	gnl\|CDD\|270916
NZ_CP022163.1\|WP_095977600.1\|2942988_2943837_+\|EamA-family-transporter	unknown	unknown	gnl\|CDD\|273359
NZ_CP022163.1\|WP_095977601.1\|2943849_2944569_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095977606.1\|2949389_2953148_-\|pullulanase-type-alpha-1,6-glucosidase	unknown	unknown	gnl\|CDD\|273974
NZ_CP022163.1\|WP_095977594.1\|2935752_2936502_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095977607.1\|2953305_2954973_+\|DUF3459-domain-containing-protein	unknown	unknown	gnl\|CDD\|200455
NZ_CP022163.1\|WP_095977593.1\|2934297_2935497_-\|ABC-transporter-substrate-binding-protein	unknown	unknown	gnl\|CDD\|380570
NZ_CP022163.1\|WP_095977596.1\|2938057_2939890_-\|molecular-chaperone-DnaK	unknown	unknown	gnl\|CDD\|234715
NZ_CP022163.1\|WP_095977590.1\|2931456_2932308_-\|ABC-transporter-ATP-binding-protein	unknown	unknown	gnl\|CDD\|223488
NZ_CP022163.1\|WP_095977592.1\|2933368_2934298_-\|branched-chain-amino-acid-ABC-transporter-permease	unknown	unknown	gnl\|CDD\|223633
NZ_CP022163.1\|WP_095977591.1\|2932307_2933360_-\|branched-chain-amino-acid-ABC-transporter-permease	unknown	unknown	gnl\|CDD\|119323
NZ_CP022163.1\|WP_095977589.1\|2930704_2931460_-\|ABC-transporter-ATP-binding-protein	unknown	unknown	gnl\|CDD\|223487

Protein	Function_ID	Function_description	E-value
NZ_CP022163.1\|WP_095977605.1\|2948513_2949266_-\|nickel-pincer-cofactor-biosynthesis-protein-LarB	gnl\|CDD\|224605	COG1691, COG1691, NCAIR mutase (PurE)-related proteins [General function prediction only].	3.65314e-93
NZ_CP022163.1\|WP_095977588.1\|2929648_2930683_+\|hypothetical-protein	gnl\|CDD\|237030	PRK12270, kgd, multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit.	0.00495896
NZ_CP022163.1\|WP_095977603.1\|2946237_2947314_-\|dipeptide-epimerase	gnl\|CDD\|239435	cd03319, L-Ala-DL-Glu_epimerase, L-Ala-D/L-Glu epimerase catalyzes the epimerization of L-Ala-D/L-Glu and other dipeptides. The genomic context and the substrate specificity of characterized members of this family from E.coli and B.subtilis indicates a possible role in the metabolism of the murein peptide of peptidoglycan, of which L-Ala-D-Glu is a component. L-Ala-D/L-Glu epimerase is a member of the enolase-superfamily, which is characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.	1.80421e-101
NZ_CP022163.1\|WP_095977602.1\|2944575_2946225_-\|FAD-dependent-monooxygenase	gnl\|CDD\|235728	PRK06184, PRK06184, hypothetical protein; Provisional.	2.42696e-110
NZ_CP022163.1\|WP_095977604.1\|2947337_2948510_-\|nickel-pincer-cofactor-biosynthesis-protein-LarC	gnl\|CDD\|376691	pfam01969, DUF111, Protein of unknown function DUF111. This prokaryotic family has no known function.	0
NZ_CP022163.1\|WP_095977597.1\|2939896_2940778_-\|nucleotide-exchange-factor-GrpE	gnl\|CDD\|271355	cd00446, GrpE, nucleotide exchange factor GrpE. GrpE is the adenine nucleotide exchange factor of DnaK (Hsp70)-type ATPases. In bacteria, the DnaK-DnaJ-GrpE (KJE) chaperone system functions at the fulcrum of protein homeostasis. GrpE participates actively in response to heat shock by preventing aggregation of stress-denatured proteins; unfolded proteins initially bind to DnaJ, the J-domain ATPase-activating protein (Hsp40 family), whereupon DnaK hydrolyzes its bound ATP, resulting in a stable complex. The GrpE dimer binds to the ATPase domain of Hsp70 catalyzing the dissociation of ADP, which enables rebinding of ATP, one step in the Hsp70 reaction cycle in protein folding. In eukaryotes, only the mitochondrial Hsp70, not the cytosolic form, is GrpE dependent. Over-expression of Hsp70 molecular chaperones is important in suppressing toxicity of aberrantly folded proteins that occur in Alzheimer's disease (AD), Parkinson's disease (PD), amyotrophic lateral sclerosis, as well as several polyQ-diseases such as Huntington's disease and ataxias.	2.60822e-62
NZ_CP022163.1\|WP_095977599.1\|2941455_2942946_+\|endonuclease/exonuclease/phosphatase-family-protein	gnl\|CDD\|197338	cd10283, MnuA_DNase1-like, Mycoplasma pulmonis MnuA nuclease-like. This subfamily includes Mycoplasma pulmonis MnuA, a membrane-associated nuclease related to Deoxyribonuclease 1 (DNase1 or DNase I, EC 3.1.21.1). The in vivo role of MnuA is as yet undetermined. This subfamily belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds.	1.2301e-18
NZ_CP022163.1\|WP_095977608.1\|2956142_2957099_-\|hypothetical-protein	gnl\|CDD\|378339	pfam09985, Glucodextran_C, C-terminal binding-module, SLH-like, of glucodextranase. Glucodextran_C is the C-terminal domain of glucodextranase-like proteins found in various prokaryotic membrane-anchored proteins. It shows homology to the carbohydrate-binding unit of some glycosidases.	4.59e-31
NZ_CP022163.1\|WP_095977595.1\|2936505_2938011_-\|serine/threonine-protein-kinase	gnl\|CDD\|270916	cd14014, STKc_PknB_like, Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.	8.84099e-85
NZ_CP022163.1\|WP_095977600.1\|2942988_2943837_+\|EamA-family-transporter	gnl\|CDD\|273359	TIGR00950, Uncharacterized_inner_membrane_transporter_YicL, Carboxylate/Amino Acid/Amine Transporter. [Transport and binding proteins, Amino acids, peptides and amines].	3.66857e-16
NZ_CP022163.1\|WP_095977606.1\|2949389_2953148_-\|pullulanase-type-alpha-1,6-glucosidase	gnl\|CDD\|273974	TIGR02103, pullulanase-like_protein_starch, alpha-1,6-glucosidases, pullulanase-type. Members of this protein family include secreted (or membrane-anchored) pullulanases of Gram-negative bacteria and pullulanase-type starch debranching enzymes of plants. Both enzymes hydrolyze alpha-1,6 glycosidic linkages. Pullulan is an unusual, industrially important polysaccharide in which short alpha-1,4 chains (maltotriose) are connected in alpha-1,6 linkages. Enzymes that cleave alpha-1,6 linkages in pullulan and release maltotriose are called pullulanases although pullulan itself may not be the natural substrate. This family is closely homologous to, but architecturally different from, the Gram-positive pullulanases of Gram-positive bacteria (TIGR02102). [Energy metabolism, Biosynthesis and degradation of polysaccharides].	0
NZ_CP022163.1\|WP_095977589.1\|2930704_2931460_-\|ABC-transporter-ATP-binding-protein	gnl\|CDD\|223487	COG0410, LivF, ABC-type branched-chain amino acid transport systems, ATPase component [Amino acid transport and metabolism].	4.12734e-122
NZ_CP022163.1\|WP_095977607.1\|2953305_2954973_+\|DUF3459-domain-containing-protein	gnl\|CDD\|200455	cd11316, AmyAc_bac2_AmyA, Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes Chloroflexi, Dictyoglomi, and Fusobacteria. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.	0
NZ_CP022163.1\|WP_095977593.1\|2934297_2935497_-\|ABC-transporter-substrate-binding-protein	gnl\|CDD\|380570	cd06347, PBP1_ABC_LivK_ligand_binding-like, type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems predicted to be involved in uptake of amino acids, peptides, or inorganic ions. This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in uptake of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, its ligand specificity has not been determined experimentally.	1.91606e-165
NZ_CP022163.1\|WP_095977596.1\|2938057_2939890_-\|molecular-chaperone-DnaK	gnl\|CDD\|234715	PRK00290, dnaK, molecular chaperone DnaK; Provisional.	0
NZ_CP022163.1\|WP_095977592.1\|2933368_2934298_-\|branched-chain-amino-acid-ABC-transporter-permease	gnl\|CDD\|223633	COG0559, LivH, Branched-chain amino acid ABC-type transport system, permease components [Amino acid transport and metabolism].	4.52808e-76
NZ_CP022163.1\|WP_095977591.1\|2932307_2933360_-\|branched-chain-amino-acid-ABC-transporter-permease	gnl\|CDD\|119323	cd06581, TM_PBP1_LivM_like, Transmembrane subunit (TM) of Escherichia coli LivM and related proteins. LivM is one of two TMs of the E. coli LIV-1/LS transporter, a Periplasmic Binding Protein (PBP)-dependent ATP-Binding Cassette (ABC) transporter involved in the uptake of branched-chain amino acids (AAs). These types of transporters generally bind type 1 PBPs. PBP-dependent ABC transporters consist of a PBP, two TMs, and two cytoplasmic ABCs, and are mainly involved in importing solutes from the environment. The solute is captured by the PBP, which delivers it to a gated translocation pathway formed by the two TMs. The two ABCs bind and hydrolyze ATP and drive the transport reaction. E. coli LivM forms a heterodimer with another TM, LivH, to generate the transmembrane pore. LivH is not included in this subgroup. The LIV-1/LS transporter is comprised of two TMs (LivM and LivH), two ABCs (LivG and LivF), and one of two alternative PBPs, LivJ (LIV-BP) or LivK (LS-BP). In addition to transporting branched-chain AAs including leucine, isoleucine and valine, the E. coli LIV-1/LS transporter is involved in the uptake of the aromatic AA, phenylalanine.	2.67937e-68
NZ_CP022163.1\|WP_095977590.1\|2931456_2932308_-\|ABC-transporter-ATP-binding-protein	gnl\|CDD\|223488	COG0411, LivG, ABC-type branched-chain amino acid transport systems, ATPase component [Amino acid transport and metabolism].	1.6485e-115

>NZ_CP022163.1|WP_095977597.1|2939896_2940778_-|nucleotide-exchange-factor-GrpE
MAGSNRDSKGSFQTDISQDVIDDALKSVERRASSPPPADEDFPEGGRTLEMDLPDGGMTLEVDVPATVFGEPSSSSGEGSSLELAETRQKLEQVQRELEQARAQLEFSQSKSRETMDRLKESHERALRAAADLENYKKRAQKEKEEVQKFGAERLLKDFLPVLDNLDRALEAAQKSADFESLRTGVEMTRKLFESAFGKQGVKGFSAVGQPFDPRLHEAMQQVESATVPAGHVVYEAVRGYTLNERLMRPALVVVARAPETAQPESTSSSTPGGEPTGGSAPEQTGTTPSENQ
>NZ_CP022163.1|WP_095977596.1|2938057_2939890_-|molecular-chaperone-DnaK
MGKVIGIDLGTTNSCVAVMEGGEPVVIPNSEGSRTTPSMVGFTESGERLVGQIAKRQAITNPENTVFAVKRLIGRKYDSPEARKAISVSPFRVVASPNGDAWVESRGKGYSPPEISAIVLMKMKQTAEDYLGEPVTEAVITVPAYFNDSQRQATKDAGRIAGLNVLRIINEPTAAALAYGLDKVGQASAERIAVYDLGGGTFDISILELNSGVFEVKSTNGDTFLGGEDFDQRLIDFLAKRFAEQNNGLDLRKDRMALQRLKEAAERAKHELSSATETEVNLPFITADATGPKHLTETVERTTFEALVSDLVERSIEPCRIALKDAGVPAQQIHQVLLVGGMTRMPAVQQKVKEFFGKEPHKGINPDEVVAVGAAIQGGVLKGEVKDVLLLDVTPLSLGVETAGGVFTKIIDKNTTIPCKKSQVFSTAVDNQPLVSVHVLQGEREMAVDNKTLARFELVGIPPAPRGVPQIEVSFDIDANGIVHVSAKDLGTGKVQQVRVVGNSGLTEAEIQAMIADASANQSSDKLKKEMAELRNNADSLIYTTEKSLEEYGNVLQEKDRTDIKADLDALKELLKGSDAAAVKEAYQKLETSAYRIADALYADQSKASS
>NZ_CP022163.1|WP_095977595.1|2936505_2938011_-|serine/threonine-protein-kinase
MASVEFPSLEAEVSFLRGLTAVTRIADEIIEDCLERGLDLDAAVDVYLTQCARLVNASAGFVGLRGSKGPVLTRVLGVLGVDVFEATGWSGCRPLPEGRMLFCAPLTLGRLELGTMGLVVAGRFDDGGALVMKLVAAMADQLDNAVLAFIALADGAHVLEKLDDLAPEEDPVTGTRARIGRYELVTPLGTGGMAQVLVARTRGPEGLGRLVALKRILPQLVSDPDMVKQFLDEARIGLRLSHSNLVTIHDFGESQGAYFLVMELVRGVDFDRLLKTLRPSAAVVSAVVVQALHGLHAAHLARGEDGRPLQLVHRDLSPHNLMVGFDGRVKVLDFGVAKARAQRTVTLPGIVKGKPLYMSPEQALGRRLDARSDLFAMGLILYEAFTGKRAFDRGDDVASMEAICDDRLSRPASIHPKLWGVLEQALAKRPEDRFAHAQQMAEALTEACPPARDGEVGQLVRTHFPERLQGFERLERVHLASGPPTSPTRATPVVPAKGPAR
>NZ_CP022163.1|WP_095977594.1|2935752_2936502_+|hypothetical-protein
MDQREEIKEGMIVRSVDGHKLGRVYAVGGTEFHIEKGLFFPKDYSVRYSEVSTIRDGEIFLAHGRDSLKKFSLDDVPNTDPLDSGRAPVARTEAPGVTSWRDLDRPASLSELSGLRTQDLGNQEIGPHNTEGASASPILTEEDRERARVNARPIEPVLREPGFPIPPSSPGDTRPPLRASSLDETVGVVSPGRDPTLERTIEEDYRAALIEDELYEETHRVQARGDADLEGQRKLNLSGEDDSSIKRGR
>NZ_CP022163.1|WP_095977593.1|2934297_2935497_-|ABC-transporter-substrate-binding-protein
MRRLTPVLLAAIALFSAACEKKSQPTTSAEAPGGQAAQPATGGKPPSSDTLLLGEVVSLTGAQATFGVSTRNGVDLALNEVNAAGGVKGKKLAVRVLDDQSKPEEAAQAATRLITQDKVLVILGDVASSNSLAMADKAQAAGIPMITPASTNPAVTEKGDFIFRVCFIDPFQGFVMAKFAREHLKVERAAILQDNKSAYSIGLTEVFSQKFKELGGTLLATESYSQGDTDFRAQLTSIKKLKPQAIYVPGYYNDVGIIARQARELGLTVPMMGADGWDSEKLFELAGNALDGSYFSNHYSPANPEPRVQKFIADYKAAYGSVPDALAALGYDAARVAIAAIEKSKDLSGPSIRDAIAQTKDFPGVAGTITLDEKRNAVKSAVILKVGNGTTEFVTTVHP
>NZ_CP022163.1|WP_095977592.1|2933368_2934298_-|branched-chain-amino-acid-ABC-transporter-permease
MSQLIQHLINGIASGTIYALIALGYTMVYGVLKLINFAHGDVMMVGVYMGYATAFALGREARGSVGGVLLIFLVAMGGCALLGFLIERFAYRPLREKPRLTALITAIGISFTLSYGFQLDIGFLPGSAPRAFPQIIKPSQWFTLGDPEFPDVVLWNWQVISLMVAVALMMGLQYLVFRTRFGRAMRAVSFDHRVAALMGIPTDRVISVTFMIGSALAAGAGLLYAIKDTSVSPLMGLYVGLKAFVAAVIGGIGNVPGAMVGGLLLGLVEEFVVGYAASTWRDAVAFGFLILVLLVRPGGLFGRVAAEKV
>NZ_CP022163.1|WP_095977591.1|2932307_2933360_-|branched-chain-amino-acid-ABC-transporter-permease
MESAAVPAPSRVPASLRGILPVLIALPVLLLAEWALSDSPFAVYLLSVMGVNVILAVSLNIVNGMTGQFSIGHAGFMAVGAYLAGVTSLALKDVAISFLPVAVSDQVFLIVALLVAGLSAALAGFLVGLPSLRLRGDYLAIVTLGFGEIIRVAVTNTEAFGRALGLSGIPQTSSVAMVWFWVFLVVLVSRRIAGSSHGRSLWAIREDEVAAEAMGVNTTGYKVRAFVVSSFFAGVAGGLFAHFVPIINPGSFTFVKSMEVVVMVVLGGLGSTTGAIVSAMVLTLLPEGLRSAFSALAPEGNLAQQVDQIRMPVYGMLLVVLMLARPQGLFGTRELWEVVPRWLTRRRKGM
>NZ_CP022163.1|WP_095977590.1|2931456_2932308_-|ABC-transporter-ATP-binding-protein
MSGPLLEAVGVSIQFGGLKALSDFNLSIHAGELQGLIGPNGAGKTTAFNVLTGVYQATQGDVRVGGQRVNGRLPHQINHAGLARTFQNIRLFRALTALDNVKVACRAQTALSDGSVGLGAKFREAMGNYRDWWRAMMLTPGFQAEEVELTRQAERLLEVMGLSHRRDEEARNLPYGEQRRLEIARALGTRPRVLLLDEPAAGMNTREKADLMVLIRKIRDDFQLGILVIEHDMKLVMGICEKITVLDHGETIARGAPAEVRSDRKVIEAYLGDSYLESQGGAA
>NZ_CP022163.1|WP_095977589.1|2930704_2931460_-|ABC-transporter-ATP-binding-protein
MSEAQVKLLGERREFPPLLAVDGVKVSYGAIQALRGVTLSVGKGEVVALIGANGAGKTSTLRAVSGMLKPVGGRITFKGEDITGAKAHQLVPRGMAHAPEGRGVFPNLTVLENLELGAYLRKDADGIASDLEKSYTLFPRLKDRRKQLAGTLSGGEQQMLAIARALLSRPTLLLLDEPSLGLAPQVTETIFRNLQDVNASGVSILLVEQNAHLALNFAHYGYVLETGEVVMAGAGKALLDSPEIRKAYLGE
>NZ_CP022163.1|WP_095977588.1|2929648_2930683_+|hypothetical-protein
MNPRSSSSTLLLSLALLLVPARQASAAQSTDPTALLALHPCVVVGEKDQDKVRDYQLACTTTVARDDVRLVPSEQVLAVLDKEPKKSCAPPASKKPSECLGRLASATQAARSVLITITPGQVTRVSGLVVSAQGDVIDQKNIQLRNRGQSQDELVRTALSRLRGQLDLVPAKQPPVAEAPTPASPPPAPPPVVTVTPPPETAPEKEKQSASTALEPIPTTTQRRSPLLGQSWKTPVAYSAAGLGVVAFGVAGFLAISGDQAMRQSNTYFADGSYPVISDLDTVIGLREQASSKRTLAGISTAVGAVLVGTGVYLWLDDRPTSPKPGITAVSVGPGSVSLFGVLP
>NZ_CP022163.1|WP_095977599.1|2941455_2942946_+|endonuclease/exonuclease/phosphatase-family-protein
MAFARLLRMLGILVLIGGCNGEPSSGTHALVLPELAPQETTEGVPYEVSLGATQGTPPLQYMVGELPPGFSFYRSTGILKGPATAAGSYAISVQVKDGTGATATRTYLLKVYPAPSIPARSLAAATQGTSYSVPFEAEGGKPPLRWELAGGALPPGLILNQEGQLMGVPTASGTYALTVRARDVHGAQVEQSFGLEVRAGTGPEPQGLELRAVNWNLEWFGHPDEGPSDEALQLANVRRVIDTTKADVWGLQEVVDTEHFNALKQQLPGYDGFVANDPGVPSGAYFYGSTDAKLALLFRSDVVSVLEKKLILTTGSNPYYFGSRPPLQVKLRITREGKSTELVVIVLHMKAYADTDSYNRRRSAALALKGYLDAQAATTPILVLGDWNDDVDVSILKNSSTGEYLPSPYQGFVDDSSDFTFVTRPLALAKQSSTVKAQNTEFIDHQLITRKLASSYVSDSVQVLHPEAYIDRYGVTTTDHYPVLSRFAFGDTALTP
>NZ_CP022163.1|WP_095977600.1|2942988_2943837_+|EamA-family-transporter
MHPSRLYILVAAVCWSTAGAAVKLSTLSAWQLTAGRSLVAALVLALALPSGRRLPSRQGVLATFAYAATVTTFIIATKLTTSANAIFLQSTAPLYVLLLSPMVLGERPSRGELLAVPVFLLGLSLFFLDQFHPGQRWGNVVAMASGISFALCILGLRAVKDEGTSVLVWGNVIAGGVALFFAMDGPRPTGMDIGLVLFLGVFQSALAYSLFQHGLRDTPAVEASLLVLLEPVLNPVWTFLLAGERPGSWALVGGTIILVATAWRTLLVSSRTGGPSAREKVP
>NZ_CP022163.1|WP_095977601.1|2943849_2944569_+|hypothetical-protein
MKTIRRTFAVTTFLLLTPLGAIAREPVKSLSEDLNGDGKKEAISLQWKEGDSTYVLKVGGSTAQGRGDESRVEGVSVVDLNTKDKWKELLVHIELPWDEHRLDIYGFDGKELKPLGSVPTLDQAHGNGIFLSDDWWGFWNRRDKYVLNREKWKIERMPQNVYYVGEEATVTTSFPLTFDRSGKDVVANLATNSKILVLAADPAIPGKLPWFLVKSSTGLLGWAEGEALTQNTTGLPFHE
>NZ_CP022163.1|WP_095977602.1|2944575_2946225_-|FAD-dependent-monooxygenase
MLDALVVGAGPTGLTMASELARHGLRCRIIEQLEAPSPLSRALAVQARTLELFEDLGLVERALASGRRTNAFNVVGTGGVRARVPLGGFEWLETRYPYILMLPQDATESMLTEHLGTFGVGVERGVALERFTQDAERVVATLRHADGRSEQVTARWLLGCDGARSRVRKGADLPFEGDTYEDACVLADVHVEWSLEEGEVFIMPTLHGVVGVFPMPGDSRYRLFFIMPRTDESDQADDIEPLSLEELQALVDRMVPLPARVSEPRWMSRYRLHRRGVPHYRRGRVFLAGDAAHIHSPAGGQGMNTGIQDAYNLAWKLALVTRGRVPEALLDTYEAERLPVGRMLLEGTDRAFMIMAGGGAISRLLRSLVVPRVARKLSGVLRAQRFASRFVSQLAIRYRESPLSTERLWGEDAGGVRMEQGPAPGSRVPELPVKGEGVERLHQVLHGPHHTLLLFTGLVPEARGADDLVALARRLEAAYGPFLKARVVVAGAEAPASHMLADTDGAVHRRFGAGSACFYLVRPDGYVGHRERPIDPRRLEAELTRRMGR
>NZ_CP022163.1|WP_095977603.1|2946237_2947314_-|dipeptide-epimerase
MQPTRITELRFEPLDLPLTEPFAIATGAPDMANNVLVRLTLADGTVGLGEAAPFTAVSGESQASTLEALGSVREAMLGKDAAAWRPIGAWLGEALPKAPSARCGLELALLDALCRHHRMPLATFFGGAGTGLDIDMTVTAGDEAHAAASARAIRARGIRTLKVKVGALSPEEDVRRMVVIRREAPEARLFADANGGYTVAGARTFLSGLEAAGIPLALFEQPVPREDWEGMAELTRSSRVPICADESARTVKDVVRLAREGGAHGVNLKFMKSGVGESLAMWNAARAFGMELMMGGMVESTLAMSSAVHFAAGLGGFDYADLDTHLFIREHAFRGGLRVEGGRVDVGHIEAGHGVVLD
>NZ_CP022163.1|WP_095977604.1|2947337_2948510_-|nickel-pincer-cofactor-biosynthesis-protein-LarC
MRKILYLEPVGGIAGDMFLAAGIDLGLSPDELTRALSGLGVPGWKLAVKRAVRHAISGTHLDVVLDEREAHPHRAYADIRQLIEAAPTLPPRAKERALAVFRAIGEAEAKVHGVSIDDIHFHEVGAVDSIVDICGAAVVLELLGDPEVFAAPPPLGSGTIRVAHGNMPIPVPATLELLKNLPVRFEGVGELTTPTGAALLKVLTHIGQPPPDFITERIGYGVGTKDFRDRPNVLRASLGRAEARAEGLWVLEANLDDSTPQLLGYLLEHVLVRGALDAWVVPATMKKARPGHVLSVLVEGGVKESVMDTLLRESTTLGVRSYPVERRALERDWVEVETPWGRVRVKRGLRNGEVLNAHPEFEDCRQVAEAAGVPLKQVMAAALAALGSGK
>NZ_CP022163.1|WP_095977605.1|2948513_2949266_-|nickel-pincer-cofactor-biosynthesis-protein-LarB
MDEKTLTRLLEQVKGGKVSVDAAVGQLKDLPFAELGYATLDTHRSLRFGFPEVVLGEPKTVEQLLGIVGKLMEVKQPVLVTRLQQDKADALRKAFPKGEYHAVARIFHVKQGKPKAGKVAVVTAGTSDIPVAEEAALTAEAMGATVNRVYDVGVAGIHRLLKRREEIQSAHAAVVVAGMEGALASAVGGLVGIPVVAVPTSVGYGANFGGVSALLAMVNSCASNVATMNIDNGFGGGFYAALISRTKGQR
>NZ_CP022163.1|WP_095977606.1|2949389_2953148_-|pullulanase-type-alpha-1,6-glucosidase
MILSSPPLGRRRARALLGALVFASAGSALAAPSDVSLVGSVCASGEPCSALTFDAGDKAWQGSFALPAGTHTFRAAVTEDGATSIYGQGGAKDGAAFTLELSTPQTVKFYYDDKSHWITTRYNSVIAVAPGSFQSELGCPGDWQPDCLGSWLKDPDGDGVYTFSTTELPAGSYEGKVAINESWDENYGAGGAPSGANIGFSVPSAGLPVIFTYDSTSHVLNIEVVGAPKGDIQLRRAHWVSGDLLVWEPSVTIPATATFALHYDPSGAMSLGPAGISGGQSIPLTRETVGLPPQLAEKFPHLVGKPVFRIADEDLFKVKDILKGQVALSLVDADQNMLDATGVQLPGVLDELYANDAALGVTWNGAEPTFRLWAPTARNVTLRLYNDATTTFWSSLPMTLDATTGVWSTVGGTLLKGHYYLYEVEVYVPSLKAVVKNLVTDPYSVSLSLNSTRSQLVDLADASLAPTGWSSLVKPALAAPEDIVLYELHVRDFSIHDNTVPAPKRGTFLAFTEANSNGMKHLRGLAAKGLTHVHLLPAFDIATIEEDRTKQQEPSGDLASFAPDSEQQQAAVVAVKDLDGFNWGYDPFHYTVPEGSYAVEPNGSARILEFRQMVKALSDSGLRVVMDVVYNHTAFGGQADKSVLDRVVPGYYQRLNADGNVETSTCCQNTASEHAMFEKLMVDSLVTWAKFYKVDGFRFDLMGHHMKSNMLKVQAKLAALTQAKDGVDGSRIYLYGEGWDFGEVTNNARGVNATQLNMSGTGIGTFSDRLRDAARGGGPFSGLQEQGFISGLWDDPNSATSGSAEDQRQRLLHYMDQIRVGLAGNLRDYSFMNKDGTVVTGAEVDYNGQPTGYTSDPQEVITYVSAHDNETLFDAVQFKASASADMDARVRMHNMGLSLVALGQGIPFFHAGDELLRSKSLDRNSYNSGDWFNTLDFTYASNNWGVGLPPEADNKDNWPTMRSLLANPALKPGPAHIRRALEHFGEVLSIRKSAALFRLRTAADIQEHVHFLNTGPSQIPGLLVMNIRNEDATDGITDAVVFFNANKEQQVFHIADYAGRSMQPHPALQASTDPVLQGATFQSSGDFIVPGRTTAVFVNTYVPPEDAGTPDAGGGIDAGPGPGEDAGTPDDAGTDTDGGTPDAGGDAGTPDDAGTDADGGTTPDAGGEIDAGPGGDAGTPDDAGTRDGGGSAPGDDGGTEPGADAGPGNDGGTAPDGPGQGGCGGCAGSGGGSFGGLALLLGGLLRSRRRQA
>NZ_CP022163.1|WP_095977607.1|2953305_2954973_+|DUF3459-domain-containing-protein
MPSLRSSCLLLPLFTLTSCVTGPATPVDGSPTPRVELAAPTANLWYQHAVFYEVFVRSFQDSNGDGKGDLAGLISRLDYLNDGDPNTTSDLGVDALWLMPVFDSPSYHGYDTTNYERIEPDYGTNADFERLCAEAHRRGMRVIVDLVINHTSSQHPWFQESAASPESAKRDWYVWSPVDPGWRQPWDLFSQGATWHPLNGAYYYGVFWGGMPDLNLRTPAVREEVKRLASFWLDKGVDGFRLDAVRYLIETSGGLTGQADTAETHAFWKEFAAHVRSVKPDAALVGEAWTNTPLIAPYYGSTAQVPQGDELPLNFNFPLAEEIIKAARLGNGNGLALKLSEMRSRYPVGVADAPFLTNHDHVRVATQLDGKPGALVTAASLVLTLPGSPFLYYGEEVGLLNGTTQNDEAKRTPMPWDGSTGGGFTSGTPWFAFAPGHENTHVAAQMTAPGSLLSRYRDLIRARHASPALERGGLTLLTSTQSRTSTLAFLRTLEGERVLVVHNLGDSAENAGPFELEGDLAEPLFVDSSVRAPERDGGTWRITLPARTTGIWRLR
>NZ_CP022163.1|WP_095977608.1|2956142_2957099_-|hypothetical-protein
MSSLHRLVPLLLLAALVSACRGTRGGTPLFVLEDPRGDDHGDGQLRYPLRQDMTPGSLDLLSLRAWAESGGTRFEATFARPIAVPQRRTVDAAGTTLADQARLGFYTFNLDVYVDQDRQEGSGSTETLPGRHLVLAPGSGWEKALILTPRPYEARDMLRKLWREAAIAEAQRTQGSLGEPALKALEAQVEQRLDTHVFFPTRARVVGHTVSFFVPEAFLGGPARASWGYAVAVTGASLNLRVALPSFLGGVTAPPEQGVMVLGIGPGVSHERFGGGRVGGSFQSPVVDLVVPDGVRQEDVLGPAMPPWPAVVPAPEGS

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Crispr_ID: NZ_CP022163_5

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP022163_5

3088422-3088492

Orphan

Consensus_repeat	Method
GCTCAAATTCTCTGACACTCTTTCAGG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP022163_5

>merge|NZ_CP022163|5|3088422-3088492|CRISPRCasFinder
GCTCAAATTCTCTGACACTCTTTCAGGTCTTACCTGGCCGTACTGCTCAAATTCTCTGACACTCTTTCAGC

>NZ_CP022163|5|4|3088422-3088492|CRISPRCasFinder
GCTCAAATTCTCTGACACTCTTTCAGG	TCTTACCTGGCCGTACT
GCTCAAATTCTCTGACACTCTTTCAGC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP022163.1\|WP_095977705.1\|3081045_3081714_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095977716.1\|3093889_3094444_+\|Wall-associated-protein-precursor	unknown	unknown	unknown
NZ_CP022163.1\|WP_157774914.1\|3088615_3089674_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_157774913.1\|3079651_3080386_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095977708.1\|3084848_3085505_-\|TetR/AcrR-family-transcriptional-regulator-C-terminal-domain-containing-protein	unknown	unknown	gnl\|CDD\|172294
NZ_CP022163.1\|WP_095977706.1\|3081804_3083472_+\|trehalase	unknown	unknown	gnl\|CDD\|366513
NZ_CP022163.1\|WP_095977702.1\|3078134_3079502_-\|DUF2156-domain-containing-protein	unknown	unknown	gnl\|CDD\|378310
NZ_CP022163.1\|WP_170115494.1\|3092712_3093624_+\|DNA/RNA-non-specific-endonuclease	unknown	unknown	gnl\|CDD\|224777
NZ_CP022163.1\|WP_002621977.1\|3076756_3077791_+\|rod-shape-determining-protein	unknown	unknown	gnl\|CDD\|237562
NZ_CP022163.1\|WP_095977707.1\|3083465_3084758_-\|MFS-transporter	unknown	unknown	gnl\|CDD\|340863
NZ_CP022163.1\|WP_157774915.1\|3090092_3090524_-\|nuclear-transport-factor-2-family-protein	unknown	unknown	gnl\|CDD\|378915
NZ_CP022163.1\|WP_095977704.1\|3080382_3080967_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095977718.1\|3096189_3097623_+\|serine/threonine-protein-kinase	unknown	unknown	gnl\|CDD\|270916
NZ_CP022163.1\|WP_095977701.1\|3077896_3078127_+\|DUF2171-domain-containing-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_157774918.1\|3095249_3096029_+\|pentapeptide-repeat-containing-protein	unknown	unknown	gnl\|CDD\|224276
NZ_CP022163.1\|WP_095982745.1\|3094898_3095120_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095977719.1\|3097609_3098179_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_157774917.1\|3092133_3092544_-\|nuclease-A-inhibitor-family-protein	unknown	unknown	gnl\|CDD\|369598
NZ_CP022163.1\|WP_157774916.1\|3090802_3092077_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095977709.1\|3085582_3087064_+\|FAD-dependent-monooxygenase	unknown	unknown	gnl\|CDD\|236199

Protein	Function_ID	Function_description	E-value
NZ_CP022163.1\|WP_170115494.1\|3092712_3093624_+\|DNA/RNA-non-specific-endonuclease	gnl\|CDD\|224777	COG1864, NUC1, DNA/RNA endonuclease G, NUC1 [Nucleotide transport and metabolism].	2.50059e-68
NZ_CP022163.1\|WP_002621977.1\|3076756_3077791_+\|rod-shape-determining-protein	gnl\|CDD\|237562	PRK13927, PRK13927, rod shape-determining protein MreB; Provisional.	0
NZ_CP022163.1\|WP_095977707.1\|3083465_3084758_-\|MFS-transporter	gnl\|CDD\|340863	cd06173, MFS_MefA_like, Macrolide efflux protein A and similar proteins of the Major Facilitator Superfamily of transporters. This family is composed of Streptococcus pyogenes macrolide efflux protein A (MefA) and similar transporters, many of which remain uncharacterized. Some members may be multidrug resistance (MDR) transporters, which are drug/H+ antiporters (DHAs) that mediate the efflux of a variety of drugs and toxic compounds, conferring resistance to these compounds. MefA confers resistance to 14-membered macrolides including erythromycin and to 15-membered macrolides. It functions as an efflux pump to regulate intracellular macrolide levels. The MefA-like family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	7.40025e-74
NZ_CP022163.1\|WP_157774915.1\|3090092_3090524_-\|nuclear-transport-factor-2-family-protein	gnl\|CDD\|378915	pfam12680, SnoaL_2, SnoaL-like domain. This family contains a large number of proteins that share the SnoaL fold.	1.70116e-09
NZ_CP022163.1\|WP_157774917.1\|3092133_3092544_-\|nuclease-A-inhibitor-family-protein	gnl\|CDD\|369598	pfam07924, NuiA, Nuclease A inhibitor-like protein. This family consists of protein sequences that are similar to the nuclease A inhibitor expressed by bacteria of the genus Anabaena ((NuiA). This sequence is organized to form an alpha-beta-alpha sandwich fold, which is similar to the PR-1-like fold. NuiA interacts with nuclease A by means of residues located at one end of the molecule, including residues making up the loop between helices III and IV and the loop between strands C and D. The mechanism of inhibition of nuclease A by NuiA is as yet incompletely understood.	5.43781e-44
NZ_CP022163.1\|WP_157774918.1\|3095249_3096029_+\|pentapeptide-repeat-containing-protein	gnl\|CDD\|224276	COG1357, COG1357, Pentapeptide repeats containing protein [Function unknown].	5.69056e-36
NZ_CP022163.1\|WP_095977718.1\|3096189_3097623_+\|serine/threonine-protein-kinase	gnl\|CDD\|270916	cd14014, STKc_PknB_like, Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.	9.90926e-55
NZ_CP022163.1\|WP_095977708.1\|3084848_3085505_-\|TetR/AcrR-family-transcriptional-regulator-C-terminal-domain-containing-protein	gnl\|CDD\|172294	PRK13756, PRK13756, TetR family transcriptional regulator.	9.76401e-35
NZ_CP022163.1\|WP_095977706.1\|3081804_3083472_+\|trehalase	gnl\|CDD\|366513	pfam01204, Trehalase, Trehalase. Trehalase (EC:3.2.1.28) is known to recycle trehalose to glucose. Trehalose is a physiological hallmark of heat-shock response in yeast and protects of proteins and membranes against a variety of stresses. This family is found in conjunction with pfam07492 in fungi.	8.87457e-122
NZ_CP022163.1\|WP_095977702.1\|3078134_3079502_-\|DUF2156-domain-containing-protein	gnl\|CDD\|378310	pfam09924, DUF2156, Uncharacterized conserved protein (DUF2156). This domain, found in various hypothetical prokaryotic proteins, has no known function.	7.49463e-34
NZ_CP022163.1\|WP_095977709.1\|3085582_3087064_+\|FAD-dependent-monooxygenase	gnl\|CDD\|236199	PRK08244, PRK08244, monooxygenase.	0

>NZ_CP022163.1|WP_095977709.1|3085582_3087064_+|FAD-dependent-monooxygenase
MRNTVDVAVVGGGPVGWMVACELALAGVSVSVHERRTERVKQSRAMTLHPRSLEILALRGLADRFLARGLPLPTAHYGVLDTRLDFSALDTAFPFTLFIPQAVTEALLEERARELGVDIHRGHQVTGLRQDPEGVDVEGTREGGTFRVRARYVVGADGARSIARTLAGIPFQGTETTMSLMLGDVVFGTLPDQPAWTTVNEHGTLMVAPLGDGRHHRVVMNDPLRSGVPVSEPVTLEELARSLRSIEGSDFGMHSPLWLSRFGNETKLAATYRSGRVFLAGDAAHIHLPAGGQGLNVGLQDAMNLGWKLAGVLRGLAPEALLDSYHRERHPVGASLLRNTLSQTALISTFNPAGLALRETVSALLTLPDANRKLAEQIAALDVAYAEPPLPAPPGLDTVSGLPGGRLPDLILRGTEGASHSLYSLYSLMHEGRWLLLRREDSAPRPALTAAWAEWTNVVTADIPAREKDWGAWTSLWVRPDGHLGYVAHGGTP
>NZ_CP022163.1|WP_095977708.1|3084848_3085505_-|TetR/AcrR-family-transcriptional-regulator-C-terminal-domain-containing-protein
MRIQREKVVRAALALLDEEGIEGVTMRKLAQRLKVQAPSFYWHFANKQALLDGMADALVESVARSVDPEAPWDEVLRGVAAELRQALRSRRDGARVFAGTYVVTENVLRVSEAMIGALRRAGASSRVAAWGCFSLVNYVLGFTMEEQGLEPRSGIDAAEFALRRERFTTLAPTRFPHVFEALADIFDEDLDARFVFGLERLITGLRADLDGSERLPGP
>NZ_CP022163.1|WP_095977707.1|3083465_3084758_-|MFS-transporter
MTAPDASARPPSVFRHRDFRLYQLVRLCAVFAMQVESVAIGWQVYEMTGSALALGYTGLAQFLPFVSFALVGGQVADRVDRRAILIVCQSVMLLCSLLLLAFSLGHIRDVRFVYGVLVLFGTARAFYAPASSALVPRLVPAEELTRAVAVNSSTWQVATIAGPAVGGLLYGWGGATGAYVGSAALCALTVVGMLSLKVRTGQVSRETFSLETLFAGFRFVRRQRMLLGSITLDLFAVLLGGAVALLPIYARDVLHTGPWGMGLLRSAPAAGAAVMAVFLASRPLGGRAGWKMFIAVAIFGLATLVFGLSHSLPLSLVALGVAGAADMVSVVVRSTLEMVATPDEMRGRVGAVNMMCVGASNELGEFRAGAFAEHMGAVSAVVSGAVGTLIVVGLWAWGFPELRRVDHLEQAAREPLPPEAPEALSAPPAH
>NZ_CP022163.1|WP_095977706.1|3081804_3083472_+|trehalase
MAGARRSRGPRWWPGLLVVLHALTASAAPPPPSDYADVRAYIARTWDVLTRSLDTCEVLKDPKVPQRSVLFLPKDFPEPESVRRLRQKCPQVRVERLPEDVTGPGQVDIRALGTHGLLYLEHPYVVPGGRFNEMYGWDSYFIVRGLVRDGRRELAQGMVRNFFFELEHYGAVLNANRTYYLSRSQPPFLTSMVRAVHEGLDEAAGRAWLTEAYPSLVREHGLWMKQAHLAGTTGLSRYFDFGLGPVPEIEDDQARYYRDVVGYFLSHPEEGKPFLREAPQGSTPESAEAPVFITQVCQRDVSATLCTAQRSVTFTPDFYQGDRAMRESGFDISFRFGPFSARTHHFAAVDLNSLLYKAETDLEFIATRLGRAAEAREWKERARQRKALVDRYLWEAQRGLYFDYDTESGQRTTYEYATTFYPLWAGLASREQAKAVAGNLGLFEQPGGLAMSTRETSAQWDLPYGWAPIQLLAIEGLRRYGHDADADRLSRKFLDMVAENFRREHTLREKYDVVKRTTEVQVTKGYALNVAGFGWTNGVFLELWRKLEPAPSRAQ
>NZ_CP022163.1|WP_095977705.1|3081045_3081714_-|hypothetical-protein
MPPRAPLFQLHDTALPGADFTRLWRRVRALGSERLRQTYQTTFWFDLGEPSNVVEEAILDLRPRVPVKGRLAGVEWWLSRMRTTDVQVDFHQDRDEKLALRGGPLVHPRFTSLLFMNRVRGGALAVTRAPPCEDNPSLAPDTDDFDLAAPRPNRFVCFRGDLTHGVLDAHNQIPDGKLPGTSRLRVTLVMNWWNQRPTDLPTFAEARVYRSLASRRHVGPAR
>NZ_CP022163.1|WP_095977704.1|3080382_3080967_+|hypothetical-protein
MKRLSLALLCPLLLAACSAQMAVDSEPTNATIPITSIGDPVYVEVAVDLPDETQELDVLINDVSATFAVYNPSTMFTLETSAKVSLTGTAVPDEPLFYYSESQLPAYYATAGDLLYPPRVFKPGERSDVSVTSPTLTQALGKQRVWIIVSNTITRAGIGTQPLPLEIRLENIVIHATVSKEFRGLEGLLGIGGL
>NZ_CP022163.1|WP_157774913.1|3079651_3080386_+|hypothetical-protein
MKPRTVFPGPRLSQAAGLLLCALTVLVPATRAHAFSHTGNARLLATDEAAPIKHAVIGLQRTALPLALGIVVDTSLLADAALAANVGLRWGIEAGRHRFVVGARYTQFLGNSIVADAISRQASQVKSFDVDFSGPSAYALYGVVLGPLLVQAELRHSRYQTTSTTATGAVVFNFAHRFAVVGELGVRVNKVGHPLRGALGLRYAGEGLGVSLGVAYVDVTEALLPYNDGRIPFLPAFDLSWTFQ
>NZ_CP022163.1|WP_095977702.1|3078134_3079502_-|DUF2156-domain-containing-protein
MRDSNEAVRARVLELLKRHGWNATSFQVVEPGYLYWFDGDDACVAYVDTGWAWVTAGAPIAPVERLAEVTARFQARAAEEGRRVCFFAVEQRLLQAVPLRALTIGEQPVWDPRYWERSVRESRHLREQLRRARAKGVRVREVSARELETPGSPVRVGVDRLMARWLESRRMAPMGFLVQLTPYEQVDERRSFVAERDGEVVAFLSAVPVYARNGWFVQHLLRDRRAPNGTVETLVDAVMRDAAAEGRSYLTLGLAPLSGAVPGWLRVARRLGKPFYDFEGLRAFKTRLRPHAWDHIHLARPAAASGALASVYDALSAFAQGGLLRFGGVTLLCRPQLLVWLLAVLLVPWTMLLALPTTTPYFPSRLVQGAWVLFDVGLTVGLFSLVRRWRRGLASLLASAISADACVTLLEAVLYNLPRVRGPVDWFVMAVAVLGPSLAAVLLLWAREHPTLQPA
>NZ_CP022163.1|WP_095977701.1|3077896_3078127_+|DUF2171-domain-containing-protein
MIDPGDIHEGMTVRDRTGRKLGTVANVGDTHFELGQGSPARRDYMVHFHRVDRVQGVDVYLAPTRTSLPSEEDTRQ
>NZ_CP022163.1|WP_002621977.1|3076756_3077791_+|rod-shape-determining-protein
MFDWLHTLFSRDLAIDLGTANTLIYIRGQGIVSNEPSVVAVQQDARGGKKVLAVGKEAKEMLGRTPGNIVAIRPMKDGVIADFEITAAMLRYFIQTAHNRKSLVSPRIVIGIPSGITEVERRAVREAAANAGAREVYLIEQPMAAAIGAGLPVTEPSGNMIVDIGGGTSDVAVISLAGIVFAKSVRIGGDKLDEAIIQYVKRKYNLLIGERTAELIKMGIGTAYPTEEVMTMEIKGRDLVAGVPRTLTVSSDEVRDALAEPVNGIVEAVKLTLERTPPELAGDIADRGIVLAGGGALLKNLDTLLREETGLPVFLAEDPLSAVVMGAGKALETLDILRQVCQPG
>NZ_CP022163.1|WP_157774914.1|3088615_3089674_-|hypothetical-protein
MATPLEGEPSLPPRACIPWISTVPPLEATACGVTSVFAHGTSQRARYDADNRLLELRTYDAVGALASVETHTWWEDLELRGRVDYADGRFEQTEWTYDAWRRLLSRVTTGSSRSSAKSLEFTYDAQGRVDEVFGAYNTFELWSQYAYDAQGRLVSINTEGVMCGGGETRCATLSYWPDGQLKRHAWIEGRYNSYVDEYSALGQLIHSTWEFTDSRGESTRAYDAAGRQIRLREDLFAPVSQRAFHSLTTRVHDPGGWRERFARDALCYEPVEGSGCDPDVDETHQRLTRRTTLICGTQLVALDEWDSNEDGVVDAHRTHERDSTGRLVREVYSGTAGLDAGPVRRDFQYDCP
>NZ_CP022163.1|WP_157774915.1|3090092_3090524_-|nuclear-transport-factor-2-family-protein
MSASFKTTLLAALAALTLGASAQASPPGTQEVWRHHINAWNDKDVAAITSDYTDSSILILNNQVFHGKAAIAHVFSQLFQIFSTGENKVDPPTIHGRTLYITWHYAPKNEKTFFGSDSFIVENGKIQVQTIASELYISHPVTH
>NZ_CP022163.1|WP_157774916.1|3090802_3092077_+|hypothetical-protein
MNARRSRTSRGVLLLMALSAAGCGTPVEPDASGEARALTIDEEFTRLSRRVPGFGGYYYDSAGALNVVLTQPTHQLAAVRELLSARGVRGSDTLLARQGRYDFEDLNRWRGRLEAEPLAGLVFTDVDEVNNRITLGMTHPDPEQVAAAMARLLIPADAVHLEQAAPNEQHQTAFTYVHQQNRPLAAGQQIKRFSNGYIYFCTLGFNVRRNGSLGFFTNTHCTNEGTVHYQGSPRIGVTTEDPLFWSNASVVYDGVTYTCSGTNVCRFSDAAYVEYDAGVQSSVKHGYIYRTEVENAYTGGAPTGIAPLKIDEAQPFFRIVGKAYHVAVGEKIHKVGQRTGWTSGLVTHSCVNTLNGSTRLFCQMKGDGAGYDGDSGSPVFRRVADSEQDVELVGIYWGSAMSPIGSIEQDFGPLDVAADSASTP
>NZ_CP022163.1|WP_157774917.1|3092133_3092544_-|nuclease-A-inhibitor-family-protein
MNTQRAAVLKSLLLSAHGLLFISETDAPFTPVDAPGSPFASLDDAAVRRLAGHPDADPVETRGVDEFFRNAVQEQPWHTPEETATVRRYRALVALLHASLPDARVYRVGAVSIDVLILGTGPGGGALGLATKVVET
>NZ_CP022163.1|WP_170115494.1|3092712_3093624_+|DNA/RNA-non-specific-endonuclease
MFLKRFVRGAAVASLSVLFACGPQEGDEALDSLSPGIENTSVPPEDIGSYSSAAGASISVHLKLGMPDSSTTSTSNPNRYLSVKSQYVISYNGSRKTPNWTAWQLNKSWMGSTSRQDTFRPDNTLPSSIPQASLADYSGSGYDRGHMCPSADRTLNTTDNSNTFYLTNMLPQAPNNNQGPWEQLESYSRTLVSSGKELFIMSGPIYSGTISTIGSGKVAVPTSTWKVITVMNATGQGPTNVTTSTRVIAVVMPNSDSKISKSADWHNYRVTARSIEQQTGLNFMADVAQSVQDVIETRVDTAQ
>NZ_CP022163.1|WP_095977716.1|3093889_3094444_+|Wall-associated-protein-precursor
MLSSLMLVVLTQVACTPGETSLVCSCKQGMVSACMTLAGDDARKAAQVLDEVQGLLEQATWKAGEEQEKQRLQAAAESLSQTLESSEPPHCKGQNHHLISRPIARGLEEHPRLRGLYKPRDPRFVSRAKDEQAHCGYQEWHREIDDEVVRWLKRTPGATPKEFMDKLREIYGRPEMIARFPHGF
>NZ_CP022163.1|WP_095982745.1|3094898_3095120_+|hypothetical-protein
MTRVDAIHGFVLEPGSWRGEDIFRPRGLVGDLVVSERFKDFAGRHGLTNMVLTPTEQYMWDPSHLGPAPLSKT
>NZ_CP022163.1|WP_157774918.1|3095249_3096029_+|pentapeptide-repeat-containing-protein
MTTYIRKREGVELFSHEGSLSEALTVATRKGVDLSRAVLDGADLSNTDLENLNLRQVSLRGANLRGANLENVNLSGANLHEADLRGANLGNTDMREVVLADANLDGANLEKARMVGANLMGLKAQGANFERADLARANLEGSNLEGSNLEDTRLSEANLSRVNLRRANLESANLDGANLTRADLRSANLEKAALRDAVLEGANCRDANLEKAQLERANLTNACLDHAQLDRANLTAAITTGASFHEASLDRVTGFQPPE
>NZ_CP022163.1|WP_095977718.1|3096189_3097623_+|serine/threonine-protein-kinase
MSTNPGEATLYSEALAPGTQVGRWRVVEPLGMGGQGAVYRVEDTEHPGDFYALKLALHARDERAEREVALMMTRAAHPHVVGFHGCARWPHPREGCLGFVMDWVPGQALDVWAETEGTTFRQLAGAGATVARTLGELHARGVLHRDLKPEHILLRASDGQPVLLDFGVGWYEGAAPLTTGPLPPATLYLLSPEAVRFLWRSSESPGTHYTFQPTDDLYALGVSLYRATTGHYPFSEWLPSELLQFAIVHVQPLAPVLVNPRVPRALSDVIVRLLAKDPQERYPSGAALHAALVAATHGEQAAWDSSIFEWEERPPEKEGALPERHLVRPPRPKPSWTSPPPDPVHVARRGRWTRRLVCAAAVLLMLVPLNRLALVTPSVRVPDEEWATDVRVDPASVQSEQAPLPARNQKLAPCTEGLEVELSGACWHSLRQRPPNCPRQTVAFKGQCLWPVPKSRPIPTSVDGGTPDAQEDSTTPP
>NZ_CP022163.1|WP_095977719.1|3097609_3098179_-|hypothetical-protein
MPKKYFKLTQEVDGSGGWDLGNPTNPQGLEVDNPWMYREGMPVSESGRLKIPIGRPGRVLDFTLAGFSIPVVHVRVASLFMELAPRDTQLLSVDIQGQPDSFRILVATRLIRCIDDEASAEVEYWTPEDGRPEKEGQYRDVYGMRIDTAKVGDAKVFRTWGWTIALIVSEEIKEALEHIGATGVKFTEV

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Crispr_ID: NZ_CP022163_7

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP022163_7

3095740-3095882

Orphan

Consensus_repeat	Method
TGCGCGGCGCCAACCTGGAGAAC	CRISPRCasFinder

2 spacers

The CRISPR arrays of NZ_CP022163_7

>merge|NZ_CP022163|7|3095740-3095882|CRISPRCasFinder
TGCGGCGCGCCAACCTGGAGAGTGCCAACCTCGACGGCGCGAACCTGACGCGCGCCGACCTGCGCTCCGCCAACCTCGAGAAAGCCGCCCTGCGCGACGCCGTCCTCGAAGGCGCCAACTGCCGGGATGCCAACCTCGAGAAG

>NZ_CP022163|7|6|3095740-3095882|CRISPRCasFinder
TGCGGCGCGCCAACCTGGAGAGT	GCCAACCTCGACGGCGCGAACCTGACGCGCGCCGACC
TGCGCTCCGCCAACCTCGAGAAA	GCCGCCCTGCGCGACGCCGTCCTCGAAGGCGCCAACT
GCCGGGATGCCAACCTCGAGAAG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP022163.1\|WP_095977710.1\|3087503_3088436_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095977716.1\|3093889_3094444_+\|Wall-associated-protein-precursor	unknown	unknown	unknown
NZ_CP022163.1\|WP_157774914.1\|3088615_3089674_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095977726.1\|3106276_3107116_+\|SDR-family-oxidoreductase	unknown	unknown	gnl\|CDD\|187632
NZ_CP022163.1\|WP_095977708.1\|3084848_3085505_-\|TetR/AcrR-family-transcriptional-regulator-C-terminal-domain-containing-protein	unknown	unknown	gnl\|CDD\|172294
NZ_CP022163.1\|WP_095977723.1\|3101180_3103736_+\|M1-family-metallopeptidase	unknown	unknown	gnl\|CDD\|341064
NZ_CP022163.1\|WP_095977725.1\|3104916_3105984_-\|DUF2804-domain-containing-protein	unknown	unknown	gnl\|CDD\|378522
NZ_CP022163.1\|WP_170115494.1\|3092712_3093624_+\|DNA/RNA-non-specific-endonuclease	unknown	unknown	gnl\|CDD\|224777
NZ_CP022163.1\|WP_095977727.1\|3107128_3108172_+\|MBL-fold-metallo-hydrolase	unknown	unknown	gnl\|CDD\|293841
NZ_CP022163.1\|WP_157774919.1\|3098194_3099466_-\|AHH-domain-containing-protein	unknown	unknown	gnl\|CDD\|379603
NZ_CP022163.1\|WP_157774915.1\|3090092_3090524_-\|nuclear-transport-factor-2-family-protein	unknown	unknown	gnl\|CDD\|378915
NZ_CP022163.1\|WP_157774916.1\|3090802_3092077_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095977721.1\|3099748_3100315_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095977709.1\|3085582_3087064_+\|FAD-dependent-monooxygenase	unknown	unknown	gnl\|CDD\|236199
NZ_CP022163.1\|WP_095977722.1\|3100437_3101019_-\|HutD-family-protein	unknown	unknown	gnl\|CDD\|377578
NZ_CP022163.1\|WP_095982745.1\|3094898_3095120_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095977719.1\|3097609_3098179_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095977724.1\|3103755_3104841_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_157774917.1\|3092133_3092544_-\|nuclease-A-inhibitor-family-protein	unknown	unknown	gnl\|CDD\|369598
NZ_CP022163.1\|WP_095977718.1\|3096189_3097623_+\|serine/threonine-protein-kinase	unknown	unknown	gnl\|CDD\|270916

Protein	Function_ID	Function_description	E-value
NZ_CP022163.1\|WP_095977722.1\|3100437_3101019_-\|HutD-family-protein	gnl\|CDD\|377578	pfam05962, HutD, HutD. HutD from Pseudomonas fluorescens SBW25 is a component of the histidine uptake and utilisation operon. HutD is operonic with the well characterized repressor protein HutC. Genetic analysis using transcriptional fusions (lacZ) and deletion mutants shows that hutD is necessary to maintain fitness in environments replete with histidine. Evidence outlined by Zhang & Rainey (2007) suggests that HutD functions as a governor that sets an upper bound on the level of hut operon transcription. The mechanistic basis is unknown, but in silico molecular docking studies based on the crystal structure of PA5104 (HutD from Pseudomonas aeruginosa) show that urocanate (the first breakdown product of histidine) docks with the active site of HutD.	1.80818e-52
NZ_CP022163.1\|WP_095977708.1\|3084848_3085505_-\|TetR/AcrR-family-transcriptional-regulator-C-terminal-domain-containing-protein	gnl\|CDD\|172294	PRK13756, PRK13756, TetR family transcriptional regulator.	9.76401e-35
NZ_CP022163.1\|WP_095977723.1\|3101180_3103736_+\|M1-family-metallopeptidase	gnl\|CDD\|341064	cd09601, M1_APN-Q_like, Peptidase M1 aminopeptidase N catalytic domain family which includes aminopeptidase N (APN), aminopeptidase Q (APQ), tricorn interacting factor F3, and endoplasmic reticulum aminopeptidase 1 (ERAP1). This M1 peptidase family includes eukaryotic and bacterial members: the catalytic domains of aminopeptidase N (APN), aminopeptidase Q (APQ, laeverin), endoplasmic reticulum aminopeptidase 1 (ERAP1) as well as tricorn interacting factor F3. Aminopeptidase N (APN; CD13; alanyl aminopeptidase; EC 3.4.11.2), a type II integral membrane protease, preferentially cleaves neutral amino acids from the N-terminus of oligopeptides and is present in a variety of human tissues and cell types (leukocyte, fibroblast, endothelial and epithelial cells). APN expression is dysregulated in inflammatory diseases such as chronic pain, rheumatoid arthritis, multiple sclerosis, systemic sclerosis, systemic lupus erythematosus, polymyositis/dermatomyosytis and pulmonary sarcoidosis, and is enhanced in tumor cells such as melanoma, renal, prostate, pancreas, colon, gastric and thyroid cancers. It is considered a marker of differentiation since it is predominantly expressed on stem cells and on cells of the granulocytic and monocytic lineages at distinct stages of differentiation. Thus, APN inhibition may lead to the development of anti-cancer and anti-inflammatory drugs. ERAP1, also known as endoplasmic reticulum aminopeptidase associated with antigen processing (ERAAP), adipocyte derived leucine aminopeptidase (A-LAP), or aminopeptidase regulating tumor necrosis factor receptor I (THFRI) shedding (ARTS-1), associates with the closely related ER aminopeptidase ERAP2, for the final trimming of peptides within the ER for presentation by MHC class I molecules. ERAP1 is associated with ankylosing spondylitis (AS), an inflammatory arthritis that predominantly affects the spine. ERAP1 also aids in the shedding of membrane-bound cytokine receptors. The tricorn interacting factor F3, together with factors F1 and F2, degrades the tricorn protease products, producing free amino acids, thus completing the proteasomal degradation pathway. F3 is homologous to F2, but not F1, and shows a strong preference for glutamate in the P1' position. APQ, also known as laeverin, is specifically expressed in human embryo-derived extravillous trophoblasts (EVTs) that invade the uterus during early placentation. It cleaves the N-terminal amino acid of various peptides such as angiotensin III, endokinin C, and kisspeptin-10, all expressed in the placenta in large quantities. APN is a receptor for coronaviruses, although the virus receptor interaction site seems to be distinct from the enzymatic site and aminopeptidase activity is not necessary for viral infection. APNs are also putative Cry toxin receptors. Cry1 proteins are pore-forming toxins that bind to the midgut epithelial cell membrane of susceptible insect larvae, causing extensive damage. Several different toxins, including Cry1Aa, Cry1Ab, Cry1Ac, Cry1Ba, Cry1Ca and Cry1Fa, have been shown to bind to APNs; however, a direct role of APN in cytotoxicity has been yet to be firmly established.	0
NZ_CP022163.1\|WP_170115494.1\|3092712_3093624_+\|DNA/RNA-non-specific-endonuclease	gnl\|CDD\|224777	COG1864, NUC1, DNA/RNA endonuclease G, NUC1 [Nucleotide transport and metabolism].	2.50059e-68
NZ_CP022163.1\|WP_095977727.1\|3107128_3108172_+\|MBL-fold-metallo-hydrolase	gnl\|CDD\|293841	cd16283, RomA-like_MBL-fold, Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain. Derepression of the romA-ramA locus results in a multidrug-resistance phenotype. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.	5.49222e-80
NZ_CP022163.1\|WP_095977725.1\|3104916_3105984_-\|DUF2804-domain-containing-protein	gnl\|CDD\|378522	pfam10974, DUF2804, Protein of unknown function (DUF2804). This is a family of proteins with unknown function.	5.55875e-83
NZ_CP022163.1\|WP_157774917.1\|3092133_3092544_-\|nuclease-A-inhibitor-family-protein	gnl\|CDD\|369598	pfam07924, NuiA, Nuclease A inhibitor-like protein. This family consists of protein sequences that are similar to the nuclease A inhibitor expressed by bacteria of the genus Anabaena ((NuiA). This sequence is organized to form an alpha-beta-alpha sandwich fold, which is similar to the PR-1-like fold. NuiA interacts with nuclease A by means of residues located at one end of the molecule, including residues making up the loop between helices III and IV and the loop between strands C and D. The mechanism of inhibition of nuclease A by NuiA is as yet incompletely understood.	5.43781e-44
NZ_CP022163.1\|WP_095977726.1\|3106276_3107116_+\|SDR-family-oxidoreductase	gnl\|CDD\|187632	cd05374, 17beta-HSD-like_SDR_c, 17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs. 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.	6.34232e-83
NZ_CP022163.1\|WP_157774915.1\|3090092_3090524_-\|nuclear-transport-factor-2-family-protein	gnl\|CDD\|378915	pfam12680, SnoaL_2, SnoaL-like domain. This family contains a large number of proteins that share the SnoaL fold.	1.70116e-09
NZ_CP022163.1\|WP_095977709.1\|3085582_3087064_+\|FAD-dependent-monooxygenase	gnl\|CDD\|236199	PRK08244, PRK08244, monooxygenase.	0
NZ_CP022163.1\|WP_157774919.1\|3098194_3099466_-\|AHH-domain-containing-protein	gnl\|CDD\|379603	pfam14412, AHH, A nuclease family of the HNH/ENDO VII superfamily with conserved AHH. AHH is a predicted nuclease of the HNH/ENDO VII superfamily of the treble clef fold. The name is derived from the conserved motif, AHH. It is found in bacterial polymorphic toxin systems and functions as a toxin module. Like WHH and LHH, the AHH nuclease contains 4 conserved histidines of which, the first one is predicted to bind a metal-ion and the other three ones are involved in activation of a water molecule for hydrolysis.	2.88223e-26
NZ_CP022163.1\|WP_095977718.1\|3096189_3097623_+\|serine/threonine-protein-kinase	gnl\|CDD\|270916	cd14014, STKc_PknB_like, Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.	9.90926e-55

>NZ_CP022163.1|WP_095982745.1|3094898_3095120_+|hypothetical-protein
MTRVDAIHGFVLEPGSWRGEDIFRPRGLVGDLVVSERFKDFAGRHGLTNMVLTPTEQYMWDPSHLGPAPLSKT
>NZ_CP022163.1|WP_095977716.1|3093889_3094444_+|Wall-associated-protein-precursor
MLSSLMLVVLTQVACTPGETSLVCSCKQGMVSACMTLAGDDARKAAQVLDEVQGLLEQATWKAGEEQEKQRLQAAAESLSQTLESSEPPHCKGQNHHLISRPIARGLEEHPRLRGLYKPRDPRFVSRAKDEQAHCGYQEWHREIDDEVVRWLKRTPGATPKEFMDKLREIYGRPEMIARFPHGF
>NZ_CP022163.1|WP_170115494.1|3092712_3093624_+|DNA/RNA-non-specific-endonuclease
MFLKRFVRGAAVASLSVLFACGPQEGDEALDSLSPGIENTSVPPEDIGSYSSAAGASISVHLKLGMPDSSTTSTSNPNRYLSVKSQYVISYNGSRKTPNWTAWQLNKSWMGSTSRQDTFRPDNTLPSSIPQASLADYSGSGYDRGHMCPSADRTLNTTDNSNTFYLTNMLPQAPNNNQGPWEQLESYSRTLVSSGKELFIMSGPIYSGTISTIGSGKVAVPTSTWKVITVMNATGQGPTNVTTSTRVIAVVMPNSDSKISKSADWHNYRVTARSIEQQTGLNFMADVAQSVQDVIETRVDTAQ
>NZ_CP022163.1|WP_157774917.1|3092133_3092544_-|nuclease-A-inhibitor-family-protein
MNTQRAAVLKSLLLSAHGLLFISETDAPFTPVDAPGSPFASLDDAAVRRLAGHPDADPVETRGVDEFFRNAVQEQPWHTPEETATVRRYRALVALLHASLPDARVYRVGAVSIDVLILGTGPGGGALGLATKVVET
>NZ_CP022163.1|WP_157774916.1|3090802_3092077_+|hypothetical-protein
MNARRSRTSRGVLLLMALSAAGCGTPVEPDASGEARALTIDEEFTRLSRRVPGFGGYYYDSAGALNVVLTQPTHQLAAVRELLSARGVRGSDTLLARQGRYDFEDLNRWRGRLEAEPLAGLVFTDVDEVNNRITLGMTHPDPEQVAAAMARLLIPADAVHLEQAAPNEQHQTAFTYVHQQNRPLAAGQQIKRFSNGYIYFCTLGFNVRRNGSLGFFTNTHCTNEGTVHYQGSPRIGVTTEDPLFWSNASVVYDGVTYTCSGTNVCRFSDAAYVEYDAGVQSSVKHGYIYRTEVENAYTGGAPTGIAPLKIDEAQPFFRIVGKAYHVAVGEKIHKVGQRTGWTSGLVTHSCVNTLNGSTRLFCQMKGDGAGYDGDSGSPVFRRVADSEQDVELVGIYWGSAMSPIGSIEQDFGPLDVAADSASTP
>NZ_CP022163.1|WP_157774915.1|3090092_3090524_-|nuclear-transport-factor-2-family-protein
MSASFKTTLLAALAALTLGASAQASPPGTQEVWRHHINAWNDKDVAAITSDYTDSSILILNNQVFHGKAAIAHVFSQLFQIFSTGENKVDPPTIHGRTLYITWHYAPKNEKTFFGSDSFIVENGKIQVQTIASELYISHPVTH
>NZ_CP022163.1|WP_157774914.1|3088615_3089674_-|hypothetical-protein
MATPLEGEPSLPPRACIPWISTVPPLEATACGVTSVFAHGTSQRARYDADNRLLELRTYDAVGALASVETHTWWEDLELRGRVDYADGRFEQTEWTYDAWRRLLSRVTTGSSRSSAKSLEFTYDAQGRVDEVFGAYNTFELWSQYAYDAQGRLVSINTEGVMCGGGETRCATLSYWPDGQLKRHAWIEGRYNSYVDEYSALGQLIHSTWEFTDSRGESTRAYDAAGRQIRLREDLFAPVSQRAFHSLTTRVHDPGGWRERFARDALCYEPVEGSGCDPDVDETHQRLTRRTTLICGTQLVALDEWDSNEDGVVDAHRTHERDSTGRLVREVYSGTAGLDAGPVRRDFQYDCP
>NZ_CP022163.1|WP_095977710.1|3087503_3088436_+|hypothetical-protein
MGWPLRMFQEEGYYFVTSRCFQGRLLLHPSPEVNEVVGGVLARAVEQSNGSVRLHAFTFLSNHFHLLVWAKGAALAGFMQYLRANLSRKVGRLVDWSGGFWERRYSAEPVLDDTALVGRLRYVLAHGVKEGLVERSIEWPGLTCLPQLLGPARRLFRWFNWTKRWSKRGHADGGDARGRFAEDWAEPVALELAPLPCWEGFEEEQRQREVKALLREVEAEACTRGRSVMGVMAVQAQHPHTRPEHLKRSPRPLGHASTRQALKELREQYRAFVTAFREAAAQWRRGNYSARFPLFSFPPRVLPGRTAQIL
>NZ_CP022163.1|WP_095977709.1|3085582_3087064_+|FAD-dependent-monooxygenase
MRNTVDVAVVGGGPVGWMVACELALAGVSVSVHERRTERVKQSRAMTLHPRSLEILALRGLADRFLARGLPLPTAHYGVLDTRLDFSALDTAFPFTLFIPQAVTEALLEERARELGVDIHRGHQVTGLRQDPEGVDVEGTREGGTFRVRARYVVGADGARSIARTLAGIPFQGTETTMSLMLGDVVFGTLPDQPAWTTVNEHGTLMVAPLGDGRHHRVVMNDPLRSGVPVSEPVTLEELARSLRSIEGSDFGMHSPLWLSRFGNETKLAATYRSGRVFLAGDAAHIHLPAGGQGLNVGLQDAMNLGWKLAGVLRGLAPEALLDSYHRERHPVGASLLRNTLSQTALISTFNPAGLALRETVSALLTLPDANRKLAEQIAALDVAYAEPPLPAPPGLDTVSGLPGGRLPDLILRGTEGASHSLYSLYSLMHEGRWLLLRREDSAPRPALTAAWAEWTNVVTADIPAREKDWGAWTSLWVRPDGHLGYVAHGGTP
>NZ_CP022163.1|WP_095977708.1|3084848_3085505_-|TetR/AcrR-family-transcriptional-regulator-C-terminal-domain-containing-protein
MRIQREKVVRAALALLDEEGIEGVTMRKLAQRLKVQAPSFYWHFANKQALLDGMADALVESVARSVDPEAPWDEVLRGVAAELRQALRSRRDGARVFAGTYVVTENVLRVSEAMIGALRRAGASSRVAAWGCFSLVNYVLGFTMEEQGLEPRSGIDAAEFALRRERFTTLAPTRFPHVFEALADIFDEDLDARFVFGLERLITGLRADLDGSERLPGP
>NZ_CP022163.1|WP_095977718.1|3096189_3097623_+|serine/threonine-protein-kinase
MSTNPGEATLYSEALAPGTQVGRWRVVEPLGMGGQGAVYRVEDTEHPGDFYALKLALHARDERAEREVALMMTRAAHPHVVGFHGCARWPHPREGCLGFVMDWVPGQALDVWAETEGTTFRQLAGAGATVARTLGELHARGVLHRDLKPEHILLRASDGQPVLLDFGVGWYEGAAPLTTGPLPPATLYLLSPEAVRFLWRSSESPGTHYTFQPTDDLYALGVSLYRATTGHYPFSEWLPSELLQFAIVHVQPLAPVLVNPRVPRALSDVIVRLLAKDPQERYPSGAALHAALVAATHGEQAAWDSSIFEWEERPPEKEGALPERHLVRPPRPKPSWTSPPPDPVHVARRGRWTRRLVCAAAVLLMLVPLNRLALVTPSVRVPDEEWATDVRVDPASVQSEQAPLPARNQKLAPCTEGLEVELSGACWHSLRQRPPNCPRQTVAFKGQCLWPVPKSRPIPTSVDGGTPDAQEDSTTPP
>NZ_CP022163.1|WP_095977719.1|3097609_3098179_-|hypothetical-protein
MPKKYFKLTQEVDGSGGWDLGNPTNPQGLEVDNPWMYREGMPVSESGRLKIPIGRPGRVLDFTLAGFSIPVVHVRVASLFMELAPRDTQLLSVDIQGQPDSFRILVATRLIRCIDDEASAEVEYWTPEDGRPEKEGQYRDVYGMRIDTAKVGDAKVFRTWGWTIALIVSEEIKEALEHIGATGVKFTEV
>NZ_CP022163.1|WP_157774919.1|3098194_3099466_-|AHH-domain-containing-protein
MSQDGLLIHLPRTGEAGPVELDEDVFSRAIANEVQRTRPPANPEMAARELFEVPPHSGWYGYTQRHGVVPLNGQSRALLGADADVRVTQEYLRFCAAIGMPGDCRKVLMNSPVLVGDGRYALAMSFALEAVIPEMMEAFKGMADPEAIKASILWTMTIYAAMWLAPEPVFSKGLATAVTASFICYVGVDTFWTLIQGWRRMVEVAELAHSFSEIREAGGKYGRVMGKNAARAFALLLTAAIGQTASSFSSKVTTLPGAAQSSAVGAARGGVRLAEVAQVEAVVVTADAVTIALAPNVVAATAQGMRGTASSPVDAEGPEHHIATDKWTDATHSGGPWTPKFQRIFDRAGMSLNDPANKVHVKGHQGPHPQTYHERVYERLDEATKGCGSIQQCQKVLTAELHRLAKQISTKGTLLNKLVTRSQ
>NZ_CP022163.1|WP_095977721.1|3099748_3100315_-|hypothetical-protein
MPKRYFDLSDDVCVSGRWHIRPPMAEDGQAVDPWMFTEGQPLQLTTKLRMALRVKGRPLDFTLAGLDVPVVHAKVATLFAELAPQDIQLFPVDIEGQPEQFSILVATKLIQCIDESASDEVRRWRAEDGCPEKTGNYRVVSGMRIDTSKVGDAKVFRTWGWSVALIVSEEIKEALEHIGATGVKFTGV
>NZ_CP022163.1|WP_095977722.1|3100437_3101019_-|HutD-family-protein
MRRWGPADYRDMPWKNGGGVTRELLRRPHPTRPEGFGVRLSIATVAAAGPFSLFPGVDRHLLLLEGQGMALTRAGASEEVVVAPGQPLFSFPGEDAWDCRLLGGPVRDFNVMVDRALAEASLERVHLEAGARHRLAASPGTQWLYGVSGRVQVAGEVLAEEDILEWDAPGALELVGESEATVLIIRLMPRAGR
>NZ_CP022163.1|WP_095977723.1|3101180_3103736_+|M1-family-metallopeptidase
MAHATEDKNFRLPLSVRPRRYAATLTLDMEARAFTGLQTIELELDTPTDEIVLHAIALKLGEVVFRAADGRIIMPAETHEAPLSETVVVRFGEKLPQGQGALDVTWTGRFTEGLRGLYMAGKVAATQFEAADARRLFPCFDEPSFKARWALTVQVPTGLTALSNGALEREESDGNMRRLTFKETEVLSSYLIALVVGPLVGTPEERVEGIPVRTWALPEKAHLTRFGQDAALAALPRLQAYFDLPYAFGKVDQVGIPDFEAGAMENAGLITYREIALLLDPATAPLSVQKRVAEVVTHELAHQWFGNWVTMVWWDDLWLNEAFATWMAYKIVDDWKPDWRVWLDFDSGKAAALHLDALRSTHPIRGEVRNAHEAGESFDLITYEKGGAVLRMIEGFLGQDAFREGMRQYMRKHARANAVADDLWRALAQASSQPVLELANAWIGQSGYPQVGVTVNGRKVKLTQRRFYSEPGVKSDERWPVPMVLKYADAGGVREQRVLLRESEAEVTLEGSGEVKWLVANAGSTGFYRVQYDATGLERLSANVDALEPSERISLLADQWALARSGQATLTAFLDLAGRYGQEEDDAVLDELVGGLAYVEGRLVEGEDQERFRRWVEKLLGAGFKKVGWDAAPGETDRVKLRRAALVRALGGVARSPEIIAEARPRVARALDGDTTALEPNLLDAAVGMVARQGDRALYEKILEKMPVEPDPATQRRYLMALTAFEDPQLADAAQKLFFTEKVKMQDVASFLTGLINNRTGRNMWWAEKQKRWKDVLARTGAAPMLLRRVVESLGALRERKQLDEVRKLLTAHPVEEAKQAMGQTLEKLEQDVVLRERALPEVRAWLQRQK
>NZ_CP022163.1|WP_095977724.1|3103755_3104841_-|hypothetical-protein
MNCSNCGQVVADESLGFCMECGEAFGASAGQGSDEDNPDAHAEGYSDSEWREPRPSVWDTLSRVLAPVRTVAGQLGDVFANILESPSVYGQMPGGSLTFLGLGFVGLALLVSVVPFIEGIGGLGSGVMFGWGVLVLLSEWREVSEAPPREGRFVDAYPAVIDKLPREVWHPGVIQAYALVTCAYALKMVGYGPIALLWLLAAGVLGYEQGRRFFYLLPQDEAALAASAEHPGLHRWVVPGVAVGVLSLLLPWGRMSGLALSIYGVDLPLSVLTLSCLLLLGCYAVKHQGLGGLHPMVLILVAVWLALWLLLMNNIYSPGSWVYLVGVLLIYTAIVRHLIPARPRAEEAPQEEPPPDLDYQG
>NZ_CP022163.1|WP_095977725.1|3104916_3105984_-|DUF2804-domain-containing-protein
MTPERELTLLPAPASVATASGEPRFGTYQGELPEVDLQKLSGPWAPAAARARLLKRKRWHYTLATTREVVALFAVVDVGYSANAFAVAVDLKERKALCDVSFLGAPGPLAEVGNKPGAGLAASFRTLGGRMSATRGPEDERYRLQVDVSRLRTGSLQSFLWNGELMVAGGAPALTVIAPVGGDGFVNVTQKRAGMLASGTLEAGGKRFQLDGGVGGTDYTQGYLARHTAWRWAFLAGRLADGTPVGLNLVEGFNESARVNENALWLGERILPLGRATFEYDRENLMRPWRVRTDDRVVDLSFQPLHVHREDHDFKLVVSHFAQPVGLFEGTLRVDGRTYTLSDMPGVTEDQDMLW
>NZ_CP022163.1|WP_095977726.1|3106276_3107116_+|SDR-family-oxidoreductase
MARVALITGTSSGIGLDTAIHLAQAGFQTVATLRDTTRAGALQERARAAGVSLDIRALDVQSDDSVSTCVREVRERYGRIDVLVNNAGSGFLGTMEQTPMDALRTVMEVNFFGVWRVTQAVFPLMREARSGRIITVTSVGGLLGQPFNDAYCAAKFACEGFLESLAPVATRLGIHLSNIEPGAVHTEFVTNVKAKLSGKPSPGDDLYQPMLDSYMAGAMDAYKAAQSGEDIAKVIVEAATAATPHFRYVTSEWVRGVASRKYTDPTGDSIVTLMGSRLK
>NZ_CP022163.1|WP_095977727.1|3107128_3108172_+|MBL-fold-metallo-hydrolase
MNTPRHLVGLLALALGTSGCFSAPTWKGTPSDHFNGERFVNREPRPRTMSFLDWMAHRKPGAWKGRPDAPFGPRPPERVGPGDLRVTFINHATVLLQLDGLNILTDPIYSERCSPVSFAGPRRMRPPGIRFEDLPPIDVVVISHNHYDHMDVATLLRLQERFPQVRVFAGLGNREFLEGEGLRHVTEVDWWQEFPLSAEVTLVSARTQHFSNRGLGDADGTLWTGYVFRGPHGRTYFAGDTASGSQFTEARERLGPMRLAVLPIGAYKPEAIMSPVHVSPREAVQASVDLGARYSVPMHYGTFRLADDGETDPLWDLAGALVERGDQAPEWWVLAFGEGRDVPPMTP

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Crispr_ID: NZ_CP022163_6

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP022163_6

3095425-3095583

Orphan

Consensus_repeat	Method
TGCGCGGCGCCAACCTGGAGAAC	CRISPRCasFinder

2 spacers

The CRISPR arrays of NZ_CP022163_6

>merge|NZ_CP022163|6|3095425-3095583|CRISPRCasFinder
TGCGCGGTGCCAACCTGCGCGGCGCCAACCTGGAGAACGTGAATCTCTCGGGCGCCAACCTGCACGAGGCCGATTTGCGCGGCGCCAACCTGGGGAACACCGACATGCGCGAGGTCGTCCTCGCGGACGCCAACCTCGATGGCGCCAACCTGGAAAAAG

>NZ_CP022163|6|5|3095425-3095583|CRISPRCasFinder
TGCGCGGTGCCAACCTGCGCGGC	GCCAACCTGGAGAACGTGAATCTCTCGGGCGCCAACCTGCACGAGGCCGATT
TGCGCGGCGCCAACCTGGGGAAC	ACCGACATGCGCGAGGTCGTCCTCGCGGACGCCAACC
TCGATGGCGCCAACCTGGAAAAAG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP022163.1\|WP_095977710.1\|3087503_3088436_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095977716.1\|3093889_3094444_+\|Wall-associated-protein-precursor	unknown	unknown	unknown
NZ_CP022163.1\|WP_157774914.1\|3088615_3089674_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095977726.1\|3106276_3107116_+\|SDR-family-oxidoreductase	unknown	unknown	gnl\|CDD\|187632
NZ_CP022163.1\|WP_095977708.1\|3084848_3085505_-\|TetR/AcrR-family-transcriptional-regulator-C-terminal-domain-containing-protein	unknown	unknown	gnl\|CDD\|172294
NZ_CP022163.1\|WP_095977723.1\|3101180_3103736_+\|M1-family-metallopeptidase	unknown	unknown	gnl\|CDD\|341064
NZ_CP022163.1\|WP_095977725.1\|3104916_3105984_-\|DUF2804-domain-containing-protein	unknown	unknown	gnl\|CDD\|378522
NZ_CP022163.1\|WP_170115494.1\|3092712_3093624_+\|DNA/RNA-non-specific-endonuclease	unknown	unknown	gnl\|CDD\|224777
NZ_CP022163.1\|WP_095977727.1\|3107128_3108172_+\|MBL-fold-metallo-hydrolase	unknown	unknown	gnl\|CDD\|293841
NZ_CP022163.1\|WP_157774919.1\|3098194_3099466_-\|AHH-domain-containing-protein	unknown	unknown	gnl\|CDD\|379603
NZ_CP022163.1\|WP_157774915.1\|3090092_3090524_-\|nuclear-transport-factor-2-family-protein	unknown	unknown	gnl\|CDD\|378915
NZ_CP022163.1\|WP_157774916.1\|3090802_3092077_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095977721.1\|3099748_3100315_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095977709.1\|3085582_3087064_+\|FAD-dependent-monooxygenase	unknown	unknown	gnl\|CDD\|236199
NZ_CP022163.1\|WP_095977722.1\|3100437_3101019_-\|HutD-family-protein	unknown	unknown	gnl\|CDD\|377578
NZ_CP022163.1\|WP_095982745.1\|3094898_3095120_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095977719.1\|3097609_3098179_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095977724.1\|3103755_3104841_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_157774917.1\|3092133_3092544_-\|nuclease-A-inhibitor-family-protein	unknown	unknown	gnl\|CDD\|369598
NZ_CP022163.1\|WP_095977718.1\|3096189_3097623_+\|serine/threonine-protein-kinase	unknown	unknown	gnl\|CDD\|270916

Protein	Function_ID	Function_description	E-value
NZ_CP022163.1\|WP_095977722.1\|3100437_3101019_-\|HutD-family-protein	gnl\|CDD\|377578	pfam05962, HutD, HutD. HutD from Pseudomonas fluorescens SBW25 is a component of the histidine uptake and utilisation operon. HutD is operonic with the well characterized repressor protein HutC. Genetic analysis using transcriptional fusions (lacZ) and deletion mutants shows that hutD is necessary to maintain fitness in environments replete with histidine. Evidence outlined by Zhang & Rainey (2007) suggests that HutD functions as a governor that sets an upper bound on the level of hut operon transcription. The mechanistic basis is unknown, but in silico molecular docking studies based on the crystal structure of PA5104 (HutD from Pseudomonas aeruginosa) show that urocanate (the first breakdown product of histidine) docks with the active site of HutD.	1.80818e-52
NZ_CP022163.1\|WP_095977708.1\|3084848_3085505_-\|TetR/AcrR-family-transcriptional-regulator-C-terminal-domain-containing-protein	gnl\|CDD\|172294	PRK13756, PRK13756, TetR family transcriptional regulator.	9.76401e-35
NZ_CP022163.1\|WP_095977723.1\|3101180_3103736_+\|M1-family-metallopeptidase	gnl\|CDD\|341064	cd09601, M1_APN-Q_like, Peptidase M1 aminopeptidase N catalytic domain family which includes aminopeptidase N (APN), aminopeptidase Q (APQ), tricorn interacting factor F3, and endoplasmic reticulum aminopeptidase 1 (ERAP1). This M1 peptidase family includes eukaryotic and bacterial members: the catalytic domains of aminopeptidase N (APN), aminopeptidase Q (APQ, laeverin), endoplasmic reticulum aminopeptidase 1 (ERAP1) as well as tricorn interacting factor F3. Aminopeptidase N (APN; CD13; alanyl aminopeptidase; EC 3.4.11.2), a type II integral membrane protease, preferentially cleaves neutral amino acids from the N-terminus of oligopeptides and is present in a variety of human tissues and cell types (leukocyte, fibroblast, endothelial and epithelial cells). APN expression is dysregulated in inflammatory diseases such as chronic pain, rheumatoid arthritis, multiple sclerosis, systemic sclerosis, systemic lupus erythematosus, polymyositis/dermatomyosytis and pulmonary sarcoidosis, and is enhanced in tumor cells such as melanoma, renal, prostate, pancreas, colon, gastric and thyroid cancers. It is considered a marker of differentiation since it is predominantly expressed on stem cells and on cells of the granulocytic and monocytic lineages at distinct stages of differentiation. Thus, APN inhibition may lead to the development of anti-cancer and anti-inflammatory drugs. ERAP1, also known as endoplasmic reticulum aminopeptidase associated with antigen processing (ERAAP), adipocyte derived leucine aminopeptidase (A-LAP), or aminopeptidase regulating tumor necrosis factor receptor I (THFRI) shedding (ARTS-1), associates with the closely related ER aminopeptidase ERAP2, for the final trimming of peptides within the ER for presentation by MHC class I molecules. ERAP1 is associated with ankylosing spondylitis (AS), an inflammatory arthritis that predominantly affects the spine. ERAP1 also aids in the shedding of membrane-bound cytokine receptors. The tricorn interacting factor F3, together with factors F1 and F2, degrades the tricorn protease products, producing free amino acids, thus completing the proteasomal degradation pathway. F3 is homologous to F2, but not F1, and shows a strong preference for glutamate in the P1' position. APQ, also known as laeverin, is specifically expressed in human embryo-derived extravillous trophoblasts (EVTs) that invade the uterus during early placentation. It cleaves the N-terminal amino acid of various peptides such as angiotensin III, endokinin C, and kisspeptin-10, all expressed in the placenta in large quantities. APN is a receptor for coronaviruses, although the virus receptor interaction site seems to be distinct from the enzymatic site and aminopeptidase activity is not necessary for viral infection. APNs are also putative Cry toxin receptors. Cry1 proteins are pore-forming toxins that bind to the midgut epithelial cell membrane of susceptible insect larvae, causing extensive damage. Several different toxins, including Cry1Aa, Cry1Ab, Cry1Ac, Cry1Ba, Cry1Ca and Cry1Fa, have been shown to bind to APNs; however, a direct role of APN in cytotoxicity has been yet to be firmly established.	0
NZ_CP022163.1\|WP_170115494.1\|3092712_3093624_+\|DNA/RNA-non-specific-endonuclease	gnl\|CDD\|224777	COG1864, NUC1, DNA/RNA endonuclease G, NUC1 [Nucleotide transport and metabolism].	2.50059e-68
NZ_CP022163.1\|WP_095977727.1\|3107128_3108172_+\|MBL-fold-metallo-hydrolase	gnl\|CDD\|293841	cd16283, RomA-like_MBL-fold, Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain. Derepression of the romA-ramA locus results in a multidrug-resistance phenotype. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.	5.49222e-80
NZ_CP022163.1\|WP_095977725.1\|3104916_3105984_-\|DUF2804-domain-containing-protein	gnl\|CDD\|378522	pfam10974, DUF2804, Protein of unknown function (DUF2804). This is a family of proteins with unknown function.	5.55875e-83
NZ_CP022163.1\|WP_157774917.1\|3092133_3092544_-\|nuclease-A-inhibitor-family-protein	gnl\|CDD\|369598	pfam07924, NuiA, Nuclease A inhibitor-like protein. This family consists of protein sequences that are similar to the nuclease A inhibitor expressed by bacteria of the genus Anabaena ((NuiA). This sequence is organized to form an alpha-beta-alpha sandwich fold, which is similar to the PR-1-like fold. NuiA interacts with nuclease A by means of residues located at one end of the molecule, including residues making up the loop between helices III and IV and the loop between strands C and D. The mechanism of inhibition of nuclease A by NuiA is as yet incompletely understood.	5.43781e-44
NZ_CP022163.1\|WP_095977726.1\|3106276_3107116_+\|SDR-family-oxidoreductase	gnl\|CDD\|187632	cd05374, 17beta-HSD-like_SDR_c, 17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs. 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.	6.34232e-83
NZ_CP022163.1\|WP_157774915.1\|3090092_3090524_-\|nuclear-transport-factor-2-family-protein	gnl\|CDD\|378915	pfam12680, SnoaL_2, SnoaL-like domain. This family contains a large number of proteins that share the SnoaL fold.	1.70116e-09
NZ_CP022163.1\|WP_095977709.1\|3085582_3087064_+\|FAD-dependent-monooxygenase	gnl\|CDD\|236199	PRK08244, PRK08244, monooxygenase.	0
NZ_CP022163.1\|WP_157774919.1\|3098194_3099466_-\|AHH-domain-containing-protein	gnl\|CDD\|379603	pfam14412, AHH, A nuclease family of the HNH/ENDO VII superfamily with conserved AHH. AHH is a predicted nuclease of the HNH/ENDO VII superfamily of the treble clef fold. The name is derived from the conserved motif, AHH. It is found in bacterial polymorphic toxin systems and functions as a toxin module. Like WHH and LHH, the AHH nuclease contains 4 conserved histidines of which, the first one is predicted to bind a metal-ion and the other three ones are involved in activation of a water molecule for hydrolysis.	2.88223e-26
NZ_CP022163.1\|WP_095977718.1\|3096189_3097623_+\|serine/threonine-protein-kinase	gnl\|CDD\|270916	cd14014, STKc_PknB_like, Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.	9.90926e-55

>NZ_CP022163.1|WP_095982745.1|3094898_3095120_+|hypothetical-protein
MTRVDAIHGFVLEPGSWRGEDIFRPRGLVGDLVVSERFKDFAGRHGLTNMVLTPTEQYMWDPSHLGPAPLSKT
>NZ_CP022163.1|WP_095977716.1|3093889_3094444_+|Wall-associated-protein-precursor
MLSSLMLVVLTQVACTPGETSLVCSCKQGMVSACMTLAGDDARKAAQVLDEVQGLLEQATWKAGEEQEKQRLQAAAESLSQTLESSEPPHCKGQNHHLISRPIARGLEEHPRLRGLYKPRDPRFVSRAKDEQAHCGYQEWHREIDDEVVRWLKRTPGATPKEFMDKLREIYGRPEMIARFPHGF
>NZ_CP022163.1|WP_170115494.1|3092712_3093624_+|DNA/RNA-non-specific-endonuclease
MFLKRFVRGAAVASLSVLFACGPQEGDEALDSLSPGIENTSVPPEDIGSYSSAAGASISVHLKLGMPDSSTTSTSNPNRYLSVKSQYVISYNGSRKTPNWTAWQLNKSWMGSTSRQDTFRPDNTLPSSIPQASLADYSGSGYDRGHMCPSADRTLNTTDNSNTFYLTNMLPQAPNNNQGPWEQLESYSRTLVSSGKELFIMSGPIYSGTISTIGSGKVAVPTSTWKVITVMNATGQGPTNVTTSTRVIAVVMPNSDSKISKSADWHNYRVTARSIEQQTGLNFMADVAQSVQDVIETRVDTAQ
>NZ_CP022163.1|WP_157774917.1|3092133_3092544_-|nuclease-A-inhibitor-family-protein
MNTQRAAVLKSLLLSAHGLLFISETDAPFTPVDAPGSPFASLDDAAVRRLAGHPDADPVETRGVDEFFRNAVQEQPWHTPEETATVRRYRALVALLHASLPDARVYRVGAVSIDVLILGTGPGGGALGLATKVVET
>NZ_CP022163.1|WP_157774916.1|3090802_3092077_+|hypothetical-protein
MNARRSRTSRGVLLLMALSAAGCGTPVEPDASGEARALTIDEEFTRLSRRVPGFGGYYYDSAGALNVVLTQPTHQLAAVRELLSARGVRGSDTLLARQGRYDFEDLNRWRGRLEAEPLAGLVFTDVDEVNNRITLGMTHPDPEQVAAAMARLLIPADAVHLEQAAPNEQHQTAFTYVHQQNRPLAAGQQIKRFSNGYIYFCTLGFNVRRNGSLGFFTNTHCTNEGTVHYQGSPRIGVTTEDPLFWSNASVVYDGVTYTCSGTNVCRFSDAAYVEYDAGVQSSVKHGYIYRTEVENAYTGGAPTGIAPLKIDEAQPFFRIVGKAYHVAVGEKIHKVGQRTGWTSGLVTHSCVNTLNGSTRLFCQMKGDGAGYDGDSGSPVFRRVADSEQDVELVGIYWGSAMSPIGSIEQDFGPLDVAADSASTP
>NZ_CP022163.1|WP_157774915.1|3090092_3090524_-|nuclear-transport-factor-2-family-protein
MSASFKTTLLAALAALTLGASAQASPPGTQEVWRHHINAWNDKDVAAITSDYTDSSILILNNQVFHGKAAIAHVFSQLFQIFSTGENKVDPPTIHGRTLYITWHYAPKNEKTFFGSDSFIVENGKIQVQTIASELYISHPVTH
>NZ_CP022163.1|WP_157774914.1|3088615_3089674_-|hypothetical-protein
MATPLEGEPSLPPRACIPWISTVPPLEATACGVTSVFAHGTSQRARYDADNRLLELRTYDAVGALASVETHTWWEDLELRGRVDYADGRFEQTEWTYDAWRRLLSRVTTGSSRSSAKSLEFTYDAQGRVDEVFGAYNTFELWSQYAYDAQGRLVSINTEGVMCGGGETRCATLSYWPDGQLKRHAWIEGRYNSYVDEYSALGQLIHSTWEFTDSRGESTRAYDAAGRQIRLREDLFAPVSQRAFHSLTTRVHDPGGWRERFARDALCYEPVEGSGCDPDVDETHQRLTRRTTLICGTQLVALDEWDSNEDGVVDAHRTHERDSTGRLVREVYSGTAGLDAGPVRRDFQYDCP
>NZ_CP022163.1|WP_095977710.1|3087503_3088436_+|hypothetical-protein
MGWPLRMFQEEGYYFVTSRCFQGRLLLHPSPEVNEVVGGVLARAVEQSNGSVRLHAFTFLSNHFHLLVWAKGAALAGFMQYLRANLSRKVGRLVDWSGGFWERRYSAEPVLDDTALVGRLRYVLAHGVKEGLVERSIEWPGLTCLPQLLGPARRLFRWFNWTKRWSKRGHADGGDARGRFAEDWAEPVALELAPLPCWEGFEEEQRQREVKALLREVEAEACTRGRSVMGVMAVQAQHPHTRPEHLKRSPRPLGHASTRQALKELREQYRAFVTAFREAAAQWRRGNYSARFPLFSFPPRVLPGRTAQIL
>NZ_CP022163.1|WP_095977709.1|3085582_3087064_+|FAD-dependent-monooxygenase
MRNTVDVAVVGGGPVGWMVACELALAGVSVSVHERRTERVKQSRAMTLHPRSLEILALRGLADRFLARGLPLPTAHYGVLDTRLDFSALDTAFPFTLFIPQAVTEALLEERARELGVDIHRGHQVTGLRQDPEGVDVEGTREGGTFRVRARYVVGADGARSIARTLAGIPFQGTETTMSLMLGDVVFGTLPDQPAWTTVNEHGTLMVAPLGDGRHHRVVMNDPLRSGVPVSEPVTLEELARSLRSIEGSDFGMHSPLWLSRFGNETKLAATYRSGRVFLAGDAAHIHLPAGGQGLNVGLQDAMNLGWKLAGVLRGLAPEALLDSYHRERHPVGASLLRNTLSQTALISTFNPAGLALRETVSALLTLPDANRKLAEQIAALDVAYAEPPLPAPPGLDTVSGLPGGRLPDLILRGTEGASHSLYSLYSLMHEGRWLLLRREDSAPRPALTAAWAEWTNVVTADIPAREKDWGAWTSLWVRPDGHLGYVAHGGTP
>NZ_CP022163.1|WP_095977708.1|3084848_3085505_-|TetR/AcrR-family-transcriptional-regulator-C-terminal-domain-containing-protein
MRIQREKVVRAALALLDEEGIEGVTMRKLAQRLKVQAPSFYWHFANKQALLDGMADALVESVARSVDPEAPWDEVLRGVAAELRQALRSRRDGARVFAGTYVVTENVLRVSEAMIGALRRAGASSRVAAWGCFSLVNYVLGFTMEEQGLEPRSGIDAAEFALRRERFTTLAPTRFPHVFEALADIFDEDLDARFVFGLERLITGLRADLDGSERLPGP
>NZ_CP022163.1|WP_095977718.1|3096189_3097623_+|serine/threonine-protein-kinase
MSTNPGEATLYSEALAPGTQVGRWRVVEPLGMGGQGAVYRVEDTEHPGDFYALKLALHARDERAEREVALMMTRAAHPHVVGFHGCARWPHPREGCLGFVMDWVPGQALDVWAETEGTTFRQLAGAGATVARTLGELHARGVLHRDLKPEHILLRASDGQPVLLDFGVGWYEGAAPLTTGPLPPATLYLLSPEAVRFLWRSSESPGTHYTFQPTDDLYALGVSLYRATTGHYPFSEWLPSELLQFAIVHVQPLAPVLVNPRVPRALSDVIVRLLAKDPQERYPSGAALHAALVAATHGEQAAWDSSIFEWEERPPEKEGALPERHLVRPPRPKPSWTSPPPDPVHVARRGRWTRRLVCAAAVLLMLVPLNRLALVTPSVRVPDEEWATDVRVDPASVQSEQAPLPARNQKLAPCTEGLEVELSGACWHSLRQRPPNCPRQTVAFKGQCLWPVPKSRPIPTSVDGGTPDAQEDSTTPP
>NZ_CP022163.1|WP_095977719.1|3097609_3098179_-|hypothetical-protein
MPKKYFKLTQEVDGSGGWDLGNPTNPQGLEVDNPWMYREGMPVSESGRLKIPIGRPGRVLDFTLAGFSIPVVHVRVASLFMELAPRDTQLLSVDIQGQPDSFRILVATRLIRCIDDEASAEVEYWTPEDGRPEKEGQYRDVYGMRIDTAKVGDAKVFRTWGWTIALIVSEEIKEALEHIGATGVKFTEV
>NZ_CP022163.1|WP_157774919.1|3098194_3099466_-|AHH-domain-containing-protein
MSQDGLLIHLPRTGEAGPVELDEDVFSRAIANEVQRTRPPANPEMAARELFEVPPHSGWYGYTQRHGVVPLNGQSRALLGADADVRVTQEYLRFCAAIGMPGDCRKVLMNSPVLVGDGRYALAMSFALEAVIPEMMEAFKGMADPEAIKASILWTMTIYAAMWLAPEPVFSKGLATAVTASFICYVGVDTFWTLIQGWRRMVEVAELAHSFSEIREAGGKYGRVMGKNAARAFALLLTAAIGQTASSFSSKVTTLPGAAQSSAVGAARGGVRLAEVAQVEAVVVTADAVTIALAPNVVAATAQGMRGTASSPVDAEGPEHHIATDKWTDATHSGGPWTPKFQRIFDRAGMSLNDPANKVHVKGHQGPHPQTYHERVYERLDEATKGCGSIQQCQKVLTAELHRLAKQISTKGTLLNKLVTRSQ
>NZ_CP022163.1|WP_095977721.1|3099748_3100315_-|hypothetical-protein
MPKRYFDLSDDVCVSGRWHIRPPMAEDGQAVDPWMFTEGQPLQLTTKLRMALRVKGRPLDFTLAGLDVPVVHAKVATLFAELAPQDIQLFPVDIEGQPEQFSILVATKLIQCIDESASDEVRRWRAEDGCPEKTGNYRVVSGMRIDTSKVGDAKVFRTWGWSVALIVSEEIKEALEHIGATGVKFTGV
>NZ_CP022163.1|WP_095977722.1|3100437_3101019_-|HutD-family-protein
MRRWGPADYRDMPWKNGGGVTRELLRRPHPTRPEGFGVRLSIATVAAAGPFSLFPGVDRHLLLLEGQGMALTRAGASEEVVVAPGQPLFSFPGEDAWDCRLLGGPVRDFNVMVDRALAEASLERVHLEAGARHRLAASPGTQWLYGVSGRVQVAGEVLAEEDILEWDAPGALELVGESEATVLIIRLMPRAGR
>NZ_CP022163.1|WP_095977723.1|3101180_3103736_+|M1-family-metallopeptidase
MAHATEDKNFRLPLSVRPRRYAATLTLDMEARAFTGLQTIELELDTPTDEIVLHAIALKLGEVVFRAADGRIIMPAETHEAPLSETVVVRFGEKLPQGQGALDVTWTGRFTEGLRGLYMAGKVAATQFEAADARRLFPCFDEPSFKARWALTVQVPTGLTALSNGALEREESDGNMRRLTFKETEVLSSYLIALVVGPLVGTPEERVEGIPVRTWALPEKAHLTRFGQDAALAALPRLQAYFDLPYAFGKVDQVGIPDFEAGAMENAGLITYREIALLLDPATAPLSVQKRVAEVVTHELAHQWFGNWVTMVWWDDLWLNEAFATWMAYKIVDDWKPDWRVWLDFDSGKAAALHLDALRSTHPIRGEVRNAHEAGESFDLITYEKGGAVLRMIEGFLGQDAFREGMRQYMRKHARANAVADDLWRALAQASSQPVLELANAWIGQSGYPQVGVTVNGRKVKLTQRRFYSEPGVKSDERWPVPMVLKYADAGGVREQRVLLRESEAEVTLEGSGEVKWLVANAGSTGFYRVQYDATGLERLSANVDALEPSERISLLADQWALARSGQATLTAFLDLAGRYGQEEDDAVLDELVGGLAYVEGRLVEGEDQERFRRWVEKLLGAGFKKVGWDAAPGETDRVKLRRAALVRALGGVARSPEIIAEARPRVARALDGDTTALEPNLLDAAVGMVARQGDRALYEKILEKMPVEPDPATQRRYLMALTAFEDPQLADAAQKLFFTEKVKMQDVASFLTGLINNRTGRNMWWAEKQKRWKDVLARTGAAPMLLRRVVESLGALRERKQLDEVRKLLTAHPVEEAKQAMGQTLEKLEQDVVLRERALPEVRAWLQRQK
>NZ_CP022163.1|WP_095977724.1|3103755_3104841_-|hypothetical-protein
MNCSNCGQVVADESLGFCMECGEAFGASAGQGSDEDNPDAHAEGYSDSEWREPRPSVWDTLSRVLAPVRTVAGQLGDVFANILESPSVYGQMPGGSLTFLGLGFVGLALLVSVVPFIEGIGGLGSGVMFGWGVLVLLSEWREVSEAPPREGRFVDAYPAVIDKLPREVWHPGVIQAYALVTCAYALKMVGYGPIALLWLLAAGVLGYEQGRRFFYLLPQDEAALAASAEHPGLHRWVVPGVAVGVLSLLLPWGRMSGLALSIYGVDLPLSVLTLSCLLLLGCYAVKHQGLGGLHPMVLILVAVWLALWLLLMNNIYSPGSWVYLVGVLLIYTAIVRHLIPARPRAEEAPQEEPPPDLDYQG
>NZ_CP022163.1|WP_095977725.1|3104916_3105984_-|DUF2804-domain-containing-protein
MTPERELTLLPAPASVATASGEPRFGTYQGELPEVDLQKLSGPWAPAAARARLLKRKRWHYTLATTREVVALFAVVDVGYSANAFAVAVDLKERKALCDVSFLGAPGPLAEVGNKPGAGLAASFRTLGGRMSATRGPEDERYRLQVDVSRLRTGSLQSFLWNGELMVAGGAPALTVIAPVGGDGFVNVTQKRAGMLASGTLEAGGKRFQLDGGVGGTDYTQGYLARHTAWRWAFLAGRLADGTPVGLNLVEGFNESARVNENALWLGERILPLGRATFEYDRENLMRPWRVRTDDRVVDLSFQPLHVHREDHDFKLVVSHFAQPVGLFEGTLRVDGRTYTLSDMPGVTEDQDMLW
>NZ_CP022163.1|WP_095977726.1|3106276_3107116_+|SDR-family-oxidoreductase
MARVALITGTSSGIGLDTAIHLAQAGFQTVATLRDTTRAGALQERARAAGVSLDIRALDVQSDDSVSTCVREVRERYGRIDVLVNNAGSGFLGTMEQTPMDALRTVMEVNFFGVWRVTQAVFPLMREARSGRIITVTSVGGLLGQPFNDAYCAAKFACEGFLESLAPVATRLGIHLSNIEPGAVHTEFVTNVKAKLSGKPSPGDDLYQPMLDSYMAGAMDAYKAAQSGEDIAKVIVEAATAATPHFRYVTSEWVRGVASRKYTDPTGDSIVTLMGSRLK
>NZ_CP022163.1|WP_095977727.1|3107128_3108172_+|MBL-fold-metallo-hydrolase
MNTPRHLVGLLALALGTSGCFSAPTWKGTPSDHFNGERFVNREPRPRTMSFLDWMAHRKPGAWKGRPDAPFGPRPPERVGPGDLRVTFINHATVLLQLDGLNILTDPIYSERCSPVSFAGPRRMRPPGIRFEDLPPIDVVVISHNHYDHMDVATLLRLQERFPQVRVFAGLGNREFLEGEGLRHVTEVDWWQEFPLSAEVTLVSARTQHFSNRGLGDADGTLWTGYVFRGPHGRTYFAGDTASGSQFTEARERLGPMRLAVLPIGAYKPEAIMSPVHVSPREAVQASVDLGARYSVPMHYGTFRLADDGETDPLWDLAGALVERGDQAPEWWVLAFGEGRDVPPMTP

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Crispr_ID: NZ_CP022163_8

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP022163_8

3981668-3981916

Orphan

Consensus_repeat	Method
GGAGATGGTGTCAAAGGATTCGAAACC	CRT

3 spacers

The CRISPR arrays of NZ_CP022163_8

>merge|NZ_CP022163|8|3981668-3981916|CRT
GAACGGTTACTCAAAGGATTCGAAACCTGGAGAGCGGAGATGGTGTCAAAGGATTCGAAACCCGGAGATGGTGTTGGAGATGGTGTCAAAGGATTCGAAACAAGGGGCCTGAGCGAGAACGAGGCTCGGGCGTGGACGGGTAACCGGAGATGGTGTCAAAGGATTCGAAACCCCGGAGATGGTGTCCGGAGATGGTGTCAAAGGATTCGAAACCCGGAGAGCGGAGATGGTGTCAAAGGATTCGAAACC

>NZ_CP022163|8|1|3981668-3981916|CRT
GAACGGTTACTCAAAGGATTCGAAACC	TGGAGAGCGGAGATGGTGTCAAAGGATTCGAAACCCGGAGATGGTGTT
GGAGATGGTGTCAAAGGATTCGAAACA	AGGGGCCTGAGCGAGAACGAGGCTCGGGCGTGGACGGGTAACC
GGAGATGGTGTCAAAGGATTCGAAACC	CCGGAGATGGTGTCCGGAGATGGTGTCAAAGGATTCGAAACCCGGAGAGC
GGAGATGGTGTCAAAGGATTCGAAACC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP022163.1\|WP_095982807.1\|3983125_3984439_-\|IS4-family-transposase	unknown	unknown	gnl\|CDD\|376573
NZ_CP022163.1\|WP_095978402.1\|3985735_3986701_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|223880
NZ_CP022163.1\|WP_095977357.1\|3980200_3981661_+\|IS66-family-transposase	unknown	unknown	gnl\|CDD\|376980
NZ_CP022163.1\|WP_095978394.1\|3973374_3974709_+\|two-component-sensor-histidine-kinase	unknown	unknown	gnl\|CDD\|226654
NZ_CP022163.1\|WP_095978403.1\|3987111_3988044_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095978397.1\|3977693_3977981_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095978406.1\|3989697_3989973_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095978404.1\|3988237_3988810_-\|dihydrofolate-reductase-family-protein	unknown	unknown	gnl\|CDD\|223340
NZ_CP022163.1\|WP_095978400.1\|3982085_3983015_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|376824
NZ_CP022163.1\|WP_157775064.1\|3979875_3980013_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095978399.1\|3978687_3979758_-\|glycoside-hydrolase-family-5-protein	unknown	unknown	gnl\|CDD\|365907
NZ_CP022163.1\|WP_095978405.1\|3989364_3989649_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095978408.1\|3990888_3992169_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095978392.1\|3971878_3972505_+\|SDR-family-oxidoreductase	unknown	unknown	gnl\|CDD\|187555
NZ_CP022163.1\|WP_095978407.1\|3990200_3990779_-\|non-canonical-purine-NTP-pyrophosphatase	unknown	unknown	gnl\|CDD\|238285
NZ_CP022163.1\|WP_095978395.1\|3974800_3976186_+\|insulinase-family-protein	unknown	unknown	gnl\|CDD\|223685
NZ_CP022163.1\|WP_095978396.1\|3976185_3977697_+\|insulinase-family-protein	unknown	unknown	gnl\|CDD\|223685
NZ_CP022163.1\|WP_095978401.1\|3984969_3985734_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|374368
NZ_CP022163.1\|WP_095978398.1\|3978092_3978635_-\|VOC-family-protein	unknown	unknown	gnl\|CDD\|319898
NZ_CP022163.1\|WP_095978393.1\|3972565_3973288_+\|class-I-SAM-dependent-methyltransferase	unknown	unknown	gnl\|CDD\|379312

Protein	Function_ID	Function_description	E-value
NZ_CP022163.1\|WP_095982807.1\|3983125_3984439_-\|IS4-family-transposase	gnl\|CDD\|376573	pfam01609, DDE_Tnp_1, Transposase DDE domain. Transposase proteins are necessary for efficient DNA transposition. This domain is a member of the DDE superfamily, which contain three carboxylate residues that are believed to be responsible for coordinating metal ions needed for catalysis. The catalytic activity of this enzyme involves DNA cleavage at a specific site followed by a strand transfer reaction. This family contains transposases for IS4, IS421, IS5377, IS427, IS402, IS1355, IS5, which was original isolated in bacteriophage lambda.	9.35647e-08
NZ_CP022163.1\|WP_095978402.1\|3985735_3986701_-\|hypothetical-protein	gnl\|CDD\|223880	COG0810, TonB, Periplasmic protein TonB, links inner and outer membranes [Cell envelope biogenesis, outer membrane].	0.000313
NZ_CP022163.1\|WP_095977357.1\|3980200_3981661_+\|IS66-family-transposase	gnl\|CDD\|376980	pfam03050, DDE_Tnp_IS66, Transposase IS66 family. Transposase proteins are necessary for efficient DNA transposition. This family includes IS66 from Agrobacterium tumefaciens.	7.25924e-59
NZ_CP022163.1\|WP_095978394.1\|3973374_3974709_+\|two-component-sensor-histidine-kinase	gnl\|CDD\|226654	COG4191, COG4191, Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal transduction mechanisms].	3.23125e-47
NZ_CP022163.1\|WP_095978404.1\|3988237_3988810_-\|dihydrofolate-reductase-family-protein	gnl\|CDD\|223340	COG0262, FolA, Dihydrofolate reductase [Coenzyme metabolism].	3.67182e-13
NZ_CP022163.1\|WP_095978400.1\|3982085_3983015_+\|hypothetical-protein	gnl\|CDD\|376824	pfam02569, Pantoate_ligase, Pantoate-beta-alanine ligase. Pantoate-beta-alanine ligase, also know as pantothenate synthase, (EC:6.3.2.1) catalyzes the formation of pantothenate from pantoate and alanine.	0.0090312
NZ_CP022163.1\|WP_095978399.1\|3978687_3979758_-\|glycoside-hydrolase-family-5-protein	gnl\|CDD\|365907	pfam00150, Cellulase, Cellulase (glycosyl hydrolase family 5).	2.27324e-59
NZ_CP022163.1\|WP_095978392.1\|3971878_3972505_+\|SDR-family-oxidoreductase	gnl\|CDD\|187555	cd05244, BVR-B_like_SDR_a, biliverdin IX beta reductase (BVR-B, aka flavin reductase)-like proteins; atypical (a) SDRs. Human BVR-B catalyzes pyridine nucleotide-dependent production of bilirubin-IX beta during fetal development; in the adult BVR-B has flavin and ferric reductase activities. Human BVR-B catalyzes the reduction of FMN, FAD, and riboflavin. Recognition of flavin occurs mostly by hydrophobic interactions, accounting for the broad substrate specificity. Atypical SDRs are distinct from classical SDRs. BVR-B does not share the key catalytic triad, or conserved tyrosine typical of SDRs. The glycine-rich NADP-binding motif of BVR-B is GXXGXXG, which is similar but not identical to the pattern seen in extended SDRs. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.	9.5073e-54
NZ_CP022163.1\|WP_095978407.1\|3990200_3990779_-\|non-canonical-purine-NTP-pyrophosphatase	gnl\|CDD\|238285	cd00515, HAM1, NTPase/HAM1. This family consists of the HAM1 protein and pyrophosphate-releasing xanthosine/ inosine triphosphatase. HAM1 protects the cell against mutagenesis by the base analog 6-N-hydroxylaminopurine (HAP) in E. Coli and S. cerevisiae. A Ham1-related protein from Methanococcus jannaschii is a novel NTPase that has been shown to hydrolyze nonstandard nucleotides such as XTP to XMP and ITP to IMP, but not the standard nucleotides, in the presence of Mg or Mn ions. The enzyme exists as a homodimer. The HAM1 protein may be acting as an NTPase by hydrolyzing the HAP triphosphate.	8.72545e-49
NZ_CP022163.1\|WP_095978395.1\|3974800_3976186_+\|insulinase-family-protein	gnl\|CDD\|223685	COG0612, PqqL, Predicted Zn-dependent peptidases [General function prediction only].	3.54261e-79
NZ_CP022163.1\|WP_095978396.1\|3976185_3977697_+\|insulinase-family-protein	gnl\|CDD\|223685	COG0612, PqqL, Predicted Zn-dependent peptidases [General function prediction only].	3.544e-85
NZ_CP022163.1\|WP_095978401.1\|3984969_3985734_-\|hypothetical-protein	gnl\|CDD\|374368	pfam16106, DUF4824, Domain of unknown function (DUF4824). This family consists of several hypothetical lipoproteins around 270 residues in length and is mainly found in Pseudomonas species. The function of this family is unknown.	0.00998598
NZ_CP022163.1\|WP_095978398.1\|3978092_3978635_-\|VOC-family-protein	gnl\|CDD\|319898	cd06587, VOC, 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 is found in a variety of structurally related metalloproteins, including the type I extradiol dioxygenases, glyoxalase I and a group of antibiotic resistance proteins. 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). Type I extradiol dioxygenases catalyze the incorporation of both atoms of molecular oxygen into aromatic substrates, which results in the cleavage of aromatic rings. They are key enzymes in the degradation of aromatic compounds. Type I extradiol dioxygenases include class I and class II enzymes. Class I and II enzymes show sequence similarity; the two-domain class II enzymes evolved from a class I enzyme through gene duplication. Glyoxylase I catalyzes the glutathione-dependent inactivation of toxic methylglyoxal, requiring zinc or nickel ions for activity. The antibiotic resistance proteins in this family use a variety of mechanisms to block the function of antibiotics. Bleomycin resistance protein (BLMA) sequesters bleomycin's activity by directly binding to it. Whereas, three types of fosfomycin resistance proteins employ different mechanisms to render fosfomycin inactive by modifying the fosfomycin molecule. Although the proteins in this superfamily are functionally distinct, their structures are similar. The difference among the three dimensional structures of the three types of proteins in this superfamily is interesting from an evolutionary perspective. Both glyoxalase I and BLMA show domain swapping between subunits. However, there is no domain swapping for type 1 extradiol dioxygenases.	1.89811e-16
NZ_CP022163.1\|WP_095978393.1\|3972565_3973288_+\|class-I-SAM-dependent-methyltransferase	gnl\|CDD\|379312	pfam13649, Methyltransf_25, Methyltransferase domain. This family appears to be a methyltransferase domain.	1.98041e-25

>NZ_CP022163.1|WP_095977357.1|3980200_3981661_+|IS66-family-transposase
MVEVDARDARIAQLEKRLEAALERIAQLEEENERLREENRWLKERLGLNSSNSSKPPSSDAPGTPRQSKRPTGRRPGGQPGHKKHERALLPPEDVQHVVELVPRECRGCKGRLNGQDTAPRRHQVVEVPPLSAIVTEYRCHALQCPGCGVVTRGEVPVHARSVFGDRLTALASLLVGKYRLSKRLVKDALSDMLGVELSVGSVSNLEGEMSEALAPPTAEALAYVQTSEAVNADETGFAQGREGGRAGRAWLWVVATALVVVFHIARSRGGKVARQLLGADFAGFLTTDRWSAYAWVDAGLRQLCWAHLTRDFQGFIDRGGRGGRIGRELMRERNRFFKWYHRVRDGTLSRERFEERMRGVERRVGQLLREAALRAEKKTAGMAREILQWEKCLWTFVDVPGLEPTNNFGERCIRHAVMYRKTSFGTQSEEGSRFVERIFTATTTLKLQGRDVLAFLTETLAAHRRGLRGPSLLPSAPEPQLALTA
>NZ_CP022163.1|WP_157775064.1|3979875_3980013_-|hypothetical-protein
MGAAMWTTGTWERVTSPNINTAYQIEPSFVPLSQAAVLERHLGKP
>NZ_CP022163.1|WP_095978399.1|3978687_3979758_-|glycoside-hydrolase-family-5-protein
MKNNRLMGWLTLGSILWGCGGPSEEPPMAPEPEARVSDAALAGPLPYRGINLAGAEFGSALPGTHGTTYVYPDPAYSNYTTADYYISKGMTTFRLPFKWERLQRTRKAAFDAAELTRLKTTVNRLLGKGAVVILDPHNYARYAGAVVGAGVPNADFADFWSRLANEFKSNPKVIFGLMNEPYSMPTEQWLGAANAAIQAIRNTGATNLILVPGNAWTGAHSWTGSWYGTSNATVMLQVKDPGNNYAFEVHQYLDSDSSGTQASCVSATIGAQRMQSFTNWLRANGKKGFLGEFAGGTDSVCLSAVDNILDHLEANSDVYLGWTYWAGGPWWGSYFFSLEPTSGVDKPQMGALSSHL
>NZ_CP022163.1|WP_095978398.1|3978092_3978635_-|VOC-family-protein
MSIHVKTPSRLHHTAYVTRDLEATRRFYEDVIGLPLVATWCESDELFGAVRTYCHVFFELGDGSALAFFQFEKPSDQELFGPRMPPSPFHHIALNVDREVQDGIERRLRAAGYSEPKMYVLEHGYCRSLYIEDPNGMIVEFTYDDPKAVTPEAARARRGEAHRELARWLAGDRASNNTFR
>NZ_CP022163.1|WP_095978397.1|3977693_3977981_-|hypothetical-protein
MARSDKPGKNARSGSTPSFNKDRVERGQEADDTRPLYAADAIHPTEEAKFSLDSDGPVGGPVADIRSPIDEADEFARQGRGRTESEEDEDVPERS
>NZ_CP022163.1|WP_095978396.1|3976185_3977697_+|insulinase-family-protein
MRRPLLALSTLAVLTASACRTAPAPVPEAPPSAPSAEAAPSPSDAEAFRARPPEPGESPALVLPRFERAQLDNGLTVLVSTRRELPLIYVGVSFAVGGAGDPQGKWGLADLTYKTMLEGAAGKDTLALDQAFQNLGVSPGVSVSSDGANLGVRVLSRNADEALALLTEVVRRPTFAAKDFERRKKLQLAELVRALGSPGFLAQQAYLRGVFGPSHPYGHPVSGLPATVEAVTARDVKAFYEAHVGPRTTALVMTGDITLEQAVALAKKSFGDWKGKAVLPPVPPAPPTPKRTQVVFVPKPGLDQTVVVLGRPGIAAGNPDEAALELATTVFGGFFGSRLNMNLREDKGYSYGANASSDPRLGVGPLTASSSVRADVTGAALTEFFNELKGLRERPISAKELESAREGLIRGFPGSFESVEGLGASASALFTLRRPLDEFERTVEGLRKATPAEVQRVAEAYLSPDTLQVVLVGDPEAVQKQVEGLGLGQWVTESPGKAPAASR
>NZ_CP022163.1|WP_095978395.1|3974800_3976186_+|insulinase-family-protein
MKAFIAAAALALGLPAFAQQQQEAKPLSPGREALAIPYEKYTLPNGLEVLLARDPKLPVVAVNIWYHVGSYDEQPGRTGFAHLFEHMMFQGSKHVPDDVHIALLEQLGATDLNGTTNFDRTNYFETVPSNQLATALWLESDRMGFLLDALDEKKLRTQQEVVKNERRQSVETRPYGLAQEKLWQALFPAPHPYFGKVIGSMADLDAATVDDVKAFFRTWYTPANATLAIVGDFDPQEARALVEKYFATLQGSPKPARPQVAPLVRAQEQVIRHDEKVGTLPLVVMSWLTPPYLSTGDAVADVLANVLGTGKSSRLYKHLVVDKGLAQSVSASQQSLGAQSVFSVEAVARPGVSSDALARELDAVLDTVRREGPSAAELDQARTRFETQMLAGLQSVGGFGGKADTLQTYNHYHGDPGFLMGDLERYDAVTPEAVRDFAREYLKPGARVVLHAVPAQPKEKP
>NZ_CP022163.1|WP_095978394.1|3973374_3974709_+|two-component-sensor-histidine-kinase
MSPPSPRPEEGPSPNQEPWPRRWRTFRVFAATLVLLYPMDWLVLGHWSLTTLGVRLVWASHVLLHGVLWRKLGSPWEKRLSSLNSVLTSLYFLTMVWFTGAGTSPYLNMALCLPLMMALVRPMDARPAILSGVTCALGVFALLWEEAQYLHAVNWASMVGTATFIGVYGSVHYRKAQEALHEASVERARREAMERLALAERHRAQTEKMATVGRLAASVMHEVNNPLAFVRSNLDFLRTEVMQQPLREESRAELAEVFEETRQGVERIRQIVSDLKGFSRMDMEEPCECALADVVTDAARLAAVRLKNVARLHVEIPPGLPEVFATRRRLAQAILNLLVNAGDALEDAQVRGGEVRVTGVAEPGRVALLVEDNGPGFAPEVLPHLFEAFFTTKGPEKGTGLGLSLSREMVERCGGTLRAENRAEGGARLRLELPVPARGPGAKA
>NZ_CP022163.1|WP_095978393.1|3972565_3973288_+|class-I-SAM-dependent-methyltransferase
MFHPKGPSLRELLYQGFQSVERGYDLLAPKFEYTPFRTPEAVVASSLLLAGADRSVDSALDICCGTGAGMRHLRPLCRERVVGLDVSQGMLDEARRQLADTPGEALLEFVRGDALAPPWREEFDLVTSFGAFGHIPEVDEPRFVEGIHQVLRPGGRFLFVTSDEPSRLRPGYWMARAFNAAMRVRNALWSPPFVMYYLTFLLPRARSLLEAQGFQVEVHRDVLPAPFDRYGLCVVIATRS
>NZ_CP022163.1|WP_095978392.1|3971878_3972505_+|SDR-family-oxidoreductase
MRLTVFGATGRVGHTLVHDALGQGHEVTAYVRDPKRLGIKHGRLVIKKGSLEDGTTVAEAIRGSEVVVSAIGARDATHAVTVVTEATRAIVTAMKAEGVQRLVTVGAAGLLPHAAGGLTGEHGLPPFLRHAFEDHRGAFLGLQDSGLDWVVVCPPVMPSGVKTGKYRTAVEALPTGGRQVYAEDVADFTLKVATGQEHHRVRVGIVGD
>NZ_CP022163.1|WP_095978400.1|3982085_3983015_+|hypothetical-protein
MGWPLRMFQEEGFYFVTSRCFQGRLLLRPSAEVNEVVGGVLARAVQQSAGNVRLHAFTFASNHFHLLVWARGAALAGFMQYLRANLSRKAGRLVDWSGGFWERRYSAEPVLDDEALVGRLRYVLAHGVKEGLVERSAEWPGLTCLPQLLGPARRVFQWFSWTKRWSKRGSEDLAAEEGRFAKEIAEPVELLVEPLPCWKRLGEEERQRAVRALVEAVESEARARDKPVLGARAVRAQHPHTRPEHLKHSPRPLGHASTRQALNELREQYRAFVAAFREAAARWMWGDFSAPPLSRSNSGSPPLWFRQGG
>NZ_CP022163.1|WP_095982807.1|3983125_3984439_-|IS4-family-transposase
MVRRTLEHALSSQWIDEVFEANREQQYTRELLFSSVVDLMGVVALGLRPSLHAAAQSDPDLTVSLAALYDKVNHTEPQVVRALVQGSAERLLPVVRPMKKQGPWAAGYQVRVLDGNHLPASEKRLKPLREFRGAALPGQSLVVYAPELSLVVDVLPAEDAHAQERALMGPVLERVREGELWLADRNFSTSRILRAVHEKRAAFIIREHGVSPNPTALGERREVGRGPAGRVYEQAVRVEGEEPLELRRIEVELEEPTEDGETAIRLLTNVPEEKLSAVEVAQLYRKRWTIEGMFGELEAVLESEVRSLGRPRAALLAFGVAVLAYNVLSVVKTAVEASHDLEAANMQVSTYYIAAEVKFAYGGMMMVVEPEDWSGQEVRSAEQLSELLLELAKKVKPSTLRKHPRAAKKKVKKGYVPGEVARKHVATARVLKGEKIS
>NZ_CP022163.1|WP_095978401.1|3984969_3985734_-|hypothetical-protein
MPATQENEIAITVHAPELVGNDGRPLAVVHGMERALPGLRLAWTISSEGKRIPVPQREAFLARGRPNGRGFPLLRNGDDDFRVTVTGLELPAGSSPGGQSQLDIHAVLPLAVDGIAAAAEVLEAIAEGARAFWGHATPFNAGVDIARQTKNWAANPQPPPRGLPALKLPWNIRSPEIPHRLGWLNYWSAAAARAIGFPDPARDVELLSRSRRTATGGWVVQLTDAPLDLDNPAHLDALKRAYERFPEIGGRATP
>NZ_CP022163.1|WP_095978402.1|3985735_3986701_-|hypothetical-protein
MRLRACIALLLFLSACTTTPPSPREPAARDPRLANLQRAATLPWTDGGRCAVREASEPWSELAERCFHALDHDRIEFHDTTGRCAVASAGAAVGVGLCVLAAPEIVVGTIIVAGVVVVGFAIKEALDVYELSWGDPEKVRPAPETRPAPETRPVPETRPVPETQIAPQKPSPKKRPKPEPKGPDFPPLEPPETSERDRPRCEPVPVPYHLGGNKLHNKCADRIPNNSFPGGDVFVNGKNFDALQLATRTLWEVKTDNFDTYPPDLREIVVESQVEKLRHERALALACGFDFRVGVRSPAHKAALERTAPELDGVIVVMEWC
>NZ_CP022163.1|WP_095978403.1|3987111_3988044_+|hypothetical-protein
MGWPLRMFQEEGFYFVTSRCFQGRLLLRPSAEVNEVVGGVLARAVQQSAGNVRLHAFTFASNHFHLLVWARGAALAGFMQYLRANLSRKAGRLVDWSGGFWERRYSAEPVLDDEALVGRLRYVLAHGVKEGLVERSAEWPGLTCLPQLLGPARRVFQWFSWTKRWSKRGSEDLAAEEGRFAKEIAEPVELLVEPLPCWKRLGEEERQRAVRALVEAVESEARARDKPVLGARAVRAQHPHTRPEHLKHSPRPLGHASTRQALNELREQYRAFVAAFREAAARWMWGDFSAPFPPFSFPPRVVPGRVARIL
>NZ_CP022163.1|WP_095978404.1|3988237_3988810_-|dihydrofolate-reductase-family-protein
MGLLTFSINVTLDGCVDHQEGIADDETHAFFTRLMDEGGAMLWGRVTYEMMESYWPAVARGDESAPPAMREWALKLEDKPKYVVSSTRKDFPWTNSHHIVGDLRTAVQKLKDATPSGVLLGSGKLATELDRLDLIDEYKFLVHPRIAGHGPTLYQSGLPSTRRLELVSAMPLRCGAVAMHYRRALTPAQA
>NZ_CP022163.1|WP_095978405.1|3989364_3989649_-|hypothetical-protein
MKMKTLLLGLVSGVLLAACGGPLPEEMDAQEQLGTTQGAVCEGWDSGARLCTWKCTSSAPQWSAVGAGVVAYGQCQSYANAQCGRTAYATCWSK
>NZ_CP022163.1|WP_095978406.1|3989697_3989973_-|hypothetical-protein
MKMLMLGLVSGLMITACGGPEPEDAQAPAEELGTTQGALCEGWDSGARKCSFQCYSYSTWWTTSATVSYGQCQEYANGQCGRTAYGACWSK
>NZ_CP022163.1|WP_095978407.1|3990200_3990779_-|non-canonical-purine-NTP-pyrophosphatase
MKNAKAAPQLLFLTGNAGKLREIQAALPEVRAWDVDLPEIQSVDPRRVIEAKLLEATRLLPGQRLMVEDTSLSLDALGGLPGPLIKWFIADGSLGLEGLADVAAARGNLQARATTWIGLLEPSATGLSLRFFEGTVRGRIVRPVGQSGFGWDPIFQPEGADKTFAQMTPEEKTRFSMRSLALDALRKAWEHG
>NZ_CP022163.1|WP_095978408.1|3990888_3992169_-|hypothetical-protein
MASITIINKTNVPINSTAVYAGVNSSWRNKINPTEFFVHSASPAVQYTLKVNYCLKRDDLYHSNWSRVAELIGLASLDLIAIGLSVVGLGMAVGAVTGASTALGFVAGTVEAGVGASAFAVDIVALGINVRDFVVDRGSADTEWTDIWGHHDVVFVAEGGMDINENNGRENPAKLKPLTLRKISQDEFERMKRTNQIYERSKLCHAIRFDEKGDRYYITPDGKHIYNPDGDEYYKAAGGTHVKYEESPPSNPARANVEWTKGITGNDRGEWQTEVHVDPRRFANGIEVREQDKYGVINARLLDGDKAHEKETFWTSKNMGDDSPTNYRQQFFDPECRIFKVEVREEEGYGITDIRFHVLCQEGMAGCVTDWLTENNEGESSKIHIRECEVPKDHAIVGLQGKEQGGFGLVDIKFAYSPFTKSQAAS

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Crispr_ID: NZ_CP022163_9

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP022163_9

4632090-4632178

Orphan

Consensus_repeat	Method
CCCGACATCAACGGCAACAAGCCGGG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP022163_9

>merge|NZ_CP022163|9|4632090-4632178|CRISPRCasFinder
CCCGACATCAACGGCAACAAGCCGGGTGCCAAGCCGGACGCGAAGCCCCAGTTCTCGCCGCGCCCCGACATCAACGGCAACAAGCCGGG

>NZ_CP022163|9|7|4632090-4632178|CRISPRCasFinder
CCCGACATCAACGGCAACAAGCCGGG	TGCCAAGCCGGACGCGAAGCCCCAGTTCTCGCCGCGC
CCCGACATCAACGGCAACAAGCCGGG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP022163.1\|WP_095978875.1\|4638903_4639257_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095978863.1\|4623188_4624280_-\|NAD(P)H-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|100006
NZ_CP022163.1\|WP_157775266.1\|4624707_4625262_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|340967
NZ_CP022163.1\|WP_095978868.1\|4628137_4628680_-\|EF-hand-domain-containing-protein	unknown	unknown	gnl\|CDD\|238008
NZ_CP022163.1\|WP_157775271.1\|4628954_4629599_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_063725069.1\|4636669_4637338_+\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|379228
NZ_CP022163.1\|WP_095978874.1\|4637421_4638054_+\|glycosyltransferase	unknown	unknown	gnl\|CDD\|213815
NZ_CP022163.1\|WP_170115548.1\|4626051_4627719_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|238046
NZ_CP022163.1\|WP_095978876.1\|4640552_4641314_+\|PIG-L-family-deacetylase	unknown	unknown	gnl\|CDD\|376836
NZ_CP022163.1\|WP_157775268.1\|4625558_4626032_-\|DUF697-domain-containing-protein	unknown	unknown	gnl\|CDD\|226125
NZ_CP022163.1\|WP_095978862.1\|4622314_4623175_+\|helix-turn-helix-transcriptional-regulator	unknown	unknown	gnl\|CDD\|225117
NZ_CP022163.1\|WP_157775274.1\|4642236_4643361_-\|site-specific-integrase	unknown	unknown	gnl\|CDD\|271189
NZ_CP022163.1\|WP_095982875.1\|4632641_4633487_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095978861.1\|4620944_4622144_+\|FAD-dependent-monooxygenase	unknown	unknown	gnl\|CDD\|180297
NZ_CP022163.1\|WP_157775263.1\|4624390_4624702_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|340967
NZ_CP022163.1\|WP_095978871.1\|4633899_4634949_+\|PspC-family-transcriptional-regulator	unknown	unknown	unknown
NZ_CP022163.1\|WP_095978872.1\|4635235_4635781_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095978870.1\|4629885_4631046_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|223065
NZ_CP022163.1\|WP_170115549.1\|4638563_4638719_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_071905527.1\|4639497_4640565_+\|acyl-CoA/acyl-ACP-dehydrogenase	unknown	unknown	gnl\|CDD\|224871

Protein	Function_ID	Function_description	E-value
NZ_CP022163.1\|WP_157775274.1\|4642236_4643361_-\|site-specific-integrase	gnl\|CDD\|271189	cd01189, INT_ICEBs1_C_like, C-terminal catalytic domain of integrases from bacterial phages and conjugate transposons. This family of tyrosine based site-specific integrases is has origins in bacterial phages and conjugate transposons. One member is the integrase from Bacillus subtilis conjugative transposon ICEBs1. ICEBs1 can be excised and transfered to various recipients in response to DNA damage or high concentrations of potential mating partners. The family belongs to the superfamily of DNA breaking-rejoining enzymes, which share the same fold in their catalytic domain and the overall reaction mechanism. The catalytic domain contains six conserved active site residues. Their overall reaction mechanism involves cleavage of a single strand of a DNA duplex by nucleophilic attack of a conserved tyrosine to give a 3' phosphotyrosyl protein-DNA adduct. In the second rejoining step, a terminal 5' hydroxyl attacks the covalent adduct to release the enzyme and generate duplex DNA.	5.86063e-06
NZ_CP022163.1\|WP_095978863.1\|4623188_4624280_-\|NAD(P)H-dependent-oxidoreductase	gnl\|CDD\|100006	cd02199, YjgF_YER057c_UK114_like_1, This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site.	2.71605e-53
NZ_CP022163.1\|WP_157775266.1\|4624707_4625262_-\|hypothetical-protein	gnl\|CDD\|340967	cd17409, MFS_NIMT_like, 2-nitroimidazole transporter and similar proteins of the Major Facilitator Superfamily of transporters. This subfamily is composed of Escherichia coli 2-nitroimidazole transporter (NIMT), also called YeaN, and similar proteins. NIMT confers resistance to 2-nitroimidazole, the antibacterial and antifungal antibiotic, by mediating the active efflux of this compound. The NIMT-like subfamily belongs to the 2-nitroimidazole and cyanate transporters like (NIMT/CynX-like) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	6.26421e-38
NZ_CP022163.1\|WP_095978868.1\|4628137_4628680_-\|EF-hand-domain-containing-protein	gnl\|CDD\|238008	cd00051, EFh, EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.	2.61566e-07
NZ_CP022163.1\|WP_170115548.1\|4626051_4627719_-\|hypothetical-protein	gnl\|CDD\|238046	cd00094, HX, Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs). This CD contains 4 instances of the repeat.	5.03099e-33
NZ_CP022163.1\|WP_095978876.1\|4640552_4641314_+\|PIG-L-family-deacetylase	gnl\|CDD\|376836	pfam02585, PIG-L, GlcNAc-PI de-N-acetylase. Members of this family are related to PIG-L an N-acetylglucosaminylphosphatidylinositol de-N-acetylase (EC:3.5.1.89) that catalyzes the second step in GPI biosynthesis.	8.17006e-26
NZ_CP022163.1\|WP_157775268.1\|4625558_4626032_-\|DUF697-domain-containing-protein	gnl\|CDD\|226125	COG3597, COG3597, Uncharacterized protein/domain associated with GTPases [Function unknown].	0.000122355
NZ_CP022163.1\|WP_095978874.1\|4637421_4638054_+\|glycosyltransferase	gnl\|CDD\|213815	TIGR03469, HpnB, hopene-associated glycosyltransferase HpnB. This family of genes include a glycosyl transferase, group 2 domain (pfam00535) which are responsible, generally for the transfer of nucleotide-diphosphate sugars to substrates such as polysaccharides and lipids. The genes of this family are often found in the same genetic locus with squalene-hopene cyclase genes, and are never associated with genes for the metabolism of phytoene. Indeed, the members of this family appear to never be found in a genome lacking squalene-hopene cyclase (SHC), although not all genomes encoding SHC have this glycosyl transferase. In the organism Zymomonas mobilis the linkage of this gene to hopanoid biosynthesis has been noted and the gene named HpnB. Hopanoids are known to feature polar glycosyl head groups in many organisms.	3.19185e-25
NZ_CP022163.1\|WP_063725069.1\|4636669_4637338_+\|GNAT-family-N-acetyltransferase	gnl\|CDD\|379228	pfam13508, Acetyltransf_7, Acetyltransferase (GNAT) domain. This domain catalyzes N-acetyltransferase reactions.	4.54647e-06
NZ_CP022163.1\|WP_157775263.1\|4624390_4624702_-\|hypothetical-protein	gnl\|CDD\|340967	cd17409, MFS_NIMT_like, 2-nitroimidazole transporter and similar proteins of the Major Facilitator Superfamily of transporters. This subfamily is composed of Escherichia coli 2-nitroimidazole transporter (NIMT), also called YeaN, and similar proteins. NIMT confers resistance to 2-nitroimidazole, the antibacterial and antifungal antibiotic, by mediating the active efflux of this compound. The NIMT-like subfamily belongs to the 2-nitroimidazole and cyanate transporters like (NIMT/CynX-like) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	3.56545e-32
NZ_CP022163.1\|WP_095978862.1\|4622314_4623175_+\|helix-turn-helix-transcriptional-regulator	gnl\|CDD\|225117	COG2207, AraC, AraC-type DNA-binding domain-containing proteins [Transcription].	5.70791e-22
NZ_CP022163.1\|WP_095978861.1\|4620944_4622144_+\|FAD-dependent-monooxygenase	gnl\|CDD\|180297	PRK05868, PRK05868, FAD-binding protein.	1.4954e-126
NZ_CP022163.1\|WP_095978870.1\|4629885_4631046_-\|hypothetical-protein	gnl\|CDD\|223065	PHA03378, PHA03378, EBNA-3B; Provisional.	0.00110337
NZ_CP022163.1\|WP_071905527.1\|4639497_4640565_+\|acyl-CoA/acyl-ACP-dehydrogenase	gnl\|CDD\|224871	COG1960, CaiA, Acyl-CoA dehydrogenases [Lipid metabolism].	1.04622e-10

>NZ_CP022163.1|WP_095978870.1|4629885_4631046_-|hypothetical-protein
MARISSMFRSTPRPSASPTSSPASSPAAFQPKPLGRATPLTNTPGASSPAAFQPKPLGRATPLANAPGANAPTGTPPKHPGMPEGGPSYTPWEKTSGESLSVSGGDNKLTAPAGAHQNMLVDKPGSPFQKDTFGGGKLSGNVGSMQASTTSHNGGGVHHYSAQAEVQGPHAALEWQKAHAGRFGVTSGQVTAEANSFKGQAQAGVSIDRNDHVYTGAMTARAETGVGVTASANHDFNRHVGGYVKGDARASAAAYAEGVASLDPRTATAMVSGQVGAGATAGAYGTAGGHLGRLHGSVTGGVVAGAAAQAGGKFGLENGFLKQSAEVNAAAGVGTYLKSDVAVDLRHHIKPSIAEGLRPSLAGATGVASPANVVQPEKSWVEKLFI
>NZ_CP022163.1|WP_157775271.1|4628954_4629599_-|hypothetical-protein
MTINRLTPRPPPPPAPKVAPREVRPTWRNGGSMPSARPCMARATTRPIRPRGFGTTAPSTPMPPGARPVQEPQPTGVPGVSADPDNSPDQAKAARQLANQTGANVICVHNGTNGFVPDVAQAAQSGQPVHVAAHSQGAIITSDALQQTKDNLRVQDMSTAQVEQTLGMGLPPNAAQAIASGQRVVVAPNPGPIYGDPFQNHGFSGYVPQAGLPS
>NZ_CP022163.1|WP_095978868.1|4628137_4628680_-|EF-hand-domain-containing-protein
MQARKFNHVFKWFDQNGDGWVTQDDVETMAGLFSAVAEENDQKNRSAMKRGFPHWWTLLLDAREDKASERIGKQEFIRIMDAVVIAPKNFEIAVVGIVDGLLGALDRDGNGSLSREEYVRMYEALGIPPTTSGEAFRRLDRNGDGELSHSEFHQAIVEYYLSSDPNAPGNWLLGSLDALD
>NZ_CP022163.1|WP_170115548.1|4626051_4627719_-|hypothetical-protein
MPKTTRADHPESPVKAGARDGADLATPPSLPEVLPVPAKQETAAGHKTSSKEPRPLPGLEVVGRGIHLRPYQPYSLAQLLFRRKEFRPISFKETRDSYSLPVGYEVNDSPPFPMNESLNQVLIEESWDRFETQMSMDASLTLSNTPFSVSASSGWNNRLRSEQDAYYAVRSSFVPLWTVYIPDPSDCIEEIREPSIPAPFSHRHRRAYDEFFGRYGSHYVRRAWVGGKSTLIFTVLKSSSLSKEDIQAGIKASFGGQDSASNMKGEASREKLKNSSQCTVIGKGGDEVSLAAMSSLDAQAYDGWLKTIPKNPQVIELDVAGIWTLVRDPNKAAALMEAYKESVSFDPITAVFELGREIYFLRGSWFVRYDRDKKVTQVPQPLSDLMPNLEEHGFDRIDTAFRGKDLVSPSGEKLDRKLFIFRHNRFIRFDVDTRQMDAGYPRLISEGWPGVPFDRIDAVLVTGHDTVYFFLGNQYVRFNPLKNRVDEGYPQPLSKRWVGVTFDRLDAAMYWGSGQAYFFKGNQQIRYDLANYRADPGFPKYIIGNYVEDWKFVDD
>NZ_CP022163.1|WP_157775268.1|4625558_4626032_-|DUF697-domain-containing-protein
MSIEDEEKSARAAKVVRNYMFGSAAAGILPIPPLLDAGLLWGVQLRMLHQLAKIYEVEFSQQRALAILGALSGLGLTVSVGTLLWMLVPVPGKILFNLAGLTLPPASTYALGQVFIQHFESGGTFLTFDEKRAKKVYEENLARGQQEAIQSYAGIKP
>NZ_CP022163.1|WP_157775266.1|4624707_4625262_-|hypothetical-protein
MRDPSTPSLVFFRAPRFESFDTISARADDAIARAVPVVTRQWLARVIEWQFRAICFVSFGGMVPSMELREHAPTKPDDRAGRARVGAESRGFIVLGVLLIAANLRAPFTGLPPVLGLIREDFGLSTAAASALTTLPLLAFALVSPSSALLARKYGLERTLFGALVSIALGIVLRSAGASALDRS
>NZ_CP022163.1|WP_157775263.1|4624390_4624702_-|hypothetical-protein
MPDQRLPAAVVAALSAIALLGLLAAPRDAALWAVLFGLGTGAGIILGLTFVSFRTSTAHQAATLSGMAQSIGYLLAAVGPIGTSTIQRSTEHEPRLALDTKEP
>NZ_CP022163.1|WP_095978863.1|4623188_4624280_-|NAD(P)H-dependent-oxidoreductase
MERPNRETTVLILINSKNGSTVRLATEIAAGVEKEHVRAVIKKVPTIDAKDAELFKEIPVATIDELPGYDGIAFGSPIHFGNMSADMRHFLDQGIKIWVDQSLAGVPATVFMAGGSGLGRESAILSFWNNLASQGMTLVTTGNIGAAAAGARALNGNTPFGITTIAGREPKNTLSEAEVDIAREQGAALARAARALSSERPHAKKSASVPAPPKRRTIDTSALGLPKAPKPVGNYRAAVRSGNLVFINQIALKDGKVLHPGVIGKDVSLEQAKEATKQTMQNVLAVLADALDGDLNRVERCVQLTGIFNTPSGFAEHAQVMNAASDYVVEVLGDAGPHARGTLGAASLPLNSAVEIQAIFEVR
>NZ_CP022163.1|WP_095978862.1|4622314_4623175_+|helix-turn-helix-transcriptional-regulator
MKRTRQPSARHLRQIPFAGAKELPVPIFFRTERMPSNATYPLMLHHWGELIYSFSGIVEVTAGDEHVLAPPRLGLWIPAETEHVGFNEAEAVHCSVYINNRLCERMPKTLCGVIVTPLVRAILEHLRDHEASDDDPAARARLLRVLVDQIANCSTTGSYIPRASDPVLDEVLSALKQNPADNRSIAELARAFHLSERTLIRRCEHDLGMSLTEWRQRLRLVTALPLLRSGRGVESVALDLGYATSSSFIAMFRRLMGTSPRQFVTQLPTPSGKAATLPARRRRTSA
>NZ_CP022163.1|WP_095978861.1|4620944_4622144_+|FAD-dependent-monooxygenase
MNSTSPTSPRVLVSGASISGLTTAYWLSRHGFAVTVVERAPHLRPGGHALDVRGPALEVAERMGILTTIRDRSTKLTGISVVDSAGEELFRSTECTLTGGRLDSPDVEILRDDLCDVLHGAVGNQVEYIFGDSIASLTQDESGVDATFVRAAPRRFALVVGADGLYSGVRRIAFGPDEQFLRALGDLYVATFGMPNFLGLERWQVMYSQPDSVGALVMGLRKDVNARTYLGFNAPRGLDYDFRDIDAQKRLLADRVAGAGWVIPRIVEHMLRATDFHFYSLSQVRMSNWSRGRVVLVGDAGYAVSLGTGQATSVAMVGAYVLAGELATHQDDLVAGVAAYEGELHDYVIRNQDIAVEQNARSDEPPDENATPGGLPDFGALTLPFALKNYQGGSRTISP
>NZ_CP022163.1|WP_095982875.1|4632641_4633487_+|hypothetical-protein
MPAELANPAPRGAPIEFEKAQGKPAEPAAPLAEDGTPIPQATDKRPEGDTRSAKDIVNDTPALAKLGRQKDIKFDELCKQTGVDPKLDLKDSKQNPDAVYRLAKVLEFIDSSQISDGGERTGKVKGGKGDGNIEGITKDGDARHGTEAGMVKDFAEKGYASLGTDHRLPTTSDTHVKKDGSNKDNFQWFAGEAGKHLWFMPGVSNVLTGIGNSEGGAGGAILGGLGGMVQTWKGAAEGLIGAVGTGKINPASALLGAYTGALGQTEAAPQEVKDLVNMLPF
>NZ_CP022163.1|WP_095978871.1|4633899_4634949_+|PspC-family-transcriptional-regulator
MGIKLGGASNLFKGGNKVPSFKPSTPKPDAKPQFSPRPDINGNKPGAKPDAKPQFSPRPDINGNKPGAKPDAKPEFSPRPDINGNKPGAKPDAKPEFSPRPDINGNKPGLNRPGFDPGNLSPNMPGSRLGGAVDAFGGVAQGVAGLAGAGLDIASTVGMMAPQLMGPMGPMGMGQQMMPPMMDPMAAAGLGQGFGGAPMMDPYAAAGGLPPELAGAPMMDPYAAAGGLPPELAGAPMMDPYAAAGGLPPELAGAPMMDPYAAAGGVPAGIGGALPTAAEALAPSAGASSQSGLGGLFDTVANAVSSVTQVAEAVTNLVNQVGGGAASAVPTLLGAAGLNPQDTQQTAVF
>NZ_CP022163.1|WP_095978872.1|4635235_4635781_-|hypothetical-protein
MNRTLQTTACALLSLAMLMAGCDGGGALVDENSDIATHVDVAQTSSSMGTQSCTANGVSPELEALTGGPYQNCYGGPIPFISVQSNSQRFSGCCGDLLRTCMVSGYSTLNTMSCTDGSCTVNGVSPQLAALPGGPYQNCQGGTFPRVEYQSGTQHFSGCCGALVRTCKVPGYSTLNTMTCM
>NZ_CP022163.1|WP_063725069.1|4636669_4637338_+|GNAT-family-N-acetyltransferase
MSTQVPPTPPRPSRSSQRIRPYQAEDWDAVYDICVRTGAMGEDARGLLADASLLPDIYAGPYLTFEPNLAFVVEDAGRVVGYTLGTANTAAFIETWRERWLPRVASRYPPPVEPTRTTDEWLVSTLHHPERMLTPEIAPYPAHLHLDLLPEARGGGNGRRLLEAFFLAAAAAGAHSVHMGTNAQAAPFFARMGFARLPEADHNNLVFFHGLTGPLPSARAGT
>NZ_CP022163.1|WP_095978874.1|4637421_4638054_+|glycosyltransferase
MIYLLLLLTGVSALYLMNLAVLLRRVMRALPRITRLEAPAPARWPRVSMIMPARDEARTLEPAMRSKLGNSYPELELVLVNDRSTDATGSLADRFAQEEPRLQVVHIEQLPADWLGKVHAMQRGLERASGEWILFSDADVHLAPKALERIVAYAEHEGLERIGRREAVLRGRAGAEGPRRAADGCRPSCEPGRCRGQAASLGMPAQAALP
>NZ_CP022163.1|WP_170115549.1|4638563_4638719_-|hypothetical-protein
MNLIVILLVLALIFGGVGLFVEGLKWLLIVSAVLFVASLVSGSVGRGRLRA
>NZ_CP022163.1|WP_095978875.1|4638903_4639257_-|hypothetical-protein
MSSKAINEQQVHAFLSGLFGQDVHTMRVLSLSLATLGIIHAASRLGLDWTDYDDDDQTTLVASLMIQHDAPRRSSGSRCRSPRSRGRAMMRSRVQVTLLADRGFADEKSTTPPVFLG
>NZ_CP022163.1|WP_071905527.1|4639497_4640565_+|acyl-CoA/acyl-ACP-dehydrogenase
MYSSGLREQSAHQEEHFSIEALQLLLGRLEGPAEEPVGLAPARGLQQLLSGGFGALPLPGRGQTLLRWRALAAVAAVDLGLIKLFEGHTDALAILAELGAEPPPAGSSWGVWASEPPQARVRVSGRADGRVELSGRKAWCSGAPQVSHALVTAWDAEERQCLVAVAMKQAGVRVTKEGWHAVGMASSASVDVLFEGAVGTRVGPPGGYTARPGFWQGGAGIAACWYGAAAAVGETLRAHCARREEPHARAHLGAVDTALGGARALLREAAAWIDAHPREDASLVAWRARAGVEAAAELVLRHTGRAVGAGPYCRDARVARRMADLPVFLRQSHAERDLEALAGLVVKEGAGGWSL
>NZ_CP022163.1|WP_095978876.1|4640552_4641314_+|PIG-L-family-deacetylase
MEPVNSRRILDEGTSARDWEAWSGLDVLPSLEPALLVPEGRRAVIVAPHPDDEVLGTGGLLARLGRLGRDVLVLAVTDGTASHPGSTSWPVERLARTRPRETQEALHRLGLGGARVERVGIPDGAVTENEERLVEWLGARLRPDDVVLATWRLDGHPDHEAVGRAASRACAALDGRCVEFPIWMWHWARPGDTRVPWSRARRIELDEATLALKRRAMEAYVSQLEPDSTTGNPPIVPPYALERLMRPFEVVFT
>NZ_CP022163.1|WP_157775274.1|4642236_4643361_-|site-specific-integrase
MFVLRKMVQGRAYTVYLDARSETEAEAELALFLRDPEGYRTRQEARQLKQEAAVYLTAETVGRFLESMRNAGTTARYVGNVGFYLATWAEALAGRDLRTVSLQELLRELARHPTGRKNRITALKSFASWLREQGALSLAEDPTVSLKVPVTRPEKAMREKGYSIETTERLYRALSGWEFKNFNQEATRRMTDVQCVRDVLCIHAKTGMHGTEIERLARGEGKVAVLEEPGEIAATVTFIHKSGNVHRQSIDRQTLAAVQRLQARGAAPVDSHIRRVVGRACKKLGIEPVRLGEYRHSFVTWASECGQEVRPKTGGLPLAAIAAVVGHHSANTTKRFYDNVKVPPMIKIPIRLEHPEDPVWLPVRAAALRLVESA

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Crispr_ID: NZ_CP022163_10

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP022163_10

6407371-6407466

Orphan

Consensus_repeat	Method
GTCCGGTGGCGGACTGATGGGGGCGCT	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP022163_10

>merge|NZ_CP022163|10|6407371-6407466|CRISPRCasFinder
GTCCGGTGGCGGACTGATGGGGGCGCTGGGCGGACTCGGGGGCCTGCTCGGAGGCCAGGGCCAGGGCGCGTCCGGGGGCGGACTGATGGGGGCGCT

>NZ_CP022163|10|8|6407371-6407466|CRISPRCasFinder
GTCCGGTGGCGGACTGATGGGGGCGCT	GGGCGGACTCGGGGGCCTGCTCGGAGGCCAGGGCCAGGGCGC
GTCCGGGGGCGGACTGATGGGGGCGCT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP022163.1\|WP_095980132.1\|6405821_6406094_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095980129.1\|6401709_6402708_-\|MoxR-family-ATPase	unknown	unknown	gnl\|CDD\|223786
NZ_CP022163.1\|WP_157775512.1\|6409937_6410537_+\|DUF2378-family-protein	unknown	unknown	gnl\|CDD\|370550
NZ_CP022163.1\|WP_095980136.1\|6410598_6411039_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095980138.1\|6413674_6414418_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095980134.1\|6407746_6409852_+\|ATP-binding-domain-containing-protein	unknown	unknown	gnl\|CDD\|226482
NZ_CP022163.1\|WP_095980142.1\|6419294_6419912_+\|ATP-dependent-Clp-endopeptidase-proteolytic-subunit-ClpP	unknown	unknown	gnl\|CDD\|178955
NZ_CP022163.1\|WP_095980137.1\|6411540_6413646_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095983025.1\|6396454_6400402_+\|protein-kinase	unknown	unknown	gnl\|CDD\|270916
NZ_CP022163.1\|WP_095980125.1\|6391842_6393126_+\|serine/threonine-protein-kinase	unknown	unknown	gnl\|CDD\|270916
NZ_CP022163.1\|WP_157775510.1\|6393103_6395407_+\|FecR-domain-containing-protein	unknown	unknown	gnl\|CDD\|212030
NZ_CP022163.1\|WP_179956477.1\|6420133_6421405_+\|ATP-dependent-Clp-protease-ATP-binding-subunit-ClpX	unknown	unknown	gnl\|CDD\|235422
NZ_CP022163.1\|WP_095983026.1\|6406142_6406898_-\|phosphate-ABC-transporter-substrate-binding-protein	unknown	unknown	gnl\|CDD\|270371
NZ_CP022163.1\|WP_095980128.1\|6400405_6401713_-\|DUF58-domain-containing-protein	unknown	unknown	gnl\|CDD\|224635
NZ_CP022163.1\|WP_095980141.1\|6417980_6419261_+\|trigger-factor	unknown	unknown	gnl\|CDD\|272913
NZ_CP022163.1\|WP_095980127.1\|6395437_6396433_+\|stage-II-sporulation-protein-M	unknown	unknown	gnl\|CDD\|376676
NZ_CP022163.1\|WP_095980130.1\|6402704_6404000_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095980139.1\|6414869_6416057_+\|heparin-lyase-I-family-protein	unknown	unknown	gnl\|CDD\|372911
NZ_CP022163.1\|WP_095980140.1\|6416205_6417294_-\|phage-recombination-protein-Bet	unknown	unknown	gnl\|CDD\|367688
NZ_CP022163.1\|WP_095980131.1\|6403992_6405819_-\|DUF4129-domain-containing-protein	unknown	unknown	gnl\|CDD\|379261

Protein	Function_ID	Function_description	E-value
NZ_CP022163.1\|WP_095980129.1\|6401709_6402708_-\|MoxR-family-ATPase	gnl\|CDD\|223786	COG0714, COG0714, MoxR-like ATPases [General function prediction only].	2.30322e-92
NZ_CP022163.1\|WP_157775512.1\|6409937_6410537_+\|DUF2378-family-protein	gnl\|CDD\|370550	pfam09536, DUF2378, Protein of unknown function (DUF2378). This family consists of a set of at least 17 paralogous proteins in Myxococcus xanthus DK 1622 and and 12 in Stigmatella aurantiaca DW4/3-1. Members are about 200 amino acids in length. The function is unknown.	7.35983e-12
NZ_CP022163.1\|WP_095980140.1\|6416205_6417294_-\|phage-recombination-protein-Bet	gnl\|CDD\|367688	pfam03837, RecT, RecT family. The DNA single-strand annealing proteins (SSAPs), such as RecT, Red-beta, ERF and Rad52, function in RecA-dependent and RecA-independent DNA recombination pathways. This family includes proteins related to RecT.	6.24455e-43
NZ_CP022163.1\|WP_095980142.1\|6419294_6419912_+\|ATP-dependent-Clp-endopeptidase-proteolytic-subunit-ClpP	gnl\|CDD\|178955	PRK00277, clpP, ATP-dependent Clp protease proteolytic subunit; Reviewed.	1.84021e-148
NZ_CP022163.1\|WP_095980134.1\|6407746_6409852_+\|ATP-binding-domain-containing-protein	gnl\|CDD\|226482	COG3973, COG3973, Superfamily I DNA and RNA helicases [General function prediction only].	8.43443e-15
NZ_CP022163.1\|WP_095980139.1\|6414869_6416057_+\|heparin-lyase-I-family-protein	gnl\|CDD\|372911	pfam14099, Polysacc_lyase, Polysaccharide lyase. This family includes heparin lyase I, EC:4.2.2.7. Heparin lyase I depolymerizes heparin by cleaving the glycosidic linkage next to an iduronic acid moiety. The structure of heparin lyase I consists of a beta-jelly roll domain with a long, deep substrate-binding groove and an unusual thumb domain containing many basic residues extending from the main body of the enzyme. This family also includes glucuronan lyase, EC:4.2.2.14. The structure glucuronan lyase is a beta-jelly roll.	2.80045e-64
NZ_CP022163.1\|WP_095980125.1\|6391842_6393126_+\|serine/threonine-protein-kinase	gnl\|CDD\|270916	cd14014, STKc_PknB_like, Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.	1.06905e-103
NZ_CP022163.1\|WP_157775510.1\|6393103_6395407_+\|FecR-domain-containing-protein	gnl\|CDD\|212030	cd00118, LysM, Lysin Motif is a small domain involved in binding peptidoglycan. LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.	5.99369e-06
NZ_CP022163.1\|WP_179956477.1\|6420133_6421405_+\|ATP-dependent-Clp-protease-ATP-binding-subunit-ClpX	gnl\|CDD\|235422	PRK05342, clpX, ATP-dependent Clp protease ATP-binding subunit ClpX.	0
NZ_CP022163.1\|WP_095983026.1\|6406142_6406898_-\|phosphate-ABC-transporter-substrate-binding-protein	gnl\|CDD\|270371	cd13653, PBP2_phosphate_like_1, Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 periplasmic binding fold superfamily. This subfamily contains uncharacterized phosphate binding domains found in PstS proteins that serve as initial receptors in the ABC transport of phosphate in eubacteria and archaea. After binding the ligand, PstS interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The PstS proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.	1.88516e-98
NZ_CP022163.1\|WP_095980128.1\|6400405_6401713_-\|DUF58-domain-containing-protein	gnl\|CDD\|224635	COG1721, COG1721, Uncharacterized conserved protein (some members contain a von Willebrand factor type A (vWA) domain) [General function prediction only].	1.64988e-64
NZ_CP022163.1\|WP_095980141.1\|6417980_6419261_+\|trigger-factor	gnl\|CDD\|272913	TIGR00115, tig, trigger factor. Trigger factor is a ribosome-associated molecular chaperone and is the first chaperone to interact with nascent polypeptide. Trigger factor can bind at the same time as the signal recognition particle (SRP), but is excluded by the SRP receptor (FtsY). The central domain of trigger factor has peptidyl-prolyl cis/trans isomerase activity. This protein is found in a single copy in virtually every bacterial genome. [Protein fate, Protein folding and stabilization].	1.14782e-115
NZ_CP022163.1\|WP_095980127.1\|6395437_6396433_+\|stage-II-sporulation-protein-M	gnl\|CDD\|376676	pfam01944, SpoIIM, Stage II sporulation protein M. SpoIIM is on e of four stage II sporulation proteins that is necessary for the forespore inside the mother-cell to be properly internalized through the breakdown of peptidoglycans trapped between the membranes of the septum separating the forespore and the mother-cell. The four proteins working in sequence are SpoIIB, pfam05036, SpoIIM, SpoIIP, pfam07454, and finally SpoIID, pfam08486. D, M and P are in a complex with each other and the complex assembles in a hierarchical manner such that M, which serves as a membrane anchor, recruits P to the septum and P, in turn, recruits D to the septum.	2.00533e-34
NZ_CP022163.1\|WP_095983025.1\|6396454_6400402_+\|protein-kinase	gnl\|CDD\|270916	cd14014, STKc_PknB_like, Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.	4.8474e-88
NZ_CP022163.1\|WP_095980131.1\|6403992_6405819_-\|DUF4129-domain-containing-protein	gnl\|CDD\|379261	pfam13559, DUF4129, Domain of unknown function (DUF4129). This presumed domain is found at the C-terminus of proteins that contain a transglutaminase core domain. The function of this domain is unknown. The domain has a conserved TXXE motif.	0.00668409

>NZ_CP022163.1|WP_095983026.1|6406142_6406898_-|phosphate-ABC-transporter-substrate-binding-protein
MLTVKGSDTLVILAQRWAEHFMKAHPGARIQVTGGGSGTGIAALINGTTDIAMASRPLEDAERRQVRQKHPQGPVELAVALDGISFYVHESNPVSGLTLAQLKAIYLGDTTRWKDVGGEDKPIVVYSRESSSGTYAYVKERVLGGQDFTERAQTLPGTAAVVNAVSLERHGIGFGGAAYLRGVKALKVGRDAQRAVFLSAETLRDGTYPLARELYFDLVRPPSGLAREFIDHALSPEGQRTVIDAGFFPVK
>NZ_CP022163.1|WP_095980132.1|6405821_6406094_-|hypothetical-protein
MIQGSGRCHSHPDRTGLGICVECRRVICRECTTQFEGINRCATCLAQRLKALEVTAERREWSVGNVLLALVGAALLYGGVWVAAHLASGL
>NZ_CP022163.1|WP_095980131.1|6403992_6405819_-|DUF4129-domain-containing-protein
MAVSALELRPRGAVAILDAALRVCVRSAGVWALTLPGGALVTAALLHLTDAVMHHRALELPALGFTLAWLARGLFQGAACHHVQELLLGTGAQPPTAWASLRAALARTPSLLCAVAYLFLFNLLSLSLTLGCAFFFLSSHLVGYAAALRGRGSPLGLYGQCGKLLGPARGNAVGVRVLLLVQGLVFINLHIAANALLYVGRKLLGIDLTFVERFASLDNTAWTVFLVAATFTLFEPLRAATATLLLVDGRVRQEGLDLIAAVQQLPVRKAALVLAALLGTGLFAPPARAEEPPLRERVEGVMGVCEEVPEEDWAHTLDSLGPEEALKFERLVRSVEKDVYDGEECEALGRLEQGIVLAAQTVALERQQKESAQARARDILARPEFQVPEPQSPQDSSKELVPPEPPGLWQRFLDWLGERLKEFFNRKETAPRPPRTNVSGGQSVANALVAILIAGALGVLAWVLWRSLAERRRADGDAGLEVSTQDAATLAADPMNALSRPPEGWAHLADTLAARGEYREAVRGLYLALLSRLHREGVIHYDSHASNWDYLLQFRGRTEWKPPFRELTLRFDFAWYGNLPVGPDGYREFRELCAPMLAPPAPTEPARA
>NZ_CP022163.1|WP_095980130.1|6402704_6404000_-|hypothetical-protein
MRDRFPLLVAGSLLVIAILGAWLVRGAARGGFADTLSTWRAQPDGSRGLYLLAEESGLEVSRRTADLLILHEPGTLVLLAVEVEGAQEADPDQTALATERDEGLRDEDVPRHGLNRLHVPELSEDETTKLLDHVWAGHTLVLVPWGSRENPLLEKLGVTLTKADTTLPMRTLVPPLSSPYTLDVQRVEARVQAYLELSGADAIPVLEDEPLGLTVAAVVTHGAGQVLIVGAPELAMNQALGRADNAQFWLSALRALGPGPYVFDEHHHGFTNERSVVDFARRYGLHFAVAQLLLGLGLWALALKRFGRPRPPPESTRVGATDALFAMSRLYREGHHHAFAAGLLTRGLTQELAQHAGLPAHAPADAVAESLAANGRTDLSQGLRALVRRAQDVASESDLMKLATRSAALRQRLHPSGPPSGAPLAPLPEEP
>NZ_CP022163.1|WP_095980129.1|6401709_6402708_-|MoxR-family-ATPase
MTSPPFATAPLPASNAVAAAHSIREGVLTEVRKAVVGQDEPLELMLVGLVAGGHVLLEGVPGVAKTLMAKALARSVSADFKRIQFTPDLMPADILGTSIFDLKSQSFVLVRGPIFTDLLLADEINRAPAKTQSALLEAMQERAVSLEGRNLTLSPLFSVFATQNPVESEGTYPLPEAQLDRFLLKIEVGYPAPEEEDAILASVHRGFDAGDLTRAGVGAAVTKEGVLEARAALNEVTVEPPVLSYVRQLVAATRTSSRIRLGAGPRAGVHLLLASKALAALRGRGFVTPEDVRFLAGPVLKHRLLLSPDAELDGATPSDVLREVVRSIEVPR
>NZ_CP022163.1|WP_095980128.1|6400405_6401713_-|DUF58-domain-containing-protein
MIPTGRLWVLLCLLAVPMMAAGFFPGFGGVVLVLDVLALALAAVDVGLARQVRLEVHRTLPPRLSVGVANKVELLLVHRGRRAVDVQVRDDVPAAFTATPEEAPLRLSADSQTRWVYRVTPAHRGRFDFGDVHVRVRGPLGLVLHERRFPAAQSVPVFPDMRGASRLLLSGAALDLVNLGLRQLRRDGRGSEFARLRDYAQGDSVREVDWKATARRSRPVTRVMESERSQSLLICVDAGRSMAARVDGLTKLDHAVNAALFLAFVAVRNGDRVGLAVFADGVKTYLPPAAGRLQYRKILDALYTTTPSLTYVDYLALFKELNVRLTRRSLLCVFTDFLDEEQASTMVAPLHRLARRHVPLCLSVRDTALAKLLRTTPSGPEQAYQQAVASELLTDRESLKAQVSAGGVHMLDVQPDELSLAAVNRYLDIKARGVL
>NZ_CP022163.1|WP_095983025.1|6396454_6400402_+|protein-kinase
MNDTKTPEDAETVPSAPSSGVLSPGTLVDERFVIEALAGRGGMGHVYRARDQETGQRVALKLLHGTPAPDALYRFHREATLLSSLRHPGLVAHVAHGATEQGQAYLVMEWLEGEELARRLSRQPLSVAESLSLLRRVAEALAHAHERGIVHRDLKPTNLFLRAGRPEDGVILDFGLARHAEPTLMGVTRSHTVVGTPGYMAPEQASCHPEIPPAADIFSLGCVLYECLTGRPPFEAPHFAAALAKILFAEPVPPRALRPGLPEALQGLVERMLAKEPSRRLPHATALLEALSLLDLGPERPPSGSLDAPWLPSLAEGEQQLVSVLLVSSLAGASPSWGREMRETLRTMLVPQGGRVEGLADGSLVATLLPVRGTATDQAALAARCALALKERWPEASVALVTGLGVLEAHLPVGEAMDKAGRLLRRIEQAPSSSVLMDEVTAGLLGAGFQLTPSGSGSFLLRSERLGVDTSRPLLGKPTPCVGREQELALLESCFATCREESNARALLVTAAPGVGKSRLRHEFLRRLEHKEEPPRVLLGRGDPMHKGVSYGLLGQVLRELGGVVEGEPLESKRSRLFQRVSRYLSEAQAREVTPFLGELCAIPFPDEDNPRLRAARQEPQLMGAQMGRALVAFLDAECAHTPVLLVLEDLHWGDVLTVTLVDRLLRDLSERPFMVLALARPEVKQLFPALWGRAVQELSLNGLSRKACARLVREVLGAGVPDAVVRQTVEQSDGNALFLEELIRMVAEGRGDAAPETVLAVLQSRLMRMEAGARQTLLVASIFGRAFWPGGVEELLGRPAGDGLVRTHLRLLVEQEVIEPVPDSRFPTAPEYRFRHALVRDAAYGLLAEAHRTLAHRLAGAWLERMGEPDVEEIATHYQLGQQPERAAPLYTRSAEQRFEHNDLQGTLRCVNAALACGVGDEVLSKLRALEALVSFWSDDVPRTLELGVPILDTLPRGGRFWCWLCGGLILGNILGGQAEETQRLCELLLRTDPEPDAVVRYIEALVSMSSTLMWSDEHQLMPVLRNRAREVGVSSMERQVLVRGYLRMMESQYLYLVESSPWRSLRQVEVALRDFEEIGSERNVCLLRNVMGLLCLELGDVPGALRCLREARDGAWRQAQYLLSSQAGYYLMQALAFSPEPEHRREALEMAREGRDIELSMAVFQGLRDSFAAQTLGVHGEWGEAETRARRACELLESLPSVRGFAQAVLSEILRRQGHLDQARSLARSGVRSLELCGTGIYMVFIHLSLVEACLAQGDDAEGEAALRKALERVRTWAHDITDAAARERFLTQVPVNARVLALARARWGDVRV
>NZ_CP022163.1|WP_095980127.1|6395437_6396433_+|stage-II-sporulation-protein-M
MEMPEFIEARRPRWQTLETLLDKAEGRGLRALELEEARSLGRLYRAVSSDLLWVRARSGSADVSEYLNDLVGRAYALTYPGERPRLADMWGFVARGFPALLRQEWRMYAASLLLFLAGLGFGYLGMWADPDAAPYLVPTEHLSLDPLRRAADEAAGEGASVEQQAQFTTFLFTHNIQVAFLAFALGITAGVGTAIMLFSNGLMLGALAQVYTAKGMAGWFWAWILPHGIPEITAICIAGAAGFVIARGQVAPKGLPRGMALRQEAVGAVRLLFGTLALFVLAGFIEGTISQIHPPKLSVAFKVSFALVVGAGVYAYLGSDWIRAGRRAAAR
>NZ_CP022163.1|WP_157775510.1|6393103_6395407_+|FecR-domain-containing-protein
MRGNPNVSGLALVFALVLCPPAISRAQQHAADDDVYVVQPGDTCGSIGRKVFGDPAKGSATLHALNKMGPPPHDLKPGTVLRVRGDPDARLTFIKPEVNSKRAGKPDWFQASTGQGLWRLDSVNTLRQAGAEMTFRDLTRLQMNENALVVLYGEDTPATDQVKKSGAVELLQGELSLSLAELRGDSLGVKMPAATVSSRSKELVVGVDSQQMTRLSVFDGQAEVNAQGQRVRVPRDHGTRVEKGKVPEQPRLLPEPPEWVGGVRSVRLLLDGQGVDEALTWTPVVRAETYRVELARDERFNDRVHEASVPAGPAVLESVARALLPGQYFARVRAVDAAGLLGRVSEVRQVEVLRVKTDRGSLGPQGLQGTYPLEFTVDGAEALEARLDGVVTSLPVRVEAVGTHTLELRPRGMPGARAETLSLTVSPPRVDVTLEPGAESFLARVRVLDAHGAPLEVPPHAVTLRGVEGTQVEPLTKQTDGSWLARAVPVVRDGERVASLEALWGNTSLQRLSARAPAPVPPPAPGVTPEAARVSVLGAPSGGRLDAAPLPTSFLPQALLVELRAQPGPGRGVDVAGSRATLFVEGRVAERVALGTALRTSPGTASALSASVSGRVWLSESPTFRALLSFEGMWAGAESDEASRGLWLRPALLLGGRWDRWALSTSQGYALRPGEARATWDSSYQGWFLPRPTLALGAELGAQIGATPREKGPHSYAAGVGARWKRGGFELGASVRRGLGPQGATVWGTWSGQLTLGWSGLLASRPQ
>NZ_CP022163.1|WP_095980125.1|6391842_6393126_+|serine/threonine-protein-kinase
MKLQTGQLIGGRFRVLRALGEGGMGAVYEAEQQGLGRLVALKVMHPHVAQAPGFVERFHREARVLARLRHEGSVEVYDYGLDAGFLFLAMERVTGETLEAVLQREGALAPRRAVGIAMRTLEVLEAAHALGIFHRDLKPSNLFLEAHPGGERVKVLDFGLATLGMPAQARLTQEGMTVGTPGFMSPEQLRGFPLDGRSDLYSLGCVLYEMLTGLVPFAAMPTVEMATSHLYRPVTPPREARPDLLVSERLSAVVMKALEKLPTARPADAAAMREELLAVLAEPGAEQVPRRRGEGKKQERVTAPLMAAPRPAPGDVSVGVLASRADLAEPLVVALAACGFQARRVGAEESWTELGVVLVVAEGRDALAQARQWVSRPGVPPLLLCGPAEDWDLVTGALEGGLFDFVPLPPDPMDLTRKVSRARKSKR
>NZ_CP022163.1|WP_095980134.1|6407746_6409852_+|ATP-binding-domain-containing-protein
MSTPDGELSPEEQAIISEEEAFLRRVLGSLEAARLRGGERTQETERLIAQLEVLRDDAVSAPVADLPHLFHQMDQTRALLDRQKVTRLPEFSAPYFAHLKVNGPVGDRDYLLGRTSYADASADVRIIDWRFAPVARVFYRYGEGDSYEEWFGERLSEGTVLVRRLVVIERGRLTRIQVGPLVLVRSPEGAWRRVGAGAMSPLAGGMGTAVRPGRLGVGQGASRREGALDVTALLDAEQFEAVNVAADEPLLVLGSAGSGKTTVALHRLAKIAFDERARYPESRMKVIVPEEGLARLSRRLLAPLGLEKVSVETLDSWAALTARIAFGAKALKVWEDTPPLVSKFKRHPALRRALAARLGVLKSSATTLPRLRKRLAELFTDRRFLEGVVSHSKGDLPLTAIDELVRHTMLQIATPLERELEGVDPDRLQTLDGKSLQSDTPDELAGTLDLEDLPLLLFLRAQGGNLGAVGRLVHVVLDETEDFSLVELFVVGRLLGDARSCTLAGDEMQQTSTSFAGWPAVLAELGIQDAATCRLQVSYRCPAPITALARHVLGTQAPSTAPQAGREGAPVGLHHFPDEAQAHLFIGEALRELLEREPHASVAVIAQGPEQARAFHRMLADTSWARLVLEGDFSFEPGVDVTDVDNVKGLEFDYVVIPDATARAYPVNDEARRRLHIAITRASHQLWLVSSGVRSPLLAGC
>NZ_CP022163.1|WP_157775512.1|6409937_6410537_+|DUF2378-family-protein
MSESRPQLLSRLARSTREQTISGMFLQAVLASAEVHGMDVVARARSRVGEGGPLVESYRYPVGCMLEMLDIIGQAAESRGLSYGEALFESGRDAGFAYVRSAVGRMRVLVASASGLHRALEGIPSAALLSVNFGERSYRRLTHSSGDLAFNQDLIGTAWNIGLVTASVSAGLALAPDALKFHVNVTDEDASSFVLHLFW
>NZ_CP022163.1|WP_095980136.1|6410598_6411039_-|hypothetical-protein
MSFSVNNRSAAATTTTQQTASTADTSKMESVKDLLSGGSFKMGVDGTSDFNAVSDAFKRFSDGNSADGYALMAEGLGKDFKGKMLASVEKKMDAWLKENPNATPAKVAEKAKSLLMNETVMFQTMKNTITQMANDAISRMRDTFEG
>NZ_CP022163.1|WP_095980137.1|6411540_6413646_+|hypothetical-protein
MDSISNKPARSSAAWEGGFASPFSGYSLQGAGAIQVNLPEWGGVLGPATLLSPAAVWARPGRQGGSLARERTLRVCLETEAGDIGPLKGEIHWNGATGEALGIQLLGVSPHQGERILTLLDAEVRRGLAVPEASPLPVQEEITGGERLRAVLRKIAALGNQAVVRRPGQAVRMTLERLDEEGGRLYWRCAEPGAGWGGASAELEVVGYNSAYRMHLETRASEGGLWVTSLPERLWRVRHRWHRRVLAPEGTRARFEHPLWSELGWHSRDVVDVSYSGLSLRSGTGDLLFPGLFLPLEVETAHGERISLRCEVRHVSFSQADGRRLCGLEARPLTPRDSVLWMRFVSQTLSPSTRSGEAWLEPLWDLYAASGYFNLAGKSSHHFDALRRDFIDLSGRAAKLPHVFCQTVWPSERGVEASLSAVKPYQNTWMLHHLGRRPGKPVNAPPVPGQILRDIYQRTLEHAQVDPDFRWLISYAESTVPWVRRTHLAFAERAHEGGESLVMYLRLMDAECSEMSGEPVGDVEIGPASMGEKLLLAREIARTRPASYADSLDLTRERLELRGASRFWKEEGLRRERRILVARREGVAVAALVLELGPPATNLFRLMDCARLFPLLPEGKDAYVALLDEARRWFAFHGRTAFVYLCEDEGGYARRARLHDDPSTQPFLWIISASLAPEFLEHIQEQSVGRQPSHTPSVLSS
>NZ_CP022163.1|WP_095980138.1|6413674_6414418_+|hypothetical-protein
MELLKNLYEPHALPARALLDTDPALRRLLDPSLNPKVLARFLIEWMARAAYMTEPVDGWIRGTGQRCIEQGMEKMGRALITHAKSETGHHLMTLEDARSLVGHWNTRYLPTLSVRELCAQPPFESMAAYRRLHDETIGGAFPVGQIAIEREVGFLAVYFGPKLMQQVERLLGPEVAGMLTFLTEHVAVDVGHTLLNERMLEEAISLSPGNARIYAETGALAMTLYIRFLGDCLHTVEDLFSPLRSVA
>NZ_CP022163.1|WP_095980139.1|6414869_6416057_+|heparin-lyase-I-family-protein
MKKTLLLVETVFALAGVVACGGPEQLDADESTQTLGVTADALSTQNCSPLSATSVIASGNDGNGPQNTLDDQLGTRWSNLGKGSWIDYDLGSARTVSGAAIAWHQGNQRTNNFAVSVSTDGMVYTPVYTGTSSGTTTVAETVSFAARTARRLRITFQGNSQNDWASIAEARACGVAAEAGSGSGVVWRGDFETGSRSQWSSTQMVNADRLQVVSSPTRQGSYAIKVTVRQGDNPISASGNRNELVRMTNEKEGDEYYYKWSTMFASDFPSAKTWQLFTQWHHSGSNGSPPVEFYVNGETIYLRMRGSTVVWQTPLVRGQWLDFVFHVKWSAKSNVGFVELYYRGNLVLPKLYGATMYSGQTNYLKVGLYRNSTIAPVGVVYHDGWVQGRSLQDVQ
>NZ_CP022163.1|WP_095980140.1|6416205_6417294_-|phage-recombination-protein-Bet
MEAHNKTETASGQWSPERVELIRRTICPRGIGEDEFALFIEQCKRSGLDPLLKEAFCVARRQNAGSREKPNWVSRHEFQPSEAGMLARAERFPDCKGIQASAVYAEDEIIVDQGKGEVVHRFNPAKRKGSLVGAWARVVREGKLPVVVWLDFAGYVQQTPLWAKIPTTMIEKCARVAALRKAYPEAFGGLYVREEMPAEEFDSPSEPISTQGLGSVKASFPTSPREVREAREEAKAPEHAPEPVKETAREPEAPAMESVKAESVKARPAPVPPPAPEPAPAAAEPAPKLKGSSVVVAFGANKGRTASELSDEELAETIDLAHEKLMEQPKAKWARAMRENLAALELEAELRCRVPAANEAKL
>NZ_CP022163.1|WP_095980141.1|6417980_6419261_+|trigger-factor
MKVQVEELSPIEKKLSIEVDTARVAEELTRAYTALGQQVKLPGFRQGKVPRRILEQRFRDRVEDDVIQRVVQSAWLQAVRDHKVEAVAPPQVTQNSGLKPNAPFSFEARVEVKPRVEAKDYQGLALTRADTQVADSDVNERLEQLRQNLARLDPIEDRDVAQAGDFATVDYEATVEGKEFAGSKAEGVTVELAPGELVESNVAALEGAKVGETRELDYTFPADYRVEDVKGKAAHFKFHVKGLKKKIIPELNDDFAKEAGQAQSLDELRTKIRADLEQGKKTKALNEEREALIKALIEKNPFEVPKAMVERTIDQMLETRLRAMARMGMDPRRLNLDFARLREDLREEALQEVRGALLFEAIALKEGIQTSDEDLEKKISELAQEANQSIDVVRKYFKGPDERQGLSLRLREEKTIEFLKGQAKYS
>NZ_CP022163.1|WP_095980142.1|6419294_6419912_+|ATP-dependent-Clp-endopeptidase-proteolytic-subunit-ClpP
MPFMPVPYVIEQTHRGERSYDIYSRLLKDRIVMLGTEIDDDVANVIVAQLLFLESEDPDKDINLYINSPGGSVTAGLAIYDTMQYVKPNVSTICVGQAASMGAVLLLAGAKGKRYALPSARIMIHQPLGGVRGQATDIEIQAKEILRMRAKLNELIVKHTGQPIERVEKDTDRDYFMGAAEAKAYGILDEVQNPRKVLLPPGERK
>NZ_CP022163.1|WP_179956477.1|6420133_6421405_+|ATP-dependent-Clp-protease-ATP-binding-subunit-ClpX
MEKRDNQSLCCSFCGKSQKEVKKLIAGPTVYICDECIGLCNDIIAEEIDREETKDTKLRIPRPSEIKAILDEYVVGQERAKKTLSVAVHNHYKRIESKVAMDDVELQKSNILLLGPTGSGKTLLAQTLARILNVPFTIADATCLTEAGYVGEDVENIIVNLLQAADHDIERAQRGIVYIDEIDKIARKSENPSITRDVSGEGVQQALLKIIEGTIANVPPKGGRKHPQQEFLQVDTTNILFICGGAFGGLEQVIERRLGGRSLGFGADIQSKKQRNLTELLKHVEPEDLLKFGMIPEFIGRLPIVTALEELDEPALVNILSQPKNALTKQYKKLFDLDGISLKFTDGALKAVSTEAIRRKAGARGLRSILESAMLDIMYELPSRKTAREVVISEEVILKKSEPVVLHSQDNKEKEPEQKKESA

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Crispr_ID: NZ_CP022163_11

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP022163_11

7266492-7266581

Orphan

Consensus_repeat	Method
CGTGGCGGCGCTGGACAACGAGGC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP022163_11

>merge|NZ_CP022163|11|7266492-7266581|CRISPRCasFinder
CGTGGCGGCGCTGGACAACGAGGCGGCGCGCAAGGCCCTGCAGGAGTTGGTGTCCCTCAAGGACGACGTGGCGGCGCTGGACATCGAGGC

>NZ_CP022163|11|9|7266492-7266581|CRISPRCasFinder
CGTGGCGGCGCTGGACAACGAGGC	GGCGCGCAAGGCCCTGCAGGAGTTGGTGTCCCTCAAGGACGA
CGTGGCGGCGCTGGACATCGAGGC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP022163.1\|WP_095980680.1\|7261256_7263755_+\|leucine--tRNA-ligase	unknown	unknown	gnl\|CDD\|234743
NZ_CP022163.1\|WP_095980678.1\|7259837_7260638_-\|Fpg/Nei-family-DNA-glycosylase	unknown	unknown	gnl\|CDD\|223344
NZ_CP022163.1\|WP_095980692.1\|7277854_7279399_+\|lysine--tRNA-ligase	unknown	unknown	gnl\|CDD\|234778
NZ_CP022163.1\|WP_095980686.1\|7269561_7270632_+\|PhoH-family-protein	unknown	unknown	gnl\|CDD\|376820
NZ_CP022163.1\|WP_095980677.1\|7259348_7259828_+\|cupin-domain-containing-protein	unknown	unknown	gnl\|CDD\|380376
NZ_CP022163.1\|WP_095980675.1\|7256638_7257478_+\|protein-glutamate-O-methyltransferase-CheR	unknown	unknown	gnl\|CDD\|224271
NZ_CP022163.1\|WP_095980691.1\|7277422_7277776_+\|zf-HC2-domain-containing-protein	unknown	unknown	gnl\|CDD\|379219
NZ_CP022163.1\|WP_095980681.1\|7263840_7264392_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095980687.1\|7270736_7273232_+\|HDIG-domain-containing-protein	unknown	unknown	gnl\|CDD\|224397
NZ_CP022163.1\|WP_179956319.1\|7273248_7274103_+\|rRNA-maturation-RNase-YbeY	unknown	unknown	gnl\|CDD\|376735
NZ_CP022163.1\|WP_095980683.1\|7264790_7265969_-\|nucleoside-triphosphate-pyrophosphohydrolase	unknown	unknown	gnl\|CDD\|236569
NZ_CP022163.1\|WP_095980693.1\|7279412_7281779_+\|ABC-transporter-permease	unknown	unknown	gnl\|CDD\|226957
NZ_CP022163.1\|WP_095980682.1\|7264404_7264677_-\|30S-ribosomal-protein-S20	unknown	unknown	gnl\|CDD\|178943
NZ_CP022163.1\|WP_095980688.1\|7274224_7275535_+\|DUF4105-domain-containing-protein	unknown	unknown	gnl\|CDD\|379156
NZ_CP022163.1\|WP_095980676.1\|7258510_7259317_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095983092.1\|7257474_7258509_+\|chemotaxis-response-regulator-protein-glutamate-methylesterase	unknown	unknown	gnl\|CDD\|234828
NZ_CP022163.1\|WP_095980694.1\|7281784_7282459_+\|ABC-transporter-ATP-binding-protein	unknown	unknown	gnl\|CDD\|213222
NZ_CP022163.1\|WP_179956320.1\|7276772_7277396_+\|sigma-70-family-RNA-polymerase-sigma-factor	unknown	unknown	gnl\|CDD\|236608
NZ_CP022163.1\|WP_095980685.1\|7268271_7269465_+\|DUF4388-domain-containing-protein	unknown	unknown	gnl\|CDD\|373017
NZ_CP022163.1\|WP_095980679.1\|7260778_7261162_+\|response-regulator	unknown	unknown	gnl\|CDD\|381110

Protein	Function_ID	Function_description	E-value
NZ_CP022163.1\|WP_095980680.1\|7261256_7263755_+\|leucine--tRNA-ligase	gnl\|CDD\|234743	PRK00390, leuS, leucyl-tRNA synthetase; Validated.	0
NZ_CP022163.1\|WP_095980678.1\|7259837_7260638_-\|Fpg/Nei-family-DNA-glycosylase	gnl\|CDD\|223344	COG0266, Nei, Formamidopyrimidine-DNA glycosylase [DNA replication, recombination, and repair].	5.79489e-58
NZ_CP022163.1\|WP_095980692.1\|7277854_7279399_+\|lysine--tRNA-ligase	gnl\|CDD\|234778	PRK00484, lysS, lysyl-tRNA synthetase; Reviewed.	0
NZ_CP022163.1\|WP_095980686.1\|7269561_7270632_+\|PhoH-family-protein	gnl\|CDD\|376820	pfam02562, PhoH, PhoH-like protein. PhoH is a cytoplasmic protein and predicted ATPase that is induced by phosphate starvation.	1.96101e-137
NZ_CP022163.1\|WP_095980677.1\|7259348_7259828_+\|cupin-domain-containing-protein	gnl\|CDD\|380376	cd06121, cupin_YML079wp, Saccharomyces cerevisiae YML079wp and related proteins, cupin domain. This family includes eukaryotic, bacterial, and archaeal proteins homologous to YML079wp, a Saccharomyces cerevisiae cupin-like protein of unknown function that structurally resembles plant seed storage and ligand-binding proteins (canavalin, glycinin, auxin binding protein) as well as the bacterial RmlC epimerase. YML079wp is non-essential in yeast and localizes to the nucleus and cytoplasm. The presence of a hydrophobic ligand within a well-conserved binding pocket inside the cupin beta-barrel and sequence similarity with bacterial epimerases suggests a possible biochemical function for YML079wp and its homologs. Also included in this family are Shewanella oneidensis So0799, Agrobacterium fabrum Atu3615 and Branchiostoma belcheri Bbduf985. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold and forms a homodimer.	1.62397e-69
NZ_CP022163.1\|WP_095980675.1\|7256638_7257478_+\|protein-glutamate-O-methyltransferase-CheR	gnl\|CDD\|224271	COG1352, CheR, Methylase of chemotaxis methyl-accepting proteins [Cell motility and secretion / Signal transduction mechanisms].	6.839e-90
NZ_CP022163.1\|WP_095980691.1\|7277422_7277776_+\|zf-HC2-domain-containing-protein	gnl\|CDD\|379219	pfam13490, zf-HC2, Putative zinc-finger. This is a putative zinc-finger found in some anti-sigma factor proteins.	3.71258e-05
NZ_CP022163.1\|WP_095980687.1\|7270736_7273232_+\|HDIG-domain-containing-protein	gnl\|CDD\|224397	COG1480, COG1480, Predicted membrane-associated HD superfamily hydrolase [General function prediction only].	2.83524e-138
NZ_CP022163.1\|WP_179956319.1\|7273248_7274103_+\|rRNA-maturation-RNase-YbeY	gnl\|CDD\|376735	pfam02130, UPF0054, Uncharacterized protein family UPF0054.	2.42517e-46
NZ_CP022163.1\|WP_095980683.1\|7264790_7265969_-\|nucleoside-triphosphate-pyrophosphohydrolase	gnl\|CDD\|236569	PRK09562, mazG, nucleoside triphosphate pyrophosphohydrolase; Reviewed.	2.09672e-109
NZ_CP022163.1\|WP_095980693.1\|7279412_7281779_+\|ABC-transporter-permease	gnl\|CDD\|226957	COG4591, LolE, ABC-type transport system, involved in lipoprotein release, permease component [Cell envelope biogenesis, outer membrane].	6.36438e-94
NZ_CP022163.1\|WP_095980682.1\|7264404_7264677_-\|30S-ribosomal-protein-S20	gnl\|CDD\|178943	PRK00239, rpsT, 30S ribosomal protein S20; Reviewed.	4.82021e-15
NZ_CP022163.1\|WP_095980688.1\|7274224_7275535_+\|DUF4105-domain-containing-protein	gnl\|CDD\|379156	pfam13387, DUF4105, Domain of unknown function (DUF4105). This is a family of uncharacterized bacterial proteins. There is a highly conserved histidine residue and a well-conserved NCT motif.	1.30743e-33
NZ_CP022163.1\|WP_095983092.1\|7257474_7258509_+\|chemotaxis-response-regulator-protein-glutamate-methylesterase	gnl\|CDD\|234828	PRK00742, PRK00742, chemotaxis-specific protein-glutamate methyltransferase CheB.	3.66957e-132
NZ_CP022163.1\|WP_095980694.1\|7281784_7282459_+\|ABC-transporter-ATP-binding-protein	gnl\|CDD\|213222	cd03255, ABC_MJ0796_LolCDE_FtsE, ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and cell division protein. This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. An FtsE null mutants showed filamentous growth and appeared viable on high salt medium only, indicating a role for FtsE in cell division and/or salt transport. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.	1.58325e-100
NZ_CP022163.1\|WP_179956320.1\|7276772_7277396_+\|sigma-70-family-RNA-polymerase-sigma-factor	gnl\|CDD\|236608	PRK09652, PRK09652, RNA polymerase sigma factor RpoE; Provisional.	7.70852e-50
NZ_CP022163.1\|WP_095980685.1\|7268271_7269465_+\|DUF4388-domain-containing-protein	gnl\|CDD\|373017	pfam14332, DUF4388, Domain of unknown function (DUF4388). This domain family is found in bacteria, and is typically between 102 and 135 amino acids in length.	5.21068e-18
NZ_CP022163.1\|WP_095980679.1\|7260778_7261162_+\|response-regulator	gnl\|CDD\|381110	cd17562, REC_CheY4-like, phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY family proteins. CheY family chemotaxis response regulators (RRs) comprise about 17% of bacterial RRs and almost half of all RRs in archaea. This subfamily contains Vibrio cholerae CheY4 and similar CheY family RRs. CheY proteins control bacterial motility and participate in signaling phosphorelays and in protein-protein interactions. CheY RRs contain only the REC domain with no output/effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.	1.12686e-33

>NZ_CP022163.1|WP_095980683.1|7264790_7265969_-|nucleoside-triphosphate-pyrophosphohydrolase
MGSAGQQLDRLAEIMARLRAPDGCPWDKKQDLRSMRPYLTEEAFEVLEEMDRVAEGSPWHPLCEELGDLLFQIVFHARLAEELGEFTLADVCASIGDKLTHRHPHVFGERREDGMPQPLANWAKLKAEERKKKTGREGSVLDGMPMGAPSLLRAERLLEKASRIGFDWPALEQVRAKLSEELGELDEAITSQDRDALEHELGDVLLALANLSRFLRTPAEDALRMALRRFTTRFQHIESALRSEGVSIGDATLDHMQRHWQAAKAAEKALPPPTRVPRAALASLRLTVGDLAAQRAFWDRVAPLLGWQAERSTAQEAVYGDGLYRLVFVAGPTTASPTLLTFEAPSEAAVRRLHTLLEDVSPGCVREGDLEPGRITFRDPSGVQWEYAVTER
>NZ_CP022163.1|WP_095980682.1|7264404_7264677_-|30S-ribosomal-protein-S20
MANTKSAEKRNRQAQKRRARNINVRTTVKDAVKNLRDTLTSDAGKAPDAFKAAASRINKAASKGVIHKRAASRRISRLAKAVNRAKAAAK
>NZ_CP022163.1|WP_095980681.1|7263840_7264392_+|hypothetical-protein
MGRMSRMRAVGWLLLLWGAGCGYRFTPRSAGLPEGVSSVCAPVFRNDTPEPGLEALFTRTLRLELVRAGVLGAQGSCDATIEGVVAGVSSAPTIVTEPVYEGNTLVAGSQLASYRASVTVGLRLMKDGAVVSETVVSGNEDFLPGTASVSGDVLEAEANRQAALHRLAETLMREGYDRLANNW
>NZ_CP022163.1|WP_095980680.1|7261256_7263755_+|leucine--tRNA-ligase
MAMNERYEPQAIESKWQNRWSEAGVFRAGSRPGAPKKYILEMLPYPSGKMHMGHVRNYLIGDVYARYFQMRGYDVLHPMGWDAFGLPAENAAIKDGVHPAVRTRENIDSFKKEIRSLGYSYDWSREVNTSEPEYYRWNQWFFIQMLEKGLVYRRFSKVNWCTGCLTVIANEQVKDGVCERCESQVLDKEMPEWAFRITRYSQALLDGLDELKEWPERITSMQRNWIGRSEGVEADFSIQGTEERLRVFTTRVDTLFGCTYVVLAPDHKLVSRITTPAQRAEVDAFVKKMAAISKTDRTDEGATKEGVFTGAHALNPFTGQPVPIWIANFVLSDYGTGAVMSVPAHDARDFDFARKYALPIRVVVQPEKGDTLPEGSALEAAFTEDGVLVDSGEYTGLSSAEARQKMGAKLQAEGRGEPKVTYRQKDWGFSRQRYWGTPIPIVYCEKCDPERKGQPVPLEQLPVRLPEIDTQAVLTGKGEPPLAKVPSFVNTTCPTCAGPARRETETMDTFVDSCWYFARYLSPRYAEAPFDPKEAQRWLPVDVYVGGPEHAVMHLLYFRFWTRVMKLLGLSPVDEPVTRLVTQGIVNGPDGRKMSKRWGNVVAPSSIVEKYGADTARAYVMFAGPPERDFDWSDDQVEGAFRFLKRVWVLAYQHQGTAGTTHEGAFEGKALEIRRAAHKCLKRVGEAIERLSFNTAIAGCMEYVNALYALGTPETSAEKAAMAEAVKVLTVVLTPFAPHLSDEIAEAYGAKDFVVTQGWPAFDPALVVDDVIPYAVQVNGKLRAEVKVAADAGEADVRAAAEADERVKAAMAGKTLRKFVFVPKRLVNFVVG
>NZ_CP022163.1|WP_095980679.1|7260778_7261162_+|response-regulator
MTRQIRALVVDDSQAMRRSLMYALQRLGTWLHTDEAQDGAEGLKKLTLGRYDLVLTDINMPLMDGLKLIRHIRQTEAYRSVPIVVITTESATEDRARAMALGASAYLVKPVQSKVVQDTVKGLLRLE
>NZ_CP022163.1|WP_095980678.1|7259837_7260638_-|Fpg/Nei-family-DNA-glycosylase
MPEGNIIHRLARVHRRWLIGRPFTADSPQGRFTAEARRLSGRVLQGVDAHGKHLFHHFEGGIRLHVHLGLVGNIRHFRASAPLPSPACRLRLASPHATLHLSGPQACELLTPDAETALRARLGEDPLRPEASPARAFEALRRARAPLATVLLDQARISGVGNILRAEALFLARLPPQRPACELRSADFERLWDALRQLMEDAARDGRIVTPQAPPTALCIPGKRREDRFCVYDREGLPCPRCATPITRVTLAGRGLFFCPRCQAPR
>NZ_CP022163.1|WP_095980677.1|7259348_7259828_+|cupin-domain-containing-protein
MIDELVRTLGLLPHPEGGFYRETWRSSSRVETPRGTRALDTAIYYLLPRGSFAAWHRVTSNELWHFYDGQALTLYLLDESTRQLETVRLGRDVTRGERPQVLIPAGILQAARPEGDYTLCGCTVSPGFDFADWEMPRGEDLAVRHPEHAALLRQLAHPG
>NZ_CP022163.1|WP_095980676.1|7258510_7259317_+|hypothetical-protein
MKTFPSEFADLLTPKGRRILEGRDNDACGKLLKPGHRFVALSGVLDARKAAACRDELDRALESTLTLMEDPIPPESIFGMTENYEELLPKTVRVRTALLESRRSRSWAAAERVGLVEMMRSDSFAAFAAAVSGRPLRRKWGIQVLCYGPGDYAGPHNDHHPEDAEAANGYVDMHLTFATRAVAHQWLIYSKQGHFSQMRSVNTLGGITLYRLPFWHYTTPLMAKPGAEADARRWVLLGTFLDAPEQRRRNTAIEPPPVSAASVLLHKR
>NZ_CP022163.1|WP_095983092.1|7257474_7258509_+|chemotaxis-response-regulator-protein-glutamate-methylesterase
MSILAPVKVLVVDDSESNRRLLTELLESAPDLRVVSTAADGNEGLRQVMALHPDVVTLDLEMPRLGGYSFLRLLKSTAPTPVIVISSYAHQADVFKALELGAIDFIAKPSRPTPEAVEKLRRELQDKVRAARQLRPDRAPPPPRRPRGLPLEPSFVVGVGASTGGPPAVQRLMEALSAEPSVSMLVCQHMPRQFTRAFAERLDRLGPFTVREAQEGDVLQPGHVFIAPGGRQLVVYRQGGQYTLGTPPPTMQDKHAPSVDRLFMSLAEVFGARSVGVVLTGMGSDGAQGARSIHKAGGEVWAESERTAVVYGMPQEAVATGAVSRVLPLGEIGPALVELARKRR
>NZ_CP022163.1|WP_095980675.1|7256638_7257478_+|protein-glutamate-O-methyltransferase-CheR
MNVEEFRLLRDFVYAYCGILVRDDMKYVMQRRLWPRLEALGLTDFGSYYRYLRFDAQRRPELETAIEALTTHETYFFREPRQLKAFSDEVLPVLERRNARTRRLRVWSAGCSSGEEAYTLAMLLKESGRFEGWDVEVHGSDISRRVLAVARQGEYGPSALRATSADQLSRYFVQLGPNRVRVRDDIRALVSFGHHNLQEPEQGSCSSRMDAVFCRNVLIYFDTPARQRVLRLIYEKLTPGGYLMLGHSENLINLSADFELVHLRGDLVYRRPELGGWSP
>NZ_CP022163.1|WP_095980685.1|7268271_7269465_+|DUF4388-domain-containing-protein
MALTGTLKDFGIADILQLIGQQQKTGVLYLKNKDQDVQVFIRDGNIVRAESVTRQKKQLLGNMLVSAELITQQQLDSALEIQKRTLKRLGDVLIATGVITQEKLRQMMRLQVTESLYGLFSWKAGNYEFKQEESVQVDADDLTPLRAESVLMEGFRMVDEWPHLRKKLSNEATTFEKVKELPPPKAQPKEDDFDAAFDDAFSEEKKDENKGEFQSIGSSERRVHALIAPGRDVNKLVDISCLGEFETWKALVNLLNLEYIRAIPPSGLSLSAASGGGAGLIFRVGGMVARAAVTFVVIAALGFVASRLRPGSWDLQGTSASSYSDPAAQRLVSRAQQARIQAALEVFRLEKGNLPERLDSLVEVGLLHHEDLRYPWRDDYYYRRTSDRQFILLPPLR
>NZ_CP022163.1|WP_095980686.1|7269561_7270632_+|PhoH-family-protein
MRNPATVEAQAVSPTSAKVDVRDNATTLALCGNQNENLKLMERRLGVRVGQRGTELHLSGPADAVAFTVKLVENLEGIIRAGRPVYREDVEQAIKVLGRGGVESLQDVMLGPVLKSSTNKQIAPKSIAQKRYVDAIRANDIVFGIGPAGTGKTYLAMAMAVSFLQDRKVKRIVLARPAVEAGEKLGFLPGDLAEKVNPYLRPLYDALHDMMPVERANHFIEQGVVEVAPLAFMRGRTLNDSFVILDEAQNTTVEQMKMFLTRLGYNSKAVITGDVTQVDLPTGKTSGLHHARSILRNIEGINISEFSDVDVVRHPLVQEVIRAYDRFDAAQQAAKALRDAEASHPPEASEESPIAD
>NZ_CP022163.1|WP_095980687.1|7270736_7273232_+|HDIG-domain-containing-protein
MAEPESSHPGPSQLDALSRRFRLGPHWGRRLASALLLLGVSVAAGFVISPGLYSQQIPALSDENLGKPFRTSSPAGFKAGRDYDILHETMTEKRRQDARSAVRPVFDLSPGVVAELRTAINGAFSAMRVRLEEKARAEEAAEAETPEPRKPVRKPAPTAEDRERQRRELESMRESFQALLFGRRDSPIDVEDFQALDAGKFSESMEAATLALVERAYGFSDPLPVYIANSREELSREGAQGITVRDLRHNGEQTLPGTAPTVVDVREAHTELERFASVPGNLLPDAPVVQRRAVLRLAKRLVRPNLTINKAETNARRAHAAAAVKDALISIKKGQRVIGDGELVNETHLVAVRGMRAQTDRLDLVQLQVGGTGLVALLITATYVFCRAAFRRFRPTRKDALLLGLLLVGMLGMAQVWVSIADAVQDRYTALPLEAFYYAFPVAAGAMLVRFVLSEELALFFAIVLACLSGVMLGNSLSFGIYALVGALVAADRITRAKDRVGIFRAGLITGVANLVAVLCLFLAEGKGLTVDTLMTAVFAFVGTALSVPVLVLALTPLIESVFGYASDLKLLELANLNHPALKELIVQAPGTYHHSIIIGTLVENAAEAIGANPLLARSCAYYHDIGKGRNPLYFSENQKGENRHDTLVPAMSAVIIKRHVTEGLEMARQYRLPKLVADAIPQHHGTRLVGYFFHKAVKEQEGKEGAPPIDESIYRYPGPKPQFREAALVMIADAVEASTRSLPDPTSPRLQAQVQKMINLIFSEGQLDECDLTLRDLNLIAQSFLHTLEGIYHARPAYPAGALQAGPKGALMVAPAAKQDSKPRPVGTGT
>NZ_CP022163.1|WP_179956319.1|7273248_7274103_+|rRNA-maturation-RNase-YbeY
MANVRLRKGKVIPRDDGKRIEEFVGAASTGTDGVSVARMLAPPGWREPAQTPEFDEVVIVLKGQLTLVVDGRRQLIEEGEMGLVPRGRRVVYRNDGQGACDYYSVCAPAFRVERAHVEDEEEAPQENRVTVQVAHPQGKRFARQVTDLAESFLEKLDLTGCELSISLVGDHAIRRLNRTWRKKDKATDVLSFPAGDAPKGTPGPRQLGDVVISLDTAKLQAREYERTLESEVARYLAHGLLHLLGHDHERPKDAQKMARAEERLLGASGMVGDAVAPRARKLMT
>NZ_CP022163.1|WP_095980688.1|7274224_7275535_+|DUF4105-domain-containing-protein
MPRLTPLMLCLLGLLLVASPGYAQDTPPWGTGESKGEDLTISLVTFGPGDDVPSWFGHGALVVEDARLRTSRLYNYGMFSFDERMLMRYAMGRLEFWVDDTRPGPTFRFYRALNRDVRLQVLNLSPAQKVELGRLLAVNVLPENREYLYHHYNDNCVTRLRDAIDKVVGGQLHQAESVPGRMTLRDHTRRYTDVGPPMSVLLDFLMNDEIDKPVTRLQEAFLPDELERQVAELQVVGEDGQERPLVEKTVTLFKAQGRPVTPEQPPRYAPVMLLMGLVLGGSAAGLAGWERRKGARLPRVLLGLQNVLVGLVFGIPGLALFIMWLGTDHTVTYRNENLFLANPLTVLALPLGIQLMRGSPRARARMWHLWRALAALGVLGLVLKVLPMFDQDNWRLIALLLPISVGMAGAMWLMRAPAAGRVPAPSVTSELKVSGS
>NZ_CP022163.1|WP_179956320.1|7276772_7277396_+|sigma-70-family-RNA-polymerase-sigma-factor
MPRGRSPVSAGEGLGREAEETPERVLLARLRRGEPDAFEELVLAHQDRLYDFCVRMLGDREEAYDLVQDVFVSAHQNLARFREDAKLSTWLYRIGKNHCINRLKYLKRRGRGRSEEYGERSEGALADALGSPPGPDAALESAREQARVQWAISQLEPDARMLVALRDIEGLAYEEIVDITELPLGTVKSRLHRAREKLADLLGRVEE
>NZ_CP022163.1|WP_095980691.1|7277422_7277776_+|zf-HC2-domain-containing-protein
MSAQLSHRETRALFIAFADEDLPADKAREVRSHLDGCGECQRGWQHYSTTVQRLKGVERHKAPPALASQVMARVKRQRRSSLRRLTQMHAHYRLPVEIIIPVLLAAAVAAYLLMSAS
>NZ_CP022163.1|WP_095980692.1|7277854_7279399_+|lysine--tRNA-ligase
MADTPENKNAEADLGSKEQEIYAQRLDKAQKWRDSGVNPYGNGHRPEHLAQVILDRHANQTAEELEKAGPVSYSVAGRIVAVRSFGKAAFVKLRDRSGEIQAHVKKDVLGDAYELFKLCDLGDFVAVEGTIFRSKTGELTLAASRFLPLTKSLRPLPEKWHGLTDVEIRYRQRYLDLVSNPEVKQTFLKRNKLIRYIRDFLDTRDFVEVETPMMHPLVSGAAARPFITHHNTLDIDLYMRIAPELYLKRLVVGGIERVYEINRNFRNEGFSTRHNPEFTMLEFYQAYATFEDLMDLTEEMLSGAAKAVTGDTKVAYQGQVLDFGKGWKRIPMTEAIREAVPSLSDKDMADADRLRHELLGKTHGQAERKAIETMHHGELVGALFEQHVESTLVHPTFITQYPTAVSPLARRNDQNPDFTDRFELFVAGREIGNAFSELNDPLDQKERFLGQLDAKKRGQQETMDYDEDYIRALEHGMPPTAGEGIGIDRVTMLFTDAPSIRDVILFPLLKPLAK
>NZ_CP022163.1|WP_095980693.1|7279412_7281779_+|ABC-transporter-permease
MNAERQTVYRWSLIWSGALVALVGAILLGVAVTQADAWVRVASVFGLSTLGWGGLVQTLNAVGLASVQSAVPSSVRVPGTEYLWLGAAAWLVGWVILASGIRRAPAPSEGPSAAAGAVLYPRLAQYRDFYWSTLGAYGGGMLLSELVLILLQTFLSSGGGSAGAERGGLAPTIAFAVSLVVASFVAFACGFVGASRARRLAMPEATIGVIYLGLPVPVGLTLMEQLPDLQVSLGYRLREVTYVADMLGRPVVGYWLVFSLLVLMLVLGINTGFIAAGSGRVDMKLGFELFVARRHVGVFRPSLLLGTLAVLLFGIVPPLIVYGIIRAVEAAVERTRIRALGLQDPLAAAAALNRLKLREQSPTMMMTALSVGGVGVGVMALIIVLSVMSGFEEDLQNKILGAHSHVVVSKYAGRLTDYKRVMQQIAKVPGVVGQTPSIDNPVMVLADDEVQGIVLKGIDPETVGSVLDLRMNMLPGGSLDNLETPEKIAPRRSLGLGSKPQTEEEPDEEFDPIIGKPTQSAEQKVLPGIVLGRELATILRVVVGDRVNVISPQGAELGPAGLIPKSRAYRVAGIFYSGMYEYDAKFAYILLGEAQKLFNSDGPTGIELKVADVDDARRISTQVSRELGGYPYRSRDWGEIHRNIFSALRLEKLVMGIILSIIIIVAAGLIVATVIMLVLEKRKEIAVLKALGVSDGGIVKIFLAEGLQIGVAGGLLGLFSGLSWCYFILKVGIKLDPSVYYIPNLPVKIEPVQTALAVVIAVLVTYLASIYPALKASSVEPVEGLKAE
>NZ_CP022163.1|WP_095980694.1|7281784_7282459_+|ABC-transporter-ATP-binding-protein
MALLSIRNVFKSYFLHGKRIDVLRGVSLDIEKGEMVSMIGASGAGKSTFLHVLGTLDMPAAGELFFEDRNVFAMNDAEIADFRNRTIGFVFQSHYLLPEFTALENVAMPALVQRRERAPSYAYARELLERVGLGARVDHRPGELSGGEAQRVALARALVLKPPVLLADEPTGNLDPVTGEGIHQLLREVNRDLGITCVVVTHNATLAESMPRRLRLNAGQVTEA

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Crispr_ID: NZ_CP022163_12

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP022163_12

7452560-7452683

Orphan

Consensus_repeat	Method
ACTTGCTCGGCATGGACCAGGGTGGGGTCACTTGC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP022163_12

>merge|NZ_CP022163|12|7452560-7452683|CRISPRCasFinder
ACTTGCTCGGCATGGACCAGGGTGGGGTCACTTGCTTGGCACGGACCAGGGTGGGGTCACTTGCCGGGAGCGAGGTTCACGGTGGGGTCACTTGCTCGGCACGGACCAGGGTGGGGTCACTTGC

>NZ_CP022163|12|10|7452560-7452683|CRISPRCasFinder
ACTTGCTCGGCATGGACCAGGGTGGGGTCACTTGC	TTGGCACGGACCAGGGTGGGGTCACTTGCCGGGAGCGAGGTTCACGGTGGGGTC
ACTTGCTCGGCACGGACCAGGGTGGGGTCACTTGC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP022163.1\|WP_157823773.1\|7458211_7460248_+\|serine/threonine-protein-kinase	unknown	unknown	gnl\|CDD\|270916
NZ_CP022163.1\|WP_095980819.1\|7447243_7448794_-\|Glu/Leu/Phe/Val-dehydrogenase	unknown	unknown	gnl\|CDD\|223411
NZ_CP022163.1\|WP_095980817.1\|7445979_7446621_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095983108.1\|7443519_7443765_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|237432
NZ_CP022163.1\|WP_095980825.1\|7456134_7457295_+\|serine/threonine-protein-kinase	unknown	unknown	gnl\|CDD\|270916
NZ_CP022163.1\|WP_095980821.1\|7450309_7450909_-\|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|378935
NZ_CP022163.1\|WP_095980826.1\|7457315_7457723_+\|helix-turn-helix-transcriptional-regulator	unknown	unknown	gnl\|CDD\|238045
NZ_CP022163.1\|WP_157823772.1\|7453176_7454250_-\|toll/interleukin-1-receptor-domain-containing-protein	unknown	unknown	gnl\|CDD\|379328
NZ_CP022163.1\|WP_043391324.1\|7457742_7458114_-\|helix-turn-helix-transcriptional-regulator	unknown	unknown	gnl\|CDD\|238045
NZ_CP022163.1\|WP_095980824.1\|7454538_7455744_-\|serine/threonine-protein-kinase	unknown	unknown	gnl\|CDD\|270916
NZ_CP022163.1\|WP_095980818.1\|7446799_7447162_+\|PilZ-domain-containing-protein	unknown	unknown	gnl\|CDD\|377796
NZ_CP022163.1\|WP_170115622.1\|7460352_7461285_+\|DUF2381-family-protein	unknown	unknown	gnl\|CDD\|131321
NZ_CP022163.1\|WP_095980829.1\|7461353_7461608_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095980815.1\|7443828_7444419_+\|nucleotide-exchange-factor-GrpE	unknown	unknown	gnl\|CDD\|366423
NZ_CP022163.1\|WP_095980822.1\|7451195_7452260_-\|AAA-family-ATPase	unknown	unknown	gnl\|CDD\|316042
NZ_CP022163.1\|WP_095980816.1\|7444527_7445964_+\|trypsin-like-peptidase-domain-containing-protein	unknown	unknown	gnl\|CDD\|273938
NZ_CP022163.1\|WP_157823771.1\|7449343_7450309_+\|tyrosine-type-recombinase/integrase	unknown	unknown	gnl\|CDD\|334163
NZ_CP022163.1\|WP_157823774.1\|7461658_7462399_-\|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|378935
NZ_CP022163.1\|WP_095980814.1\|7441311_7443387_+\|ATP-dependent-zinc-metalloprotease-FtsH	unknown	unknown	gnl\|CDD\|273520
NZ_CP022163.1\|WP_157823775.1\|7463066_7464218_+\|hypothetical-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_CP022163.1\|WP_157823773.1\|7458211_7460248_+\|serine/threonine-protein-kinase	gnl\|CDD\|270916	cd14014, STKc_PknB_like, Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.	3.27128e-64
NZ_CP022163.1\|WP_095980819.1\|7447243_7448794_-\|Glu/Leu/Phe/Val-dehydrogenase	gnl\|CDD\|223411	COG0334, GdhA, Glutamate dehydrogenase/leucine dehydrogenase [Amino acid transport and metabolism].	2.30705e-139
NZ_CP022163.1\|WP_095983108.1\|7443519_7443765_+\|hypothetical-protein	gnl\|CDD\|237432	PRK13572, PRK13572, anthranilate synthase component I; Provisional.	0.0075116
NZ_CP022163.1\|WP_095980825.1\|7456134_7457295_+\|serine/threonine-protein-kinase	gnl\|CDD\|270916	cd14014, STKc_PknB_like, Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.	1.09973e-39
NZ_CP022163.1\|WP_095980821.1\|7450309_7450909_-\|helix-turn-helix-domain-containing-protein	gnl\|CDD\|378935	pfam12728, HTH_17, Helix-turn-helix domain. This domain is a DNA-binding helix-turn-helix domain.	6.5524e-06
NZ_CP022163.1\|WP_095980826.1\|7457315_7457723_+\|helix-turn-helix-transcriptional-regulator	gnl\|CDD\|238045	cd00093, HTH_XRE, Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the xenobiotic response element family of transcriptional regulators.	3.92074e-08
NZ_CP022163.1\|WP_157823772.1\|7453176_7454250_-\|toll/interleukin-1-receptor-domain-containing-protein	gnl\|CDD\|379328	pfam13676, TIR_2, TIR domain. This is a family of bacterial Toll-like receptors.	3.13644e-14
NZ_CP022163.1\|WP_043391324.1\|7457742_7458114_-\|helix-turn-helix-transcriptional-regulator	gnl\|CDD\|238045	cd00093, HTH_XRE, Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the xenobiotic response element family of transcriptional regulators.	2.17144e-12
NZ_CP022163.1\|WP_095980824.1\|7454538_7455744_-\|serine/threonine-protein-kinase	gnl\|CDD\|270916	cd14014, STKc_PknB_like, Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.	1.8685e-81
NZ_CP022163.1\|WP_095980818.1\|7446799_7447162_+\|PilZ-domain-containing-protein	gnl\|CDD\|377796	pfam07238, PilZ, PilZ domain. PilZ is a c-di-GMP binding domain which is found C terminal to pfam07317. Proteins which contain PilZ are known to interact with the flagellar switch-complex proteins FliG and FliM. This interaction results in a reduction of torque generation and induces CCW motor bias. This domain forms a beta barrel structure.	1.8628e-05
NZ_CP022163.1\|WP_170115622.1\|7460352_7461285_+\|DUF2381-family-protein	gnl\|CDD\|131321	TIGR02268, TIGR02268, Myxococcus xanthus paralogous family TIGR02268. This family consists of at least 8 paralogs in Myxococcus xanthus, a member of the Deltaproteobacteria. The function is unknown.	1.94033e-64
NZ_CP022163.1\|WP_095980815.1\|7443828_7444419_+\|nucleotide-exchange-factor-GrpE	gnl\|CDD\|366423	pfam01025, GrpE, GrpE.	1.60243e-29
NZ_CP022163.1\|WP_095980822.1\|7451195_7452260_-\|AAA-family-ATPase	gnl\|CDD\|316042	pfam13481, AAA_25, AAA domain. This AAA domain is found in a wide variety of presumed DNA repair proteins.	1.18774e-25
NZ_CP022163.1\|WP_095980816.1\|7444527_7445964_+\|trypsin-like-peptidase-domain-containing-protein	gnl\|CDD\|273938	TIGR02037, Probable_periplasmic_serine_protease_do/HhoA-like, periplasmic serine protease, Do/DeqQ family. This family consists of a set proteins various designated DegP, heat shock protein HtrA, and protease DO. The ortholog in Pseudomonas aeruginosa is designated MucD and is found in an operon that controls mucoid phenotype. This family also includes the DegQ (HhoA) paralog in E. coli which can rescue a DegP mutant, but not the smaller DegS paralog, which cannot. Members of this family are located in the periplasm and have separable functions as both protease and chaperone. Members have a trypsin domain and two copies of a PDZ domain. This protein protects bacteria from thermal and other stresses and may be important for the survival of bacterial pathogens.// The chaperone function is dominant at low temperatures, whereas the proteolytic activity is turned on at elevated temperatures. [Protein fate, Protein folding and stabilization, Protein fate, Degradation of proteins, peptides, and glycopeptides].	1.41832e-135
NZ_CP022163.1\|WP_157823771.1\|7449343_7450309_+\|tyrosine-type-recombinase/integrase	gnl\|CDD\|334163	pfam00589, Phage_integrase, Phage integrase family. Members of this family cleave DNA substrates by a series of staggered cuts, during which the protein becomes covalently linked to the DNA through a catalytic tyrosine residue at the carboxy end of the alignment. The catalytic site residues in CRE recombinase are Arg-173, His-289, Arg-292 and Tyr-324.	1.54703e-10
NZ_CP022163.1\|WP_157823774.1\|7461658_7462399_-\|helix-turn-helix-domain-containing-protein	gnl\|CDD\|378935	pfam12728, HTH_17, Helix-turn-helix domain. This domain is a DNA-binding helix-turn-helix domain.	0.00103551
NZ_CP022163.1\|WP_095980814.1\|7441311_7443387_+\|ATP-dependent-zinc-metalloprotease-FtsH	gnl\|CDD\|273520	TIGR01241, ATP-dependent_zinc_metalloprotease_FtsH, ATP-dependent metalloprotease FtsH. HflB(FtsH) is a pleiotropic protein required for correct cell division in bacteria. It has ATP-dependent zinc metalloprotease activity. It was formerly designated cell division protein FtsH. [Cellular processes, Cell division, Protein fate, Degradation of proteins, peptides, and glycopeptides].	0

>NZ_CP022163.1|WP_095980822.1|7451195_7452260_-|AAA-family-ATPase
MLYPSTRHEGTETDCHCPQAVPIKKFIEEAGDPPEPVVDGLLTPGIAVLIGAPGCGKTHLANELARAVGRGESAFDRFRTKKGAVLIIEEEHHEGDLSERYERAGMEDAEIFILHAENARLDVPSWVDWIAREVERTHSILCILDPFADLHEKDESSNTEMKEVTNGLKELKQRCPGTAFLVIHHPTKGASKEGVEPEMSDGRGAGRLMGMADAVYSMACKDRSPQALKISFRCRKRRDGPAIEPQTLSLKFTEQGAAWAVDAAPSEEPDTKLRERIEKKLREARERGQLFPNRTALKSAVGGNSTQTGKVIGQMIDAKRIIEDKKKKVIDLADDAPAGLAAKDGPAANNDQEQ
>NZ_CP022163.1|WP_095980821.1|7450309_7450909_-|helix-turn-helix-domain-containing-protein
MKQRSWVCWACYYDDFGENVSPYAVGYFDPRSLDERCSCCGAGPTLQDQFKLHLLARRDAIEELLREPEDTPEGMLTLATFAGMKVAGELSRDAVPPMKRKQQRKSTSHLLSMREAARRFGIDRNTTLREMIDAGHIRAVPFRGGLRIPASEVDRVCAEGLTPLRRPQRQRITPPPIRTPRVRRSEGESIGEKIRGLKI
>NZ_CP022163.1|WP_157823771.1|7449343_7450309_+|tyrosine-type-recombinase/integrase
MYVIRRQLHGKRYVVSTRAHSLRAALQHLARFEADPEGYRPSGEPHEAPIYLDEALALEFLTWSRDVQKNTPKWVGEQRLYLGWWGDRLARVDLRRASLRDHILPALQGATARGPRIAVLKRLYSYLRKVKHVLSSEEDPTQELMVPQARPEQWTRVKAIPREDFLRVRDHLTGSWRDGMDVLAGTGWHVTELVRFVRAGVIELLPESLEGVAGVLICPRTKGGELLRTPVSSAVMEAAERLRERGTFSAQKFAMAIKAACRAAGVEEFGPGQFRHSVATWAVNKGASLAAVADFLNHKSPRTTAKFYAVHATPTKVPTLL
>NZ_CP022163.1|WP_095980819.1|7447243_7448794_-|Glu/Leu/Phe/Val-dehydrogenase
MANEENFMRVPAPTPKRTVYTEAMEIFHRAADLIGLDKRVRLELEEPDYEHIFYVTAKLKDRLVPLTPEQARDFSDLQPTQVRNPEGLERLADGKIILNGRALLGSDVSIRRGHLRLPDGHVYQLVPGESQRFKAYRVQHNQARGPYKGGIRYHREVSLDLFKALAAEMTWKTAISEVPFGGGKGGIQIDPRAYGREELENITLRFMYKLKSMIGPNIDIPAPDVGTNGDIMALMYRQYSDGERDRHGMRGIVTGKDVRIGGSEGRAAATGQGVAFCIEDYYAEKGENLRGKSFILQGFGNVGSHGAAILQRMGARLLAVNDADGTIYNGDGIDVTALLAHVNDPKNLRRSVLGFAGAQKIDKKDFWEVQADICLPAALGGEITADVAERLKVKLVAEGANGPTTPEADRVLQKRGIDMIPDIIANAGGVTVSYYEWIQNKRMERWSEPEVNQRLEHAMKRNYRIIRDISRNQSRRSDTHDSRPFCIGKEVDPRCAAMILALKRIEAHYLLEGFSQ
>NZ_CP022163.1|WP_095980818.1|7446799_7447162_+|PilZ-domain-containing-protein
MAQVQVRERRAHLRFDKVFTIYLSTQGGLSRGIGRNISQQGLFVETRESMSLGERVKVTFAGEDGTEMTCLCEVRYQVALSYGRKDGREGNSRGVGLRIVAYEVQEDAPLLLVARERVMH
>NZ_CP022163.1|WP_095980817.1|7445979_7446621_-|hypothetical-protein
MRRLILAALLLPTLALADVDSRFAQLRDQAEALGSLGTFLDKYIGECSSFFSGLGCRGAAEEFRKQYEGKKLYMIVGESAASMVQPGPYQPGSGNYTILVTPSFPGGSYHLTQGAPSQLGSEDQPLVPPVRVTGTTPVGWNATDFMRLFSNHQVRLQIVFSPEGIWGLERNQGRGKLYGVSCRVEGVLLSNARTGKPLGMWLADEPADKAPRK
>NZ_CP022163.1|WP_095980816.1|7444527_7445964_+|trypsin-like-peptidase-domain-containing-protein
MAPVLNSPVFRPWVRLAGLFVWLLAPAVWAEPDSLDAWLTARAREHAAWTEDSARSSGGAPGLWREWTSKEPMLPGFVPPSSLAPLIRAVEAGVVNISVTGEVGRGGTRSASGSGFLLTPEGLVVTNNHVVARGSEVASEIVVRLSDGREFQAEVVGRDASTDVALLRLLGREVRGLPAVYLGDSDQLEVGDWVVAIGNPFGLDHSVSHGMISAKERVIGVGPFDDFIQTDALINPGNSGGPLFNMRGEVVGVNTAIISEGQGIGFAVPSNMVKDLLPNLSKNGQLQRGWLGVVVDEQAQAGTRAAVVTHVYPHSPAEQAGLLPGDLLVGVNGKPVDSFPQLLRKVAMLVPETQVTLSLVREGTAREVRVKLTARPVQEGLSASGNLGEFGLVLRDITPVVGATLGLEPYAGVLVSGVVPRSPAAREGLRAGDVVIEVNRSRVRELRAVKAALEKSTGRTLLLRVQRGDVQQYVALEP
>NZ_CP022163.1|WP_095980815.1|7443828_7444419_+|nucleotide-exchange-factor-GrpE
MNGNPRTDEPIQEAQEARPQDDVISPEAPAAASAAEVARLTAELEAARRRVDQLARAYQELEKDREEFKQRLSRERERMLDVERGKVATQLLEAVDELDLCLSMSAPDESSGLAKGVKLIRDGLLSKLQQSGVERLQLVGQPYDPNTAEATDMEITPNPEEDQRVVAEARAGYRFKDRIIRPARVKVARYIPPASA
>NZ_CP022163.1|WP_095983108.1|7443519_7443765_+|hypothetical-protein
MENRIGKSYTARKSLFAKGLRDGRLTVQEIEEALPAGTLTAAERWLLYYSLRAAQVEIIDEVTGQVDHGFMTEPPSVPAEH
>NZ_CP022163.1|WP_095980814.1|7441311_7443387_+|ATP-dependent-zinc-metalloprotease-FtsH
MKPQNTPPSGEGPRAKKQDKTPPPPAKGFRFGSPLAYIFLLVLGFILFRNVFQDAGVQRVSYSRFRDAVTEGRFNRVQVAPDWVKGYLKEGSAPAQGTDGPPSTGTGAAGPLRSEPGALPWMAYRVQGDTDLVPLLEQEGVQYEAVPQSNFSDVLWIWLVPLALAFVFWSFMMRRMAGGIGQGPQSVMSFGKTRAKVQAEADTGVGFKDVAGVDEAVDELREIVEFLKTPEKFRRLGGRIPKGVLLVGPPGTGKTLLARAVAGEAGVPFFSLSGSEFVEMFVGVGAARVRDLFAQATAKAPCIIFIDELDAIGKSRNAGVAGGHDEREQTLNQLLAEMDGFDSRAGLIIIAATNRPEILDSALMRPGRFDRQVLVDRPDKRGRERVLEIHSKGVKLGPDVDIKSIAARTPGFAGADLANVVNEAALLAARKNRDAVLKADFEEAIERVVAGLQKKNRRMNEREKEIVAHHEAGHTVVGWMLPNAERVTKVSIIPRGLAALGYTMSLPLEDRYLMSFDELRDKMAAMMGGRAAEEIFVGEVSTGASNDLKQATDVAKMMVRDYGMSTLGPVALGADQGAGFLRSAGMPETRTYSEQTARMVDEEIRKMVTEALDRARAVLTQHRDKVEALAARLLATEVVDEDDLKVLLGPKATSSRGLLHPEARQVISAHPVSEETPPPGAQHATGTLPDA
>NZ_CP022163.1|WP_157823772.1|7453176_7454250_-|toll/interleukin-1-receptor-domain-containing-protein
MARATTKRIPNRSVFISHAASDAEFVNYFVDTLLTAGIGIGQEHIFNTSSPTSPIRAGSNFNPEIRSAIRMAKVVIAVVTPTYFDRPFAMAELGAAWASERLVPILVPPLDFNTLEGVLDGIQCIRVGDEKKLHELYDRFDADDLNKERWFNRNGSGTFNAKLREFLSGLPARLTKVSPSATAATSEGKSKAVSPTTADSQKKSAVPVKEEWATFERFLDELRTALEQLPWIVSWGFMYEACGDWGIARDQDTKDAAKDAEYRGLLRISKEFSLDPAENRWLYRPTKSSQRARNVYEIMDKLKSFLEKASRDFHLEYEQKHDHPAILSIYPFWDGHDLVGVDGEKTPQQSSESSSSE
>NZ_CP022163.1|WP_095980824.1|7454538_7455744_-|serine/threonine-protein-kinase
MAAPSLSSDISTGEIPAGYVSHFEKRGFVLEGRLGSGASGNVFRATQRSLGRTVAIKICDHPHGRQNTGIRKRFEREAQILAKLTHPSIPYVITNGQLPTTQDASIPYTVLQFIDGSNLESLLKTQHRLKPRSAVQYMAQVLSALDCAHKQQIVHRDVKPSNILVLPSGHCYLIDFSIGVALEPSPGLTRITGDGRSPATADYASPEQIAGKKVDSRTDVYSAGVVLFEMLTGHFRVKPDLLDEQLRQVPAVLRTAIRRACHPKPGERFQSADEFRQTLLRFEANPVEQAQARPTTALCVNHLCPDAQWLYGERGTQYYKGPRIIEESVASYCSKCGKDLEYPCQKCGHPFEGDQFCAVCGNEMYSIPACGRCGALLARSEIGTDTEKNGCSQCDDEGIPF
>NZ_CP022163.1|WP_095980825.1|7456134_7457295_+|serine/threonine-protein-kinase
MIGANNPPTDTGPFTFESDGFRYEVLRSLLEHVDYDTLWLARCRPLNEKVRRRLVVLKQVEVPEGREGRTRAIEEVQLAEHLHHPRIGHVLRLAEYQGSPYVVLEHTTGAFLATVIGSALLLERKLSPALAAFITAEVANALDYAHHCEDDRGRELHIIHRAVSPMTIRIGSNGRVKLTNFGAAFSELLGRVPTPPKVLRGNFAYAAPEIIRSISEKGRAGLLSPKGIDSRADIFSLGLVLLEIIAGNHPLDPLDTLPSDVSRRALRLVSGVKAEHSAWASIEVLADRLLRFGPEDVERIARQAPAPLKQVAHRALRSNPAERYQSAAEMRDDLRAYLRSLRQPFGVSEAAAELADILKKASALKRKAAHPVEIGVLPWPKALSVQ
>NZ_CP022163.1|WP_095980826.1|7457315_7457723_+|helix-turn-helix-transcriptional-regulator
MTSRQNEKKKLVVHLAAAVREARKKAELTQADVADRVGLVTEVFGRLERGHLLPSVTTFRRLCRVLRLDANVVLGLDAVKAPLLEVPETEADDPPELRRLVRTLRRMDAAQLAVVSSTANAVMRHTAQHPDDQAE
>NZ_CP022163.1|WP_043391324.1|7457742_7458114_-|helix-turn-helix-transcriptional-regulator
MDEELQRSLGEVARAARERLGLTQAQVAQKVGLVPGVYGRIERGDMMPSVPSLRRISIVLGISSDALMGVSPSQVAATVDEAPPDGSLSPELRRIVHQLRTWSPKRLKVLSKVLTVLASSFED
>NZ_CP022163.1|WP_157823773.1|7458211_7460248_+|serine/threonine-protein-kinase
MGLVYRLPEIGEMVGGYRIVEKLGSGSYGYVYKAEQAGCFYAVKILRGRLLNDRAKREIGILNHMDHPDVVRFFGCGYWPDPFVGHPYIVMEFAGGRTLETYASEENPSARRSARIVLDIGLTLGEVLRQGVMHRDLKPDNVIIRDGNARPLLIDFGVSTLTGLPAPTSSRLPPGTIEFRAPEAWRFSRENDSGSYDYSPADELWALGVSFYWLLTDILPFGDREDEEEGGLAERILHQSPVAPHVLNPRVPRALSDICMRMLEKDPAARYESVVEFCAALDAAMANAEADASWDLPLFEPDSPHTRTTEEDPSLVDVDDSKRWLRRWLKKEHQRGRKPPKKVPALAPQAMEKAGEAPAPEAEVVAVVPEQQAPVAAAVPVSEMAPPEPVPPPASQAPAPFEAPRAAAAPTRPVSRRRSRFAAAVGFAVVALGAFLFATSLPTGSGSAPLHTSSEAAPTQQAGPGREVAQPAKPLDPPSGEGAEPAMGSISAPVMITMLRKDDSSEKLQEKKTKVLGRAGKALGSAALCTALSGCPAPQVRPTPEPAPCPAGSVEAMADKLGVRVGQSVSAYLNLEGSAQVITVHEGSASAQLGPRRVGESGGRIFLSGTLTIGEGRVYGRFTEARDLLGDGQPFPVCFEMSDGLKGGRGAIIREGGGGPGSARIYSTVDVWAVRSFD
>NZ_CP022163.1|WP_170115622.1|7460352_7461285_+|DUF2381-family-protein
MFASSSAALLMLLLVAGSSATAKTCPPPGETEDRCIELTADGTKEVSEVQISPGQPSTFIFDSDLRADGLTLEGRERFEVADPGKRTLTLVPSEEIRGEKPSKVTVCFADDAAPACASFRLIVHPAIGERHVRIFRHPRPVESVQADLKKSYEENARLRAENDRLRAERDRPDGLTGLFASGMMDEKGIPCSKVDFILRPKAALSAGRVITCRTPGRMLVQVELKAPDGAAPWMTQGAKLVGPKGEELEGSIWQPRPLLPGQPLTLYIEVQTEDVQTAGPFVLKLWETDGPRTVTLGNVTFPALTEGPGL
>NZ_CP022163.1|WP_095980829.1|7461353_7461608_-|hypothetical-protein
MATKKKQKPEDIVLFASLETEDDVEVEVAIHAPNRASARRVIAEITRAVTGDDPEEANAGGRIVLSEGRGLPNQARPKSEESEG
>NZ_CP022163.1|WP_157823774.1|7461658_7462399_-|helix-turn-helix-domain-containing-protein
MTAPTEGTPPAPEWLPVPEAAAAAGVPVRSLYRWIEKKRVPTRQERGTTVVDVAAVCAYAARRAALKASGARAGIADTSAVTAPTVRPVGTGDAGSDRARGIERTGASGTPPTVTRPALTTSGNATPATSDAELAAEVFTRFEEGDTPVDVVREMRIPPERVRALHREWTELRAMGGGGGPSITDRLAELESRLKELTETLPFEVMSVEVNANNAIGRLEGRLEVLERRVAGSSVPPPGFNFGPRR
>NZ_CP022163.1|WP_157823775.1|7463066_7464218_+|hypothetical-protein
MSTRLASPRIPRARLYPLLRGWFLICLFLQAACATGVPRSGPRVGASYRPPTFRFHEDARPSSAESEAEEGEAADERVRLSLPTRFGAVQVSDFELNEALATLVLNMPLRVAGSHFPLYLHRKLALASAPLSGEAWRTPLARSYGSFCERQGTPGDCLELFKDGPGLDGEDKRDLALALSVNAALEARDAELRGMFSTTQLWTALSLTIIGYLALVAAPEPVSKGVAAALAVLMWGYLGWELFDLVRAYFQLWEEAAEASTFAELREAGDRFGKVIGPNSVRILLLLGTAAVGETAALVSKAPKLPGFAKAADALKSHAGIRDVLTAVQEADKVKVAVAEGTFSVVLPANVLSMAARGAPARADPPKKKPEVHHTAMSGRARR

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Crispr_ID: NZ_CP022163_13

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP022163_13

8618207-8618284

Orphan

Consensus_repeat	Method
CCGTGGCGCACGCGCGCGTCGGAC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP022163_13

>merge|NZ_CP022163|13|8618207-8618284|CRISPRCasFinder
CCGTGGCGCACGCGCGCGTCGGACGCTCGGCCGCTCTGCTCGGACAGCCCCGGCCCGTGGAGCACGCGCGCGTCGGAC

>NZ_CP022163|13|11|8618207-8618284|CRISPRCasFinder
CCGTGGCGCACGCGCGCGTCGGAC	GCTCGGCCGCTCTGCTCGGACAGCCCCGGC
CCGTGGAGCACGCGCGCGTCGGAC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP022163.1\|WP_095981585.1\|8608006_8609353_+\|insulinase-family-protein	unknown	unknown	gnl\|CDD\|223685
NZ_CP022163.1\|WP_095981592.1\|8618744_8619143_+\|transposase	unknown	unknown	unknown
NZ_CP022163.1\|WP_095981587.1\|8610719_8611424_+\|RNA-pseudouridine-synthase	unknown	unknown	gnl\|CDD\|211346
NZ_CP022163.1\|WP_095981599.1\|8628669_8629266_-\|glutathione-S-transferase-family-protein	unknown	unknown	gnl\|CDD\|223698
NZ_CP022163.1\|WP_095981593.1\|8619532_8621050_+\|IS66-family-transposase	unknown	unknown	gnl\|CDD\|376980
NZ_CP022163.1\|WP_157823862.1\|8623481_8624855_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095981594.1\|8621226_8621859_-\|ankyrin-repeat-domain-containing-protein	unknown	unknown	gnl\|CDD\|293786
NZ_CP022163.1\|WP_095981597.1\|8626792_8627533_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_170115661.1\|8603918_8605916_-\|PAS-domain-containing-protein	unknown	unknown	gnl\|CDD\|223715
NZ_CP022163.1\|WP_157823861.1\|8621862_8622648_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|373919
NZ_CP022163.1\|WP_095981589.1\|8612743_8612968_-\|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|378935
NZ_CP022163.1\|WP_095982807.1\|8614811_8616125_+\|IS4-family-transposase	unknown	unknown	gnl\|CDD\|376573
NZ_CP022163.1\|WP_095981600.1\|8629371_8630283_+\|LysR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|176114
NZ_CP022163.1\|WP_095981591.1\|8617273_8617543_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095981588.1\|8611559_8612747_-\|site-specific-integrase	unknown	unknown	gnl\|CDD\|271189
NZ_CP022163.1\|WP_095981598.1\|8627619_8628429_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095976450.1\|8619136_8619517_+\|IS66-family-insertion-sequence-element-accessory-protein-TnpB	unknown	unknown	gnl\|CDD\|377551
NZ_CP022163.1\|WP_095981586.1\|8609355_8610723_+\|insulinase-family-protein	unknown	unknown	gnl\|CDD\|223685
NZ_CP022163.1\|WP_095981583.1\|8606026_8606560_-\|superoxide-dismutase-family-protein	unknown	unknown	gnl\|CDD\|238186
NZ_CP022163.1\|WP_095981584.1\|8606677_8607907_-\|cytochrome-P450	unknown	unknown	gnl\|CDD\|225035

Protein	Function_ID	Function_description	E-value
NZ_CP022163.1\|WP_095981585.1\|8608006_8609353_+\|insulinase-family-protein	gnl\|CDD\|223685	COG0612, PqqL, Predicted Zn-dependent peptidases [General function prediction only].	5.46255e-95
NZ_CP022163.1\|WP_095981587.1\|8610719_8611424_+\|RNA-pseudouridine-synthase	gnl\|CDD\|211346	cd02869, PseudoU_synth_RluA_like, Pseudouridine synthase, RluA family. This group is comprised of eukaryotic, bacterial and archeal proteins similar to eight site specific Escherichia coli pseudouridine synthases: RsuA, RluA, RluB, RluC, RluD, RluE, RluF and TruA. Pseudouridine synthases catalyze the isomerization of specific uridines in a n RNA molecule to pseudouridines (5-ribosyluracil, psi) requiring no cofactors. E. coli RluC for example makes psi955, 2504 and 2580 in 23S RNA. Some psi sites such as psi1917 in 23S RNA made by RluD are universally conserved. Other psi sites occur in a more restricted fashion, for example psi2819 in 21S mitochondrial ribosomal RNA made by S. cerevisiae Pus5p is only found in mitochondrial large subunit rRNAs from some other species and in gram negative bacteria. The E. coli counterpart of this psi residue is psi2580 in 23S rRNA. psi2604in 23S RNA made by RluF has only been detected in E.coli.	9.4284e-60
NZ_CP022163.1\|WP_095981599.1\|8628669_8629266_-\|glutathione-S-transferase-family-protein	gnl\|CDD\|223698	COG0625, Gst, Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones].	1.27116e-37
NZ_CP022163.1\|WP_095981593.1\|8619532_8621050_+\|IS66-family-transposase	gnl\|CDD\|376980	pfam03050, DDE_Tnp_IS66, Transposase IS66 family. Transposase proteins are necessary for efficient DNA transposition. This family includes IS66 from Agrobacterium tumefaciens.	1.68361e-79
NZ_CP022163.1\|WP_095981594.1\|8621226_8621859_-\|ankyrin-repeat-domain-containing-protein	gnl\|CDD\|293786	sd00045, ANK, ankyrin repeats. Ankyrin repeats are one of the most abundant repeat motifs, and generally function as scaffolds for protein-protein interactions in processes including cell cycle, transcriptional regulation, signal transduction, vesicular trafficking, and inflammatory response. Although predominantly found in eukaryotic proteins, they are also found in some bacterial and viral proteins. Less is known of their physiological roles in prokaryotes. Some bacterial ANK proteins play key roles in microbial pathogenesis by mimicking or manipulating host function(s). The pathogen Providencia alcalifaciens N-formyltransferase ankyrin repeats function in small molecule binding and allosteric control. Ankyrin-repeat proteins have been associated with a number of human diseases.	6.25221e-17
NZ_CP022163.1\|WP_170115661.1\|8603918_8605916_-\|PAS-domain-containing-protein	gnl\|CDD\|223715	COG0642, BaeS, Signal transduction histidine kinase [Signal transduction mechanisms].	5.35551e-42
NZ_CP022163.1\|WP_157823861.1\|8621862_8622648_-\|hypothetical-protein	gnl\|CDD\|373919	pfam15523, Ntox16, Novel toxin 16. A predicted RNase toxin found in bacterial polymorphic toxin systems. The toxin possesses an all-alpha helical fold and conserved (DNE)xxH motif and arginine residue. In bacterial polymorphic toxin systems, the toxin is exported by the type 2, type 6, or Photorhabdus virulence cassette (PVC)-type secretion system.	2.93225e-06
NZ_CP022163.1\|WP_095981589.1\|8612743_8612968_-\|helix-turn-helix-domain-containing-protein	gnl\|CDD\|378935	pfam12728, HTH_17, Helix-turn-helix domain. This domain is a DNA-binding helix-turn-helix domain.	9.92643e-10
NZ_CP022163.1\|WP_095976450.1\|8619136_8619517_+\|IS66-family-insertion-sequence-element-accessory-protein-TnpB	gnl\|CDD\|377551	pfam05717, TnpB_IS66, IS66 Orf2 like protein. This protein is found in insertion sequences related to IS66. The function of these proteins is uncertain, but they are probably essential for transposition.	6.23085e-34
NZ_CP022163.1\|WP_095981600.1\|8629371_8630283_+\|LysR-family-transcriptional-regulator	gnl\|CDD\|176114	cd08422, PBP2_CrgA_like, The C-terminal substrate binding domain of LysR-type transcriptional regulator CrgA and its related homologs, contains the type 2 periplasmic binding domain. This CD includes the substrate binding domain of LysR-type transcriptional regulator (LTTR) CrgA and its related homologs. The LTTRs are acting as both auto-repressors and activators of target promoters, controlling operons involved in a wide variety of cellular processes such as amino acid biosynthesis, CO2 fixation, antibiotic resistance, degradation of aromatic compounds, nodule formation of nitrogen-fixing bacteria, and synthesis of virulence factors, to name a few. In contrast to the tetrameric form of other LTTRs, CrgA from Neisseria meningitides assembles into an octameric ring, which can bind up to four 63-bp DNA oligonucleotides. Phylogenetic cluster analysis further showed that the CrgA-like regulators form a subclass of the LTTRs that function as octamers. The CrgA is an auto-repressor of its own gene and activates the expression of the mdaB gene which coding for an NADPH-quinone reductase and that its action is increased by MBL (alpha-methylene-gamma-butyrolactone), an inducer of NADPH-quinone oxidoreductase. The structural topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.	3.48742e-70
NZ_CP022163.1\|WP_095981588.1\|8611559_8612747_-\|site-specific-integrase	gnl\|CDD\|271189	cd01189, INT_ICEBs1_C_like, C-terminal catalytic domain of integrases from bacterial phages and conjugate transposons. This family of tyrosine based site-specific integrases is has origins in bacterial phages and conjugate transposons. One member is the integrase from Bacillus subtilis conjugative transposon ICEBs1. ICEBs1 can be excised and transfered to various recipients in response to DNA damage or high concentrations of potential mating partners. The family belongs to the superfamily of DNA breaking-rejoining enzymes, which share the same fold in their catalytic domain and the overall reaction mechanism. The catalytic domain contains six conserved active site residues. Their overall reaction mechanism involves cleavage of a single strand of a DNA duplex by nucleophilic attack of a conserved tyrosine to give a 3' phosphotyrosyl protein-DNA adduct. In the second rejoining step, a terminal 5' hydroxyl attacks the covalent adduct to release the enzyme and generate duplex DNA.	5.97803e-38
NZ_CP022163.1\|WP_095982807.1\|8614811_8616125_+\|IS4-family-transposase	gnl\|CDD\|376573	pfam01609, DDE_Tnp_1, Transposase DDE domain. Transposase proteins are necessary for efficient DNA transposition. This domain is a member of the DDE superfamily, which contain three carboxylate residues that are believed to be responsible for coordinating metal ions needed for catalysis. The catalytic activity of this enzyme involves DNA cleavage at a specific site followed by a strand transfer reaction. This family contains transposases for IS4, IS421, IS5377, IS427, IS402, IS1355, IS5, which was original isolated in bacteriophage lambda.	9.35647e-08
NZ_CP022163.1\|WP_095981586.1\|8609355_8610723_+\|insulinase-family-protein	gnl\|CDD\|223685	COG0612, PqqL, Predicted Zn-dependent peptidases [General function prediction only].	3.5101e-91
NZ_CP022163.1\|WP_095981583.1\|8606026_8606560_-\|superoxide-dismutase-family-protein	gnl\|CDD\|238186	cd00305, Cu-Zn_Superoxide_Dismutase, Copper/zinc superoxide dismutase (SOD). superoxide dismutases catalyse the conversion of superoxide radicals to molecular oxygen. Three evolutionarily distinct families of SODs are known, of which the copper/zinc-binding family is one. Defects in the human SOD1 gene causes familial amyotrophic lateral sclerosis (Lou Gehrig's disease). Cytoplasmic and periplasmic SODs exist as dimers, whereas chloroplastic and extracellular enzymes exist as tetramers. Structure supports independent functional evolution in prokaryotes (P-class) and eukaryotes (E-class) [PMID:.8176730].	4.09342e-49
NZ_CP022163.1\|WP_095981584.1\|8606677_8607907_-\|cytochrome-P450	gnl\|CDD\|225035	COG2124, CypX, Cytochrome P450 [Secondary metabolites biosynthesis, transport, and catabolism].	5.48488e-94

>NZ_CP022163.1|WP_095981591.1|8617273_8617543_+|hypothetical-protein
MHSWIKTDDLAAFYLSRFGTERLPFDMPTIAKRRGITPGSMDMRIRNFEAYVGKGGLVNIAKKSVEVFEQYKDTPEPELRNLAFPELAR
>NZ_CP022163.1|WP_095982807.1|8614811_8616125_+|IS4-family-transposase
MVRRTLEHALSSQWIDEVFEANREQQYTRELLFSSVVDLMGVVALGLRPSLHAAAQSDPDLTVSLAALYDKVNHTEPQVVRALVQGSAERLLPVVRPMKKQGPWAAGYQVRVLDGNHLPASEKRLKPLREFRGAALPGQSLVVYAPELSLVVDVLPAEDAHAQERALMGPVLERVREGELWLADRNFSTSRILRAVHEKRAAFIIREHGVSPNPTALGERREVGRGPAGRVYEQAVRVEGEEPLELRRIEVELEEPTEDGETAIRLLTNVPEEKLSAVEVAQLYRKRWTIEGMFGELEAVLESEVRSLGRPRAALLAFGVAVLAYNVLSVVKTAVEASHDLEAANMQVSTYYIAAEVKFAYGGMMMVVEPEDWSGQEVRSAEQLSELLLELAKKVKPSTLRKHPRAAKKKVKKGYVPGEVARKHVATARVLKGEKIS
>NZ_CP022163.1|WP_095981589.1|8612743_8612968_-|helix-turn-helix-domain-containing-protein
MSAPPLTASNAPAFLTVEEAAELLRVNRKTLYEAIRFDQVPGVARLGRILRIHRDTLLTWSPGNSRPALGDKKP
>NZ_CP022163.1|WP_095981588.1|8611559_8612747_-|site-specific-integrase
MSVRLRQWKTKESKVQEAWWVDVKYQHPSGRVERIRKASPINTRRGAEEYERQIRHALLTGTFGKENSAGRVPTLGEFVPRFLTYSENNNKHSSVVTKRQILDDHLIPAFGNTSLDAIGPAEIEDFKAAMRKKPSGARARKEAPTRAALLKRKGSGGVKLLSLKSINNVLTVLHKLLALAQEQGVIQHVPRVKLFKTDKPAFDFLSFEEAERLINAAEPEWRTLILVALKIGLRLGELIGLQWADLDLQRGKLHVRRTIWRGVVGLPKGGRERTVDLPASAVEVLKAHRHLRGPYVFCQPDGQPLTAGMTKHPLLRALRMAGISRPEGIIGWHDLRHTYGSHLAMRGVALKVIQELMGHATIEMTMRYAHLSPEARESAVKELDRPIPQPRAALG
>NZ_CP022163.1|WP_095981587.1|8610719_8611424_+|RNA-pseudouridine-synthase
MSGLRVLFEGAGLLAVDKPAGMLVIPGRSEDAAPSLREELEARLKRKVYVVHRLDRDTSGVVVFALTPEVHRTLSMAFESGQVHKRYLALVEGRLEARHVVDAALASGRKGRMRVARPGEEGKPSTTKFRPVEVFASASLVEAEPLTGRTHQIRVHLLSLGHPLLVDHQYGRDTPWTARELGGVGEGQVLARTPLHAARLEWPALPGVEARVLESPLPEDMASAVTLLRAGMST
>NZ_CP022163.1|WP_095981586.1|8609355_8610723_+|insulinase-family-protein
MATKRPKSVAVKAASATSGLMLPTFHESTTSSGLTVLAAQRGPLPLVAVRLAVRAGSAVDPQDKHGLADFTARLMRRGTARQSADEIDEAIEFVGASFAVGSNEDLLSFYVTTPAEHFPAMLSLLGELVREPSFPEREVELARERALAGFANDLDDPSVIADRAFTRALWGKHPYGHDVGGSTAHVRTFTREDLVRFHRERLGPKVALLSVVGAVEPGLVAEEAEKAFGAWKGGPDKPEQPPAAGKIASGRILLVDKPDQTQTQVRLGGPGFRMGHEDYFPSAAMNNVLGGGFTSRLVNEVRVERGLTYGINSYFDMLNVGGVFAISTFTQTERTREMLDVSLAEVAKVRESGISAAELKKAQRYLAGLYPLRTETNESVASVIGDIRVHGLGDDWVEKFRERLFAVKPKQTQEVAAKYLFAKAPLIVLLGKASAVKKQLKGLGSVTVVPASDYE
>NZ_CP022163.1|WP_095981585.1|8608006_8609353_+|insulinase-family-protein
MAKAQAKTAPRTADPILQSLFDVQEATLPNGLRVRLLANPQTPVVSLYTFFQVGSRNERPGITGISHLFEHMMFNGAKKYGPKKFDQVLESNGGRSNAYTSTDMTVYYEDFAADALETVLDLESDRMRSLRINDAALTSERQVVMEERRVRVDNDITGIMDEELGTLVWKAHAYRWPVIGWMKDIENITRQDCEQYFRTYYAPNNAVLYIVGDIDPKKTLALVRKYYGDIPKGPTPAPVLNAEPEQKGERRAEVRHPAQSPALMIAYRGPSAREEDTLLLDILQYVMTKGEGSRLVKKLVYDTQLAVSVGVDWGWRVDPGIILFFLELKPDSDPRKVEEALYAELALLAAEGVTERELQKAKNNLRADHLRELATNSGRAHAMGHYEALLGSWRDGLSLPSVYAAATHEQVRAVARKYFAPERRSVVTLLPSAPEAGEEVAADGKEVA
>NZ_CP022163.1|WP_095981584.1|8606677_8607907_-|cytochrome-P450
MQPQAMWSPENLRNPYPFYAALRESAPVHVLAAFGGTHAITRYDDIAPILKNPALFSSQRIAPGLHLPKEVGEQARRFFRAQNNLIASDPPQHTRLRTLVSKAFTPRRVAEMEPRIRAITRQLLESMLAHEEFDLMAELAVPLPVIVISEMLGVEPERRQDFKRWSDHVVQTVALSQGKLDPGPILQSLEQLHAYLEETIERRRREPQDDLISALVEAAEGFLEVEDLISFTRLLLVAGNETTTNLLGNALVSLLRAPSELARLQATPTLVPSAIEETLRYEGPVQSLMRMTTQDTQIAGHPIPEGTRLFLVLAAANRDPRRFKEPERFDITREDQGQLAFGHGVHFCLGAPLARLEARVALEELLPRVRQLAFASGQEHDIDWGESFLLRGPRRLRLRAERCPSPLPK
>NZ_CP022163.1|WP_095981583.1|8606026_8606560_-|superoxide-dismutase-family-protein
MTIRALLIAATLTTTPALAQTPEAGTKAPPPKGETAKAPLKDAQGKDVGEVTFEQTPTGVLVKGTLTNLPPGEHAIHIHEAGKCEAPAFTTAGGHFNPKKKAHGILSPKGKHEGDLPNLYVDKEGRVQFDFFAPDLKVKGLFDKDGSAVVVHAKLDDYHSDPAGDAGGRIACGVVEK
>NZ_CP022163.1|WP_170115661.1|8603918_8605916_-|PAS-domain-containing-protein
MSQLADVLEARQGELIKRWTDNVRHDLPHKAISCFELEDHLPALIQELARNLRSPPERDSNAASHKYQEMGRAHGAQRFGLGFDLDTLVREYDLLRGMLFDLIEENALPITLGEIRLLTDFVANSIAEAVSEYSRQKEAERDRLLQETERLRATAELGRARLSALFMQAPVAIGIFRGPELVIDVANPLICRLWGRTLEQVLGKPLMDAMPELQGQGFDEILYEVIRTGVPFVGTEIPVRLIRTAGRLPENVYFNFVYEPLRDEAGVTEGIIVVATEVTQVVLDRRRMEALLHRSHEAERARTALLDALSAQSLIAVAYQRGPEHVFEMANPLYHQWMGGRELVGKTLQQALPELVGQDFDILLRHVYQTGQPFVGQERVVRLDRRGDGVLSEMRVNLTYQPVRTVDGVIEGVIVLALDVTEAVRARWEAQRLAEEESARRGFEQQLIGIVSHDLRNPLGAILLGVQLLLRREDLDAPIIRALARLQTSAERAVRMVRDLLDFTQARLGGGLRIERKPVDLHAVVRASVDELEATHPDRELRLERRGDALGIWDADRLAQLVGNLVGNALKYSPPDTPVHIRVLGDPEGVCFEVHNQGEPIPADALPRLFQPLQRAVVGVDNMTRSVGLGLYIVDQIVRAHGGGLSVTSTERDGTTFSVRLPRGT
>NZ_CP022163.1|WP_095981592.1|8618744_8619143_+|transposase
MEKELEQFRQEVQRLRAGRAKGSGPFPEPMRAFAVRYLAQALEKGETLKSVVERLGVSEPTLQAWRRGQTPGSKARGSEPRRAGLVPVVVHEEKVPARPREGTTLAVVSPQGWRVEGLGVEEAVEVLRRVAC
>NZ_CP022163.1|WP_095976450.1|8619136_8619517_+|IS66-family-insertion-sequence-element-accessory-protein-TnpB
MLTLTRAVRVYASAVPVDMRKGFDGLSALVEQQLGGQLLKGDVFLFVGRCRQRAKVLYFDGTGLVLLTKRLFKGRFARPWAQAGAVSVELTVAELSLFLEGCELAGRWKLSPPAFEEKELAVEAAV
>NZ_CP022163.1|WP_095981593.1|8619532_8621050_+|IS66-family-transposase
MVPLGQVKDLETAKQMAALLEAENARLHQRLEALVQENARLKGEDAQARLQLELTQLQEQLARMQQRLFGASSEKRPSAQQEEPAAHECQQRGHGPRAQPELPVQEVLLPLDEADKVCGLCGGALAEWRGQTEDSEEVSVVERHFVLKRYRRQKYRCPEGCAPVTAPTAPRLIPGGRYAVDFAVHVALQKYAFHLPLARQERMYRREGLVVDTQTLWDQLSALARHLQPSYEALLTVVFASPLIHADETHWHLLDKGPGKKWYAWTVASPRAVHHRILPSRSGATARQVLGNYQGVAMVDGYAAYQTATKPGADGPASCSLVFCWAHVRRKFVEAEQVAPACAQVLSLIGQLYAIEAGLPDPHALEGAQQTAALALRLLVRREQSVPLVAAIREWALAQRALPGSGLRKALEYMLALWSGLTVFLSNPWVPLDNNLVERQLRDLVLGRKNHYGSKSLRGTEVAALFYSLIETARLGGEDPGRYLLRAALAAIDNPGTFTLPSSLD
>NZ_CP022163.1|WP_095981594.1|8621226_8621859_-|ankyrin-repeat-domain-containing-protein
MSKDLFAAIKQHDTARVKALLEGGANPNEPQSEGRGLRPLQEAIFALCDGGEVDMLKVLIEHGADVNAWDVERDQTPLLTAVCEQEVAALEVLVRAGADPNVRSGGGDTPLRICAESGYLAMAALLLFAGAVRTINDWGGISGYTALGLAALRLDLPMIKLLLAAGADPRAPDEDKRPAHYCMPPRAESDSQTWDEVFELLGGAKDRMPL
>NZ_CP022163.1|WP_157823861.1|8621862_8622648_-|hypothetical-protein
MDRKLTAAERAFERFSRAAKASGQAAKVVRGAEGVAQAGRARTLAEFLPRVGPLLVGLVLLYPFSTAGPEIDRRPEWVDAQREYEARLLDVAEESRRLMEEFERQEAEEVVPDFDSAPLMAVREPKTWRTTVNPATGKFYTTVEEYDRVPRHEGQICKNSKLDELEEEKRVLYTKIPILDPRHPNSSNERWEPEIPCSNIRNRLKAMQKVLDKREEIKKKCFGGKSDAGHDKAIGDLQKGIAYLKRLEGTNCVSGHPMADR
>NZ_CP022163.1|WP_157823862.1|8623481_8624855_+|hypothetical-protein
MSRVLYDFLSESFLFRDDYISAQYGNISEAQLESELRKYREHALSRLDELRSNLTTSPSRLSVYFDSTASVSTSVLKQSALYYDRAIMDDPIFRESRPHDPMPEFRQMVGHPRKTVDRAALAQSAHFMKEVTPMVAGGFAGFAPISLTHEPPKMVPLLASGNFFEERVPPELRAFFDERTSAFSVEVLPGGKGYVRHGPLAPCRHIGVKFGDYPSQWGYFLPQLESTRIIDEERRIVEFVQSMPDTPPDETVFLNWVRQSKNLAAADLLNHVATDVNNAAATRSYLCANSAFVADLLALERTSSTPEEDIARLALRLELPIVDGVSMADLMCIRSNEGESFEIFRTELAAKLRDIRHVADPAAQEAKLRDLEHDFSVTQVERLSQQLVRLKRDLWPSLALGAVSMTAILIEPQIKILGLAGVAISATAAGVKYLNSARQIPALFLWKLKKNLRPKDR
>NZ_CP022163.1|WP_095981597.1|8626792_8627533_+|hypothetical-protein
MKNSGRRTRSILGLAGFLLVLVTALGAQAAPPSKLPGRKPDSTEPWGAFLGRAAHLAIGRQYSVQYPTNAVFLDTVNLYRIVEEGKLGNPKRLSEFVRLLRPDITDTRALVLFEIKPDNEEGRKEGREQAGRYLAALNEAVEPGKKLAGGTGFEGSLFLEFENGGALWQLSWRTPEPGVTLYRWSYRRKKSNASWKERAAQKEEELPKEEGEQRGEVAEQALRAAYEGGELPSNFQGQVYLPVDCR
>NZ_CP022163.1|WP_095981598.1|8627619_8628429_+|hypothetical-protein
MTVPQSPVLEFPAMLHGSIGAIRREVRAKGQGWAREYLKTGAFTLPRRMLQVPPGEPLVMHSAAEFEFIRRSSWRIHMFGDVFMSLDEGVSSEDEHQRMRDAFESFCLSTPWGALCYAVSPPPLRSAERMAKRLAALLRFWNVLRSPRYAYRVPDTHHTIDGLMDYIYRKMLEAWCPGGPASVREHMALTVERMSRATREDCMEAVLRVIPVLVEADTEFKHREELSDPGFLRERLAALPPKDFEDFSSAYKYTVTMQLADWDRALGRH
>NZ_CP022163.1|WP_095981599.1|8628669_8629266_-|glutathione-S-transferase-family-protein
MKLYFAPRTRATRARWLLEELEVPYELVKLDVAKQETTTPAHLALHPLGEVPVLVDGATVLFESLAICLCLADRFPEKQLAPPLDSAERGPYLQWIVFAEVTLEPLVLEHYRNTQLPEEKKANLARQHARLHEVLRAIDVRLEGREFVAGGTFTAADVALASILHLAHTMRLLEEYPKLVEYVMRQTKRPATRRAVSG
>NZ_CP022163.1|WP_095981600.1|8629371_8630283_+|LysR-family-transcriptional-regulator
MVSPADMILFAAVVREGSFTRAARQLGITKQTASERIGKLEEQLGVRLLERTTRRLRMTESGTTYYDRCAAIAAQIDEANSEVRQRQAEPVGLLRVSSPMLYGRRYLAPVVADFLSRYPKASVELVLADRRVDLIEEGLDLAIRIGTIDDSSLVARKLGEGPVYFVASPGFLSKYGIPSARELRSARCIGFSPFETWEAENVKSRIDPVLTVNDLEVACEAAIAGVGIARVPELLCREAIQDGRLKLLFGSKPTMLRTIYAVYPSRLNLPAKVRLFVDALATLTEPVSPPPTLPHGRAGRKHR

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Crispr_ID: NZ_CP022163_14

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP022163_14

8668702-8668880

Orphan

Consensus_repeat	Method
AGCCGTGGGTGCCCATGACGCCGTCGATGGGGCCCGTGTACCCACCC	PILER-CR

2 spacers

The CRISPR arrays of NZ_CP022163_14

>merge|NZ_CP022163|14|8668702-8668880|PILER-CR
CGCCATCGATGGGGCCCATGTACCCACCCAGGCGCGCGACCCGCTGGAGCGCCGCGTAGCTGTGGGTGCCCATGACGCCGTCGATGGGGCCCGTGTACCCAAAGCCCCTCAGGACGGTCTGCACGCCTTTCCAGCCGTTGGTGCCCATGACGCCGTCGATGGGGCCCGTATAGCCTCCC

>NZ_CP022163|14|2|8668702-8668880|PILER-CR
CGCCATCGATGGGGCCCATGTACCCACCCAGGCGCGCGACCCGCTGG	AGCGCCGCGTAGCTGTGGGTGCCCATGA
CGCCGTCGATGGGGCCCGTGTACCCAAAGCCCCTCAGGACGGTCTGC	ACGCCTTTCCAGCCGTTGGTGCCCATGACGC
CGTCGATGGGGCCCGTATAGCCTCCC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP022163.1\|WP_095981628.1\|8671145_8671787_+\|hydrolase	unknown	unknown	gnl\|CDD\|238494
NZ_CP022163.1\|WP_095981618.1\|8657382_8657841_-\|immunity-26/phosphotriesterase-HocA-family-protein	unknown	unknown	gnl\|CDD\|379725
NZ_CP022163.1\|WP_095981637.1\|8681597_8682053_+\|VOC-family-protein	unknown	unknown	gnl\|CDD\|319910
NZ_CP022163.1\|WP_095982807.1\|8665253_8666567_-\|IS4-family-transposase	unknown	unknown	gnl\|CDD\|376573
NZ_CP022163.1\|WP_157823870.1\|8677014_8677824_-\|class-I-SAM-dependent-methyltransferase	unknown	unknown	gnl\|CDD\|379312
NZ_CP022163.1\|WP_095981630.1\|8672883_8673846_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|283530
NZ_CP022163.1\|WP_095981635.1\|8679903_8680905_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095981621.1\|8660221_8662282_-\|PAS-domain-S-box-protein	unknown	unknown	gnl\|CDD\|236901
NZ_CP022163.1\|WP_095981619.1\|8657981_8658641_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095981631.1\|8674118_8675774_+\|response-regulator	unknown	unknown	gnl\|CDD\|226654
NZ_CP022163.1\|WP_095981622.1\|8662344_8662773_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095981632.1\|8675765_8676725_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|173835
NZ_CP022163.1\|WP_157823871.1\|8680917_8681469_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095981620.1\|8658810_8660124_+\|PQQ-dependent-sugar-dehydrogenase	unknown	unknown	gnl\|CDD\|369642
NZ_CP022163.1\|WP_095981629.1\|8671843_8672608_-\|heparin-lyase-I-family-protein	unknown	unknown	gnl\|CDD\|372911
NZ_CP022163.1\|WP_095981624.1\|8664466_8665192_+\|hydrolase	unknown	unknown	gnl\|CDD\|238494
NZ_CP022163.1\|WP_095981634.1\|8678019_8679735_-\|LysM-peptidoglycan-binding-domain-containing-protein	unknown	unknown	gnl\|CDD\|212030
NZ_CP022163.1\|WP_095981625.1\|8666812_8667556_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095981626.1\|8667641_8668445_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095981623.1\|8663119_8664334_+\|methyltransferase	unknown	unknown	gnl\|CDD\|379330

Protein	Function_ID	Function_description	E-value
NZ_CP022163.1\|WP_095981628.1\|8671145_8671787_+\|hydrolase	gnl\|CDD\|238494	cd01012, YcaC_related, YcaC related amidohydrolases; E.coli YcaC is an homooctameric hydrolase with unknown specificity. Despite its weak sequence similarity, it is structurally related to other amidohydrolases and shares conserved active site residues with them. Multimerisation interface seems not to be conserved in all members.	2.60766e-64
NZ_CP022163.1\|WP_095981637.1\|8681597_8682053_+\|VOC-family-protein	gnl\|CDD\|319910	cd07246, 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.	2.86724e-48
NZ_CP022163.1\|WP_157823870.1\|8677014_8677824_-\|class-I-SAM-dependent-methyltransferase	gnl\|CDD\|379312	pfam13649, Methyltransf_25, Methyltransferase domain. This family appears to be a methyltransferase domain.	8.69501e-27
NZ_CP022163.1\|WP_095981630.1\|8672883_8673846_+\|hypothetical-protein	gnl\|CDD\|283530	pfam05891, Methyltransf_PK, AdoMet dependent proline di-methyltransferase. This protein is expressed in the tail neuron PVT and in uterine cells in C. elegans [worm-base]. In Saccharomyces cerevisiae this is AdoMet dependent proline di-methyltransferase. This enzyme catalyzes the di-methylation of ribosomal proteins Rpl12 and Rps25 at N-terminal proline residues. The methyltransferases described here specifically recognize the N-terminal X-Pro-Lys sequence motif, and they may account for nearly all previously described eukaryotic protein N-terminal methylation reactions. A number of other yeast and human proteins also share the recognition motif and may be similarly modified. As with other methyltransferases, this family carries the characteristic GxGxG motif.	0.00514875
NZ_CP022163.1\|WP_095981621.1\|8660221_8662282_-\|PAS-domain-S-box-protein	gnl\|CDD\|236901	PRK11360, PRK11360, two-component system sensor histidine kinase AtoS.	5.40312e-67
NZ_CP022163.1\|WP_095981618.1\|8657382_8657841_-\|immunity-26/phosphotriesterase-HocA-family-protein	gnl\|CDD\|379725	pfam15428, Imm26, Immunity protein 26. A predicted immunity protein with mostly all-beta fold and several conserved hydrophobic residues. Proteins containing this domain are present in bacterial polymorphic toxin systems as an immediate gene neighbor of the toxin gene, usually containing a domain of the Tox-URI1 or Tox-HNH family. The protein is also found heterogeneous poly-immunity loci.	2.71544e-13
NZ_CP022163.1\|WP_095981632.1\|8675765_8676725_-\|hypothetical-protein	gnl\|CDD\|173835	cd00687, Terpene_cyclase_nonplant_C1, Non-plant Terpene Cyclases, Class 1. This CD includes terpenoid cyclases such as pentalenene synthase and aristolochene synthase which, using an all-trans pathway, catalyze the ionization of farnesyl diphosphate, followed by the formation of a macrocyclic intermediate by bond formation between C1 with either C10 (aristolochene synthase) or C11 (pentalenene synthase), resulting in production of tricyclic hydrocarbon pentalenene or bicyclic hydrocarbon aristolochene. As with other enzymes with the 'terpenoid synthase fold', they have two conserved metal binding motifs, proposed to coordinate Mg2+ ion-bridged binding of the diphosphate moiety of FPP to the enzymes. Metal-triggered substrate ionization initiates catalysis, and the alpha-barrel active site serves as a template to channel and stabilize the conformations of reactive carbocation intermediates through a complex cyclization cascade. These enzymes function in the monomeric form and are found in fungi, bacteria and Dictyostelium.	2.13932e-10
NZ_CP022163.1\|WP_095981620.1\|8658810_8660124_+\|PQQ-dependent-sugar-dehydrogenase	gnl\|CDD\|369642	pfam07995, GSDH, Glucose / Sorbosone dehydrogenase. Members of this family are glucose/sorbosone dehydrogenases that possess a beta-propeller fold.	3.86411e-175
NZ_CP022163.1\|WP_095981629.1\|8671843_8672608_-\|heparin-lyase-I-family-protein	gnl\|CDD\|372911	pfam14099, Polysacc_lyase, Polysaccharide lyase. This family includes heparin lyase I, EC:4.2.2.7. Heparin lyase I depolymerizes heparin by cleaving the glycosidic linkage next to an iduronic acid moiety. The structure of heparin lyase I consists of a beta-jelly roll domain with a long, deep substrate-binding groove and an unusual thumb domain containing many basic residues extending from the main body of the enzyme. This family also includes glucuronan lyase, EC:4.2.2.14. The structure glucuronan lyase is a beta-jelly roll.	4.05642e-84
NZ_CP022163.1\|WP_095981624.1\|8664466_8665192_+\|hydrolase	gnl\|CDD\|238494	cd01012, YcaC_related, YcaC related amidohydrolases; E.coli YcaC is an homooctameric hydrolase with unknown specificity. Despite its weak sequence similarity, it is structurally related to other amidohydrolases and shares conserved active site residues with them. Multimerisation interface seems not to be conserved in all members.	7.71493e-64
NZ_CP022163.1\|WP_095981634.1\|8678019_8679735_-\|LysM-peptidoglycan-binding-domain-containing-protein	gnl\|CDD\|212030	cd00118, LysM, Lysin Motif is a small domain involved in binding peptidoglycan. LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.	1.19823e-15
NZ_CP022163.1\|WP_095982807.1\|8665253_8666567_-\|IS4-family-transposase	gnl\|CDD\|376573	pfam01609, DDE_Tnp_1, Transposase DDE domain. Transposase proteins are necessary for efficient DNA transposition. This domain is a member of the DDE superfamily, which contain three carboxylate residues that are believed to be responsible for coordinating metal ions needed for catalysis. The catalytic activity of this enzyme involves DNA cleavage at a specific site followed by a strand transfer reaction. This family contains transposases for IS4, IS421, IS5377, IS427, IS402, IS1355, IS5, which was original isolated in bacteriophage lambda.	9.35647e-08
NZ_CP022163.1\|WP_095981631.1\|8674118_8675774_+\|response-regulator	gnl\|CDD\|226654	COG4191, COG4191, Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal transduction mechanisms].	1.27754e-51
NZ_CP022163.1\|WP_095981623.1\|8663119_8664334_+\|methyltransferase	gnl\|CDD\|379330	pfam13679, Methyltransf_32, Methyltransferase domain. This family appears to be a methyltransferase domain.	5.08178e-13

>NZ_CP022163.1|WP_095981626.1|8667641_8668445_+|hypothetical-protein
MTVSQSPVLEFPAMLHGLTGAVLRKVRAKGQGWAREYLKTGGFTQPRQMLQVTPGEVLIMHSGADSNLLPYPRWRVHLFSDVFLSLDEGVPKEERQRAREAFESFCLSTPWGALHHVVSPRPRRSAERMARRLAALVRFWDVLQGPRYAFWFEREYTLEELVEDIYGKTLEAWCPEGSVSVREHLALTVERMSRATREDCMEAVLRMIPVLVEVDTGFKHREELGDPGFLRERLATLPPKDFEDISSAYKYTVSMQLADWDRALGRH
>NZ_CP022163.1|WP_095981625.1|8666812_8667556_+|hypothetical-protein
MKERATKTRSTWRLAGFLLVLGVALGAHAEPPSSNLPGRKPDTSEPWGAFLGRAAHEAIGRQYRVQHPTHAVFLDTVNLSTIVEEGRLGDPERLSKFARRLRPDITDTRALVLFEIKPDNEDGRKEGRAQAGRYLAALNAAVEPHKQLSGGTGFDGSLFIEFENGGALWQLSWRTPEPGVTLYRWSYRRKQPNASWKERAAQKEEALPREEIEQRGGWVEQALRAAYERGDWPSGFQGQVYLPVDCR
>NZ_CP022163.1|WP_095982807.1|8665253_8666567_-|IS4-family-transposase
MVRRTLEHALSSQWIDEVFEANREQQYTRELLFSSVVDLMGVVALGLRPSLHAAAQSDPDLTVSLAALYDKVNHTEPQVVRALVQGSAERLLPVVRPMKKQGPWAAGYQVRVLDGNHLPASEKRLKPLREFRGAALPGQSLVVYAPELSLVVDVLPAEDAHAQERALMGPVLERVREGELWLADRNFSTSRILRAVHEKRAAFIIREHGVSPNPTALGERREVGRGPAGRVYEQAVRVEGEEPLELRRIEVELEEPTEDGETAIRLLTNVPEEKLSAVEVAQLYRKRWTIEGMFGELEAVLESEVRSLGRPRAALLAFGVAVLAYNVLSVVKTAVEASHDLEAANMQVSTYYIAAEVKFAYGGMMMVVEPEDWSGQEVRSAEQLSELLLELAKKVKPSTLRKHPRAAKKKVKKGYVPGEVARKHVATARVLKGEKIS
>NZ_CP022163.1|WP_095981624.1|8664466_8665192_+|hydrolase
MSKPYSRLDINNAAVLLVDHQAGLLSLVRDFNPDQFKNNVLALADLADYFKLPTLLTTSFEDGPNGPLMPELKAKFPQAPFIARPGQINAWDNEDFVKAVKATGRKQLLIAGVVTEVCVAFLALSAIEAGFEVFIVTDASGTFNEVSRHTAWNRMSEAGAQLVTWFAAACELHRDWRRDVEGLGSLLSNHIPDYRNLITSYSAFKAHPFQGRIVARHLYGLDRADEGASVKLGRPSDIAMP
>NZ_CP022163.1|WP_095981623.1|8663119_8664334_+|methyltransferase
MNFRDRLEALTLLLRPWSELWSRSILQNWPESGAAYPDSWLSYAESLDEAGERRLDEGALPGAPPQSLQSLLLALHALTELPWHQGVQRLAVADAQGLNAKKIHEVERVLALLEPRTRTIRQAVDIGGGMGHLARLCVKSFNWTFHSIDRDAALQEKGRDWLRRARTLPRDKLCFIHTSVEDGPQPAIDPLFSGRESASMGLHTCGPLALTQIRKSQDAGLLLNFGCCYDKLDAARDLPVSRFGEAHRLPFTRHALFLATRGRRDKTEAEFALMKRVYGQRFALDLLLRRRFPERGFVRAGDAPKALYAESFAVYARDRLDRLGLDVGMTEAELNSFEASVRSETRRIFLCHLLRDRFARALEVVILLDRAILLEEMGFQVELLQVFDPRLSPRNIALIASRAD
>NZ_CP022163.1|WP_095981622.1|8662344_8662773_-|hypothetical-protein
MISWLVVECGGVTEKCGGPVALAPRRDVAYFVDAKTAERDAHAFAAYKNAQHEGRVLEPAPTAELRWHMPYAWDHQIFSPLLRWGVLEWNGQSGKPGPRPDVAYFLDPDTAESDAKWFSRERDHWLAHRSSAPALALTRRAG
>NZ_CP022163.1|WP_095981621.1|8660221_8662282_-|PAS-domain-S-box-protein
MHVTLLGIPDFVSEELEREFHAEALAIECRRVALERRLLPQVIPPGLVVLWDPGGPLEQMRGICQRLASLGSLSRTCLVVLTRRDEVERETLVLAGASECIPPEGERWAPHLLVLTRRMGVPTRTGVQSETPGTSRVPPERALQTLLAATTADLGHDFFRTLVKQLAEAFRVTCTMVGEMSSGKESIQTLAFWSRGAFQENVTYPLRGTPCYNAVACSICHYADDVSQHFPEDLMLTDLGLRGYLGAALRSTTGEVIGVLAILHEQQLEAGEMDFSLLGAFAARAGAELERIRAHAELERTRDFLRNTLDAVPDPLFVRDRDHRWVMVNTAFCQLMGHPAEALLGRSSIDFLPSRESQAYWLQDEQALASGRPDESELSFTDRTGLTRTLLTRRAVFPGANGQPALVSVIRELTERKRLETQLRLADRMASMGTLAAGVAHEINNPLAYISSNLTFLSEQLSRAALPPEALPELCEVVAETQEGAGRVQSIVQDLKTFARADEERRGPVNVHQVIDGALRLVRNELQRQNTRLERSLDPVPAVLGNEARLGQVLVNLLVNALQAFPEQRATANLIRITTRRGGPRQVVLEIEDNGVGMSPEVMQRIFDPFFTTKPVGVGTGLGLAICHTIIQSMGGQIDVRSTQGKGTTFLVSMSVFGDEDEEEGLVQPTRLAEDAPPPALLRVYG
>NZ_CP022163.1|WP_095981620.1|8658810_8660124_+|PQQ-dependent-sugar-dehydrogenase
MRTLSMTILLAALLSGCSSSKTPDPTDGTPQPPEDAGIPSEDAGIPSEDAGIPEEPLPSGPPVPTGPPNVPEFEPAFPGQTRAPAIQTKTAFQVTEIASGFRNPWAIAFLPDQRMLVTEKPTGALYIVTPQGEKSPAVTGLPPVDGRGQGGLLDVEIGPDYAQSGLIYWTYYEPRAGGNGLAVARAKLVEGAQPRVEDVQIIFRMMPTLESTLHAGGRLVFTPDGKLFVTLGERSILEGRVQARDVKSHFGKIVRINPDGSVPQDNPYVNTEGAKPEIWSVGHRNILSAALDSQKRLWTVEMGPRGGDELNRPEAGKDYGWPTIGYGEEYSGAPIHESTQGPGMEQPVYYWDPVMSPSGMTIYTGDLFPEWRNNIFIGGLSSQALVRLMVRNDRVVGEERLLTDLKARIREVVQGPEGALYLLTDATNGKLLKLTPR
>NZ_CP022163.1|WP_095981619.1|8657981_8658641_+|hypothetical-protein
MLLALLGLTLLASTPTVPPTSCLFANGKTACGYSCQRSVNDVRCASTPYGTCAMFHDRVYCFDPPLAAIHHPPDEGLRPECKGIGDEAACGFNCLVAQGKIACARTPYGVCREHLGELKCWDPPESVIHELGARTPRPGCLTASTALECGYDCKASRAEVKCAATPRGRCEKNDFRLECFDPPSLTHCAHAQPPDPAEVRKPKHQRREVQAEESGSAAR
>NZ_CP022163.1|WP_095981618.1|8657382_8657841_-|immunity-26/phosphotriesterase-HocA-family-protein
MSKQRHKAGTFVRLALADGSFGYGRLLAPPYLAFYNLRTESPDADVDGIASRSVLFKIAVNLLALKAWEPIGWRELEEDLIQPLVQFRQDVGDFRRCTIFDTTGNKRAAEPQDCVGLERAAVWEQASVEERLLDALRGRLNSAVEHLKVRLR
>NZ_CP022163.1|WP_095981628.1|8671145_8671787_+|hydrolase
MSKPYSRLDINNAAVLLVDHQAGLLSLVRDFNPDQFKNNVLALADLADYFKLPTLLTTSFEDGPNGPLMPELKAKFPQAPFIARPGQINAWDNEDFVKAVKATGRKQLLIAGVVTEVCVAFLALSAIEAGFEVFIVTDASGTFNEVSRHTAWNRMSEAGAQLVTWFAAACELHRDWRRDVEGLGSLLSNHIPDYRNLITSYSTFKAASSPAKP
>NZ_CP022163.1|WP_095981629.1|8671843_8672608_-|heparin-lyase-I-family-protein
MKTQNISAVVGGSLLAFALTAEADPFRNTGTVSGWNSINREHKGTVQEVTNLSYEGPTSIKVTQVYDPSYSGRYHSEVVKNNVYRRGDTGFYGFAFRLQQDWQFQSQSFNIAQFIADFSNTGCDDYMPSSMIWLQGNQLFTRVKQGSICAQKTVTFGNLATVTAGEWHKVIVQAKWASDGTGFYKLWFDGKKVLEQYNLSTTISDDRYFQFRVGLYANGWHDNGYMQGSQGTRSIWFDEISAGTTFAEADPDQW
>NZ_CP022163.1|WP_095981630.1|8672883_8673846_+|hypothetical-protein
MSDDFLTVWNHYRTEGLGAAARAATSTPESLLYLAMLAFADERYAEAATFAERAARAAPDALLPRAAATYLTRVAREGKRNVYVSAEGFSVFIRGGGNVPLYRETSAALVRCYPSEPFELLDIGVGDGRALLPALTPAVRRVTLVEPATPLLERTTQELATRGVAFDAFAGGLGEFAAEPHSRSRRWAVAQATFSLQSLEPSARLPLLSWLRARCDALLIAEFDPPSMDEPLKPETARHVLARYREGLAEYVGADFETVAQGFLMPVLFGYVDRGATRTNFEQPLSQWERLLGEAGFSRVERRPLYPYWWAPAGLLVARA
>NZ_CP022163.1|WP_095981631.1|8674118_8675774_+|response-regulator
MQEEDDGHQGLGRATLLRALVELEQINPDGCVVLRAIRDQNRVITDFEFIFSNDVESMKLVQPGLVVGRRLSEAVPPAMNGRFAIFCQVVETRQPVKSEVYYPHCWFRSTVMPFLDGIIVRFQDVTALVRDELERKARLEREQSSRQEAEALVRNQAGQLQAAQEKLVQSGKLMVAGQLATGVGHEINNPLSFVTGNLHVALEQLGALSQELPPPSAERLRELTHALEDARKGAERIRTIVKELRTLARSSETHTGPVDVGAALEFSLSMAMPHIRHRAQVVRRLERVPRVLGNESRLGQVLLNLLINAAQAIPEGDATHHAITLSTRVEGSQVVIEVRDTGKGMSAEVLARIFEPFFTTKPPGEGTGLGLPISRDIIREMGGELRVQSELGRGSSFQVVLPVLDETMTPVVAPPVVKQQAPPRRRVLIIDDEPSIGSMMKRVLGRNHEVKVVHSGREALALLSADPGFDRVFCDLMMGDMTGMDLHAELARRQPDYLPRFIFMTGGAFTDRARAFLADASVTSLDKPFEPVTLREMVERLPPGGKGPDSR
>NZ_CP022163.1|WP_095981632.1|8675765_8676725_-|hypothetical-protein
MDELIQKLGSKDKVAFDIQVDGARHRVDWPLDFSEYRVIASTYPVALGLCERGSFPELEQLRSHLTHSDLDLLTYFTSSSDSPLYLQNSQDRMDWFFALDYFVDGPSVPPELREEVVRDLTGWLDDRSHVSRLPWVNTLNALLRIVLEDIEREGLDTSIIVRDTRGYFEGFLLEFDQKVPLERYLENRCKTIGMRPELEFCFAYLGTPLPAHERDLAERMKRAAADLVALQNDVLSLSKEEAQEQEHLRLKSYFPDSRRYVSFLNRFYEARFTSFLALRPREPGPLEAFWEVCSQWISGSLVWHLTSRRYNLGQFAILP
>NZ_CP022163.1|WP_157823870.1|8677014_8677824_-|class-I-SAM-dependent-methyltransferase
MNYVLESKSEFNRLEHQSGLSGYDYQRELALSGLPAIQDGMRVLDAGCGSGIVTRYLAQEHPGCEVEGCDLSEVRVAQARDAAKGFSRLRFKVQDLARLDYPEAHFDIILCRYVVQHLPPESHSAVLTGFLRCLKPGGHLLLIDFDGGFLNLHPQPSEWLREALRKMETRFPVDLRIGRKLPHLLVKAGFIQTQWRIDVLEWSGDMLAQERMLLDQRILALEPVLSHVLGSVPEARRFHREYLEALDTPGCVLFYNKFIVTGRKPSHVE
>NZ_CP022163.1|WP_095981634.1|8678019_8679735_-|LysM-peptidoglycan-binding-domain-containing-protein
MTGVSSYKVRSGDTLSGIAKSNNTTVDALAQANGIKDPNKLAAGQTLRMPDSFDAKGSTPYTVRSGDTLSGIAKRNNTTVSALAQANGIKDPNKLAVGQKLQLPGASGTRPATGSSGDNFEPGKATGPSGTQQQPPASAPAGEVLGGLSRKYEARGAGTVSTGKGDNGGVSYGSYQFASKNGSAQNFVDSLKTSHPQYHAALAGKTPGTEAFSTAWKQLAAKDPKGFDQAQHDYIKATHYDVGAAEIKKATGLDVNTRSHALRDVAWSTSVQHGPKAADDIFKAALKGRDPATVSDAQLIKDIYAERGRRGANGELVHFSRSSRDVQEGVADRFVKESKDALAMLSREGSQPAATPSNVPTPTPRPADARPSSPANQGPTTETDNDTTPVKQGALPAKHVKVPYYSQFEGGHGYTPSDTACFKAATAMAGAAGAKVLGPADRIQVGTSENSKGQLAINSKKAAEGRSYIDQQLDKGKPVVVGVSHKDSNYNVDGLTDHFVTITGRGVDDKGRTYYTFHDPGTRHTSKGSDTNANNRFYVDEKTGAMTRPGSAATGSVTERRYDVAMVRRNG
>NZ_CP022163.1|WP_095981635.1|8679903_8680905_+|hypothetical-protein
MYNAARRMMGITCGVVWGWALAAGAQSAGDPSGVYEKDGAGLVIVQGSNETLVRYEAGFPQGESVGTCDCAFVVGNKSASRWTLSGADAEGEWSLRVAPGSFVLEGSGQGCCGAGWPGSDTFSRATAKPLTSCQVKGARAVFHASDAANTARKAYVVAGDKVETVIPASEPALVPARFKGPSKVTAGLLERTQLECAAPGGVKAEQLQPLAGTWISLTKKGKGYVISKPCSAETPSFTVEPSTAQMEIQLGQESTRVQVTKLTPGAGAGAWSLELTGGNGGAREQVEWKVTDAAKGLVTLRGSQLFAKSRVYVRGDKKSAYPVEAEKGCDEYE
>NZ_CP022163.1|WP_157823871.1|8680917_8681469_-|hypothetical-protein
MTPFVSSGIRRGATGLLLGASLLTGCGPSGRCEGFVGGTRIQGDIDGDSMLVIRPMPFRPSNTGAYVRGAQLELLYGDGALRLLLEIRLPAEQDTTELPLVLTEDESNQRLPQDGRVSIWSIQTPTDAPELRGGSLTVKLADANNLEGKIDARFEDGSQLECTYDVRGRNFFPGDDPTYNGPP
>NZ_CP022163.1|WP_095981637.1|8681597_8682053_+|VOC-family-protein
MPKAIPDGFHSLTPYLSLRDAAKAVEFYKAALGAVELYTLPMPGGKIAHGELQIGDSRLMFSDEMPEWGNKSAKSYGGTPVGLCVYTEDVDALAERFVKAGGKVVRPLENQFYGDRSGQFEDPEGYKWTLSQHVEEVSPEEMQRRMAKMGG

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Crispr_ID: NZ_CP022163_15

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP022163_15

9886595-9886696

Orphan

Consensus_repeat	Method
CGAGGACTCGCCCTACGCCTACCCGGACGA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP022163_15

>merge|NZ_CP022163|15|9886595-9886696|CRISPRCasFinder
CGAGGACTCGCCCTACGCCTACCCGGACGAGGAGGAGCAGTCGGACTCCCCTCGCCGGCGCTCCTCGTCCTCCGAGGACTCGCCCTACGCCTACCCGGACGA

>NZ_CP022163|15|12|9886595-9886696|CRISPRCasFinder
CGAGGACTCGCCCTACGCCTACCCGGACGA	GGAGGAGCAGTCGGACTCCCCTCGCCGGCGCTCCTCGTCCTC
CGAGGACTCGCCCTACGCCTACCCGGACGA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP022163.1\|WP_095982467.1\|9894476_9895562_-\|tRNA-preQ1(34)-S-adenosylmethionine-ribosyltransferase-isomerase-QueA	unknown	unknown	gnl\|CDD\|234666
NZ_CP022163.1\|WP_095982469.1\|9896742_9897303_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095982457.1\|9882316_9883234_-\|diacylglycerol-kinase-family-lipid-kinase	unknown	unknown	gnl\|CDD\|224513
NZ_CP022163.1\|WP_095982459.1\|9885234_9886515_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|341059
NZ_CP022163.1\|WP_095982450.1\|9873158_9873602_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|276809
NZ_CP022163.1\|WP_095982453.1\|9876396_9878031_+\|tryptophan-7-halogenase	unknown	unknown	gnl\|CDD\|368139
NZ_CP022163.1\|WP_095982454.1\|9878117_9879230_+\|DUF1864-family-protein	unknown	unknown	gnl\|CDD\|255115
NZ_CP022163.1\|WP_095982466.1\|9893274_9894459_-\|tRNA-guanosine(34)-transglycosylase-Tgt	unknown	unknown	gnl\|CDD\|234642
NZ_CP022163.1\|WP_095982458.1\|9883251_9885072_-\|aspartate--tRNA-ligase	unknown	unknown	gnl\|CDD\|234775
NZ_CP022163.1\|WP_095982470.1\|9897425_9897833_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP022163.1\|WP_095982455.1\|9879297_9881019_+\|tryptophan-7-halogenase	unknown	unknown	gnl\|CDD\|380163
NZ_CP022163.1\|WP_095982456.1\|9881075_9882251_+\|Rieske-2Fe-2S-domain-containing-protein	unknown	unknown	gnl\|CDD\|239611
NZ_CP022163.1\|WP_095982461.1\|9887549_9887771_+\|YHS-domain-containing-protein	unknown	unknown	gnl\|CDD\|309878
NZ_CP022163.1\|WP_095982452.1\|9875806_9875977_-\|rubredoxin	unknown	unknown	gnl\|CDD\|238372
NZ_CP022163.1\|WP_095982464.1\|9890951_9892721_-\|protein-translocase-subunit-SecD	unknown	unknown	gnl\|CDD\|223419
NZ_CP022163.1\|WP_179956492.1\|9887777_9889484_-\|single-stranded-DNA-specific-exonuclease-RecJ	unknown	unknown	gnl\|CDD\|273193
NZ_CP022163.1\|WP_095982451.1\|9873655_9875791_+\|sulfatase	unknown	unknown	gnl\|CDD\|293767
NZ_CP022163.1\|WP_095982468.1\|9895610_9896693_-\|SpoIID/LytB-domain-containing-protein	unknown	unknown	gnl\|CDD\|274252
NZ_CP022163.1\|WP_095982465.1\|9892720_9893071_-\|preprotein-translocase-subunit-YajC	unknown	unknown	gnl\|CDD\|235518
NZ_CP022163.1\|WP_095982463.1\|9889751_9890927_-\|protein-translocase-subunit-SecF	unknown	unknown	gnl\|CDD\|237275

Protein	Function_ID	Function_description	E-value
NZ_CP022163.1\|WP_095982467.1\|9894476_9895562_-\|tRNA-preQ1(34)-S-adenosylmethionine-ribosyltransferase-isomerase-QueA	gnl\|CDD\|234666	PRK00147, queA, S-adenosylmethionine:tRNA ribosyltransferase-isomerase; Provisional.	0
NZ_CP022163.1\|WP_095982457.1\|9882316_9883234_-\|diacylglycerol-kinase-family-lipid-kinase	gnl\|CDD\|224513	COG1597, LCB5, Sphingosine kinase and enzymes related to eukaryotic diacylglycerol kinase [Lipid metabolism / General function prediction only].	4.89384e-57
NZ_CP022163.1\|WP_095982459.1\|9885234_9886515_+\|hypothetical-protein	gnl\|CDD\|341059	cd09596, M36, Peptidase M36 family, also known as fungalysin family. The M36 peptidase family, also known as fungalysin (elastinolytic metalloproteinase) family, includes endopeptidases from pathogenic fungi. Fungalysin can hydrolyze extracellular matrix proteins such as elastin and keratin, with a preference for cleavage on the amino side of hydrophobic residues with bulky side-chains. This family is similar to the M4 (thermolysin) family due to the presence of the HEXXH motif in the active site residues, as well as its fold prediction. Some of these enzymes also contain a protease-associated (PA) domain insert. The eukaryotic M36 and bacterial M4 families of metalloproteases also share a conserved domain in their propeptides called FTP (fungalysin/thermolysin propeptide). Aspergillus fumigatus causes the pulmonary disease aspergillosis by invading the lungs of immuno-compromised animals; it secretes fungalysin that possibly breaks down proteinaceous structural barriers. A solid lesion known as an aspergilloma can grow in a lung cavity, particularly following recovery from tuberculosis. Fungalysins are also found as multiple copies in the human and animal pathogenic fungi such as Microsporum canis, Trichophyton rubrum and T. mentagrophytes, which cause cutaneous infections.	0.00366022
NZ_CP022163.1\|WP_095982450.1\|9873158_9873602_-\|hypothetical-protein	gnl\|CDD\|276809	sd00006, TPR, Tetratricopeptide repeat. The Tetratricopeptide repeat (TPR) typically contains 34 amino acids and is found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans. It is present in a variety of proteins including those involved in chaperone, cell-cycle, transcription, and protein transport complexes. The number of TPR motifs varies among proteins. Those containing 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accommodate an alpha-helix of a target protein. It has been proposed that TPR proteins preferentially interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes.	0.000530476
NZ_CP022163.1\|WP_095982453.1\|9876396_9878031_+\|tryptophan-7-halogenase	gnl\|CDD\|368139	pfam04820, Trp_halogenase, Tryptophan halogenase. Tryptophan halogenase catalyzes the chlorination of tryptophan to form 7-chlorotryptophan. This is the first step in the biosynthesis of pyrrolnitrin, an antibiotic with broad-spectrum anti-fungal activity. Tryptophan halogenase is NADH-dependent.	0
NZ_CP022163.1\|WP_095982454.1\|9878117_9879230_+\|DUF1864-family-protein	gnl\|CDD\|255115	pfam08933, DUF1864, Domain of unknown function (DUF1864). This domain has no known function. It is found in various hypothetical and conserved domain proteins.	2.77899e-114
NZ_CP022163.1\|WP_095982466.1\|9893274_9894459_-\|tRNA-guanosine(34)-transglycosylase-Tgt	gnl\|CDD\|234642	PRK00112, tgt, queuine tRNA-ribosyltransferase; Provisional.	0
NZ_CP022163.1\|WP_095982458.1\|9883251_9885072_-\|aspartate--tRNA-ligase	gnl\|CDD\|234775	PRK00476, aspS, aspartyl-tRNA synthetase; Validated.	0
NZ_CP022163.1\|WP_095982455.1\|9879297_9881019_+\|tryptophan-7-halogenase	gnl\|CDD\|380163	NF033113, halo_ClmS, chloramphenicol-biosynthetic FADH2-dependent halogenase CmlS.	5.74594e-23
NZ_CP022163.1\|WP_095982456.1\|9881075_9882251_+\|Rieske-2Fe-2S-domain-containing-protein	gnl\|CDD\|239611	cd03537, Rieske_RO_Alpha_PrnD, This alignment model represents the N-terminal rieske domain of the oxygenase alpha subunit of aminopyrrolnitrin oxygenase (PrnD). PrnD is a novel Rieske N-oxygenase that catalyzes the final step in the pyrrolnitrin biosynthetic pathway, the oxidation of the amino group in aminopyrrolnitrin to a nitro group, forming the antibiotic pyrrolnitrin. The biosynthesis of pyrrolnitrin is one of the best examples of enzyme-catalyzed arylamine oxidation. Although arylamine oxygenases are widely distributed within the microbial world and used in a variety of metabolic reactions, PrnD represents one of only two known examples of arylamine oxygenases or N-oxygenases involved in arylnitro group formation, the other being AurF involved in aureothin biosynthesis.	6.619e-78
NZ_CP022163.1\|WP_095982461.1\|9887549_9887771_+\|YHS-domain-containing-protein	gnl\|CDD\|309878	pfam04945, YHS, YHS domain. This short presumed domain is about 50 amino acid residues long. It often contains two cysteines that may be functionally important. This domain is found in copper transporting ATPases, some phenol hydroxylases and in a set of uncharacterized membrane proteins. This domain is named after three of the most conserved amino acids it contains. The domain may be metal binding, possibly copper ions. This domain is duplicated in some copper transporting ATPases.	1.40719e-11
NZ_CP022163.1\|WP_095982452.1\|9875806_9875977_-\|rubredoxin	gnl\|CDD\|238372	cd00730, rubredoxin, Rubredoxin; nonheme iron binding domains containing a [Fe(SCys)4] center. Rubredoxins are small nonheme iron proteins. The iron atom is coordinated by four cysteine residues (Fe(S-Cys)4), but iron can also be replaced by cobalt, nickel or zinc. They are believed to be involved in electron transfer.	2.24108e-21
NZ_CP022163.1\|WP_095982464.1\|9890951_9892721_-\|protein-translocase-subunit-SecD	gnl\|CDD\|223419	COG0342, SecD, Preprotein translocase subunit SecD [Intracellular trafficking and secretion].	1.97506e-135
NZ_CP022163.1\|WP_179956492.1\|9887777_9889484_-\|single-stranded-DNA-specific-exonuclease-RecJ	gnl\|CDD\|273193	TIGR00644, recJ, single-stranded-DNA-specific exonuclease RecJ. All proteins in this family are 5'-3' single-strand DNA exonucleases. These proteins are used in some aspects of mismatch repair, recombination, and recombinational repair. [DNA metabolism, DNA replication, recombination, and repair].	0
NZ_CP022163.1\|WP_095982451.1\|9873655_9875791_+\|sulfatase	gnl\|CDD\|293767	cd16148, sulfatase_like, uncharacterized sulfatase subfamily. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.	3.4398e-55
NZ_CP022163.1\|WP_095982468.1\|9895610_9896693_-\|SpoIID/LytB-domain-containing-protein	gnl\|CDD\|274252	TIGR02669, stage_II_sporulation_protein_D, SpoIID/LytB domain. This model describes a domain found typically in two or three proteins per genome in Cyanobacteria and Firmicutes, and sporadically in other genomes. One member is SpoIID of Bacillus subtilis. Another in B. subtilis is the C-terminal half of LytB, encoded immediately upstream of an amidase, the autolysin LytC, to which its N-terminus is homologous. Gene neighborhoods are not well conserved for members of this family, as many, such as SpoIID, are monocistronic. One early modelling-based study suggests a DNA-binding role for SpoIID, but the function of this domain is unknown. [Unknown function, General].	5.53126e-84
NZ_CP022163.1\|WP_095982465.1\|9892720_9893071_-\|preprotein-translocase-subunit-YajC	gnl\|CDD\|235518	PRK05585, yajC, preprotein translocase subunit YajC; Validated.	4.07883e-33
NZ_CP022163.1\|WP_095982463.1\|9889751_9890927_-\|protein-translocase-subunit-SecF	gnl\|CDD\|237275	PRK13022, secF, protein translocase subunit SecF.	1.06869e-95

>NZ_CP022163.1|WP_095982459.1|9885234_9886515_+|hypothetical-protein
MVRKLTATAALLALSCAPQTQVPMKVRALVLSSNGAYEPTEVELKTVTDIVSLEGKVARIQGNAILRLASTDPEVQAAQTEEALARAMTKDEGRSITASYITDPQGVLWPADFHTWNLVTTYYNLERAWDYFTNVVAVPQAELPQTTVHYFPEFVLADVSDQPQRDNALFYPPLKSFLVLPFDKLQKAPLATNASILTHEYAHLVFNRRVYGGSALPAPLNNWAQSGDFTPGLNVIKALDEGLADFHAYVASCQDVKRFGCNTRVLAYSFEDVAVNERDLATPRCMGQLMYNNLTRSSVNVLPNLAYEVGTLLANALFMSTTTDAEKQTMARAIVAAYSDTDAARPGFNQLAASSLNDQTTFTLIKAAKAIIQHIPAGNVDLRQKVCTNFATRLQIPVNALTGNTEYDCPASTTTTTDCPAINLNP
>NZ_CP022163.1|WP_095982458.1|9883251_9885072_-|aspartate--tRNA-ligase
MAVPFITEVKRTHTCGQLTKAQIGEEVVLFGWVQNRRDHGGAVFIDLRDREGLTQVVFEPDIAKEAHETAGQLRLEYCVGIKGKVVSRGSQVNPKLKTGEIEIKASDLTIFNRSEPTPFLVEDNIDTAEEKRLAYRFLDLRRRPLQQSLITRSKMNAITRSYLNDNRFLELETPFMGKYTPGGARNFLVPSRLNPGKFYALAESPQLYKQLFMVAGFDRYFQIVKCFRDEDLRLDRQPEFTQIDIEMSFVTQDDIFTIVEGLIKKLWGEVLGIDVPTPFMRMDFDESMAKYGNDKPDLRFGLEHIVLTELIRQHGAAGGVPMIWDAVEQGGIVKAMVVPGDKPMSRAESDKLEEFAKQNGAKGLARAKVAEGGEWTQSPLSKTITPALRQAINQACGVKTGDLLLFQFGRESLVHTVMANLRVHVAKKLGLIPEYGSGGVWKFLWVVNPPLFEYDEESKTWAAAHHAFTRPHDEHVQYLQTDPGRVKCHRYDVVLNGFEIGGGSIRLHDPKVQAEVFKALGIGEEEARVKFGFLLDALKFGAPPHGGLALGMDRLAMLLTGAESLRDVIPFPKTKTGTDLMTGAPGDVDDRQLREVHVRAAPLPQK
>NZ_CP022163.1|WP_095982457.1|9882316_9883234_-|diacylglycerol-kinase-family-lipid-kinase
MKTFLVVNPRSANGETGRRWAEISGQVTRSIGDFGFGFTERAMDAVRLTRDALADGYECVAAVGGDGTVNEVVNGFFADGKPINPQAALGLIPRGTGGDFRRAFGWELDLESALARLSSDKTEPFDVGVAEYVNHEGQAESRYFANIASFGVSATIAHEVNVGSKAFGGNLSFLWGTVKTLAKYKDRQVRLRVDGGEPETLGITVVAASNGRYFGSGMCVAPKALTDDGRFDLTLWQDYRLSDFIIKSKGVYNGDHTTWNKTRYLQCRTLEAESDEEVFLEMDGEVPGKLPCRIRLLPGAIRLKV
>NZ_CP022163.1|WP_095982456.1|9881075_9882251_+|Rieske-2Fe-2S-domain-containing-protein
MSVDTELEQNRIRPLPGLNDITTQLSASWYVALRSEDLKQKPVELKLFGQPLVAWRDKAGRPVVMERYCSHMGANLADGKVVDGCIECPFHRWRYDSAGACTHVPGHSQEVPKLEPIPPTARQSIYRTTERYGYVWVWYGTKAPLFPLPELPSADVGNKDYLNLRFSFDTKTSVLRIVENFYDAQHAEAVHQLPISAFKISVHDDWRDWHLSRDMESLAKADAWFGGSMEFKVNRYFGIIGILSRTLGLNISKMQLHFDGYPGGCIMTVSLDDQVKYKLLQCVTPVDKNETVMHMLITMKKADGALRNAANLIMFGLQTRQAAGYDVAIWNSLKTDGGGAFSKYDQLILKYRTFYRRWVNKVGQEQPAEHAPESRANMPEQKNTAQAMPSL
>NZ_CP022163.1|WP_095982455.1|9879297_9881019_+|tryptophan-7-halogenase
MQQPVNELKSPRGESTGNSNHFDVIILGSGMSGTQMGAILAKQGFRVLIVEESAHPRFTIGESSIPETSLMNRIIADRYGVPEIGDITSFYSTFKKVSSSTGIKRNFGFVFHREGQEHDPKEYTQCVIPELPWGPESHYYRQDVDAYLLHAAIRYGCTVRQRISITDYEVSKTGVAVTSAQGERFTGRYMIDCGGPRAPLAMKFGLRETPCRYRTHSRTLYTHMVGVKPFDDIFKLQGQRWRWHEGTLHHMFHGGWLWVIPFNNHDRATNDLVSVGLQLDPRIHPKTDIPAQQEFDEFLARFPTIAEQFKNAKPVRDWVKSDRLQYSSKTTVGDRYCLMLHAAGFIDPLFSRGLENTSVALHALAARLIKALRDDDFSPERFEYIDRLQQKLLEHNDDFVSCCYTSFSDFRLWDAFHRLWAVGTMLGQFRLVQAHARFKESRDERHLDHLDDNPPYLGYLCADMEGYYRLFNDCKAEVFAVAEQRKSSADAAARIHQLIDAQEFAKPLFSFGYCISGAWKHVNNSKYSLIPALRLLHWTQSGAPPEVRKYFDYNPMMSMLRTYVENRVALALK
>NZ_CP022163.1|WP_095982454.1|9878117_9879230_+|DUF1864-family-protein
MEQGQNFASMHAAITALDPLDALATMRRLPELNQQKDVPGILRLLHGILPPPGKARTWSYVEAAAAMRDIGFFLGSLKRHGHEPVEIVPALEPILLELARVTDLPPRETLLHVTVWNPPSPDAERRYTCCQAEVHLLESVRISMVSLESALHRLVELYELPIGSRLFAPMCDDVAEKLKKMVESIVYAYRTIPPRVFVQELRPYYDPIQVGGQSYLGPGAVEMPLFLLDHILWGSRSEHAEYKSFKETYLPYVLPQLRTLHGRFLGHISLLERVLEEVEAMGTLEEPVRGGLKSLDKIFEVLLRFRAPHVGLAEQAYQVESETHSVGSGGYAPSMLGDLLALTRDARSRLTAVLRGAEVSEPPARMSMAR
>NZ_CP022163.1|WP_095982453.1|9876396_9878031_+|tryptophan-7-halogenase
MNTNQIPDDNDGRVRNLIIVGGGSSGWIAAAYLSKALNFNVNITLIESANIGRIGVGEATIPTIKEELFDFLGVPEEEWMTECKASYKLGIRFQNWKKPASEGGDHYYHNFGEMPVVKGVPLSHVWMYKHQQQGFAKTLDYSCYSASPICDAMKSPRYMDGTKALHYAYHFDALLVSEFLKKWSIARGLTHITDDIIGTDLSETGDIQALRGASGRKYEADLYIDCTGFAGLLIEKALGEPKVTFHDCLLTDRAVAINIPSDSAAEGIRPFTTASAFSSGWTWEIPLNNRSGNGYVYSSAFQTAEDAEREVRAWFGKKADKVDVRHIKFISGRRRRSWVKNCVSIGLSSSFLEPLESTGLYFVYAALYQLMACFPNKDIDPALRNKFNERVSYMVDDVRDFIVLHFCTSPRTDTPYWRANQNELKLPDTLKEALELQKAGIPIRKSYHSNNSLYDSFEAGFDRFWTNSNFQSIFAGVNYLPKQPMPLLRHRPDILLEAERVFDDIQKKTDQMMAQLPSQYDYLASLYTKGKTGEQAVRSVQQAG
>NZ_CP022163.1|WP_095982452.1|9875806_9875977_-|rubredoxin
MSLKKYQCIPCGHIYDPAVGDPDSGIPPGTAFESLPETWCCPDCGAMKADFEPIED
>NZ_CP022163.1|WP_095982451.1|9873655_9875791_+|sulfatase
MNKLSGEMPPPTPLPFTRVLAWACRGGLCAFLGLYSLCAVLNMQLGYQGNENSELTSLVWREFRRDVLLQVARLITAHTVLGMFAGLVTGLAAWGLGATGRARVFLGGLGGSLLLALLVCLGDIAQHPHLYAATLYARSAWTKQVLLSISQTEPATWRTLAALLVLAAPVLASWRWRARRGTGGERTRPRALNGTGLARPLGVVLVGAILAGLLLAWNTTPTPPPGSRPNLLILASDGLRPDHLSGNGYPRRTSPHIDRLLREGSHFEQTIIQIPRTGPSWTTLLSSQWAGQHPIRHTMVGPEARASRFPTLATALREAGWRTAVLSDYAGDIFSRLPLGFEHVEAPAFNFPELIRQRMLITQVALLPWTALLPSFFPERQQFPELTDPSPLSASSRRALEDFREGEAPFALLVFASVTHFPYAAPHPYEGRFLAPGERGPWRFGATPQMEPPPAPPRPEDVAALVANYDAGVLAFDAFVGRMMEEMERRGLADNTLVVILSDHGEHLEERDRGLGHGEHLWGPEALRVPFILRWPGKVAAGRELTTRARAIDVAPTLLELLGVPAPASFQGRSLASQLVPGGAVPELDELPALLETDIWFSDRDGQRYQRFRLPYPWLYETLTVEKGSGDISLKPEWEETVEKARHRGLYLGRWKLLELPTPEGPRVELYDVHADPEERHEISAANPEVVADLRARLHRERSWAVLPAPR
>NZ_CP022163.1|WP_095982450.1|9873158_9873602_-|hypothetical-protein
MSAVDGDNPVVRLCAEGMRAEAEGRPQDARALFLQAWELSRDDYEACIAAHYVARHQDSSRDALHWNQTAFDRARAVGDERVLGFQASLLLNLGKSHEDLGAFTEARALYERAFRALDAVPESPYRDIVQGGITRGLERVAIALADT
>NZ_CP022163.1|WP_095982461.1|9887549_9887771_+|YHS-domain-containing-protein
MKSVQKKQLDPVCGKHLEAPEGRPSTEYKKRRYFFCSERCRSAFERQAERFRMNDLARAGALLTPGRVRWGIA
>NZ_CP022163.1|WP_179956492.1|9887777_9889484_-|single-stranded-DNA-specific-exonuclease-RecJ
MMPEVPQEQAALLAAELELHPLSARVLVHRGLRTPEAASAFLSDKLADLPDPFRMKGMVAAVERLARALRDKERITLYGDYDVDGVCSTSLLALFLRELGIRPATYIPHRLDEGYGLNLQAVEKIAAEGTQVLVTLDCGVTSVAEISRARDLGLDVVVVDHHTVPPTLPPAVAVLNPHQPGCEYPTKHLCAAGVAFNLCMGLRKRLREEGWFSTRKEPNLKALMDLVAMATVADVVPLTGANRILVHHGLQELSAGRRPGVRALKEVAGLDADTPVTAGQVGYRLGPRINAAGRLHDASLGLQLLCSESVDAARPLAQMLDRANAERQGLESSILTEALAQAGEIAERGARGFVLYADGWHPGVIGIVASRVVERFHRPTVMVGVKDGVGKGSARSIEGFHLYDALSGCADLFVRFGGHKHAAGLTVEAPQLPAFREAFERIAMQRLTPEDLIPRCKVDAVVGVSELDEGAVEALQRLGPFGQGNPEPVLVLRRQVARPRVLPHKTGGSGHLKLALVDAPAVDAIGFGMADRLALTEGPVDLAFQASFDTFRGQRRLSLKLKDLRSAA
>NZ_CP022163.1|WP_095982463.1|9889751_9890927_-|protein-translocase-subunit-SecF
MQILKNKTNFDFIGKRKPAFFISTALNLVILVGIAVFGFNLGVDFAGGTVVEVQFNHPVNASDVRERVESSGQLHDVSVQSIGSANENSFLVRLGGVTQLTEAGAEKASEAIQKLGQVDPKDIRPDLSNGMIRVRSKQPLDAAQMEKAVEDTGTGVDEVRDLGQAQSGDYEYQVVASGMADRIRAALMHGVQNPESPDFEMRRTEYVGPQVGKQLRNRGFQALLFSMVAILIYVAFRFDFKFGPGALLAMLHDVIMVAGFYLFSRAEFSLTSIAALLTVVGYSVNDTIVIYDRIREDMAKYPNRPLAEVINIAVNDTLVRTILTSGVTALSLVGLLIFGVGEIRDFAWAMLVGIVVGTYSSVYIASPVTLWLDERAASREKKSGTEQPKVA
>NZ_CP022163.1|WP_095982464.1|9890951_9892721_-|protein-translocase-subunit-SecD
MDRGWYWRLGLVIGVTLLTIWFLIPSYYSLFHVDRSQRNNLAAIDAAMPKWAPPAKYRINLGLDLQGGIHMVMRVDTKTALEKRTERRGDQIARYINDKQIGQVKVDTDPDRLQVTLTAQEPATMDAIEKEVLATFTDFSKVSRDGAKLVLSPDDTQTNRFREESVDQAMLVIRKRIDKWGVAEVDVRKLGTDAIQISLPGRNNPEQAKELVGTTAQLEFHMVDDTTDFFRQTYQTTPPPEGSNITLTTADGFPQLEGPNREALLEYVKGKVPQDRLVLLECIASATRKGVCDSYRTYLVEKEAPLTGESLTGADASLSQLNEPEVNISFDAAGARQFEQLTEKGVGRRMAIVLDDYVQSAPRINERIGGGRARITMGRSGGRPLEQWLADAQTLALALKAGALPAPVTTGEIRQVGASLGDELIRKGGLAAGVGVLCVIIFMVIYYRSAGLIADVALILNGLLIFGGLAFFNATLTLPGIAGFVLTLGIAVDANVLINERIREELAHGKTARAAVDQGYDRAFWTIFDAHVTSLIAGFILFFTGTGPVRGFATTLIIGLLASLFTSILVTRVIMTYFVHGKNAQTVSV
>NZ_CP022163.1|WP_095982465.1|9892720_9893071_-|preprotein-translocase-subunit-YajC
MADSYLVLAQAAGGPGGAWNIAFFIGLFAIMYFMMIRPQQKQLKTHRELISSLKKGDEVVTQGGIIGRIQVVAEREVTLEVASGTRIRVLKTSVAGRYAAGESASAAKIEDKKEEK
>NZ_CP022163.1|WP_095982466.1|9893274_9894459_-|tRNA-guanosine(34)-transglycosylase-Tgt
MGEPREEKGDTRVPPSLVRYELLHEDASGTRARRGRLHTPHGMVETPIFMPVGTVGSVKGVGPDELLTLDAQIILGNTYHLMLRPGDDLVGEMGGLHRFISWDRPMLTDSGGFQVFSLSEKRKITEEGAAFQSHLDGRKLLLTPERSIEIQETLGADIIMAFDECPPSTESRAYLEKSLARTTRWLHRCVKAWRRERSSLFGIVQGGMDPQLRKAHAEEVCAVDLPGYALGGYAVGETPEAMYEGVAYSAPLLPRDKPRYLMGVGTPVDLINCVEQGVDMFDCVLPTRCARNGLLFTTEGKLVIRNATWAKDPRPVDPACSCYTCRTFSRAYLRHLFVAGEILAMRLNTLHNLHYFLTLMKQVREAIAEDRYASFARDFREKARAQEAERTRTK
>NZ_CP022163.1|WP_095982467.1|9894476_9895562_-|tRNA-preQ1(34)-S-adenosylmethionine-ribosyltransferase-isomerase-QueA
MSSLLSDYDFALPEAQIAQTPLATRDASRLLVVSRASGAWTHRHFAELPGLLREGDLLVVNDARVIPARLLGSKADTGGRVELLVVRPASSTLTSHALGGDAEALEWICLGQASKGLKPGARLSFSGGLAAEVLEALGGGEYRVRFLAAPGTSLAEVLNQAGRLPLPPYITRAPEAADAERYQTVYARASGAVAAPTAGLHFTDAIFQALAARGIQRVEVTLDVGPGTFLPVREENLEKHRMHPERYFVPEATARAVNAAKAEGRRVVAVGTTVVRTLESAWDAAAGSLREGPGETEIFIRPGFDFRAVDVLLTNFHLPRSTLVVLVSALLGRERTLAAYREAVAAGYRFFSYGDAMLVTE
>NZ_CP022163.1|WP_095982468.1|9895610_9896693_-|SpoIID/LytB-domain-containing-protein
MLRPVAVMLLLLAPLHALAVETMRIAMGDAQGDVRVSGKGLSFGSDTEDARFSPLEQEAVVVRRRGSRLELNGAPVMGSAVRFRAGLDSQALRAGDMAVRGDVVVRLYKDGLQLINVIPLEDYLAAVLGGEMPVSFPPEALKAQAVAARTYALQKKLEAYGAPFYVGSSVLHQVYGGVNREDARTRIAVEATRGEVLTYDLAPIEAYFHASCGGHTESGWDALQRDLPYLQAVDCPCGRLPASRWSATVTDAELRAALGQSPEGFRVTSRTATHRVNRVTASGGASVDGVTLRRKLGYTKLKSLDFDAERTSGGWRLNGRGYGHGAGLCQWGAKALADQGRSYRDILQHYYPGTELQQLY
>NZ_CP022163.1|WP_095982469.1|9896742_9897303_+|hypothetical-protein
MTENAAPVSPAPDASRFSTADFVTALRALPSRPATLLLMRLAQGRSLPDSASFYGISPDAFSIHLLRAALALTQAATLPVRTPENDTEEDLWARVLAESLEREAVTIPPSMMATVALCKRMRALGPELTAALRAAERAEEDSPKRRREDWLRRLAVLALLGLTAYLYLHRTEEPPERPPAPRSRQR
>NZ_CP022163.1|WP_095982470.1|9897425_9897833_+|hypothetical-protein
MRHIKGVCIGAIAAALLLGTGCKPNQPVRPQNPSMEQGTGGSSIQSPESTDSAMGTGTGGSGLSNDTGSSPYMGTHDAGTGGVQGQEPGGMGGSGPTGSGTQQDNNTREPAPGTTQGNDASHRNTDPGADQGPNR

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Self-targeting detection

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_ID	Protospacer_location	Mismatch	Identity
NZ_CP022163_5	5.1\|3088449\|17\|NZ_CP022163\|CRISPRCasFinder	3088449-3088465	17	NZ_CP022163.1	3088405-3088421	0	1.0
NZ_CP022163_8	8.2\|3981770\|43\|NZ_CP022163\|CRT	3981770-3981812	43	NZ_CP022163.1	3981959-3982001	0	1.0
NZ_CP022163_8	8.2\|3981770\|43\|NZ_CP022163\|CRT	3981770-3981812	43	NZ_CP022163.1	3986851-3986893	0	1.0
NZ_CP022163_8	8.2\|3981770\|43\|NZ_CP022163\|CRT	3981770-3981812	43	NZ_CP022163.1	3986985-3987027	0	1.0
NZ_CP022163_1	1.1\|214999\|67\|NZ_CP022163\|PILER-CR	214999-215065	67	NZ_CP022163.1	215230-215296	8	0.881

1. spacer 5.1|3088449|17|NZ_CP022163|CRISPRCasFinder matches to position: 3088405-3088421, mismatch: 0, identity: 1.0

tcttacctggccgtact	CRISPR spacer
tcttacctggccgtact	Protospacer
*****************

2. spacer 8.2|3981770|43|NZ_CP022163|CRT matches to position: 3981959-3982001, mismatch: 0, identity: 1.0

aggggcctgagcgagaacgaggctcgggcgtggacgggtaacc	CRISPR spacer
aggggcctgagcgagaacgaggctcgggcgtggacgggtaacc	Protospacer
*******************************************

3. spacer 8.2|3981770|43|NZ_CP022163|CRT matches to position: 3986851-3986893, mismatch: 0, identity: 1.0

aggggcctgagcgagaacgaggctcgggcgtggacgggtaacc	CRISPR spacer
aggggcctgagcgagaacgaggctcgggcgtggacgggtaacc	Protospacer
*******************************************

4. spacer 8.2|3981770|43|NZ_CP022163|CRT matches to position: 3986985-3987027, mismatch: 0, identity: 1.0

aggggcctgagcgagaacgaggctcgggcgtggacgggtaacc	CRISPR spacer
aggggcctgagcgagaacgaggctcgggcgtggacgggtaacc	Protospacer
*******************************************

5. spacer 1.1|214999|67|NZ_CP022163|PILER-CR matches to position: 215230-215296, mismatch: 8, identity: 0.881

ccaggccaccctcgccgagacgcagacgacgctcgcctccaccgaggccaagctctcggc	CRISPR spacer
ccaggccaccctcaccgagacgcagacgacgctcgcctccaccgaggccaagctctcggc	Protospacer
*************.**********************************************

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity
NZ_CP022163_14	14.1\|8668749\|28\|NZ_CP022163\|PILER-CR	8668749-8668776	28	NZ_CP028969	Aminobacter sp. MSH1 plasmid pUSP1, complete sequence	363268-363295	4	0.857
NZ_CP022163_14	14.1\|8668749\|28\|NZ_CP022163\|PILER-CR	8668749-8668776	28	NZ_CP026266	Aminobacter sp. MSH1 plasmid pAM01, complete sequence	360454-360481	4	0.857
NZ_CP022163_13	13.1\|8618231\|30\|NZ_CP022163\|CRISPRCasFinder	8618231-8618260	30	MN908685	Microbacterium phage PauloDiaboli, complete genome	93379-93408	5	0.833
NZ_CP022163_14	14.1\|8668749\|28\|NZ_CP022163\|PILER-CR	8668749-8668776	28	NZ_CP015293	Rhodobacter sphaeroides strain MBTLJ-20 plasmid e, complete sequence	16251-16278	5	0.821
NZ_CP022163_13	13.1\|8618231\|30\|NZ_CP022163\|CRISPRCasFinder	8618231-8618260	30	NZ_CP012748	Paraburkholderia caribensis MBA4 plasmid unnamed, complete sequence	1538830-1538859	6	0.8
NZ_CP022163_14	14.1\|8668749\|28\|NZ_CP022163\|PILER-CR	8668749-8668776	28	AP021850	Deinococcus grandis ATCC 43672 plasmid: pDEGR-1 DNA, complete genome	130066-130093	6	0.786
NZ_CP022163_14	14.1\|8668749\|28\|NZ_CP022163\|PILER-CR	8668749-8668776	28	NZ_CP041156	Leisingera aquaemixtae strain R2C4 plasmid unnamed1, complete sequence	78328-78355	6	0.786
NZ_CP022163_14	14.1\|8668749\|28\|NZ_CP022163\|PILER-CR	8668749-8668776	28	NZ_CP045122	Rubrobacter sp. SCSIO 52915 plasmid unnamed1, complete sequence	184426-184453	6	0.786
NZ_CP022163_14	14.1\|8668749\|28\|NZ_CP022163\|PILER-CR	8668749-8668776	28	NZ_CP007130	Gemmatirosa kalamazoonesis strain KBS708 plasmid 2, complete sequence	593607-593634	6	0.786
NZ_CP022163_14	14.1\|8668749\|28\|NZ_CP022163\|PILER-CR	8668749-8668776	28	NZ_CP021127	Rhizobium sp. Kim5 plasmid pRetKim5c, complete sequence	525164-525191	6	0.786
NZ_CP022163_14	14.1\|8668749\|28\|NZ_CP022163\|PILER-CR	8668749-8668776	28	NZ_CP015090	Pelagibaca abyssi strain JLT2014 plasmid pPABY2, complete sequence	8222-8249	6	0.786
NZ_CP022163_14	14.1\|8668749\|28\|NZ_CP022163\|PILER-CR	8668749-8668776	28	NC_011961	Thermomicrobium roseum DSM 5159 plasmid unnamed, complete sequence	309537-309564	6	0.786
NZ_CP022163_14	14.1\|8668749\|28\|NZ_CP022163\|PILER-CR	8668749-8668776	28	NZ_CP019063	Rahnella sp. ERMR1:05 plasmid unnamed1, complete sequence	469992-470019	6	0.786
NZ_CP022163_14	14.1\|8668749\|28\|NZ_CP022163\|PILER-CR	8668749-8668776	28	NC_013859	Azospirillum sp. B510 plasmid pAB510e, complete sequence	200015-200042	6	0.786
NZ_CP022163_14	14.1\|8668749\|28\|NZ_CP022163\|PILER-CR	8668749-8668776	28	NZ_CP020333	Martelella mediterranea DSM 17316 strain MACL11 plasmid pMM170, complete sequence	113532-113559	6	0.786
NZ_CP022163_14	14.1\|8668749\|28\|NZ_CP022163\|PILER-CR	8668749-8668776	28	MH047631	Microbacterium phage Triscuit, complete genome	58389-58416	6	0.786
NZ_CP022163_14	14.2\|8668824\|31\|NZ_CP022163\|PILER-CR	8668824-8668854	31	NZ_CP021994	Cryobacterium sp. LW097 plasmid unnamed1	111613-111643	6	0.806
NZ_CP022163_13	13.1\|8618231\|30\|NZ_CP022163\|CRISPRCasFinder	8618231-8618260	30	NZ_CP022775	Ralstonia solanacearum strain T12 plasmid unnamed, complete sequence	227654-227683	7	0.767
NZ_CP022163_13	13.1\|8618231\|30\|NZ_CP022163\|CRISPRCasFinder	8618231-8618260	30	NZ_CP021653	Ralstonia solanacearum strain RS 488 plasmid unnamed, complete sequence	452558-452587	7	0.767
NZ_CP022163_13	13.1\|8618231\|30\|NZ_CP022163\|CRISPRCasFinder	8618231-8618260	30	NZ_CP022762	Ralstonia solanacearum strain T95 plasmid unnamed, complete sequence	231797-231826	7	0.767
NZ_CP022163_13	13.1\|8618231\|30\|NZ_CP022163\|CRISPRCasFinder	8618231-8618260	30	NZ_CP023440	Thauera sp. K11 plasmid pTX1, complete sequence	135607-135636	7	0.767
NZ_CP022163_13	13.1\|8618231\|30\|NZ_CP022163\|CRISPRCasFinder	8618231-8618260	30	NZ_CP012688	Ralstonia solanacearum strain UY031 plasmid unnamed, complete sequence	452567-452596	7	0.767
NZ_CP022163_13	13.1\|8618231\|30\|NZ_CP022163\|CRISPRCasFinder	8618231-8618260	30	NZ_CP023017	Ralstonia solanacearum strain SL3022 plasmid unnamed, complete sequence	213981-214010	7	0.767
NZ_CP022163_13	13.1\|8618231\|30\|NZ_CP022163\|CRISPRCasFinder	8618231-8618260	30	NZ_CP014703	Ralstonia solanacearum strain KACC 10722 plasmid, complete sequence	231797-231826	7	0.767
NZ_CP022163_13	13.1\|8618231\|30\|NZ_CP022163\|CRISPRCasFinder	8618231-8618260	30	NC_017575	Ralstonia solanacearum Po82 megaplasmid, complete sequence	244606-244635	7	0.767
NZ_CP022163_13	13.1\|8618231\|30\|NZ_CP022163\|CRISPRCasFinder	8618231-8618260	30	NZ_CP022771	Ralstonia solanacearum strain T51 plasmid unnamed, complete sequence	231806-231835	7	0.767
NZ_CP022163_13	13.1\|8618231\|30\|NZ_CP022163\|CRISPRCasFinder	8618231-8618260	30	NZ_CP022777	Ralstonia solanacearum strain T11 plasmid unnamed, complete sequence	231824-231853	7	0.767
NZ_CP022163_13	13.1\|8618231\|30\|NZ_CP022163\|CRISPRCasFinder	8618231-8618260	30	NZ_CP022799	Ralstonia solanacearum strain SL2064 plasmid unnamed, complete sequence	231796-231825	7	0.767
NZ_CP022163_13	13.1\|8618231\|30\|NZ_CP022163\|CRISPRCasFinder	8618231-8618260	30	NZ_CP026308	Ralstonia solanacearum strain IBSBF 2571 plasmid unnamed, complete sequence	244593-244622	7	0.767
NZ_CP022163_13	13.1\|8618231\|30\|NZ_CP022163\|CRISPRCasFinder	8618231-8618260	30	CP047139	Ralstonia solanacearum strain CFBP 8695 plasmid unnamed, complete sequence	453310-453339	7	0.767
NZ_CP022163_13	13.1\|8618231\|30\|NZ_CP022163\|CRISPRCasFinder	8618231-8618260	30	CP047137	Ralstonia solanacearum strain CFBP 8697 plasmid unnamed, complete sequence	430373-430402	7	0.767
NZ_CP022163_13	13.1\|8618231\|30\|NZ_CP022163\|CRISPRCasFinder	8618231-8618260	30	NZ_CP022764	Ralstonia solanacearum strain T82 plasmid unnamed, complete sequence	227673-227702	7	0.767
NZ_CP022163_13	13.1\|8618231\|30\|NZ_CP022163\|CRISPRCasFinder	8618231-8618260	30	NZ_CP022797	Ralstonia solanacearum strain SL2312 plasmid unnamed, complete sequence	227671-227700	7	0.767
NZ_CP022163_13	13.1\|8618231\|30\|NZ_CP022163\|CRISPRCasFinder	8618231-8618260	30	NZ_CP022758	Ralstonia solanacearum strain T101 plasmid unnamed, complete sequence	227668-227697	7	0.767
NZ_CP022163_13	13.1\|8618231\|30\|NZ_CP022163\|CRISPRCasFinder	8618231-8618260	30	NZ_CP012940	Ralstonia solanacearum strain UW163 plasmid unnamed, complete sequence	1757709-1757738	7	0.767
NZ_CP022163_13	13.1\|8618231\|30\|NZ_CP022163\|CRISPRCasFinder	8618231-8618260	30	NZ_CP012944	Ralstonia solanacearum strain IBSBF1503 plasmid unnamed, complete sequence	1774399-1774428	7	0.767
NZ_CP022163_13	13.1\|8618231\|30\|NZ_CP022163\|CRISPRCasFinder	8618231-8618260	30	NZ_CP051295	Ralstonia solanacearum strain CIAT_078 plasmid megaplasmid, complete sequence	1737635-1737664	7	0.767
NZ_CP022163_14	14.1\|8668749\|28\|NZ_CP022163\|PILER-CR	8668749-8668776	28	NZ_CP011274	Planctomyces sp. SH-PL62 plasmid pPL62-1, complete sequence	86921-86948	7	0.75
NZ_CP022163_14	14.1\|8668749\|28\|NZ_CP022163\|PILER-CR	8668749-8668776	28	NZ_CP022549	Sphingorhabdus sp. YGSMI21 plasmid unnamed, complete sequence	47668-47695	7	0.75
NZ_CP022163_14	14.1\|8668749\|28\|NZ_CP022163\|PILER-CR	8668749-8668776	28	NC_015685	Oligotropha carboxidovorans OM5 plasmid pOC167, complete sequence	116813-116840	7	0.75
NZ_CP022163_13	13.1\|8618231\|30\|NZ_CP022163\|CRISPRCasFinder	8618231-8618260	30	NC_016591	Burkholderia sp. YI23 plasmid byi_2p, complete sequence	275559-275588	8	0.733
NZ_CP022163_14	14.2\|8668824\|31\|NZ_CP022163\|PILER-CR	8668824-8668854	31	NZ_CP032346	Azospirillum brasilense strain MTCC4039 plasmid p1, complete sequence	883177-883207	8	0.742
NZ_CP022163_7	7.2\|3095823\|37\|NZ_CP022163\|CRISPRCasFinder	3095823-3095859	37	NZ_CP050953	Rhodococcus sp. DMU1 plasmid unnamed	446737-446773	9	0.757
NZ_CP022163_14	14.2\|8668824\|31\|NZ_CP022163\|PILER-CR	8668824-8668854	31	NZ_CP029776	Deinococcus actinosclerus strain Deinococcus actinosclerus SJTR plasmid unnamed2, complete sequence	146169-146199	9	0.71
NZ_CP022163_7	7.2\|3095823\|37\|NZ_CP022163\|CRISPRCasFinder	3095823-3095859	37	MK494095	Mycobacterium phage Daegal, complete genome	1049-1085	10	0.73
NZ_CP022163_7	7.2\|3095823\|37\|NZ_CP022163\|CRISPRCasFinder	3095823-3095859	37	NZ_CP035710	Sphaerotilus natans subsp. sulfidivorans strain D-507 plasmid pSna507_unt10, complete sequence	141179-141215	10	0.73
NZ_CP022163_13	13.1\|8618231\|30\|NZ_CP022163\|CRISPRCasFinder	8618231-8618260	30	NZ_CP024895	Amycolatopsis sp. AA4 plasmid unnamed1, complete sequence	294642-294671	10	0.667

1. spacer 14.1|8668749|28|NZ_CP022163|PILER-CR matches to NZ_CP028969 (Aminobacter sp. MSH1 plasmid pUSP1, complete sequence) position: , mismatch: 4, identity: 0.857

aggcgcgcgacccgctggagcgccgcgt	CRISPR spacer
cgccgggcgacccgctggagcgcggcgt	Protospacer
 * ** ***************** ****

2. spacer 14.1|8668749|28|NZ_CP022163|PILER-CR matches to NZ_CP026266 (Aminobacter sp. MSH1 plasmid pAM01, complete sequence) position: , mismatch: 4, identity: 0.857

aggcgcgcgacccgctggagcgccgcgt	CRISPR spacer
cgccgggcgacccgctggagcgcggcgt	Protospacer
 * ** ***************** ****

3. spacer 13.1|8618231|30|NZ_CP022163|CRISPRCasFinder matches to MN908685 (Microbacterium phage PauloDiaboli, complete genome) position: , mismatch: 5, identity: 0.833

-gctcggccgctctgctcggacagccccggc	CRISPR spacer
ggcgcag-cgctctgctcgaacagccacggc	Protospacer
 ** *.* ***********.****** ****

4. spacer 14.1|8668749|28|NZ_CP022163|PILER-CR matches to NZ_CP015293 (Rhodobacter sphaeroides strain MBTLJ-20 plasmid e, complete sequence) position: , mismatch: 5, identity: 0.821

aggcgcgcgacccgctggagcgccgcgt	CRISPR spacer
aggcgcgcgacctgctggagccgggcgg	Protospacer
************.********   ***

5. spacer 13.1|8618231|30|NZ_CP022163|CRISPRCasFinder matches to NZ_CP012748 (Paraburkholderia caribensis MBA4 plasmid unnamed, complete sequence) position: , mismatch: 6, identity: 0.8

gctcggccgctctgctcggacagccccggc	CRISPR spacer
ccgttgccgctctgctcgaacagcaccggc	Protospacer
 * . *************.***** *****

6. spacer 14.1|8668749|28|NZ_CP022163|PILER-CR matches to AP021850 (Deinococcus grandis ATCC 43672 plasmid: pDEGR-1 DNA, complete genome) position: , mismatch: 6, identity: 0.786

aggcgcgcgacccgctggagcgccgcgt	CRISPR spacer
ccatgcgcgacctgctggagcggcgcgt	Protospacer
  ..********.********* *****

7. spacer 14.1|8668749|28|NZ_CP022163|PILER-CR matches to NZ_CP041156 (Leisingera aquaemixtae strain R2C4 plasmid unnamed1, complete sequence) position: , mismatch: 6, identity: 0.786

aggcgcgcgacccgctggagcgccgcgt	CRISPR spacer
aggcgcgcgacgcgctggagcgggtggg	Protospacer
*********** **********    *

8. spacer 14.1|8668749|28|NZ_CP022163|PILER-CR matches to NZ_CP045122 (Rubrobacter sp. SCSIO 52915 plasmid unnamed1, complete sequence) position: , mismatch: 6, identity: 0.786

aggcgcgcgacccgctggagcgccgcgt	CRISPR spacer
gcgcgcgcgagccgctggagcgcccgct	Protospacer
. ******** *************   *

9. spacer 14.1|8668749|28|NZ_CP022163|PILER-CR matches to NZ_CP007130 (Gemmatirosa kalamazoonesis strain KBS708 plasmid 2, complete sequence) position: , mismatch: 6, identity: 0.786

aggcgcgcgacccgctggagcgccgcgt	CRISPR spacer
tcgcgcgcgagccgctcgagcgccggga	Protospacer
  ******** ***** ******** *

10. spacer 14.1|8668749|28|NZ_CP022163|PILER-CR matches to NZ_CP021127 (Rhizobium sp. Kim5 plasmid pRetKim5c, complete sequence) position: , mismatch: 6, identity: 0.786

aggcgcgcgacccgctggagcgccgcgt	CRISPR spacer
aggcgcgcgacacgctgaagcgcattgc	Protospacer
*********** *****.*****  .*.

11. spacer 14.1|8668749|28|NZ_CP022163|PILER-CR matches to NZ_CP015090 (Pelagibaca abyssi strain JLT2014 plasmid pPABY2, complete sequence) position: , mismatch: 6, identity: 0.786

aggcgcgcgacccgctggagcgccgcgt	CRISPR spacer
tggcgcgcgacctgatggagcgccagat	Protospacer
 ***********.* *********. .*

12. spacer 14.1|8668749|28|NZ_CP022163|PILER-CR matches to NC_011961 (Thermomicrobium roseum DSM 5159 plasmid unnamed, complete sequence) position: , mismatch: 6, identity: 0.786

aggcgcgcgacccgctggagcgccgcgt	CRISPR spacer
gggcgctcgacccgctggagcgtgatgt	Protospacer
.***** ***************. ..**

13. spacer 14.1|8668749|28|NZ_CP022163|PILER-CR matches to NZ_CP019063 (Rahnella sp. ERMR1:05 plasmid unnamed1, complete sequence) position: , mismatch: 6, identity: 0.786

aggcgcgcgacccgctggagcgccgcgt	CRISPR spacer
aggcgcgcgacgtgctggagcgcacccg	Protospacer
*********** .**********  *

14. spacer 14.1|8668749|28|NZ_CP022163|PILER-CR matches to NC_013859 (Azospirillum sp. B510 plasmid pAB510e, complete sequence) position: , mismatch: 6, identity: 0.786

aggcgcgcgacccgctggagcgccgcgt	CRISPR spacer
aggcgcgcgaccggctggaccgcatgat	Protospacer
************ ****** ***   .*

15. spacer 14.1|8668749|28|NZ_CP022163|PILER-CR matches to NZ_CP020333 (Martelella mediterranea DSM 17316 strain MACL11 plasmid pMM170, complete sequence) position: , mismatch: 6, identity: 0.786

aggcgcgcgacccgctggagcgccgcgt	CRISPR spacer
aggcgcgcgatacgctggagcgcgccac	Protospacer
**********. ***********  *..

16. spacer 14.1|8668749|28|NZ_CP022163|PILER-CR matches to MH047631 (Microbacterium phage Triscuit, complete genome) position: , mismatch: 6, identity: 0.786

aggcgcgcgacccgctggagcgccgcgt	CRISPR spacer
ggctgcgcggcccgctggagcaccgcga	Protospacer
.* .*****.***********.*****

17. spacer 14.2|8668824|31|NZ_CP022163|PILER-CR matches to NZ_CP021994 (Cryobacterium sp. LW097 plasmid unnamed1) position: , mismatch: 6, identity: 0.806

aagcccctcaggacggtctgcacgcctttcc	CRISPR spacer
aggtcggtcaggacgttctgcacgcccttcc	Protospacer
*.*.*  ******** **********.****

18. spacer 13.1|8618231|30|NZ_CP022163|CRISPRCasFinder matches to NZ_CP022775 (Ralstonia solanacearum strain T12 plasmid unnamed, complete sequence) position: , mismatch: 7, identity: 0.767

gctcggccgctctgctcggacagccccggc	CRISPR spacer
acgcagccgctctgctcgcacagcgccgat	Protospacer
.* *.************* ***** ***..

19. spacer 13.1|8618231|30|NZ_CP022163|CRISPRCasFinder matches to NZ_CP021653 (Ralstonia solanacearum strain RS 488 plasmid unnamed, complete sequence) position: , mismatch: 7, identity: 0.767

gctcggccgctctgctcggacagccccggc	CRISPR spacer
acgcagccgctctgctcgcacagcgccgag	Protospacer
.* *.************* ***** ***.

20. spacer 13.1|8618231|30|NZ_CP022163|CRISPRCasFinder matches to NZ_CP022762 (Ralstonia solanacearum strain T95 plasmid unnamed, complete sequence) position: , mismatch: 7, identity: 0.767

gctcggccgctctgctcggacagccccggc	CRISPR spacer
acgcagccgctctgctcgcacagcgccgat	Protospacer
.* *.************* ***** ***..

21. spacer 13.1|8618231|30|NZ_CP022163|CRISPRCasFinder matches to NZ_CP023440 (Thauera sp. K11 plasmid pTX1, complete sequence) position: , mismatch: 7, identity: 0.767

gctcggccgctctgctcggacagccccggc	CRISPR spacer
gccgcgccgctctgctcggacggcaccgta	Protospacer
**.  ****************.** ***

22. spacer 13.1|8618231|30|NZ_CP022163|CRISPRCasFinder matches to NZ_CP012688 (Ralstonia solanacearum strain UY031 plasmid unnamed, complete sequence) position: , mismatch: 7, identity: 0.767

gctcggccgctctgctcggacagccccggc	CRISPR spacer
acgcagccgctctgctcgcacagcgccgag	Protospacer
.* *.************* ***** ***.

23. spacer 13.1|8618231|30|NZ_CP022163|CRISPRCasFinder matches to NZ_CP023017 (Ralstonia solanacearum strain SL3022 plasmid unnamed, complete sequence) position: , mismatch: 7, identity: 0.767

gctcggccgctctgctcggacagccccggc	CRISPR spacer
acgcagccgctctgctcgcacagcgccgat	Protospacer
.* *.************* ***** ***..

24. spacer 13.1|8618231|30|NZ_CP022163|CRISPRCasFinder matches to NZ_CP014703 (Ralstonia solanacearum strain KACC 10722 plasmid, complete sequence) position: , mismatch: 7, identity: 0.767

gctcggccgctctgctcggacagccccggc	CRISPR spacer
acgcagccgctctgctcgcacagcgccgat	Protospacer
.* *.************* ***** ***..

25. spacer 13.1|8618231|30|NZ_CP022163|CRISPRCasFinder matches to NC_017575 (Ralstonia solanacearum Po82 megaplasmid, complete sequence) position: , mismatch: 7, identity: 0.767

gctcggccgctctgctcggacagccccggc	CRISPR spacer
acgcagccgctctgctcgcacagcgccgag	Protospacer
.* *.************* ***** ***.

26. spacer 13.1|8618231|30|NZ_CP022163|CRISPRCasFinder matches to NZ_CP022771 (Ralstonia solanacearum strain T51 plasmid unnamed, complete sequence) position: , mismatch: 7, identity: 0.767

gctcggccgctctgctcggacagccccggc	CRISPR spacer
acgcagccgctctgctcgcacagcgccgat	Protospacer
.* *.************* ***** ***..

27. spacer 13.1|8618231|30|NZ_CP022163|CRISPRCasFinder matches to NZ_CP022777 (Ralstonia solanacearum strain T11 plasmid unnamed, complete sequence) position: , mismatch: 7, identity: 0.767

gctcggccgctctgctcggacagccccggc	CRISPR spacer
acgcagccgctctgctcgcacagcgccgat	Protospacer
.* *.************* ***** ***..

28. spacer 13.1|8618231|30|NZ_CP022163|CRISPRCasFinder matches to NZ_CP022799 (Ralstonia solanacearum strain SL2064 plasmid unnamed, complete sequence) position: , mismatch: 7, identity: 0.767

gctcggccgctctgctcggacagccccggc	CRISPR spacer
acgcagccgctctgctcgcacagcgccgat	Protospacer
.* *.************* ***** ***..

29. spacer 13.1|8618231|30|NZ_CP022163|CRISPRCasFinder matches to NZ_CP026308 (Ralstonia solanacearum strain IBSBF 2571 plasmid unnamed, complete sequence) position: , mismatch: 7, identity: 0.767

gctcggccgctctgctcggacagccccggc	CRISPR spacer
acgcagccgctctgctcgcacagcgccgag	Protospacer
.* *.************* ***** ***.

30. spacer 13.1|8618231|30|NZ_CP022163|CRISPRCasFinder matches to CP047139 (Ralstonia solanacearum strain CFBP 8695 plasmid unnamed, complete sequence) position: , mismatch: 7, identity: 0.767

gctcggccgctctgctcggacagccccggc	CRISPR spacer
acgcagccgctctgctcgcacagcgccgag	Protospacer
.* *.************* ***** ***.

31. spacer 13.1|8618231|30|NZ_CP022163|CRISPRCasFinder matches to CP047137 (Ralstonia solanacearum strain CFBP 8697 plasmid unnamed, complete sequence) position: , mismatch: 7, identity: 0.767

gctcggccgctctgctcggacagccccggc	CRISPR spacer
acgcagccgctctgctcgcacagcgccgag	Protospacer
.* *.************* ***** ***.

32. spacer 13.1|8618231|30|NZ_CP022163|CRISPRCasFinder matches to NZ_CP022764 (Ralstonia solanacearum strain T82 plasmid unnamed, complete sequence) position: , mismatch: 7, identity: 0.767

gctcggccgctctgctcggacagccccggc	CRISPR spacer
acgcagccgctctgctcgcacagcgccgat	Protospacer
.* *.************* ***** ***..

33. spacer 13.1|8618231|30|NZ_CP022163|CRISPRCasFinder matches to NZ_CP022797 (Ralstonia solanacearum strain SL2312 plasmid unnamed, complete sequence) position: , mismatch: 7, identity: 0.767

gctcggccgctctgctcggacagccccggc	CRISPR spacer
acgcagccgctctgctcgcacagcgccgat	Protospacer
.* *.************* ***** ***..

34. spacer 13.1|8618231|30|NZ_CP022163|CRISPRCasFinder matches to NZ_CP022758 (Ralstonia solanacearum strain T101 plasmid unnamed, complete sequence) position: , mismatch: 7, identity: 0.767

gctcggccgctctgctcggacagccccggc	CRISPR spacer
acgcagccgctctgctcgcacagcgccgat	Protospacer
.* *.************* ***** ***..

35. spacer 13.1|8618231|30|NZ_CP022163|CRISPRCasFinder matches to NZ_CP012940 (Ralstonia solanacearum strain UW163 plasmid unnamed, complete sequence) position: , mismatch: 7, identity: 0.767

gctcggccgctctgctcggacagccccggc	CRISPR spacer
acgcagccgctctgctcgcacagcgccgag	Protospacer
.* *.************* ***** ***.

36. spacer 13.1|8618231|30|NZ_CP022163|CRISPRCasFinder matches to NZ_CP012944 (Ralstonia solanacearum strain IBSBF1503 plasmid unnamed, complete sequence) position: , mismatch: 7, identity: 0.767

gctcggccgctctgctcggacagccccggc	CRISPR spacer
acgcagccgctctgctcgcacagcgccgag	Protospacer
.* *.************* ***** ***.

37. spacer 13.1|8618231|30|NZ_CP022163|CRISPRCasFinder matches to NZ_CP051295 (Ralstonia solanacearum strain CIAT_078 plasmid megaplasmid, complete sequence) position: , mismatch: 7, identity: 0.767

gctcggccgctctgctcggacagccccggc	CRISPR spacer
acgcagccgctctgctcgcacagcgccgag	Protospacer
.* *.************* ***** ***.

38. spacer 14.1|8668749|28|NZ_CP022163|PILER-CR matches to NZ_CP011274 (Planctomyces sp. SH-PL62 plasmid pPL62-1, complete sequence) position: , mismatch: 7, identity: 0.75

aggcgcgcgacccgctggagcgccgcgt	CRISPR spacer
tcggccgcgacccgctggagcgcggccg	Protospacer
  *  ****************** **

39. spacer 14.1|8668749|28|NZ_CP022163|PILER-CR matches to NZ_CP022549 (Sphingorhabdus sp. YGSMI21 plasmid unnamed, complete sequence) position: , mismatch: 7, identity: 0.75

aggcgcgcgacccgctggagcgccgcgt	CRISPR spacer
tcgcgcgcgaaccgcttgagcgccggtg	Protospacer
  ******** ***** ********

40. spacer 14.1|8668749|28|NZ_CP022163|PILER-CR matches to NC_015685 (Oligotropha carboxidovorans OM5 plasmid pOC167, complete sequence) position: , mismatch: 7, identity: 0.75

aggcgcgcgacccgctggagcgccgcgt	CRISPR spacer
cagcgtgcgacccgctggaccgccggcg	Protospacer
 .***.************* *****

41. spacer 13.1|8618231|30|NZ_CP022163|CRISPRCasFinder matches to NC_016591 (Burkholderia sp. YI23 plasmid byi_2p, complete sequence) position: , mismatch: 8, identity: 0.733

gctcggccgctctgctcggacagccccggc	CRISPR spacer
gctcggccgctctgctcgaagaggcttcag	Protospacer
******************.* ** *.. .

42. spacer 14.2|8668824|31|NZ_CP022163|PILER-CR matches to NZ_CP032346 (Azospirillum brasilense strain MTCC4039 plasmid p1, complete sequence) position: , mismatch: 8, identity: 0.742

aagcccctcaggacggtctgcacgcctttcc	CRISPR spacer
gcgcccatcaggacggtctggacgcgctcgc	Protospacer
. **** ************* **** .*. *

43. spacer 7.2|3095823|37|NZ_CP022163|CRISPRCasFinder matches to NZ_CP050953 (Rhodococcus sp. DMU1 plasmid unnamed) position: , mismatch: 9, identity: 0.757

gccgccctgcgcgacgccgtcctcgaaggcgccaact--	CRISPR spacer
cgcacactgcgcgacggcgtcctcgaagacgc--gctgg	Protospacer
  *.* ********** ***********.***  .**

44. spacer 14.2|8668824|31|NZ_CP022163|PILER-CR matches to NZ_CP029776 (Deinococcus actinosclerus strain Deinococcus actinosclerus SJTR plasmid unnamed2, complete sequence) position: , mismatch: 9, identity: 0.71

aagcccctcaggacggtctgcacgcctttcc	CRISPR spacer
tgctcccccaggacggtctgcacgccgggac	Protospacer
 . .***.******************    *

45. spacer 7.2|3095823|37|NZ_CP022163|CRISPRCasFinder matches to MK494095 (Mycobacterium phage Daegal, complete genome) position: , mismatch: 10, identity: 0.73

gccgccctgcgcgacgccgtcctcgaaggcgccaact	CRISPR spacer
gccgccctgcgcgacgccgtcgccgaagcgattgaag	Protospacer
********************* .*****  ....*

46. spacer 7.2|3095823|37|NZ_CP022163|CRISPRCasFinder matches to NZ_CP035710 (Sphaerotilus natans subsp. sulfidivorans strain D-507 plasmid pSna507_unt10, complete sequence) position: , mismatch: 10, identity: 0.73

gccgccctgcgcgacgccgtcctcgaaggcgccaact	CRISPR spacer
ttcccagtgcgcgacgccggcctcgaaggcaccacgc	Protospacer
 .* *  ************ **********.***  .

47. spacer 13.1|8618231|30|NZ_CP022163|CRISPRCasFinder matches to NZ_CP024895 (Amycolatopsis sp. AA4 plasmid unnamed1, complete sequence) position: , mismatch: 10, identity: 0.667

gctcggccgctctgctcggacagccccggc	CRISPR spacer
ttctccgcgctcttctcggacagccccgcg	Protospacer
 ...   ****** **************

Prophage detection

Region

Region Position

Protein_number

Hit_taxonomy

Key_proteins

Att_site

Prophage annotation

DBSCAN-SWA_1

188269 : 263670

Erwinia_phage(11.11%)

protease,tRNA,plate

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

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_095975636.1\|188269_189670_-\|protease	ATP-dependent protease ATPase subunit HslU	A0A2H5BJT2	Erwinia_phage	2.0e-41	28.7
WP_095975637.1\|189682_190210_-\|protease	ATP-dependent protease subunit HslV	NA	NA	NA	NA
WP_095975638.1\|190284_191193_-	tyrosine recombinase XerC	W8EHC2	Mycobacterium_phage	1.1e-14	27.8
WP_095982489.1\|191345_191693_+	PilZ domain-containing protein	NA	NA	NA	NA
WP_095982490.1\|191699_192638_-	PhcB	NA	NA	NA	NA
WP_095975639.1\|192824_193373_+	DUF2378 family protein	NA	NA	NA	NA
WP_095975640.1\|193389_194994_-	gliding motility protein	NA	NA	NA	NA
WP_095975641.1\|194990_196337_-\|tRNA	methylenetetrahydrofolate--tRNA-(uracil(54)- C(5))-methyltransferase (FADH(2)-oxidizing) TrmFO	NA	NA	NA	NA
WP_095975642.1\|196588_196978_+	TraR/DksA family transcriptional regulator	NA	NA	NA	NA
WP_095975643.1\|197027_199649_-	type I DNA topoisomerase	A0A1V0SCS0	Indivirus	1.2e-103	38.2
WP_095975644.1\|199657_200776_-	DNA-processing protein DprA	NA	NA	NA	NA
WP_095975645.1\|200935_202162_-	LysM peptidoglycan-binding domain-containing protein	G3MBQ1	Bacillus_virus	2.9e-07	39.7
WP_095975646.1\|202186_202909_-	tetratricopeptide repeat protein	NA	NA	NA	NA
WP_095975647.1\|203076_203844_-	peptidoglycan editing factor PgeF	NA	NA	NA	NA
WP_095975648.1\|204015_205923_+	diguanylate cyclase	A0A127AWB9	Bacillus_phage	5.8e-15	35.4
WP_095975649.1\|205936_207388_-	trypsin-like peptidase domain-containing protein	A0A1B1IT49	uncultured_Mediterranean_phage	8.6e-27	32.3
WP_095975650.1\|207516_209106_-	DUF1957 domain-containing protein	NA	NA	NA	NA
WP_095975651.1\|209116_210700_-	DUF4912 domain-containing protein	NA	NA	NA	NA
WP_095975652.1\|210833_212945_+	glycosyltransferase	NA	NA	NA	NA
WP_095975653.1\|213070_217375_+	response regulator	NA	NA	NA	NA
WP_095982491.1\|217420_217639_-	hypothetical protein	NA	NA	NA	NA
WP_095975654.1\|217823_218765_+	MoxR family ATPase	NA	NA	NA	NA
WP_095975655.1\|218864_219812_+	branched-chain amino acid transaminase	NA	NA	NA	NA
WP_095975656.1\|219883_221218_+	AAA family ATPase	NA	NA	NA	NA
WP_095975657.1\|221351_222188_+	Fic family protein	NA	NA	NA	NA
WP_095975658.1\|222330_223458_+	bifunctional oligoribonuclease/PAP phosphatase NrnA	NA	NA	NA	NA
WP_095975659.1\|223454_224603_+	cysteine desulfurase	H7BUW1	unidentified_phage	6.1e-36	38.6
WP_170115419.1\|224606_224774_-	hypothetical protein	NA	NA	NA	NA
WP_095975661.1\|224879_225821_-	serine/threonine protein kinase	A0A0U2U263	Niemeyer_virus	3.0e-12	25.9
WP_157774690.1\|225817_226738_-	tetratricopeptide repeat protein	NA	NA	NA	NA
WP_095975663.1\|227090_227714_+	5-formyltetrahydrofolate cyclo-ligase	NA	NA	NA	NA
WP_095975664.1\|227725_228502_+	TIGR00282 family metallophosphoesterase	NA	NA	NA	NA
WP_095975665.1\|228564_229827_+\|tRNA	tyrosine--tRNA ligase	NA	NA	NA	NA
WP_095975666.1\|229913_231857_+	sodium:proton antiporter	NA	NA	NA	NA
WP_095975667.1\|231829_232858_+	EndoU domain-containing protein	NA	NA	NA	NA
WP_095975668.1\|232900_233593_+	SOS response-associated peptidase	V9IQW7	Stenotrophomonas_phage	1.1e-35	41.7
WP_095975669.1\|233596_234319_-	hypothetical protein	NA	NA	NA	NA
WP_095975670.1\|234330_234972_-	RlmE family RNA methyltransferase	NA	NA	NA	NA
WP_157774691.1\|235048_235462_+	hypothetical protein	NA	NA	NA	NA
WP_095975671.1\|235465_235753_+	hypothetical protein	NA	NA	NA	NA
WP_095975672.1\|235756_236515_-	xanthine dehydrogenase accessory protein XdhC	NA	NA	NA	NA
WP_095975673.1\|236602_237604_+	DUF3616 domain-containing protein	NA	NA	NA	NA
WP_170115421.1\|237652_239206_-	hypothetical protein	NA	NA	NA	NA
WP_157824001.1\|239328_241407_+	PQQ-like beta-propeller repeat protein	NA	NA	NA	NA
WP_157774693.1\|241612_246718_+	Ig-like domain repeat protein	NA	NA	NA	NA
WP_095975678.1\|246765_248574_-	OmpA family protein	NA	NA	NA	NA
WP_095982492.1\|248841_249411_+	type VI secretion system lipoprotein TssJ	NA	NA	NA	NA
WP_095975679.1\|249407_250775_+\|plate	type VI secretion system baseplate subunit TssK	NA	NA	NA	NA
WP_095975680.1\|250786_251494_+	DotU family type IV/VI secretion system protein	NA	NA	NA	NA
WP_095982493.1\|251493_255162_+	type VI secretion system membrane subunit TssM	NA	NA	NA	NA
WP_095975681.1\|255161_256103_+	type VI secretion system-associated protein TagF	NA	NA	NA	NA
WP_095975682.1\|256099_257740_+	type VI secretion system protein TssA	NA	NA	NA	NA
WP_095975683.1\|257819_258332_+	type VI secretion system contractile sheath small subunit	NA	NA	NA	NA
WP_095975684.1\|258355_259843_+	type VI secretion system contractile sheath large subunit	NA	NA	NA	NA
WP_095975685.1\|259950_260442_+	type VI secretion system tube protein Hcp	NA	NA	NA	NA
WP_095975686.1\|260505_260904_+\|plate	type VI secretion system baseplate subunit TssE	NA	NA	NA	NA
WP_095975687.1\|260914_262663_+\|plate	type VI secretion system baseplate subunit TssF	NA	NA	NA	NA
WP_170115422.1\|262626_263670_+\|plate	type VI secretion system baseplate subunit TssG	NA	NA	NA	NA

DBSCAN-SWA_2

391391 : 416474

Enterobacteria_phage(50.0%)

transposase

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_157774705.1\|391391_391748_-\|transposase	transposase	NA	NA	NA	NA
WP_095975768.1\|391768_393286_-\|transposase	IS66 family transposase	NA	NA	NA	NA
WP_095982516.1\|393264_393612_-	IS66 family insertion sequence element accessory protein TnpB	NA	NA	NA	NA
WP_095975769.1\|393659_394058_-\|transposase	transposase	NA	NA	NA	NA
WP_157774706.1\|394349_395063_+\|transposase	transposase	NA	NA	NA	NA
WP_095975772.1\|395251_396193_-	hypothetical protein	NA	NA	NA	NA
WP_095975773.1\|396189_397905_-	AAA family ATPase	Q2P9X8	Enterobacteria_phage	1.2e-16	20.7
WP_179956366.1\|397898_399080_-	restriction endonuclease subunit S	NA	NA	NA	NA
WP_095975774.1\|399076_400585_-	SAM-dependent DNA methyltransferase	J7I0U9	Acinetobacter_phage	1.5e-34	30.2
WP_095982518.1\|400581_403998_-	DEAD/DEAH box helicase family protein	NA	NA	NA	NA
WP_170115696.1\|404050_405664_-	sigma 54-interacting transcriptional regulator	NA	NA	NA	NA
WP_157774707.1\|405629_405845_-	hypothetical protein	NA	NA	NA	NA
WP_095975777.1\|406940_410243_+	hypothetical protein	NA	NA	NA	NA
WP_095975778.1\|410718_413544_-	SEC-C domain-containing protein	NA	NA	NA	NA
WP_095975779.1\|414184_414583_+\|transposase	transposase	NA	NA	NA	NA
WP_095982516.1\|414630_414978_+	IS66 family insertion sequence element accessory protein TnpB	NA	NA	NA	NA
WP_095975768.1\|414956_416474_+\|transposase	IS66 family transposase	NA	NA	NA	NA

DBSCAN-SWA_3

1861247 : 1924460

Bacillus_phage(20.0%)

protease,transposase

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_095976830.1\|1861247_1862120_-\|protease	M48 family metalloprotease	NA	NA	NA	NA
WP_095976831.1\|1863063_1863477_+	DoxX family protein	NA	NA	NA	NA
WP_095976832.1\|1863546_1865973_-	sel1 repeat family protein	NA	NA	NA	NA
WP_170115460.1\|1866332_1866473_-	hypothetical protein	NA	NA	NA	NA
WP_170115461.1\|1867015_1868206_+\|transposase	ISAs1 family transposase	NA	NA	NA	NA
WP_157774808.1\|1868641_1871356_-	ATP-binding protein	NA	NA	NA	NA
WP_095982646.1\|1872030_1872282_+	helix-turn-helix domain-containing protein	NA	NA	NA	NA
WP_170115462.1\|1872205_1872955_+\|transposase	IS630 family transposase	NA	NA	NA	NA
WP_157774809.1\|1873601_1873961_-\|transposase	transposase	NA	NA	NA	NA
WP_157774810.1\|1874008_1874413_-\|transposase	transposase family protein	NA	NA	NA	NA
WP_095976836.1\|1874752_1875223_+	NUDIX hydrolase	NA	NA	NA	NA
WP_095976837.1\|1875379_1876738_+	hypothetical protein	NA	NA	NA	NA
WP_095976838.1\|1876867_1881397_+	hypothetical protein	NA	NA	NA	NA
WP_095976839.1\|1881505_1882087_+	hypothetical protein	NA	NA	NA	NA
WP_095976840.1\|1882096_1883200_+	NAD(P)/FAD-dependent oxidoreductase	NA	NA	NA	NA
WP_095976841.1\|1883221_1883614_-	hypothetical protein	NA	NA	NA	NA
WP_095976842.1\|1883827_1884451_-	YceI family protein	NA	NA	NA	NA
WP_095976843.1\|1884646_1886287_+	sigma-54-dependent Fis family transcriptional regulator	NA	NA	NA	NA
WP_095976844.1\|1886299_1887028_-	DUF1751 domain-containing protein	NA	NA	NA	NA
WP_095976845.1\|1887196_1887394_-	hypothetical protein	NA	NA	NA	NA
WP_095982647.1\|1887548_1887764_-	hypothetical protein	NA	NA	NA	NA
WP_095976846.1\|1887793_1888990_-	acetyl-CoA C-acetyltransferase	NA	NA	NA	NA
WP_095976847.1\|1889069_1889729_-	hypothetical protein	NA	NA	NA	NA
WP_095976848.1\|1889887_1890598_+	trypsin-like peptidase domain-containing protein	NA	NA	NA	NA
WP_095976849.1\|1890739_1891123_+	response regulator	W8CYM9	Bacillus_phage	3.8e-06	30.5
WP_095982648.1\|1891205_1892843_+	L-glutamate gamma-semialdehyde dehydrogenase	NA	NA	NA	NA
WP_095976850.1\|1892857_1893328_-	hypothetical protein	NA	NA	NA	NA
WP_095976851.1\|1893338_1894406_-	esterase	NA	NA	NA	NA
WP_095976852.1\|1894582_1896424_+	5'-nucleotidase C-terminal domain-containing protein	NA	NA	NA	NA
WP_095976853.1\|1896433_1899175_-	sensor histidine kinase	NA	NA	NA	NA
WP_095976854.1\|1899328_1900045_+	purine-nucleoside phosphorylase	NA	NA	NA	NA
WP_157774812.1\|1900038_1901583_-	sugar transferase	NA	NA	NA	NA
WP_095976856.1\|1902100_1903390_+	O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase	A0A0B5JD48	Pandoravirus	5.5e-17	25.9
WP_095976857.1\|1903418_1905782_+	alpha/beta fold hydrolase	NA	NA	NA	NA
WP_095976858.1\|1905785_1906859_-	potassium channel protein	NA	NA	NA	NA
WP_095982649.1\|1906929_1908138_-	twin-arginine translocase subunit TatC	A0A1B1IVR7	uncultured_Mediterranean_phage	3.6e-18	36.7
WP_179956397.1\|1908174_1908558_-	twin-arginine translocase subunit TatB	NA	NA	NA	NA
WP_095982650.1\|1908678_1910700_-	HAMP domain-containing protein	A0A2H4J162	uncultured_Caudovirales_phage	1.0e-17	39.7
WP_095976859.1\|1910904_1911939_+	histone deacetylase	A0A2K9KZC4	Tupanvirus	2.4e-55	37.4
WP_095976860.1\|1911966_1912509_+	hypothetical protein	NA	NA	NA	NA
WP_095976861.1\|1912527_1913205_+	glutathione S-transferase N-terminal domain-containing protein	NA	NA	NA	NA
WP_095976862.1\|1914688_1915453_+	SDR family NAD(P)-dependent oxidoreductase	NA	NA	NA	NA
WP_095976863.1\|1915449_1918023_-	PBP1A family penicillin-binding protein	NA	NA	NA	NA
WP_095976864.1\|1918019_1918985_-	RluA family pseudouridine synthase	NA	NA	NA	NA
WP_095976865.1\|1919028_1920504_+	pentapeptide repeat-containing protein	NA	NA	NA	NA
WP_095976866.1\|1920520_1921498_-	MBL fold metallo-hydrolase	NA	NA	NA	NA
WP_170115463.1\|1921604_1922531_-	EamA family transporter	NA	NA	NA	NA
WP_157774813.1\|1922692_1923247_+	hypothetical protein	NA	NA	NA	NA
WP_179956398.1\|1923390_1923912_+	helix-turn-helix domain-containing protein	NA	NA	NA	NA
WP_157774815.1\|1923917_1924460_+\|transposase	IS630 family transposase	NA	NA	NA	NA

DBSCAN-SWA_4

6736935 : 6752535

Moraxella_phage(100.0%)

transposase

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_095980339.1\|6736935_6738087_-\|transposase	IS4 family transposase	NA	NA	NA	NA
WP_157775548.1\|6738215_6738380_+	hypothetical protein	NA	NA	NA	NA
WP_157775551.1\|6738376_6739162_-	hypothetical protein	NA	NA	NA	NA
WP_095980340.1\|6739395_6740262_-	transcriptional regulator	NA	NA	NA	NA
WP_095980341.1\|6740282_6741341_-	ATP-binding protein	A0A0R6PCP6	Moraxella_phage	1.9e-52	41.3
WP_095980342.1\|6741367_6741685_-	hypothetical protein	NA	NA	NA	NA
WP_095980343.1\|6741690_6742173_-	hypothetical protein	NA	NA	NA	NA
WP_095980344.1\|6742179_6742659_-	hypothetical protein	NA	NA	NA	NA
WP_170115606.1\|6742934_6744425_-\|transposase	IS66 family transposase	NA	NA	NA	NA
WP_157775558.1\|6744467_6744761_-	IS66 family insertion sequence element accessory protein TnpB	NA	NA	NA	NA
WP_095980347.1\|6744953_6746267_-\|transposase	IS4 family transposase	NA	NA	NA	NA
WP_095976365.1\|6746479_6747691_-\|transposase	ISAs1 family transposase	NA	NA	NA	NA
WP_095980348.1\|6748214_6748613_-\|transposase	transposase	NA	NA	NA	NA
WP_157775561.1\|6748729_6749119_+	DUF2381 family protein	NA	NA	NA	NA
WP_095980350.1\|6749166_6749796_-	ankyrin repeat domain-containing protein	NA	NA	NA	NA
WP_095980351.1\|6749799_6750651_-	hypothetical protein	NA	NA	NA	NA
WP_095982608.1\|6751221_6752535_+\|transposase	IS4 family transposase	NA	NA	NA	NA

DBSCAN-SWA_5

6945244 : 6957893

Bodo_saltans_virus(50.0%)

transposase

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_095980494.1\|6945244_6945451_+\|transposase	transposase	NA	NA	NA	NA
WP_157775601.1\|6946927_6947749_+	hypothetical protein	NA	NA	NA	NA
WP_157775604.1\|6947761_6948859_+	DUF2075 domain-containing protein	NA	NA	NA	NA
WP_095983073.1\|6948858_6951069_+	alpha-ketoglutarate-dependent dioxygenase AlkB	A0A2H4UTW3	Bodo_saltans_virus	1.8e-23	35.5
WP_095983074.1\|6951745_6952951_+\|transposase	IS701 family transposase	NA	NA	NA	NA
WP_157775607.1\|6953483_6954362_+\|transposase	IS66 family transposase zinc-finger binding domain-containing protein	NA	NA	NA	NA
WP_157775611.1\|6954374_6955346_+\|transposase	transposase family protein	NA	NA	NA	NA
WP_157775614.1\|6955584_6956382_+\|transposase	IS5 family transposase	A0A0N9SHJ4	Paenibacillus_phage	5.1e-05	28.6
WP_095982807.1\|6956579_6957893_-\|transposase	IS4 family transposase	NA	NA	NA	NA

DBSCAN-SWA_6

9763797 : 9770088

Enterobacteria_phage(33.33%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_095982364.1\|9763797_9765399_+	ATP-binding cassette domain-containing protein	A0A2K9L0W2	Tupanvirus	9.1e-54	26.7
WP_095982365.1\|9765448_9766483_-	YihY/virulence factor BrkB family protein	H9YQA7	environmental_Halophage	1.4e-07	30.0
WP_095982366.1\|9766615_9767167_-	dTDP-4-dehydrorhamnose 3,5-epimerase	I7HJC4	Enterobacteria_phage	3.0e-49	52.6
WP_095982367.1\|9767163_9768045_-	glucose-1-phosphate thymidylyltransferase RfbA	K7QKA7	Escherichia_phage	6.0e-100	59.6
WP_095982368.1\|9768151_9769051_-	SDR family oxidoreductase	A0A291LA50	Escherichia_phage	1.5e-13	25.2
WP_095982369.1\|9769068_9770088_-	dTDP-glucose 4,6-dehydratase	I7HTA3	Enterobacteria_phage	1.3e-82	48.5

DBSCAN-SWA_7

9854654 : 9862208

Burkholderia_phage(100.0%)

transposase,integrase

attL 9854254:9854272|attR 9863099:9863117

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
9854254:9854272	attL	NA	NA	NA	NA
WP_157823993.1\|9854654_9855473_-\|transposase	IS66 family transposase	NA	NA	NA	NA
WP_095977357.1\|9855502_9856963_+\|transposase	IS66 family transposase	NA	NA	NA	NA
WP_157823994.1\|9857223_9857811_+\|transposase	transposase family protein	NA	NA	NA	NA
WP_157823995.1\|9857959_9859327_+\|integrase,transposase	DDE-type integrase/transposase/recombinase	NA	NA	NA	NA
WP_095982433.1\|9859323_9860136_+	AAA family ATPase	Q6QIE1	Burkholderia_phage	3.0e-05	26.2
WP_095982434.1\|9860137_9860428_+	hypothetical protein	NA	NA	NA	NA
WP_095982435.1\|9860559_9861420_-\|transposase	transposase	NA	NA	NA	NA
WP_095982436.1\|9861435_9861816_-	IS66 family insertion sequence element accessory protein TnpB	NA	NA	NA	NA
WP_157823996.1\|9861809_9862208_-\|transposase	transposase	NA	NA	NA	NA
9863099:9863117	attR	NA	NA	NA	NA

Anti-CRISPR protein detection

Acr_ID: NZ_CP022163.1|WP_170115419.1|224606_224774_-|hypothetical-protein

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Acr ID

Acr position

Acr size

Homology with known anti

Neighbor HTH/AcRanker

Neighbor Aca

In prophage

Protospacer in prophage

NZ_CP022163.1|WP_170115419.1|224606_224774_-|hypothetical-protein

224606_224774_-

55 aa aa

188269-263670

yes

CRISPR ID	CRISPR type	Spacer info	Spacer location	Spacer length	Protospacer location	Mismatch
NZ_CP022163_1	Orphan	1.1\|214999\|67\|NZ_CP022163\|PILER-CR	214999-215065	67	215230-215296	8

1. spacer 1.1|214999|67|NZ_CP022163|PILER-CR matches to NZ_CP022163 position: 215230-215296, mismatch: 8

ccaggccaccctcgccgagacgcagacgacgctcgcctccaccgaggccaagctctcggc	CRISPR spacer
ccaggccaccctcaccgagacgcagacgacgctcgcctccaccgaggccaagctctcggc	Protospacer
*************.**********************************************

Overview of predicted results

Overview of the results

Cas Category Instructions

Results visualization

1. NZ_CP022163

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CRISPR-Cas detection and classification

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Self-targeting detection

MGE targeting detection<

Prophage detection

Anti-CRISPR protein detection

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