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_CP043451	Mucilaginibacter rubeus strain P2 chromosome, complete genome	9 crisprs	csa3,DEDDh,RT,cas3,WYL,PD-DExK,PrimPol	0	0	1	0

Results visualization

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CRISPR-Cas detection and classification

Crispr_ID: NZ_CP043451_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP043451_1

162355-162438

Orphan

Consensus_repeat	Method
AGTAGCAGTTGGCAGTGGCAGTT	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP043451_1

>merge|NZ_CP043451|1|162355-162438|CRISPRCasFinder
TGCAGTAAGTAGCAGTAGCAGTTGGCAGTGGCAGTTTGTATAGAGCGGCAATTTTTCAGTAAGTAGCAGTTGGCAGTGGCAGTT

>NZ_CP043451|1|1|162355-162438|CRISPRCasFinder
TGCAGTAAGTAGCAGTAGCAGTT	GGCAGTGGCAGTTTGTATAGAGCGGCAATTTTTCAGTA
AGTAGCAGTTGGCAGTGGCAGTT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP043451.1\|WP_112653584.1\|172684_173182_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043451.1\|WP_112653577.1\|161989_162349_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043451.1\|WP_112683133.1\|157820_158054_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043451.1\|WP_112653580.1\|166211_167384_-\|RsmB/NOP-family-class-I-SAM-dependent-RNA-methyltransferase	unknown	unknown	gnl\|CDD\|223222
NZ_CP043451.1\|WP_112653579.1\|164307_165471_+\|MFS-transporter	unknown	unknown	gnl\|CDD\|340888
NZ_CP043451.1\|WP_112657833.1\|156734_156986_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043451.1\|WP_112658802.1\|159823_160837_+\|IS1595-family-transposase	unknown	unknown	gnl\|CDD\|372298
NZ_CP043451.1\|WP_112658804.1\|161401_161818_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043451.1\|WP_112658800.1\|157657_157849_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043451.1\|WP_112657835.1\|157122_157461_-\|single-stranded-DNA-binding-protein	unknown	unknown	gnl\|CDD\|239942
NZ_CP043451.1\|WP_112657831.1\|155821_156439_+\|class-I-SAM-dependent-methyltransferase	unknown	unknown	gnl\|CDD\|379312
NZ_CP043451.1\|WP_112653582.1\|170449_171415_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|319899
NZ_CP043451.1\|WP_112653578.1\|162653_164210_+\|amino-acid-permease	unknown	unknown	gnl\|CDD\|129987
NZ_CP043451.1\|WP_022833680.1\|159139_159619_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043451.1\|WP_090528388.1\|171411_171732_-\|winged-helix-turn-helix-transcriptional-regulator	unknown	unknown	gnl\|CDD\|238042
NZ_CP043451.1\|WP_022833677.1\|160950_161268_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043451.1\|WP_146750442.1\|167380_168634_-\|amino-acid-ABC-transporter-substrate-binding-protein	unknown	unknown	gnl\|CDD\|380492
NZ_CP043451.1\|WP_090529629.1\|168590_170120_-\|glutamine-hydrolyzing-GMP-synthase	unknown	unknown	gnl\|CDD\|234614
NZ_CP043451.1\|WP_090528400.1\|165483_166056_+\|MarC-family-protein	unknown	unknown	gnl\|CDD\|280149
NZ_CP043451.1\|WP_112653583.1\|172019_172574_-\|DUF1572-family-protein	unknown	unknown	gnl\|CDD\|311521

Protein	Function_ID	Function_description	E-value
NZ_CP043451.1\|WP_112653580.1\|166211_167384_-\|RsmB/NOP-family-class-I-SAM-dependent-RNA-methyltransferase	gnl\|CDD\|223222	COG0144, Sun, tRNA and rRNA cytosine-C5-methylases [Translation, ribosomal structure and biogenesis].	8.69597e-31
NZ_CP043451.1\|WP_112653579.1\|164307_165471_+\|MFS-transporter	gnl\|CDD\|340888	cd17330, MFS_SLC46_TetA_like, Eukaryotic Solute carrier 46 (SLC46) family, Bacterial Tetracycline resistance proteins, and similar proteins of the Major Facilitator Superfamily of transporters. This family is composed of the eukaryotic proteins MFSD9, MFSD10, MFSD14, and SLC46 family proteins, as well as bacterial multidrug resistance (MDR) transporters such as tetracycline resistance protein TetA and multidrug resistance protein MdtG. MDR transporters are drug/H+ antiporters (DHA) that mediate the efflux of a variety of drugs and toxic compounds, and confer resistance to these compounds. TetA proteins confer resistance to tetracycline while MdtG confers resistance to fosfomycin and deoxycholate. The Solute carrier 46 (SLC46) family is composed of three vertebrate members (SLC46A1, SLC46A2, and SLC46A3), the best-studied of which is SLC46A1, which functions both as an intestinal proton-coupled high-affinity folate transporter involved in the absorption of folates and as an intestinal heme transporter which mediates heme uptake. MFSD10 facilitates the uptake of organic anions such as some non-steroidal anti-inflammatory drugs (NSAIDs) and confers resistance to such NSAIDs. The SLC46/TetA-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.	1.26218e-71
NZ_CP043451.1\|WP_112658802.1\|159823_160837_+\|IS1595-family-transposase	gnl\|CDD\|372298	pfam12762, DDE_Tnp_IS1595, ISXO2-like transposase domain. This domain probably functions as an integrase that is found in a wide variety of transposases, including ISXO2.	6.47596e-43
NZ_CP043451.1\|WP_112653582.1\|170449_171415_-\|hypothetical-protein	gnl\|CDD\|319899	cd06588, PhnB_like, Escherichia coli PhnB and similar proteins. The Escherichia coli phnB gene is found next to an operon of fourteen genes (phnC-to-phnP) related to the cleavage of carbon-phosphorus (C-P) bonds in unactivated alkylphosphonates, supporting bacterial growth on alkylphosphonates as the sole phosphorus source. It was originally considered part of that operon. PhnB appears to play no direct catalytic role in the usage of alkylphosphonate. Although many of the proteins in this family have been annotated as 3-demethylubiquinone-9 3-methyltransferase enzymes by automatic annotation programs, the experimental evidence for this assignment is lacking. In Escherichia coli, the gene coding 3-demethylubiquinone-9 3-methyltransferase enzyme is ubiG, which belongs to the AdoMet-MTase protein family. PhnB-like proteins adopt a structural fold similar to bleomycin resistance proteins, glyoxalase I, and type I extradiol dioxygenases.	4.84547e-37
NZ_CP043451.1\|WP_112657831.1\|155821_156439_+\|class-I-SAM-dependent-methyltransferase	gnl\|CDD\|379312	pfam13649, Methyltransf_25, Methyltransferase domain. This family appears to be a methyltransferase domain.	1.13884e-08
NZ_CP043451.1\|WP_112657835.1\|157122_157461_-\|single-stranded-DNA-binding-protein	gnl\|CDD\|239942	cd04496, SSB_OBF, SSB_OBF: A subfamily of OB folds similar to the OB fold of ssDNA-binding protein (SSB). SSBs bind with high affinity to ssDNA. They bind to and protect ssDNA intermediates during DNA metabolic pathways. All bacterial and eukaryotic SSBs studied to date oligomerize to bring together four OB folds in their active state. The majority (e.g. Escherichia coli SSB) have a single OB fold per monomer, which oligomerize to form a homotetramer. However, Deinococcus and Thermus SSB proteins have two OB folds per monomer, which oligomerize to form a homodimer. Mycobacterium tuberculosis SSB varies in quaternary structure from E. coli SSB. It forms a dimer of dimers having a unique dimer interface, which lends the protein greater stability. Included in this group are OB folds similar to Escherichia coli PriB. E.coli PriB is homodimeric with each monomer having a single OB fold. It does not appear to form higher order oligomers. PriB is an essential protein for the replication restart at forks that have stalled at sites of DNA damage. It also plays a role in the assembly of primosome during replication initiation at the bacteriophage phiX174 origin. PriB physically interacts with SSB and binds ssDNA with high affinity.	5.35314e-31
NZ_CP043451.1\|WP_112653578.1\|162653_164210_+\|amino-acid-permease	gnl\|CDD\|129987	TIGR00909, putative_amino_acid_transporter, amino acid transporter. [Transport and binding proteins, Amino acids, peptides and amines].	5.17883e-113
NZ_CP043451.1\|WP_090528388.1\|171411_171732_-\|winged-helix-turn-helix-transcriptional-regulator	gnl\|CDD\|238042	cd00090, HTH_ARSR, Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric repressors. ARSR subfamily of helix-turn-helix bacterial transcription regulatory proteins (winged helix topology). Includes several proteins that appear to dissociate from DNA in the presence of metal ions.	1.09002e-16
NZ_CP043451.1\|WP_112653583.1\|172019_172574_-\|DUF1572-family-protein	gnl\|CDD\|311521	pfam07609, DUF1572, Protein of unknown function (DUF1572). These proteins, from several diverse bacteria, share a short conserved sequence towards their N termini.	6.66725e-92
NZ_CP043451.1\|WP_146750442.1\|167380_168634_-\|amino-acid-ABC-transporter-substrate-binding-protein	gnl\|CDD\|380492	cd06268, PBP1_ABC_transporter_LIVBP-like, periplasmic binding domain of ATP-binding cassette transporter-like systems that belong to the type 1 periplasmic binding fold protein superfamily. Periplasmic binding domain of ATP-binding cassette transporter-like systems that belong to the type 1 periplasmic binding fold protein superfamily. They are mostly present in archaea and eubacteria, and are primarily involved in scavenging solutes from the environment. ABC-type transporters couple ATP hydrolysis with the uptake and efflux of a wide range of substrates across bacterial membranes, including amino acids, peptides, lipids and sterols, and various drugs. These systems are comprised of transmembrane domains, nucleotide binding domains, and in most bacterial uptake systems, periplasmic binding proteins (PBPs) which transfer the ligand to the extracellular gate of the transmembrane domains. These PBPs bind their substrates selectively and with high affinity. Members of this group include ABC-type Leucine-Isoleucine-Valine-Binding Proteins (LIVBP), which are homologous to the aliphatic amidase transcriptional repressor, AmiC, of Pseudomonas aeruginosa. The uncharacterized periplasmic components of various ABC-type transport systems are included in this group.	0.000103192
NZ_CP043451.1\|WP_090529629.1\|168590_170120_-\|glutamine-hydrolyzing-GMP-synthase	gnl\|CDD\|234614	PRK00074, guaA, GMP synthase; Reviewed.	0
NZ_CP043451.1\|WP_090528400.1\|165483_166056_+\|MarC-family-protein	gnl\|CDD\|280149	pfam01914, MarC, MarC family integral membrane protein. Integral membrane protein family that includes the protein MarC. MarC was thought to be a multiple antibiotic resistance protein. Nevertheless, a study has shown that MarC is not involved in multiple antibiotic resistance. The function of this family is unclear.	1.07959e-22

>NZ_CP043451.1|WP_112653577.1|161989_162349_+|hypothetical-protein
MNQERVCLDCGTPLQGRADKKFCNDLCRNNYNNQLNSNSYNLVRNINNILRRNRRVLEELNPTGKTKTTRKKLAAKGFDFDHITSIYQTKTGSTYFFNYEYGYLLLDNDEVLLVKREGE
>NZ_CP043451.1|WP_112658804.1|161401_161818_-|hypothetical-protein
MDLTDEQVLAQLKVRRVKLKMELDRVEVAIKAFENIGEINILDAMPYMMEDLEVDEDLLISTLMYNPKMTAEKKVIFTLSKIGKGDASDITEYILRIDGHIKDTKRAFERITYVCSRMFKSGKITAERVGKKNVYMLR
>NZ_CP043451.1|WP_022833677.1|160950_161268_-|hypothetical-protein
MSDNASNQPSLDEVVNSLSKAVVYLIKDITATRKTLSDGLNKIDDNFKEINKKIDALSKDTGENFVDVHMNLKSIKSEISKINKVTGYEETMKNLSIVHNKSKQQ
>NZ_CP043451.1|WP_112658802.1|159823_160837_+|IS1595-family-transposase
MEQEHPPLGKTLPFRTINDIAIHFRDKAVCIEYLTQLRWAGNVKCAHCGHDKVYELKGAYKGYKCAKCRKKFTAIKGTIFENSPIELSKWFMAIFILSTHRKGISSVQIARDIGVTQKTAWFMMQRVRYAFKMKSFESNEKIGKSTFDNKGNEVKAVVEVDETYIGGKVANMHKHKAEAIEKKGSSSKIGVIGAIERGGKVKLQPLKATDHENVIPFLVKSVHQGTKLMTDEHVAYNTMNRVYEHQTIKHMLKEYVRGEVHTNTIENFWSLLKRGVYGTYHFISPKHVHQYLEEFAFRFNSRELTEAQRFDKLISLSNYKITYKVLTYEPKETQANA
>NZ_CP043451.1|WP_022833680.1|159139_159619_+|hypothetical-protein
MYNNQFISELRAQRLNVLEQLKHIDAMLKLYGVNLDEEEIPAYSGIEALVYERPYKKDASNKEKIAGLLKLTNRFLSINEMTSLVMEFEPKSKVEEVKASLSSAKNILLKDGSIVKVQVGTNNSNTFYGSPTWIDEQGFPLPEHKYSDDAVQLKTKIVI
>NZ_CP043451.1|WP_112683133.1|157820_158054_-|hypothetical-protein
MGLPINVIRAIVKRKTANNLPSSSQTEILIPIESIAAYKHLSGVDYQLYLKKDCEINLGYEIESITGKIKSPHIQFL
>NZ_CP043451.1|WP_112658800.1|157657_157849_+|hypothetical-protein
MGNEIVRTIDQGAIELSNKVEKIANSILPLLNGLTAYECERVLSKAKAIVFEEIPIKIECEEI
>NZ_CP043451.1|WP_112657835.1|157122_157461_-|single-stranded-DNA-binding-protein
MNSLRNSVRLVGNLGMDPEVKVFDSNKKMVRLSIATNESYKNDKGEKITDTQWHNLIFWGTQAKLAEDLLKKGDEVAVEGKLANRNYTDKDGIKRYVSEVIVNEFLKVGVKG
>NZ_CP043451.1|WP_112657833.1|156734_156986_-|hypothetical-protein
MALHFVAEWIGAARLMPTPQQRILRDHCRSRLFYMRQQNKTQNRPLKIFESNNIKLRSVSSIKKKPAMDMIRMFATGATDKEQ
>NZ_CP043451.1|WP_112657831.1|155821_156439_+|class-I-SAM-dependent-methyltransferase
MKENRQGHWEHVYATKSSNEVSWTQTVPQTSLNFIHSFNLPKDAKIIDIGGGDSNLVDHLLNEGYRNISVLDISEAALNRAKMRLGPKANLVTWIVSEITDFKPSEIYDVWHDRATFHFLTTQQQIASYISIARNAVKRNLVVGTFSENGPEKCSGLSVNRYSKLQLEQVMSNGFQKLKCINEDHITPFNTVQNFTFCSFERCYT
>NZ_CP043451.1|WP_112653578.1|162653_164210_+|amino-acid-permease
MKLFIKKPIAQLMAASAETEKSLKRTLGVGSLIALGIGAIIGAGIFVRTAAAAGEHAGPAVTISFLIAAAGCALAGLCYAEFASMIPIAGSAYTYSYATMGEFIAWIIGWDLVLEYALGAATVAIGWSQYFNEFLTTFFNVHIPYAWSHSFMEVSNTTAGMYAAEMGTRGIVNLPAILILFLLTLLLIRGTAESAVVNNIIVIVKVAIVLMIIGLGWHFINPAFHTPYTIPADAGKIKVSAGVVDYADTFNHGWLGVLRGASVVFFAFIGFDAVSTAAQEAKNPQRDMPKGILISLVFCTALYILFSHVLTGLVSYKDFLIQGKEASVSYAIKTAMPGYGWLASFVTVSILAGFSSVILVMLMGQTRVFYTMSTDGLIPKVFSKLHPKFRTPYKSQWLFFVFVSLFAGFIPDKYVGDMVSIGTLFAFVLVCIGIFILRRTDPGIERPFKTPAYMIVCPLGALICLCMIASEGWENWARLIVWLLIGFAVYFGYSIKRSHVRHGKVEGANNPINPKFVE
>NZ_CP043451.1|WP_112653579.1|164307_165471_+|MFS-transporter
MKGDKNLWVLVFVCIINSLGFGIIVPILYSYGKTFGVTGETLGILTASFSIAQFFATPVLGSLSDKWGRKPLLVISLAGTCISFILFAEARSMIMLFAARILDGLTGGNVSVAQAMVSDTARPDNRARRFGILSSAFGFGFVIGPAIGGFLNSYGMQVPFYFAAGISLIGTLCSLFFLKETNPPDKSKKDSEKTKFSFVALITTLKRPVIGTAVFTGFMLTMAQFTMIIAFQTFTVDVLKINPTQIGILYAGFGVSGIIMQLCVPLFTKWYSSKSTILTLSTSLCFVAMFVTGLTNHFIAFVIGICIYGLFNGLRNPMLNAIIADHIDHQEQGKILGINQSYASIGQTLGPVTAGFAALLSVHAIFFLSSCYILAALLLSIRLKKKE
>NZ_CP043451.1|WP_090528400.1|165483_166056_+|MarC-family-protein
MPHPFIFKEIISVTMILFAIIDILGAIPVIIQLRQRVGHIESEKASIAVLVLMVTFLFIGDELLAVIGLDISSFAIAGSLVIFIIAMEMILGVDFFKEELPQAASIVPLAFPLIAGAGTMTTLLSLKSQYQTQNILVGIVLNTLVVYLVLKNVKWLERLLGPIGLSVLRKAFGIILLAIAIKLFRSNTHL
>NZ_CP043451.1|WP_112653580.1|166211_167384_-|RsmB/NOP-family-class-I-SAM-dependent-RNA-methyltransferase
MKAINQLKTFQRILGEYPADTPLSKFLPGFYRQNKQMGSTDRRVANRLVYNYFRLGRALPDVSEDERLLVAEFLCNTQTNSYLQHFKPEWAVCVGFSDDDKLALVKTAYPDFKLADVFPWSSQLSEGIDKEAFLKSFFCQPDLFIRVRNGYDHLVKAELTKAQVVFKDEGNGCYSLPNGTRLETIFPKQHWFEVQDYSSQQTGNYFKPQRWDSWWDACAASGGKSLLLHEDEPNIKLVVSDIRESILANLDERFQLAGLTKYQKKALDLTQNIDSVMHDYAFDGIILDAPCSGSGTWGRTPEMIAQFDVHKIEFFQKLQKSIAQNVVKYLKPGKPLIYITCSAFKGENEDVVDYLVNELGLKLEEKAVLKGYERKADTMFVARLSPSPIV
>NZ_CP043451.1|WP_146750442.1|167380_168634_-|amino-acid-ABC-transporter-substrate-binding-protein
MISVQNHRPLLSGNKWLPFFCIALLLAACSPKTRPVATTVKKPTDTEKKPDNTSEKPVKAPEQKVATIAMILPLNLEHLNPAQKYSPIQLSQANIAVEYYQGFKLALDSLTAYGNNYRLQIFDSKDEAMQAHDLALNAFIRSSDLIVGPVFPDGVKSFSAALSYSKGPILSPLSPANPSTIKSKNLITAIPPLEYHAWGAAEYINRTVKPKKIFVLRSGFNQESDYAINFKKAIDSLSKKKVKVTNVYVIRGKLSSLLPQLSKTEKNVFVIPATDQAFLGVTLRSLDTLNKHYPVMVFGHPSWEKFSFLKPQLLQRLNTHITSTEKINYKAGATITFLRNYRRAYHVEPTEYAIKGFDEGLYFGKLLFMDKGMQSIEETDFTGLHNGFHFVKKPGQGWINTHVNILMYTNFELKQVE
>NZ_CP043451.1|WP_090529629.1|168590_170120_-|glutamine-hydrolyzing-GMP-synthase
MQEKILILDFGSQFTQLIARRVRELNIYCEIHPFNHYPEIDSTVKGIILSGSPYSVRQEDAPHFEFEKFHTTRPILGVCYGAQYVAHFHGGEVLPSSTREYGRANLEYIKQDNPLFKDVPGGSQVWMSHGDTIATIGDNFEVIASTDSVKVAAYQVTGTQTYGIQFHPEVTHSIDGKQLLQNFLVDICGCKQDWTPDSFIETTVAALREKLGDDKVVLGLSGGVDSSVAAVLLHHAIGKNLHCIFVDNGLLRKDEFEQVLDSYQHMGLNIKGIDAKQRFYDALAGLTDPEKKRKAIGRVFIEVFDDAAHEVQDVKWLGQGTIYPDVIESVSVKGPSATIKSHHNVGGLPDFMKLKVVEPLNTLFKDEVRKVGKALGIDPNILGRHPFPGPGLAIRILGDITPEKVAILQEADAIYINNLRAAGVYDKVWQAGAIFLPVQSVGVMGDERTYENVICLRAVESVDGMTADWCHLPYDLLAKISNEIINNVKGINRVVYDISSKPPATIEWE
>NZ_CP043451.1|WP_112653582.1|170449_171415_-|hypothetical-protein
MTNNETVFTKDLQNKRLNVVRTFDAPLNLVWQAWTESEILDQWWAPHPYRTETKTQDFREGGYWLYQMVGPEHTEHPTWCKEEYKTIVVPQKIANAVSFCDENAVTNTNFPVMNWEKNFTGEGEHTTVNIDIYFDKVEDMQTIVGMGFQEGFTAGLSNLDHYLSTAFRIRKDLKPGNAARVTTYLNFPGNTEEALTFYKEVFKGEFTGKKLTRFSDIELPAEVRMNEADKKMIIHGELTIMGGHVLMATDAPESMGFKLQTGNNMHINVEPESREETERLFNELSVGGVVTMPLSDMFFGAYFAELTDKFGINWMLNYQNV
>NZ_CP043451.1|WP_090528388.1|171411_171732_-|winged-helix-turn-helix-transcriptional-regulator
MRRDVFQAIADPTRRAIISLLALQAMTPNAIAEHFQSSRQAVSKHIQILSECQLVNQKQTGREIYYHFNAQKMKEVDVWMDQFRALWETRFSQLDNVLQNLKNKQS
>NZ_CP043451.1|WP_112653583.1|172019_172574_-|DUF1572-family-protein
MENDYLTSVKKQFAYYKSLGEKTFEQLTDEQLYWQYNPESNSIAMIVKHMSGNMISRWTDIFTTDGEKPTRNREAEFTPSTPTRQTITETWEQGWQCLFDTLDKLTADDLGKIVYIRNQGHTAMEAINRQLAHYPYHVGQIVFLGKMLCNENWHSLSIPRGQSENYNADKFAQEKRKVHFTDEK
>NZ_CP043451.1|WP_112653584.1|172684_173182_-|hypothetical-protein
MKKYIDSGILEVFVMGIATDEEVRELMYMKAKHPEVEEALKQLETDMEKLAGEMAIAPPPHMWEKIEDEIDGLIHQGNPAQPIKFRTSGDGHNKHKKTSPEDQFIPIESESNHMRLHKSWRWIFAAVFVIGKIFLGFAIYFYLENRQSQQQLQELKTEVRELKKR

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Crispr_ID: NZ_CP043451_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP043451_2

458874-458966

Orphan

Consensus_repeat	Method
CCCGTCATTGCGAGGGACGAAGCAAT	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP043451_2

>merge|NZ_CP043451|2|458874-458966|CRISPRCasFinder
CCCGTCATTGCGAGGGACGAAGCAATTGCGAACTGTGCAGGGCAAACGTGCAAAGCCCCCTCACCACCCCGTCATTGCGAGGCACGAAGCAAT

>NZ_CP043451|2|2|458874-458966|CRISPRCasFinder
CCCGTCATTGCGAGGGACGAAGCAAT	TGCGAACTGTGCAGGGCAAACGTGCAAAGCCCCCTCACCAC
CCCGTCATTGCGAGGCACGAAGCAAT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP043451.1\|WP_112652616.1\|462136_462985_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|225518
NZ_CP043451.1\|WP_112652919.1\|454884_455964_+\|AAA-family-ATPase	unknown	unknown	gnl\|CDD\|316042
NZ_CP043451.1\|WP_091175129.1\|450471_452394_+\|ABC-F-family-ATP-binding-cassette-domain-containing-protein	unknown	unknown	gnl\|CDD\|223562
NZ_CP043451.1\|WP_112652621.1\|469939_470746_+\|polysaccharide-deacetylase-family-protein	unknown	unknown	gnl\|CDD\|200566
NZ_CP043451.1\|WP_112652915.1\|448358_448856_-\|tryptophan-rich-sensory-protein	unknown	unknown	gnl\|CDD\|320706
NZ_CP043451.1\|WP_112652628.1\|458638_458797_-\|GIY-YIG-nuclease-family-protein	unknown	unknown	gnl\|CDD\|198395
NZ_CP043451.1\|WP_090527735.1\|464117_464801_+\|NUDIX-hydrolase	unknown	unknown	gnl\|CDD\|223979
NZ_CP043451.1\|WP_112652615.1\|461134_462130_-\|type-I-glyceraldehyde-3-phosphate-dehydrogenase	unknown	unknown	gnl\|CDD\|223135
NZ_CP043451.1\|WP_091175120.1\|447758_448292_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043451.1\|WP_112653556.1\|457719_458631_+\|IS982-family-transposase	unknown	unknown	gnl\|CDD\|372648
NZ_CP043451.1\|WP_112652916.1\|449014_449374_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|380412
NZ_CP043451.1\|WP_091175145.1\|462992_463979_-\|6-phosphofructokinase	unknown	unknown	gnl\|CDD\|235111
NZ_CP043451.1\|WP_112652917.1\|449496_450270_+\|SGNH/GDSL-hydrolase-family-protein	unknown	unknown	gnl\|CDD\|238872
NZ_CP043451.1\|WP_112652918.1\|452949_454200_+\|DUF5103-domain-containing-protein	unknown	unknown	gnl\|CDD\|379920
NZ_CP043451.1\|WP_112652619.1\|467533_468688_+\|DUF2029-domain-containing-protein	unknown	unknown	gnl\|CDD\|378217
NZ_CP043451.1\|WP_112652617.1\|465306_466167_-\|N-acetylglucosamine-kinase	unknown	unknown	gnl\|CDD\|225518
NZ_CP043451.1\|WP_112652614.1\|459239_460331_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|212735
NZ_CP043451.1\|WP_112652920.1\|456247_457219_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043451.1\|WP_112652618.1\|466496_467426_-\|NGG1p-interacting-factor-NIF3	unknown	unknown	gnl\|CDD\|376614
NZ_CP043451.1\|WP_112652620.1\|468990_469959_+\|glycosyltransferase-family-2-protein	unknown	unknown	gnl\|CDD\|133030

Protein	Function_ID	Function_description	E-value
NZ_CP043451.1\|WP_112652616.1\|462136_462985_-\|hypothetical-protein	gnl\|CDD\|225518	COG2971, COG2971, Predicted N-acetylglucosamine kinase [Carbohydrate transport and metabolism].	6.94073e-11
NZ_CP043451.1\|WP_112652919.1\|454884_455964_+\|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.	1.17565e-14
NZ_CP043451.1\|WP_091175129.1\|450471_452394_+\|ABC-F-family-ATP-binding-cassette-domain-containing-protein	gnl\|CDD\|223562	COG0488, Uup, ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only].	0
NZ_CP043451.1\|WP_112652621.1\|469939_470746_+\|polysaccharide-deacetylase-family-protein	gnl\|CDD\|200566	cd10941, CE4_PuuE_HpPgdA_like_2, Putative catalytic domain of uncharacterized prokaryotic polysaccharide deacetylases similar to bacterial PuuE allantoinases and Helicobacter pylori peptidoglycan deacetylase (HpPgdA). This family contains many uncharacterized prokaryotic polysaccharide deacetylases (DCAs) that show high sequence similarity to the catalytic domain of bacterial PuuE allantoinases and Helicobacter pylori peptidoglycan deacetylase (HpPgdA). PuuE allantoinase appears to be metal-independent and specifically catalyzes the hydrolysis of (S)-allantoin into allantoic acid. Different from PuuE allantoinase, HpPgdA has the ability to bind a metal ion at the active site and is responsible for a peptidoglycan modification that counteracts the host immune response. Both PuuE allantoinase and HpPgdA function as homotetramers. The monomer is composed of a 7-stranded barrel with detectable sequence similarity to the 6-stranded barrel NodB homology domain of DCA-like proteins in the CE4 superfamily, which removes N-linked or O-linked acetyl groups from cell wall polysaccharides. In contrast to typical NodB-like DCAs, PuuE allantoinase and HpPgdA do not exhibit a solvent-accessible polysaccharide binding groove and might only bind a small molecule at the active site.	4.36189e-67
NZ_CP043451.1\|WP_112652915.1\|448358_448856_-\|tryptophan-rich-sensory-protein	gnl\|CDD\|320706	cd15904, TSPO_MBR, Translocator protein (TSPO)/peripheral-type benzodiazepine receptor (MBR) family. This family contains tryptophan-rich translocator protein (TSPO), an integral membrane protein that is highly conserved from bacteria to mammals. In eukaryotes, it is mainly found in the outer mitochondrial membranes of steroid-synthesizing cells of the nervous system where it transports cholesterol into mitochondria. It is known to be highly expressed in metastatic cancer, steriodogenic tissues, as well as inflammatory and neurological diseases such as Alzheimer's and Parkinson's. TSPO is also known as the peripheral benzodiazepine receptor (MBR) and its ligands include benzodiazepine drugs, implicated in regulating apoptosis. In human, a single polymorphism A147T is associated with psychiatric disorders; the mutation causes structural changes in a region implicated in cholesterol binding. TSPO is homologous to bacterial tryptophan-rich sensory proteins, and their tryptophan residues are believed to be functionally important. In bacteria, TSPO acts as a negative regulator of expression of specific photosynthesis genes in response to oxygen/light; it catalyzes a photooxidative degradation of Proto porphyrine (PpIX). R. sphaeroides TSPO (RsTSPO) is involved in porphyrin transport, similar to human, while Arabidopsis translocator protein (AtTSPO) is regulated at multiple levels in response to salt stress and perturbations in tetrapyrrole metabolism.	1.12273e-48
NZ_CP043451.1\|WP_112652628.1\|458638_458797_-\|GIY-YIG-nuclease-family-protein	gnl\|CDD\|198395	cd10448, GIY-YIG_unchar_3, GIY-YIG domain of uncharacterized hypothetical protein found in bacteria. The family includes a group of uncharacterized bacterial proteins with a GIY-YIG domain that shows statistically significant similarity to the N-terminal catalytic domains of GIY-YIG family of intron-encoded homing endonuclease I-TevI and catalytic GIY-YIG domain of nucleotide excision repair endonuclease UvrC.	6.10831e-21
NZ_CP043451.1\|WP_090527735.1\|464117_464801_+\|NUDIX-hydrolase	gnl\|CDD\|223979	COG1051, COG1051, ADP-ribose pyrophosphatase [Nucleotide transport and metabolism].	1.21402e-20
NZ_CP043451.1\|WP_112652615.1\|461134_462130_-\|type-I-glyceraldehyde-3-phosphate-dehydrogenase	gnl\|CDD\|223135	COG0057, GapA, Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate transport and metabolism].	0
NZ_CP043451.1\|WP_112653556.1\|457719_458631_+\|IS982-family-transposase	gnl\|CDD\|372648	pfam13612, DDE_Tnp_1_3, Transposase DDE domain. Transposase proteins are necessary for efficient DNA transposition. This domain is a member of the DDE superfamily, which contains 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.	9.44762e-83
NZ_CP043451.1\|WP_112652916.1\|449014_449374_+\|hypothetical-protein	gnl\|CDD\|380412	cd07009, cupin_BLL0285-like, Bradyrhizobium japonicum BLL0285 and related proteins, cupin domain. This family includes bacterial proteins homologous to BLL0285, a Bradyrhizobium japonicum protein of unknown function. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.	1.64533e-32
NZ_CP043451.1\|WP_091175145.1\|462992_463979_-\|6-phosphofructokinase	gnl\|CDD\|235111	PRK03202, PRK03202, ATP-dependent 6-phosphofructokinase.	1.45948e-157
NZ_CP043451.1\|WP_112652917.1\|449496_450270_+\|SGNH/GDSL-hydrolase-family-protein	gnl\|CDD\|238872	cd01834, SGNH_hydrolase_like_2, SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.	2.16745e-43
NZ_CP043451.1\|WP_112652918.1\|452949_454200_+\|DUF5103-domain-containing-protein	gnl\|CDD\|379920	pfam17116, DUF5103, Domain of unknown function (DUF5103). This is a family of Bacteroidetes proteins of unknown function.	6.92899e-109
NZ_CP043451.1\|WP_112652619.1\|467533_468688_+\|DUF2029-domain-containing-protein	gnl\|CDD\|378217	pfam09594, GT87, Glycosyltransferase family 87. The enzymes in this family are glycosyltransferases. PimE is involved in phosphatidylinositol mannoside (PIM) synthesis, a major class of glycolipids in all mycobacteria. PimE is a polyprenol-phosphate-mannose-dependent mannosyltransferase that transfers the fifth mannose of PIM. The family also includes alpha(1-->3) arabinofuranosyltransferase, invloved in the synthesis of of mycobacterial arabinogalactan.	2.82878e-15
NZ_CP043451.1\|WP_112652617.1\|465306_466167_-\|N-acetylglucosamine-kinase	gnl\|CDD\|225518	COG2971, COG2971, Predicted N-acetylglucosamine kinase [Carbohydrate transport and metabolism].	1.12096e-12
NZ_CP043451.1\|WP_112652614.1\|459239_460331_+\|hypothetical-protein	gnl\|CDD\|212735	cd11801, SH3_JIP1_like, Src homology 3 domain of JNK-interacting proteins 1 and 2, and similar domains. JNK-interacting proteins (JIPs) function as scaffolding proteins for c-Jun N-terminal kinase (JNK) signaling pathways. They bind to components of Mitogen-activated protein kinase (MAPK) pathways such as JNK, MKK, and several MAP3Ks such as MLK and DLK. There are four JIPs (JIP1-4); all contain a JNK binding domain. JIP1 and JIP2 also contain SH3 and Phosphotyrosine-binding (PTB) domains. Both are highly expressed in the brain and pancreatic beta-cells. JIP1 functions as an adaptor linking motor to cargo during axonal transport and also is involved in regulating insulin secretion. JIP2 form complexes with fibroblast growth factor homologous factors (FHFs), which facilitates activation of the p38delta MAPK. The SH3 domain of JIP1 homodimerizes at the interface usually involved in proline-rich ligand recognition, despite the lack of this motif in the domain itself. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.	0.00919906
NZ_CP043451.1\|WP_112652618.1\|466496_467426_-\|NGG1p-interacting-factor-NIF3	gnl\|CDD\|376614	pfam01784, NIF3, NIF3 (NGG1p interacting factor 3). This family contains several NIF3 (NGG1p interacting factor 3) protein homologs. NIF3 interacts with the yeast transcriptional coactivator NGG1p which is part of the ADA complex, the exact function of this interaction is unknown.	1.19209e-26
NZ_CP043451.1\|WP_112652620.1\|468990_469959_+\|glycosyltransferase-family-2-protein	gnl\|CDD\|133030	cd04187, DPM1_like_bac, Bacterial DPM1_like enzymes are related to eukaryotic DPM1. A family of bacterial enzymes related to eukaryotic DPM1; Although the mechanism of eukaryotic enzyme is well studied, the mechanism of the bacterial enzymes is not well understood. The eukaryotic DPM1 is the catalytic subunit of eukaryotic Dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. The enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. This protein family belongs to Glycosyltransferase 2 superfamily.	1.59539e-76

>NZ_CP043451.1|WP_112652628.1|458638_458797_-|GIY-YIG-nuclease-family-protein
MQRGGCVYIITNKNNSVLYTGVTSDIIGRIFDHKNKTYPQSFTAKYNCNKLT
>NZ_CP043451.1|WP_112653556.1|457719_458631_+|IS982-family-transposase
MLTSDKIIEIFVKVDDFCKECEEQIAKHKLDAGNYKVRDRKASLADSEIITIVIAFHSGHFTNLKHFYITHICSHYKDFFPGLVSYNRFVELQQRVAVPMMLFLKTHCLGRSRGINFIDSTHIKVCHNRRIHNHKVFAATAERGQCSIGWFYGFKLHLIINDKGEILSFYLTKGNVDDRNVKLMTSMTEEIFGKLFGDKGYISKALADLLWGNGIQMITKPRKNMKDFNISQADKIMLRKRAIIECVYDELKNICKLQHTRHRSVNNFLMNIMGSLCAYHFFPKKPSLNIVFEEQDNQLLLAA
>NZ_CP043451.1|WP_112652920.1|456247_457219_+|hypothetical-protein
MKYQLQPYQGMQSRYSCPVCNHHKCFVRYIDIQTGQHLAPHVGRCGREDKCGYHLTPRNYFATLPGYKPYQPKRSRYMPGKSPAQPAVNPARSPRPEPKYIINPYWVSATLYNYQDNNFVQYLIKRLGRDITQAAIKRYHIGTHNHWPGACVFWQYDTEGDVRTGKIMLYNKETGKRVKVPFNHITWAHTLAIKEAATAGDDTTFILQQCLFGEHLLSANPAMPVAIVESEKTAIIASALIPDFIWLASGSLQGLNPAKCGVLKGRRVMLFPDVNAYDKWKLKARELHTALPNTAFSVSAVLEDIATDEDRQNGIDIGDVVGW
>NZ_CP043451.1|WP_112652919.1|454884_455964_+|AAA-family-ATPase
MITQNLNNSTATCITAGSLAQQSLQQMDEQQLPQNNDDVLMVRHADHWMAEAHERAIPLMLFGKFWHQGEVCILFADSNLGKSIVAVQVADGVSKGSGKYPFDVEAPAQPVLYCDFELTDKQFEARYSVDYEYHYHFGKNFYRAELNPDMELPHEFADFDDYLIYSLERSVLQTGAKVLVIDNLTYLRSETERAKDALPLMKQLKALKNKYNLSILVLAHTPKRDMAQPITRNDLQGSKMLMNFCDSAFAIGESKTDVNMRYLKQIKQRNTEQLYGEGNVCLCQIGKPYNFLKYEFVSFGKEWEQLSPQNDPEQEQIMANANELKQQGLTLRQIGQKLGISHQKADRLLKAYAKLNANV
>NZ_CP043451.1|WP_112652918.1|452949_454200_+|DUF5103-domain-containing-protein
MKKLYIILFILLSLNSFAQSPYNNNVYSPAIKSVEFYNTAKQGTFPVINLGTDEKVLLTFDDLRGGSRNYYYTIEHCDANWNSSNLSSAEYLQSFTDDRLYNYSYSTGTMQKYTHYEISLPNNNIAPKISGNYVLKVYEDGDQSKMVLTRRLYVLGKRVSIAADLVASANNATRQTNQKINFTVDYSGLVVQNPAYALRTFIMQNARTETAVLNGQPTYIRGSQLIYNDVSVNDFPGRNEFRLFDTRTLKLNSQRVAKIYKDSTNVVVLLGDPVRDQPNYIFQYDNDGKFYILNNDGTTPATDADYAHVYFTLSTNKDPKEGSPYVVGQFNNYRLDDSNKLHPLDNGRYTVNMLLKQGVYDYEYVWVDAKTGKADDIPFEGSHFETENEYQVLTYYRPPAARWDELVGFRELVTKR
>NZ_CP043451.1|WP_091175129.1|450471_452394_+|ABC-F-family-ATP-binding-cassette-domain-containing-protein
MIAINNLTFEIGARALYDEANWHIKPGEKIGLIGANGTGKTTLLKIIVGDYKPTSGTVSMAKDLTMGYLNQDLLSYSSDKNIVHVAMEAFERQNQLHDEIENLLKKLETDYSEELLNKLSDKQHEFELLDGYNIEYKAHEILAGLGFSDEDCKRKLSTFSGGWRMRVMLAKILLQAPDILLLDEPTNHLDLPSIQWLEDYLKSFPGAIIIVSHDRWFLDKVINRTVESRKGKLTVYAGNYSFYLEEKALREEIQRGEFKNQQSKIKQEERLIERFRAKASKAKMAQSRIKMLDKMERIDDVDDDNPSVNFAFRFSKQSGRHVITLEDITKKYPAIDILDHAEAVIEKGDKIALIGANGKGKSTLLRIIASADKDYTGTVTTGHNVTTTFFAQHQLESLHLENQILQELQSFAPKHTDTELRTILGSFLFTGDDVFKKIKVLSGGEKSRVALAKALTADANFLVLDEPTNHLDMQSVNILIQALDQYEGTFIVVSHDRYFLDNVANKIWFIEDQKIKIYPGTYAEFDEWYAKRKLEPKAAAPAPQPKKEEKKPEPVKQPQGENKHQQLKKLNQDLAKMEQQIADLEKEVKHFETQLADEKIYSDNGKLKQTNAAYSAKQTELKQMQDKWEALAEQILELES
>NZ_CP043451.1|WP_112652917.1|449496_450270_+|SGNH/GDSL-hydrolase-family-protein
MKDTKQNYRRHFLKTTAVGTLAAMGIPSIVSSALAAEKPAKKLTFNQGDVVLFQGDSITDWGRDHSKTEPNTTSALGSGYALLTASQLLLKHADKGLKIYNKGISGNKVYQLAERWDIDCLALKPNILSIHIGVNDFWHTLTSGYKGTIDTYIADYRALLTRTKQALPDIKLVICEPFAEKNVKAVDDKWYPTFDLFRKAAKDIAAEFDAVFVPYQSAFDKAEQTAPATYWNLDGVHPSVAGEALMAQTWLKAVGAL
>NZ_CP043451.1|WP_112652916.1|449014_449374_+|hypothetical-protein
MIKAYRLYTGDDGHSHIQKGMVDLGTLNEALAVRFQESEPHAFYDYHNAPTNQYVITLTGTLEFETYPGEKFILKPGEILIAQDTTGTAHKWRLMDDEPWKRVYVTFDPAKPINFVADK
>NZ_CP043451.1|WP_112652915.1|448358_448856_-|tryptophan-rich-sensory-protein
MSVAVSTKRFQFFPYLISLLIVLFIGFVASLVTRPEIAGWYSTLKKPSFNPPPWLFAPVWTAIYIMIATAAYLVWKHRSRKPVYIIARSIYFIQLILNFSWSIVFFGMHQIAAAAVVIILLWLSIVVNINWFNKFSRTASWLLVPYLLWVSFASILNMSIYFLNR
>NZ_CP043451.1|WP_091175120.1|447758_448292_-|hypothetical-protein
MKKLLLIFCLITAAHSFAFADKTAINNFVVKENPFAVDEVAVVATDTAGVIQENVNGVFTFVMNGFTEELKFDKGTAFYRHKLDRSTFLYAKHMNDSGTHAILYYIYKHDSKLSPFHISWVLLIAIPLLLVLLAYMFKRFIIIAVVIFCIFLYFNYHNGLSIPTFFESIIDGLKNMF
>NZ_CP043451.1|WP_112652614.1|459239_460331_+|hypothetical-protein
MLKVEYAKHEDDQTYYLVVNDIPYYQSSYNDRTYRSAYINEIELGELLASYSSKELSEFFDSLNMGDYDFDAWPLGVDISFSFKKTYKSSDYPNFNVELNVDTEDWASGWSIKSFSEALKIIIKDRDNKNVRYFQLDDDFVSNGLGIAVAINDLDTPIGTLIDNAFPEFESIINDANLYLASVVDNQSVISFFNFPDSIKGPCQQYLMYFAQFLKDLGIEAETEIKEQAHSTLFKITPNNKDEALDKIKDALEIYTNAPALNDLQFQGMNNGDIAFMQLQANVMHLKSQIMLNNAALQMKDATIEALQLSNYQLKAIVVESNEKLKQEEEIIPGIMSIKKYDGEWFSLNLPEMLNRLKRRFIK
>NZ_CP043451.1|WP_112652615.1|461134_462130_-|type-I-glyceraldehyde-3-phosphate-dehydrogenase
MKIGINGFGRIGRLAFRAAIERPDIEVVGINDLVEPDYMAYMLKYDSTHGQFNGTIAVEGGHLVVNGKTIRVTAEKDPANLKWNEVGAEVVIESTGLFLTQETAQKHIDAGAKKVVMSAPAKDDTPTFVMGVNHKALKADQNIVSNASCTTNCLAPIAKVLDDKFGIEEGLMTTVHAVTATQKTVDGPSAKDWRGGRGAYQNIIPSSTGAAKAVGLVLPQLKGKLTGMSLRVPVADVSVVDLTVRLKNGASYEAIKAAMKEASEGELKGILGYTEDEVVSEDFKGDSRTSIFDAKAGIGLNENFVKVVSWYDNEWGYSNKLIDLVQELGKL
>NZ_CP043451.1|WP_112652616.1|462136_462985_-|hypothetical-protein
MIAVVYSGSYFAHWRLTDKGRTVASFKTNGINPYFNDEKHILQLLNKNINLIHHAEVIRRIYFFGAGASSDERKKIVHSAFSTFFKFGKISIEHDIAGAAIACCKNEPGIVSICGSGSNAAWYDGKRVWPNNYGLGYILADEGSGNWLGRQLIKEFMNDTLPLSIRKKFIHKYDADRKNLLEKVYRQKQPALFLSSFTDFYLDNKNDHHLQNVIKKGFSKLISTYLLPLYQQHPGTSVHFAGSVAFNFQEHLYEAAAEADLQITNIIKEPINNLLTYYSSKN
>NZ_CP043451.1|WP_091175145.1|462992_463979_-|6-phosphofructokinase
MRKISKIGVLTSGGDAPGMNPCIRAVVRTALYNGLEVVGIRQGYKGLIENDMYEMDKRSVSNILNLGGTILKTARCLPFKTDEGMEIAYQNAKARGIDALVVIGGDGTFTGALRFSRKYPDIAVMGVPGTIDNDLCGSTYTLGFDTATNTVIQAIDKIRDTADAHDRLFFIEVMGRDSGAIALRAGISCGAEAILLPERATAIDDLIVNLKEGHMNKKSSSIVIVAEGDKNGGVYDVAKAVQQEVKNYDIKVTILGHLQRGGAPSSFDRILGSRLGFAAVNALVAGESQKMVGLQANQIMMTDLEAALNHHEFKLEEDLLQMMDILSI
>NZ_CP043451.1|WP_090527735.1|464117_464801_+|NUDIX-hydrolase
MLPKFDSVFSIDCVIFGFEAGELKILLIERNEEPYKDWLALPGYIVEQDESIDDAAERILYELTGLRDLHMQQFHTFGEVNRHPQGRVITVAYYALIRINGQKELRPVTQYAKKAFWHPVSELPKLAFDHSEIFKTGFNKIKRRLHYQPIAFELLPEKFTLTQLQSLYEAVLDKKLDKRNFRKKMLSYGFLKELDEKQKGVSYRAAKLYKFDKRKYGKIFQGEMNLV
>NZ_CP043451.1|WP_112652617.1|465306_466167_-|N-acetylglucosamine-kinase
MIIIADGGSTKTNWCLVTEEGKKVYFNTEGYNPYFSSTEYIIQSLNESLPTDLEKNLITEVNYYGAGCSTPEMRKIVEEAMKVVFVGAKVNIGHDLLAAARALLGNTEGFAAILGTGTNTCIYDGKEVVHNIDSGAYILGDEGSGCYIGKKLLTDYLRGYMPEPVRALFWETYKLTPDDINEQVYTQPRANRFCASFSKFVYDNNVHIEYSRNLVRTSFEDFFRNLVTHYPDYQKYTFNCIGSVGYNFRNVLEEVVTENGMVVGNIIRSPIDNLVKYHLELAPSSL
>NZ_CP043451.1|WP_112652618.1|466496_467426_-|NGG1p-interacting-factor-NIF3
MNSNLSPINHNPDRRKFITQLSALAGTAALLSTPFAVDAITFTNPDEHITVGQIIDLFMKQVPGAPFPNTVDTLKSGNRDIVVTGIITTMFATIGIIEKAISLGANFIIAHEPTFYNHADETAWLASDDIFQYKKQLLDKHNIVIWRNHDTIHSLKPDGVGIGLLKQLDWVSYYKPETGNLLTIPSTSLSSLIETLKKKLKIEKVRYIGDPSQSCQKVLLLPGAAGGKRQITEMSTKKPDVLICGEISEWETAEYVRDAQAKGDKLSLIVLGHIASEEPGSEFMTGWLKQNVPGIKATHIHPGNSLAFM
>NZ_CP043451.1|WP_112652619.1|467533_468688_+|DUF2029-domain-containing-protein
MQKLAKLITNKPFVYSLWFGLSLFLVIKGVLTHQGFNNYTIFKYNFLNTIHQHNLYAYQPEHYYDLNHYGPVFSIIMAPFAILPDSIGVILWVLFNAFILFKAIQLLPLKKDQYVIVLLLCAHELMTASANVQSNPMIAALIILGFNFIKREQDFWAALMIALGAFIKLYGIVGLAFFFFSTNKPKFVLSFIFWSAVLFVLPMAISSPSFIIQTYHDWYTDLVIKNSDNQQSYMQEICVTGFIRRAFHYQDLKNMYVIGPALVLFGLSYLRVKAYKVLEYQRLILSSVLIFAVIFSSSAESSTYIIAFVGVAVWFMNLNRPVTGFEIFLLVLALLITSLSPSDLFPSFIRTQYIVPYKLKSIPCFLIWIKIIYETLTRDFVNEK
>NZ_CP043451.1|WP_112652620.1|468990_469959_+|glycosyltransferase-family-2-protein
MTYLADKKISIVIPSHNEEKNISYLIEQLRETLSPTGYAYELIFVDDGSRDNTLNELKINAELHPNVFYVELSRNFGKDYALKAGIAMAQGDAVITMDADLQHPPQLILKMLNLWENGYDIVYTYREGENPHGKGYQKVTSKLFYKGLNMLSDIKMENGTADFRLIDEKVVKQLKLIDEYEIFFRGIIKWAGYKQVGIPYVPSKRHTGEASYSFSKLVKLAVGSIVAFSARPLYIVSIIGLLVSSLAILYIPYVLVSYFLGYAVSGWASIIATIAFFGGLQLLVMSVIGVYVGKIFMQSKHRPHYIIRSSNVVIVDNDFIRV
>NZ_CP043451.1|WP_112652621.1|469939_470746_+|polysaccharide-deacetylase-family-protein
MILLGFDVEEFDMPFEYGKSIPFDEQLEISTRGTNAILKLLEQKNIKVTFFCTANYAINRPDVIKQMVTEGHEVASHGYYHSDFKVEHLMQSKLALENISGTEVTGFRMARMMPVDEAEIAKAGYEYNSSINPTWLPGRYNNFDKPRTWFYDHDVLQIPASVSPVIRFPLFWLSFHNLPLSLLKRMASATLKKDGYLNLYFHPWEFTNLHDKEKFGFPGYVSRNSGEAFARRIADFIDWASDKGYIFRRTDGFCEIIKNKIKQEAVLH

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Crispr_ID: NZ_CP043451_3

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP043451_3

465016-465103

Orphan

Consensus_repeat	Method
GATTGCTTCGTGCCTCGCAATGACG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP043451_3

>merge|NZ_CP043451|3|465016-465103|CRISPRCasFinder
GATTGCTTCGTGCCTCGCAATGACGGGGAGGGGCTATGCAAGTAGCCGCCCTGTAAAGTTCGCGATTGCTTCGTACCTCGCAATGACG

>NZ_CP043451|3|3|465016-465103|CRISPRCasFinder
GATTGCTTCGTGCCTCGCAATGACG	GGGAGGGGCTATGCAAGTAGCCGCCCTGTAAAGTTCGC
GATTGCTTCGTACCTCGCAATGACG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP043451.1\|WP_112652616.1\|462136_462985_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|225518
NZ_CP043451.1\|WP_091175145.1\|462992_463979_-\|6-phosphofructokinase	unknown	unknown	gnl\|CDD\|235111
NZ_CP043451.1\|WP_112652624.1\|472741_473710_-\|aldehyde-reductase	unknown	unknown	gnl\|CDD\|187538
NZ_CP043451.1\|WP_112652621.1\|469939_470746_+\|polysaccharide-deacetylase-family-protein	unknown	unknown	gnl\|CDD\|200566
NZ_CP043451.1\|WP_112652623.1\|471943_472729_-\|helix-turn-helix-transcriptional-regulator	unknown	unknown	gnl\|CDD\|225117
NZ_CP043451.1\|WP_112652614.1\|459239_460331_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|212735
NZ_CP043451.1\|WP_112652628.1\|458638_458797_-\|GIY-YIG-nuclease-family-protein	unknown	unknown	gnl\|CDD\|198395
NZ_CP043451.1\|WP_090527735.1\|464117_464801_+\|NUDIX-hydrolase	unknown	unknown	gnl\|CDD\|223979
NZ_CP043451.1\|WP_112652615.1\|461134_462130_-\|type-I-glyceraldehyde-3-phosphate-dehydrogenase	unknown	unknown	gnl\|CDD\|223135
NZ_CP043451.1\|WP_112652622.1\|471066_471540_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043451.1\|WP_112653556.1\|457719_458631_+\|IS982-family-transposase	unknown	unknown	gnl\|CDD\|372648
NZ_CP043451.1\|WP_090534923.1\|474191_474779_+\|sigma-70-family-RNA-polymerase-sigma-factor	unknown	unknown	gnl\|CDD\|274376
NZ_CP043451.1\|WP_112652918.1\|452949_454200_+\|DUF5103-domain-containing-protein	unknown	unknown	gnl\|CDD\|379920
NZ_CP043451.1\|WP_112652619.1\|467533_468688_+\|DUF2029-domain-containing-protein	unknown	unknown	gnl\|CDD\|378217
NZ_CP043451.1\|WP_112652617.1\|465306_466167_-\|N-acetylglucosamine-kinase	unknown	unknown	gnl\|CDD\|225518
NZ_CP043451.1\|WP_112652625.1\|474869_475862_+\|FecR-family-protein	unknown	unknown	gnl\|CDD\|226235
NZ_CP043451.1\|WP_112652919.1\|454884_455964_+\|AAA-family-ATPase	unknown	unknown	gnl\|CDD\|316042
NZ_CP043451.1\|WP_112652920.1\|456247_457219_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043451.1\|WP_112652618.1\|466496_467426_-\|NGG1p-interacting-factor-NIF3	unknown	unknown	gnl\|CDD\|376614
NZ_CP043451.1\|WP_112652620.1\|468990_469959_+\|glycosyltransferase-family-2-protein	unknown	unknown	gnl\|CDD\|133030

Protein	Function_ID	Function_description	E-value
NZ_CP043451.1\|WP_112652616.1\|462136_462985_-\|hypothetical-protein	gnl\|CDD\|225518	COG2971, COG2971, Predicted N-acetylglucosamine kinase [Carbohydrate transport and metabolism].	6.94073e-11
NZ_CP043451.1\|WP_091175145.1\|462992_463979_-\|6-phosphofructokinase	gnl\|CDD\|235111	PRK03202, PRK03202, ATP-dependent 6-phosphofructokinase.	1.45948e-157
NZ_CP043451.1\|WP_112652624.1\|472741_473710_-\|aldehyde-reductase	gnl\|CDD\|187538	cd05227, AR_SDR_e, aldehyde reductase, extended (e) SDRs. This subgroup contains aldehyde reductase of the extended SDR-type and related proteins. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it has an NADP-binding motif consensus that is slightly different from the canonical SDR form and lacks the Asn of the extended SDR active site tetrad. Aldehyde reductase I catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.	6.19208e-110
NZ_CP043451.1\|WP_112652621.1\|469939_470746_+\|polysaccharide-deacetylase-family-protein	gnl\|CDD\|200566	cd10941, CE4_PuuE_HpPgdA_like_2, Putative catalytic domain of uncharacterized prokaryotic polysaccharide deacetylases similar to bacterial PuuE allantoinases and Helicobacter pylori peptidoglycan deacetylase (HpPgdA). This family contains many uncharacterized prokaryotic polysaccharide deacetylases (DCAs) that show high sequence similarity to the catalytic domain of bacterial PuuE allantoinases and Helicobacter pylori peptidoglycan deacetylase (HpPgdA). PuuE allantoinase appears to be metal-independent and specifically catalyzes the hydrolysis of (S)-allantoin into allantoic acid. Different from PuuE allantoinase, HpPgdA has the ability to bind a metal ion at the active site and is responsible for a peptidoglycan modification that counteracts the host immune response. Both PuuE allantoinase and HpPgdA function as homotetramers. The monomer is composed of a 7-stranded barrel with detectable sequence similarity to the 6-stranded barrel NodB homology domain of DCA-like proteins in the CE4 superfamily, which removes N-linked or O-linked acetyl groups from cell wall polysaccharides. In contrast to typical NodB-like DCAs, PuuE allantoinase and HpPgdA do not exhibit a solvent-accessible polysaccharide binding groove and might only bind a small molecule at the active site.	4.36189e-67
NZ_CP043451.1\|WP_112652618.1\|466496_467426_-\|NGG1p-interacting-factor-NIF3	gnl\|CDD\|376614	pfam01784, NIF3, NIF3 (NGG1p interacting factor 3). This family contains several NIF3 (NGG1p interacting factor 3) protein homologs. NIF3 interacts with the yeast transcriptional coactivator NGG1p which is part of the ADA complex, the exact function of this interaction is unknown.	1.19209e-26
NZ_CP043451.1\|WP_112652628.1\|458638_458797_-\|GIY-YIG-nuclease-family-protein	gnl\|CDD\|198395	cd10448, GIY-YIG_unchar_3, GIY-YIG domain of uncharacterized hypothetical protein found in bacteria. The family includes a group of uncharacterized bacterial proteins with a GIY-YIG domain that shows statistically significant similarity to the N-terminal catalytic domains of GIY-YIG family of intron-encoded homing endonuclease I-TevI and catalytic GIY-YIG domain of nucleotide excision repair endonuclease UvrC.	6.10831e-21
NZ_CP043451.1\|WP_090527735.1\|464117_464801_+\|NUDIX-hydrolase	gnl\|CDD\|223979	COG1051, COG1051, ADP-ribose pyrophosphatase [Nucleotide transport and metabolism].	1.21402e-20
NZ_CP043451.1\|WP_112652615.1\|461134_462130_-\|type-I-glyceraldehyde-3-phosphate-dehydrogenase	gnl\|CDD\|223135	COG0057, GapA, Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate transport and metabolism].	0
NZ_CP043451.1\|WP_112653556.1\|457719_458631_+\|IS982-family-transposase	gnl\|CDD\|372648	pfam13612, DDE_Tnp_1_3, Transposase DDE domain. Transposase proteins are necessary for efficient DNA transposition. This domain is a member of the DDE superfamily, which contains 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.	9.44762e-83
NZ_CP043451.1\|WP_090534923.1\|474191_474779_+\|sigma-70-family-RNA-polymerase-sigma-factor	gnl\|CDD\|274376	TIGR02985, Sig70_bacteroi1, RNA polymerase sigma-70 factor, Bacteroides expansion family 1. This group of sigma factors are members of the sigma-70 family (TIGR02937) and are found primarily in the genus Bacteroides. This family appears to have resulted from a lineage-specific expansion as B. thetaiotaomicron VPI-5482, Bacteroides forsythus ATCC 43037, Bacteroides fragilis YCH46 and Bacteroides fragilis NCTC 9343 contain 25, 12, 24 and 23 members, respectively. There are currentlyonly two known members of this family outside of the Bacteroides, in Rhodopseudomonas and Bradyrhizobium.	8.17806e-32
NZ_CP043451.1\|WP_112652918.1\|452949_454200_+\|DUF5103-domain-containing-protein	gnl\|CDD\|379920	pfam17116, DUF5103, Domain of unknown function (DUF5103). This is a family of Bacteroidetes proteins of unknown function.	6.92899e-109
NZ_CP043451.1\|WP_112652619.1\|467533_468688_+\|DUF2029-domain-containing-protein	gnl\|CDD\|378217	pfam09594, GT87, Glycosyltransferase family 87. The enzymes in this family are glycosyltransferases. PimE is involved in phosphatidylinositol mannoside (PIM) synthesis, a major class of glycolipids in all mycobacteria. PimE is a polyprenol-phosphate-mannose-dependent mannosyltransferase that transfers the fifth mannose of PIM. The family also includes alpha(1-->3) arabinofuranosyltransferase, invloved in the synthesis of of mycobacterial arabinogalactan.	2.82878e-15
NZ_CP043451.1\|WP_112652617.1\|465306_466167_-\|N-acetylglucosamine-kinase	gnl\|CDD\|225518	COG2971, COG2971, Predicted N-acetylglucosamine kinase [Carbohydrate transport and metabolism].	1.12096e-12
NZ_CP043451.1\|WP_112652614.1\|459239_460331_+\|hypothetical-protein	gnl\|CDD\|212735	cd11801, SH3_JIP1_like, Src homology 3 domain of JNK-interacting proteins 1 and 2, and similar domains. JNK-interacting proteins (JIPs) function as scaffolding proteins for c-Jun N-terminal kinase (JNK) signaling pathways. They bind to components of Mitogen-activated protein kinase (MAPK) pathways such as JNK, MKK, and several MAP3Ks such as MLK and DLK. There are four JIPs (JIP1-4); all contain a JNK binding domain. JIP1 and JIP2 also contain SH3 and Phosphotyrosine-binding (PTB) domains. Both are highly expressed in the brain and pancreatic beta-cells. JIP1 functions as an adaptor linking motor to cargo during axonal transport and also is involved in regulating insulin secretion. JIP2 form complexes with fibroblast growth factor homologous factors (FHFs), which facilitates activation of the p38delta MAPK. The SH3 domain of JIP1 homodimerizes at the interface usually involved in proline-rich ligand recognition, despite the lack of this motif in the domain itself. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.	0.00919906
NZ_CP043451.1\|WP_112652625.1\|474869_475862_+\|FecR-family-protein	gnl\|CDD\|226235	COG3712, FecR, periplasmic ferric-dicitrate binding protein FecR, regulates iron transport through sigma-19 [Inorganic ion transport and metabolism, Signal transduction mechanisms].	3.93725e-21
NZ_CP043451.1\|WP_112652919.1\|454884_455964_+\|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.	1.17565e-14
NZ_CP043451.1\|WP_112652623.1\|471943_472729_-\|helix-turn-helix-transcriptional-regulator	gnl\|CDD\|225117	COG2207, AraC, AraC-type DNA-binding domain-containing proteins [Transcription].	2.36076e-16
NZ_CP043451.1\|WP_112652620.1\|468990_469959_+\|glycosyltransferase-family-2-protein	gnl\|CDD\|133030	cd04187, DPM1_like_bac, Bacterial DPM1_like enzymes are related to eukaryotic DPM1. A family of bacterial enzymes related to eukaryotic DPM1; Although the mechanism of eukaryotic enzyme is well studied, the mechanism of the bacterial enzymes is not well understood. The eukaryotic DPM1 is the catalytic subunit of eukaryotic Dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. The enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. This protein family belongs to Glycosyltransferase 2 superfamily.	1.59539e-76

>NZ_CP043451.1|WP_090527735.1|464117_464801_+|NUDIX-hydrolase
MLPKFDSVFSIDCVIFGFEAGELKILLIERNEEPYKDWLALPGYIVEQDESIDDAAERILYELTGLRDLHMQQFHTFGEVNRHPQGRVITVAYYALIRINGQKELRPVTQYAKKAFWHPVSELPKLAFDHSEIFKTGFNKIKRRLHYQPIAFELLPEKFTLTQLQSLYEAVLDKKLDKRNFRKKMLSYGFLKELDEKQKGVSYRAAKLYKFDKRKYGKIFQGEMNLV
>NZ_CP043451.1|WP_091175145.1|462992_463979_-|6-phosphofructokinase
MRKISKIGVLTSGGDAPGMNPCIRAVVRTALYNGLEVVGIRQGYKGLIENDMYEMDKRSVSNILNLGGTILKTARCLPFKTDEGMEIAYQNAKARGIDALVVIGGDGTFTGALRFSRKYPDIAVMGVPGTIDNDLCGSTYTLGFDTATNTVIQAIDKIRDTADAHDRLFFIEVMGRDSGAIALRAGISCGAEAILLPERATAIDDLIVNLKEGHMNKKSSSIVIVAEGDKNGGVYDVAKAVQQEVKNYDIKVTILGHLQRGGAPSSFDRILGSRLGFAAVNALVAGESQKMVGLQANQIMMTDLEAALNHHEFKLEEDLLQMMDILSI
>NZ_CP043451.1|WP_112652616.1|462136_462985_-|hypothetical-protein
MIAVVYSGSYFAHWRLTDKGRTVASFKTNGINPYFNDEKHILQLLNKNINLIHHAEVIRRIYFFGAGASSDERKKIVHSAFSTFFKFGKISIEHDIAGAAIACCKNEPGIVSICGSGSNAAWYDGKRVWPNNYGLGYILADEGSGNWLGRQLIKEFMNDTLPLSIRKKFIHKYDADRKNLLEKVYRQKQPALFLSSFTDFYLDNKNDHHLQNVIKKGFSKLISTYLLPLYQQHPGTSVHFAGSVAFNFQEHLYEAAAEADLQITNIIKEPINNLLTYYSSKN
>NZ_CP043451.1|WP_112652615.1|461134_462130_-|type-I-glyceraldehyde-3-phosphate-dehydrogenase
MKIGINGFGRIGRLAFRAAIERPDIEVVGINDLVEPDYMAYMLKYDSTHGQFNGTIAVEGGHLVVNGKTIRVTAEKDPANLKWNEVGAEVVIESTGLFLTQETAQKHIDAGAKKVVMSAPAKDDTPTFVMGVNHKALKADQNIVSNASCTTNCLAPIAKVLDDKFGIEEGLMTTVHAVTATQKTVDGPSAKDWRGGRGAYQNIIPSSTGAAKAVGLVLPQLKGKLTGMSLRVPVADVSVVDLTVRLKNGASYEAIKAAMKEASEGELKGILGYTEDEVVSEDFKGDSRTSIFDAKAGIGLNENFVKVVSWYDNEWGYSNKLIDLVQELGKL
>NZ_CP043451.1|WP_112652614.1|459239_460331_+|hypothetical-protein
MLKVEYAKHEDDQTYYLVVNDIPYYQSSYNDRTYRSAYINEIELGELLASYSSKELSEFFDSLNMGDYDFDAWPLGVDISFSFKKTYKSSDYPNFNVELNVDTEDWASGWSIKSFSEALKIIIKDRDNKNVRYFQLDDDFVSNGLGIAVAINDLDTPIGTLIDNAFPEFESIINDANLYLASVVDNQSVISFFNFPDSIKGPCQQYLMYFAQFLKDLGIEAETEIKEQAHSTLFKITPNNKDEALDKIKDALEIYTNAPALNDLQFQGMNNGDIAFMQLQANVMHLKSQIMLNNAALQMKDATIEALQLSNYQLKAIVVESNEKLKQEEEIIPGIMSIKKYDGEWFSLNLPEMLNRLKRRFIK
>NZ_CP043451.1|WP_112652628.1|458638_458797_-|GIY-YIG-nuclease-family-protein
MQRGGCVYIITNKNNSVLYTGVTSDIIGRIFDHKNKTYPQSFTAKYNCNKLT
>NZ_CP043451.1|WP_112653556.1|457719_458631_+|IS982-family-transposase
MLTSDKIIEIFVKVDDFCKECEEQIAKHKLDAGNYKVRDRKASLADSEIITIVIAFHSGHFTNLKHFYITHICSHYKDFFPGLVSYNRFVELQQRVAVPMMLFLKTHCLGRSRGINFIDSTHIKVCHNRRIHNHKVFAATAERGQCSIGWFYGFKLHLIINDKGEILSFYLTKGNVDDRNVKLMTSMTEEIFGKLFGDKGYISKALADLLWGNGIQMITKPRKNMKDFNISQADKIMLRKRAIIECVYDELKNICKLQHTRHRSVNNFLMNIMGSLCAYHFFPKKPSLNIVFEEQDNQLLLAA
>NZ_CP043451.1|WP_112652920.1|456247_457219_+|hypothetical-protein
MKYQLQPYQGMQSRYSCPVCNHHKCFVRYIDIQTGQHLAPHVGRCGREDKCGYHLTPRNYFATLPGYKPYQPKRSRYMPGKSPAQPAVNPARSPRPEPKYIINPYWVSATLYNYQDNNFVQYLIKRLGRDITQAAIKRYHIGTHNHWPGACVFWQYDTEGDVRTGKIMLYNKETGKRVKVPFNHITWAHTLAIKEAATAGDDTTFILQQCLFGEHLLSANPAMPVAIVESEKTAIIASALIPDFIWLASGSLQGLNPAKCGVLKGRRVMLFPDVNAYDKWKLKARELHTALPNTAFSVSAVLEDIATDEDRQNGIDIGDVVGW
>NZ_CP043451.1|WP_112652919.1|454884_455964_+|AAA-family-ATPase
MITQNLNNSTATCITAGSLAQQSLQQMDEQQLPQNNDDVLMVRHADHWMAEAHERAIPLMLFGKFWHQGEVCILFADSNLGKSIVAVQVADGVSKGSGKYPFDVEAPAQPVLYCDFELTDKQFEARYSVDYEYHYHFGKNFYRAELNPDMELPHEFADFDDYLIYSLERSVLQTGAKVLVIDNLTYLRSETERAKDALPLMKQLKALKNKYNLSILVLAHTPKRDMAQPITRNDLQGSKMLMNFCDSAFAIGESKTDVNMRYLKQIKQRNTEQLYGEGNVCLCQIGKPYNFLKYEFVSFGKEWEQLSPQNDPEQEQIMANANELKQQGLTLRQIGQKLGISHQKADRLLKAYAKLNANV
>NZ_CP043451.1|WP_112652918.1|452949_454200_+|DUF5103-domain-containing-protein
MKKLYIILFILLSLNSFAQSPYNNNVYSPAIKSVEFYNTAKQGTFPVINLGTDEKVLLTFDDLRGGSRNYYYTIEHCDANWNSSNLSSAEYLQSFTDDRLYNYSYSTGTMQKYTHYEISLPNNNIAPKISGNYVLKVYEDGDQSKMVLTRRLYVLGKRVSIAADLVASANNATRQTNQKINFTVDYSGLVVQNPAYALRTFIMQNARTETAVLNGQPTYIRGSQLIYNDVSVNDFPGRNEFRLFDTRTLKLNSQRVAKIYKDSTNVVVLLGDPVRDQPNYIFQYDNDGKFYILNNDGTTPATDADYAHVYFTLSTNKDPKEGSPYVVGQFNNYRLDDSNKLHPLDNGRYTVNMLLKQGVYDYEYVWVDAKTGKADDIPFEGSHFETENEYQVLTYYRPPAARWDELVGFRELVTKR
>NZ_CP043451.1|WP_112652617.1|465306_466167_-|N-acetylglucosamine-kinase
MIIIADGGSTKTNWCLVTEEGKKVYFNTEGYNPYFSSTEYIIQSLNESLPTDLEKNLITEVNYYGAGCSTPEMRKIVEEAMKVVFVGAKVNIGHDLLAAARALLGNTEGFAAILGTGTNTCIYDGKEVVHNIDSGAYILGDEGSGCYIGKKLLTDYLRGYMPEPVRALFWETYKLTPDDINEQVYTQPRANRFCASFSKFVYDNNVHIEYSRNLVRTSFEDFFRNLVTHYPDYQKYTFNCIGSVGYNFRNVLEEVVTENGMVVGNIIRSPIDNLVKYHLELAPSSL
>NZ_CP043451.1|WP_112652618.1|466496_467426_-|NGG1p-interacting-factor-NIF3
MNSNLSPINHNPDRRKFITQLSALAGTAALLSTPFAVDAITFTNPDEHITVGQIIDLFMKQVPGAPFPNTVDTLKSGNRDIVVTGIITTMFATIGIIEKAISLGANFIIAHEPTFYNHADETAWLASDDIFQYKKQLLDKHNIVIWRNHDTIHSLKPDGVGIGLLKQLDWVSYYKPETGNLLTIPSTSLSSLIETLKKKLKIEKVRYIGDPSQSCQKVLLLPGAAGGKRQITEMSTKKPDVLICGEISEWETAEYVRDAQAKGDKLSLIVLGHIASEEPGSEFMTGWLKQNVPGIKATHIHPGNSLAFM
>NZ_CP043451.1|WP_112652619.1|467533_468688_+|DUF2029-domain-containing-protein
MQKLAKLITNKPFVYSLWFGLSLFLVIKGVLTHQGFNNYTIFKYNFLNTIHQHNLYAYQPEHYYDLNHYGPVFSIIMAPFAILPDSIGVILWVLFNAFILFKAIQLLPLKKDQYVIVLLLCAHELMTASANVQSNPMIAALIILGFNFIKREQDFWAALMIALGAFIKLYGIVGLAFFFFSTNKPKFVLSFIFWSAVLFVLPMAISSPSFIIQTYHDWYTDLVIKNSDNQQSYMQEICVTGFIRRAFHYQDLKNMYVIGPALVLFGLSYLRVKAYKVLEYQRLILSSVLIFAVIFSSSAESSTYIIAFVGVAVWFMNLNRPVTGFEIFLLVLALLITSLSPSDLFPSFIRTQYIVPYKLKSIPCFLIWIKIIYETLTRDFVNEK
>NZ_CP043451.1|WP_112652620.1|468990_469959_+|glycosyltransferase-family-2-protein
MTYLADKKISIVIPSHNEEKNISYLIEQLRETLSPTGYAYELIFVDDGSRDNTLNELKINAELHPNVFYVELSRNFGKDYALKAGIAMAQGDAVITMDADLQHPPQLILKMLNLWENGYDIVYTYREGENPHGKGYQKVTSKLFYKGLNMLSDIKMENGTADFRLIDEKVVKQLKLIDEYEIFFRGIIKWAGYKQVGIPYVPSKRHTGEASYSFSKLVKLAVGSIVAFSARPLYIVSIIGLLVSSLAILYIPYVLVSYFLGYAVSGWASIIATIAFFGGLQLLVMSVIGVYVGKIFMQSKHRPHYIIRSSNVVIVDNDFIRV
>NZ_CP043451.1|WP_112652621.1|469939_470746_+|polysaccharide-deacetylase-family-protein
MILLGFDVEEFDMPFEYGKSIPFDEQLEISTRGTNAILKLLEQKNIKVTFFCTANYAINRPDVIKQMVTEGHEVASHGYYHSDFKVEHLMQSKLALENISGTEVTGFRMARMMPVDEAEIAKAGYEYNSSINPTWLPGRYNNFDKPRTWFYDHDVLQIPASVSPVIRFPLFWLSFHNLPLSLLKRMASATLKKDGYLNLYFHPWEFTNLHDKEKFGFPGYVSRNSGEAFARRIADFIDWASDKGYIFRRTDGFCEIIKNKIKQEAVLH
>NZ_CP043451.1|WP_112652622.1|471066_471540_+|hypothetical-protein
MKPYFKVITTLFLISVVKVSFAQTPSFGNYKTKIFIGRAAKLKIKGNALAERYKTAISNSYNDDPYIRKFHGKGGLNFAGHYCFAYWGCGSDCQQSAIVDLQTGKVYDGPTAARQFEYRRWSRLLIVNRPGDKSDCAVCQPEYWILNEQTKHFVKIK
>NZ_CP043451.1|WP_112652623.1|471943_472729_-|helix-turn-helix-transcriptional-regulator
MITSSLQSCHLGPGMSPEQVISDHFFLYLLKGSMLAYSGDKHYHFHPGDSCIARKNHLLRYTKQQQDGDFKKIVIVLDEAFLKRFLARHRVDPSIATSDYSIRPVKDDQLLTSFIHSLEPYYRGEAEIEEAFADLKREELLLILLKNDPGLAAVLFNFGAPQKIDIEAFMTRNFRFNVPLERFAFLTGRSLSAFKRDFQQIYNDTPGRWLTKKRLEEAYFLIHQQSQKPKDIYLELGFENLSHFSFAFKKQFGLAPTAVLY
>NZ_CP043451.1|WP_112652624.1|472741_473710_-|aldehyde-reductase
MENNIKQPTVLVTGGTGFIGIYCILQLLQQGYTVKTTLRSLKRKDEVINLLKGAGIKSFENLAFVEADLTNDLNWNWAADGCTYVLHVASPFPAEEPEDANDLIIPARDGALRVLKAARHAGVKRVVLTSSFAAIGYSKDPKGYTFTEEDWTDPELTDRAYIKSKTIAEKAAWDWINSEGDGMELTVINPVGVFGPALGKDFSTSIGFVKGVLDGQIKETLPFTFGVVDVRDVAYIHLKAMTHPAAAGERFLATATGVMSLYDVAELIRKERPEYAGNIANLKPLDESFYIAISNEKAQRVLNWYPRSKEEVILASVDSLLN
>NZ_CP043451.1|WP_090534923.1|474191_474779_+|sigma-70-family-RNA-polymerase-sigma-factor
MKPIELNHTDDVLLLQQIEQGSQHAFNLLYEKHWGNAYSEAYKRLKDSDQAKDIVQEVFTHIWLKKESLRIHNLPAYLTVAIRNKVFKLVEKQKIIHPFFDVIDDLPASCQQADDNLLWKEFLISYEALLNTLPPKRQIIFRLHYQNDLPTKEIAAQLGLTRKTVQNQLLKAIEKLKVSLLPFLSLLIILFGAIK
>NZ_CP043451.1|WP_112652625.1|474869_475862_+|FecR-family-protein
MDKQYFLELLHKYLNNEATDEEQQFLVKYYELFSAEPDIISLLSDEQKNEIKEEINASIWENIDKHTGVDKKIIRLKTWVNKIAAAAAIIGVCGIGYLFLHNKSVVKPPQSYSAHRPKPNLFLVLPDGSRVILSYGSKLSYASSFDGLTKREVYLTGEAFFDIKHNNLKPFVVHTGKIKTTVLGTAFDVKAVPGDKTITVTVTRGKVKVSNNNKLLGIIVPNQQITFDRQKSISMQTNINAKNYTIWTAKDDLYFEDVTFGEAAKVLEDRFKVKILFTDQLVRSKHFTSTFNKSANLDQALKSICEFNDATYSYDKAKTTITITTKSQTN

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Crispr_ID: NZ_CP043451_4

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP043451_4

1032444-1032573

Orphan

Consensus_repeat	Method
GCAGGAATAGTGGGTGGAGTACTCGTGACTTCATCTTCA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP043451_4

>merge|NZ_CP043451|4|1032444-1032573|CRISPRCasFinder
GCAGGAATAGTGGGTGGAGTACTCGTGACTTCATCTTCAGCGGTGGCACGGGGACTTTCATTTTTAACTGTCACTGGCGCGAGTATGCAGTGCAGGAATAGTGGGTGGAGTACTCGTGACTTCATCTTCA

>NZ_CP043451|4|4|1032444-1032573|CRISPRCasFinder
GCAGGAATAGTGGGTGGAGTACTCGTGACTTCATCTTCA	GCGGTGGCACGGGGACTTTCATTTTTAACTGTCACTGGCGCGAGTATGCAGT
GCAGGAATAGTGGGTGGAGTACTCGTGACTTCATCTTCA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP043451.1\|WP_112654130.1\|1035390_1036254_+\|SIR2-family-protein	unknown	unknown	gnl\|CDD\|379106
NZ_CP043451.1\|WP_112654144.1\|1019079_1019553_+\|DNA-starvation/stationary-phase-protection-protein	unknown	unknown	gnl\|CDD\|153102
NZ_CP043451.1\|WP_112654143.1\|1020071_1021832_+\|family-78-glycoside-hydrolase-catalytic-domain	unknown	unknown	gnl\|CDD\|379971
NZ_CP043451.1\|WP_112654126.1\|1040148_1040835_-\|NUDIX-hydrolase	unknown	unknown	gnl\|CDD\|223979
NZ_CP043451.1\|WP_112654129.1\|1036415_1037318_-\|ribose-phosphate-pyrophosphokinase	unknown	unknown	gnl\|CDD\|223538
NZ_CP043451.1\|WP_112654138.1\|1026180_1027320_+\|XdhC-family-protein	unknown	unknown	gnl\|CDD\|379212
NZ_CP043451.1\|WP_112654137.1\|1027769_1029062_+\|NAD(P)/FAD-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|224172
NZ_CP043451.1\|WP_112654131.1\|1034395_1035385_+\|ParA-family-protein	unknown	unknown	gnl\|CDD\|224113
NZ_CP043451.1\|WP_112654136.1\|1029744_1031289_+\|carboxylesterase-family-protein	unknown	unknown	gnl\|CDD\|365897
NZ_CP043451.1\|WP_112654135.1\|1031375_1032269_+\|flavin-reductase-family-protein	unknown	unknown	gnl\|CDD\|224766
NZ_CP043451.1\|WP_146750447.1\|1041004_1041634_+\|RNA-polymerase-sigma-70-factor	unknown	unknown	gnl\|CDD\|274376
NZ_CP043451.1\|WP_112654139.1\|1024033_1026166_+\|xanthine-dehydrogenase-family-protein-molybdopterin-binding-subunit	unknown	unknown	gnl\|CDD\|224446
NZ_CP043451.1\|WP_112654141.1\|1022368_1023004_+\|(2Fe-2S)-binding-protein	unknown	unknown	gnl\|CDD\|224991
NZ_CP043451.1\|WP_167516081.1\|1033243_1033417_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043451.1\|WP_112654127.1\|1038807_1039704_-\|NUDIX-domain-containing-protein	unknown	unknown	gnl\|CDD\|235436
NZ_CP043451.1\|WP_112654142.1\|1021836_1022208_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|319937
NZ_CP043451.1\|WP_112654128.1\|1037384_1038803_-\|nicotinate-phosphoribosyltransferase	unknown	unknown	gnl\|CDD\|236407
NZ_CP043451.1\|WP_112654140.1\|1023000_1023993_+\|xanthine-dehydrogenase-family-protein-subunit-M	unknown	unknown	gnl\|CDD\|224238
NZ_CP043451.1\|WP_112654133.1\|1032640_1033210_+\|transposase	unknown	unknown	gnl\|CDD\|376616
NZ_CP043451.1\|WP_112654132.1\|1033487_1033964_-\|hypothetical-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_CP043451.1\|WP_112654130.1\|1035390_1036254_+\|SIR2-family-protein	gnl\|CDD\|379106	pfam13289, SIR2_2, SIR2-like domain. This family of proteins are related to the sirtuins.	1.99325e-22
NZ_CP043451.1\|WP_112654144.1\|1019079_1019553_+\|DNA-starvation/stationary-phase-protection-protein	gnl\|CDD\|153102	cd01043, DPS, DPS protein, ferritin-like diiron-binding domain. DPS (DNA Protecting protein under Starved conditions) domain is a member of a broad superfamily of ferritin-like diiron-carboxylate proteins. Some DPS proteins nonspecifically bind DNA, protecting it from cleavage caused by reactive oxygen species such as the hydroxyl radicals produced during oxidation of Fe(II) by hydrogen peroxide. These proteins assemble into dodecameric structures, some form DPS-DNA co-crystalline complexes, and possess iron and H2O2 detoxification capabilities. Expression of DPS is induced by oxidative or nutritional stress, including metal ion starvation. Members of the DPS family are homopolymers formed by 12 four-helix bundle subunits that assemble with 23 symmetry into a hollow shell. The DPS ferroxidase site is unusual in that it is not located in a four-helix bundle as in ferritin, but is shared by 2-fold symmetry-related subunits providing the iron ligands. Many DPS sequences (e.g., E. coli) display an N-terminal extension of variable length that contains two or three positively charged lysine residues that extends into the solvent and is thought to play an important role in the stabilization of the complex with DNA. DPS Listeria Flp, Bacillus anthracis Dlp-1 and Dlp-2, and Helicobacter pylori HP-NAP which lack the N-terminal extension, do not bind DNA. DPS proteins from Helicobacter pylori, Treponema pallidum, and Borrelia burgdorferi are highly immunogenic.	4.89855e-48
NZ_CP043451.1\|WP_112654143.1\|1020071_1021832_+\|family-78-glycoside-hydrolase-catalytic-domain	gnl\|CDD\|379971	pfam17389, Bac_rhamnosid6H, Bacterial alpha-L-rhamnosidase 6 hairpin glycosidase domain. This family consists of bacterial rhamnosidase A and B enzymes. L-Rhamnose is abundant in biomass as a common constituent of glycolipids and glycosides, such as plant pigments, pectic polysaccharides, gums or biosurfactants. Some rhamnosides are important bioactive compounds. For example, terpenyl glycosides, the glycosidic precursor of aromatic terpenoids, act as important flavouring substances in grapes. Other rhamnosides act as cytotoxic rhamnosylated terpenoids, as signal substances in plants or play a role in the antigenicity of pathogenic bacteria.	3.8152e-16
NZ_CP043451.1\|WP_112654126.1\|1040148_1040835_-\|NUDIX-hydrolase	gnl\|CDD\|223979	COG1051, COG1051, ADP-ribose pyrophosphatase [Nucleotide transport and metabolism].	4.78461e-33
NZ_CP043451.1\|WP_112654129.1\|1036415_1037318_-\|ribose-phosphate-pyrophosphokinase	gnl\|CDD\|223538	COG0462, PrsA, Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism / Amino acid transport and metabolism].	4.81152e-64
NZ_CP043451.1\|WP_112654138.1\|1026180_1027320_+\|XdhC-family-protein	gnl\|CDD\|379212	pfam13478, XdhC_C, XdhC Rossmann domain. This entry is the rossmann domain found in the Xanthine dehydrogenase accessory protein.	5.81388e-47
NZ_CP043451.1\|WP_112654137.1\|1027769_1029062_+\|NAD(P)/FAD-dependent-oxidoreductase	gnl\|CDD\|224172	COG1252, Ndh, NADH dehydrogenase, FAD-containing subunit [Energy production and conversion].	1.83067e-122
NZ_CP043451.1\|WP_112654131.1\|1034395_1035385_+\|ParA-family-protein	gnl\|CDD\|224113	COG1192, Soj, ATPases involved in chromosome partitioning [Cell division and chromosome partitioning].	4.00994e-30
NZ_CP043451.1\|WP_112654136.1\|1029744_1031289_+\|carboxylesterase-family-protein	gnl\|CDD\|365897	pfam00135, COesterase, Carboxylesterase family.	1.01512e-127
NZ_CP043451.1\|WP_112654135.1\|1031375_1032269_+\|flavin-reductase-family-protein	gnl\|CDD\|224766	COG1853, COG1853, Conserved protein/domain typically associated with flavoprotein oxygenases, DIM6/NTAB family [General function prediction only].	1.27935e-31
NZ_CP043451.1\|WP_146750447.1\|1041004_1041634_+\|RNA-polymerase-sigma-70-factor	gnl\|CDD\|274376	TIGR02985, Sig70_bacteroi1, RNA polymerase sigma-70 factor, Bacteroides expansion family 1. This group of sigma factors are members of the sigma-70 family (TIGR02937) and are found primarily in the genus Bacteroides. This family appears to have resulted from a lineage-specific expansion as B. thetaiotaomicron VPI-5482, Bacteroides forsythus ATCC 43037, Bacteroides fragilis YCH46 and Bacteroides fragilis NCTC 9343 contain 25, 12, 24 and 23 members, respectively. There are currentlyonly two known members of this family outside of the Bacteroides, in Rhodopseudomonas and Bradyrhizobium.	2.54776e-44
NZ_CP043451.1\|WP_112654139.1\|1024033_1026166_+\|xanthine-dehydrogenase-family-protein-molybdopterin-binding-subunit	gnl\|CDD\|224446	COG1529, CoxL, Aerobic-type carbon monoxide dehydrogenase, large subunit CoxL/CutL homologs [Energy production and conversion].	0
NZ_CP043451.1\|WP_112654141.1\|1022368_1023004_+\|(2Fe-2S)-binding-protein	gnl\|CDD\|224991	COG2080, CoxS, Aerobic-type carbon monoxide dehydrogenase, small subunit CoxS/CutS homologs [Energy production and conversion].	1.3919e-80
NZ_CP043451.1\|WP_112654127.1\|1038807_1039704_-\|NUDIX-domain-containing-protein	gnl\|CDD\|235436	PRK05379, PRK05379, bifunctional nicotinamide-nucleotide adenylyltransferase/Nudix hydroxylase.	7.20937e-13
NZ_CP043451.1\|WP_112654142.1\|1021836_1022208_-\|hypothetical-protein	gnl\|CDD\|319937	cd08349, BLMA_like, Bleomycin binding protein (BLMA) and similar proteins. BLMA also called Bleomycin resistance protein, confers Bm resistance by directly binding to Bm. Bm is a glycopeptide antibiotic produced naturally by actinomycetes. It is a potent anti-cancer drug, which acts as a strong DNA-cutting agent, thereby causing cell death. BLMA is produced by actinomycetes to protect themselves against their own lethal compound. BLMA has two identically-folded subdomains, with the same alpha/beta fold; these two halves have no sequence similarity. BLMAs are dimers and each dimer binds to two Bm molecules at the Bm-binding pockets formed at the dimer interface; two Bm molecules are bound per dimer. BLMA belongs to a conserved domain superfamily that is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. As for the larger superfamily, this family contains members with or without domain swapping.	1.0891e-21
NZ_CP043451.1\|WP_112654128.1\|1037384_1038803_-\|nicotinate-phosphoribosyltransferase	gnl\|CDD\|236407	PRK09198, PRK09198, putative nicotinate phosphoribosyltransferase; Provisional.	0
NZ_CP043451.1\|WP_112654140.1\|1023000_1023993_+\|xanthine-dehydrogenase-family-protein-subunit-M	gnl\|CDD\|224238	COG1319, CoxM, Aerobic-type carbon monoxide dehydrogenase, middle subunit CoxM/CutM homologs [Energy production and conversion].	4.04856e-79
NZ_CP043451.1\|WP_112654133.1\|1032640_1033210_+\|transposase	gnl\|CDD\|376616	pfam01797, Y1_Tnp, Transposase IS200 like. Transposases are needed for efficient transposition of the insertion sequence or transposon DNA. This family includes transposases for IS200 from E. coli.	0.0023084

>NZ_CP043451.1|WP_112654135.1|1031375_1032269_+|flavin-reductase-family-protein
MKLRTIDASSLTPAEMQAYLHYAIAPRPICFVSTIDKNGGVNLSPFSFFNVFSINPPICVFSPTSRARDNTTKHTLENVLEVPECVINIVNYDMVQQTYLTSMDYKKGVNEFAKAGFTELASDTVKPPRVAESTVQLECAVNDVISLGKNGGAGNLVIAEVKRIHISEAILDANDKIDPHKIDLVARLGGDWYCRVTGDNLFKISKPTGSAGIGIGVDAFPIDVKYSKVLTGNDLGVLGLVETLPSYEEVSAFSKTDEMKELVDAATSDTRTLHLHLKAKQLLDNGRVMDAWKVLLM
>NZ_CP043451.1|WP_112654136.1|1029744_1031289_+|carboxylesterase-family-protein
MRRLIFMLASVLTVVAANAQPAPVKVNEGLLQGTFENSLTVYKGIPFAAPPVGKLRWCPPQPAAKWDGVRLADKFAPEPMQGGNPVSGKSEDCLYLNVWTPAKSPDSKIPVLVWIYGGAFNAGGTAEPAYNGANLAKKNVVLVSIAYRVGQLGFLAHPELSAESPNHVSGNYGLLDMIAALKWIKQNIAAFGGDPGKVTIFGESAGGIAVSMLCASPLAKGLFRGAISESGGSFGPTRTTTFPGENMKKLHDAEAAGEAYAKGAGYPSIDSLRKVDADKLPAVRGLAWPIVDGWVIPDDQYKLYEAGKYNDIPILVGYNSDEGASFSPPKTTDDYIAAVKNRYGKFADELIKAYPPGTGTVAKTARDLTRDAAFGWHTWSWATLQAKRGKSKVFYYYFDRHPEYPAGSPQAGYGSPHAQEVAYVFGLLNASGAQAKADLDISDAMSTYWTNFAKYGDPNGAGKPQWPAYSPARPVVMYFSQTAHTGPVPDLASLKVLDAYFRWRRSPDGEADVK
>NZ_CP043451.1|WP_112654137.1|1027769_1029062_+|NAD(P)/FAD-dependent-oxidoreductase
MTSITPQSGKKKIVIVGGGFAGLNIAQQLYKNKYYDVTLVDKNNYNYFTPLLYQVATSFLEPSSISYPFRKLFRDKRLSFRMAAVVKVDPAAKILYLSNGELSYDYLVFAAGASTNFYGIESIKQNAISLKEIDDALRMRNSLIKTMEKAAITTDPVERQKLLTIVVAGGGPTGVEVAGMLAEMKNYILKKDYPELMNAKGKIYIVDGGPDLLAPMSDKTHKETRQALIEWGVEVKLNAHVNDFNNGVITFADGETLEAKTLIWAAGIIANTFEGIPASSLGIGRRMITDEYNRVKDLEDIYAIGDISVQITDPVYPKGHPQLAQVAIQMGRNTAKNFIAMAKGKAIKPFKYFDRGDMAIVGRHNAVVDLFKHKVHLSGIAALFVWLFIHLMSLVNYNNKIKTLYNWAVAFLTRDQALRMIFGSGQSRAD
>NZ_CP043451.1|WP_112654138.1|1026180_1027320_+|XdhC-family-protein
MKEIIDIVAAYDEAHAQGKKTALATVVLVEGSAYRRAGARMLITEDGQLTGAISGGCLEGDALRKARLVILQQQPLLVTYDTTDDDDAKLGVGLGCNGIIHILIEPITSDINNPISLLKNIVSNGQHAVLATVFSVKDRKATQPGTCLCLTEDKLTVSHSGQLPYQVALVSDAERVLEEQRSEIRFYQADTEYTAFVEHIKPMISLVIVGAGNDAIPLTRIAAVLGWNITVIDGRPNYAVKQRFPFAQNIVTAKPADVLSHIKTNDRTAIVMMTHNYNYEVALLKELLPTSLPYIGILGPKKKLDRMLAEVEHAGISISEAQMNNIYGPVGLDIGAEGAEEIALSIMSEIKAVLSARQGYSLKYKPAPIHISNLQYLVK
>NZ_CP043451.1|WP_112654139.1|1024033_1026166_+|xanthine-dehydrogenase-family-protein-molybdopterin-binding-subunit
MKKDAIGDSLSRVDGRLKVTGGAKYSGEYKVPNLTYGVLVSATIASGTVTALDTRAAERAPGVLAVITPFNAPKVPGYQAGAERPVRGLKLFNDNKIYFNAQPIALVVADTFERATYAASLVKATYNTEPFETDFHKNIDKGVTPQKGNYKDYVRGEANAYKNAPVVVEEEYQLPTEVHNPMELHVTTAFWDGDDKVTLYTKSQGVKGSQRSIAAAFGLNPDNVQINSRFVGGAFGSSLRTWPHEIAAAQAAKLVKRPVKLTLTREQMFTQVGYRPLTIQKIGLGATADGKLIGITHESHSQTAVYEEFTEGAVNVSQFLYNSPNVNTLYKVVPLNVGVPAPMRGPGEATGSFALESALDELSYKLNLDPIELRLRNYTDTDPERNKPWSSKYLKECYQKGAEAIGWADRKAQPGANKEGEWLVGYGIGCGAFGAYRGNAVAKIKLTADGSVNIQSATSDIGPGTGTSMVLIAADTLGIPADKITFELGNSAFPNAPTQGGSATVSSVGSAVYDVCVALKQKLYTMAGKPADSMEPIDYVAVLKQNNMPSVELTQESKGNPEAQKYSMYSFSAHFAKVHVHPLTGQVKIKKIVACVDAGKIVNHKTASSQMIGGAVGGVGMAMTEEAVFDDRYGRYINGNFADYHVPVNADIQQIEAIFIDKPDPVLNPVGTKGIGEISLIGVAPALANAIYNATGKRVRELPITPDKLI
>NZ_CP043451.1|WP_112654140.1|1023000_1023993_+|xanthine-dehydrogenase-family-protein-subunit-M
MNQFQYTRPAETAVAIKSLAKEPNGYFLAGGTNLVDMMKMGLVVPDKLIDINRLPLKKIERTPTGIHIGALASNSEVAEHAYIKAQYPLLALAINAGASPQLRNMATVGGNLMQRTRCPYFFDTAMPCNKRTPGSGCGALQGINRMHALFGASDKCIAVNPSDMNVALAALDATIHVTGVKGPRAINIGDFHRLPGNHPELDNTLQKGELITSVDLPAASSAYNKHVYYLKIRDRTSYAFALVSVAAALHIENNTITGARLAMGGVAHKPWRLTAAEIFLKGKAITEDNFKQAAQIAMQGAKAYEYNKFKLKLAPNAIVQSLKLATGLAS
>NZ_CP043451.1|WP_112654141.1|1022368_1023004_+|(2Fe-2S)-binding-protein
MSTTKPCTPTDGEDNSNGTRRDFLKQTSLLTAIALTPGTVVKAAENQWDEKLAGVFEKQALHLEVNGVKHELMVEPRVTLLEVLREHLDLTGTKKGCDRGQCGACTVHVNGVRVNSCLSLALTNDGKKIDTIEGLAKEEELHPMQEAFIKHDGFQCGYCTSGQIMSAVALLKEGHAGSETEIREFMSGNICRCGAYPNIVKAIQEVKGGMV
>NZ_CP043451.1|WP_112654142.1|1021836_1022208_-|hypothetical-protein
MKMIPLFKCRDLRQAVGFYTNVLDFRLKYPEATADDGVIDLVSEFGELQLTIYESDRLFGSVVNVWIDDVDSEFKRYISRGLDTSVKKESPVHQGPTDQTWGAREFYVTDTDGNTLRFCQRQR
>NZ_CP043451.1|WP_112654143.1|1020071_1021832_+|family-78-glycoside-hydrolase-catalytic-domain
MKKIIGILILTIIYFICKAQKLPPVFDAKRSAEAQSTETVRKYLSPIRILWKSPDAATNIINAEKLLKQGDGQADLSGNELCILQSNEKGKPGLLLDFGKELHGGLQLVTDQSRGGKPVRVRIRFGESASEAMSDIDTIKGATNDHAMRDMIISLPWLGKLEIGNTGFRFVRIDLVDDNSQLKLKEARAIFVYRDIPYLGSFKCSDTLLNKIWLTGAYTVHLNMQDYLWDGIKRDRLVWVGDMHPETSTIAAVFGDNPVVSKSLDLARDITPLPGYMNGMVSYSMWWILIQRDWYMHTGNLKYLQQQKAYLVKLLNQYAVQVDANGSEKLDGAGRFLDWPSSENKPAIHAGLQAMLLMTLNAGAELCKILNDQATAKKCEAAIAKLKNNVPDASGSKQAAALLCLSGLLPAEKANDILSKDGVHNYSTFFGYYMLLTKAKAGDYQGGIDAIRNFWGPMLNLGATTFWEDFNIDWLPNASRIDELVPDGKKDIHGDYGAYCYKGFRHSLSHGWASGPTPWLTEYVLGVKIMAPGCKVIKIEPHLGDLSFAEGTYPTPYGIVKIKHVKQADGKVKTIINAPAGVKVVQ
>NZ_CP043451.1|WP_112654144.1|1019079_1019553_+|DNA-starvation/stationary-phase-protection-protein
MKTNIGINEADRQAVSDQLAKLLADEFVLYTKTRNAHWNIEGPDFHSMHVFFEQQYNELDEIMDSVAERIRKIGHYAPATLTQLLQLTHLTEKLDHKNDSAGFLKELLEDHESIIEFIRGNINPFANQFNDAGTSDFITGLMETHEGMAWMLRSHFR
>NZ_CP043451.1|WP_112654133.1|1032640_1033210_+|transposase
MSTKYKFRKQEQLYFISFSVINWIDLFIRTEYKQIMLESWKYCQQNKGLEIYAWCIMTSHIHMIIGSEEEKLENIMRDMKKHTSLALKAAIKQHPSESRREWMLWMMERAGKKNSQNIDFQLWQQDNHPIELYDNRILNQKLDYIHNNPVIAGFVEKPEDYLNYLYSSARDYSGMPGLVDVILVSPVVL
>NZ_CP043451.1|WP_167516081.1|1033243_1033417_-|hypothetical-protein
MTLICVNTVFAQKTSLHSVKIEWESFSTESFRDVSCDDFEYSFLDTPPTGASMQRWQ
>NZ_CP043451.1|WP_112654132.1|1033487_1033964_-|hypothetical-protein
MLIHKEVKDRELYVYMNGKLIYKRWLDTGASKVFDVMAYDKYTLASIREIKQEEHQLISVKALIKLKATKDGGRRTGILSGYRPNHVFEYDKDGNRFETYIGDIRWDDGFTIEPGEEKAVTVRFFLGWKIERYLNIGRKWWIHEGPRCVGEAELIEFM
>NZ_CP043451.1|WP_112654131.1|1034395_1035385_+|ParA-family-protein
MQSIVVFNNKGGVGKTTLMCNIAAYLKIKKRKKVLIVDADPQCNATAYMFPYPQIEDIYSKSESTIFEIVKPLQRGKGYISNKLPILKSPYFEVDVIPGDTQLSLSEDFLSKDWLDGKAGDFRGLQTTLLFKDLLLRLDKYDYVFFDVGPSLGALNRSVLAASDFFIVPMSSDIFSLQALENISKSLKDWEKQLSRGLSDFKTREQEPFQIDGQTISWHLQFGGYVTQQYTAKTVNGKKQPVNAYERIIKKIPSTIQKHLLTLNKISITYPQIGEITNLHSLVPLSQNSSVPIFNLKSEHGVVGAHFNKVREYEATLSEMVEKLITNLN
>NZ_CP043451.1|WP_112654130.1|1035390_1036254_+|SIR2-family-protein
MINWPEELIDDIARRRCVIVLGAGVSKNSTNAAGARPKDWKEFLISASEDINGKTEIRKQIGSGDFLTACELIKKELGRDDFNSLMRREFLTPQFQPADIHKFIYNLDSRFVITPNFDKIYDTYANTTSHGSIIVKKFTENDIADCIRRPEHLIIKIHGSVESPDNLIFTRKDYSESRTKYRDFYHLIDALSITHTFVFVGCGTNDPDIRLILEDYSFKFPQNKKHYIIMPKGAMNSKVREIISETMSLKALLYDSSDYHRILTSSIADLVSKVEIRRSDLCLTMDW
>NZ_CP043451.1|WP_112654129.1|1036415_1037318_-|ribose-phosphate-pyrophosphokinase
MKKLLFAITDYEYLAEKVLALGHCERGEIEVSHFTDGERYQRILSNVEGRDVLLIGGTVNDSATLELYDLASSLVSYGADSLTLVIPYFGYSTMERAVKAGEIVTAKTRARLLSAIPKSNRGNKVMLFDLHSEGIQYYFEQDLYPVHVYCKDIVIEAATRYGGDNFVMASTDAGRAKWVESLANDMGVNAAFILKRRLKGDHTEVSAINADVAGKTVIIYDDMIRSGGSIVNAAMTYKNAGAGDIYVITTHGLFVNDGIGKLKACGAIKKLICTDTHVNCKDLEGDDFVEVRTVAGLICG
>NZ_CP043451.1|WP_112654128.1|1037384_1038803_-|nicotinate-phosphoribosyltransferase
MKKENLILLADAYKYAHHKFYYPGTTHIYSYLESRGGMFNETVFFGLQYFLKEYLQGPAFNQVDLDEADEFLKQVFGRDDVFDCSKFQYILDKYNGHLPVRIKAVAEGSSVPIGNVLMTIENTDPECYWLTNFLETLLMQVWYPCTVATLSHEVKKTVTQYYEETATPEAFGGIGFVLNDFGFRGVSSVESAKIGGAAHLLSFAGSDNLAGSGMAITYYHAEKVYGLSIPATEHSICTLLGQEGELEVFKHVLRSFPTGVIACVSDSYNIFRACSEYWGEDLKQEILKRDGTLVIRPDSGDPVMTLLEIFNILFDKFGFVTNARGYKVLPPQVRVIQGDGVNYTEIGVIYKALKENGISAENLVLGMGGALLQKVDRDTQKFALKCSSAVIDGKEVAVEKSPAEMDASGNISTSFKKSKGGRLKLVKTAEGYKTIQHDEQPELADQLQTVFENGHIIKDFTFEQLIDTLQHQ
>NZ_CP043451.1|WP_112654127.1|1038807_1039704_-|NUDIX-domain-containing-protein
MKTGVIIARFQTPYLHEGHRELIAQVKQNHAKLIILLGVSPIKGSRKNPYDYYTREKMIKKDYPEIVVLPISDNPSDKVWSDNLDNLLKSVFNAEQFCLYGSRDSFIPYYSGKFETIELPEHGDYNATELRKQYADKVFDSNDFRAGILYAYYNQYPKVYPTVDVALFRNNRSEILLGKKAINNKWRFVGGFTDPEDTCYEDAAKRELAEECGEMQTTAMEYETSAKINDWRYRSEADKIITLLFSSDFIEGEPKAQDDIADLAWFKLTDLPLMIKDGSISEEHVELFNFITGKYLKN
>NZ_CP043451.1|WP_112654126.1|1040148_1040835_-|NUDIX-hydrolase
MSVAQNIKVAVDAVVFGYTSKEGLSVLLIKRNIEPFKNSWALPGGLVADHESLEEAIQRELREETGVNITYLEQLYSFGQPGRDPRNRVISITYYGLVRPDAFVVKAATDASDVNWFNIKKLPALAFDHTTIISVARERLKSKMLYQPVGFELLEEKFPFSELEKLYLAVLDRPIDRRNFKKKITKYGFLEETTEKQALEGAGRPGNLFRFNEEKYFQLKKEGISFEI
>NZ_CP043451.1|WP_146750447.1|1041004_1041634_+|RNA-polymerase-sigma-70-factor
MPYQSVNRFTAAMHHDKEYQMWPDARLLEQLRLDDRKAFEILYHKYSSKLFYAAYNLFRDKDVCEDLVQELFIDLWTKRNQLNITSLEAYLKVAIRHRVLFYLRTKKASVDLAVIETLVEKYSADSKLFQDDIAHLLEDGVAQLPEKCRQIFTLSRKEYLSNKEIATRLNISIKTVENQITIALRYLRTGLTDYLPSVVALVLLHMFGK

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Crispr_ID: NZ_CP043451_5

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP043451_5

2976156-2976257

Orphan

Consensus_repeat	Method
CTTCTTTTTTAGCTTTTGGTGCAG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP043451_5

>merge|NZ_CP043451|5|2976156-2976257|CRISPRCasFinder
CTTCTTTTTTAGCTTTTGGTGCAGTAGCTTTCTTTGCTTTTGGAGCTTCTTCAGCAGCAGGAGCTTCAACAGCTTTAGCTTCTTTTTTAGCTTTTGGTGCAG

>NZ_CP043451|5|5|2976156-2976257|CRISPRCasFinder
CTTCTTTTTTAGCTTTTGGTGCAG	TAGCTTTCTTTGCTTTTGGAGCTTCTTCAGCAGCAGGAGCTTCAACAGCTTTAG
CTTCTTTTTTAGCTTTTGGTGCAG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP043451.1\|WP_112655044.1\|2969872_2972011_+\|ribonuclease-R	unknown	unknown	gnl\|CDD\|273947
NZ_CP043451.1\|WP_112655055.1\|2981735_2984093_-\|GAF-domain-containing-protein	unknown	unknown	unknown
NZ_CP043451.1\|WP_112655047.1\|2973450_2973864_+\|energy-transducer-TonB	unknown	unknown	gnl\|CDD\|367555
NZ_CP043451.1\|WP_112655046.1\|2973088_2973448_+\|energy-transducer-TonB	unknown	unknown	gnl\|CDD\|367555
NZ_CP043451.1\|WP_112655045.1\|2972100_2973075_+\|polyprenyl-synthetase-family-protein	unknown	unknown	gnl\|CDD\|376322
NZ_CP043451.1\|WP_091168300.1\|2976973_2977396_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043451.1\|WP_112655052.1\|2979461_2979989_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043451.1\|WP_112655049.1\|2975634_2976051_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043451.1\|WP_090525007.1\|2980030_2980528_+\|RNA-polymerase-sigma-factor	unknown	unknown	gnl\|CDD\|224511
NZ_CP043451.1\|WP_112655041.1\|2964895_2967286_+\|penicillin-binding-protein-1C	unknown	unknown	gnl\|CDD\|273954
NZ_CP043451.1\|WP_112655054.1\|2981130_2981682_+\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|366181
NZ_CP043451.1\|WP_112655040.1\|2964087_2964813_-\|glycosyltransferase-family-2-protein	unknown	unknown	gnl\|CDD\|133022
NZ_CP043451.1\|WP_090467954.1\|2976589_2976898_-\|50S-ribosomal-protein-L21	unknown	unknown	gnl\|CDD\|235510
NZ_CP043451.1\|WP_112655042.1\|2967386_2968097_+\|3'-5'-exonuclease	unknown	unknown	gnl\|CDD\|99825
NZ_CP043451.1\|WP_112655048.1\|2974037_2975630_+\|M1-family-metallopeptidase	unknown	unknown	gnl\|CDD\|341066
NZ_CP043451.1\|WP_112655056.1\|2984117_2987723_-\|BamA/TamA-family-outer-membrane-protein	unknown	unknown	gnl\|CDD\|277324
NZ_CP043451.1\|WP_112655053.1\|2980514_2981105_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043451.1\|WP_112655379.1\|2987775_2988636_-\|SdiA-regulated-family-protein	unknown	unknown	gnl\|CDD\|197380
NZ_CP043451.1\|WP_112655043.1\|2968096_2969794_+\|ABC-transporter-ATP-binding-protein	unknown	unknown	gnl\|CDD\|224048
NZ_CP043451.1\|WP_112655051.1\|2977903_2979295_-\|dicarboxylate/amino-acid:cation-symporter	unknown	unknown	gnl\|CDD\|224220

Protein	Function_ID	Function_description	E-value
NZ_CP043451.1\|WP_112655044.1\|2969872_2972011_+\|ribonuclease-R	gnl\|CDD\|273947	TIGR02063, Ribonuclease_R, ribonuclease R. This family consists of an exoribonuclease, ribonuclease R, also called VacB. It is one of the eight exoribonucleases reported in E. coli and is broadly distributed throughout the bacteria. In E. coli, double mutants of this protein and polynucleotide phosphorylase are not viable. Scoring between trusted and noise cutoffs to the model are shorter, divergent forms from the Chlamydiae, and divergent forms from the Campylobacterales (including Helicobacter pylori) and Leptospira interrogans. [Transcription, Degradation of RNA].	0
NZ_CP043451.1\|WP_112655047.1\|2973450_2973864_+\|energy-transducer-TonB	gnl\|CDD\|367555	pfam03544, TonB_C, Gram-negative bacterial TonB protein C-terminal. The TonB_C domain is the well-characterized C-terminal region of the TonB receptor molecule. This protein is bound to an inner membrane-bound protein ExbB via a globular domain and has a flexible middle region that is likely to help in positioning the C-terminal domain into the iron-transporter barrel in the outer membrane. TonB_C interacts with the N-terminal TonB box of the outer membrane transporter that binds the Fe3+-siderophore complex. The barrel of the transporter, consisting of 22 beta-sheets and an inside plug, binds the iron complex in the barrel entrance.	4.19132e-15
NZ_CP043451.1\|WP_112655046.1\|2973088_2973448_+\|energy-transducer-TonB	gnl\|CDD\|367555	pfam03544, TonB_C, Gram-negative bacterial TonB protein C-terminal. The TonB_C domain is the well-characterized C-terminal region of the TonB receptor molecule. This protein is bound to an inner membrane-bound protein ExbB via a globular domain and has a flexible middle region that is likely to help in positioning the C-terminal domain into the iron-transporter barrel in the outer membrane. TonB_C interacts with the N-terminal TonB box of the outer membrane transporter that binds the Fe3+-siderophore complex. The barrel of the transporter, consisting of 22 beta-sheets and an inside plug, binds the iron complex in the barrel entrance.	5.73898e-11
NZ_CP043451.1\|WP_112655045.1\|2972100_2973075_+\|polyprenyl-synthetase-family-protein	gnl\|CDD\|376322	pfam00348, polyprenyl_synt, Polyprenyl synthetase.	1.29371e-85
NZ_CP043451.1\|WP_090525007.1\|2980030_2980528_+\|RNA-polymerase-sigma-factor	gnl\|CDD\|224511	COG1595, RpoE, DNA-directed RNA polymerase specialized sigma subunit, sigma24 homolog [Transcription].	2.41382e-33
NZ_CP043451.1\|WP_112655041.1\|2964895_2967286_+\|penicillin-binding-protein-1C	gnl\|CDD\|273954	TIGR02073, Includes:_Penicillin-insensitive_transglycosylase, penicillin-binding protein 1C. This subfamily of the penicillin binding proteins includes the member from E. coli designated penicillin-binding protein 1C. Members have both transglycosylase and transpeptidase domains and are involved in forming cross-links in the late stages of peptidoglycan biosynthesis. All members of this subfamily are presumed to have the same basic function. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan].	0
NZ_CP043451.1\|WP_112655054.1\|2981130_2981682_+\|GNAT-family-N-acetyltransferase	gnl\|CDD\|366181	pfam00583, Acetyltransf_1, Acetyltransferase (GNAT) family. This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.	1.33709e-16
NZ_CP043451.1\|WP_112655040.1\|2964087_2964813_-\|glycosyltransferase-family-2-protein	gnl\|CDD\|133022	cd04179, DPM_DPG-synthase_like, DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily. DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. The UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate. This protein family belongs to Glycosyltransferase 2 superfamily.	1.70879e-54
NZ_CP043451.1\|WP_090467954.1\|2976589_2976898_-\|50S-ribosomal-protein-L21	gnl\|CDD\|235510	PRK05573, rplU, 50S ribosomal protein L21; Validated.	4.08392e-43
NZ_CP043451.1\|WP_112655042.1\|2967386_2968097_+\|3'-5'-exonuclease	gnl\|CDD\|99825	cd05782, DNA_polB_like1_exo, Uncharacterized bacterial subgroup of the DEDDy 3'-5' exonuclease domain of family-B DNA polymerases. A subfamily of the 3'-5' exonuclease domain of family-B DNA polymerases. This subfamily is composed of uncharacterized bacterial family-B DNA polymerases. Family-B DNA polymerases contain an N-terminal DEDDy DnaQ-like exonuclease domain in the same polypeptide chain as the polymerase domain, similar to family-A DNA polymerases. This exonuclease domain contains three sequence motifs termed ExoI, ExoII and ExoIII, with a specific YX(3)D pattern at ExoIII. These motifs are involved in metal binding and catalysis. The exonuclease domain of family-B DNA polymerases has a fundamental role in proofreading activity. It contains a beta hairpin structure that plays an important role in active site switching in the event of a nucleotide misincorporation. Family-B DNA polymerases are predominantly involved in DNA replication and DNA repair.	1.63447e-63
NZ_CP043451.1\|WP_112655048.1\|2974037_2975630_+\|M1-family-metallopeptidase	gnl\|CDD\|341066	cd09603, M1_APN_like, Peptidase M1 family similar to aminopeptidase N catalytic domain. This family contains mostly bacterial and some archaeal M1 peptidases with smilarity to the catalytic domain of aminopeptidase N (APN; CD13; alanyl aminopeptidase; EC 3.4.11.2), a type II integral membrane protease belonging to the M1 gluzincin family. APN preferentially cleaves neutral amino acids from the N-terminus of oligopeptides and, in higher eukaryotes, is present in a variety of human tissues and cell types (leukocyte, fibroblast, endothelial and epithelial cells). APN expression is dysregulated in inflammatory diseases such as chronic pain, rheumatoid arthritis, multiple sclerosis, systemic sclerosis, systemic lupus erythematosus, polymyositis/dermatomyosytis and pulmonary sarcoidosis, and is enhanced in tumor cells such as melanoma, renal, prostate, pancreas, colon, gastric and thyroid cancers. It is predominantly expressed on stem cells and on cells of the granulocytic and monocytic lineages at distinct stages of differentiation, thus considered a marker of differentiation. Thus, APN inhibition may lead to the development of anti-cancer and anti-inflammatory drugs. APNs are also present in many pathogenic bacteria and represent potential drug targets. Some APNs have been used commercially, such as one from Lactococcus lactis used in the food industry. APN also serves as a receptor for coronaviruses, although the virus receptor interaction site seems to be distinct from the enzymatic site and aminopeptidase activity is not necessary for viral infection. APNs have also been extensively studied as putative Cry toxin receptors. Cry1 proteins are pore-forming toxins that bind to the midgut epithelial cell membrane of susceptible insect larvae, causing extensive damage. Several different toxins, including Cry1Aa, Cry1Ab, Cry1Ac, Cry1Ba, Cry1Ca and Cry1Fa, have been shown to bind to APNs; however, a direct role of APN in cytotoxicity has been yet to be firmly established.	1.4602e-135
NZ_CP043451.1\|WP_112655056.1\|2984117_2987723_-\|BamA/TamA-family-outer-membrane-protein	gnl\|CDD\|277324	cd07378, MPP_ACP5, Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain. Acid phosphatase 5 (ACP5) removes the mannose 6-phosphate recognition marker from lysosomal proteins. The exact site of dephosphorylation is not clear. Evidence suggests dephosphorylation may take place in a prelysosomal compartment as well as in the lysosome. ACP5 belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.	1.83947e-11
NZ_CP043451.1\|WP_112655379.1\|2987775_2988636_-\|SdiA-regulated-family-protein	gnl\|CDD\|197380	cd09971, SdiA-regulated, SdiA-regulated. This model represents a bacterial family of proteins that may be regulated by SdiA, a member of the LuxR family of transcriptional regulators. The C-terminal domain included in the alignment forms a five-bladed beta-propeller structure. The X-ray structure of Escherichia coli yjiK (C-terminal domain) exhibits binding of calcium ions (Ca++) in what appears to be an evolutionarily conserved site. Sequence analysis suggests a distant relationship to proteins that are characterized as containing NHL-repeats. The latter also form beta-propeller structures, with several examples known to form six-bladed beta-propellers. Several of the six-bladed beta-propellers containing NHL repeats have been characterized functionally, including members with enzymatic functions that are dependent on metal ions. No functional characterization is available for this family of five-bladed propellers, though.	3.39031e-07
NZ_CP043451.1\|WP_112655043.1\|2968096_2969794_+\|ABC-transporter-ATP-binding-protein	gnl\|CDD\|224048	COG1123, COG1123, ATPase components of various ABC-type transport systems, contain duplicated ATPase [General function prediction only].	0
NZ_CP043451.1\|WP_112655051.1\|2977903_2979295_-\|dicarboxylate/amino-acid:cation-symporter	gnl\|CDD\|224220	COG1301, GltP, Na+/H+-dicarboxylate symporters [Energy production and conversion].	1.95337e-116

>NZ_CP043451.1|WP_112655049.1|2975634_2976051_+|hypothetical-protein
MRYLLVFGLIILPVALFAQGKAKREHVKPDTTVYKTVDVQPEFPGGTEKWTNYLFKVPIPKDYDKENTQASFLIQMIIETDGSVTHASVRRKINEAMCKAFIAHVNKSPKWKPGRINGKPVRVLYSSPISCFMLQSDE
>NZ_CP043451.1|WP_112655048.1|2974037_2975630_+|M1-family-metallopeptidase
MKKFSFILIILLASASLYAQTLTSGGKLKPEQAIMDVRHYTISLAVDPVQKTINGFTTIDVIMEKPTRVLLFDLLDSLTISKVLVNGKQEAFEYKNNLITINTAKELPAGKASVKVIYGGKPHVARRPPWDDGFIWTRDSTGHQWMAITAEGTGGKLYFPCKDHPSDEPNDGVDMFITVPKDLVVAGPGLLKSVSKQKGTATFHWQTKYTINNYSILFNAGDYTVVTRPYTTVDGHNVPLQFYVLKEHASKAEHHLDIFVKTIKEQEKYFGEYPWVKEKIGIVETPHLGMEHQTMNAYGAKFKYTKVWGEDYDGLMHHEFGHEWWGNKVTAKDWADYWIHEGICTYGDALYVREFEGEKAYIKFFQNSALSFGNKIPIVIGKDIDEESAYNGDIYGKGAFFMHTLRYIMGDSIFFPTLRGFVTDPRYTYSNLASTDDVIQYFSKAAGQDLKPLFDLYIYSINKLEIHIKAQRGDKYQVQLLNIDMPLPVDITTDGVTKRYTLDKKGITVTSKTIPVIDPDTYYLKKLIIE
>NZ_CP043451.1|WP_112655047.1|2973450_2973864_+|energy-transducer-TonB
MKKIFVIISLSFWPILVKAQTETSKIDTEEYKCNCGIKVDKQPEFPGGTNNFFIFVRKNLRWPVKSQEIEGRVIVEVTITKNGKLTDPIVKRGLSREQDKEALRLINKSPKWEPAMLNGKAIDFKYYIIISFKRDIE
>NZ_CP043451.1|WP_112655046.1|2973088_2973448_+|energy-transducer-TonB
MKKILPILIILMVSLSAKAQKLAPPHFRGGDKAFHEFLDQNLKWPKDSAVKQGIVKVSFYVESNGLLSDIKLVQGFAHEFDKEALRVINLSPRWVPATRDGKFIKSKYSVPILYESIEL
>NZ_CP043451.1|WP_112655045.1|2972100_2973075_+|polyprenyl-synthetase-family-protein
MKQLTELQLLINDAVGKLSYPAYPADLYEPISYILSIGGKRMRPALLLLACDLFGGDVDKAIEPALAIEVFHNFTLMHDDIMDKAPLRRGKATVHEKWNANVAILSGDAMMVEANRLMMKVDDSILRNVLDVFNDTATGVCEGQQIDMSFEQRNNVSIEEYINMIRLKTAVLLGGTLKIGSIIGGAALTDADLIDSFGVNLGIAFQLQDDILDVYGDPEKFGKQVGGDIISNKKTFLLIRALELAKDGQAQTLNQWLCAAEFDTAEKVKAITNIYNELDIRQHAEKAMQTYADKAFVALDAINLPEDHKQYLRDFADGLLVREN
>NZ_CP043451.1|WP_112655044.1|2969872_2972011_+|ribonuclease-R
MSKRKKNNSSIHQVLTQMVLDIFEQNGNTPLNYKQVSAKLNVRDPESREIIYDILKDEVKKSVLKEIAPGKFQLLELKTFIEGVVDLTNDGSAFIVTDDEFESDIFIAPRKLRTALNGDRVKVYVYAKSKGKHKEGEVIEILQRAKMEFTGIVKLSERYAFFIPDDRKMMHDIFIPISELNGAKNGIKAVAEITDWPTEAKNPIGRIKHILGAQGENDTEMNAILAEYGFPLSFPAEVEHDAEEIPDVITPEEIAKRRDFRNITTFTIDPFDAKDFDDALSYRVLHNGNYEVGVHIADVSHYITPDSALDKEALDRATSVYLVDRVIPMLPERLSNGLCSLRPKEEKLCFSAVFEMDENANIITEWYGKTIIYSDRRFTYEEVQEVIETGKGDFKEEIFKLNALAYKLRDRKFKNGAISFETTEVKFKLDENGKPTGVYVKERKDAHKLIEDFMLLANRKVAERVSKMGKGKHKYTFVYRVHDSPKPDALANFAQFAARFGYKINTKSDKETAKSLNYLMEDVEGKKEQNVLTHLAIRSMAKAIYTTKSSSHYGLAFDHYTHFTSPIRRYPDVMVHRLLFHYLSGGQSANAEFYEKLCSHSSLMEKKAADAERSSVKYKQAEYLRDQVGNTFMGIISGVTEWGMYVEIIENKCEGMIRLRDISDDFYTLDEKNYAIIGQRKKKIYQLGDEVKIKVKQVDLTKKQIDFILVQE
>NZ_CP043451.1|WP_112655043.1|2968096_2969794_+|ABC-transporter-ATP-binding-protein
MLKVSDLSVSFKNGKNQFTAVKGISFTLNKGETIGIVGESGSGKSVTSLALMRLLNEDQAVIGGSVLLNGVCLCKLSEDEMRHVRGNQVAMIFQEPMTSLNPVLTCGFQLTEAIRLHLGSSKAEAKQKTIELFKEVQLPRPEAIFNSYPHQISGGQKQRVMIAMALACNPEILIADEPTTALDVTVQKTIIELLHKLKAERHMSLIFISHDLGVIKEIADRVLVMYKGEIIEEAAVKDLFANPRHPYTKGLLACRPSPQQHLKKLPVVADFLDEARPAVTIESIRELYHYPDTEIAERKRKLYEQQPLLKADKLNTWFPTDTGFFKRKDHVVKAVNNVSFDVYPGETLGLVGESGCGKTTLGRSILRLIEPTSGRVIFGGTELQGLKKNELRQIRKDIQIIFQDPYSSLNPKLTVGQSLMEPLQVHQFYSNDTTRKRKVLELLERVNLQPAHFNRYPHEFSGGQRQRIVIARALALQPKFIICDESVSALDVSVQAQVLNLIRELQDELKLTYIFISHDLAVIKHISDRMMVMNKGEIVETGYPDDIYYRPKEEYTKRLIASIPG
>NZ_CP043451.1|WP_112655042.1|2967386_2968097_+|3'-5'-exonuclease
MLEQYDLHNLLVIDIETVPQYSTHEQLPENLQVLWELKTRHQRKDEPADIHYERAGIWAEFGKIVCISVGIFIAGKNIGLRVKSFASHDEKELLTKFCNLLVSQPPTLILCAHNGKEFDFPYLCRRLLVNGIPIPPQLQIAGKKPWEIVHLDTMELWKFGDHKHYTSLNLLTTIFNIPTSKDDIDGSDVGRVYWHENQLERICAYCQKDVIATAQLLRRYRGEELIADEFITIVGS
>NZ_CP043451.1|WP_112655041.1|2964895_2967286_+|penicillin-binding-protein-1C
MQFVLKRAKSYLKKPKVTVSLFFLFVLTLIFWFCLPNPLFNSPTSYVIDDDQGQLLGASIANDGQWRFPYNPTVPEKFKQCIITFEDKRFEHHPGFDIVAFSRAIKQNLSSKKVSSGGSTLTMQVIRLATRHKRNIWNKLKEIFMAMRLEVTHSKSEILALYTSNAPFGTNVIGLDAASWRYFGRSPDKLSWGEMAAMAVLPNSPSLVHPGRNRAILLRKRNSLLDKLHKAGIIDSTTAALARLEPVPDRPMALPQLAPHLLQRFKADHQAKPEGDTRITSSIKSSLQQQVNNILEQHHSLLKANDINNIAAIVLDVETGATLAYAGNISHREDPQMESDVDVIDAPRSPGSTLKPLLYAAMLHDGLILPNSLMPDVPTMIAGYHPENFDLGYDGAVPASRALSRSLNVPAVKMLQQYKYERFYDFLHKAGITTLTKPADHYGLSLILGGGENTLWELSGAYADMARVLNHYNKNNGKYDPADFHNPVYEKKAAAKPELEKSGLLDAASIYYTFQAMEEVMRPGEEMLWQQFSSSQRVAWKTGTSFGFRDGWAIGVTPKYVVGVWVGNTDGEGRPGLTGINTAAPALFEIFRLLPVSRDWFEMPMGEMVKINVCKQSGYRAGQYCQDADEQYVPKSGLKALVCPYHQLVHLSADAKWQVNGNCEPPDNILNKSWFVLPPSMEYYYKARNYQYHVLPPFRPDCTQAENGNTMEVIYPKNGAKIYVPLEADGTRGRMICNAAHRQPGMKIFWHLDDQYVGETKDFHQVALNPPPGKHILTLVDGNGNTISIEFEVLKK
>NZ_CP043451.1|WP_112655040.1|2964087_2964813_-|glycosyltransferase-family-2-protein
MTIQKLSIIIPAYNEGKTIHLILDKIKEVNLINDIEKEVIIVNDCSKDDTEAAIYKYKLANPEVNIQYFKHESNKGKGAALHTGIAKATGDYLIIQDADLEYDPAEYNDLLKPVVAGFADVVYGSRFMGSNPHRILFFWHTIGNRWLTFASNMFSNLNLTDMETCYKLFNTKVIQSIKLTEKRFGFEPEVTQKISRVHRIRIYEVGISYYGRTYEEGKKIGWKDGVRAIYCILKYGLFKSK
>NZ_CP043451.1|WP_090467954.1|2976589_2976898_-|50S-ribosomal-protein-L21
MYAIVSIAGQQFKVAKDQQIFVHRLQGDEGASIEFDSVLLAENEGKFKLGSDLKGAKVSAKIVSHLKGDKVIIFKKKRRKGYKKKNGHRQQFTKIEITGITL
>NZ_CP043451.1|WP_091168300.1|2976973_2977396_-|hypothetical-protein
MIKNAPYRFVDFESISFQYGHKDSLVNKYDSRTGMFQYLDRRDSLVKEHLRLTKDDLLYLHRKAADLGFWDFPSKETGDTSKVADGKAVRYIIEFKYKEKTKRVIFDTDYFGNPKLIDANQRLIAEIQKKLTDVENRGKK
>NZ_CP043451.1|WP_112655051.1|2977903_2979295_-|dicarboxylate/amino-acid:cation-symporter
MKKSRLTLFIFIALVLGVIAGYIYNTYVFADLNKQLSSAGAAIKSIDKKIEALPDTTVAAYKDFKLQRIALVKLQSQATDAREDKLELYNILSKIFLNLIKMIVAPLVFTTLVVGVAKVGDIKAVGRIGGKTMLWFISATLVSLLLGMLLVNLFEPGKTMHLPLPDSHLSTGIKKSALSLTEFVGHVFPKSFIEAMANNEILQIVVFSLFFGVATAAIGEQGKIVIKAMDAFAHVIMKITGYVMKMAPLAVFGAITAVVAKQGIGVLSTYGIFISEFYFSLIVLWSVIILAGYIVLRKPVFRLINRIKDAMLIAFSTSTSEAAYPKVLEELERFGCSNKIVSFVLPLGYSFNLDGSMMYMTFASLFLAQSYDIHLSFGHQLSMLLVLMLTSKGVAGVPRASLVVIAGTLAMFNIPEAGLFLLIGIDPLLDMGRSATNVLGNAMATAVVSKWEGEEVGTQIIRE
>NZ_CP043451.1|WP_112655052.1|2979461_2979989_+|hypothetical-protein
MTTTAYGLQHIKKEIQHLPNEHLAELMLRLARYKKENKELLAYLLFEAHDEAAFIEKVKAEAGFMFSQLSSLSYNAAKGMRKILRLLSKYTKFMASKGAEIELLINFCENYLEYADRRTSYKPLRLILIRQVEKIRGLINKLHEDLQFDYQDSYNKLISDAESKLGWFKKNDHLL
>NZ_CP043451.1|WP_090525007.1|2980030_2980528_+|RNA-polymerase-sigma-factor
MANKEAAFKQIYEANSKKIFHLCYGYTGDDDAANDLLQETFLKVWQNLEKFRNQAMISTWIYRIAVNTCLTYLRSEKRQAKDELTPQLAETKREELSDKNEQVALLYKCISKLEESERIIITMVLDEVPYPEIAEISGISEGNLRVKIYRIKQKLTELYNQYERL
>NZ_CP043451.1|WP_112655053.1|2980514_2981105_+|hypothetical-protein
MKDFDHLMSVWQGQPKPDQLSVDEVLKQVKKGIRSITQKLYWSIVAMVVTVAFAFVVTFFLAFKSAVTTIGILIVLVTMLMYLSLMVRHYHILSKRDATLNPAEYLDSLKAYQKNRSKVIGWFYYTYILLLSAGLAMYFIEVLEHSSLTFKIVTYTSIGVWFLFTTFYLKPRMFKNEEEKLNLMIDRLVRLKEQFD
>NZ_CP043451.1|WP_112655054.1|2981130_2981682_+|GNAT-family-N-acetyltransferase
MAISETVTIQKLTLADADVLLELSKKTFFDFFAHLNKPEDMEAYASVAFTPQKIQAELSDPNSHFFFAMLDGEITGYLKLNYCHAQTEFQDPAAVEIERIYVLAEYHGKKIGHQFIDFTLKAATDKHLQYVWLGVWEHNLKAIAFYEKHGFEVFSSHEFTLGSDKQTDLLMKKAILSSSKPKA
>NZ_CP043451.1|WP_112655055.1|2981735_2984093_-|GAF-domain-containing-protein
MHTEVLNISKNECTICQVETCLTFNPFVAHLKERIATEKTLKSEFYRYVLERFEHDICIDLDMRPTDAEKYREMLELIYSILTPPIANEKEFHWALSTPVPDKIFFSTEAFYDFHSSHHSNLYALNVSKNEMFSDRQKRFIYNLILERMYGFSSAIKNELLFSYEDPETGLSRYFNIQTDARFVEIELNGELPELSFDTIEPYLHSHTSLELIEKVIPLNIFKFKGFSIITLTDVTLTHALENIRTELVNHSANEEEQYAHIISSLKSLAESPGIEFGLMPFLTINNEPIFDNDECSRSILLKAAKDFNLAEETFDAIIDDYNQNPRPIFFNSITDEKIGKFPFLQVLKQAGIKSYGIFPVYYNKKNVGIMEVFSYKEIVFYEKLLSKLQATIPLIAQLLQNSIDQFEARISSVIKNKFTSLQPSVQWKFNEVAWNYLKEKRKKKKSPEIETVSFSHVYPLFGAVDIRNSTVERNSALQEDLKNLLTILIETLQVLNENIHLSLTGKLVSKCEEWLERISGYITTNDELMLDTFLHNEINPFLEHFRNNYPAERETIDRYFNAMNEETGASFENRRKLETSMQLINTSINQYLEQAQTEVQESFPCYFEKFRTDGVEYDIYIGQSIAPQRVFDMLYLKNIRLWQLRSMAEIARMTNDLGDQLSRPLQTTHLIFIHSNAIDISFRNDERRFDVEGAYNIRYEVVKKRIDKVLIAGTFERLTQPGKIAMVYFNPTEAAEYDEYIRYLQVQGYLLDDLEYLELEELQGVTGLKALRVGVNYQLPLLNS
>NZ_CP043451.1|WP_112655056.1|2984117_2987723_-|BamA/TamA-family-outer-membrane-protein
MIKKLPLLFVSLLGMLKTQAQDSVQYRMILIGDAGEMDLQQSAVLKHAAANVLKNKTSVFYLGDNIYPRGMGLPGSPEEAETQKILQSQYQPMRAAVAPVYFIPGNHDWDKMGPLGLAKIKRQWEYLDQQGDKLLKMVPENGCPDPVEINLTNDLTVIAFDSEWWLYPFNKSNPGAECDCKNKDDVADKIKLIFERNKDKVIILASHHPFQSYGTHGGYFSLKDHIFPLTVANKDLWVPLPVIGSLYPFLRSAFSNPEDLGHPLYKDMIKKVDAVFGSFPNLIHVAGHEHGLQFIKSKQLQVVSGAGAKQTYAIKGKYSLFADATQGYVTADLLIDKRMRFTYYIDSDKGVKQVFTYTQPYTSVKNIPDTLHTPIKADSIMVRVHPKYDSVSNFHRRWFGENYRKEWAAETKLPVIRLSEIHGGLKAESIGGGFQTHSLRLIDKDGKEWVLRSVEKQPEKILPDEFQETFAKDWVNDAMSAQHPFSALIVPPLADAARVPHANPIIGVVSADPVLGQYANIFANKVCLLEEREPGGKSDNTVKMIGKMLEDNGNTVDGDEFLRARLLDLLIGDWDRHGDQWRWRDEDKGKGKFYTAIPRDRDQVFYTNQGILPTIAAQPWIAPNLQGFSGEIYSVKYSLWKTMFMQRWPSVQYSHEQWTKIVNDFVAAETDEVLEAGLRRLPESSYKLRHDVLLKQLKERRANIPAEMEYYYKFINKIVDIHTSNKNELVTVKDEPNGSLNVVINKINKDGNIKDTLMNQNYHPDITKELRIYVSGGDDKVVLDNATSPIKLRFIDSTGTKTYNIVKSLNTVQLYDRGKKLSITGDESKVNKYISKDSANTSYLRVNLMNVIAPLANISYNPDEGVLLGAGFKYTHQEGFQKLPYNDVQTVFASHSFTTKAFKIKYNGEWIHAFGKADFLMDAQLDFPDNINFFGRGNETPFVKVGDYRKYYRTRFDNFTFSPAFRWRNESGTSVTVGPAFRYYKLDVDDNIGRFITYPLLTNAPDSYTFDKTKMHAGIVVNFTSDKRNDKVLPAWGSFVNIKLQEFNGLNNNSTSFAQLIPQVALYKSLNAKSTIVLADRVGGGITIGKTAFYQSLFLGGQDNLLGYRLYRFAGQHSFYNNLELRIKLTDFASYIVPGQIGVIGFYDIGRVWENGQSSDKWHNGTGAGFYVAPARLAVIKIIAGYSEEGWYPYLSTSFRF
>NZ_CP043451.1|WP_112655379.1|2987775_2988636_-|SdiA-regulated-family-protein
MTLYVAGMLAVAVVFLIISCKNKEKAIPDSPPGYDLNNPVKYKMPEDLTEISGFAFHNGKNDSVYAEQDEEGFLFNLKLGDKKANYTKFGKSGDYEDVAICREQVIMLKSDGTLFTFPFNQVRTKEVTNVQKTKGQLPEGEFEAMCADEKTGLVYVLCKRCADEKTSKRSTGYILKLQADGTLKQTGSFAIDVREIERLADKKRVPFRPSAIAKNTFTNEWYVLSSVNKMLVVTDVNWKVKNVYPLSVTIFGQPEGMAFDNQRNLYISNEGDQLSAGNILKFSFKK

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Crispr_ID: NZ_CP043451_6

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP043451_6

4342737-4342854

Orphan

Consensus_repeat	Method
TTCTACAAACCTTTTGCCCCTCTGGGGCA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP043451_6

>merge|NZ_CP043451|6|4342737-4342854|CRISPRCasFinder
TTCTACAAACCTTTTGCCCCTCTGGGGCAGCTCAGGCTTGCCCAATAATTCCCCTTCCAAATATTATTAATTTATCAAAAGCTACTAACTTCTACAAATCTTTTGCCCCTCTGGGGCA

>NZ_CP043451|6|6|4342737-4342854|CRISPRCasFinder
TTCTACAAACCTTTTGCCCCTCTGGGGCA	GCTCAGGCTTGCCCAATAATTCCCCTTCCAAATATTATTAATTTATCAAAAGCTACTAAC
TTCTACAAATCTTTTGCCCCTCTGGGGCA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP043451.1\|WP_091172493.1\|4346300_4346696_-\|DUF4783-domain-containing-protein	unknown	unknown	gnl\|CDD\|379759
NZ_CP043451.1\|WP_112654772.1\|4334728_4336162_+\|serine/threonine-protein-phosphatase	unknown	unknown	gnl\|CDD\|223704
NZ_CP043451.1\|WP_112654774.1\|4340266_4341061_+\|FHA-domain-containing-protein	unknown	unknown	gnl\|CDD\|238017
NZ_CP043451.1\|WP_090531854.1\|4344536_4345190_-\|glycerol-3-phosphate-1-O-acyltransferase-PlsY	unknown	unknown	gnl\|CDD\|234691
NZ_CP043451.1\|WP_090531867.1\|4348990_4349641_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|276809
NZ_CP043451.1\|WP_112654783.1\|4352617_4353049_-\|DUF1801-domain-containing-protein	unknown	unknown	gnl\|CDD\|378058
NZ_CP043451.1\|WP_112654782.1\|4350009_4352484_+\|endopeptidase-La	unknown	unknown	gnl\|CDD\|223542
NZ_CP043451.1\|WP_112654770.1\|4332225_4333653_+\|serine/threonine-protein-kinase	unknown	unknown	gnl\|CDD\|270916
NZ_CP043451.1\|WP_112654768.1\|4328556_4329492_-\|ring-cleaving-dioxygenase	unknown	unknown	gnl\|CDD\|319934
NZ_CP043451.1\|WP_112654773.1\|4336165_4340242_+\|FtsW/RodA/SpoVE-family-cell-cycle-protein	unknown	unknown	gnl\|CDD\|223843
NZ_CP043451.1\|WP_112654775.1\|4341145_4341943_-\|DUF3050-domain-containing-protein	unknown	unknown	gnl\|CDD\|378614
NZ_CP043451.1\|WP_112654779.1\|4345293_4346139_-\|carboxylating-nicotinate-nucleotide-diphosphorylase	unknown	unknown	gnl\|CDD\|238806
NZ_CP043451.1\|WP_112654767.1\|4327924_4328548_-\|phospholipase	unknown	unknown	gnl\|CDD\|334855
NZ_CP043451.1\|WP_112654776.1\|4342211_4342679_+\|IS200/IS605-family-transposase	unknown	unknown	gnl\|CDD\|376616
NZ_CP043451.1\|WP_149466841.1\|4348444_4348969_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043451.1\|WP_112654778.1\|4343727_4344531_-\|M48-family-metallopeptidase	unknown	unknown	gnl\|CDD\|320690
NZ_CP043451.1\|WP_112654777.1\|4342949_4343681_-\|DUF2071-domain-containing-protein	unknown	unknown	gnl\|CDD\|378271
NZ_CP043451.1\|WP_112654771.1\|4333671_4334637_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043451.1\|WP_112654769.1\|4329673_4331983_+\|family-20-glycosylhydrolase	unknown	unknown	gnl\|CDD\|119333
NZ_CP043451.1\|WP_112654780.1\|4346892_4348416_+\|2,3-bisphosphoglycerate-independent-phosphoglycerate-mutase	unknown	unknown	gnl\|CDD\|235463

Protein	Function_ID	Function_description	E-value
NZ_CP043451.1\|WP_091172493.1\|4346300_4346696_-\|DUF4783-domain-containing-protein	gnl\|CDD\|379759	pfam16022, DUF4783, Domain of unknown function (DUF4783). This family of proteins is found in bacteria. Proteins in this family are approximately 130 amino acids in length. There is a single completely conserved residue F that may be functionally important. Recent structures show this domain has an NTF2 fold.	1.57482e-28
NZ_CP043451.1\|WP_112654772.1\|4334728_4336162_+\|serine/threonine-protein-phosphatase	gnl\|CDD\|223704	COG0631, PTC1, Serine/threonine protein phosphatase [Signal transduction mechanisms].	3.34684e-65
NZ_CP043451.1\|WP_112654774.1\|4340266_4341061_+\|FHA-domain-containing-protein	gnl\|CDD\|238017	cd00060, FHA, Forkhead associated domain (FHA); found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain. FHA domains may bind phosphothreonine, phosphoserine and sometimes phosphotyrosine. In eukaryotes, many FHA domain-containing proteins localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. Members of the FHA family include: Dun1, Rad53, Cds1, Mek1, KAPP(kinase-associated protein phosphatase),and Ki-67 (a human nuclear protein related to cell proliferation).	0.000167426
NZ_CP043451.1\|WP_112654780.1\|4346892_4348416_+\|2,3-bisphosphoglycerate-independent-phosphoglycerate-mutase	gnl\|CDD\|235463	PRK05434, PRK05434, 2,3-bisphosphoglycerate-independent phosphoglycerate mutase.	0
NZ_CP043451.1\|WP_090531867.1\|4348990_4349641_-\|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.	2.86961e-10
NZ_CP043451.1\|WP_112654783.1\|4352617_4353049_-\|DUF1801-domain-containing-protein	gnl\|CDD\|378058	pfam08818, DUF1801, Domain of unknown function (DU1801). This large family of bacterial proteins is uncharacterized. They contain a presumed domain about 110 amino acids in length.	5.1092e-06
NZ_CP043451.1\|WP_112654782.1\|4350009_4352484_+\|endopeptidase-La	gnl\|CDD\|223542	COG0466, Lon, ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones].	0
NZ_CP043451.1\|WP_112654770.1\|4332225_4333653_+\|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.	4.20352e-53
NZ_CP043451.1\|WP_112654768.1\|4328556_4329492_-\|ring-cleaving-dioxygenase	gnl\|CDD\|319934	cd08346, PcpA_N_like, N-terminal domain of Sphingobium chlorophenolicum 2,6-dichloro-p-hydroquinone 1,2-dioxygenase (PcpA), and similar proteins. The N-terminal domain of Sphingobium chlorophenolicum (formerly Sphingomonas chlorophenolica) 2,6-dichloro-p-hydroquinone1,2-dioxygenase (PcpA), and similar proteins. PcpA is a key enzyme in the pentachlorophenol (PCP) degradation pathway, catalyzing the conversion of 2,6-dichloro-p-hydroquinone to 2-chloromaleylacetate. This domain belongs to a conserved domain superfamily that is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases.	9.01968e-63
NZ_CP043451.1\|WP_112654773.1\|4336165_4340242_+\|FtsW/RodA/SpoVE-family-cell-cycle-protein	gnl\|CDD\|223843	COG0772, FtsW, Bacterial cell division membrane protein [Cell division and chromosome partitioning].	8.98485e-59
NZ_CP043451.1\|WP_112654775.1\|4341145_4341943_-\|DUF3050-domain-containing-protein	gnl\|CDD\|378614	pfam11251, DUF3050, Protein of unknown function (DUF3050). This bacterial family of proteins has no known function.	9.37228e-144
NZ_CP043451.1\|WP_112654779.1\|4345293_4346139_-\|carboxylating-nicotinate-nucleotide-diphosphorylase	gnl\|CDD\|238806	cd01572, QPRTase, Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called nicotinate-nucleotide pyrophosphorylase, is involved in the de novo synthesis of NAD in both prokaryotes and eukaryotes. It catalyses the reaction of quinolinic acid (QA) with 5-phosphoribosyl-1-pyrophosphate (PRPP) in the presence of Mg2+ to produce nicotinic acid mononucleotide (NAMN), pyrophosphate and carbon dioxide. QPRTase functions as a homodimer with two active sites, each formed by the C-terminal region of one subunit and the N-terminal region of the other.	2.88672e-145
NZ_CP043451.1\|WP_112654767.1\|4327924_4328548_-\|phospholipase	gnl\|CDD\|334855	pfam02230, Abhydrolase_2, Phospholipase/Carboxylesterase. This family consists of both phospholipases and carboxylesterases with broad substrate specificity, and is structurally related to alpha/beta hydrolases pfam00561.	2.52382e-19
NZ_CP043451.1\|WP_112654776.1\|4342211_4342679_+\|IS200/IS605-family-transposase	gnl\|CDD\|376616	pfam01797, Y1_Tnp, Transposase IS200 like. Transposases are needed for efficient transposition of the insertion sequence or transposon DNA. This family includes transposases for IS200 from E. coli.	1.11929e-36
NZ_CP043451.1\|WP_112654778.1\|4343727_4344531_-\|M48-family-metallopeptidase	gnl\|CDD\|320690	cd07331, M48C_Oma1_like, Peptidase M48C, integral membrane endopeptidase. This subfamily contains peptidase M48C Oma1 (also called mitochondrial metalloendopeptidase OMA1) protease homologs that are mostly uncharacterized. Oma1 is part of the quality control system in the inner membrane of mitochondria, with its catalytic site facing the matrix space. It cleaves and thereby promotes the turnover of mistranslated or misfolded membrane proteins. Oma1 can cleave the misfolded multi-pass membrane protein Oxa1, thus exerting a function similar to the ATP-dependent m-AAA protease for quality control of inner membrane proteins; it cleaves a misfolded polytopic membrane protein at multiple sites. It has been proposed that in the absence of m-AAA protease, proteolysis of Oxa1 is mediated by Oma1 in an ATP-independent manner. Oma1 is part of highly conserved mitochondrial metallopeptidases, with homologs present in higher eukaryotes, eubacteria and archaebacteria, all containing the zinc binding motif (HEXXH). It forms a high molecular mass complex in the inner membrane, possibly a homo-hexamer.	2.06375e-91
NZ_CP043451.1\|WP_112654777.1\|4342949_4343681_-\|DUF2071-domain-containing-protein	gnl\|CDD\|378271	pfam09844, DUF2071, Uncharacterized conserved protein (COG2071). This conserved protein (similar to YgjF), found in various prokaryotes, has no known function.	8.03069e-63
NZ_CP043451.1\|WP_090531854.1\|4344536_4345190_-\|glycerol-3-phosphate-1-O-acyltransferase-PlsY	gnl\|CDD\|234691	PRK00220, PRK00220, glycerol-3-phosphate 1-O-acyltransferase PlsY.	1.83026e-65
NZ_CP043451.1\|WP_112654769.1\|4329673_4331983_+\|family-20-glycosylhydrolase	gnl\|CDD\|119333	cd06563, GH20_chitobiase-like, The chitobiase of Serratia marcescens is a beta-N-1,4-acetylhexosaminidase with a glycosyl hydrolase family 20 (GH20) domain that hydrolyzes the beta-1,4-glycosidic linkages in oligomers derived from chitin. Chitin is degraded by a two step process: i) a chitinase hydrolyzes the chitin to oligosaccharides and disaccharides such as di-N-acetyl-D-glucosamine and chitobiose, ii) chitobiase then further degrades these oligomers into monomers. This GH20 domain family includes an N-acetylglucosamidase (GlcNAcase A) from Pseudoalteromonas piscicida and an N-acetylhexosaminidase (SpHex) from Streptomyces plicatus. SpHex lacks the C-terminal PKD (polycystic kidney disease I)-like domain found in the chitobiases. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself.	0

>NZ_CP043451.1|WP_112654776.1|4342211_4342679_+|IS200/IS605-family-transposase
MASNNTYSQLYIHIVFAVKYRMALIEDTWAERLRMYITSIIQNQGHKLIAINNMPDHLHLFIGLNPNQSISEIVRIMKSDSSEWINKQKLANGGFQWQEGYGAFSNSRSQIDKVVNYIANQQEHHRKITFLDEYRKMLNDFNIEFDEQYIFKLPQ
>NZ_CP043451.1|WP_112654775.1|4341145_4341943_-|DUF3050-domain-containing-protein
MANYSNRIAQLKNEIHPLRDQLINHELYKNITSLDELTVFMEHHVFAVWDFMSLLKALQQKLTCTVTPWMPTGNANTRYLINEIVAGEESDIDERGNRASHFELYLRAMQQAGSQAEGINNLFNELNFGKHIDEALIIANIPVAARNFVQHTFDVIDTNKDHLQAAVFTFGREDLIPDMFVSIVKELSQQLPGKVDILLYYLERHIEVDGDHHSQLAYQMTAELCGNDDSKWAEATVAVKEALRARIALWDGILEAIKVQEISSL
>NZ_CP043451.1|WP_112654774.1|4340266_4341061_+|FHA-domain-containing-protein
MAFSLFKRSGEKQPWDVKSLREAILRFIKESLQKIEGGEGGHIKELKLFIVADAEDKPIYEGAVYVHDKALFKNEVQKIADDFDINLPPDWTLDVEFTEELPAEAKRIPDLDAAFIMNTRKQVAHNAASFTAYLRILSGEAEKEEYLIKATDPKLYIGRDKKSVTENGSFRLNQFVFPGESRDESNKYISRQHAHIEWDGESERFMIFADEGGVPPRNKTKIHIAADGKMIKLNSTQIGHPLSEGDQVILGESAVFLYTTIANR
>NZ_CP043451.1|WP_112654773.1|4336165_4340242_+|FtsW/RodA/SpoVE-family-cell-cycle-protein
MAQENPKVPGRRMERLFLLLTGILLAVLFVKLFGVLQLKFTDVDKRLKDGTIVNLNSPNTAQNVKALLKKGYYFDDPKDIDYIESVIASRKTTGEQVDNTGELNKRKYYVNADEAFEKGGETFKKRVLTSRTLLGYTGDDSIRFEQELKNPPALGAQTDLNLGEYSIKGTIAHKGEPVPGVLVKLTMILPRDSIFSDEETGAKTSYSENASSYKKLYVLNDQKKKVLQSLTAFARTDEQGRFVFAKLPTGKAFSVLPMQPGFEFGRSQGVDELDKDVSFKFSQAPHSIKLLSTRDFNILKKEGAFIVRYQEEFNMWYWIIAGSFFAGFIIVHLLLSARYPDADQIILPLIMMLTGISFLTLLSLQDPLRDRFLAKDTLVYLGIGMAGICIIQLFNLRRLNPDSGFYRLLVFKWSRSAANGWPWAIVAMGILFSTILFGTGPEGSGVKVNLLGFQPSEIVKYLIVIFLAGFFATNEKFISQYASWSKRWSFFSFALIATIITLLLFLVLGDLGPAMVICFTFIILFSFSRGDFLYMAGFVVLFVLTTWFFDNIWLSAGITFFSLGSVVFFRRRRLSESAIMALVVITAFLTIDKIPGLDKIIPGPVERLVERKAIWQDAWNNEVYGGDQVANGLWAMASGGVNGQGVGQGFAKTIPEAHTDMILPSIGEEFGWAGMAAVFILFLLYLHRSIIIGRQTGMPLLFYLSAGIGVCTFVQFLLIAGGSIGALPLSGVSLPFESYGGSSLVINLLAAGFLLSVSSVRGTAVQMDYITKQQDKNLVPALAAALAGVVLLVVNVSRYTTDNKQWVVKPALVADKSGLRMFSYNPRIAILMNRLQAGTIYDRNGLILATSKPELIEKQKNKLSASGMLHYDLDSAMHKRLDRFYPFEEQTFFWTGDQNTGVFNGSTNGYFAEYEHAAELRGFHMPITNYNVKASRYQEDRFLPRGMKEMTVAKKDYSALANLLVSDINGPEVEAFKNKNRDVKLTMDADLQTSIQQSIASDTSLYDNRVSVVIMESNTGDVLTSAQYPLPPVHNWDQLTMPLADQNKLATWLTTTDLGFTYASQPGSTAKVLTAMSAFNKLGIAASAIQYHVSTQERIRTKGIEPDETGMITMERAIAKSNNVYFIKLANQEHLEEYMATLYLKTGMFLHGVGGYYYNKPVLNATQEDKWRTLWRKTEFNTKPRYDPNNIHKTRAKGISGMAWGQGELIATPAAVARLVSGVANDGILLPNRYALKIADSTVAVKSGIKLAEDPRYAALLKQYMIEQSAPKTPILGIKVAGKTGTPERIVRNQSVNDGWYVFFAPKEKGSGYLVVCIRVESTRGSSDAVHLAGNHVIPFLLKKGYIKSMETETTTEE
>NZ_CP043451.1|WP_112654772.1|4334728_4336162_+|serine/threonine-protein-phosphatase
MANNFFGITDTGRQRQNNEDVFIAEKSGDGNFIIACVVDGVGGYAGGEIAAEIARATILEQLQYIAGDIVPLLVNTFTIANQRIYDEKVQNKDLENMACVLTLAVVDMINNKFYYAHVGDTRLYLLRDYSLIKISKDHSFVGFLEDSGRLTEEAAMDHPKRNEINKALGFAGQIGQDPDFVETGNSPFLPGDILLICSDGLTDLVDKSKITNILTSSDNLPEKGKKLIDAANNRGGKDNVTVVLVHNDKERKQHSATKPVVAAVKAAEQPEAITPAPAKRQEEPNPVVKTKGNGGTVAVLTLLCFIFLGGFIWQFKKNADQAAVPKKTDTLIAQHIKNAVELKLQDTINKLKGHTLLLSAADFQQPIVLSDTLHINKDSLYIKTKGAVVFKKDSTYSGPAIALAANCKYVVLDSVAFDGFGTAIVTHNDALVLKNVQFNNCLTPVQALYMFPNKKYISGRLFGSMFKTDSVPTKATH
>NZ_CP043451.1|WP_112654771.1|4333671_4334637_+|hypothetical-protein
MEPKSTFWKRIGLQDWFLPNGKPVNEEAVKIKALTPDDVYLYIIEKFKESIKQLSFADRIVFYHEFIISFNEEDYQDFVNNRSGLFGIIVNESVKKFYELLREHQEVGKKVEPSSSKWVFRLVSHPDYKRGDKGFIGKLLPGTSAKKEENLRVTFIPRQTGVAQTLDISNEVLKGFTYYSEGYYELPYANDLHYNEKDVAKPGTKVLARLETIMPDKQFVGRKVEYLIKDDDIVVSGSDEEREEQAVFKVPSEWVNTPHLRIRLNKADGKFYMASFGERTLINELEVAGSDVNSPQWVELPFNSRILLNGIVGINIFKPEP
>NZ_CP043451.1|WP_112654770.1|4332225_4333653_+|serine/threonine-protein-kinase
MSKVFTITEGLENMGALRTGGQGSVYKGRRYGPIITAVKLLPTPIHTESTDDKNFRNFQNEVEKLKKVNEEPNPNVVKILNSGITESGSFPFIEMEYIDGPDLEDLLKPPHEAIFSIKEIIKLADQLANALSHCHKVSVKHGDIKSNNVKFNVHTGNYVLLDFGLSAMSDDQRRTSIRHAGAIEFMAPEQNEGLMYFQTDVYSYGIILYELIGGQVPFPLKDNGETARNAVMLAHMESEIPDVMELRRKNLPESWSDEKKEMQMQVPAWLLQIVAKCLQKDINNRYANGIELQEALMQGSIGAISPTHPDESWNTEVLLKENERLQGLVLYYQENENKQPAQVVNSEPVDNKAVRMSKPIFVLFMILLCGFTVFSAVVMDKFGGRIYNGVVSRLFKPSKKATDSAASNKIILPQKKDSVQQPKASDYKDESNIPPEVDSTADSILRNIQRAKQQKEDTQFYRDSVKKADTSNLNF
>NZ_CP043451.1|WP_112654769.1|4329673_4331983_+|family-20-glycosylhydrolase
MSSYNLFFSRPIKIIVFILCVAFALPGKAQIYKQGVIPQPVKIKSNDITYAFPREFVIGLGPSIKASNVTFFRHYINLARDIHETEPFVNHKMAASNLWLQLDPKSISQPEGYTLVVKPHQITITGHDEAGVFYGLQSLIQLLDIGKDKITVKGYTITDYPRFAYRGMHLDVSRHFFKPEAIKKWIDLLALYKINTFHWHLTDDQGWRIEIKKYPLLQSISAYRDETIIGHKKDSPHKFDGVRYGGYYTQDEVKEIVKYATQRHITVIPEIEMPGHALAALAAYPQLGCTDGPYKTATFWGIFDDVYCAGNDETFAFLQNVMDEVLPLFPSKYIHIGGDECPKTKWKVCPKCQQRIKDEHLKDEKELQSYFIGRMEKYLNSKGRQIIGWDEILEGGLTSGATVMSWTGEEGGIAAAKQHHDAIMTPEKYVYLDYYQSLYPAEPLAGGGYTPLSKVYNYEPITGDLSGEEAKYIKGVQANAWSEYMTSPAQAERQLFPRMLALAEVAWSPKQSKNYDDFLKRLRYHQPLSNLDINAAKVFDEITDSVIETANHQVALNLQTTLPGAKIFYTTDGTEPGLNSKGYISAITIASSGIIKAAVFNNGRQQGRTYEKSFSIHKAIGKTVALKNQPQGGFNPGNTFSLVNGIFGSKLYNDGQWYGFAGDDLEAVVDLGSMQNVSKLGINILKYHWQKMWEPTLLTFEVSADGSNYTEVYRQTDFPDNGINAVRANIKTQQARYIRVKATNKEIIPPGEYIAGAKAWLMVDEIVIQ
>NZ_CP043451.1|WP_112654768.1|4328556_4329492_-|ring-cleaving-dioxygenase
MENTINGIHHITAIAGNAKKNYDFYTRVLGLRLVKKTVNFDDPGTYHLYYGDGNGTPGSILTFFPWEGIATGRRGARQVTEIGYSVPEGSLDFWLKRFEDNNVIYNKPAEKFGEQYLTFLDPDGLKFELIVPKKADNRTPWETAEVTAANATKGFHSITITSNKIEATAKILTGVLGYRLLEQHVNRYRFITDAVDNAAIVDLVEVPGEVAGHVAGGSVHHVAFRVPNEKVLMEYREKIANLGLHITDKIDRNYFYSLYFREPGGVLFEIATDNPGFAVDEPAELLGTGLKLPAQYENLRGELEKTLPSLV
>NZ_CP043451.1|WP_112654767.1|4327924_4328548_-|phospholipase
MYRHTKQVVSAGVPAEQAKKAIIMLHGRGASASSMISLKDHLELDGYAIYAPEANQHSWYPYSFMAPVQNNQPALDSALEVIDELVEDLRQKGIAKENIYFLGFSQGACLTLEYTGRNAGRYGGIIAFTGGLIGEELVKENYKGDFNNTPVLITTGDPDPHVPVSRVNDSVEILKELNADLTLKIYKGRQHTISHEEIVLANEILKN
>NZ_CP043451.1|WP_112654777.1|4342949_4343681_-|DUF2071-domain-containing-protein
MAKSEFLKAQWKNLVMINYEVDAAILKPYTPAGTVLDLWEGKALVSMVGFMFSDTRVLGIKWPWHVNFEEVNLRFYVRYFNGTEWKRGAVFISEIVPKSMIVLIANNLYKEHYRALPMRSSITSAADNHTQFLYEWKLNGRWNKLGATASNELVDIKAGSAEEFILEHYWGYNSLSPIKTMEYQVEHVSWQTGLVREYVFDADVAALYGEAFRPFLEKEPVSAFYALGSDIVVRMGEKIVVGK
>NZ_CP043451.1|WP_112654778.1|4343727_4344531_-|M48-family-metallopeptidase
MKKFKPLLVLIAIMAVFSCSTVPLTGRKQLSLVGDAEVNQSAAASYKQLLSDPKTKVVASGADAQRVKTIGNRLAVAIEKYLKENGYGDQYSFNWEFNLIQSSEVNAWCMPGGKVAVYSGLLPVANTDAYLAVVMGHEIGHAIARHSAERISQEMLVQGGGQLVGAATSQQSQATQTAISTLYGVGSQLKLLAYSRKQESEADRLGLTFMAMAGYDPHNAIAFWQRMAAQNKGGSPPEFLSTHPADATRIADIQNLIPEAMKYYKKY
>NZ_CP043451.1|WP_090531854.1|4344536_4345190_-|glycerol-3-phosphate-1-O-acyltransferase-PlsY
MITVYSVTALIMAYLCGSIPTAVWIGMAFYNVDVREYGSGNAGATNTFRVLGKKAGIPVMLLDIFKGWAATNFAYFIGASATGAINSTAYTNYELALGIAAVMGHLFPIFAGFRGGKGVATLFGMILAIHFHAALLCIVVFITVLLISKYVSLSSIAAAFTYPIGVTFVFPTPIRSIVIYGMCICVLVLVTHQKNIERLIRGKESKVNFFKKKTTAA
>NZ_CP043451.1|WP_112654779.1|4345293_4346139_-|carboxylating-nicotinate-nucleotide-diphosphorylase
MDKELIHQFINNALSEDVGDGDHTSLSTIPADATGKAKLLVKDEGILAGIELAAEIFHVVDPNLKLNVFLQDGAPVKYNDIAFEVEGNSRSILTAERLVLNCMQRMSGIATKTRQIVDLLKGTNTKVLDTRKTTPGLRYLEKWAVRIGGGVNHRFGLYDMILIKDNHVDYAGGIRQAIESANQYLTDSGKKLAIEIEVRNLDELEQVLQTGRVNRILLDNFNFDDLRQAVGIIQGRYITEASGGITIDNIREYADCGVDYISVGALTHSVKSLDLSLKAVK
>NZ_CP043451.1|WP_091172493.1|4346300_4346696_-|DUF4783-domain-containing-protein
MKLIYLPSFIFLLLLPYVSSADAIDNVANLLKTGNTKELSKLFANNVEITIMEDENVYSQNQATVILDKFFARNKPKSIKLLHKINSGGNYHFGVYILNTDKGEFRVAITLKDAGKGTNVVELKIEDEKVK
>NZ_CP043451.1|WP_112654780.1|4346892_4348416_+|2,3-bisphosphoglycerate-independent-phosphoglycerate-mutase
MENKKKLALIILDGWGYGRNDQSNAILAANTPFVDGLLKQYPNSKLEASGTAVGLPAGQMGNSEVGHMNLGAGRVVYQELGRIHKAVDDNELPTIPVLKDAFEYAKQNNKDVHFIGLVSDGGVHSHIRHVKGLCDTAKQLDVNNVYIHAFLDGRDTDPKSGLGFVTELEEHIAGAGAKIASAIGRYYAMDRDNRWERVKLAYDLMVNGIGTPTQNVTDLIKHSYLEDVTDEFVKPIVAVDDAGKPLAVIKDGDVVICFNFRTDRGREISIALTQKSFPEYNMHPLAIRYITMTPYDETFKNVQVVFNKEDLTKTLGEILQNAGKSQIRIAETEKYPHVTFFFSGGREKEFANEKRLLVPSPKVATYDLQPEMSAAGIRDAIIPELETGWPDFVCLNFANTDMVGHTGVFSAVVKAAETADSCTKAVVEAGLANGYSFIILADHGNADYMINEDGSPNTAHTTNLVPCIVIDKDVKEVKDGKLGDVAPTILSILGVAIPPEMTGNVLV
>NZ_CP043451.1|WP_149466841.1|4348444_4348969_+|hypothetical-protein
MGGFLLLIANLFSCRPDNRQSGAKLVYFDLKEFFRADSARLTRLNPAVNKTVTHNGVTETKVVHIGNWNQELNLFIQSDINRPAWKNSYTVSTSDSAIIYKARTPELKTRRIIIKKAGDKVAWILIYNHTKNLLYETNEKLSYFPDSLYLIQKTQHVKLMGRNDYKVQGTLPKR
>NZ_CP043451.1|WP_090531867.1|4348990_4349641_-|hypothetical-protein
MKLSVILPLLIMSSLESAIAQNAYVRLGQQALMDGDFRSAVSHLEKACITDSTNANAMWMLGYSYYHSDNYKKSILAYTKVIAVKPADATAYYYRARAKSYLGRDSQASAADKELYLLGAIVDLTKAISINSDLRDNKYYQNRGIAYRDYGMFKLQATSRFYDKARGINSLKASVADLEKVLADNPGRMDISALIDQSKEKLIQATTGVNTLVKQH
>NZ_CP043451.1|WP_112654782.1|4350009_4352484_+|endopeptidase-La
MNFDPFDFKNALPVINEDSEFFPLMSSEDEEEMNNEELPDVMPILPLRNTVLFPGVVIPITVGRDKSIKLIRDANKGSRMIGVVSQQDVGIEDPTFNQLNKVGTIALIIKMLQMPDGNTTVIIQGKKRFYLKEEVQSEPYIKATVEPFHEIKIKEDKEFKAMVSSIKDMAMNIIQLSPNIPSEAGIAIRNIESTSFLINFISSNMNADMTAKQHLLEIANLRERANLVLEHLTLDLQMLELKNQIQTKVRVDLDKQQRDYFLNQQLKTIQEELGGNTPDLEIESLRQRGIKKKWAKEVKDHFNKELEKLSRTNPAAADYSVQINYLELLLDLPWNEFTKDNFDLKRAQRILDKDHFGLDKVKQRIIEYLAVLKLKHDMKAPILCLVGPPGVGKTSLGKSIAKALGRKYVRMALGGIRDEAEIRGHRKTYIGAMPGRIIQSIKKAGASNPVFILDEIDKVGNDFRGDPSSALLEVLDPEQNGTFSDHYVEMDYDLSNVMFIATANSLSTIQPALLDRMEIIEVNGYTIEEKIEIAKQHLVPKQREAHGLKIKDVSLKADVIEKVIVDYTRESGVRSLEKKIGSVVRGVAKNIAMEEPYNSVVSKKDIEKILGAPIFDKDLYEGNDVAGVVTGLAWTSVGGDILFIEASLSPGKGRLTLTGSLGDVMKESVTIALAYLRAHAADFDINPKLFDQWDVHVHVPAGATPKDGPSAGVTMLTALVSAFTQRKVKPNLAMTGEITLRGRVLPVGGIKEKILAAKRANIKEIILCKSNQKDILEIKEDYIKDLSFHYVTDMRDVITLALLNEKVKNPINLTVKEDEKAAIN
>NZ_CP043451.1|WP_112654783.1|4352617_4353049_-|DUF1801-domain-containing-protein
MNVQQQTEEYIASQPEPKRGDMQTLHRHILQILPGCKLWFEDGRNAEGRIVSNPNVGYGSYTIKYANGTTREFFQVGMSANTTGISIYILGIKDKKYLAQTYGKEIGKANVTGYCIKFNNLKDINIDILEAAIRDGVEITNEN

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Crispr_ID: NZ_CP043451_7

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP043451_7

4700276-4700373

Orphan

Consensus_repeat	Method
ACTTTGAAATACAAAGTACTTTATA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP043451_7

>merge|NZ_CP043451|7|4700276-4700373|CRISPRCasFinder
ACTTTGAAATACAAAGTACTTTATACTATATTTGTCACAGGCTTAACAAAGAGCCCTTTCTTTTTAATTATAAACTTTGAAATACAAAGTACTTCATA

>NZ_CP043451|7|7|4700276-4700373|CRISPRCasFinder
ACTTTGAAATACAAAGTACTTTATA	CTATATTTGTCACAGGCTTAACAAAGAGCCCTTTCTTTTTAATTATAA
ACTTTGAAATACAAAGTACTTCATA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP043451.1\|WP_112652677.1\|4697320_4697602_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043451.1\|WP_167516351.1\|4708260_4709031_+\|dihydropteroate-synthase	unknown	unknown	gnl\|CDD\|273657
NZ_CP043451.1\|WP_112652674.1\|4692377_4693334_-\|rhodanese-related-sulfurtransferase	unknown	unknown	gnl\|CDD\|234663
NZ_CP043451.1\|WP_112652683.1\|4703631_4704027_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043451.1\|WP_112652672.1\|4686092_4689119_-\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|274948
NZ_CP043451.1\|WP_112652680.1\|4699451_4700033_+\|TetR/AcrR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224228
NZ_CP043451.1\|WP_112652721.1\|4704135_4704648_+\|phosphoribosyltransferase	unknown	unknown	gnl\|CDD\|235365
NZ_CP043451.1\|WP_112652681.1\|4700384_4701719_+\|cell-envelope-integrity-protein-CreD	unknown	unknown	gnl\|CDD\|377608
NZ_CP043451.1\|WP_112652684.1\|4704764_4705268_-\|shikimate-kinase	unknown	unknown	gnl\|CDD\|140006
NZ_CP043451.1\|WP_091172165.1\|4699038_4699452_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|225057
NZ_CP043451.1\|WP_112652686.1\|4706341_4707505_-\|DoxX-family-protein	unknown	unknown	gnl\|CDD\|225168
NZ_CP043451.1\|WP_112652673.1\|4689380_4692275_-\|transcriptional-regulator	unknown	unknown	gnl\|CDD\|369392
NZ_CP043451.1\|WP_112652679.1\|4698004_4699042_+\|phenylalanine--tRNA-ligase-subunit-alpha	unknown	unknown	gnl\|CDD\|234780
NZ_CP043451.1\|WP_112652675.1\|4693478_4695959_-\|carboxypeptidase-like-regulatory-domain-containing-protein	unknown	unknown	gnl\|CDD\|372685
NZ_CP043451.1\|WP_090534301.1\|4707510_4708002_-\|DUF1599-domain-containing-protein	unknown	unknown	gnl\|CDD\|377892
NZ_CP043451.1\|WP_112652682.1\|4702052_4703459_+\|23S-rRNA-(uracil(1939)-C(5))-methyltransferase-RlmD	unknown	unknown	gnl\|CDD\|225174
NZ_CP043451.1\|WP_112652685.1\|4705278_4706337_-\|ABC-transporter-permease	unknown	unknown	gnl\|CDD\|223674
NZ_CP043451.1\|WP_112652676.1\|4696088_4697279_+\|glycine-C-acetyltransferase	unknown	unknown	gnl\|CDD\|235893
NZ_CP043451.1\|WP_112652688.1\|4709040_4709526_+\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|366181
NZ_CP043451.1\|WP_112652678.1\|4697591_4698008_+\|PIN-domain-containing-protein	unknown	unknown	gnl\|CDD\|379205

Protein	Function_ID	Function_description	E-value
NZ_CP043451.1\|WP_167516351.1\|4708260_4709031_+\|dihydropteroate-synthase	gnl\|CDD\|273657	TIGR01496, Dihydropteroate_synthase, dihydropteroate synthase. This model represents dihydropteroate synthase, the enzyme that catalyzes the second to last step in folic acid biosynthesis. The gene is usually designated folP (folic acid biosynthsis) or sul (sulfanilamide resistance). This model represents one branch of the family of pterin-binding enzymes (pfam00809) and of a cluster of dihydropteroate synthase and related enzymes (COG0294). Other members of pfam00809 and COG0294 are represented by model TIGR00284. [Biosynthesis of cofactors, prosthetic groups, and carriers, Folic acid].	3.07803e-111
NZ_CP043451.1\|WP_112652674.1\|4692377_4693334_-\|rhodanese-related-sulfurtransferase	gnl\|CDD\|234663	PRK00142, PRK00142, rhodanese-related sulfurtransferase.	7.41891e-159
NZ_CP043451.1\|WP_112652672.1\|4686092_4689119_-\|TonB-dependent-receptor	gnl\|CDD\|274948	TIGR04056, OMP_RagA_SusC, TonB-linked outer membrane protein, SusC/RagA family. This model describes a distinctive clade among the TonB-linked outer membrane proteins (OMP). Members of this family are restricted to the Bacteriodetes lineage (except for Gemmatimonas aurantiaca T-27 from the novel phylum Gemmatimonadetes) and occur in high copy numbers, with over 100 members from Bacteroides thetaiotaomicron VPI-5482 alone. Published descriptions of members of this family are available for RagA from Porphyromonas gingivalis, SusC from Bacteroides thetaiotaomicron, and OmpW from Bacteroides caccae. Members form pairs with members of the SusD/RagB family (pfam07980). Transporter complexes including these outer membrane proteins are likely to import large degradation products of proteins (e.g. RagA) or carbohydrates (e.g. SusC) as nutrients, rather than siderophores. [Transport and binding proteins, Unknown substrate].	0
NZ_CP043451.1\|WP_112652680.1\|4699451_4700033_+\|TetR/AcrR-family-transcriptional-regulator	gnl\|CDD\|224228	COG1309, AcrR, Transcriptional regulator [Transcription].	7.78294e-14
NZ_CP043451.1\|WP_112652721.1\|4704135_4704648_+\|phosphoribosyltransferase	gnl\|CDD\|235365	PRK05205, PRK05205, bifunctional pyr operon transcriptional regulator/uracil phosphoribosyltransferase PyrR.	7.56042e-26
NZ_CP043451.1\|WP_112652681.1\|4700384_4701719_+\|cell-envelope-integrity-protein-CreD	gnl\|CDD\|377608	pfam06123, CreD, Inner membrane protein CreD. This family consists of several bacterial CreD or Cet inner membrane proteins. Dominant mutations of the cet gene of Escherichia coli result in tolerance to colicin E2 and increased amounts of an inner membrane protein with an Mr of 42,000. The cet gene is shown to be in the same operon as the phoM gene, which is required in a phoR background for expression of the structural gene for alkaline phosphatase, phoA. Although the Cet protein is not required for phoA expression, it has been suggested that the Cet protein has an enhancing effect on the transcription of phoA.	3.60951e-176
NZ_CP043451.1\|WP_112652684.1\|4704764_4705268_-\|shikimate-kinase	gnl\|CDD\|140006	PRK13949, PRK13949, shikimate kinase; Provisional.	2.16174e-56
NZ_CP043451.1\|WP_091172165.1\|4699038_4699452_+\|hypothetical-protein	gnl\|CDD\|225057	COG2146, {NirD}, Ferredoxin subunits of nitrite reductase and ring-hydroxylating dioxygenases [Inorganic ion transport and metabolism / General function prediction only].	1.20345e-07
NZ_CP043451.1\|WP_112652686.1\|4706341_4707505_-\|DoxX-family-protein	gnl\|CDD\|225168	COG2259, COG2259, Predicted membrane protein [Function unknown].	0.000456018
NZ_CP043451.1\|WP_112652673.1\|4689380_4692275_-\|transcriptional-regulator	gnl\|CDD\|369392	pfam07495, Y_Y_Y, Y_Y_Y domain. This domain is mostly found at the end of the beta propellers (pfam07494) in a family of two component regulators. However they are also found tandemly repeated in CTC_02402 without other signal conduction domains being present. It's named after the conserved tyrosines found in the alignment. The exact function is not known.	9.1016e-06
NZ_CP043451.1\|WP_112652679.1\|4698004_4699042_+\|phenylalanine--tRNA-ligase-subunit-alpha	gnl\|CDD\|234780	PRK00488, pheS, phenylalanyl-tRNA synthetase subunit alpha; Validated.	0
NZ_CP043451.1\|WP_112652675.1\|4693478_4695959_-\|carboxypeptidase-like-regulatory-domain-containing-protein	gnl\|CDD\|372685	pfam13715, CarbopepD_reg_2, CarboxypepD_reg-like domain. This domain family is found in bacteria, archaea and eukaryotes, and is approximately 90 amino acids in length. The family is found in association with pfam07715 and pfam00593.	1.78668e-14
NZ_CP043451.1\|WP_090534301.1\|4707510_4708002_-\|DUF1599-domain-containing-protein	gnl\|CDD\|377892	pfam07659, DUF1599, Domain of Unknown Function (DUF1599).	2.14838e-32
NZ_CP043451.1\|WP_112652682.1\|4702052_4703459_+\|23S-rRNA-(uracil(1939)-C(5))-methyltransferase-RlmD	gnl\|CDD\|225174	COG2265, TrmA, SAM-dependent methyltransferases related to tRNA (uracil-5-)-methyltransferase [Translation, ribosomal structure and biogenesis].	5.23904e-122
NZ_CP043451.1\|WP_112652685.1\|4705278_4706337_-\|ABC-transporter-permease	gnl\|CDD\|223674	COG0601, DppB, ABC-type dipeptide/oligopeptide/nickel transport systems, permease components [Amino acid transport and metabolism / Inorganic ion transport and metabolism].	8.63107e-102
NZ_CP043451.1\|WP_112652676.1\|4696088_4697279_+\|glycine-C-acetyltransferase	gnl\|CDD\|235893	PRK06939, PRK06939, 2-amino-3-ketobutyrate coenzyme A ligase; Provisional.	0
NZ_CP043451.1\|WP_112652688.1\|4709040_4709526_+\|GNAT-family-N-acetyltransferase	gnl\|CDD\|366181	pfam00583, Acetyltransf_1, Acetyltransferase (GNAT) family. This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.	3.18553e-12
NZ_CP043451.1\|WP_112652678.1\|4697591_4698008_+\|PIN-domain-containing-protein	gnl\|CDD\|379205	pfam13470, PIN_3, PIN domain. Members of this family of bacterial domains are predicted to be RNases (from similarities to 5'-exonucleases).	2.72763e-11

>NZ_CP043451.1|WP_112652680.1|4699451_4700033_+|TetR/AcrR-family-transcriptional-regulator
MEADKIKDSIKRAAQELFRKFGYHKTSVNEIAKKAKIAKATIYKYFDSKEAVLHVLLMDYIKASVDDLVQVNANDIDEEAYLNNLIMKTCRLSYTVCNEFIGWDFIRESTNSQDFLKNLSNELEELLMASFIQLPGIRKHETYQQRLRFLIKCSKSIVFSFAFTSVSDSDVRKNFVSFQKEILPYLVKAAVSV
>NZ_CP043451.1|WP_091172165.1|4699038_4699452_+|hypothetical-protein
MRKLTIILLVVIGCFSCGKATDNVPSVPVNFQAALGTPALSPLNVAGGAVAINGYGVSGLIIYRKVNGTYAAYDRCSSYQPEKKCAVTIDNTGFTVTDPCSGSKFSLEDGTPVKAPATKALRTYRVAVTQFEIQVTN
>NZ_CP043451.1|WP_112652679.1|4698004_4699042_+|phenylalanine--tRNA-ligase-subunit-alpha
MMQAQIDQYTAEINAFSPANADELEAFRIKFLGTKGIIKDLFEQFKSVSPEEKRTFGKVLNEFKQLTEAKYNELKENIVTGTQSKGNDLDLTLPGDGFTVGSRHPLSLVRNEIIDIFKRLGFVVAEGPEIEDDWHNFSALNFPEEHPARDMQDTFFIKKNNGKDDIALRTHTSSVQVRMMEAGKPPFRAIMPGRVYRNEAISARAHCFFHQVEGLYVDENVSFSDLKQTLYHFVQELYGEGTRVRFRPSYFPFTEPSAEMDISCTICGGAGCNMCKHSGWVEILGCGMVDPNVLENCGIDSKKYTGFAFGMGMERIANLKYVIRDLRLFSENDVRFLKQFQTEML
>NZ_CP043451.1|WP_112652678.1|4697591_4698008_+|PIN-domain-containing-protein
MAYKRLFLDSDVLLDMFLKREPFFFHTQILLIECIKRNIELRTSSLVIANIVYVLRKQAGILKAKENLKNLFNSAKVLPFEFDAIETAILSDITDFEDAIQFHIAQKHNCDAIITRNIKDYKNSTIPVLTAEQFLNTL
>NZ_CP043451.1|WP_112652677.1|4697320_4697602_+|hypothetical-protein
MESTKLTLSVKADSLSLVKEYAKRQHTSVSKLVQEFLDGIAEQEKKDDPIKEKYKNVEIPEWITQLTGIVKDPNPDMSYDDMKQEYFKEKYGL
>NZ_CP043451.1|WP_112652676.1|4696088_4697279_+|glycine-C-acetyltransferase
MYNTLKPVLQQELTEIENAGLYKKERIITSPQGADITVQGGAEVINFCANNYLGLSGNAKVVQAAKDAMDTHGYGLSSVRFICGTQDIHKELEKKIAEFLGTEDTILYAAAFDANGGVFEPLFNDQDAIISDELNHASIIDGVRLCKAQRYRYKHDDMADLEEKLKATQELRHRIIVTDGAFSMDGTIAQLDKICDLADKYNALVMIDESHCSGFMGKNGRGTHEHHNVMGRIDIITGTLGKALGGASGGFTSGRKEIIDMLRQRSRPYLFSNTLAPAITGASIAVLDMLSETTELRDKLESNTQYFRQKMTEAGFDIKPGVHPIVPVMLYDAKLAQEFAAKMLDEGIYVIGFYYPVVPQGKARIRVQISAAHDMHHLDKAIAAFTKVGKQLGVLK
>NZ_CP043451.1|WP_112652675.1|4693478_4695959_-|carboxypeptidase-like-regulatory-domain-containing-protein
MRKYILLLITAFSVITASAQQSLLTGKITDKNGQVIPFVSIYIRNSTYGTTANENGIYQFKLAPGTYNVIYRYVGYTEKIEEVTIADHDQEHNVQMADEVFATNRVAETYRKNRDAADTIMKQVLKKRKYYIEEATSYSCAVYIKGVQKLLSVPKSLLGQEVRKTLDLDTNGRGILYQSESLSEYNFQKPNKVREITIANRMAGQNTAFGYKKASDLQANFYQNVFTINGLATRGFVSPVASYGPRFYNYKLLGTSVENGHTIHKIQVIPKRGHGQYFQGDIYIVDGDWRIYSVDLFIENKTSNLNLVDTLKIRQQYVAITDSVWMPASTQYSFKGAVFGFKFGGYYAAVYNNYKINPTFPDNFFTGEILKIDTVANIKKPGYWADARPIPLTAFEDRDYKKKDAFEEYKKTDTYLDSLQHHKNHINYPGYLIFGYAASNKSNRDSLYIFPFIQTFYYNTVEGFGINAKVSYIRTIDDFHSLTITPALRYGFSNKIFSANMGFEYKNDPFHNAKFYADFGSDVLDLNNVGTRSLYFNTLSTLLSENNYVKYYRSHYGDFGYQREVLNGVFLKGGLSYSSRSQLYNTSFSKIKDIKDRQFTSNNPLAPPGTPADDHSFLFPDNQALVFNASATFTFDQRYETRPTGKFNLPSKYPTLTVNYRKGFKNIIGSDVDYDFASVDLSQDHIRVGLSGYSSFKVSGGGFFNNNNLYYMDYNHFLGNQGTTFDPTYVGSFHFLPFYTYSTNGAFLEAHYQHNFAGSLFNHIPLLRKWKLEEIIGANYLTTKNNRNYREFYVGVQRLIFRVDYGISYAGDKKYIQGFRIFYGIR
>NZ_CP043451.1|WP_112652674.1|4692377_4693334_-|rhodanese-related-sulfurtransferase
MKMYNTLLYYCYSTIANAEQFAADHLKFCKSLGLTGRIIVADEGLNGTVSGTVEACKTYMDTVHADERFAGIDFKIDEVDTPSFVKMHVRYKSEIVHSGLRDPNVIDPKQKTGKHLEPKEFLAMKDRDDVVVLDVRSNYEHSLGKFKNAVTLDIENFRDFPAMINELAQYKDKKILTYCTGGIKCEKASALLLHEGFPEVYQLHGGIIKYGKEAGGEDFEGKCYVFDNRLSVDVNSVNPVVISTCLNCGKTTPKMINCANPECNEHFTQCDECGTAMDGCCSDACKEHPRKRVYDGTGYYVKVPQPVNVSKNKLQPIA
>NZ_CP043451.1|WP_112652673.1|4689380_4692275_-|transcriptional-regulator
MRKTLCIIIVLAFISVWPAWSVDIKSVGVPYVQNYTKALYQFGNQNWSVTRDEHDIMYFGNAEGLLTFDGKYWQQYHMPNGLIVRSVSADGKGRVYAGGYGEFGYWHNDGKGILKYTSLISLVPKNFLPVTEEIWKIYCDNNRVLFQSFGAIYIYSAGKIEVVKTHEPYLFLFKCGSRYFAEQLTKGLFELKGSRLEYIEGSNILGASGVLSILPFQQGKYLIGTAKNGLFIYDGKTVKPWVSQANDFLKTYQLNNGAAIADKYFAYGTILNGIVIVDTAGRVVQHINKASGMQNNTVLSLYTDASQNLWAGLDNGIDRIEVNSPLYFYFDKTGKFGTVYSSIIFDKKIYLGTNQGLFYSDWLPDNHNSPFQTFDFKLIPGSQGQVWDLSLQDNRLLCGHNDGTYQVNGASLKKISDVTGGWTIKKMAPDMLMQGTYTGLVIYRKDAAGNWQFSHKLAGFSEPSRYVERDAKGQIWVSHAYKGIYKLTLSADQRTVVSHVYYDQKQGLPGSYNINVFDLDNRTVFSSDLGFYVYDDITDRFYKYQQLNSKLGTFATSSKIIKAIGKKYWFINQGRVGLADMSVTGKLTIDTNRFSILNGQMVQHYETINRINNSTYLISVDDGFVILNDADAQLPNRIKIPDVLIRRIENVTDKVSLITEAAEQSNNIEIPYAENNIRISYSLPYYTQAKIRFQYYLEGYSHQWSEWMPQSQKEFTNLNQGTYNFKVRAKINDQYQSAVSTITFTVLPPWYAGKIALVFYVLLAVLLFYVIRYYYGLKLKKHQQQIQQKLQKEKEEFLKQEAIANEQHIINIKNEQLQADLASKSRELANSAMNIVYKNELLQKISDELTHLKGGDGKKLADEQLRRIQKVIDEGMSDERDWNIFETSFNEAHENFFKKLKAGHPDLVPNDLKLCAYLRMNMSSKEMASLLNISLRGVEIRRYRLRKKLNLEHDKNLTEFLIEL
>NZ_CP043451.1|WP_112652672.1|4686092_4689119_-|TonB-dependent-receptor
MKRIFTISGLMLLLLFSFDAAFAQNVTVKGKITDAATGEALIGVSVQEKGTTNGTQTDVNGLYSIKASKNGILTITYIGYATKSVPVNEQTTLNVTLQAQANELAQVVVVGYGTQRKLDVTGSVASVKGTEISKQASVNPISGLQGKVAGVQITNSGSPGASPAVSIRGLGTVFGNVSPLFVVDGVWYDDISFLNPQDIENISILKDASSTAIYGIRAANGVVLVTTKRGAKGKPVINYNGYAGWQSVTNQVKMANATEYATAINELYTSNNVSPVLFSDPASYGKGTDWYGQILRNAFVTNHELSVSGGTEKVTYHLSFGYLDQDGLAKTNNYRRYTLHLSNDFKPVKGLKLGYTLSGLSGKSADVNGGIFHQLFGVAPTLPVYYKDGAYGDPNDYHTGDGNNYNPQATLDFFNQKSRNMRFTYNGYGEVSFLKNFKFKTSFGGDIGQAEVRGYTPVYAATFAQKSLVSNLDVNHSETRNWIWENTLTYDVKIKDHKITALLGYSAQNYRTKQLDAHAQNVPYVSSGSQRGSFPDTAKVTYYATPGSQVYTRALSQFARVNYSFKDKYLLNASIRRDGASQFYGDHTYGYFPSVGGGWVITNEDFMKDQKVFNTLKLRASWGKVGNSGVPINPSILTVSADPYLTAIFGTPQTTFPGASVNTVVPPTIFWEKTQSTDFGIEGAILNSKLSFEADYYDRKTKDAIYPLPILGSLGTNGGVVLGNQATIQNRGVEFLLSWKDQATKDFYYSISANLGINTNKVLNVLSGNIPIYQGGNGIANGQLATRTVVGQPIGEFYGYQVTGIFQTPQEVAASKQTSAKPGDFKYQDTNNDGVIDSKDRVVLGSPLPKYNYGINTSFTYRNFDLALDFQGTADVSVYNANIAYRFGNENFTKDFFDHRWHGPGTSNTYPSVNVGSTDNAKPNSFYVESGAYFRLRNAQLGYTLSGSILSKWKIQKVRLFANAQNALNFFGYKGFSPEVGGSIGNMGIDANVYPLYATYNFGVNVTF
>NZ_CP043451.1|WP_112652681.1|4700384_4701719_+|cell-envelope-integrity-protein-CreD
MIEEQSPKQTTLGWLRESATFKLIFIGLLALLLLIPSAFVQNLVTERAVRQGETAKEVSESWSASQIIKGPILVIPYKKGINMTDTAKQAPIENLYILPDNLHIKAGLTTQLRHRGIFDVAVYNTQVKVSGNFARLDLSSLGININQLLLNKARFEFSVSDLKGLKSNPVIKTTQPILGAEPSLESVFGNGLQAGVNLSAINNNEIPFDFTLDLKGSEGLSFLQMGKTTDVRVNGNWSSPSFDGNFLPDDAKVDTGGFSASWRMMYYNRPFPQQWTGQQKTLDNDKKLEEATFGVKLRLPVDQYQKTMRTSKYAIFIILLTFISLFLTEVIRKQPIHMFNYILIGAAMVIYYTLLLSFSEQVGYNMAYLIASVSTIALISVFISSLLKNGKAALLFAFILAVFYTFIFVIIQLEDLALMVGSIALFIIIAVLMYFSRKINWDKN
>NZ_CP043451.1|WP_112652682.1|4702052_4703459_+|23S-rRNA-(uracil(1939)-C(5))-methyltransferase-RlmD
MSKANKPKFFENVQIIDIAEEGKGVGKADDFVLFVDKAVPGDVADVQLYRSKKNFGEGKITELKQASEYRTQAFCEHFGTCGGCKWQHMTYEAQLKFKQKSVVDALSRLAKINVEGIMPIVPSPADRYYRNKLEFTFSNKRWLYDGENKEDGTLNMNALGFHIPGRFDKILDVNHCYLQAEPSNSLRNEIRDFTIQQGYTYYDLRNHSGMLRNLVVRTSSTGEIMVIVVFAYAEQSEIDSLMSHIDARFPEITSLLYIVNQKKNDTIFDQDVVAFKGPEYIHEEMNGIKFRIGPKSFYQTNSIQALRLYEITRDFADFKGDELVYDLYTGAGTIANFVAGHVREVVGVEYVPTAIEDAKVNSAINNITNTKFYAGDMKDVLVADFVAEHGKPDVIITDPPRAGMHPDVVARLMEIEAPKIVYVSCNAATQARDLLVLKEKYDTVKIQPVDMFPHTQHVENVVLLLLRD
>NZ_CP043451.1|WP_112652683.1|4703631_4704027_+|hypothetical-protein
MNPEELLNEGNERNKPAAESPLISLERDLKYFNDSIKEIAEEIINEGLSSYPIFIAHQHELSLGELILDRHDLNSEWSIHASTLEEFVERDVIKPVLKERFVNSYKDPYQFMCVFVVVPEGANFVFFPYAK
>NZ_CP043451.1|WP_112652721.1|4704135_4704648_+|phosphoribosyltransferase
MPEKKLLILNKQQIQQKLDRMAYQILEDNFDEDEILIAGILPRGNHIAERLKTILDGIAPFKSRIITIELEKQSSSLSANIDFEVEECSNKVVILVDDVLNSGKTLAYGFGVFLDVPLKKLRTAVLVDRNHKSFPITTDFAGVALSTVIKEHVDVVLDEEDGEEDAVYLR
>NZ_CP043451.1|WP_112652684.1|4704764_4705268_-|shikimate-kinase
MKYFIVGFMGCGKTTWGRKLAAKWGYEFIDLDHVLEAKAGMSIAEYFSSFGEDAFRKLESQVLKETEYAENTVVSTGGGLPCFFDNMDWMNANGKTLYIKLSPKTLADRLENSKTIRPVLQGKKGDELIEFITGKLAEREGFYLQASNIVEGIDMSVEKLEEALGYN
>NZ_CP043451.1|WP_112652685.1|4705278_4706337_-|ABC-transporter-permease
MIPYLLRKLMYGLAVMLGVVFVVFFLFNILPVDPARMTQGQRADVQSLQAVRKEFGLDKPVPVQFAYYLNDLSPLGIHLNTADEQQRYGYVKLFPVSKSKVLALKWPYLRRSYQTRKDVASLLMEVIPNTLVLAAAAMIFAIIIGVFLGVASAVNKDTWIDKLAISFSTLGISAPSFFAGIIIAWTFGFVLSNYTHLNMSGSLYSYDPFKGEVITLKNLVLPVITLGLRPLAIIVQLTRNAMLDVLGQDYIRTAKAKGLSNRTIIYRHALKNAMNPVITAIANWFASLLAGSFFVEYIFGYNGLGKATVDALEMSDFPVVMGSILFIAFIFVVISILVDVIYVWIDPRVKLS
>NZ_CP043451.1|WP_112652686.1|4706341_4707505_-|DoxX-family-protein
MKNTSSNSAVIWIPRLLVGLLFIFSGAIKANDPLGFSYKLVEYFEVFHITFLNGLALTMAIVLCALEMLLGFALLIGARAVKVAWGLLLLIIFFGFLTFYSAFFKVVQTCGCFGDAIPLTPWQSFSKDMVLLALVLVLFVKRKEIKPLFSAKVGDKWLICAAVVSVGFGVYTYNFSPVIDFLPYKIGANLPDEMKIPPGAPLDEFELTYHLKNKKTGATKVMNDKEYLKSNIWKDASWEVVGDPENRLVKKGYEPKIRDLAIQDEQRNDYTKELLSSPFYSLFIVAYDLSETDKDAINRLNALAINLTDNYNIRTVLLTSNSAADAKAFAKEHKLISEIFYADGVPLKSMVRSNPGVLLIKNGTVINKWHYHSVPKYEDIVKEYLQK
>NZ_CP043451.1|WP_090534301.1|4707510_4708002_-|DUF1599-domain-containing-protein
MKKTRDYGTAWRILRPQSITDQIFIKAQRIRTLEEKKISKVGDDITGEYIGIVNYCVIAMMQLECGPEMSTELNPDHVSQMFDEKVNETKELMFAKNHDYGEAWRDMRISSLTDLILMKLLRVKQIEDNQGLTEASEGVKANYQDMLNYAVFALIKLNIHLGK
>NZ_CP043451.1|WP_167516351.1|4708260_4709031_+|dihydropteroate-synthase
MGIINITPDSFFADSRKPGVDEALQQAEKMLTDGATFLDIGAYSSRPGAVDISAQEETDRLLPVVEAIAAQFPEVIMSIDTFRANVAEAAVKGGAHIINDISGGMLDADMFATVARLQVPYILMHMKGTPQTMNQLAKYDDVFGEVFDYFISKYSELKRLGVHDVILDPGFGFAKKAEHSYELMSRMNEFNILGLPVLTGISRKRMIYGLLGNTAEEALNGTTALNTIALTKGTNILRVHDVKEAAEAVQIWEACQ
>NZ_CP043451.1|WP_112652688.1|4709040_4709526_+|GNAT-family-N-acetyltransferase
MEILPATTNDIDEITNVEIRSKMASFPSLVEPHDIDFETRQYRWKTWFAAQSPATSKPQRVLFKAVADNSIIGYIAVHLTTRYEKDAEIQSFYVLKEYQRKGIGTGLLLNAVNWLETQHTKSLCVGIAKNTPYRAFYIKYGGGHLNEHWICWEDVAAIIMS

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Crispr_ID: NZ_CP043451_8

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP043451_8

4977262-4977360

Orphan

Consensus_repeat	Method
AGATATGAGACGTGAGATTTGAGAT	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP043451_8

>merge|NZ_CP043451|8|4977262-4977360|CRISPRCasFinder
AAAAAATAGATATGAGACGTGAGATTTGAGATATGAGATTTTTTTCTCTAACTTGAATACTCGCTTCTTCAAAGAGATATGAGACGTGAGATATGAGAT

>NZ_CP043451|8|8|4977262-4977360|CRISPRCasFinder
AAAAAATAGATATGAGACGTGAGAT	TTGAGATATGAGATTTTTTTCTCTAACTTGAATACTCGCTTCTTCAAAG
AGATATGAGACGTGAGATATGAGAT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP043451.1\|WP_112651386.1\|4985950_4986430_+\|DinB-family-protein	unknown	unknown	gnl\|CDD\|378981
NZ_CP043451.1\|WP_112656080.1\|4973304_4973691_+\|GxxExxY-protein	unknown	unknown	gnl\|CDD\|275083
NZ_CP043451.1\|WP_112651382.1\|4983042_4984068_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043451.1\|WP_091174116.1\|4968014_4969751_+\|biosynthetic-type-acetolactate-synthase-large-subunit	unknown	unknown	gnl\|CDD\|272915
NZ_CP043451.1\|WP_112651390.1\|4987772_4989281_-\|FAD-binding-protein	unknown	unknown	gnl\|CDD\|130740
NZ_CP043451.1\|WP_112651384.1\|4984078_4985800_-\|glycosyltransferase-family-39-protein	unknown	unknown	gnl\|CDD\|379080
NZ_CP043451.1\|WP_112656086.1\|4974457_4975255_+\|methyltransferase-domain-containing-protein	unknown	unknown	gnl\|CDD\|181382
NZ_CP043451.1\|WP_112656070.1\|4980037_4981060_+\|proline-iminopeptidase-family-hydrolase	unknown	unknown	gnl\|CDD\|188121
NZ_CP043451.1\|WP_091174059.1\|4965464_4965716_+\|ATP-synthase-F1-subunit-epsilon	unknown	unknown	gnl\|CDD\|213395
NZ_CP043451.1\|WP_090530083.1\|4969772_4970375_+\|acetolactate-synthase-small-subunit	unknown	unknown	gnl\|CDD\|183365
NZ_CP043451.1\|WP_146750324.1\|4986426_4987695_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043451.1\|WP_090531289.1\|4970611_4971670_+\|ketol-acid-reductoisomerase	unknown	unknown	gnl\|CDD\|273093
NZ_CP043451.1\|WP_112656072.1\|4978646_4979897_+\|threonine-ammonia-lyase-IlvA	unknown	unknown	gnl\|CDD\|236318
NZ_CP043451.1\|WP_112656078.1\|4973779_4974370_+\|3-isopropylmalate-dehydratase-small-subunit	unknown	unknown	gnl\|CDD\|179314
NZ_CP043451.1\|WP_112656084.1\|4975312_4976383_+\|3-isopropylmalate-dehydrogenase	unknown	unknown	gnl\|CDD\|234832
NZ_CP043451.1\|WP_112656068.1\|4981114_4981954_+\|DUF2911-domain-containing-protein	unknown	unknown	gnl\|CDD\|378565
NZ_CP043451.1\|WP_112656074.1\|4977477_4978644_+\|2-isopropylmalate-synthase	unknown	unknown	gnl\|CDD\|234864
NZ_CP043451.1\|WP_112651380.1\|4982175_4982901_-\|DUF2490-domain-containing-protein	unknown	unknown	gnl\|CDD\|378471
NZ_CP043451.1\|WP_090531285.1\|4966199_4967876_+\|dihydroxy-acid-dehydratase	unknown	unknown	gnl\|CDD\|234861
NZ_CP043451.1\|WP_112656082.1\|4971833_4973261_+\|3-isopropylmalate-dehydratase-large-subunit	unknown	unknown	gnl\|CDD\|235490

Protein	Function_ID	Function_description	E-value
NZ_CP043451.1\|WP_112651386.1\|4985950_4986430_+\|DinB-family-protein	gnl\|CDD\|378981	pfam12867, DinB_2, DinB superfamily. The DinB family are an uncharacterized family of potential enzymes. The structure of these proteins is composed of a four helix bundle.	1.50179e-16
NZ_CP043451.1\|WP_112656080.1\|4973304_4973691_+\|GxxExxY-protein	gnl\|CDD\|275083	TIGR04256, conserved_hypothetical_protein, GxxExxY protein. Members of this protein family average about 130 residues in length and include an almost perfectly conserved motif GxxExxY. Members occur in a wide range of prokaryotes, including Proteobacteria, Perrucomicrobia, Cyanobacteria, Bacteriodetes, Archaea, etc.	4.45715e-47
NZ_CP043451.1\|WP_091174116.1\|4968014_4969751_+\|biosynthetic-type-acetolactate-synthase-large-subunit	gnl\|CDD\|272915	TIGR00118, Probable_acetolactate_synthase_large_subunit, acetolactate synthase, large subunit, biosynthetic type. Two groups of proteins form acetolactate from two molecules of pyruvate. The type of acetolactate synthase described in this model also catalyzes the formation of acetohydroxybutyrate from pyruvate and 2-oxobutyrate, an early step in the branched chain amino acid biosynthesis; it is therefore also termed acetohydroxyacid synthase. In bacteria, this catalytic chain is associated with a smaller regulatory chain in an alpha2/beta2 heterotetramer. Acetolactate synthase is a thiamine pyrophosphate enzyme. In this type, FAD and Mg++ are also found. Several isozymes of this enzyme are found in E. coli K12, one of which contains a frameshift in the large subunit gene and is not expressed. [Amino acid biosynthesis, Pyruvate family].	0
NZ_CP043451.1\|WP_112651390.1\|4987772_4989281_-\|FAD-binding-protein	gnl\|CDD\|130740	TIGR01679, bact_FAD_ox, FAD-linked oxidoreductase. This model represents a family of bacterial oxidoreductases with covalently linked FAD, closely related to two different eukaryotic oxidases, L-gulonolactone oxidase (EC 1.1.3.8) from rat and D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) from Saccharomyces cerevisiae.	3.69833e-16
NZ_CP043451.1\|WP_112651384.1\|4984078_4985800_-\|glycosyltransferase-family-39-protein	gnl\|CDD\|379080	pfam13231, PMT_2, Dolichyl-phosphate-mannose-protein mannosyltransferase. This family contains members that are not captured by pfam02366.	1.04848e-19
NZ_CP043451.1\|WP_112656086.1\|4974457_4975255_+\|methyltransferase-domain-containing-protein	gnl\|CDD\|181382	PRK08317, PRK08317, hypothetical protein; Provisional.	2.51473e-27
NZ_CP043451.1\|WP_112656070.1\|4980037_4981060_+\|proline-iminopeptidase-family-hydrolase	gnl\|CDD\|188121	TIGR01250, Proline_iminopeptidase, proline-specific peptidase, Bacillus coagulans-type subfamily. This model describes a subfamily of the alpha/beta fold family of hydrolases. Characterized members include prolinases (Pro-Xaa dipeptidase, EC 3.4.13.8), prolyl aminopeptidases (EC 3.4.11.5), and a leucyl aminopeptidase.	3.37384e-104
NZ_CP043451.1\|WP_091174059.1\|4965464_4965716_+\|ATP-synthase-F1-subunit-epsilon	gnl\|CDD\|213395	cd12152, F1-ATPase_delta, mitochondrial ATP synthase delta subunit. The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The extrinisic membrane domain, F1, is composed of alpha, beta, gamma, delta, and epsilon subunits with a stoichiometry of 3:3:1:1:1. Alpha and beta subunit form the globular catalytic moiety, a hexameric ring of alternating subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton translocating domain. In bacteria, which is lacking a eukaryotic epsilon subunit homolog, this subunit is called the epsilon subunit.	9.60373e-27
NZ_CP043451.1\|WP_090530083.1\|4969772_4970375_+\|acetolactate-synthase-small-subunit	gnl\|CDD\|183365	PRK11895, ilvH, acetolactate synthase 3 regulatory subunit; Reviewed.	3.31894e-26
NZ_CP043451.1\|WP_090531289.1\|4970611_4971670_+\|ketol-acid-reductoisomerase	gnl\|CDD\|273093	TIGR00465, Ketol-acid_reductoisomerase, ketol-acid reductoisomerase. This is the second enzyme in the parallel isoleucine-valine biosynthetic pathway [Amino acid biosynthesis, Pyruvate family].	4.25606e-109
NZ_CP043451.1\|WP_112656072.1\|4978646_4979897_+\|threonine-ammonia-lyase-IlvA	gnl\|CDD\|236318	PRK08639, PRK08639, threonine dehydratase; Validated.	0
NZ_CP043451.1\|WP_112656078.1\|4973779_4974370_+\|3-isopropylmalate-dehydratase-small-subunit	gnl\|CDD\|179314	PRK01641, leuD, 3-isopropylmalate dehydratase small subunit.	3.23024e-94
NZ_CP043451.1\|WP_112656084.1\|4975312_4976383_+\|3-isopropylmalate-dehydrogenase	gnl\|CDD\|234832	PRK00772, PRK00772, 3-isopropylmalate dehydrogenase; Provisional.	0
NZ_CP043451.1\|WP_112656068.1\|4981114_4981954_+\|DUF2911-domain-containing-protein	gnl\|CDD\|378565	pfam11138, DUF2911, Protein of unknown function (DUF2911). This bacterial family of proteins has no known function.	3.18426e-66
NZ_CP043451.1\|WP_112656074.1\|4977477_4978644_+\|2-isopropylmalate-synthase	gnl\|CDD\|234864	PRK00915, PRK00915, 2-isopropylmalate synthase; Validated.	0
NZ_CP043451.1\|WP_112651380.1\|4982175_4982901_-\|DUF2490-domain-containing-protein	gnl\|CDD\|378471	pfam10677, DUF2490, Protein of unknown function (DUF2490). This is a bacterial family of uncharacterized proteins. They appear to belong to the outer membrane beta barrel superfamily.	1.53877e-42
NZ_CP043451.1\|WP_090531285.1\|4966199_4967876_+\|dihydroxy-acid-dehydratase	gnl\|CDD\|234861	PRK00911, PRK00911, dihydroxy-acid dehydratase; Provisional.	0
NZ_CP043451.1\|WP_112656082.1\|4971833_4973261_+\|3-isopropylmalate-dehydratase-large-subunit	gnl\|CDD\|235490	PRK05478, PRK05478, 3-isopropylmalate dehydratase large subunit.	0

>NZ_CP043451.1|WP_112656084.1|4975312_4976383_+|3-isopropylmalate-dehydrogenase
MKKYILVIPGDGIGPEVTTWGKAVLEKIGRDFGHEFTFDEALMGHAGIEATGNPLPDETLAKAKASDAILFGAIGHIKYDNDPSAKVRPEQGLLKIRKELGLYANLRPIMLFDELLDASSLKPEILKGTDILFFRELTGDVYFGEKKRSEDRNTASDLMIYSRYEVERIAIKAYEAARVRGKRLCSVDKANVLEASRLWREVVQEIAKKYPDVETEHMFIDNAAMQLVKNPKKFDVVLTANLFGDILTDEASQIAGSMGMLASASVGDGTGFFEPIHGSAHDIAGQDKANPLASILSVALMLEISFGLKEEAKKITDAIDKALKDGYRTGDIADANTDKVKILGTTAMGQKVLEYL
>NZ_CP043451.1|WP_112656086.1|4974457_4975255_+|methyltransferase-domain-containing-protein
MNQQKHIQREGKGTAKLFDERSLANDYATLAPLLRPGLKVLDVGCGTGAISKDIAALIGESGHVTGIDNTEYFIQSGKETYASVQNMELIYTDLFSFDPEEKYDLIVSARVLQWLSNPVEALKKMYSLLKPGGTVSILDYNHEALQWQPQPPASMQRFYATFLRWRGDAGMNNHIAEDLPEYLQEAGFENIEVFNADEVYQKGEYNFEGKAGIWAKVAQSKQMVEEGYIDDESRLLAIDEYTNWVENEAEQMVMKLKEVRGVKPE
>NZ_CP043451.1|WP_112656078.1|4973779_4974370_+|3-isopropylmalate-dehydratase-small-subunit
MATKIFKHVQTSVVPLPIENIDTDQIIPARFLKATTRDGFGNNLFRDWRFDENDNPKADFVLNHPTFSGKVLVAGKNFGCGSSREHAAWAISDYGFDAVVSSFFADIFKGNALNNGLLPVQVSDDFLKKIFDAVYADHKAEVEIDLESQTITISSTGEKESFEINPYKKACLINGYDDIDYILSQQGKIEEFELAR
>NZ_CP043451.1|WP_112656080.1|4973304_4973691_+|GxxExxY-protein
MEKDRLTYDIIGCAMRVRNTLGNGFQEVIYQKCLAIELEKAGISFVRELEHPIFYDGIEVGKRRADFVIEGKLSVEIKALINLEDVHLAQAKNYTVAYDFPIGLLINFGSQSLQYKLIFNPKYNIKLN
>NZ_CP043451.1|WP_112656082.1|4971833_4973261_+|3-isopropylmalate-dehydratase-large-subunit
MGQTLFDKIWDAHVVSSSEGFPDILYIDTHFIHEVTSPQAFDGLRQRGLPVFRPKQTVATADHNVPTIDQHLPIKEELSRYQVDMLTKNCKEFGVELYGLGHPYQGIVHVIGPELGITRPGGTYVCGDSHTSTHGAFGAIAFGIGTSQVEQVLATQCLLQSRPKRMKIEVNGKLQKGVGAKDIILYIIAQISAAGGTGYAVEYAGDTIRSLSMEGRMTICNMSIEMGARCGLIAPDETTINYVKGREFAPKGKEWDKAVAYWKTLYSDADASFDEVLYFKAEDIEPMITYGTNPGMGIGVTQHVPETASFEAKEQGSYKKALDYMGLHDDETLLGKPIDYVFIGSCTNSRIEDLRQVAEFVKGKHKADNVTVWVVPGSKQVQQQAIAEGLDKIFDAAGFPLREPGCSACLGMNEDKIPAGKYCVSTSNRNFEGRQGPNSRTFLASPLTAAASAITGVVTDIREMLSESEFSELKN
>NZ_CP043451.1|WP_090531289.1|4970611_4971670_+|ketol-acid-reductoisomerase
MAKLNFGGTEENVVTREEFPLSKAQEVLKDEVVAVIGYGVQGPGQALNQKDNGINVIVGQRKGTKTWDKAISDGFVPGETLFEIEEALQRGTVICYLLSDAAQIALWPTVKKHLTPGKALYFSHGFGITFNEQTGIVPPADVDVFLVAPKGSGTSLRRMFLQGRGLNSSYAIFQDATGKAFDRVIALGIAVGSGYLFETNFKKEVYSDLTGERGTLMGCVQGIFAAQYDVLRSHGHSPSEAFNETVEELTQSLMPLVAENGMDWMYANCSTTAQRGALDWWKKFRDATKPVFEELYESVATGKESQRSIDSNSQPDYREKLDAELKELRESELWQAGKTVRSLRPENQVVEA
>NZ_CP043451.1|WP_090530083.1|4969772_4970375_+|acetolactate-synthase-small-subunit
MSEAEKKQEFNITIYTENQIGLLSRIAIIFTRRKINIDSLNTSPSEIESIHRFNIVINEYEEVVRKLTRQIEKQVEVLKAYYHTNEDVIWQELALYKVSTDVIAEKVSVERLLRENGARAVVIRKDYTVFETTGHREETDNLINILQPYGLIEFVRSARVAIIKDSEGFNSKLREFERLEPGEEVIENEYLNQGEKVFTM
>NZ_CP043451.1|WP_091174116.1|4968014_4969751_+|biosynthetic-type-acetolactate-synthase-large-subunit
METAQETLTAPAATETVNVSGSVALLEALIAEGTDTIFGYPGGAIMPIYDALFDYNDKLNHILVRHEQGGIHAGQGYARTSGKVGVVFATSGPGATNLVTGLADAQIDSTPLVCITGQVFAHLLGTDAFQETDVINITTPVTKWNYQVTDATEIPEVIAKAFYIARSGRPGPVLIDITKNAQIQLFDFAGYKPCDHIRSYRPKPIVRPQYIEQAAELINSAKKPFILFGQGVILGGAEQEFKAFVEKSGIPAAWTVLGAGAIPSDHPLNVGMLGMHGNYGPNVLTNECDVLIAIGMRFDDRVTGRLDKYAKQAKVVHLDIDPAEIDKNVKSTVPVWGDCKETLPLLTKAIEKKEHTEWLAKFNDYTRQEVEAVIHNELNPTTPEMTMGEVIKQLNEITKGEAVIVTDVGQHQMVACRYAKFNNTRSNVTSGGLGTMGFALPAAIGAKFGAQDRTVVAIIGDGGFQMTCQELGTIMQSGIDVKIIILNNRFLGMVRQWQELFNQRRYSFVDIQSPDFVALAAAYRIPGKLVDDRADLTAALNEMLTAPGSFLLEIMVTKENNVFPMVPQGCSVSEIRLK
>NZ_CP043451.1|WP_090531285.1|4966199_4967876_+|dihydroxy-acid-dehydratase
MELNKYSKTFTQDPTQPAAQAMLYGIGLTDDDMRKAQVGVASMGYDGNTCNMHLNDLAKLVKQGIWDEDMVGLIFHTIGVSDGMSNGTEGMRYSLVSRDIIADSIEAVTGAQYYDGLITLPGCDKNMPGSIMAMGRLNRPSIMVYGGTIKPGHWKGEDLNIVSAFEALGKKIAGQIDDVDFMGVIKNACPSAGACGGIYTANTMAAAIEALGMSLPYSSSNPALSAEKKAECLAAGKAIKVLLEKDIKPSDIMTREAFENAIVVIMVLGGSTNAVLHLIAMAKSVDVKLTQDDFQAVSNRIPVLADMKPSGKYMMEDLHNIGGVPAVMKYCLEQGWLHGDCLTVTGKTIAENLAEIPALEFETQKIIKPKENPIKATGHLQILYGNLAEGGSVAKITGKEGERFTGPARVFDGEFELIAGIQSGRVKKGDVVVIRNVGPKGAPGMPEMLKPTSAIFGAGLGSSVALITDGRFSGGTHGFVVGHITPEAYDGGFIAMVKDDDIINIDAVANTINVSLPQEEIAARRAAWQKPALKVTKGVLYRYAKNVTTAAEGCVTDE
>NZ_CP043451.1|WP_091174059.1|4965464_4965716_+|ATP-synthase-F1-subunit-epsilon
MTLEILTPDKKVYEGEATSVTLPGALGLFEILNNHAPIISTLQDGKLTVRGGAAKEEVFFIKGGVVEALNNKVTVLAEGIQHK
>NZ_CP043451.1|WP_112656074.1|4977477_4978644_+|2-isopropylmalate-synthase
MLHDPNRVYVFDTTLRDGEQVPGCQLTTPEKIEIAKELELLGVDIIEAGFPVSSPGDFQSVVEISKAVKEPTVCALTRANKGDIDAAVASLQYAKRPRIHTGIGSSDMHIKHKFNSTREEILERAVEAVKYAKKSVEDIEFYAEDAGRADVVYLAQMVEAVIAAGATVVNIPDTNGYCLPDQYGSKIKFLKENVKNIDKAIISVHCHNDLGLATANSIAGLQNGARQIEGTINGIGERAGNTSIEEVVMILKTHHTLGLHTNIDSKRFYELSQMIRTQMRMPVQPNKAIVGANAFAHSSGIHQDGFLKMRENYEIIRPEDVGFPSATIVLTARSGRHALKFHLERLGYTLDKEELGFVYNNFLTLADSKLDINDQDLQSLMAHRLVKN
>NZ_CP043451.1|WP_112656072.1|4978646_4979897_+|threonine-ammonia-lyase-IlvA
METDTKSQLNFEAAYQRIKDVVKRTPLQYNAGLSAKYECEVYLKREDLQVVRSYKLRGAYNMISQLNDDELSRGVVCASAGNHAQGVAFSCNKKNIKGVIFMPEITPKQKVKQTAMFGNGNIEIVLTGDTFDDCLAEALAYTEKNQMTFIPPFDDYRVIEGQGTVGVEILQDLPDIEVAIMPIGGGGFASGTGTYLKNNVPNIHLIGVEPEGAPSMLGAINHGKPITLDEIDRFVDGAAVKRVGALTYDICKDILDDMLLVPEGKICTTILKLYNEDAIVVEPAGALSVAALDACKEQIKGKKVVCIISGGNNDIARMQEIKEKSLLYEGLKHYFIVRFPQRPGALKLFVNSVLGPGDDITRFEFIKKNEKENGPALVGIELKNAEDYPALLQRMHAHRFNVIELNKDQTLFEYLV
>NZ_CP043451.1|WP_112656070.1|4980037_4981060_+|proline-iminopeptidase-family-hydrolase
MKKLFFILIAACFCACKNPSKPAADTATESSNTPYEIKTGGNKLIKVAGKYNVWTKKVGDGKIKVLLLHGGPGFSHDYMECFEDFLPKEGIEFYYYDQLGCGNSDAPADTSLWNIPRYVEEVEEVRKGLGLDNFYILGHSWGGMLAMEYLHKYQSHVKGAVLSNMTAGIKGYVAYAAELKKKFFTPRDITVFDSLDRLKQYDSPQYNDLLMNKLYTQVICRLPLENWPEPLWRAFKKANHTIYIQMQGVDEFHVTGNFKGWEFWDKLQNIKTPTLVLGGVHDEMNPEDMKKEGRLLPNSRTYLCPNGSHMSMYDDQQNYFKNLIAFLKDVDAGTFNADKK
>NZ_CP043451.1|WP_112656068.1|4981114_4981954_+|DUF2911-domain-containing-protein
MKKLFTCIITTMIFTAVNVYAQLTPQPSSTQSIVQDFGLGKISLVYSRPDVRSRKIFGGMEPYGKVWRTGANSATVIKFTDEVSMEGNKIPAGEYGLFSIPGENEWTIILSKQPKQWGAYNYKEADDFLRFKVKTEHLKALTETMTLAFSNVTATTCDLQMMWEHSGFTIHMTTDIDVKVMARIDSAMNTDKKPYYEALIYYYNNNKDMDKALAWATELEKDKNFPPFVPKLWKARILLKKGDKAAAIATAQEGVKMATDMKTDEYVRLNNELIAQAKK
>NZ_CP043451.1|WP_112651380.1|4982175_4982901_-|DUF2490-domain-containing-protein
MQLKKQLLIFAVLLLAAPARLLAQDNQFSGWAAIFHSQKLSEHWGYSFDGQLRSHDEVSYLKHILLRPSVNYYFAKNKVGALGYAYIATYGRTPSNETTFRPEHRIWQQYTYTHKLTKHVQLAHRFRLEQRFLGNTADNKNDRYFAQRFRYFARAVIPMKPDSDVFTEGTFVALQNEAFVNVQNKNKVNKHFFDQNRAYVAVGYRFSKSFDAEAGYLNQYIKQADAYVVNHVAQLAFYTRF
>NZ_CP043451.1|WP_112651382.1|4983042_4984068_-|hypothetical-protein
MFKRIYLFVFFSIITATAALAQGSLDIHFNGLGFMDNREYKDFVARSRTYSGVRTTLDLGLNVDSLNHFIVGVNGIHEFGAKPYFLKVNPVAYYSFTGKNWLFNAGAFPREGLLDDYPRALLNDTLRYYRPNVEGLLTRFHNAHFTETAWIDWVSRQTVTDREQFLFGFSGKYRPSLTGPFYVSHYFLLMHDAGAEVLLPNDHIQDNGGGQIRLGLDLSHKTILDSLSIEAGGMMSFERVRGVDGFHKPAGFVANAYLSWKRFALFDEFYKGQGSHIIYGDAFFEKKTYNRLDIIYTPFLYKRVKGQFILSLHQTPGYSSNQEAFRVTVDLGRQTLVRFKD
>NZ_CP043451.1|WP_112651384.1|4984078_4985800_-|glycosyltransferase-family-39-protein
MQDTSLNSAPVKYNKPIIYFLLLWALLNAVQAFTLEIHADEAYYWVYSRFLDWGYYDHPPMVAVFIKAGYSLIHNEFGARLFTVISTTASLYLMWMMLKRYRVDAINFILVISGIFVFHIYGFTTTPDAPLLFFTVLFLYFYQQYIEEDSLKLAIILGVVIACLLYSKYHGILLVAFTLVSNIKLLRRGAFYGIVLLALALYAPHILWQVNHDYPSISYHLSERSADDYQLDNTYLYPLGQLIMAGPLIGWFLFYKGFTTKIQDVFTRTLLVNSIGILAFFFLTSFKGEVQLHWTLIAYVPLSMLVLINFARPGGKPVWFNRLAVINVSLILLVRICIIWGPPFLLKIDAMKSFFGFKDWAHQIKQKAGDNYVIFYEGFQDPSKYNFYNNTTRGLAYDSRHYRRTQYDIWPIEDSLQHKKTYYVLDVWLPGVTTDSINVFAGKWYGGWVNDTRTYQRVEFETKAHKETVSPGQKIDFDLTLKNPYPFAIDFSNKNQKHPVFFEACFFKKTDQISNQNADDSFYNIALKPGESTHFKFNVTAPEQPGRYQLIFSLRTEPFFGGRNSKSINITVK
>NZ_CP043451.1|WP_112651386.1|4985950_4986430_+|DinB-family-protein
MKQEFEVIKKPRLMLLNVVKDLSPEQLNHIPAGFNNNLIWNLAHMISGQQGICYTRAGVPIVVDDKYYTPYRPETKPQSFINADDIAEVKELLISTIDKMEEDYQTRIFSNYQPMTTRYGVTLSNIEEAIRFLPFHDGLHTGYIMALKRAVLEEMSKLV
>NZ_CP043451.1|WP_146750324.1|4986426_4987695_-|hypothetical-protein
MQSKAQTTTQIINEIKAINSKVTNYSNSTGHGMLISNKSMNIFLSNKVSSYLSGNEDLSLYKNYVNINAEEGMISINHNFHQPVDSDDWVRSFVVAGARVNIANAYSAKSANRYYDNQLGFTIQKTWMGKPRTYYAANGDFKKEMDAARALIVNTIAQSINKKAEEFEQSLNALKQEEVPGQNLNEVKSKLRKTFYASLRADYLQQFSEQQSELLVNTGSYDLIADNWTSLGVYIPVIPQKFMVSNDVKAQVNRYYNYPLELFVSHTRFWESPKLGRFFLTFASKGFVNNAVQSGSLFSADVTGAQGADGINIVTINKGDRYIGQYKNFITPVAAGKLVYIPGTSHVGISFRIEKNWGTYKALNSIIGIPIVLIDKKGVPTINFEAQLLLQDMNNSLKNTRLPYNKTAIGLTVGIPFSKIVY
>NZ_CP043451.1|WP_112651390.1|4987772_4989281_-|FAD-binding-protein
MKVIKTGVSSWENRHETFSEQIKDLYELGNEDNLDALEGYNDATKGLQNLIKEAIETGTPLRSLGAGWSWTKIATVKDGVMLDTKPLNTRFTVADTAVNPAYAGNKDHLLFAQSGNGIWELGAFLKNRGLSLKTSGASNRQTIAGAVSTGTHGSAFDFGATPDFVVGLHIVVSPDRHIWLERASAPVVAQRFVDLLQTELVQDDELFNAALVSFGSFGIIHGVLMETEPLFLLETYVQRLPYDTELQGMMATLDFSDTDKLPCSNERPFHFSVLLNPYDLDKGAFVTTMYKRPYRTNYQPPVDNAAGIGPGDDAASFIGTITDAVPALVPVVVTKVLNISMTTNTDPHFGTLGEIFSNTTLRGKLLSSAIGFPAELSPRVADLMLKINKDIGPFSGVFSFRFVKQTKATLGFTRFVHTCIMELDAPLSDKAYNFYSQVWLMLEHENIPFTFHWGKANEITPQRIQRMYGDAATRWINARKTMLNADCQKVFTNQITQQWGLA

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Crispr_ID: NZ_CP043451_9

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP043451_9

6146641-6146799

Unclear

Consensus_repeat	Method
AGTTGCCGTGTCCCCACGGCAACA	CRISPRCasFinder

2 spacers

cas3

The CRISPR arrays of NZ_CP043451_9

>merge|NZ_CP043451|9|6146641-6146799|CRISPRCasFinder
AGTTGTCGTGAGGACACGACAACCGGGGAGGGGGAAAAGGCATGGAAAGTTCTACCCAGTTGCCGTGTCCCCACGGCAACATCTACCTTTCTTCCCCCGCGTTGAACATATACTTTGGATAACCTCGGTAAAAAAAGTTGCCATGTCCCCACGGCAACA

>NZ_CP043451|9|9|6146641-6146799|CRISPRCasFinder
AGTTGTCGTGAGGACACGACAACC	GGGGAGGGGGAAAAGGCATGGAAAGTTCTACCC
AGTTGCCGTGTCCCCACGGCAACA	TCTACCTTTCTTCCCCCGCGTTGAACATATACTTTGGATAACCTCGGTAAAAAA
AGTTGCCATGTCCCCACGGCAACA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP043451.1\|WP_112656411.1\|6148131_6148632_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|274948
NZ_CP043451.1\|WP_112656407.1\|6149434_6150667_+\|insulinase-family-protein	unknown	unknown	gnl\|CDD\|223685
NZ_CP043451.1\|WP_112656413.1\|6147534_6148035_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043451.1\|WP_112656417.1\|6143221_6146569_+\|transcription-repair-coupling-factor	cas3	cd09639_cas3_CAS-I	gnl\|CDD\|224118
NZ_CP043451.1\|WP_090533497.1\|6139104_6140376_+\|serine--tRNA-ligase	unknown	unknown	gnl\|CDD\|235461
NZ_CP043451.1\|WP_112568308.1\|6150684_6151257_+\|peptide-deformylase	unknown	unknown	gnl\|CDD\|234668
NZ_CP043451.1\|WP_112656423.1\|6138256_6138985_-\|16S-rRNA-(cytidine(1402)-2'-O)-methyltransferase	unknown	unknown	gnl\|CDD\|381175
NZ_CP043451.1\|WP_112656409.1\|6148747_6149287_-\|hypoxanthine-phosphoribosyltransferase	unknown	unknown	gnl\|CDD\|223707
NZ_CP043451.1\|WP_112656429.1\|6135018_6135768_+\|glucose-1-dehydrogenase	unknown	unknown	gnl\|CDD\|187620
NZ_CP043451.1\|WP_167516287.1\|6154799_6155507_-\|thiosulfate-reductase	unknown	unknown	gnl\|CDD\|226602
NZ_CP043451.1\|WP_112656534.1\|6140462_6141404_-\|nitrilase	unknown	unknown	gnl\|CDD\|143609
NZ_CP043451.1\|WP_090533817.1\|6151451_6152336_+\|sugar-phosphate-isomerase/epimerase	unknown	unknown	gnl\|CDD\|224007
NZ_CP043451.1\|WP_091176158.1\|6142353_6142608_-\|DUF2752-domain-containing-protein	unknown	unknown	gnl\|CDD\|378499
NZ_CP043451.1\|WP_112656419.1\|6142654_6143065_-\|DUF4199-domain-containing-protein	unknown	unknown	gnl\|CDD\|379395
NZ_CP043451.1\|WP_112656427.1\|6135868_6136450_+\|TetR/AcrR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224228
NZ_CP043451.1\|WP_112656415.1\|6146814_6147336_-\|transposase	unknown	unknown	unknown
NZ_CP043451.1\|WP_112656421.1\|6141475_6142285_-\|AraC-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|378964
NZ_CP043451.1\|WP_112656403.1\|6154015_6154825_-\|molybdopterin-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|224952
NZ_CP043451.1\|WP_112656405.1\|6152593_6153961_-\|MFS-transporter	unknown	unknown	gnl\|CDD\|225121
NZ_CP043451.1\|WP_112656425.1\|6136469_6138104_-\|apolipoprotein-N-acyltransferase	unknown	unknown	gnl\|CDD\|143595

Protein	Function_ID	Function_description	E-value
NZ_CP043451.1\|WP_112656411.1\|6148131_6148632_-\|hypothetical-protein	gnl\|CDD\|274948	TIGR04056, OMP_RagA_SusC, TonB-linked outer membrane protein, SusC/RagA family. This model describes a distinctive clade among the TonB-linked outer membrane proteins (OMP). Members of this family are restricted to the Bacteriodetes lineage (except for Gemmatimonas aurantiaca T-27 from the novel phylum Gemmatimonadetes) and occur in high copy numbers, with over 100 members from Bacteroides thetaiotaomicron VPI-5482 alone. Published descriptions of members of this family are available for RagA from Porphyromonas gingivalis, SusC from Bacteroides thetaiotaomicron, and OmpW from Bacteroides caccae. Members form pairs with members of the SusD/RagB family (pfam07980). Transporter complexes including these outer membrane proteins are likely to import large degradation products of proteins (e.g. RagA) or carbohydrates (e.g. SusC) as nutrients, rather than siderophores. [Transport and binding proteins, Unknown substrate].	1.6578e-05
NZ_CP043451.1\|WP_112656407.1\|6149434_6150667_+\|insulinase-family-protein	gnl\|CDD\|223685	COG0612, PqqL, Predicted Zn-dependent peptidases [General function prediction only].	1.40158e-89
NZ_CP043451.1\|WP_112656417.1\|6143221_6146569_+\|transcription-repair-coupling-factor	gnl\|CDD\|224118	COG1197, Mfd, Transcription-repair coupling factor (superfamily II helicase) [DNA replication, recombination, and repair / Transcription].	0
NZ_CP043451.1\|WP_090533497.1\|6139104_6140376_+\|serine--tRNA-ligase	gnl\|CDD\|235461	PRK05431, PRK05431, seryl-tRNA synthetase; Provisional.	0
NZ_CP043451.1\|WP_112568308.1\|6150684_6151257_+\|peptide-deformylase	gnl\|CDD\|234668	PRK00150, def, peptide deformylase; Reviewed.	1.80852e-71
NZ_CP043451.1\|WP_112656423.1\|6138256_6138985_-\|16S-rRNA-(cytidine(1402)-2'-O)-methyltransferase	gnl\|CDD\|381175	cd11648, RsmI, Ribosomal RNA small subunit methyltransferase I (RsmI), also known as rRNA (cytidine-2'-O-)-methyltransferase. RsmI is an S-AdoMet (S-adenosyl-L-methionine or SAM)-dependent methyltransferase responsible for the 2'-O-methylation of cytidine 1402 (C1402) at the P site of bacterial 16S rRNA. Another S-AdoMet-dependent methyltransferase, RsmH (not included in this family), is responsible for N4-methylation at C1402. These methylation reactions may occur at a late step during 30S assembly in the cell. The dimethyl modification is believed to be conserved in bacteria, may play a role in fine-tuning the shape and functions of the P-site to increase the translation fidelity, and has been shown for Staphylococcus aureus, to contribute to virulence in host animals by conferring resistance to oxidative stress.	7.44542e-126
NZ_CP043451.1\|WP_112656409.1\|6148747_6149287_-\|hypoxanthine-phosphoribosyltransferase	gnl\|CDD\|223707	COG0634, Hpt, Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism].	1.72766e-62
NZ_CP043451.1\|WP_112656429.1\|6135018_6135768_+\|glucose-1-dehydrogenase	gnl\|CDD\|187620	cd05362, THN_reductase-like_SDR_c, tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs. 1,3,6,8-tetrahydroxynaphthalene reductase (4HNR) of Magnaporthe grisea and the related 1,3,8-trihydroxynaphthalene reductase (3HNR) are typical members of the SDR family containing the canonical glycine rich NAD(P)-binding site and active site tetrad, and function in fungal melanin biosynthesis. This subgroup also includes an SDR from Norway spruce that may function to protect against both biotic and abitoic stress. 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.	3.62212e-94
NZ_CP043451.1\|WP_167516287.1\|6154799_6155507_-\|thiosulfate-reductase	gnl\|CDD\|226602	COG4117, COG4117, Thiosulfate reductase cytochrome B subunit (membrane anchoring protein) [Energy production and conversion].	1.97813e-26
NZ_CP043451.1\|WP_112656534.1\|6140462_6141404_-\|nitrilase	gnl\|CDD\|143609	cd07585, nitrilase_7, Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases). The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.	4.09832e-120
NZ_CP043451.1\|WP_090533817.1\|6151451_6152336_+\|sugar-phosphate-isomerase/epimerase	gnl\|CDD\|224007	COG1082, IolE, Sugar phosphate isomerases/epimerases [Carbohydrate transport and metabolism].	6.23163e-26
NZ_CP043451.1\|WP_091176158.1\|6142353_6142608_-\|DUF2752-domain-containing-protein	gnl\|CDD\|378499	pfam10825, DUF2752, Protein of unknown function (DUF2752). This family is conserved in bacteria. Many members are annotated as being putative membrane proteins.	6.97623e-11
NZ_CP043451.1\|WP_112656419.1\|6142654_6143065_-\|DUF4199-domain-containing-protein	gnl\|CDD\|379395	pfam13858, DUF4199, Protein of unknown function (DUF4199). This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 167 and 182 amino acids in length.	0.000484723
NZ_CP043451.1\|WP_112656427.1\|6135868_6136450_+\|TetR/AcrR-family-transcriptional-regulator	gnl\|CDD\|224228	COG1309, AcrR, Transcriptional regulator [Transcription].	3.73443e-11
NZ_CP043451.1\|WP_112656421.1\|6141475_6142285_-\|AraC-family-transcriptional-regulator	gnl\|CDD\|378964	pfam12833, HTH_18, Helix-turn-helix domain.	6.90206e-15
NZ_CP043451.1\|WP_112656403.1\|6154015_6154825_-\|molybdopterin-dependent-oxidoreductase	gnl\|CDD\|224952	COG2041, COG2041, Sulfite oxidase and related enzymes [General function prediction only].	3.68467e-41
NZ_CP043451.1\|WP_112656405.1\|6152593_6153961_-\|MFS-transporter	gnl\|CDD\|225121	COG2211, MelB, Na+/melibiose symporter and related transporters [Carbohydrate transport and metabolism].	6.73073e-55
NZ_CP043451.1\|WP_112656425.1\|6136469_6138104_-\|apolipoprotein-N-acyltransferase	gnl\|CDD\|143595	cd07571, ALP_N-acyl_transferase, Apolipoprotein N-acyl transferase (class 9 nitrilases). ALP N-acyl transferase (Lnt), is an essential membrane-bound enzyme in gram-negative bacteria, which catalyzes the N-acylation of apolipoproteins, the final step in lipoprotein maturation. This is a reverse amidase (i.e. condensation) reaction. This subgroup belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 9.	7.81549e-75

>NZ_CP043451.1|WP_112656417.1|6143221_6146569_+|transcription-repair-coupling-factor
MNIRDILDRYKADDRIKTLATALNASKNPRVQLRGLVGSSDSAMAVALYFLQHKHMVFVLPDREEAGYFQADLENLTGKEALLFPSSYRKPFEFTQPDSSNVLARAEVLNELNHSSEYGQLIVTYPEALAEKVIDRSSLEKNTLEIAVSNKLSIDFINEFLIEYDFERVDFVYEPGQFSIRGGIVDIFSFSHMLPYRVEFFGDFIESIRTFEIESQLSVEHVKSITIVPNVQSKFLTENNISLLEYVEAGTQVWIKDVQFTLDIIQTGYKKAVNLWKALSADEKAQNPDWIDPKFGFTDEKLIGDQLHDFPVIEFGKQFFYHDATAINFDMRPQPSFNKDFTLLIHNFKNNEADKIENFIFTDSAKQVERLYAILDDLDKTVKFTPVSISIREGFIDHEQKIACYTDHQIFDRYYKYKTRKGYQRSQAITLKELRDLKPGDYVTHIDHGIGKYAGLEKVDVNGKQQEMIRLIYADNDLLYVNINSLNRISKFSGKEGSVPKMNKLGTDTWERLKKTTKKKVKDIARDLIKLYALRKAQHGNAFSPDSYLQTELEASFLYEDTPDQEKATADFKKDMESPHPMDRLICGDVGFGKTEVAVRAAFKAVADSKQVAILVPTTILAAQHYKTFTDRLKGFPANIDYVNRFKSTRQIKDTLEKLKEGKVDIIIGTHRLVSKDVKFKDLGLMIIDEEQKFGVSTKEKLKQMRANVDTLTLTATPIPRTLHFSLMGARDLSIISTPPPNRQPVVTELHVFNDKLIKEAVEFEIDRGGQVFFIHNRVADLPQLGGMIRKLVPKARIGIAHGQLEGDDLEDVMLKFVNHEYDVLVATTIIEAGLDIPNANTIIINYAHMFGLSDLHQMRGRVGRSNKKAYCYLLSPPLSTLTSEARKRLSAIEEFSDLGSGFNVAMRDLDIRGSGNLLGAEQSGFIAEIGFEMYHKILDEAIQELKEDEFKGVFPEDKPRPYISFTQIDTDLEILIPDEYVTNLSERYNLYTELSKLENEVELQAFQQKLHDRFGPVPAQVDGLLNTLRLQWLGKAIGFEKISLKKNVLRGYFITNQQSSYFETEAFRNVLDFVKNNPRRTNLKEVKNTLRLGIEGIDSVDEALRMLSEVAGII
>NZ_CP043451.1|WP_112656419.1|6142654_6143065_-|DUF4199-domain-containing-protein
MKNAVLSGGIIGVLSIIWIFAMPRLGVMPQKDVVAPVEYFSFIIPAIGLFFGIMSYRKNECNGQMGFLEALFQSFKILIVGGIIAVFGSILYISYVSSSEANIKDFSERIFGALIVGVLLAFAVSLLFTNKANKLD
>NZ_CP043451.1|WP_091176158.1|6142353_6142608_-|DUF2752-domain-containing-protein
MLSLAMTSPTEASHFTLCPLKLMGIGWCPGCGLGHSIIYLFHGDISNSFRAHWLGIPAVAVIFNRIYVLTKARLLERNQFKSLT
>NZ_CP043451.1|WP_112656421.1|6141475_6142285_-|AraC-family-transcriptional-regulator
MQIAPHPLLSDIVKHYLIIAHDQRVALNYRLFSDGNPGMVFHLKAPLLQYNQQHTVASKQPGSFVYGQITNYNDIVSVGELAMLIVVLQPNTLLSLLGVAACELNNNTVPLKDLFGQETFDLEDQIANAANLPAATVITEQFLLNKMASKRKRADITDRAINIIHANKGIINVKNLLDVMPVTERQLERKFDEEVGISPKKYIDVVKFQNYLKQLQKLSSIKELSSLSYACGYYDQAHLNNFFRKHTGLTPLQYKANHHLLAINFMPLV
>NZ_CP043451.1|WP_112656534.1|6140462_6141404_-|nitrilase
MENLTIATAQFENRSGDKAYNLSVIEKMTADAAAQGAQAIAFHECSITGYTFARKLDKAQMLELAEEIPCGPSIAALTEYARRYDIAILAGLFEKDKDDNLFKAYLCADKTGIVAKHRKLHPFINPHLLPGTAYTVFDLYGWKCGILICYDNNIIENVRATTLLGAQIIFMPHVTMCTPSTRPGAGFVDPELWKDKEANAVLLRQEFDSLKGRQWLMKWLPARAYDNAIYAVFANPIGMDDDQLKNGCSMILDPYGDIIAECRSLNNELVLAELTADKLTKAGGYRYIQARKPELYRDIIGREHESFQKVVWL
>NZ_CP043451.1|WP_090533497.1|6139104_6140376_+|serine--tRNA-ligase
MLQVSYIRDNREQVLERLAVKNFKQPQLVDEIIELDDKRRSTQTSMDNVSAEANAAAKQIGELMRAGKKEEAEGLKGKTGAWKEEIKKLGDLLTITEEELYQKLVLLPNLPHSSVPKGLTPEDNEVVLENGTRPELPADALPHWELAAKYNLIDFELGVKITGAGFPVYKNKGAKLQRALINYFIDEAEKAGYSEVSVPLMVNEASGFGTSQLPDKEGQMYHVGVDNLYLIPTAEVPITNLYREVILKEDQLPVRNCGHTPCFRREAGSYGAHVRGLNRLHQFDKVEIVTIAHPDKSYEILELMSSHVQGLLQKLGLPYRVLRLCGGDMGFGSALTYDMETWSAAQQRWLEVSSVSNFETFQSNRLKLRFRNADGKTQLAHTLNGSALALPRIVATLLENNQTEKGIKVPEVLVPYTKFEWID
>NZ_CP043451.1|WP_112656423.1|6138256_6138985_-|16S-rRNA-(cytidine(1402)-2'-O)-methyltransferase
MNNPIGKLYLVPTPIGNLEDMTFRAIRVLKEVDLILAEDTRTSAPMLKHFEIHQKVFAHHQHNEHQSSNEIIKFLLQGKNIALISDAGTPAISDPGFFLVREALKFNIAVECLPGATAFVPALVNSGFPTDKFCFEGFLPLKKGRQTRYKFLAEEERTIILYESPHRLLKTLDEMATYFGADRQISVSRELTKMFEETVRGTVVEVKQYFETHPMKGEFVMCVAGAAAKPAKGKYERDEEED
>NZ_CP043451.1|WP_112656425.1|6136469_6138104_-|apolipoprotein-N-acyltransferase
MKKNLPLAILSGLFLWIAWPPTPYTTFLLFIGFVPMLLAIENIINDDKPKKGKRVFNVTFIGFFIWNSLSVYWVYNALKIVGEIVAIPITLIPYSLGPLLMATAIWLYYRFRLVAPRWVALIGLVCFWIGYEYLHQSWDLYFPWMTLGNGFAVSHQWVQWYEYTGVYGGTLWIWVVNILAFLIYTSLREGQTKRHRMALIMAIVIVVTVPLGYSLSVYHNYVEEVNPSNIVIAQPNIDPYEKDGTIPPASQLDILIQLSRQVAQPNTEFFIWPETAIPAPVYINEEQIGQNDFIKQAQIFLRKYPNGNLVTGAETYRLYNNRATPTAIPSPWGGDQFADFYSTALNIENGDRIQTYHKSRLVPGAESLPFGDALSFLKPVFEHLGGATGNYAPEKDAKVLYSQSGIGVDPVICYESIWGGYIARSVKKGAQFIAIITNDGWWENTSGKDQHLDYAKLRAIETRRWVCQSANTGISGFINQRGDVVKHTEWWTKTSIKQDINLNSELTFYVKHGDYIPQAGSIFAGIGILFLLGMRLRKKQTLTV
>NZ_CP043451.1|WP_112656427.1|6135868_6136450_+|TetR/AcrR-family-transcriptional-regulator
MARSKDFDEAEVLSKAVCIFWHKGYNGTSMQDLVDGLGISRSSLYDTFGDKHALYIKALDSYQKAGGNQMCDIINNSASAKEAIQKLLELTMRDLLNDEQRKGCFMVNAEIELAPHDVEVKNVVCRNEQQFEDAILQAIKKGQASGEVRNSQDSLALARFIMNAVRGMQVSAKATADKAFFDDIIKTTLSVLD
>NZ_CP043451.1|WP_112656429.1|6135018_6135768_+|glucose-1-dehydrogenase
MKKLENKVAVVTGASKGIGAGIAKSLASAGAAVVVNYASDKNGADKVVAEITAEGGKAIAVQGSVAKKADVDRLFAETKEAFGGVDVLVNNAGVYQFTPIEAVTEEEFHRQFDINVLGLLLATQGAVNSFGDKGGSIINISSTVTRITPPQSAIYTGTKGAVDSITQVLSKELGPKKIRVNAINPGMVETEGTHTAGFIGSDFQAQIESTTPLGRIGQPDDIAPVAVFLASDDSRWLTGEIILASGGVR
>NZ_CP043451.1|WP_112656415.1|6146814_6147336_-|transposase
MEFDEIYFYTATINKWIPLLQSDKFKHIVLNSLIHLVKQRKIEIYGFVIMPNHIHLIWSGSEMNGKEKPFASFIKFTGHQFLDELRATDNPLLVKFKTDLKNRNYLFWQTNSLPIRVFDRKMLEQKLDYIHLNPLQAHWNLTDDPNNYYFSSCSFYEQEDKKFDWLIHYMDVM
>NZ_CP043451.1|WP_112656413.1|6147534_6148035_-|hypothetical-protein
MKRIFIAFSVLLLIIAVGMSLTGYTLAIPLSQINSDRLNTPLPKARSDQNLQPLSDCDFSKGNWTAYIVISTDDFNDLNPLIGKRVCWKTNSKALLMKMKKDWVFKYRENSDMGTVNSSFYLVQDGVMVFESGIVLDKNNQGLQNSKYGWMQPVNGMAFCKYLQGL
>NZ_CP043451.1|WP_112656411.1|6148131_6148632_-|hypothetical-protein
MKYTSLLLSGCIAASFLFSSCDKKGPATSTVAITITDGQTGAASVGATVKLYDDVNKPNTGEAPSYTLTTDASGKATAVVAYIGEYYIVAEKGTQKSYYNGLIPIGIFKTQADIDSSPKQTPAAIIGSVKFKDTNNDGVINDSDKAKAPNLFLQEGQTLNYSLAVY
>NZ_CP043451.1|WP_112656409.1|6148747_6149287_-|hypoxanthine-phosphoribosyltransferase
MTKQIADLEFEILLTADKIEERVKAIGAQLNEDYNNSVPVFIGVLNGSFLFIADLIKQVSIPCEINFTKLASYYGGTSSTLKIREDIDLTVDIKGRDVLIIEDIVDTGNTAHYLIQKLKEREPASLRLCSLLLKPAALQKKIEELKYVGFEIENEFVVGYGLDYKEMGRNLKDIYKKVG
>NZ_CP043451.1|WP_112656407.1|6149434_6150667_+|insulinase-family-protein
MIDYQLYTLPNGIRILYKHWPSAITHCCFIVNAGSRDEAPGQGGLAHFIEHLLFKETERRNTSQILNRLELVGADLNAYTTKEYTCIHASLLNQHLDRTMDLFEDILFHSTFPDDEQEKERGVILDEIASYLDQPEEAIQDDFEELLFKEHPIGQNILGTPETVGRLNGDDIRGFIAANYNTTEMIFAVHGNYEFRKLAAMSEKYFGHVPLNELKKNRVKPVQGTGSIHIVNKPISQTHCIIGTQAYSSSHEHKWGLLLLNNLLGGVGMSSRLNLEIREKHGIAYTVESNYTPLTDTGIFSIYFGTDTEKANKASKLIHKELKKLREQKLGSLQLHQARQKFIGQIALAEENRMSLIIAMAKSMIDFNRVDTLEEIFAKINLVSAEQLLTISNEIFDNNRLITLLFEPKQ
>NZ_CP043451.1|WP_112568308.1|6150684_6151257_+|peptide-deformylase
MKYPIIAYGDPVLRKKATAIEPDEYPHIKELVENMFETMYAARGVGLAAPQVGMSMRLFVVDATPFDDDEPELKDFKKAFINATILEETGEEWGFNEGCLSIPDIREDVYRKPVVRMSYYDADWKHHEETFKGMAARVIQHEYDHIEGKLFTDKLSPLRKRLIEKKLNDISKGMVDVDYKMKFPNVKKGR
>NZ_CP043451.1|WP_090533817.1|6151451_6152336_+|sugar-phosphate-isomerase/epimerase
MTTRRSFLKTSALLSAGLLAAPNLFAYDKKYIGLQLYTVRDAMAADPVAALAKVAKTGFTSVEGATYTGTELFYGMRPGDFANVLKQNGLIMPSAHYRLGEELVNGEQQKGTIMNDWKKAVDDAAEAGVQYMVCAYLSQSERGNLDHYKNVANMLDIAGETCKGAGIQLCYHNHDFEFIQENGKYPYEILLENTDKDLVKMEMDLYWVNKANQDPIALIDKHPGRFPLWHVKDMDKTPEKKFTEVGNGVIDFKKIFTQAKKSGLKYFFVEQDVCPGDPFVSIAQSISYIKKNLV
>NZ_CP043451.1|WP_112656405.1|6152593_6153961_-|MFS-transporter
MPANKLPLSKQLAYACGMIGWSIMTNIIIVMLPYFYLPPNNAGLTTLVPQLLLFGLFNIMSVITASGRLVDAFFDPFIASLSDKSENRRGRRIPFMQWAILPAALFCGLTFYPMVKGESIHNAYWLTFTLICFFMGATAYIIPYNALLPELTRTGSERVKLSSLQQVGFVIGIILSAMVNNFADWVQRFAGTPNRDTAVQYTIWGLAVFAGLVMLVPVFAIDEKRYSNGHPSHLSLLPAIQKTFQNRNFKYYLISDFSYYMALSIISSGLLFFLKSLLNLPESMGGELMATMVLVSLLFYPLVNYLSQKIGKKPIVLFSFGLLSLIFVAIFFLGKLPFTPQVQIYTLVISASFPLASLGILPNAILAEIAQNEAKRTGENREGMFFAVKYLFVKLGQTLGIALFAFLTIYGKDPGNDYGLRLNGVCGCVLCLLAFVFFNRFRERRNRGKKRTAHH
>NZ_CP043451.1|WP_112656403.1|6154015_6154825_-|molybdopterin-dependent-oxidoreductase
MKLTKKLNKIFSKNKGSKKELTVEQKISRRNFISFGSFLVLGGAAYGGWRWLYNSPNEAPGITGEAHKPLRAVLNANEKVVRQLYSNKNLVKTYPKEMAAKVVRHNSDIGSEGLIDVDAWKLSVKRQSGEMLSIGIDELKKLPKTEIIYDFKCVEGWDQISHWGGVKFSDFIAHFKLDAETRFEYVGMETPDKEYYVGVDMPSAMHPQTLLAYEVNEKPLPPKHGAPLRLIIPVKYGIKNLKRIGSITFSNSRPRDYWAEQGYDYYAGL
>NZ_CP043451.1|WP_167516287.1|6154799_6155507_-|thiosulfate-reductase
MKIIKEKHPLLMRWTHWVNFPILTIMIWSGLLIYWANDTYTFTLFGVTFIRFFPQGFYDALHIPRRLAEGMAFHFLFMWFFALNGLLYVSYTIISGQWRELVPNRHSFKEAWLVVLHDLHIRKMAPPQNKYNAAQRIAYTAIIVMGFGSLITGLAIYKPVQFNYLAWICGGYHLARIWHFVLTIAYVLFFLVHVVQVVLAGWNNFRSVISGFEVIDEKPLPAIQIQNDETNEKTE

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Self-targeting detection

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_ID	Protospacer_location	Mismatch	Identity

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity

Prophage detection

Region

Region Position

Protein_number

Hit_taxonomy

Key_proteins

Att_site

Prophage annotation

DBSCAN-SWA_1

3488188 : 3498604

uncultured_phage(50.0%)

tail,protease,transposase

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_091171169.1\|3488188_3488647_-\|tail	phage tail protein	NA	NA	NA	NA
WP_112652161.1\|3488649_3489081_-\|tail	phage tail protein	A0A059XP41	uncultured_phage	5.9e-32	54.1
WP_112652162.1\|3489205_3491197_-\|tail	phage tail protein	NA	NA	NA	NA
WP_112652163.1\|3491208_3492663_-\|tail	phage tail sheath family protein	J9PVC2	Bacillus_phage	1.1e-24	27.3
WP_112652164.1\|3492681_3493866_-	hypothetical protein	NA	NA	NA	NA
WP_090524152.1\|3493905_3494490_-	DUF4255 domain-containing protein	NA	NA	NA	NA
WP_112652165.1\|3494909_3495506_+	FMN-dependent NADH-azoreductase	NA	NA	NA	NA
WP_112652172.1\|3495554_3496667_-	metallophosphoesterase	NA	NA	NA	NA
WP_149354031.1\|3496895_3498017_+\|transposase	ISAs1 family transposase	NA	NA	NA	NA
WP_112655407.1\|3498082_3498604_+\|protease	protease	NA	NA	NA	NA

Anti-CRISPR protein detection

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

Overview of predicted results

Overview of the results

Cas Category Instructions

Results visualization

1. NZ_CP043451

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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