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_CP049246	Sphingobacterium lactis strain DSM 22361 chromosome, complete genome	15 crisprs	cas3,DEDDh,csa3,WYL	1	0	1	0

Results visualization

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CRISPR-Cas detection and classification

Crispr_ID: NZ_CP049246_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP049246_1

128638-128716

Orphan

Consensus_repeat	Method
CTACACCCTTTCTATCTCATATCTC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP049246_1

>merge|NZ_CP049246|1|128638-128716|CRISPRCasFinder
CTACACCCTTTCTATCTCATATCTCTAATCTAACAACTCATATCTCAAACCCACCTACACCCTTTCTATCTCATATCTC

>NZ_CP049246|1|1|128638-128716|CRISPRCasFinder
CTACACCCTTTCTATCTCATATCTC	TAATCTAACAACTCATATCTCAAACCCAC
CTACACCCTTTCTATCTCATATCTC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP049246.1\|WP_103907694.1\|116828_117491_-\|MgtC/SapB-family-protein	unknown	unknown	gnl\|CDD\|224204
NZ_CP049246.1\|WP_103907691.1\|114214_115036_-\|SDR-family-oxidoreductase	unknown	unknown	gnl\|CDD\|236216
NZ_CP049246.1\|WP_094255405.1\|127673_128117_-\|50S-ribosomal-protein-L11	unknown	unknown	gnl\|CDD\|234661
NZ_CP049246.1\|WP_103904685.1\|137225_138581_-\|sigma-54-dependent-Fis-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|225114
NZ_CP049246.1\|WP_103907692.1\|115178_116171_+\|sugar-kinase	unknown	unknown	gnl\|CDD\|238571
NZ_CP049246.1\|WP_103907699.1\|126952_127651_-\|50S-ribosomal-protein-L1	unknown	unknown	gnl\|CDD\|180071
NZ_CP049246.1\|WP_103907708.1\|131978_132980_+\|BamA/TamA-family-outer-membrane-protein	unknown	unknown	gnl\|CDD\|366466
NZ_CP049246.1\|WP_160003584.1\|138597_139905_-\|TolC-family-protein	unknown	unknown	gnl\|CDD\|224455
NZ_CP049246.1\|WP_103907698.1\|126431_126950_-\|50S-ribosomal-protein-L10	unknown	unknown	gnl\|CDD\|234632
NZ_CP049246.1\|WP_103907701.1\|129792_130980_-\|elongation-factor-Tu	unknown	unknown	gnl\|CDD\|183708
NZ_CP049246.1\|WP_103904684.1\|135902_137222_-\|HAMP-domain-containing-histidine-kinase	unknown	unknown	gnl\|CDD\|223715
NZ_CP049246.1\|WP_103904687.1\|140259_141513_+\|HlyD-family-efflux-transporter-periplasmic-adaptor-subunit	unknown	unknown	gnl\|CDD\|273776
NZ_CP049246.1\|WP_103907700.1\|129343_129538_-\|preprotein-translocase-subunit-SecE	unknown	unknown	gnl\|CDD\|376355
NZ_CP049246.1\|WP_103907693.1\|116173_116827_+\|bifunctional-4-hydroxy-2-oxoglutarate-aldolase/2-dehydro-3-deoxy-phosphogluconate-aldolase	unknown	unknown	gnl\|CDD\|235939
NZ_CP049246.1\|WP_103907697.1\|125971_126352_-\|50S-ribosomal-protein-L7/L12	unknown	unknown	gnl\|CDD\|234671
NZ_CP049246.1\|WP_103907695.1\|117647_121925_-\|DNA-directed-RNA-polymerase-subunit-beta'	unknown	unknown	gnl\|CDD\|234794
NZ_CP049246.1\|WP_103907696.1\|121997_125792_-\|DNA-directed-RNA-polymerase-subunit-beta	unknown	unknown	gnl\|CDD\|234749
NZ_CP049246.1\|WP_103904683.1\|135404_135878_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP049246.1\|WP_093098554.1\|128775_129321_-\|transcription-termination/antitermination-factor-NusG	unknown	unknown	gnl\|CDD\|180161
NZ_CP049246.1\|WP_164527198.1\|134224_135106_+\|IS3-family-transposase	unknown	unknown	gnl\|CDD\|222853

Protein	Function_ID	Function_description	E-value
NZ_CP049246.1\|WP_103907694.1\|116828_117491_-\|MgtC/SapB-family-protein	gnl\|CDD\|224204	COG1285, SapB, Uncharacterized membrane protein [Function unknown].	2.5672e-42
NZ_CP049246.1\|WP_103907691.1\|114214_115036_-\|SDR-family-oxidoreductase	gnl\|CDD\|236216	PRK08277, PRK08277, D-mannonate oxidoreductase; Provisional.	3.66935e-120
NZ_CP049246.1\|WP_094255405.1\|127673_128117_-\|50S-ribosomal-protein-L11	gnl\|CDD\|234661	PRK00140, rplK, 50S ribosomal protein L11; Validated.	1.22344e-91
NZ_CP049246.1\|WP_103904685.1\|137225_138581_-\|sigma-54-dependent-Fis-family-transcriptional-regulator	gnl\|CDD\|225114	COG2204, AtoC, Response regulator containing CheY-like receiver, AAA-type ATPase, and DNA-binding domains [Signal transduction mechanisms].	3.50644e-153
NZ_CP049246.1\|WP_103907692.1\|115178_116171_+\|sugar-kinase	gnl\|CDD\|238571	cd01166, KdgK, 2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form 2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the common intermediate product, that allows organisms to channel D-glucuronate and/or D-galacturinate into the glycolysis and therefore use polymers, like pectin and xylan as carbon sources.	2.24752e-63
NZ_CP049246.1\|WP_103907699.1\|126952_127651_-\|50S-ribosomal-protein-L1	gnl\|CDD\|180071	PRK05424, rplA, 50S ribosomal protein L1; Validated.	3.72071e-135
NZ_CP049246.1\|WP_103907708.1\|131978_132980_+\|BamA/TamA-family-outer-membrane-protein	gnl\|CDD\|366466	pfam01103, Bac_surface_Ag, Surface antigen. This entry includes the following surface antigens; D15 antigen from H.influenzae, OMA87 from P.multocida, OMP85 from N.meningitidis and N.gonorrhoeae. The family also includes a number of eukaryotic proteins that are members of the UPF0140 family. There also appears to be a relationship to pfam03865 (personal obs: C Yeats). In eukaryotes, it appears that these proteins are not surface antigens; S. cerevisiae YNL026W (SAM50) is an essential component of the Sorting and Assembly Machinery (SAM) of the mitochondrial outer membrane. The protein was localized to the mitochondria.	4.33317e-14
NZ_CP049246.1\|WP_103907698.1\|126431_126950_-\|50S-ribosomal-protein-L10	gnl\|CDD\|234632	PRK00099, rplJ, 50S ribosomal protein L10; Reviewed.	3.92503e-42
NZ_CP049246.1\|WP_103907701.1\|129792_130980_-\|elongation-factor-Tu	gnl\|CDD\|183708	PRK12735, PRK12735, elongation factor Tu; Reviewed.	0
NZ_CP049246.1\|WP_103904684.1\|135902_137222_-\|HAMP-domain-containing-histidine-kinase	gnl\|CDD\|223715	COG0642, BaeS, Signal transduction histidine kinase [Signal transduction mechanisms].	4.47806e-34
NZ_CP049246.1\|WP_103904687.1\|140259_141513_+\|HlyD-family-efflux-transporter-periplasmic-adaptor-subunit	gnl\|CDD\|273776	TIGR01730, COG0845:_Membrane-fusion_protein, RND family efflux transporter, MFP subunit. This model represents the MFP (membrane fusion protein) component of the RND family of transporters. RND refers to Resistance, Nodulation, and cell Division. It is, in part, a subfamily of pfam00529 (Pfam release 7.5) but hits substantial numbers of proteins missed by that model. The related HlyD secretion protein, for which pfam00529 is named, is outside the scope of this model. Attributed functions imply outward transport. These functions include nodulation, acriflavin resistance, heavy metal efflux, and multidrug resistance proteins. Most members of this family are found in Gram-negative bacteria. The proposed function of MFP proteins is to bring the inner and outer membranes together and enable transport to the outside of the outer membrane. Note, however, that a few members of this family are found in Gram-positive bacteria, where there is no outer membrane. [Transport and binding proteins, Unknown substrate].	4.32652e-24
NZ_CP049246.1\|WP_103907700.1\|129343_129538_-\|preprotein-translocase-subunit-SecE	gnl\|CDD\|376355	pfam00584, SecE, SecE/Sec61-gamma subunits of protein translocation complex. SecE is part of the SecYEG complex in bacteria which translocates proteins from the cytoplasm. In eukaryotes the complex, made from Sec61-gamma and Sec61-alpha translocates protein from the cytoplasm to the ER. Archaea have a similar complex.	2.49068e-10
NZ_CP049246.1\|WP_103907693.1\|116173_116827_+\|bifunctional-4-hydroxy-2-oxoglutarate-aldolase/2-dehydro-3-deoxy-phosphogluconate-aldolase	gnl\|CDD\|235939	PRK07114, PRK07114, bifunctional 4-hydroxy-2-oxoglutarate aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase.	2.17515e-80
NZ_CP049246.1\|WP_103907697.1\|125971_126352_-\|50S-ribosomal-protein-L7/L12	gnl\|CDD\|234671	PRK00157, rplL, 50S ribosomal protein L7/L12; Reviewed.	5.60157e-39
NZ_CP049246.1\|WP_103907695.1\|117647_121925_-\|DNA-directed-RNA-polymerase-subunit-beta'	gnl\|CDD\|234794	PRK00566, PRK00566, DNA-directed RNA polymerase subunit beta'; Provisional.	0
NZ_CP049246.1\|WP_103907696.1\|121997_125792_-\|DNA-directed-RNA-polymerase-subunit-beta	gnl\|CDD\|234749	PRK00405, rpoB, DNA-directed RNA polymerase subunit beta; Reviewed.	0
NZ_CP049246.1\|WP_160003584.1\|138597_139905_-\|TolC-family-protein	gnl\|CDD\|224455	COG1538, TolC, Outer membrane protein [Cell envelope biogenesis, outer membrane / Intracellular trafficking and secretion].	6.71112e-40
NZ_CP049246.1\|WP_093098554.1\|128775_129321_-\|transcription-termination/antitermination-factor-NusG	gnl\|CDD\|180161	PRK05609, nusG, transcription antitermination protein NusG; Validated.	6.86957e-62
NZ_CP049246.1\|WP_164527198.1\|134224_135106_+\|IS3-family-transposase	gnl\|CDD\|222853	PHA02517, PHA02517, putative transposase OrfB; Reviewed.	1.88139e-47

>NZ_CP049246.1|WP_094255405.1|127673_128117_-|50S-ribosomal-protein-L11
MAKEVSALVKLQVKGGAANPSPPVGPALGAKGVNIMDFCKQFNARTQDKPGQVLPVVITVYADKSFDFIIKTPPVAVQLKDAAKLKSGSGEPNRKKVASITWDQVKTIAEDKMPDLNAFTVESAMRMVAGTARSMGITVSGDAPWKN
>NZ_CP049246.1|WP_103907699.1|126952_127651_-|50S-ribosomal-protein-L1
MARLTKNQKAALSKIEAGKAYSLKEAAALVKEITNTKFDASVDIDVRLGVDPRKANQMVRGIATLPHGTGKTVRVLVLCTPDKEEEAKAAGADYVGLDDYISKIEGGWTDVDIIITMPSVMAKVGKLGRILGPRNLMPNPKTGTVTTEVGKAVTEVKGGKIDFKVDKTGIIHTSVGKVSFDADKIYDNALEVLQTISRLKPSAAKGTYFKSIHISSTMSPGIHVETKSVAGI
>NZ_CP049246.1|WP_103907698.1|126431_126950_-|50S-ribosomal-protein-L10
MRKELKHEIVEALAEQIKSYGNFYITDTANLSVEKVNNIRRKCFEQNIEIKVVKNTLIKKALLEAGVDSEEIFGVLKGASTLLFSETGNAPAKLIKQLRKEGDKPVLKAAYIQETAFVGDNQLDALVTLKSKEELIADVIALLQSPAKNVISALQSGGNTISGLVKALEERG
>NZ_CP049246.1|WP_103907697.1|125971_126352_-|50S-ribosomal-protein-L7/L12
MADLKQLAEQLVNLTVKEVKELADILKDEYGIEPAAAAVAVAAAPGAGDGAAAAEEKTSFDVILKEAGGQKLAVVKLVKDLAGLGLKEAKDLVDGAPKELKSGVSKDEAEALKKQLEEAGAVVEIK
>NZ_CP049246.1|WP_103907696.1|121997_125792_-|DNA-directed-RNA-polymerase-subunit-beta
MQKERINFATSKKVIDYPDFLDVQLESFKEFFQLETTSDNRHQEGLYKVFAENFPISDSRNIFVLEFLDYFIDPPRYDIQECIERGLTYSVPLKAKLKLSCNDEEHEDFETIVQDVYLGTIPYMTPKGTFVINGAERVIVSQLHRSPGVFFGQSRHTNGTKLYSARVIPFKGSWIEFATDVNNVMYAYIDRKKKFPVTTLLRAIGFDSDKDILELFDLADEVKVSKSGLKKYVGRRLAARVLNKWTEDFVDEDTGEVVSIDRNEIILERETILEEDHIDLIIEAGVKSIILTKEDEANNADYSIIYNTLQKDTSNSEKEAVEHIYRQLRNAEPPDEETARGIIDRLFFSDKRYDLGDVGRYRINRKLNLDTPSDTKVLTREDIIAIVKYLINLINSKAEVDDIDHLSNRRVRTVGEQLYAQFGVGLARMARTIRERMNIRDNEVFTPTDLINARTLSSVINSFFGTNQLSQFMDQTNPLAEITHKRRLSALGPGGLSRERAGFEVRDVHYTHYGRLCTIETPEGPNIGLISSLSVHAKINNLGFIETPYRIVEDGKVVVDQPVVYLSAEDEDDKTIAQANALYDDKGNFLDAKVKARYEGDFPIIEPEKLDYMDVSPNQITSIAASLIPFLEHDDANRALMGSNMQRQAVPLLRPQAPVVGTGLEGRVAKDSRTLINAEGSGVVEYVDAQEIHIRYDRNDNDRLVSFDDDVKVYKLTKFKKTNQNTCINLKPIVQKGQRVEKGQVLCEGYATEDGELALGRNLKVAFMPWQGYNFEDAIVISERVVSQDLFTSLHIEEFELEVRDTKRGEEELTADIPNVSEEATKDLDENGIIRIGAEVGEGDILIGKITPKGESDPSPEEKLLRAIFGDKAGDVKDASLKTPPSIKGVVIDTKLFSRAKKMSKEVERKALEKLEVAHDRNIKALKDRLVEKLFTIVNGKTSQGIYNVYKELLVAKGAKFTQKILTDLDYNNVNPTGWTTDDDKNDMIKIALHNYNIKVNEELGAFKREKFAISVGDELPSGIVQMAKVYVAKKRKLKVGDKMAGRHGNKGIVARIVRDEDMPFLEDGTPVDIVLNPLGVPSRMNLGQIYETVLGWAGQKLGVKFATPIFDGAEMDQVEEWVEKAGLPKSGRTYLYNGLTGERFDQPTTVGVIYMLKLGHMVDDKMHARSIGPYSLITQQPLGGKAQFGGQRFGEMEVWALEAFGASNILQEILTVKSDDVVGRAKTYEAIVKGNNLPTPSVPESFNVLVHELRGLGLDITLD
>NZ_CP049246.1|WP_103907695.1|117647_121925_-|DNA-directed-RNA-polymerase-subunit-beta'
MSYKKDNKIKSNFTSITISLASPETILERSSGEVTKPETINYRTYKPERDGLFCERIFGPVKDYECHCGKYKRIRYKGIVCDRCGVEVTEKKVRRERMGHINLVVPVAHIWYFRSLPNKIGYLLGLPTKKLDMIIYYERYVVIQPGIKEEDGLSYMDFLTEEEYLDILDTLPKENQFLDDTDPQKFVAKMGAEALEDLLKRLDLDQLSYDLRHQAANETSQQRKNEALKRLHVVEAFRGANDHIENRPEWMIVKIVPIIPPELRPLVPLDGGRFATSDLNDLYRRVIIRNNRLKRLIEIKAPEVILRNEKRMLQEAVDSLFDNSRKVNAVKTEGNRALKSLSDILKGKQGRFRQNLLGKRVDYSARSVIVVGPHLKLHECGLPKDMAAELYKPFIIRKMIERGIVKTVKSAKKIVDRKDPVVWDILENVLKGHPVLLNRAPTLHRLGIQAFQPTLVEGKAIQLHPLVCTAFNADFDGDQMAVHLPLGNAAILEAQILMLAAHNILNPANGSPVTVPSQDMVLGLYYITKGRKTDDSRIMKGEGTTFYSPEEVIIALNEGKVDLHAFIKVKTQIKTKEGEFKDAIIDTTVGRVIFNQIVPEEVGYINELLTKKSLRNVIGEIVKNTGMARAAKFLDDMKELGFQTAFKGGLSFNLQDLNIPAAKADLIQQATNEVEEVMNNYNMGFITNNERYNQIIDIWTRINNRLTSHVMDILSNDNQGFNSVYMMLDSGARGSKEQIRQLCGMRGLMAKPQKSGTSGGEIIENPILSNFKEGLSVLEYFISTHGARKGLADTALKTADAGYLTRRLHDVAQDMIVVEQDCNGLRGIYTTALKDNDDIVEPLYDRILGRTPLNDVVHPETNELIVAANEDITEEVAEAIENAGIEGLEIRSVLTCESKRGVCACCYGRNLASGKRVQLGEAVGVIAAQSIGEPGTQLTLRTFHVGGTASNIAAESSIIAKYDGKIEFENVRTVEKEGEDGPYQVVLGRSGEIKVVNEDRKVLYQQIIPYGSNLFVKEGEKVEKGTKLVDWDPYNAVIISEFAGKVEFDAIIEGVTFREESDEQTGHKEKVIIETRDKTKNPMIKVLDNKGEIIRSYNIPVGAHVSVSDGQKVKEGAVLVKIPRSTGKTRDITGGLPRVTELFEARNPSNPAVVTEIDGVVALGGVKRGNREISIESRDGQVKKYLVPLSKHILVQDNDFIKAGMPLSDGQISPGDILSIKGPSAVQEYIVNGIQEVYRLQGVKINDKHFETIVHQMMQKVNIEDPGDTRFLEKEAVNKWDFMEENDSLYDKKVIVDAGDSKTLRPGQIVTMRKLREENSSLKRQDMKLVEVRDAIPATSSPLLQGITRASLGTKSFISAASFQETTKVLNEAAIAGKRDNLLGLKENVIVGHLIPSGTGLRQYSNIIVGSREEYDQLLASKEED
>NZ_CP049246.1|WP_103907694.1|116828_117491_-|MgtC/SapB-family-protein
MDFLFNQIEWDWNDLVKAILSLLAGFVLGFEREWKDKSAGFKTISIICLGSTLFSLLSLKLGAGDSEDATRIASYVVSGIGFLGAGVIFKDGVNVNGLTTASIIWMSAAVGMAIGFGIYLTAGIFLLACFFIIISGPLLNKYVIHNIVRIATICVDQEDIETRQEIIRDLKPLVKQFKMKKQTLQEGRLTMEIEVLIDKRNIREFEHVLLSNKHIKELSL
>NZ_CP049246.1|WP_103907693.1|116173_116827_+|bifunctional-4-hydroxy-2-oxoglutarate-aldolase/2-dehydro-3-deoxy-phosphogluconate-aldolase
MNEQLLEKILNNPVIPVFYDDDLQTCIAILKSCYAGGIRVFEFVNRGREAKANFKALLAYKEEHFPDLSLGIGTIMNPEDAERFIDLGTDFLVSPIFNESIAAIAQKNNILWIPGCMTPSEIAAANLAGCTYIKLFPGDTLGPGFLKSIRPVFPNIRFMPTGGVECAADNIKTWFEAGVSSVGLGSKLFSKKDGQYDLAQIEDNCRNLLAWATKKGT
>NZ_CP049246.1|WP_103907692.1|115178_116171_+|sugar-kinase
MPHVLTFGEILLRLQGSSEQLLAPGANDLKIYPGGSEANVAVTLAKMGNPVYYSSAFPNNGLAKELIHVLESSGVDCSKHIQSGDRIGLYFLLSANGLTSGEVIYDRKYSSFSLLKAEELDFDTLFADVDWLHWSALTPALSAEMADLMALVLQEAKQRDITISVDLNYRSKLWQYGRTPLEVMPELVQHCDVIMGNIWAAHNMLGSPIEENLDKHTERAHYLHLSQQTADYIFSHYPQAKHIANTFRFIDNPKHNLFYGTYHSREEQAISQQYETHEVVDRIGSGDAFMGGLIHALRQPWDASAIIEYATATGYQKLFVEGDFGDGKAL
>NZ_CP049246.1|WP_103907691.1|114214_115036_-|SDR-family-oxidoreductase
MSILSKFSLQDKVIVITGGTGILGKSFVKAIAEAGAKLCILGRNQEKIDERVATAREIGAEAIGLVADVMDEESVKAARGAVLAHYGTIDGLVNAVGGNIPGATIGDDQNIFDNKIQDTIKAIELNLYGTMIPTMIFGEVIAEKGAGSIINISSLAASRPLTRVLGYTVAKHGIDGFTRWMSTELALRYGDKVRVNAIAPGVFLTEQNRTLLTNTDGSYTDRAQKFINGTPYRRLGDPSELEGTLIYLLSEASAFVSGETVFVDGGFNSWCGV
>NZ_CP049246.1|WP_093098554.1|128775_129321_-|transcription-termination/antitermination-factor-NusG
MADQSLKWYVVRAVSGKEKKVKQYLEAEINRLGIQHLVTQVLIPMEKYYQMRDGKKVAKERNYYPGYVLIEAALDGEIEHAIKNVNSVIGFLGDKAGNAIPLRPAEVNRILGKVDEMAEQGESISVPYYVGETVKVNDGPFNGFTGEIEEVHEDKKKLTVMVKVFGRKTPLELNYMQVEKE
>NZ_CP049246.1|WP_103907700.1|129343_129538_-|preprotein-translocase-subunit-SecE
MAKVLDFFKDSYTEITEKVTWPTWSQLQSHAVIVLVASVIIALVIFVMDKASSNVMELLYNTAS
>NZ_CP049246.1|WP_103907701.1|129792_130980_-|elongation-factor-Tu
MAKEKFDRSKPHLNIGTIGHVDHGKTTTTAAITKVLADKGFSEARSFDSIDSAPEEKERGITINTSHVEYQTANRHYAHVDCPGHADYVKNMVTGAAQMDGAIIVVAATDGPMPQTREHILLARQVGVPALVVFLNKVDLVDDAELLDLVEMEVRELLSFYEFPGDDVPVIKGSALGALNGEDQWVESIMELMDAVDNYIPIPPRLTDLPFLMPIEDVFSITGRGTVATGRIERGVINSGDPVEILGMGAENLKSTVTGVEMFRKILDYGEAGDNVGLLLRGIEKTDIRRGMVICKPGSVTPHTDFKAEVYVLSKAEGGRHTPFFNKYRPQFYFRTTDVTGEISLEEGTEMVMPGDNVTITVKLINAIAMEKGLRFAIREGGRTVGAGQVTEIIK
>NZ_CP049246.1|WP_103907708.1|131978_132980_+|BamA/TamA-family-outer-membrane-protein
MVLPAVGYAQETGLEYGIASTYNFYVDKQDLESRTSNITLIGTLTTKKQKNIKLTSDLWTKGNEYHILSELRYRDWPFNFYGIGNDTWKADEDYLDQKLYRIKLDGEKRFAPNFYAGVNMNYEHFQFQDMEAGGIYESPGVYGKEGGQYLALGVSALYDTRNNTTYTTNGFYGRAKYSYAPNFFGKDNFTGNQVEVDLRGFYPITKQLTVTAQGLYRGTYGKNVPFYVMRDLGGDMTMRGYYLGRYKDKNYLTAQAELRYRFHPRVGIAGFLGTGSTFSKQHDMRLLPSYGGGLRYFFSLEHNSSIRFDYAFGEQRPGEKRQSGFYLSISEAF
>NZ_CP049246.1|WP_164527198.1|134224_135106_+|IS3-family-transposase
MGIRLICGLFGRTRHAYYDRQWRVQDVGLKDEIILQHVLRIRSEQKRIGTRKLLHMLAGPLQEHGIRIGRDYLFALMREHSLQIRVRKRKAVTTDSRHWMKKYRNLIKELAVERPEQVWVSDITYVQLNRRWGYLSLVTDAYSRKIVGWAFRGDLSAQGCIDALQMALQQRQYPGKGLIHHSDRGSQYCSKGYVDILRTNGIGVSMTENGDPYENAIAERVNGILKAEFDLYASQSGLRETTRKIRENIRVYNNLRPHASCDYLTPEQAHMRSGALRKRWRPKKYPIVQKEFV
>NZ_CP049246.1|WP_103904683.1|135404_135878_-|hypothetical-protein
MRFLLSYTYHFVVSNSRHGTHSPFVYALAEKVIYNPSFKSARYVDMPDGLTGKFMTLLRNILAFWKLDRLSADLEDHTAPAYWVDAPPISEESILQHLHRGKVVFLHKPYARKHRSLWQNLIADERVVVSINLFYFGILIHRSGQRKEDFLLRYPGI
>NZ_CP049246.1|WP_103904684.1|135902_137222_-|HAMP-domain-containing-histidine-kinase
MTRLAIKDFLRMVILMAFAVGIAYLAFKGYYLYATLAFIGLVVLAYRTFSTHRFLLKQLVEFSEAVKYRDFTRRFLVKSERTAEGQVFKAFNQINEIYKNISIDQALQHQYLNKVINMLDTAIIFYHAETGKVIWLNEAFKDLFQVPHLGNIAGMQKRHPELYEKTMQLRVGRHQMETAHSSKGKIKLLMQSSGFDTQDGSFRIIVYQNINEAIDETETRAWHKLLRVLTHEIMNSIGPISSLAETLHERLAHWDEKQDIEDLKLGIFTIKRRSEGLLQFAKSYRMINKVDQPQFSDIQVVQLFENIYQLLEPNLIQRNIDVDIIIKNTRLVLMADQNLLEQVLINLLLNAIEAVKEVEEPYISLSAIETKDHIQVKVQDNGIGMSAEIQEQIFTPFFTTKKTGTGVGLTLSKQIMLMHNGNLFVDSREGEGSTFTLQF
>NZ_CP049246.1|WP_103904685.1|137225_138581_-|sigma-54-dependent-Fis-family-transcriptional-regulator
MKKARILVVDDDQDLLTATRILLRPNVKEVLVEHNPERLMGLLEKNDIDIVLLDMNYKSAINTGNEGLFWLNKIKEKFPKVDVVMITAYGAVDLAVKSLKQGASDFIVKPWQNEQLLQTLQTIYNERLPTPKAKAQPTERDQHGLIGKSAIMEDLHYKLDKVAPTEANILILGENGTGKDLIANAIHQRSLRQRESFVKVDVGALTETLFESELFGYKKGAFTDAREDRKGRFEHAHLGTLFLDEIGNISLQQQAKLLSVLQNRAVVPLGSSQPIPVDIRLISATNVPLKVLADESRFRKDLIYRINTLEIQVPPLRERGEDIVLLAEHFLKFYSDKYHKNIAGLESNALSKLKGYHFPGNVRELQYSIERAVIMSDQQSIRAEDILFSPIEQQLPEERFDSGMESHNLEEIERKAIKSAMERYNGNISKAAKELGLTRAALYRRLEKYNL
>NZ_CP049246.1|WP_160003584.1|138597_139905_-|TolC-family-protein
MRNFLLIVYIFVCCLVSTAKGQDGYLSLADCLRMAIKNNPTLQRDELLVSRSDLAYKQAKYDRLPSLNANLSHNITQGRSINPTTNQYIDQNNSSGSQSLNLSVPIFNGFYIIHNIRMKSNALEAGKLEYQGQINELKLNVIEAYVKVLTAQDMLKQVEGQLGVTKEQLHRTEVLHREGAANPGDLFDIKGQFSADLNTVELTKQSLNNARVELAGLLNAELDSLPELEPMDVPSEVQAMRAADLFQQSLQVLPQFKAMDWRIKELEEGIQVAKSNYWPSLSLNGGLSSNYSRGEGAVFTQIKNNIYKGVGLSLSIPIFNQFKNRTQVRLAQVNLDEAYFNREILRNELRMQTARAVFDLHLTQRNVHNLREQELSYAESFRIATVHFEAGNSNSVIYLTAKNKLDNTRSQLIIRQYEWLMQKYVNDYYAGSLDL
>NZ_CP049246.1|WP_103904687.1|140259_141513_+|HlyD-family-efflux-transporter-periplasmic-adaptor-subunit
MDRPIQQKKWNTKRILTVAGIAGIVALIGASYYYTSGNSRLNVDAERISIFEVKENTFQEFIPINGSVMPISSIYLDASVGGRVEEKYVEDGAHLHKGDPIMRLSNTDMEMSLIQQEVQVLNLLTQAQIAQTNAQQATISNKNQMADVEQAYKEAERVYELNKKLLAEKAIGSQEYQKSLNEYNYQKERVGLTKQILKQDEVSNSQKLHQDRETYKRTQNALDLNRKKVGDLILRAPVDGQLTSFDAEIGQNKNPGERLGQIDVLTGFKVRADIDEHYINRIFPDLRGQFTIGNKSYDLRIKKVYTQVKDGRFQVDMEFVGERPESIRRGQTLTIRLALSDETKAILLAKGGFYQQTAGNWIFKLDKSGNTAYRTDIQLGRQNPEYYEVLNGLKPGDKVVVSSYETYDKIQELNIKH

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Crispr_ID: NZ_CP049246_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP049246_2

190360-190475

Unclear

Consensus_repeat	Method
TTTTAGGCACAAGAGATCCTCCGCACAGGCCT	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP049246_2

>merge|NZ_CP049246|2|190360-190475|CRISPRCasFinder
TTTTAGGCACAAGAGATCCTCCGCACAGGCCTGGCGCACAACTCTTGCGCCAGCGGGTGGCTCAGTAATAAAAAGGGGGAAGATTTTGAGGCACAAGAGATCCTCCGCACAGGCCT

>NZ_CP049246|2|2|190360-190475|CRISPRCasFinder
TTTTAGGCACAAGAGATCCTCCGCACAGGCCT	GGCGCACAACTCTTGCGCCAGCGGGTGGCTCAGTAATAAAAAGGGGGAAGAT
TTTGAGGCACAAGAGATCCTCCGCACAGGCCT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP049246.1\|WP_103904741.1\|201066_204273_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|225519
NZ_CP049246.1\|WP_103904724.1\|182344_183340_+\|sugar-phosphate-isomerase/epimerase	unknown	unknown	gnl\|CDD\|224007
NZ_CP049246.1\|WP_103904736.1\|197389_197773_+\|molecular-chaperone-DnaK	unknown	unknown	gnl\|CDD\|274124
NZ_CP049246.1\|WP_103904731.1\|188851_189535_-\|zinc-metallopeptidase	unknown	unknown	gnl\|CDD\|377289
NZ_CP049246.1\|WP_103904725.1\|183464_183965_-\|5-(carboxyamino)imidazole-ribonucleotide-mutase	unknown	unknown	gnl\|CDD\|376377
NZ_CP049246.1\|WP_103904722.1\|180948_181653_+\|UMP-kinase	unknown	unknown	gnl\|CDD\|239787
NZ_CP049246.1\|WP_146060557.1\|187972_188674_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP049246.1\|WP_103904729.1\|186427_187771_-\|signal-recognition-particle-protein	unknown	unknown	gnl\|CDD\|236780
NZ_CP049246.1\|WP_103904732.1\|190653_191244_-\|sigma-70-family-RNA-polymerase-sigma-factor	unknown	unknown	gnl\|CDD\|183566
NZ_CP049246.1\|WP_103904738.1\|198546_199497_+\|M20/M25/M40-family-metallo-hydrolase	unknown	unknown	gnl\|CDD\|349913
NZ_CP049246.1\|WP_103904723.1\|181680_182244_+\|ribosome-recycling-factor	unknown	unknown	gnl\|CDD\|178850
NZ_CP049246.1\|WP_103904733.1\|191482_192754_-\|serine-hydroxymethyltransferase	unknown	unknown	gnl\|CDD\|234571
NZ_CP049246.1\|WP_103904739.1\|199484_200408_+\|SDR-family-oxidoreductase	unknown	unknown	gnl\|CDD\|187564
NZ_CP049246.1\|WP_103904734.1\|193041_193395_+\|iron-sulfur-cluster-assembly-accessory-protein	unknown	unknown	gnl\|CDD\|223393
NZ_CP049246.1\|WP_103904727.1\|185138_185651_-\|NADH-quinone-oxidoreductase-subunit-B	unknown	unknown	gnl\|CDD\|235797
NZ_CP049246.1\|WP_103904726.1\|183987_185130_-\|5-(carboxyamino)imidazole-ribonucleotide-synthase	unknown	unknown	gnl\|CDD\|235674
NZ_CP049246.1\|WP_103904728.1\|185650_186235_-\|NADH-quinone-oxidoreductase-subunit-A	unknown	unknown	gnl\|CDD\|376344
NZ_CP049246.1\|WP_103904740.1\|200409_200937_+\|acyl-CoA-thioesterase	unknown	unknown	gnl\|CDD\|224523
NZ_CP049246.1\|WP_103904735.1\|193972_197386_+\|isoleucine--tRNA-ligase	unknown	unknown	gnl\|CDD\|235681
NZ_CP049246.1\|WP_103904737.1\|197828_198479_+\|lipoprotein-signal-peptidase	unknown	unknown	gnl\|CDD\|237816

Protein	Function_ID	Function_description	E-value
NZ_CP049246.1\|WP_103904724.1\|182344_183340_+\|sugar-phosphate-isomerase/epimerase	gnl\|CDD\|224007	COG1082, IolE, Sugar phosphate isomerases/epimerases [Carbohydrate transport and metabolism].	6.56756e-20
NZ_CP049246.1\|WP_103904736.1\|197389_197773_+\|molecular-chaperone-DnaK	gnl\|CDD\|274124	TIGR02420, RNA_polymerase-binding_transcription_factor_DksA, RNA polymerase-binding protein DksA. The model that is the basis for this family describes a small, pleiotropic protein, DksA (DnaK suppressor A), originally named as a multicopy suppressor of temperature sensitivity of dnaKJ mutants. DksA mutants are defective in quorum sensing, virulence, etc. DksA is now understood to bind RNA polymerase directly and modulate its response to small molecules to control the level of transcription of rRNA. Nearly all members of this family are in the Proteobacteria. Whether the closest homologs outside the Proteobacteria function equivalently is unknown. The low value set for the noise cutoff allows identification of possible DksA proteins from outside the proteobacteria. TIGR02419 describes a closely related family of short sequences usually found in prophage regions of proteobacterial genomes or in known phage. [Transcription, Transcription factors, Regulatory functions, Small molecule interactions].	4.21202e-14
NZ_CP049246.1\|WP_103904731.1\|188851_189535_-\|zinc-metallopeptidase	gnl\|CDD\|377289	pfam04298, Zn_peptidase_2, Putative neutral zinc metallopeptidase. Zinc metallopeptidase zinc binding regions have been predicted in some family members by a pattern match (Prosite:PS00142), of the characteristic HEXXH motif.	4.22235e-112
NZ_CP049246.1\|WP_103904725.1\|183464_183965_-\|5-(carboxyamino)imidazole-ribonucleotide-mutase	gnl\|CDD\|376377	pfam00731, AIRC, AIR carboxylase. Members of this family catalyze the decarboxylation of 1-(5-phosphoribosyl)-5-amino-4-imidazole-carboxylate (AIR). This family catalyze the sixth step of de novo purine biosynthesis. Some members of this family contain two copies of this domain.	1.04032e-88
NZ_CP049246.1\|WP_103904722.1\|180948_181653_+\|UMP-kinase	gnl\|CDD\|239787	cd04254, AAK_UMPK-PyrH-Ec, UMP kinase (UMPK)-Ec, the microbial/chloroplast uridine monophosphate kinase (uridylate kinase) enzyme that catalyzes UMP phosphorylation and plays a key role in pyrimidine nucleotide biosynthesis; regulation of this process is via feed-back control and via gene repression of carbamoyl phosphate synthetase (the first enzyme of the pyrimidine biosynthesis pathway). The UMP kinase of E. coli (Ec) is known to function as a homohexamer, with GTP and UTP being allosteric effectors. Like other related enzymes (carbamate kinase, aspartokinase, and N-acetylglutamate kinase) the E. coli and most bacterial and chloroplast UMPKs (this CD) have a conserved, N-terminal, lysine residue proposed to function in the catalysis of the phosphoryl group transfer, whereas most archaeal UMPKs appear to lack this residue and the Pyrococcus furiosus structure has an additional Mg ion bound to the ATP molecule which is proposed to function as the catalysis instead. Members of this CD belong to the Amino Acid Kinase Superfamily (AAK).	2.27169e-156
NZ_CP049246.1\|WP_103904735.1\|193972_197386_+\|isoleucine--tRNA-ligase	gnl\|CDD\|235681	PRK06039, ileS, isoleucyl-tRNA synthetase; Reviewed.	0
NZ_CP049246.1\|WP_103904729.1\|186427_187771_-\|signal-recognition-particle-protein	gnl\|CDD\|236780	PRK10867, PRK10867, signal recognition particle protein; Provisional.	0
NZ_CP049246.1\|WP_103904732.1\|190653_191244_-\|sigma-70-family-RNA-polymerase-sigma-factor	gnl\|CDD\|183566	PRK12513, PRK12513, RNA polymerase sigma factor; Provisional.	3.82535e-41
NZ_CP049246.1\|WP_103904738.1\|198546_199497_+\|M20/M25/M40-family-metallo-hydrolase	gnl\|CDD\|349913	cd05663, M28_like_PA_PDZ_associated, M28 Zn-peptidase containing a protease-associated (PA) domain insert and associated with a PDZ domain. Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This subfamily is composed of uncharacterized proteins, many of which contain a protease-associated (PA) domain insert which may participate in substrate binding and/or promote conformational changes, influencing the stability and accessibility of the site to substrate. Proteins in this subfamily are also associated with the PDZ domain, a widespread protein module that has been recruited to serve multiple functions during the course of evolution.	2.71584e-86
NZ_CP049246.1\|WP_103904723.1\|181680_182244_+\|ribosome-recycling-factor	gnl\|CDD\|178850	PRK00083, frr, ribosome recycling factor; Reviewed.	7.7127e-100
NZ_CP049246.1\|WP_103904733.1\|191482_192754_-\|serine-hydroxymethyltransferase	gnl\|CDD\|234571	PRK00011, glyA, serine hydroxymethyltransferase; Reviewed.	0
NZ_CP049246.1\|WP_103904739.1\|199484_200408_+\|SDR-family-oxidoreductase	gnl\|CDD\|187564	cd05254, dTDP_HR_like_SDR_e, dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs. dTDP-6-deoxy-L-lyxo-4-hexulose reductase, an extended SDR, synthesizes dTDP-L-rhamnose from alpha-D-glucose-1-phosphate, providing the precursor of L-rhamnose, an essential cell wall component of many pathogenic bacteria. This subgroup has the characteristic active site tetrad and NADP-binding motif. This subgroup also contains human MAT2B, the regulatory subunit of methionine adenosyltransferase (MAT); MAT catalyzes S-adenosylmethionine synthesis. The human gene encoding MAT2B encodes two major splicing variants which are induced in human cell liver cancer and regulate HuR, an mRNA-binding protein which stabilizes the mRNA of several cyclins, to affect cell proliferation. Both MAT2B variants include this extended SDR domain. 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.	5.86069e-72
NZ_CP049246.1\|WP_103904734.1\|193041_193395_+\|iron-sulfur-cluster-assembly-accessory-protein	gnl\|CDD\|223393	COG0316, sufA, Fe-S cluster assembly scaffold protein [Posttranslational modification, protein turnover, chaperones].	3.56589e-40
NZ_CP049246.1\|WP_103904727.1\|185138_185651_-\|NADH-quinone-oxidoreductase-subunit-B	gnl\|CDD\|235797	PRK06411, PRK06411, NADH-quinone oxidoreductase subunit NuoB.	9.50877e-91
NZ_CP049246.1\|WP_103904726.1\|183987_185130_-\|5-(carboxyamino)imidazole-ribonucleotide-synthase	gnl\|CDD\|235674	PRK06019, PRK06019, phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed.	8.35064e-141
NZ_CP049246.1\|WP_103904728.1\|185650_186235_-\|NADH-quinone-oxidoreductase-subunit-A	gnl\|CDD\|376344	pfam00507, Oxidored_q4, NADH-ubiquinone/plastoquinone oxidoreductase, chain 3.	3.6488e-42
NZ_CP049246.1\|WP_103904740.1\|200409_200937_+\|acyl-CoA-thioesterase	gnl\|CDD\|224523	COG1607, COG1607, Acyl-CoA hydrolase [Lipid metabolism].	5.34928e-55
NZ_CP049246.1\|WP_103904741.1\|201066_204273_-\|hypothetical-protein	gnl\|CDD\|225519	COG2972, COG2972, Predicted signal transduction protein with a C-terminal ATPase domain [Signal transduction mechanisms].	5.55316e-32
NZ_CP049246.1\|WP_103904737.1\|197828_198479_+\|lipoprotein-signal-peptidase	gnl\|CDD\|237816	PRK14788, PRK14788, lipoprotein signal peptidase; Provisional.	2.99093e-85

>NZ_CP049246.1|WP_103904731.1|188851_189535_-|zinc-metallopeptidase
MYWILFIGIMLVSWIVQFRFKSKFKKYSEMPLSSGLSGAEIAQKMLNENGISDVQVISVEGQLTDHYNPANRTVNLSPDVYHGRSVAAAAVAAHECGHAVQHATAYSWLQFRSAMVPIVSVASRLTTWVLLIGVMLMAFTQNPLVLGIGVAALALTTLFSFITLPVEFDASNRALAWLNSAQVTHSTEEHDGAKDALKWAAMTYVVAALSALVTLLYYASILFGRRD
>NZ_CP049246.1|WP_146060557.1|187972_188674_-|hypothetical-protein
MNKQLFLTLLTGAFLSSATAQTDTLYYKLNVFGNLIRETDRKPELQTDPQFFKRVSVRRKGIPDVYEPDYKIEYNSMRLLSNGQLIWERSYPMDLSMDDLLVKLFETGYFQENQTINETVFLKLKGLGIAYDQMGRSKFSVPNDLTGALLEGAVTLQQEGDRVKVRLSNILVNQPSTGSGESFRGSQQIPLENLGVRQGVVEKWFRDYHRKFLNFTFENLFGNILGQDSPDNR
>NZ_CP049246.1|WP_103904729.1|186427_187771_-|signal-recognition-particle-protein
MFSNLQDKLDRAFKVLKGQGNITEINVAETMKEIRKALLDADVNYKTAKTFTDEVKQKALGQNVLSSISPGQLLTKIMSDELTELMGGSVTELETSKNPTVILIAGLNGAGKTTFSGKLANYLKATKGKKPLLVAGDVYRPAAIDQLEVLGEQVGVPVYVDRESTDPIAIAVAGVEAAKKNGQNMVIIDTAGRLAIDEALMKEITAVKDATQPHEILFVVDSMTGQDAVNTAKTFNDRLDFTGVVLTKLDGDTRGGAALSIKSVVNKPIKFIGTGEKMEALDVFHPDRMASRILGMGDVISLVERAQQQFDEKQAAELQKKIRKNKFDFNDFKSQIQQIKKMGNMKDLMGMIPGVGKAIKDIEIEDDAFKPIEAIIDSMTPFERENPDAIDQKRRTRIAKGSGTDINEVNKLMKQFTDMRKVMKQMSNPGMAAKMMRNMPKMPGKPF
>NZ_CP049246.1|WP_103904728.1|185650_186235_-|NADH-quinone-oxidoreductase-subunit-A
MDDPGQISEYGKILMMAIIGFILVSATIFLARVLSPKNPNPIKLSTYECGEDTTGTSWVQFNPRFYVIALVFLLFDVELIFIFPWATVFGQAELNAADARWGWFTLIEMAIFLGVLIVGLIYVWKSGDISWIKPTHKKLTVAVGIPASAYDALNQKAYALRDYKEQEIKEELAEKAASPVKIGFKPKFKKPSTE
>NZ_CP049246.1|WP_103904727.1|185138_185651_-|NADH-quinone-oxidoreductase-subunit-B
MSLDQRLQQNNGVIIAKMDDLLNWARLSSMWPISFGIACCAIEMMGAMAATYDLDRLGVFPRPSPRQSDVMIIAGTVTFKMADRIKKLYEQMPDPKYVISMGSCSNCGGPYWQHGYHVVKGVDKVIPVDVYVQGCPPRPEALISAFLELQKIIEQQSLLKGDIFPMEVEQ
>NZ_CP049246.1|WP_103904726.1|183987_185130_-|5-(carboxyamino)imidazole-ribonucleotide-synthase
MAKDFYGDLRLGILGGGQLGRMLIQEAINFNVNIHVLDPDPNAPCKKLCNQFEVGSLSDFDTVYNFGKDLDMITIEIEKVNVDALEKLEDEGVLVYPQSRVIRLIQDKGLQKQFFKQNDIPTSAFQFISNRDGLANCQIALPYIQKLRKDGYDGKGVKKISSSADYADAFDAPSIVEEMVDFEKEIAVIVARNDRGDMATFPMVEMEFNPQANLVEFLISPSTYSFDIQSKAESIALKIANDLQIVGVLAVEMFLTKDGDILVNELAPRPHNSGHQTIEGNFTSQFGQHLRAIFNLPLGNTESRANAIMVNLLGEEGYEGLAEYDGIEEALSIEGVYVHLYGKKYTKPFRKMGHVCIINQDRALAIENARKVQELIKVIA
>NZ_CP049246.1|WP_103904725.1|183464_183965_-|5-(carboxyamino)imidazole-ribonucleotide-mutase
MENTKVSVIMGSKSDLPVMQDAIEVLKYLGVTCEVSIVSAHRTPKRMFDFAEQAASRGIKVIIAGAGGAAHLPGMVASITTLPVIGVPVKSSNSIDGWDSVLSILQMPNGIPVATVALNAAKNAGILAAQILATSDEALVQRIQEFKDELREKVEETAEEVERLRF
>NZ_CP049246.1|WP_103904724.1|182344_183340_+|sugar-phosphate-isomerase/epimerase
MAQSRRNFLKLAGLGLVGGLVAPHLISCESMKNAPGSPLKNIGLQLFTLRDLLAQDPKQVLKSVAGIGYTHVETYGADPTNGTLWGVSVDELKKILNDNNLKSHSGHYDLGKYLDKDSKDKENIEKYIEIAHNLGQQYIIAPVPPMHRLNQLNQSDYQYMAEQLNKAGEMSEKAGITMGYHNHFWEFKQFGNNTNGLDVLLAFTDPKLVVFELDMYWISKAGERPQKYFEHHKGRFPLWHIKDMDRNFSVPLEQNKINPKTGKPDTLDMMETMKDIKYAEVGTGSIDFINLAQYANESGLKYAFVEQDEIYSNDKYGSIKKSFDYMQKNFK
>NZ_CP049246.1|WP_103904723.1|181680_182244_+|ribosome-recycling-factor
MNELISLQLDDSKESMAKAIAHTENELTKIRAGKASPGMLDGIYVDYYGTSTPLAQVANVNTPDARTIVVQPWEKSLLSAIEKSIMDSNIGLNPQNDGSIIRLAVPPLTEERRRDLVKKVKEEAEKGRVAIRNIRKDGNEAIKKLKNDGISEDEIKSGEAEVQKLTDAYIVKVDQLADLKEKDIMTV
>NZ_CP049246.1|WP_103904722.1|180948_181653_+|UMP-kinase
MKYKRILLKLSGEALMGEQSYGIDINRVQQYAQDIQELHSLGMEIAIVIGGGNIYRGLSAEKAGMDRVQADYMGMLATVINSMALQDALEKEGMKTRLLTAIKMEQICEPFIRRRAVRHLEKGRIVIFGAGTGNPYFTTDTAASLRAIEINADAVLKGTRVDGIYTADPEKDPNAKKFDHISFTDVYEKGLNVMDMTAFTLCQENNLPIIVFDMNKPGNLMKLANGEHVGTVVS
>NZ_CP049246.1|WP_103904732.1|190653_191244_-|sigma-70-family-RNA-polymerase-sigma-factor
MKLLNKKSDQELVQAYVKGEEKALQVLLERYKTKIYTSIYHQVKDQYLAEDIFQETFIKVINTLKAGRYNDEGKFLPWVMRIAHNMVIDHFRREKRAPNVINNDGFDIFEVLQFSDDSVEARMVKDQRDVDLKRIIQLLPDDQKEVLIMRLFCDMSFKDIADITEVSINTALGRMRYALSNLRKMIEENNMMFQLG
>NZ_CP049246.1|WP_103904733.1|191482_192754_-|serine-hydroxymethyltransferase
MERDQSIFNLIADELKRQEEGIELIASENFVSKQVMEAAGSVLTNKYAEGLPGKRYYGGCEVVDKIETIAIDRAKELFGAEWVNVQPHSGAQANAAVFLAILKPGDKILGFDLSHGGHLTHGSPANFSGKLYQPLFYGVKEDTGLIDYETLEETARKEKPKVIICGASAYSRDWDYARIRKVADEIGALVVADISHPAGLIARGLLNDPLPHCHIVTTTTHKTLRGPRGGMIMVGKDFENPWGIKTPKGEVRTITQLLDLAVFPGTQGGPLEHTIAAKAIAYGEALSDEYLTYIQQVKKNAAALAQFFVEKDYKIISGGTDNHLMLVDLRNKDISGKEAEAVLGLAGITTNKNMVPFDSRSPFVTSGVRFGTAAITTRGIKENEIIQIGELIDEAINNRSDEAALDRIHGKVREMMAQFPLYK
>NZ_CP049246.1|WP_103904734.1|193041_193395_+|iron-sulfur-cluster-assembly-accessory-protein
MASENLTAAAPVTLTEGALNELKKLIDQQEIGPDFGLRVGVEGGGCSGMSYILGFDQKKDGDSEYEVEGIRLFMNKAHGLYLAGMEIDFKNGLDARGFTFNNPNATSTCGCGSSFSA
>NZ_CP049246.1|WP_103904735.1|193972_197386_+|isoleucine--tRNA-ligase
MYKEYKQLNLSEIGKEVLKRWDANNIFEKSISNRPASKPYTFYEGPPSANGMPGIHHVMARTIKDIFCRYKTLKGYQVKRKGGWDTHGLPIELAVEKTLGITKEDIGKKISVEEYNNACRKEVMKYTDVWNDLTEKMGYWVDLEDPYITYQNEYIETLWFLLKDLYKKGLLYKGYTIQPFSPAAGTGLSSHELNQPGTYKDVKDTTIVAEFRLDKQQIHPMMERLVDNPDEDVAFLAWTTTPWTLPGNSALTVGKNIDYVKIKTFNQYTGTAVSVILAKNLIPKHFKSEGQQISFQDYKFGDKLIPWEVVAEFKGAEIEGLRYHQLMPYVTSEELREKAFRVILGDFVTTEDGTGIVHTSPTYGADDFRVARESGIPSIMVKDENGKEVPTVDRTGRFVKEITDFAGRFVKEEYYSDAERADKDFRPTDVLIAIKLKEENKAFDVKKYEHTYPHCWRTDKPVLYYPLDSWFIKTTAVKEEMVALNKTINWKPEATGSGRFGNWLENLVDWNLSRSRYWGTPLPIWRSEDENEEICIGSMPELKALLEASLASDVLSVEERNTNQAYLDKFGTPDLDLHRPYVDDIVLVSEGGQKLYREPDLIDVWFDSGAMPYAQWGLDYEKLEKGEALPFKDPYFSAFPADFIAEGVDQTRGWFFTLHAISTMVRGSVAFKNVVSNGLVLDKNGNKMSKRLGNGVDPFATIDKYSADATRWYMISNAAPWDNLKFNEEGLDEVRRKFFGTLYNTYAFFALYANIDKFSYAEPEIPIEKRPEIDRWVISLLNSLSKEVDEYYADYEPTKAARAIQNFVDEHLSNWYVRLCRRRFWKGEYSEDKISAYQTLYTCLDTIAKLIAPVSPFFADQLYLDLNAATQKESFESVHLADFPAYHIELVDKALEERMALAQDISSLTLSLRKKTGINVRQPLSKILVPVLDSSFQAKVEKVKDLILSETNIKDIEFITDTTGIIKKKVKPNFKVLGAKVGKDMKLVAAAIQALDAAQIQDLENNGSLALSGTEYVISSEDVEIIAEDVEGWQVANLGRLTVALDVHISAELKDEGIARELINRIQNLRKEKNFEVTDRINVALSQNTEIQQAVENNFSYICTEILADRLIFDADLANGDAIEIDGENLLLFIEKI
>NZ_CP049246.1|WP_103904736.1|197389_197773_+|molecular-chaperone-DnaK
MGNTEKTRYSDAELQEFKAIILEKLRVAKEELSSLTTSLSNSNANGTDDTAGTYKTLEDGSATLEKEQINQLAARQKKFIDNLEAALVRIENKTYGVCRETGKLIQKERLKAVPHTTLSIEAKNKQY
>NZ_CP049246.1|WP_103904737.1|197828_198479_+|lipoprotein-signal-peptidase
MKGYSKPLILITIILLVDQLSKFWVKMNMTIGQNFKVLGDKFLIHFIENPGMAYGMEFGGEYGKLFLSVFRIIAVIGIGYGLHYMIKNKYNRGFILNVALIFAGALGNIIDSAFYGLIFSESTPYSKAVLFPDGGGYASFLHGKVVDMLYFPLVSGTFPTWFPIWGGENFMFFRPVFNIADSAISVGVFLILIFQKRYFKEEHTEKTGVNSEILED
>NZ_CP049246.1|WP_103904738.1|198546_199497_+|M20/M25/M40-family-metallo-hydrolase
MKNFRIVFSVVLSLLCLAGGHTTQAQVNPQNLQKHIDYLSTDRMKGRETGQKGSKKAASYIEKYFKKYNLQPKGEKGYRQEFMAQVRRGKATGQQRKSENIIGFLDNKAPYTIVVGAHYDHLGLGDIGGSRDSLGVGKIHNGADDNASGVAGLLELARHYATNSVQESYNMLFIGFGAEELGLVGSKYFTEHPTIPLDSVQWMLNMDMIGRYSPENGLAIIGYGTSSAFPKIFEGLSSSITFNLSKDGNGGSDQTSFYKKNIPVLFFHTGGHDDYHKPTDDADKIDYKAMEAILNLEIQVIDNSMKQPKMDFQWTN
>NZ_CP049246.1|WP_103904739.1|199484_200408_+|SDR-family-oxidoreductase
MDKLSTRILLTGSNGFLGQKLTDHLTERKDVELCCTSQSANRNPNTSGYTFVELDLRDGKQLEKLIHYFKPTHIIHTAALTSVEICEQDPEGCKALNVDVVAHLANICREDDIHLTFLSTDFVFDGQNGPYDERAATNPCNAYGQSKLDAERAILASGCRAAILRTILVYGIIADRGRSNLVLWAKGKLEAGEPINVVSDQWRMPTFVDDLANACILAVERNAEGVFHISSDQMLTIQEAVEQVADYWQLDKTLISSITAKEIGQDKNRPQKTGFILDKAKQELGYQPTPFQASLSAIDQQLKLFRK
>NZ_CP049246.1|WP_103904740.1|200409_200937_+|acyl-CoA-thioesterase
MQEKYARESYTEMNELVLPNDTNTFGNLMGGRLLYWMDICSAMAAQKHCNNQVVTVSVDNVSFKRSIKLGEVVTIEAQVTRAFNTSVEVRMEIFAQNLPQGTKVKSNEAYYTFVSIDEENRPKPIPKLIPETDKEKTLFDEALQRREMRLLLAGKLKPEDADGIKNLIQVFQHKD
>NZ_CP049246.1|WP_103904741.1|201066_204273_-|hypothetical-protein
MKYICYCLILMLCCSQIRLSAQERSYTFLHFTEKDGLSSNVIADLVQDSSGMIWITSKRGLSYFDGKRFHHVQLRSNPDLSTNYLGNMAIDSKNRIWITTNTRGLLCYDRSLPLDQEIKVYAAKIAASGLTKTNLYDVMVSRTGLVYFSGQETDLQVLDPETDIIRQLPFKGIKGPKQVSIYRIEEHSDGSIWLGTRYHGLIRYSPKDGTYQQIDLQNDGENGVAGFVFGSDHFFAGYYDYDLISANYTFQDLQTRLLDWSTNQNYYDNFITTMCYVPSEQALVLGHVSNGLWRFDPRTKIKTHIRWDDLMPDLPKSSRVHALCAVDSGFWVGTESGLFFYSSHRNRINQLIPPKKSEKPILQLLQWHNAIWYRTENSFGRMSPDLKNRLSATSLQGIAVSNWNATQDALYFSTYDQGVYSYTHTAKQLIPLPIKGDSQHFRRADCNVVLQDSIAGYNYLWIGAWNSGIYRYDLTKKTIRLFGPREGLPDHKVISIGKDGDGTIWLGMDGYGLVKMDNKLHPTFTQYTHTTQGSDNLQSNTVLSFFLDAKKRFWYGSGASGIGEIVKTPQGYSFRHYRDLSAAPYLYPTWIGADQQQQLWIKALDGTMIFHPEHKQFVHLKAGDGSYPNSTYKSYGYLIDGNQLIWCTDKGLLVGMLPDLFRNQIRGLQPKISRFQLDHNDESYRLYGSEIDLKAGENNISFAYGLPAQVNREGLRFAYMLEGQDMDWILGSDEQAAYYNNLEGGHYTFKVRVGDALGNWSPAVATVGVHLDRYWYATLWFKLLMVGLLVLLISLFYRYRLREHKRIHQLQVDYNTKLEADLAVKVQTIQEQAAAMERDRQEKLETEYKQKLYESELKAIRSQMNPHFIFNVLNSIEAYVVENDSHNASQLIQKFATLSRIVLENSQYAMVSLRSEIQLLSLYLELERERFNQGFDFEIQYDRALNMEGYSIPSMLIQPLVENAVHHGIRNKHPDQGNVLVDIQVADYAVHITIWDNGIGFEKSEGKGKRGFKSNSFGIKGVQERIMIINQAWKPDSACLEINVGEMRPGFTTKVYLRLPLEVGPGMG

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Crispr_ID: NZ_CP049246_3

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP049246_3

500658-500791

Orphan

Consensus_repeat	Method
GTGACCCTCTGCTTGTAAGGCAGATGCTCTGAACCAGCTGAGCTAA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP049246_3

>merge|NZ_CP049246|3|500658-500791|CRISPRCasFinder
GTGACCCTCTGCTTGTAAGGCAGATGCTCTGAACCAGCTGAGCTAAGCCTCCTTTTTTATTTTGGTGGAGAATACTGGATTCGAACCAGTGACCCTCTGCTTGTAAGGCAGATGCTCTGAACCAGCTGAGCTAA

>NZ_CP049246|3|3|500658-500791|CRISPRCasFinder
GTGACCCTCTGCTTGTAAGGCAGATGCTCTGAACCAGCTGAGCTAA	GCCTCCTTTTTTATTTTGGTGGAGAATACTGGATTCGAACCA
GTGACCCTCTGCTTGTAAGGCAGATGCTCTGAACCAGCTGAGCTAA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP049246.1\|WP_103904989.1\|510956_511409_-\|flavin-reductase	unknown	unknown	gnl\|CDD\|214900
NZ_CP049246.1\|WP_103904980.1\|498231_498939_+\|DUF1080-domain-containing-protein	unknown	unknown	gnl\|CDD\|368908
NZ_CP049246.1\|WP_103904987.1\|507507_508596_-\|LLM-class-flavin-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|366009
NZ_CP049246.1\|WP_103904979.1\|497586_498108_+\|NAD(P)H-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|377026
NZ_CP049246.1\|WP_103904978.1\|496570_497371_-\|ParA-family-protein	unknown	unknown	gnl\|CDD\|379293
NZ_CP049246.1\|WP_160003598.1\|500900_501338_-\|acyl-CoA-thioesterase	unknown	unknown	gnl\|CDD\|223894
NZ_CP049246.1\|WP_103904985.1\|504530_506690_-\|indolepyruvate-ferredoxin-oxidoreductase-subunit-alpha	unknown	unknown	gnl\|CDD\|226684
NZ_CP049246.1\|WP_103904975.1\|494139_494883_-\|4-hydroxy-tetrahydrodipicolinate-reductase	unknown	unknown	gnl\|CDD\|234595
NZ_CP049246.1\|WP_103904977.1\|495645_496569_-\|ParB/RepB/Spo0J-family-partition-protein	unknown	unknown	gnl\|CDD\|275105
NZ_CP049246.1\|WP_103904988.1\|508638_510939_-\|bifunctional-salicylyl-CoA-5-hydroxylase/oxidoreductase	unknown	unknown	gnl\|CDD\|236203
NZ_CP049246.1\|WP_103904974.1\|492693_494136_-\|signal-peptidase-I	unknown	unknown	gnl\|CDD\|182787
NZ_CP049246.1\|WP_103904990.1\|512711_513494_-\|SDR-family-oxidoreductase	unknown	unknown	gnl\|CDD\|236209
NZ_CP049246.1\|WP_103904986.1\|506722_507490_-\|cyclase-family-protein	unknown	unknown	gnl\|CDD\|224790
NZ_CP049246.1\|WP_103905077.1\|490989_491775_-\|TIGR00159-family-protein	unknown	unknown	gnl\|CDD\|224539
NZ_CP049246.1\|WP_103904983.1\|501356_502928_-\|NAD(P)/FAD-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|224154
NZ_CP049246.1\|WP_103904984.1\|502932_504534_-\|indolepyruvate-oxidoreductase-subunit-beta-family-protein	unknown	unknown	gnl\|CDD\|236234
NZ_CP049246.1\|WP_103904976.1\|494899_495646_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP049246.1\|WP_103905078.1\|511429_512674_-\|alanine-phosphoribitol-ligase	unknown	unknown	gnl\|CDD\|380046
NZ_CP049246.1\|WP_103904973.1\|491891_492608_+\|pyridoxine-5'-phosphate-synthase	unknown	unknown	gnl\|CDD\|377117
NZ_CP049246.1\|WP_103904981.1\|499223_499550_+\|hypothetical-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_CP049246.1\|WP_103904989.1\|510956_511409_-\|flavin-reductase	gnl\|CDD\|214900	smart00903, Flavin_Reduct, Flavin reductase like domain. This entry represents the FMN-binding domain found in NAD(P)H-flavin oxidoreductases (flavin reductases), a class of enzymes capable of producing reduced flavin for bacterial bioluminescence and other biological processes. This domain is also found in various other oxidoreductase and monooxygenase enzymes... This domain consists of a beta-barrel with Greek key topology, and is related to the ferredoxin reductase-like FAD-binding domain. The flavin reductases have a different dimerisation mode than that found in the PNP oxidase-like family, which also carries an FMN-binding domain with a similar topology.	1.04797e-42
NZ_CP049246.1\|WP_103904980.1\|498231_498939_+\|DUF1080-domain-containing-protein	gnl\|CDD\|368908	pfam06439, DUF1080, Domain of Unknown Function (DUF1080). This family has structural similarity to an endo-1,3-1,4-beta glucanase belonging to glycoside hydrolase family 16. However, the structure surrounding the active site differs from that of the endo-1,3-1,4-beta glucanase.	3.39556e-50
NZ_CP049246.1\|WP_103904987.1\|507507_508596_-\|LLM-class-flavin-dependent-oxidoreductase	gnl\|CDD\|366009	pfam00296, Bac_luciferase, Luciferase-like monooxygenase.	2.20367e-60
NZ_CP049246.1\|WP_103904979.1\|497586_498108_+\|NAD(P)H-dependent-oxidoreductase	gnl\|CDD\|377026	pfam03358, FMN_red, NADPH-dependent FMN reductase.	6.86399e-27
NZ_CP049246.1\|WP_103904978.1\|496570_497371_-\|ParA-family-protein	gnl\|CDD\|379293	pfam13614, AAA_31, AAA domain. This family includes a wide variety of AAA domains including some that have lost essential nucleotide binding residues in the P-loop.	1.02374e-96
NZ_CP049246.1\|WP_103904975.1\|494139_494883_-\|4-hydroxy-tetrahydrodipicolinate-reductase	gnl\|CDD\|234595	PRK00048, PRK00048, dihydrodipicolinate reductase; Provisional.	2.47174e-56
NZ_CP049246.1\|WP_160003598.1\|500900_501338_-\|acyl-CoA-thioesterase	gnl\|CDD\|223894	COG0824, FcbC, Predicted thioesterase [General function prediction only].	3.23842e-21
NZ_CP049246.1\|WP_103904977.1\|495645_496569_-\|ParB/RepB/Spo0J-family-partition-protein	gnl\|CDD\|275105	TIGR04285, parB-like_partition_protein, nucleoid occlusion protein. This model describes nucleoid occlusion protein, a close homolog to ParB chromosome partitioning proteins including Spo0J in Bacillus subtilis. Its gene often is located near the gene for the Spo0J ortholog. This protein bind a specific DNA sequence and blocks cytokinesis from happening until chromosome segregation is complete.	7.39939e-80
NZ_CP049246.1\|WP_103904988.1\|508638_510939_-\|bifunctional-salicylyl-CoA-5-hydroxylase/oxidoreductase	gnl\|CDD\|236203	PRK08255, PRK08255, bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase.	0
NZ_CP049246.1\|WP_103904974.1\|492693_494136_-\|signal-peptidase-I	gnl\|CDD\|182787	PRK10861, PRK10861, signal peptidase I.	1.76145e-15
NZ_CP049246.1\|WP_103904985.1\|504530_506690_-\|indolepyruvate-ferredoxin-oxidoreductase-subunit-alpha	gnl\|CDD\|226684	COG4231, COG4231, Indolepyruvate ferredoxin oxidoreductase, alpha and beta subunits [Energy production and conversion].	0
NZ_CP049246.1\|WP_103905077.1\|490989_491775_-\|TIGR00159-family-protein	gnl\|CDD\|224539	COG1624, COG1624, Uncharacterized conserved protein [Function unknown].	3.46324e-61
NZ_CP049246.1\|WP_103904983.1\|501356_502928_-\|NAD(P)/FAD-dependent-oxidoreductase	gnl\|CDD\|224154	COG1233, COG1233, Phytoene dehydrogenase and related proteins [Secondary metabolites biosynthesis, transport, and catabolism].	9.68902e-97
NZ_CP049246.1\|WP_103904984.1\|502932_504534_-\|indolepyruvate-oxidoreductase-subunit-beta-family-protein	gnl\|CDD\|236234	PRK08312, PRK08312, indolepyruvate oxidoreductase subunit beta family protein.	0
NZ_CP049246.1\|WP_103904990.1\|512711_513494_-\|SDR-family-oxidoreductase	gnl\|CDD\|236209	PRK08265, PRK08265, short chain dehydrogenase; Provisional.	8.95125e-87
NZ_CP049246.1\|WP_103905078.1\|511429_512674_-\|alanine-phosphoribitol-ligase	gnl\|CDD\|380046	pfam17885, Smoa_sbd, Styrene monooxygenase A putative substrate binding domain. This domain is found in the 46 kDa FAD-specific styrene epoxidase (SMOA) protein, comprises a part of the styrene monooxygenase (SMO) two-component flavoprotein monooxygenase enzyme. Structural analysis indicates that SMOA monomer comprises two globular domains spanned by a long alpha-helix. This domain contains a putative substrate binding site.	3.82389e-59
NZ_CP049246.1\|WP_103904973.1\|491891_492608_+\|pyridoxine-5'-phosphate-synthase	gnl\|CDD\|377117	pfam03740, PdxJ, Pyridoxal phosphate biosynthesis protein PdxJ. Members of this family belong to the PdxJ family that catalyzes the condensation of 1-deoxy-d-xylulose-5-phosphate (DXP) and 1-amino-3-oxo-4-(phosphohydroxy)propan-2-one to form pyridoxine 5'-phosphate (PNP). This reaction is involved in de novo synthesis of pyridoxine (vitamin B6) and pyridoxal phosphate.	8.92621e-129
NZ_CP049246.1\|WP_103904986.1\|506722_507490_-\|cyclase-family-protein	gnl\|CDD\|224790	COG1878, COG1878, Kynurenine formamidase [Amino acid transport and metabolism].	4.19024e-63

>NZ_CP049246.1|WP_103904981.1|499223_499550_+|hypothetical-protein
MGKCQIKILAKNDMGFISMPAGQNIIHVCFNNLLINFSKEDFFTFRNLVKDIFDDNKPIVFPDGKNRILLHTPYEGINFSFDQFEMLELVKTLDEAFYMEKIYSYLEN
>NZ_CP049246.1|WP_103904980.1|498231_498939_+|DUF1080-domain-containing-protein
MSTLLNKSWLLVPFLLVLSCTQSTNQSKSEGNREFFNGQDLAGWHIYNKGAAESKWKVADGELICDPTAPGEFGDIISDREYENFELEFEWKVKKGGNSGVFINVKEDSTYAATFATGLEMQLLDNANAEHRHQIDSTHWAGCLYSVECIGSNSKPNPFGEWNKGKIKQQNGTVTFWLNDRITFEDDVNSTAFKNKVANSNMKNYPAFGTFPKGKIAFQNHTDSVSFRNIRIQEL
>NZ_CP049246.1|WP_103904979.1|497586_498108_+|NAD(P)H-dependent-oxidoreductase
MNLIISGTNRKHSNSLKVAKFYQKEFRNRGEEFEILSLEDLPADIINTDLYGKRSPEFAEIQQMVSEAKKFVFIIPEYNGSYPGVLKVFVDACAFPASFFHKKAALVGLSTGKYGNIRGVDHFTGVCNYVRLHVLPLKIHIPLIQNEINQEGDFTDPLTLKFITEQIEEIVRY
>NZ_CP049246.1|WP_103904978.1|496570_497371_-|ParA-family-protein
MGKIIAIANQKGGVGKTTTSINLAASLAVLEYKTLLVDADPQANSTSGIGFDPRGIKTSIYECLVNDVTAREAIQQTDTPNLDLLPAHIDLVGAEIEMINLEEREYKMKRLLDEVKDAYDFIIIDCSPSLGLITINALTASDSVIIPVQCEYFALEGLGKLLNTIKIVQTRLNTDLEIEGILLTMYDVRLRLSNQVVEEVRTHFNDLVFDTIIQRNTRLSEAPSFGVSVIMHDASCKGAVNYLNLAREILEKNGLLKENNKETVTV
>NZ_CP049246.1|WP_103904977.1|495645_496569_-|ParB/RepB/Spo0J-family-partition-protein
MAAQQRKTGLGKGLGALLQQEVVETPKGQTAETPVAKTSSSPAGSINFIKIDQVSINPFQPRTDFDEQALRELSESIELQGLIQPITVRQIGKNEYQLISGERRLRASKLAGITEIPAYVRTANDQQMLEMALIENIQRENLNAIEIALSFQRMIEECSLKQEELGDRVSKNRSTVTNYLRLLKLPPVIQAAIRDGDLTMGHARALINVGEVEKQLFIFKEIVEKGLSVRKAEELVREVQQARDKKQKGAKKETPLTFQYQKIEDDLASKFATRVKLNVKTNKGKGAIEIPFDSEDDLSRILELLDW
>NZ_CP049246.1|WP_103904976.1|494899_495646_-|hypothetical-protein
MHKLGLLFGLMLLFTGAMGQVKDTIPDSTKMVQLQDSLKAGDAQDTTRKETRAERRARKKAEKEREKYYYKDILKDSTRLEIERLSRVAWKRSLILPGWGQYTNGGIWWVKTPIIYGGFVAAYLTFDYWNWYYNMFLDELKYREEFGQPSSGPLGFETNWSDQGLIAQKDYGRRNRDLTILVTVGWYGLNVVEAYVDSILKNRWNISNDLSFKISPTLMPNYAYTPGTGMFSGTSFVTPGVKMTFKIR
>NZ_CP049246.1|WP_103904975.1|494139_494883_-|4-hydroxy-tetrahydrodipicolinate-reductase
MKIVLLGYGKMGQLIERFAMKRGHEVVLIVDEQNRSSIQVDDLEDADIAIDFSTPNAALENISLCFEADLPLVVGTTGWYEHLEEVKETCLEANQSLLYGSNFSIGVNIFFHINKMLAKAIEPYKQYDVQVEEIHHIHKLDAPSGTAITIAEGILEHIPAKQSWVNSVEGSGEEVIPKPNELLIESLRIEEVPGTHTVLYSSEVDQIEFKHTAHSREGFALGAVIAAEWLLGKKGFFQVTEMFDFNK
>NZ_CP049246.1|WP_103904974.1|492693_494136_-|signal-peptidase-I
MWYIILAIYIIGSLYGLFLLYKKAGRQGWEAIVPFYAQYVMAQLVGRPTWWIVWLFVPIVNIFIFYDLYLNLIKAFGKRRFWENAAAVLVPFIVLPMWGRDPNVKYLGQSTTEEFKKKYPYKKSVGREWADAIIFATVAATLIRGFLIEAYMIPTGSMERSLLVGDFLFVSKLNYGPRIPMTPIAFPFAHHTMPVTGGKAYSEIIKVPYKRLPGFQEIKRNDVVVFNYPVEADEPYNRPVDKRENYIKRCVGMPGDIVSMERTKLFVNGKPAFEDDDFQTNYQVFTDPNGLNLQKLLDMRVELDPLYTNPSEGIYGMHMTKGEAAEIKSWASVKEVREIIFEPGDNNPNFRAFPFYENGIIWNYDNFGPIQVPKKGWTVKLDSLNVPLYQRAITVYEGNNFEQRQDGYYINGLKTDSYTFKMDYYWMMGDNRHNSLDSRGWGFVPEDHIVGKALFTWLSWDEDGSFLTKIRWNRIFRGIR
>NZ_CP049246.1|WP_103904973.1|491891_492608_+|pyridoxine-5'-phosphate-synthase
MTKLSVNINKIATLRNSRGGNVPNVLSAALACERFGAEGITVHPRPDERHIRYQDVYDLKANIATEFNIEGNCREQKFVDLVLANNPTQVTLVPDELGQITSNHGWDTIKYKDYLTDMVKLFQGQGIRVSIFVDPVEDMVEGAAETGTDRIELYTEAYAAEFTANKEAAIAPYIKAAEKAQEVGLGLNAGHDLDLNNLQYFQQHIPGLLEVSIGHALIADALYLGLEETIKRYLAALK
>NZ_CP049246.1|WP_103905077.1|490989_491775_-|TIGR00159-family-protein
MDFNLLSGFRLLDFIDILLVAIIIYYVYSLIKGTIAVNILIGVGLFYGIYLVVKQMEMRLLTEIFGGFISVGSIALIVVFQQEIRRFLLHIGKNISLRRKKFFWTIFGAKKSTHKDNSEFIKPIVEACQNMSKSKTGALLVFSRYFDEEYYQTSGTIIDAPISKRLLETIFFKNSPLHDGAVIVVDNRIMTASSVLPLSDSEDLPPQFGLRHRAAIGVTEVSEAVAVIVSEETGEISFAKDGNINMNLTAEELEKILAEEL
>NZ_CP049246.1|WP_160003598.1|500900_501338_-|acyl-CoA-thioesterase
MAQIFKKQQKVKFQHCDAAGIVFYPRFLEMLNELVEDWFEEELGFPFKELHHGEGVPTADLKVAFSSPARMGDTFEKSMYVSKLGDSSLTYQFKFAFQDRIILRGECVLVHVILSDEKLKAMPWAHQVRMNIERFHHPDGIKDEI
>NZ_CP049246.1|WP_103904983.1|501356_502928_-|NAD(P)/FAD-dependent-oxidoreductase
MNQDVIIIGSGINSLVCAALLAKKGKKVTVIERYPVLGGCVQTEWIEGCHIDTYSTAYPLFVTSAAYPLLKDDLEENGVEFLTNDVPTGVLMSDGQYCILKTDRAANIAAFNALADGDGDRFAAEMDWVNQHADILFTILGGELMTMKMGKFLAKYVWKQGIGQASENAQEFLKSVRADLPDHFQSKALLANLAPWVLHSGLSPESPLSATMAKVTAMSIEMVGLPLVKGGSYRLVDAFKTIIEENGGRFVQNMHVERILVDKYGKAEGVVLEDDSIHLSKYVVANVTPTQLYGRLLVNEPKVSKKVEIQARNYKYGKGNMQIHLILNEAPNWVQPALEKVTYVHLTDGIDDISRAVNEATRQELPAKGTICIAQPTALDPSRAPEGKHILWIQVPECPNYPVADAGGALGDLCQGEWTDELREAYADRIIDRIAAYIPNIKSATVIRKVVSPKDLSRANINLVHGDPYSGQCSLDQYLLWRPMAGVKNHETPIKNLYHIGASTHPGPGLSGASGFLVAQKIK
>NZ_CP049246.1|WP_103904984.1|502932_504534_-|indolepyruvate-oxidoreductase-subunit-beta-family-protein
MSENIKKVVEPIKVALIAVGGDGGGVLTQWIVQLASKNGYWAQSTTIAGVAQRTGSTVYYLELFPEDAIPKDGGKRISPVLAQMPAPEDVDVVMATELIEAGRAIQRGFVSKKTTLIFSTHRNLAIQEKEKPGDGILDGTSIFELARKYAKHSVYANLKDLAENHKSVISATLFGALAASGSLPFSVEQFEETIKAGGVAVPTSLAAFKAAFGLVGLGLSAKEATPYVPELSPAKFEALPASNANRKFNAAIQQIRNEFPESTHEVVYAGIKHVVEWGGISWGNEYLDYLKPILKVERDFRNKDNILTNRVAQYLALAMAYDDLVNVADIKTRAERWDTVFQQVGAKKGEIVKTTDYFHPRFEEVYGFMPVGLGKRMENSESAHRFFTKYLDKDRRMDTHNIFWFFILYCIGGMKGYRKKTLRHAEEIENIADWLERICDISAVNYELAVQLARSYRLKKGYGDTYARGHSKFKMVNEFAVKHVNVRGIADIVSELIEFGLKNHETEQLQGQIALVEAEMENRSSNASEFNNN
>NZ_CP049246.1|WP_103904985.1|504530_506690_-|indolepyruvate-ferredoxin-oxidoreductase-subunit-alpha
MAEKSFKKEVETLRKGAGEVFHGEGILAVTKALLECGVGYVGGYQGSPISHLMDVFADAEPLLEELGVYFENSASEAAAAAMLSASVYYPIRGAVTWKSTVGTNVASDALSNLASGGVTGGTLVIVGEDYGEGSSIMQERTHAFAMKSQIWLLDPRPNLESIVKSVELGFELSEASNSPVILQLRVRSCHLHGQFIARDNQPPKVKISDCLNDPKRDVSRIVLPPATFLHEKEKVEKRLPKAIQFIKDQQINEFLKGDREDIGIIVQGGLFNNLNRALVSLGLSDNLGNVKIPVYVMNVAYPVIPDEVVDFCRDKKSVLMIEEAQPNYIEQNIGYLLHKHHLTTKLYGKNVLPEVGDYTIGVVKEGLVKYFEDIGEELTTAQREVFTKKISEEDNKQLLEKVPVRPAGFCTGCPERPIFAALKIVQERIGQHHIAGDIGCHLFSILPPFNIGATTMGYGLGASSAAAFNLFNTPTQEGQKRPIAIMGDGGFWHNGLTSGIGNAVYNKFDGLIIIIDNYYAAATGGQDIPSSRAYNFLRTTNNPIEKAVKGVGVQYVKIIDRTYDVERMVKELTRALTTKEKGPKVIIAQSECSLNKERRKKRIFKKRVEEGKRVENEKFGVDAKVCTGDHACMRLSGCPSLTLKYTDNPLREDPVAHIEQSCVACGNCGEVAEAAALCPAFYSAKVIRNAGFMEKLIYKIQYGMISFLQKRRASKQIIT
>NZ_CP049246.1|WP_103904986.1|506722_507490_-|cyclase-family-protein
MQSLQALLTGGNIRFVDLTHTLNENFPGLPLPPEMGQVATFKKTEISRYNDKGPGWYWNNITLGEHFGTHFDAPVHWITGKDHPNNTVDTIPTEHFMAAAQIIDASEEVIGNPDFVLTPEFIQKWESEHGILRANEWVLFRTDWHKRPIGAEFLNTGADGLNHTPGPSKEAVEYMINRNVLGFGVETLNTDAGMSFVWDMPLPCHTLMHGAGKYGLQCLRNLDQLPVRGAIIVAAPLKIEDGSGSPLRVFAIVPS
>NZ_CP049246.1|WP_103904987.1|507507_508596_-|LLM-class-flavin-dependent-oxidoreductase
MTEKHPFLKKDKFLLGTFSTNCGGGMTVSKLPDRWRANWENNLKLGLLLDEAGIDFMLPIARWVGYGGETDFHGEVMETITWATALLARTKQITVFATIHTVANHPVVVAKQIATMAQISNDRVGLNIVAGWNKPEYDALGIPLPPDHETRYGYAQEWFNFIKRLWKEEGPFNFDGSYFKTTRSYGNPRPTYLPPIFNAAGSGQGRDFAIENANFLFTPAIDLNRSKAEITELKQKGVDAGKDINVLTFSHIICRPTEEEAQAERQRVMDNIDWSATDNLINLQFAHAQSFPHDLLNSIREGMALGHGGFPMVGTPQQVADGLIALHEAGFKGTTLSFFDYAAEFPYFRDNVLPILAEKGIR
>NZ_CP049246.1|WP_103904988.1|508638_510939_-|bifunctional-salicylyl-CoA-5-hydroxylase/oxidoreductase
MKIAVVGGGPAGMYFSILVKKAMPEVEINIYEQNKLSDSFGFGVVFSDETLSEFLTKDPRSYELIRSKFAYWDNLDVYRDGEVVRITGNGFCGCSRRTLLELLAQRCAEEGVTIHSQYRINSLKDVPESDIIVAADGINSVIRTELQADFGTVVIPKKNKFVWMGSTKPLDAFTYFFKTTAYGPFVAHSYQYEEGKSTWVIETTEETFEKAGFVVDDEAGTRLKLEAIFAQELDGHPLLTNKSHWRSFPLITNTRWHKDNVILLGDAVATAHFSIGSGTKLAMQEAIALAQSVIENKEDVQQIFASYEANFRPHVEAIQNAANISMAWFEGMDRHVEQADFMAFAFSVMSRSRKVTYENQAIRDKAFTQQVLAAFNARTKQKVGQSPAFSTYKLREMNLPNRMVMSAMGQYSAVDGRVQDWHLMHYGSRATGGVGLIITEMTAVSDSGRISPGCAGIYTDEQAQEWERIVDFVHTNSSAKIAMQLGHAGPKGAVQRRWQGAFEPLNGQGWPLKAASAKPYGSGYPIPKAIDRAEMQEIIEQFVSAAKRADQAGFDMIELSACHGMLLASFLSPLTNLRDDEFGGAIENRVKFPVQVFEAIRSVVDSQKPISVKISVEDWKEGGNTINEGIAIAKAFKDAGADLISVTSGGTVPDQEIKEGPMWQVPLADAIKHDVGIPVMAIGQFTTIDQINTTLLADRADLIAMGKTLLVNPGFVLQSAAYEQESLDSLVPDPYRVGIPQLNKTQAWMRKEFERMKVALKPQSHR
>NZ_CP049246.1|WP_103904989.1|510956_511409_-|flavin-reductase
MRAFRNACGKFATGIVVITTEHEGKVHGMTANGFMSVSLDPNLVLISIDNSKRMHQFLHESKKYAISVLAHHQEKWSRHFAGSPQDDLLVEFVDFHGAKVVPEACAYFETSVVSTHIEGDHTLFVGQVNNFACTEDDPILYFKGSYMKLV
>NZ_CP049246.1|WP_103905078.1|511429_512674_-|alanine-phosphoribitol-ligase
MRRIAIVGAGQAGLQTAIGLLKNGGYEVTVFSNRTPEQIRTGKVMSSQCMFDMALSHEREIGINYWDESCPPVQGLGVTVPNPEKPGEKLFTWAGRLEKEAQAVDQRIKMPRLIEELQKLGGKFVVEDVGIESMERMTEDYDLVIVAAGKGEIVRVFERDADRSPFDKPMRALALTYVKNMEPIRPFSKVSFNLIPGVGEYFVFPSETINGDCEIMVFEGVPGGPMDCWGDVTTPEQHLEKSLWILKTFLPWEYERCQNVTLTDDNGVLAGRFAPTVRKPVATLPNGGKVFGIADVVVVNDPITGQGSNNASKCSKVYLDEILAHGDQPYTEAWMNATFEKYYAYAQTVTNWTNSMLTPPPPHILNLMGAASVAQSLADLIANNFSDPSQFTPWWFDADQTEAVIASHMSKVAI
>NZ_CP049246.1|WP_103904990.1|512711_513494_-|SDR-family-oxidoreductase
MRDFEKKVCLLTGAATIGLAIADKFIQLGASVVVGALELGSDVDRKAAYAEQFDFIKTDITSDASLRALLDFTLQKYGRVDVLVNCAAAYADDGPLTSRETWLRTLDTNVVSAAVFGEMVRPYLKASVGNIINIGSVSGVFPHIQRWSYPVSKAALLHLTKTQAVEYAADKIRVNMVRLGHVWSLPFEGLTKNDRAHADEVTSSFNLMGRIANAEEVANVVAFVASAEASYMTGNETVVDGGYSAMGPEQHEPLFPKLAK

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Crispr_ID: NZ_CP049246_4

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP049246_4

676587-676690

Orphan

Consensus_repeat	Method
CATGATATCACAAATCTCAAATCT	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP049246_4

>merge|NZ_CP049246|4|676587-676690|CRISPRCasFinder
CATGATATCACAAATCTCAAATCTCACTTCTCATATCTAATCTTAATACTTAATTCTAACTACTAAATACTTTAAAAACCCATGATATCGCAAATCTCAAATCT

>NZ_CP049246|4|4|676587-676690|CRISPRCasFinder
CATGATATCACAAATCTCAAATCT	CACTTCTCATATCTAATCTTAATACTTAATTCTAACTACTAAATACTTTAAAAACC
CATGATATCGCAAATCTCAAATCT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP049246.1\|WP_103906513.1\|681131_681467_-\|PadR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224609
NZ_CP049246.1\|WP_103906512.1\|679279_681100_-\|PspC-domain-containing-protein	unknown	unknown	gnl\|CDD\|377200
NZ_CP049246.1\|WP_103906509.1\|674434_675844_+\|glucuronate-isomerase	unknown	unknown	gnl\|CDD\|376859
NZ_CP049246.1\|WP_103906515.1\|682046_682742_-\|ComF-family-protein	unknown	unknown	gnl\|CDD\|223970
NZ_CP049246.1\|WP_103906505.1\|666999_669420_-\|TonB-dependent-receptor-plug-domain-containing-protein	unknown	unknown	gnl\|CDD\|238657
NZ_CP049246.1\|WP_103906507.1\|670531_672454_-\|glucosamine-6-phosphate-deaminase	unknown	unknown	gnl\|CDD\|235005
NZ_CP049246.1\|WP_103906502.1\|664567_664984_-\|DUF2147-domain-containing-protein	unknown	unknown	gnl\|CDD\|378304
NZ_CP049246.1\|WP_103906511.1\|676800_679227_-\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|379720
NZ_CP049246.1\|WP_103906504.1\|665632_666985_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP049246.1\|WP_103906519.1\|686286_687372_+\|23S-rRNA-(adenine(2503)-C(2))-methyltransferase-RlmN	unknown	unknown	gnl\|CDD\|223890
NZ_CP049246.1\|WP_103906508.1\|673477_674299_-\|ATP-binding-protein	unknown	unknown	gnl\|CDD\|271333
NZ_CP049246.1\|WP_103906506.1\|669509_670451_+\|helix-turn-helix-transcriptional-regulator	unknown	unknown	gnl\|CDD\|225117
NZ_CP049246.1\|WP_103906510.1\|675846_676434_-\|TIGR00730-family-Rossman-fold-protein	unknown	unknown	gnl\|CDD\|129813
NZ_CP049246.1\|WP_103906503.1\|665133_665481_+\|phage-holin-family-protein	unknown	unknown	gnl\|CDD\|377198
NZ_CP049246.1\|WP_160003744.1\|684717_685596_+\|DUF4349-domain-containing-protein	unknown	unknown	gnl\|CDD\|379526
NZ_CP049246.1\|WP_103906520.1\|687484_688066_-\|tRNA-(ms[2]io[6]A)-hydroxylase	unknown	unknown	gnl\|CDD\|153119
NZ_CP049246.1\|WP_103906514.1\|681657_682041_+\|glycine-cleavage-system-protein-H	unknown	unknown	unknown
NZ_CP049246.1\|WP_160003746.1\|685652_686147_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP049246.1\|WP_103906687.1\|672713_673379_+\|TlpA-family-protein-disulfide-reductase	unknown	unknown	gnl\|CDD\|239264
NZ_CP049246.1\|WP_103906688.1\|682890_683922_+\|LLM-class-flavin-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|274817

Protein	Function_ID	Function_description	E-value
NZ_CP049246.1\|WP_103906513.1\|681131_681467_-\|PadR-family-transcriptional-regulator	gnl\|CDD\|224609	COG1695, COG1695, Predicted transcriptional regulators [Transcription].	5.07232e-20
NZ_CP049246.1\|WP_103906512.1\|679279_681100_-\|PspC-domain-containing-protein	gnl\|CDD\|377200	pfam04024, PspC, PspC domain. This family includes Phage shock protein C (PspC) that is thought to be a transcriptional regulator. The presumed domain is 60 amino acid residues in length.	3.96752e-26
NZ_CP049246.1\|WP_103906509.1\|674434_675844_+\|glucuronate-isomerase	gnl\|CDD\|376859	pfam02614, UxaC, Glucuronate isomerase. This is a family of Glucuronate isomerases also known as D-glucuronate isomerase, uronic isomerase, uronate isomerase, or uronic acid isomerase, EC:5.3.1.12. This enzyme catalyzes the reactions: D-glucuronate <=> D-fructuronate and D-galacturonate <=> D-tagaturonate. It is not however clear where the experimental evidence for this functional assignment came from and thus this family has no literature reference.	0
NZ_CP049246.1\|WP_103906515.1\|682046_682742_-\|ComF-family-protein	gnl\|CDD\|223970	COG1040, ComFC, Predicted amidophosphoribosyltransferases [General function prediction only].	5.96931e-32
NZ_CP049246.1\|WP_103906505.1\|666999_669420_-\|TonB-dependent-receptor-plug-domain-containing-protein	gnl\|CDD\|238657	cd01347, ligand_gated_channel, TonB dependent/Ligand-Gated channels are created by a monomeric 22 strand (22,24) anti-parallel beta-barrel. Ligands apparently bind to the large extracellular loops. The N-terminal 150-200 residues form a plug from the periplasmic end of barrel. Energy (proton-motive force) and TonB-dependent conformational alteration of channel (parts of plug, and loops 7 and 8) allow passage of ligand. FepA residues 12-18 form the TonB box, which mediates the interaction with the TonB-containing inner membrane complex. TonB preferentially interacts with ligand-bound receptors. Transport thru the channel may resemble passage thru an air lock. In this model, ligand binding leads to closure of the extracellular end of pore, then a TonB-mediated signal facillitates opening of the interior side of pore, deforming the N-terminal plug and allowing passage of the ligand to the periplasm. Such a mechanism would prevent the free diffusion of small molecules thru the pore.	3.21053e-35
NZ_CP049246.1\|WP_103906507.1\|670531_672454_-\|glucosamine-6-phosphate-deaminase	gnl\|CDD\|235005	PRK02122, PRK02122, glucosamine-6-phosphate deaminase-like protein; Validated.	0
NZ_CP049246.1\|WP_103906502.1\|664567_664984_-\|DUF2147-domain-containing-protein	gnl\|CDD\|378304	pfam09917, DUF2147, Uncharacterized protein conserved in bacteria (DUF2147). This domain, found in various hypothetical prokaryotic proteins, has no known function.	6.55467e-48
NZ_CP049246.1\|WP_103906511.1\|676800_679227_-\|TonB-dependent-receptor	gnl\|CDD\|379720	pfam14905, OMP_b-brl_3, Outer membrane protein beta-barrel family. This family includes proteins annotated as TonB dependent receptors. But it is also likely to contain other membrane beta barrel proteins of other functions.	2.38228e-106
NZ_CP049246.1\|WP_103906519.1\|686286_687372_+\|23S-rRNA-(adenine(2503)-C(2))-methyltransferase-RlmN	gnl\|CDD\|223890	COG0820, COG0820, Predicted Fe-S-cluster redox enzyme [General function prediction only].	8.97901e-145
NZ_CP049246.1\|WP_103906508.1\|673477_674299_-\|ATP-binding-protein	gnl\|CDD\|271333	cd14963, NHL_like_5, Uncharacterized NHL-repeat domain in bacterial proteins. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.	0.000153745
NZ_CP049246.1\|WP_103906506.1\|669509_670451_+\|helix-turn-helix-transcriptional-regulator	gnl\|CDD\|225117	COG2207, AraC, AraC-type DNA-binding domain-containing proteins [Transcription].	2.28936e-25
NZ_CP049246.1\|WP_103906510.1\|675846_676434_-\|TIGR00730-family-Rossman-fold-protein	gnl\|CDD\|129813	TIGR00730, LOG_family_protein_YJL055W, TIGR00730 family protein. This model represents one branch of a subfamily of proteins of unknown function. Both PSI-BLAST and weak hits by this model show a low level of similarity to and suggest an evolutionary relationship of the subfamily to the DprA/Smf family of DNA-processing proteins involved in chromosomal transformation with foreign DNA. Both Aquifex aeolicus and Mycobacterium leprae have one member in each of two branches of this subfamily, suggesting that the branches may have distinct functions. [Hypothetical proteins, Conserved].	6.6006e-63
NZ_CP049246.1\|WP_103906503.1\|665133_665481_+\|phage-holin-family-protein	gnl\|CDD\|377198	pfam04020, Phage_holin_4_2, Mycobacterial 4 TMS phage holin, superfamily IV. These proteins are predicted transmembrane proteins with probably four transmembrane spans. The 1.E.40 is represented by the mycobacterial 4 phage holin, but it also contains many cyanobacterial. proteobacterial and firmicute proteins. Holins are encoded within the genomes of Gram-positive and Gram-negative bacteria as well as in those of the bacteriophage of these organisms. The primary function of holins appears to be transport of murein hydrolases across the cytoplasmic membrane to the cell wall where these enzymes hydrolyze the cell wall polymer as a prelude to cell lysis. When chromosomally encoded the enzymes are therefore autolysins. Holins may also facilitate leakage of electrolytes and nutrients from the cell cytoplasm, thereby promoting cell death. Some may catalyze export of nucleases.	4.28609e-18
NZ_CP049246.1\|WP_160003744.1\|684717_685596_+\|DUF4349-domain-containing-protein	gnl\|CDD\|379526	pfam14257, DUF4349, Domain of unknown function (DUF4349). This family of proteins is found in bacteria and archaea. Proteins in this family are typically between 282 and 353 amino acids in length. There is a single completely conserved residue D that may be functionally important.	3.32007e-53
NZ_CP049246.1\|WP_103906520.1\|687484_688066_-\|tRNA-(ms[2]io[6]A)-hydroxylase	gnl\|CDD\|153119	cd07910, MiaE, MiaE tRNA-modifying nonheme diiron monooxygenase, ferritin-like diiron-binding domain. MiaE is a nonheme diiron monooxygenase that catalyzes the posttranscriptional allylic hydroxylation of a modified nucleoside in tRNA called 2-methylthio-N-6-isopentenyl adenosine (ms2i6A). ms2i6A is found at position 37, next to the anticodon at the 3' position in almost all eukaryotic and bacterial tRNA's that read codons beginning with uridine. The miaE gene is absent in Escherichia coli, a finding consistent with the absence of the hydroxylated derivative of ms2i6A in this species.	7.75003e-91
NZ_CP049246.1\|WP_103906687.1\|672713_673379_+\|TlpA-family-protein-disulfide-reductase	gnl\|CDD\|239264	cd02966, TlpA_like_family, TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are bacterial protein disulfide reductases with important roles in cytochrome maturation. They are membrane-anchored proteins with a soluble TRX domain containing a CXXC motif located in the periplasm. The TRX domains of this family contain an insert, approximately 25 residues in length, which correspond to an extra alpha helix and a beta strand when compared with TRX. TlpA catalyzes an essential reaction in the biogenesis of cytochrome aa3, while ResA and DsbE are essential proteins in cytochrome c maturation. Also included in this family are proteins containing a TlpA-like TRX domain with domain architectures similar to E. coli DipZ protein, and the N-terminal TRX domain of PilB protein from Neisseria which acts as a disulfide reductase that can recylce methionine sulfoxide reductases.	4.23758e-38
NZ_CP049246.1\|WP_103906688.1\|682890_683922_+\|LLM-class-flavin-dependent-oxidoreductase	gnl\|CDD\|274817	TIGR03858, LLM_2I7G, probable oxidoreductase, LLM family. This model describes a highly conserved, somewhat broadly distributed family withing the luciferase-like monooxygenase (LLM) superfamily. Most members are from species incapable of synthesizing coenzyme F420, bound by some members of the LLM superfamily. Members, therefore, are more likely to use FMN as a cofactor.	0

>NZ_CP049246.1|WP_103906510.1|675846_676434_-|TIGR00730-family-Rossman-fold-protein
MKLKNIVVFCASSPGHGPSFVEAAKVVGQVFVERGIRLVFGGGRVGLMGAVADSVMAHGGSVVGVIPKFLNSKEIGHTGITELIEVDTMHERKTKMNNLCDGVIALPGGFGTMEELFEMTTWGQLGLHKKPIGILNVDGFYDHLINFIQHMVDTGLLKAENQKMILHSDNIEDLLEQMESFEAPPVPKWLNIAST
>NZ_CP049246.1|WP_103906509.1|674434_675844_+|glucuronate-isomerase
MKPFLDDNFLLQSSIAEELYHNYAKDLPIIDYHNHLPPQEVAENKKFKNITEIWLQGDHYKWRAMRANGIPEEYITGQASDRDKFRQWSETVPYTLRNPLYHWTHLELQRYFGVHDLLGPDTADNIFDRATSMLQDEQMRVHGLLEQMKVEVICTTDDPIDSLEYHQAYNEKPGNFAMYPAFRPDKAMSPEIPEVFNTYVEKLAAASNSDINTFQHYLDALKSRHDFFAAQGCCVSDHGLSHLYADDYTATEIAAIFDQVRSGKTLNTDQLNKFKSAMLVQFAEWDHEKNWVQQFHVGAFRNTNTGALQKLGPDTGFDSIGDYRQGDGLVKFLGKMAEKDQLGKTILYNLNAADNDLFAAMAGNFNDGSIAGKMQYGSAWWFHDQKDGMTKQINSLSNIGLISRFVGMLTDSRSFLSFPRHEYFRRLLCNIFAEDVVNGELPNDTKWIGKIIQDICYYNAKAYFPFPKK
>NZ_CP049246.1|WP_103906508.1|673477_674299_-|ATP-binding-protein
MKTSILTLVLACTSLVGFSQSKLTQLWESTEQLPTPESVLYVPGQSALYVSLIDGDGSAKDGKGGVAILNMDGTMKDATWVQGLNAPKGMALYKDLLYVADIDEVVVIDVVTGNVINQVKVPESVFLNDVTVDDNGKVYVSDTRKGEIHLIHNGKSSLFMKDVKDVNGLRVVNGSLYAMAGPELWKIDNNKNKTVIAKGLALGGDGLEPVGDGSFLVTCWGGLIYHIKADGTVTQLLDVRDKMKTADLGYNQKEKILYVPTFLNNSVVAYKLD
>NZ_CP049246.1|WP_103906687.1|672713_673379_+|TlpA-family-protein-disulfide-reductase
MKKLLLLIICLPTFLFAQTKEELINQVKANPADKNSIRIIQKVGGYFPDYNELNTLFKGLDKKVRKSTEGKIFERYLDALKNTMVGKKAPSITQFDLNGDPYSLSDLKGKYVLIDFWASWCPPCREENPKLVKTYAEFKDKNFEILGVSFDKEFTAWEKAIKDDNLTWKHVSDLQGWNNSAGQSYGVKAIPQNLLVDPEGKVIARNLHGEELNAKLRELLK
>NZ_CP049246.1|WP_103906507.1|670531_672454_-|glucosamine-6-phosphate-deaminase
MARLNLLEETRFEKVPVTVYPSQDEASVKVAQRIAGIIQDKQAKGEKAVLGLATGATPIKVYKELVRLHKEEGLSFENVVTFNLDEYYPMQPTAEQSYVAFMEKHLFGHVNIPQENINIPDGTLAPEDVQAFCIAYEQKISNLGGLDIQILGIGRTGHIGFNEPGSAPNSGTRLVTLDDLTRRDASRDFGGKENVPTKAITMGVGTIFKAKEIVLMAWNEKKAEIVKKAVEGEISSDIPATYLQMSDNVEFVLDKDAASALTRFNLPWLAHDVVWEDKLVKKAVVWLSLHLDKAILKLTDDDYNNNGMAQLITEQGPAYSINIRIFNELQRTITGWPGGKPGVDDSNRPERAEPAHKNVILFSPHPDDDVISMGGTFIRLADQGHNVHVAYQTSGNTAVWDDDVLRYLEFVQDFAVAIEDDNGITRNIYDEARAFFKVKQPNQVDPEIIRTIKGLIRKGEAIAGARFVGLPDENIHFMDLPFYDRGKFSKEVDFEDDIQQTMALLREVKPEQVFAAGDFADPHGTHKVCFDIILEALMRLRETDEWTKDCWLWLYRGAWHEYPIHDIEMAVPLSPQEVKRKRLAIFKHQSQKDLPVFPGDDPREFWVRAEDRTSETAGLYHQLGLANYEAIEAFVRWKFN
>NZ_CP049246.1|WP_103906506.1|669509_670451_+|helix-turn-helix-transcriptional-regulator
MTQSEKKISQSEILPPSSLEPARNMQELGTQLYFTVLKGRQRFRFTSPIDGYLNFLLDEDSNHCSVVIANQDYLVQAGENILFHLKKGDQMELKSINSDNNMLLMLIPSDKFPAYHDKYQADETRFRNGMLTKADKRIGLALQQIFHLYLADSYLNQLKIQSLMLDIIIHQVETLYVENENKEILVNKTHFDKIQLAKKMIEEDLSRNHTISELAKAVGTNEQYLKKHFKQYYGKTVMNFITEMKMEHAKRLIMMGKYRISDVARMTGYKHSTHFTTAFKKYFGIIPNSLRYSFLVAHEGILAIPDLISSFTV
>NZ_CP049246.1|WP_103906505.1|666999_669420_-|TonB-dependent-receptor-plug-domain-containing-protein
MKHFYLILLFLLTCTLVFGQTATIRGKVQSTGGKAIAKATVRLEGTKIVSVTNEDGGYELKEVPYGQQHIVVTSVEIQPKRLPVLVESRMHVLPIALELRGDIGLEEVRVEGKTEKRKIETSGFAVNVIETQEAATRNVQTNELLDRTVGVRVRQSGGVGAEVQYNLNGMTGRSVGIFVDGIEISTYGASFNLNNIPPAMIERIEVYKGVLPAHLSGDLLGGAINIVLNKRNVKNNLNASLSYGSFNTTQADVSGFYRDQKTGFTTRISGAFLNSDNDYEIWGKFSKYIEPNGVVRRNFRTKRFFDGYRSATARFEFGFSDVKWADSFFLGYNFSDVYNEIQHGQTMGTPYMGRTSQGQANALNLHYNKRDLFVKGLSLNVNGVYSFRNTAILDTVPWAYNWDGAIRLDLNGKPLKTLTGAQQGKPTHIDIDRQVANIRSNLAYEVFKGHRLSANHVFYTVDRKDTDLLNVVAAQEFRSKNDLSKNVFSFNYEASTLNDRLLTNLFYKLYQQTIGNTWYTSAQVGQQAVAVKEEVRDARTNSGYGLSVSYAIIPKVYLLTSAERAVRMPADSETFGSPEDNVLSNFSIKPEVSDNYNAGFRLGMYEFGNHRLSLSGNAFWRNIKDRIMPKANENISAQEIEVTQFINLGRAQTLGFEGEFTYGYKNKLTAMVNFSKFNSLFKQQYDDEGREMTYYNKQVPNEPFFTINGNVHYRFENLIQRNSQLNMFYTVGYVAPFRTIWPETDWFITPRQWAQNVGASYTFPSRRLIASVDVKNLFNAEVYDNFGVQKPGRGYYLKLSYSLFKF
>NZ_CP049246.1|WP_103906504.1|665632_666985_-|hypothetical-protein
MKATFLKLALMGFAVTAITTTSCTKTGSEPVKEDDNTRWITVSGALMQTTAGDGNGGGRVFSLTVEDAKNPNFEVNVFDGGAEIKSERTARLQASSDGKYLFNIQYLGDDGGVFQKYRVLGGNRISPEGPQVATASYVSKTPRWLKVSDGVGVGVRAEAKASEYTGTFPNLTYVETSAKTDVITLDLKDPKITKTNSFDLKLSPDEVAAGYYVSRIDMPVLNKANNKVFIGVATSKKNTTSPTADDKGVVSYPVDRNAPRIAAKTLVLDYPSLANPKLITSTKTKGSTNGYRAPMQYLGTDGHVYQATSGETAGTGGSRILRINSETNEYDNTFEFNLDKALGITDSYIETWLYTGGGKGFVVYKIAGKGGYFAKIDLNAGTAKKYNLPNEDKLRFGQIQHVGMEGNDVFLAVAPVGENGNIYVFDKNSDKMEKGAKLINKTGNQYIGIY
>NZ_CP049246.1|WP_103906503.1|665133_665481_+|phage-holin-family-protein
MRFIISLLVTGLVVAIASWIIPGVTVAGFGWAILTGLVIGLVNAIVGGILRLFTFPLNWLTFGLVSFIITVLMIMLSDSIMGSKFDVDGFWPAALFAIVVAIIEMIIGKLGSDKK
>NZ_CP049246.1|WP_103906502.1|664567_664984_-|DUF2147-domain-containing-protein
MKQLVATFCALLFTMMVFGQNNDPILGKWENPSGEGRIEIYKKNNKFYGKLYWIKNAGRKDAKNPDPNLRTRDIQGLEILTGFTKKGKTYEDGEIYDPKSGKTYSCKMTLKGDNQLDIRGYMGISLLGRTETWKRITK
>NZ_CP049246.1|WP_103906511.1|676800_679227_-|TonB-dependent-receptor
MGRIIAILILYVASLLNHSYAAARAQDADIKGKVVNPENQPVASASVYLMSSTGNVLIKSAVTDENGAYTILKAPKGNYYIEVTSVGYGKARSAAFDLDDKLVTVEDIKLLPASQTIETVTVQGQMPTVKNVNGKLVLNVENSTLAAGNNALEVVKRAPGVSVDKDDNLQLMGQQGVNVTIDGRLTYMSGEQLATFLKSTDAAQIKSVEVTTTRQAKDDAEGAIGTINIVLKKNNTEGFNGSFVASAGHGKYFRGNSSLALNYKKKNTTLFGSYAYTNNKEINELDIIRDIAGKERTTYFNQEADMIEKNQSHTFRVGVEQKTSNSNTLMFQVSGNNYLEDANNNSITNIGFTPTTIDTVLRSPSIVDMSFGRISFNLNNEYKIDTLGSKLTLDLDYSLFKNRSDMDYVYRTEHPNTGALFYPEEREHSNMPTDIDIYVGKLDYIKPLKKGSLEAGLKYSNVKSDNNMMFERLVGSTWENVEDRTNHFIYTEQISAGYVDYSRPLGKKWSAKVGVRAEYTISDGNLVTNNSTVKRDYLDFFPSANIGYNINENHILSLSYAKKVSRPNYRSLNPFRYYIDKLTYQLGNPYVNPQYTHGFSLNYTLMKMFNFTLGTDITNDAIVESMGQDSIRTWVTKENLGKSVTSYLNMNIPYRVGKFWTMNNNITALYMHFKGPIAGYEIDKGSFFIQGNSYHNFRLGQQWSAEATINGNTPFVYNLFKIHARIGVDIGANYNFKDQKSSLKLAVTDVFRSNRNNLTTNFNEFQSKIRQYNDRQTVRLTYTYKFGNLKQQIRKSDSRNEEKDRVSQ
>NZ_CP049246.1|WP_103906512.1|679279_681100_-|PspC-domain-containing-protein
MNKTIIININSIVFHIEEDAYETLRSYMIEIKRHFGKSEDSREILEDIENRIAEMFSERIQTGRKEVINREDVDQVIAQMGRVSDFESEFSEEPRVEEPASAQAAFSSEPQPEEPALGGEAQAEEQKVDSEPSFTEYLTSKKLMRDPDDKIIGGVCSGLGHYFNIEAKWVRIIFVLFFLFGGSGVLLYFVLMAVMPKAITRADRLAMRGEQPNLQNFKKSFDEEMKGVRENFSGAGEHFNRGARSVGDSLGRIFSVIGKVLAVLLLIFAGLNVVGIFIFFVFNALNLMGYQNPIFFPPLEIMDSTSGFFALLAGTLAVGIPFLALFFIMLRVVFKSNPMNNYASMSLWAAWVGSIVMILYFVIVTNQDFIEESTISVEKPLEKKDTYILSMNDVRVIKTSDEEFSKKNLNLGKYGLIGNHLRDDIGIRFEPLDSLKAPYLQYNYQAKGNSYGDASARASKIKYQVVQNGENILFDSHFALQEKQLIRDQRVQMVVYLPVGTTVMLNRDLDYKVRDIWAYDCRVNDEAKYAEFTMTKDGLKCVAKLKEEKEKALEDAKEDAEKRAKEAKERAEDLEKEAKELEKEKKKENSEAAAGDGESSAADSRA
>NZ_CP049246.1|WP_103906513.1|681131_681467_-|PadR-family-transcriptional-regulator
MIAENTQTQMRKGILEYCILSIISRGEIYASDIISELKKAELLVVEGTLYPLLTRLKNNGLLSYSWKESTSGPPRKYYQITAEGMEVLKKLDVTWKELLFAVETSLQNREL
>NZ_CP049246.1|WP_103906514.1|681657_682041_+|glycine-cleavage-system-protein-H
MNWIINYAWAILWAIIMMVLLLLPPNNLPSVGYFPGFDKLVHTGCFYLLTTLIIFGRVVDTKRRATKLKTFIIVFCVASVFAFMTEAAQMYFTKTRQADWHDIFADYVGIGMALFSYLLLYNRKFQY
>NZ_CP049246.1|WP_103906515.1|682046_682742_-|ComF-family-protein
MFLSRLWRALLHLIYPELCMGCGIVLFDQENLICSECLYHLPYTDFHLDPNNPVMQQVKGRADVEFGTAMLFLFPKTIVQNLIYNLKYKNHPQVGERLGEMYGHILQKACVFEAVHVLVPIPLHPDRRAKRGYNQCEYICKGLSRSMEKPIDLNLLYRRIHHKSQTRLSRVERAQNVENIFECRHLDAISDQHILIVDDVFTTGATLCAAVECVKEAFPQCRVSILTIAKA
>NZ_CP049246.1|WP_103906688.1|682890_683922_+|LLM-class-flavin-dependent-oxidoreductase
MELGIGMFGDLQIDAQTGNIQAPQQRLQEIIEEVKLMDEVGVDFFGIGEHHRPDYAVASPEIVLAAAATVTKRIKLGSAVSVLSSTDPVKLYQNFATVDLISNGRAEIMAGRGSFIESFPLFGYDLKDYSSLFEEKLDLLLKINKNQTVNWTGKHRASLVNQSIYPRAVHDSMPIWIAVGGTTESVIRAGRLGLPVMFAIIGGSPINFKPLFEVYEQAYQDNGHDMSKFQVGVHMHSFFGENSREVADWYYPFYSAQMNRIGASRGWPPYQRTQYDYGRSNHGHLIVGDVNESVDKILALQESFGLTRFSAHMDVGSPDHSKMMKAIELYGNQIIPKVKDALK
>NZ_CP049246.1|WP_160003744.1|684717_685596_+|DUF4349-domain-containing-protein
MKRKIIWGILLSMTLGACNQIQGVKDEMVAPEAEAYGMAATGEVAADAAAVEGKAAAAPQQAEPQKFVDNGIKIVRTGNLSLESKDINASKQNLDRLIKRFQGYYEEESANNTQDFTSYNLIIRIPSTSFDQFLTAISSGSDKVTSKTISASDVSMTYFDLASRLKSKRAYLEKYQAMVASAKNVKELLEIQEQIRQLQEDIDSSESLMRNMNSQIKYSTLTINLFEYQANLPMGTNSFWIQLKDALAFGMSLIRSIVLGIIGLWPIWIVTALAVWIVLRIRKTRKAKSIGQ
>NZ_CP049246.1|WP_160003746.1|685652_686147_-|hypothetical-protein
MVKSLSHNIFLLANLVAIALLFSCADRDEPSCLTALKADLQDPNMMADVDFNAVHCFAWDSLMLITSYHYDQQILEETGIRIPPTLREKGEHLIHIAFIKDHQVAQILSLEKGKCDFTDYIQQEVFSRSYLFVDRKASFFVRNSKGQFQQPKDTLDTQLAVEVD
>NZ_CP049246.1|WP_103906519.1|686286_687372_+|23S-rRNA-(adenine(2503)-C(2))-methyltransferase-RlmN
MYLCIVEKAVKTVDIRSLSLAQLKDALVNMGEQGFRAKQIYEWLWQKSCTDFDEMSNLSKSLRETLKQHFTINAVRVKESQISADKTIKSSFFLYDNNVIEGVLIPAEDRMTACVSSQVGCSLTCKFCATGYMDRKRNLNADEIYDQVVLIAKQAEDKYNHPLTNIVYMGMGEPLLNYSNMMKSVERITAPDGLNMAAKRITVSTAGIAKMIKKLGDDQVRFNLALSLHAANDKKRNEIMPINEQNSLAALADALKYFYAKTKNPITFEYIVFHHFNDELEDAKELARFCKHVPCKVNIIEYNPIALADFVNAEADKIEEFADYLRSQGIITNVRRSRGKDIDAACGQLAIKEKDKEADPA
>NZ_CP049246.1|WP_103906520.1|687484_688066_-|tRNA-(ms[2]io[6]A)-hydroxylase
MLGLKLLTDPRWANIAESNLEEILTDHAWCEQKAASNAISLITQNSEHEDLVHELTAIAIEEMEHFKMVIDIIQERGYTLGRERKDDYVGQLMKFAKKDGSRNMAFIDRLLFAAMIEARSCERFRVLSKNINDQELAKFYHDLMVSEANHYTTFLNFAKKYSTDVDVDKRWKQWLEFEGELIQSYGKKEHIHG

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Crispr_ID: NZ_CP049246_5

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP049246_5

811979-812077

Orphan

Consensus_repeat	Method
TGAGATATGAGAAAGTCTGGGTGCTATT	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP049246_5

>merge|NZ_CP049246|5|811979-812077|CRISPRCasFinder
TGAGATATGAGAAAGTCTGGGTGCTATTAGGCAACCATTAGTAATATCTGACAGATATGAGATGTTAGATTTGAGATATGAGAAAGTCTGGGTGCTATT

>NZ_CP049246|5|5|811979-812077|CRISPRCasFinder
TGAGATATGAGAAAGTCTGGGTGCTATT	AGGCAACCATTAGTAATATCTGACAGATATGAGATGTTAGATT
TGAGATATGAGAAAGTCTGGGTGCTATT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP049246.1\|WP_093100014.1\|818270_818462_+\|cold-shock-domain-containing-protein	unknown	unknown	gnl\|CDD\|239905
NZ_CP049246.1\|WP_103906608.1\|804166_807463_+\|preprotein-translocase-subunit-SecA	unknown	unknown	gnl\|CDD\|237256
NZ_CP049246.1\|WP_103906613.1\|810189_811497_-\|M20/M25/M40-family-metallo-hydrolase	unknown	unknown	gnl\|CDD\|349874
NZ_CP049246.1\|WP_103906614.1\|811589_811904_+\|rhodanese-like-domain-containing-protein	unknown	unknown	gnl\|CDD\|238089
NZ_CP049246.1\|WP_103906623.1\|818574_819294_-\|DNA-repair-protein-RecO	unknown	unknown	gnl\|CDD\|378775
NZ_CP049246.1\|WP_103906609.1\|807475_807931_+\|SPOR-domain-containing-protein	unknown	unknown	gnl\|CDD\|335993
NZ_CP049246.1\|WP_103906616.1\|813894_814200_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP049246.1\|WP_103906607.1\|802883_803150_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP049246.1\|WP_103906615.1\|812437_813862_+\|Glu/Leu/Phe/Val-dehydrogenase	unknown	unknown	gnl\|CDD\|223411
NZ_CP049246.1\|WP_103906621.1\|816913_817393_-\|DUF4112-domain-containing-protein	unknown	unknown	gnl\|CDD\|379180
NZ_CP049246.1\|WP_103906695.1\|803165_804035_+\|1,4-dihydroxy-6-naphthoate-synthase	unknown	unknown	gnl\|CDD\|270353
NZ_CP049246.1\|WP_103906610.1\|807943_809134_+\|amidohydrolase	unknown	unknown	gnl\|CDD\|349882
NZ_CP049246.1\|WP_103906622.1\|817394_818120_-\|SIMPL-domain-containing-protein	unknown	unknown	gnl\|CDD\|225516
NZ_CP049246.1\|WP_103906611.1\|809137_809710_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP049246.1\|WP_103906618.1\|814477_815557_-\|glycine-cleavage-system-aminomethyltransferase-GcvT	unknown	unknown	gnl\|CDD\|234742
NZ_CP049246.1\|WP_103906617.1\|814196_814442_+\|sortase	unknown	unknown	unknown
NZ_CP049246.1\|WP_103906606.1\|802100_802880_+\|5'/3'-nucleotidase-SurE	unknown	unknown	gnl\|CDD\|234732
NZ_CP049246.1\|WP_103906612.1\|809706_810201_+\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|366181
NZ_CP049246.1\|WP_103906620.1\|816509_816878_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|372990
NZ_CP049246.1\|WP_103906619.1\|815814_816510_-\|pseudouridylate-synthase	unknown	unknown	gnl\|CDD\|211333

Protein	Function_ID	Function_description	E-value
NZ_CP049246.1\|WP_103906608.1\|804166_807463_+\|preprotein-translocase-subunit-SecA	gnl\|CDD\|237256	PRK12901, secA, preprotein translocase subunit SecA; Reviewed.	0
NZ_CP049246.1\|WP_103906613.1\|810189_811497_-\|M20/M25/M40-family-metallo-hydrolase	gnl\|CDD\|349874	cd03877, M28_like, M28 Zn-peptidase, many containing a protease-associated (PA) domain insert. Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This subfamily is composed of uncharacterized proteins, many of which contain a protease-associated (PA) domain insert which may participate in substrate binding and/or promote conformational changes, influencing the stability and accessibility of the site to substrate. Some proteins in this subfamily are also associated with the PDZ domain, a widespread protein module that has been recruited to serve multiple functions during the course of evolution.	2.00332e-61
NZ_CP049246.1\|WP_103906614.1\|811589_811904_+\|rhodanese-like-domain-containing-protein	gnl\|CDD\|238089	cd00158, RHOD, Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. The cysteine containing enzymatically active version of the domain is also found in the Cdc25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and certain stress proteins such as senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions (no active site cysteine) are also seen in dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases, where they are believed to play a regulatory role in multidomain proteins.	3.1337e-27
NZ_CP049246.1\|WP_103906623.1\|818574_819294_-\|DNA-repair-protein-RecO	gnl\|CDD\|378775	pfam11967, RecO_N, Recombination protein O N terminal. Recombination protein O (RecO) is involved in DNA repair and pfam00470 pathway recombination. This domain forms a beta barrel structure.	4.41729e-16
NZ_CP049246.1\|WP_103906609.1\|807475_807931_+\|SPOR-domain-containing-protein	gnl\|CDD\|335993	pfam05036, SPOR, Sporulation related domain. This 70 residue domain is composed of two 35 residue repeats found in proteins involved in sporulation and cell division such as FtsN, DedD, and CwlM. This domain is involved in binding peptidoglycan. Two tandem repeats fold into a pseudo-2-fold symmetric single-domain structure containing numerous contacts between the repeats. FtsN is an essential cell division protein with a simple bitopic topology, a short N-terminal cytoplasmic segment fused to a large carboxy periplasmic domain through a single transmembrane domain. These repeats lay at the periplasmic C-terminus. FtsN localizes to the septum ring complex.	8.35433e-07
NZ_CP049246.1\|WP_093100014.1\|818270_818462_+\|cold-shock-domain-containing-protein	gnl\|CDD\|239905	cd04458, CSP_CDS, Cold-Shock Protein (CSP) contains an S1-like cold-shock domain (CSD) that is found in eukaryotes, prokaryotes, and archaea. CSP's include the major cold-shock proteins CspA and CspB in bacteria and the eukaryotic gene regulatory factor Y-box protein. CSP expression is up-regulated by an abrupt drop in growth temperature. CSP's are also expressed under normal condition at lower level. The function of cold-shock proteins is not fully understood. They preferentially bind poly-pyrimidine region of single-stranded RNA and DNA. CSP's are thought to bind mRNA and regulate ribosomal translation, mRNA degradation, and the rate of transcription termination. The human Y-box protein, which contains a CSD, regulates transcription and translation of genes that contain the Y-box sequence in their promoters. This specific ssDNA-binding properties of CSD are required for the binding of Y-box protein to the promoter's Y-box sequence, thereby regulating transcription.	2.06905e-20
NZ_CP049246.1\|WP_103906622.1\|817394_818120_-\|SIMPL-domain-containing-protein	gnl\|CDD\|225516	COG2968, COG2968, Uncharacterized conserved protein [Function unknown].	9.75661e-18
NZ_CP049246.1\|WP_103906619.1\|815814_816510_-\|pseudouridylate-synthase	gnl\|CDD\|211333	cd02563, PseudoU_synth_TruC, tRNA pseudouridine isomerase C. Pseudouridine synthases catalyze the isomerization of specific uridines in an tRNA molecule to pseudouridines (5-ribosyluracil, psi). No cofactors are required. TruC makes psi65 in tRNAs. This psi residue is not universally conserved.	3.89162e-86
NZ_CP049246.1\|WP_103906621.1\|816913_817393_-\|DUF4112-domain-containing-protein	gnl\|CDD\|379180	pfam13430, DUF4112, Domain of unknown function (DUF4112). This family has several highly conserved GD sequence-motifs of unknown function. The family is found in bacteria, archaea and fungi.	1.96592e-27
NZ_CP049246.1\|WP_103906615.1\|812437_813862_+\|Glu/Leu/Phe/Val-dehydrogenase	gnl\|CDD\|223411	COG0334, GdhA, Glutamate dehydrogenase/leucine dehydrogenase [Amino acid transport and metabolism].	8.10681e-129
NZ_CP049246.1\|WP_103906610.1\|807943_809134_+\|amidohydrolase	gnl\|CDD\|349882	cd03886, M20_Acy1, M20 Peptidase Aminoacylase 1 family. Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; acylase I; amido acid deacylase; IAA-amino acid hydrolase; dehydropeptidase II; N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) subfamily. ACY1 is the most abundant of the aminoacylases, a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. It is encoded by the aminoacylase 1 gene (Acy1) on chromosome 3p21 that comprises 15 exons. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney, suggest a role of the enzyme in amino acid metabolism of these organs. Defects in ACY1 are the cause of aminoacylase-1 deficiency (ACY1D), resulting in a metabolic disorder manifesting encephalopathy and psychomotor delay.	5.89148e-162
NZ_CP049246.1\|WP_103906618.1\|814477_815557_-\|glycine-cleavage-system-aminomethyltransferase-GcvT	gnl\|CDD\|234742	PRK00389, gcvT, glycine cleavage system aminomethyltransferase GcvT.	0
NZ_CP049246.1\|WP_103906606.1\|802100_802880_+\|5'/3'-nucleotidase-SurE	gnl\|CDD\|234732	PRK00346, surE, 5'(3')-nucleotidase/polyphosphatase; Provisional.	1.89405e-127
NZ_CP049246.1\|WP_103906612.1\|809706_810201_+\|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.	2.45266e-10
NZ_CP049246.1\|WP_103906620.1\|816509_816878_-\|hypothetical-protein	gnl\|CDD\|372990	pfam14271, DUF4359, Domain of unknown function (DUF4359). This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are approximately 130 amino acids in length. There are two completely conserved residues (P and S) that may be functionally important.	0.00485953
NZ_CP049246.1\|WP_103906695.1\|803165_804035_+\|1,4-dihydroxy-6-naphthoate-synthase	gnl\|CDD\|270353	cd13635, PBP2_Ttha1568_Mqnd, A menaquinone biosynthetic enzyme exhibits the type 2 periplasmic-binding protein fold. This group includes Ttha1568 (MqnD) from Thermus thermophilies HB8, an enzyme within an alternative menaquinone biosynthetic pathway that catalyzes the conversion of cyclic de-hypoxanthine futalosine to 1,4-dihydroxy-6-naphthoate. Menaquinone (MK; vitamin K) is an essential lipid-soluble carrier that shuttles electrons between membrane-bound protein complexes in the electron transport chain. Ttha1568 has significant structural homology with the members of type 2 periplasmic-binding fold protein superfamily. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.	8.16462e-139

>NZ_CP049246.1|WP_103906614.1|811589_811904_+|rhodanese-like-domain-containing-protein
MKEISVQELKDMMDHNTEFQLIDVREPFEYEVSNLNGVNIPLSGVVIESDKISKDLPVVIHCRSGKRSAQAIMLLEQEGFTNLSNLQGGILAWKEAFDPEMDVY
>NZ_CP049246.1|WP_103906613.1|810189_811497_-|M20/M25/M40-family-metallo-hydrolase
MIKHFLSLCSLGLFFQLSYAQVAEITTTENISRILNTLASDEMRGRSALVPADIDRAADFIAAEFKEIGLQPYVGNNFKQEFAVNRSKVSSQRVTIANKELADEDFLIFGDFQGSLSAKENKIKTLQITADDDFSQKFREIVQKDPEDAIIAVDKKHAAFLARFKKIYNREQITIKGQERPKSPTKVFVVAESIPADYTVQVEKTGNDFTMANVAAIIPGKSKADEYVVFSCHYDHIGIIQAVGQDSIANGADDDASGTTAMIELARYYKKLNNNERTLIFVAFTAEEIGMFGSKYFSNNIDPEKVAAMINIEMIGKDSKFGPNTMYITGFTASNLGQLMQENLKGSAFTFHPDPYTTQNLFYRSDNAVLAALGVPAHTFSTSQIDKDSYYHTVKDEVSTLDINNIKSSIEAIAAGAIGIVKGEQTPTRVEKLRD
>NZ_CP049246.1|WP_103906612.1|809706_810201_+|GNAT-family-N-acetyltransferase
MITIRKATAEDAVLIHELAHAIWYPTYGPILSQDQIAFMLEKMYATEVLEAAILEDQVQFYLLYDQTDNAVGFLGLQPKADCLRIEKIYLLPITQGKGYGKLLIEFSADRAKELGLPELELNVNRGNQAYHFYLKQGFEVVEEVDIPYYGYVMDDYVMRKRLIS
>NZ_CP049246.1|WP_103906611.1|809137_809710_+|hypothetical-protein
MSSHHIVRENQEPALFIADPHCLQEGYLHQLLEWSPTIITLAQHYEHLQSLQIKVDVLLAKEEVSGMDLEEHLQVVSYGDSSPTAALFTYLHSKNNYAVNILTNDEQISPYIPFLSDFTIIFLNDGGKHLLVRKYEKWLPKGFVLGIAGVEDITDLENLDAISDGKFTVRADGFVRITEQPHYFRITEEL
>NZ_CP049246.1|WP_103906610.1|807943_809134_+|amidohydrolase
MSTTKQTVQQFAQSFFEDTLNKRRFLHQNPELSFEEYNTSAFVKQVLTDLCIPFESMADTGVVGLIQGELPSDKVIALRADMDALPITEVEGRSYGSQNIGVMHACGHDVHTASLLGVARILMAMRAEFGGTVKLIFQPGEERLPGGASLMIKDGVLENPKPQGIIGQHVMPFIEAGKVGFRSGKYMASCDELFMTIRGKGGHGAQPHQNIDPIAITAQVITAMQQVVSRNADPRIPSVLSWGKIIGNGATNVIPDEVYLEGTFRTFDEKWRAEAHEKMTKMAVGIAESMGATCDFQVAKGYPFLINEPQITAASRRYAEEYLGAENVVELDLWPAAEDFAYYSQETNACFYRLGTGNVEKGITSAVHTPTFDIDETALQTSIGLMAYIALRQLEA
>NZ_CP049246.1|WP_103906609.1|807475_807931_+|SPOR-domain-containing-protein
MKYPGFLVSCLLLCALSSSAQTQESKVVVEKDSLIDLLQQARTHFALNPTSTKTVPLEPKVLDKSRASRVKVRGFRVQIYSGTSRSEAQTVQNSFIRQNSGTNAYLDYVEPNYRVKVGDFTSRSAATEYMRQLRGRYRNVFVFVEDVWTWR
>NZ_CP049246.1|WP_103906608.1|804166_807463_+|preprotein-translocase-subunit-SecA
MLKFLSKLFGSKSERDIKGVHPLVNKIKEEYEKLSGLTHDELRAKTTEFKERISTYLQDIDKEIDELKGQADATEDMEKKTSIYDQVDKLTKDRDKKLEEILLEILPEAFAVVKDTARRFTENKEIEVTASQFDRDLAARKPNVQVNGDKAIWKNTWNAAGTEVTWNMVHYDVQLIGGIVLHQGKIAEMSTGEGKTLVGTLPTYLNALAGQGIHIVTVNDYLARRDSEWNGPIFEFHGMSVDCIDKYQPNSPQRRQAYMSDIVYGTNNEFGFDYLRDNMTNTKEAMVQRKLHFAMIDEVDSVLIDDARTPLIISGPIPMGDQHEFHQLKPRIERLVNAQKAYINTVLNQAKKAIAENDTDPEKGGLALFRAYRGLPKNKALIKYLSEGNHRQILQKVENFYMSEQNRHMPKADAELFFVIDEKNNQVELTDKGIELITASGEDPSFFILPDVGTEIAEIEKADIALEEKAAKKEELMRDYSVKAERIHSINQLLKAYTLFERDDQYIVDEGKVKIVDEQTGRIMDGRRYSDGLHQAIEAKENVKVEDATQTYATITLQNYFRMYHKLSGMTGTASTEAGELWEIYKLDVVEIPTNKGIQRDDRQDFIYRTAREKYNAVAQEIQTLTEQGRPVLVGTTSVEISELLSRMLKLRGVKHNVLNAKLHQKEADIVAEAGRPGQVTIATNMAGRGTDIKLTEEVINAGGLAIIGTERHESRRVDRQLRGRAGRQGDPGSSQFFVSLEDPLMRLFASERISNLMVKMGVEDGEVMQHSMLTKSIERAQRKVEENNFGIRKRLLEYDDVMNSQRTVIYTKRKNALFGERLDVDLNNTIYDVVEDVVLQAKEDNSFDEFQIEVIRIFAVNPAITQDEFTSTSANNLVEKLFTQVIDHYHQKAENIANQTLPVLTNVLAERGGMIENIIVPFTDGIRGIQVATNLKKAVETNGKEVFKSFEKGIVLALIDEAWKEHLREMDDLKQSVQNAVYEQKDPIIIYKMEAYNLFKTMLAGMNKDIVSFLFKGEIPGQQQEPENVQAARPEAPKVKVKETKEELASPTGVSEEDLNTQAPQVTQPIRKDQEVGRNDECPCGSGLKYKNCHGKQ
>NZ_CP049246.1|WP_103906695.1|803165_804035_+|1,4-dihydroxy-6-naphthoate-synthase
MNLTLGFSPCPNDTFIFDALIHDKIDCHDLRFHVEYHDVETLNAKAFRGELDITKLSYHAFAYAVEDYELLDAGSALGFGVGPLLICKDAELAEELAQYIGGELPEHLRDLRVGIPGKYTTANFLLGLAFPTLQQKEELLFSEIEESLLDGRIDVGLIIHENRFTYMDKGLHKIADLGDFWEKTTGSPIPLGGIVIKRSLPDAVKKRVNALITESVRFGFANPKSGLDYIRSHAQEMNEQVMYQHIELYVNKYSENLGEIGREAIQKLFDQARALNLVPVTEKNIFLEK
>NZ_CP049246.1|WP_103906607.1|802883_803150_+|hypothetical-protein
MKNSILVGFLLGILAPIAAFLLMRYTDVQMEVFPDKPTALYVIAAAINLVSCWICYKQERDKIGNGLVLATFVGMMILVLTKNIQIDM
>NZ_CP049246.1|WP_103906606.1|802100_802880_+|5'/3'-nucleotidase-SurE
MTKKKPTILVVNDDGITAPGIKVLLEVMQEIGEVVVVAPDSPQSGMGHAITIGKPLRLDKIDLYPGVEMYKCSGTPVDCVKLAVHKIFKGKKPDLCVSGINHGLNYSINVLYSGTMSAAVEGAIEGIPSVGYSLDDFAYHADFEHTRVWVKTIAEQVLKNGLPKNSLLNVNFPNKSVEIKGIKICRQANAKWFEEFDERLDPYKREYFWMTGNFDLQDRGEDTDAHAINNGYVSIVPTQFDMTAHHVIPELNSWSFDIS
>NZ_CP049246.1|WP_103906615.1|812437_813862_+|Glu/Leu/Phe/Val-dehydrogenase
MDNQSNNTYTFFEGVARNFDKAAKFTKFSSGILDQIKACNSILRVKFPVKIGDNIEVIEAYRVQHSHHKLPCKGGIRFSMEVDQDEVMALASLMTYKCAIVNVPFGGAKGGIKIDSKKYSEYELEKITRRYTTELVKKNFIGPGTDVPAPDYGTGAREMSWIVDTYTTLNPNEINAQACVTGKPISQGGVRGRTEATGLGVFFGVREACKVQEDMEALGLTVGVEDKRVIVQGLGNVGYHAAKYFQEAGSKLVGLIEYEGAIYNANGLDLDAVVAHRKTTGSILDFPGAENVADSARALEYPCDILIPAALESVINISNADRIQAQIIGEAANGPLTPEADEILNSKGKLIIPDIYLNAGGVTVSYFEWLKNLSHVRYGRLEKRFSENMYAEILNIIESMTNQKVSKLERKIILRGPDEVDLVYSGLEDTMIGSYQEIHQIWKNTEGVTDLRTAAFICAINKVGESYKELGIFP
>NZ_CP049246.1|WP_103906616.1|813894_814200_+|hypothetical-protein
MNKLFLQTKQAFLFSLAFYIFSLLFLLLKIGFAPILLSIAMLVSLIWVVLVLLEIIKSTRISDGERLLLVLFVIVGNIIAGIVYFYFVRERVTGYKVIKKK
>NZ_CP049246.1|WP_103906617.1|814196_814442_+|sortase
MTKKFILNILLNLGIVFLVLSAWAGYNSGQMLYLGISIALLVVLIYLKVVLIKQVKRDVRAKEEEKIKMAQQQARKKKRAK
>NZ_CP049246.1|WP_103906618.1|814477_815557_-|glycine-cleavage-system-aminomethyltransferase-GcvT
MKNTALTNVHIALGAKMVPFAGFNMPVQYSGINDEHETVRTGVGMFDVSHMGEFILKGEKALDLIQKVSSNDASKLYDGKVQYGYLPNEDGGIVDDFLTYKIDDTTYLLVVNASNIEKDWNWISKFNTEGVEMKDISDETSLFAIQGPKAADALQQLTDIELAPMEYYTFQKGVFAGVENVLVSATGYTGAGGFEIYVANEHAEQVWNAIMEAGKAYGIKPIGLGARDTLRLEMGFCLYGNDIDDTTSPLAAGLGWVTKFTKDFVNSENLKAEKEQGVSQKLVGFEMIDRGIPRHDYEIVDAEGNKIGRVTSGTQSPSLKKSIGLGYVDTAFAKEGTEIFVSIRNTPIKAVVKKPPFVK
>NZ_CP049246.1|WP_103906619.1|815814_816510_-|pseudouridylate-synthase
MLEIIYRDADLIAINKPHGLLVHRSSIAADTAEFALQLLRDQIGQPVYPAHRIDRKTGGVLLFSLNKEMDSLIQTAFAENRIEKEYLALLRGHTEPAGTIDYPLKKENGTLQDALTHYTTIALSEIDLPFGKFPTSRYALVSARPQTGRMHQIRRHFAHIFHPIIGDRPHGCNKQNKLWKETFQHDTMLLHAKNIKFQHPRTKETIFIEAQLQPEFKRALNIASLDVRCEY
>NZ_CP049246.1|WP_103906620.1|816509_816878_-|hypothetical-protein
MSKTRIFALLGIAILLIAVFTNPPKEKIEQALTVKAKDILKKQLNYEHKDAVDFGMMLFGDQVVREFVNSYTYTNNYYLFSLTKISWNGEKYIIGGGAFGKVWISPKLDEKAEVLIEALKNQ
>NZ_CP049246.1|WP_103906621.1|816913_817393_-|DUF4112-domain-containing-protein
MPRQEHYNLEKIDKDFSWVKRLSVLMDSRFRIGNFKFGLDPLLNFIPFAGQIATLTISLILVIVMYRNGASSKLAVKMLWNVTWDALVGSIPLIGNVFDFFNKANEKNIKLLQEHYYENKHQGSAKRMLITFGIILFILMVLFIYLMYYLTVSLFEWIF
>NZ_CP049246.1|WP_103906622.1|817394_818120_-|SIMPL-domain-containing-protein
MKHMKKLMVLAALVGLISTASAQTNTMENSRRVATRGYAEKEVTPDIIYLSVSLKEYYQDGNTKKKVQIEQLEKQLFDAAMKNGVRKEDFTIQNIYSYNTVDKKKTNEIMQSRQYRIKVTDLKKLNPMLEEVDPRGIQSTSINGYDHSQKREIEKELKTAAVKDARTNADILAAADGESVGKVLMINDNSSLNWNDIAPQPRMYAMKSANAVLEDGSAQGPELEVRPIKLTCNIDAVFELK
>NZ_CP049246.1|WP_093100014.1|818270_818462_+|cold-shock-domain-containing-protein
MQEGVVKFFNEAKGFGFIIPNSGESEIFVHVSGLVDKVRENDHVSYEVQQGRKGLNAVNVKLI
>NZ_CP049246.1|WP_103906623.1|818574_819294_-|DNA-repair-protein-RecO
MLQRTKGITLKLTNYSESSVVAQIYTEALGLQSYLINGARKPKAKISTNMLQPFHLLELVVYNKENNNLQRIKEAQQTPVLKSIPLDIVKSSIAIFLNEVLYKVLRHQHPEPQLFHFLESAISWLDETDEGLANYHLVFLAKLSHYLGFRPIVTEQAYFDLVEGQFSSLLPAHTYTLQEPYSGYLRQILRASFSNSKDIRLSREDRSYLLQKLVDYYRLHTENFGEINSLFILEEIFGN

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Crispr_ID: NZ_CP049246_6

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP049246_6

1280529-1280631

Orphan

Consensus_repeat	Method
AAACTCGCCGACGGGATCGCTGGCGCACGTC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP049246_6

>merge|NZ_CP049246|6|1280529-1280631|CRISPRCasFinder
AAACTCGCCGACGGGATCGCTGGCGCACGTCTTTTGTAGTGGGCTGCGCGTTGGCCGACTTGTGCCCGGCCCAAACTCGCAGACGGGATCGCTGGCGCACGTC

>NZ_CP049246|6|6|1280529-1280631|CRISPRCasFinder
AAACTCGCCGACGGGATCGCTGGCGCACGTC	TTTTGTAGTGGGCTGCGCGTTGGCCGACTTGTGCCCGGCCC
AAACTCGCAGACGGGATCGCTGGCGCACGTC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP049246.1\|WP_103906708.1\|1305162_1307415_-\|family-20-glycosylhydrolase	unknown	unknown	gnl\|CDD\|119333
NZ_CP049246.1\|WP_103906704.1\|1295893_1296961_+\|formylglycine-generating-enzyme-family-protein	unknown	unknown	gnl\|CDD\|335469
NZ_CP049246.1\|WP_103907961.1\|1273367_1274063_-\|rhomboid-family-intramembrane-serine-protease	unknown	unknown	gnl\|CDD\|223777
NZ_CP049246.1\|WP_103907964.1\|1279218_1280373_+\|acyl-CoA-dehydrogenase	unknown	unknown	gnl\|CDD\|173840
NZ_CP049246.1\|WP_103907956.1\|1267548_1268946_-\|class-II-fumarate-hydratase	unknown	unknown	gnl\|CDD\|234779
NZ_CP049246.1\|WP_103907963.1\|1277436_1278966_-\|aldehyde-dehydrogenase-family-protein	unknown	unknown	gnl\|CDD\|143448
NZ_CP049246.1\|WP_103907959.1\|1271364_1272465_-\|endonuclease/exonuclease/phosphatase-family-protein	unknown	unknown	gnl\|CDD\|197318
NZ_CP049246.1\|WP_103907958.1\|1269745_1271368_+\|S41-family-peptidase	unknown	unknown	gnl\|CDD\|223864
NZ_CP049246.1\|WP_103906707.1\|1302130_1304950_-\|carbamoyl-phosphate-synthase-large-subunit	unknown	unknown	gnl\|CDD\|235393
NZ_CP049246.1\|WP_103906700.1\|1288600_1289662_+\|efflux-RND-transporter-periplasmic-adaptor-subunit	unknown	unknown	gnl\|CDD\|273776
NZ_CP049246.1\|WP_103906703.1\|1294320_1295730_+\|Gfo/Idh/MocA-family-oxidoreductase	unknown	unknown	gnl\|CDD\|223745
NZ_CP049246.1\|WP_103907966.1\|1276139_1277432_-\|L-lysine-6-transaminase	unknown	unknown	gnl\|CDD\|236224
NZ_CP049246.1\|WP_103906701.1\|1289672_1292750_+\|efflux-RND-transporter-permease-subunit	unknown	unknown	gnl\|CDD\|223911
NZ_CP049246.1\|WP_103907962.1\|1274081_1275941_-\|DNA-mismatch-repair-endonuclease-MutL	unknown	unknown	gnl\|CDD\|234630
NZ_CP049246.1\|WP_103906699.1\|1287829_1288450_+\|response-regulator-transcription-factor	unknown	unknown	gnl\|CDD\|225107
NZ_CP049246.1\|WP_103906705.1\|1297446_1300599_+\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|274948
NZ_CP049246.1\|WP_103907960.1\|1272464_1273340_-\|rhomboid-family-intramembrane-serine-protease	unknown	unknown	gnl\|CDD\|223777
NZ_CP049246.1\|WP_103906702.1\|1292751_1294056_+\|TolC-family-protein	unknown	unknown	gnl\|CDD\|224455
NZ_CP049246.1\|WP_103906706.1\|1300611_1302063_+\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	unknown	unknown	gnl\|CDD\|185760
NZ_CP049246.1\|WP_103907957.1\|1269038_1269605_-\|hypothetical-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_CP049246.1\|WP_103906708.1\|1305162_1307415_-\|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_CP049246.1\|WP_103907961.1\|1273367_1274063_-\|rhomboid-family-intramembrane-serine-protease	gnl\|CDD\|223777	COG0705, COG0705, Membrane associated serine protease [Amino acid transport and metabolism].	4.16899e-24
NZ_CP049246.1\|WP_103907964.1\|1279218_1280373_+\|acyl-CoA-dehydrogenase	gnl\|CDD\|173840	cd01151, GCD, Glutaryl-CoA dehydrogenase. Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, which catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and carbon dioxide in the catabolism of lysine, hydroxylysine, and tryptophan. It uses electron transfer flavoprotein (ETF) as an electron acceptor. GCD is a homotetramer. GCD deficiency leads to a severe neurological disorder in humans.	0
NZ_CP049246.1\|WP_103907956.1\|1267548_1268946_-\|class-II-fumarate-hydratase	gnl\|CDD\|234779	PRK00485, fumC, fumarate hydratase; Reviewed.	0
NZ_CP049246.1\|WP_103907963.1\|1277436_1278966_-\|aldehyde-dehydrogenase-family-protein	gnl\|CDD\|143448	cd07130, ALDH_F7_AASADH, NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B. Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.	0
NZ_CP049246.1\|WP_103907959.1\|1271364_1272465_-\|endonuclease/exonuclease/phosphatase-family-protein	gnl\|CDD\|197318	cd09084, EEP-2, Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; uncharacterized family 2. This family of uncharacterized proteins belongs to a superfamily that includes the catalytic domain (exonuclease/endonuclease/phosphatase, EEP, domain) of a diverse set of proteins including the ExoIII family of apurinic/apyrimidinic (AP) endonucleases, inositol polyphosphate 5-phosphatases (INPP5), neutral sphingomyelinases (nSMases), deadenylases (such as the vertebrate circadian-clock regulated nocturnin), bacterial cytolethal distending toxin B (CdtB), deoxyribonuclease 1 (DNase1), the endonuclease domain of the non-LTR retrotransposon LINE-1, and related domains. These diverse enzymes share a common catalytic mechanism of cleaving phosphodiester bonds; their substrates range from nucleic acids to phospholipids and perhaps, proteins.	1.24632e-81
NZ_CP049246.1\|WP_103907958.1\|1269745_1271368_+\|S41-family-peptidase	gnl\|CDD\|223864	COG0793, Prc, Periplasmic protease [Cell envelope biogenesis, outer membrane].	1.03962e-80
NZ_CP049246.1\|WP_103906707.1\|1302130_1304950_-\|carbamoyl-phosphate-synthase-large-subunit	gnl\|CDD\|235393	PRK05294, carB, carbamoyl-phosphate synthase large subunit.	0
NZ_CP049246.1\|WP_103906700.1\|1288600_1289662_+\|efflux-RND-transporter-periplasmic-adaptor-subunit	gnl\|CDD\|273776	TIGR01730, COG0845:_Membrane-fusion_protein, RND family efflux transporter, MFP subunit. This model represents the MFP (membrane fusion protein) component of the RND family of transporters. RND refers to Resistance, Nodulation, and cell Division. It is, in part, a subfamily of pfam00529 (Pfam release 7.5) but hits substantial numbers of proteins missed by that model. The related HlyD secretion protein, for which pfam00529 is named, is outside the scope of this model. Attributed functions imply outward transport. These functions include nodulation, acriflavin resistance, heavy metal efflux, and multidrug resistance proteins. Most members of this family are found in Gram-negative bacteria. The proposed function of MFP proteins is to bring the inner and outer membranes together and enable transport to the outside of the outer membrane. Note, however, that a few members of this family are found in Gram-positive bacteria, where there is no outer membrane. [Transport and binding proteins, Unknown substrate].	5.32498e-72
NZ_CP049246.1\|WP_103906703.1\|1294320_1295730_+\|Gfo/Idh/MocA-family-oxidoreductase	gnl\|CDD\|223745	COG0673, MviM, Predicted dehydrogenases and related proteins [General function prediction only].	1.19639e-18
NZ_CP049246.1\|WP_103907966.1\|1276139_1277432_-\|L-lysine-6-transaminase	gnl\|CDD\|236224	PRK08297, PRK08297, L-lysine aminotransferase; Provisional.	0
NZ_CP049246.1\|WP_103906701.1\|1289672_1292750_+\|efflux-RND-transporter-permease-subunit	gnl\|CDD\|223911	COG0841, AcrB, Cation/multidrug efflux pump [Defense mechanisms].	0
NZ_CP049246.1\|WP_103907962.1\|1274081_1275941_-\|DNA-mismatch-repair-endonuclease-MutL	gnl\|CDD\|234630	PRK00095, mutL, DNA mismatch repair endonuclease MutL.	0
NZ_CP049246.1\|WP_103906699.1\|1287829_1288450_+\|response-regulator-transcription-factor	gnl\|CDD\|225107	COG2197, CitB, Response regulator containing a CheY-like receiver domain and an HTH DNA-binding domain [Signal transduction mechanisms / Transcription].	3.06185e-16
NZ_CP049246.1\|WP_103906705.1\|1297446_1300599_+\|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_CP049246.1\|WP_103907960.1\|1272464_1273340_-\|rhomboid-family-intramembrane-serine-protease	gnl\|CDD\|223777	COG0705, COG0705, Membrane associated serine protease [Amino acid transport and metabolism].	3.156e-07
NZ_CP049246.1\|WP_103906704.1\|1295893_1296961_+\|formylglycine-generating-enzyme-family-protein	gnl\|CDD\|335469	pfam03781, FGE-sulfatase, Sulfatase-modifying factor enzyme 1. This domain is found in eukaryotic proteins required for post-translational sulfatase modification (SUMF1). These proteins are associated with the rare disorder multiple sulfatase deficiency (MSD). The protein product of the SUMF1 gene is FGE, formylglycine (FGly),-generating enzyme, which is a sulfatase. Sulfatases are enzymes essential for degradation and remodelling of sulfate esters, and formylglycine (FGly), the key catalytic in the active site, is unique to sulfatases. FGE is localized to the endoplasmic reticulum (ER) and interacts with and modifies the unfolded form of newly synthesized sulfatases. FGE is a single-domain monomer with a surprising paucity of secondary structure that adopts a unique fold which is stabilized by two Ca2+ ions. The effect of all mutations found in MSD patients is explained by the FGE structure, providing a molecular basis for MSD. A redox-active disulfide bond is present in the active site of FGE. An oxidized cysteine residue, possibly cysteine sulfenic acid, has been detected that may allow formulation of a structure-based mechanism for FGly formation from cysteine residues in all sulfatases. In Mycobacteria and Treponema denticola this enzyme functions as an iron(II)-dependent oxidoreductase.	3.9491e-77
NZ_CP049246.1\|WP_103906706.1\|1300611_1302063_+\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	gnl\|CDD\|185760	cd08977, SusD, starch binding outer membrane protein SusD. SusD-like proteins from Bacteroidetes, members of the human distal gut microbiota, are part of the starch utilization system (Sus). Sus is one of the large clusters of glycosyl hydrolases, called polysaccharide utilization loci (PULs), which play an important role in polysaccharide recognition and uptake, and it is needed for growth on amylose, amylopectin, pullulan, and maltooligosaccharides. SusD, together with SusC, a predicted beta-barrel porin, forms the minimum outer-membrane starch-binding complex. The adult human distal gut microbiota is essential for digestion of a large variety of dietary polysaccharides, for which humans lack the necessary glycosyl hydrolases.	3.23116e-43
NZ_CP049246.1\|WP_103906702.1\|1292751_1294056_+\|TolC-family-protein	gnl\|CDD\|224455	COG1538, TolC, Outer membrane protein [Cell envelope biogenesis, outer membrane / Intracellular trafficking and secretion].	7.20258e-33

>NZ_CP049246.1|WP_103907964.1|1279218_1280373_+|acyl-CoA-dehydrogenase
MDYLNLEELFLPEHLLVRDTVREFVRSEIRPVIDSYAQDHREIPDLMRKLGAVGALGPFIPVEYGGAGLDQISYGLIMQELEVGDSAIRSAASVQSSLVMFPIYKYGSEEQRLRFLPKLATGELIGAFGLTEPNHGSDPGSMETKLVRDGDGYRLSGAKMWITNAPLCDIAVVWARDEEKKIRGVIVERGFAGFTTPETKNKWSLRASKTGELVFEDVFIPQANVLPEVSSMRGPLSCLNSARYGISWGAIGAAVDCYETALRYAKERTQFGKPIAAFQLQQKKLAEMLTEICKAQLLSLRVGQLKDEDRATAAQISMAKRNNVHMALQVAREARQVLGAMGIVGDYPIMRHMMNLESVITYEGTHDIHLLITGMDITGISGFQ
>NZ_CP049246.1|WP_103907963.1|1277436_1278966_-|aldehyde-dehydrogenase-family-protein
MTSKELKALGIENENLGGSTGNKWFAKGELIESYSPTNGKLIGKVRSTTKKEYEKVIQEAEKAKLVWRDIPAPKRGEIVRQLGEKLRELKPILGKLVSYEMGKSYQEGLGEVQEMIDICDFAVGLSRQLYGNTIHSERPGHRMYDQYHPLGTVGIITAFNFPVAVWSWNAALALVCGDVVVWKPSEKTPLCAVACQHIIADILKANKLPEGISSIITGDAEVGKWIAEDERIPLVSATGSTRMGKQVAATVAQRLGKSLLELGGNNAIIVTPSADLKMTIIGAVFGAVGTAGQRCTSTRRLIIHESIYDKVKKSLVDAYKQIKIGDPLDSNNHMGPLIDTAAVDMYLSALDKVKAEGGKLLTKGEVLKGKGYESGCYVTPVIAEVENEYEIVQHETFAPILYLIKYTGEVDNAIALQNGVKQGLSSAIMTNSLRESELFLSQNGSDCGIANVNIGTSGAEIGGAFGGEKDTGGGRESGSDAWKIYMRRQTNTINYTTNLPLAQGIKFDL
>NZ_CP049246.1|WP_103907966.1|1276139_1277432_-|L-lysine-6-transaminase
MMRETHQKLARHILADGLPVVMDLEKSHGSYIVDIDGKEYLDMFSMFASSPVGYNHPYILANTAQLEKASVNKLALSDIYPDEYADFLETFERVGIPQELGYCFFIDGGGLAVENALKAAFDWKTRLNLANGIDQEASQVIHFKQAFHGRTGYTLSLTNTKDPRKYMYFPKFDWPRITNPKLKFPLTEETINETIEVEKQAIQEIEAAIAKNPNDIACLILEPIQAEGGDNHFRKEFFQQLREICDKNDIILILDEVQTGIAMTGKMWCYQHYGIVPDVISFGKKTQVCGILASKEKFDRVEKNVFKESSRINSTFGGNLVDMVRFKLILEIIEQENLVEKAATLGEYLQGKLQDLAEKHDAISNVRGKGLLAAFDLPSEEARDKFVADLMKENLLILGCGDRSIRFRPHLTVTKEDLDKALAIIDKTIA
>NZ_CP049246.1|WP_103907962.1|1274081_1275941_-|DNA-mismatch-repair-endonuclease-MutL
MSDIIQLLPDSVANQIAAGEVVQRPASAVKELMENAIDAGADHIKLIIKDAGKSLIQVIDNGCGMSVTDARLCFERHATSKIRKAEDLFAIRTMGFRGEAMASIAAIAHVELKTRRVENELGTVIEIEGSEVIQQFPDQAPAGTSISVKNLFYNIPARRNFLKSNSVELRHVIDEFQRIALAHPEIFFSFHSDGNELFHLPKEALKQRIVHLFGNSYNQRLVPVEETTTILNIKGFIGKPEFAKKTRGEQFFFVNNRFIKDPYLNHAVLNAYEEILPADTFPLYVLFIDIDPSKIDINVHPTKTEIKYEDEKAIYAILRSAVKRSLGRFNIAPTLDFNQETGFDTLITPKPLDEIQAPTISFNPNFNPFDDGTARPTRTYTAPEQLERKTSIPQNWDSLYQITETEEVEQLSLLPEESSSEKEFIQPSDQPKKQFFQLHNRYIVSQIHSGFMLIDQQAAHERILFEQFQQQLVQNQGSSQQSLFPQTVDLNPADFALVQEILPEIHALGFQLRPFGKTTYIVDGIPADLENINESQIIEKLLEDFKHQSDLRLSKRERLAKSLAKNASIKPGTKLDNEGMADLIDRLFACESPNISLTGKPVIITITLQELAERFGRTN
>NZ_CP049246.1|WP_103907961.1|1273367_1274063_-|rhomboid-family-intramembrane-serine-protease
MNNFLGNLPTITKNLLIINVLLFLATLAFEPLYGLLGVFYPDSPNFKVWQVISYMFMHGGIGHIFFNMFALVMFGSVIENVLGQKKFFNYYFICGLGALVLQYGVQAFEVFQITNTIMPWHKYGTAFMNNLTMEQADVISSIYRTPLVGASGAIYGLLLAYGYLFPNAELMLIFLPVPIKAKYFIPILIVIEVVLGFSSSGSSIAHLAHVGGALFGFILLKVWGIRRTNYY
>NZ_CP049246.1|WP_103907960.1|1272464_1273340_-|rhomboid-family-intramembrane-serine-protease
MKKESGIKMFFRTTYQTGSPIPYILSIQVLLFVLIHIADLLVELNVIKFPLYDWLVGQLSLPNTFAAFIRQPWSLITYPFLYVGLFNIVFDCLWLYWIGNSFLNFLNKRQFLFVFFSSFLLSGVVYLALGNIDFLAKGSMPFLFSNAMGLASVVAGLLLLAPNMEIRLFLFGTVKFRTIAIIFFTLQLLFYIFANRSGAVAYGFAIAWGFLFMQQLKNGNDWSTIFSIKPKQKLKIVHQTPKTPSYRSYKADLPNQEVIDDILDKISQSGYESLSSREKEILFKVSREEQE
>NZ_CP049246.1|WP_103907959.1|1271364_1272465_-|endonuclease/exonuclease/phosphatase-family-protein
MLIKKKNLGFFSKTIMLGNFAAILVLLLCYSASMINPKSFWPISFLGLGYLPILIINIGFIVYWVLRKPKYAIFSLVAILIGWNLMSKHITFHTPDPVKTGDSSLRVMTYNVHMLAPVDKSDKPAKERFAEVIEEVNPDVLCLQEFSSTIKGTKRFSETIKERAKFDSYYFAPSQQNEYNAYGQVIFSKFPIINSGLIKKNEYGINRIIYVDIVKNADTLRVYNVHLRSFGLQDEDKEFIQNPKNAGGNEETKTKRVGRKLKWAFEQRSLQAESLFAHMKETKFPKIVMGDFNDTPMSYSVNLIGKDMKNAFQEKGNGWGVTHFEMLPILQIDYIFCEKNFMVNNYQIVKKKLSDHYPVYADLRVN
>NZ_CP049246.1|WP_103907958.1|1269745_1271368_+|S41-family-peptidase
MQKGRKRNIFVAATYAATLLLGLILGQNYSDQQRVTSGGSLVPIGLSDNAYKIQQVVDLISTRYVDSINMDSVQNGAINHIISHLDPYSTFLMPNESQSQTEILEGTFEGIGMEYFNLNDTLLVVGLITNGPADKGGFKVGDRILRIGKKELAGKTVSKEEVEKLMRGKRGSSVEMAVLRDSLTTPLVLKAVRDQINVSSLDVAYMLEPTVGFIRIRRFSLKTAEEFKTAVIDLKKQGAKNLILDLRDNGGGYFHIAIKMASEFFTDQRLVVYTEGAHELRQDYLSEGKGAYAQGKLILLVNERTASASEVVSGAIQDWDRGTLIGRRTYGKATVQELFDFSDGSTINLSIARYYTPLGRSIQRKYTPNWSNMQDYASMYHGLWSLDTTYAHAMSYQTKLGKKLYSGGGIVPDVIVPVDSNEVSLLYQDLMRSSMLEQFVYSRFTKKLPAYSIENFLQGYTLPASEYNGFMRFLADKGWRISPRKQQDLHDLIQSDIEALVGRYYFGREAYFKVKNRNDAFVEQALGQIKPVQTLASNRR
>NZ_CP049246.1|WP_103907957.1|1269038_1269605_-|hypothetical-protein
MHEIEPYYNWRDDYIASEDERSPFFGTIYNEFEFDKQVYNYLLHPQWDFFGSQTLYLKVLYVDYDLSYTIIELIGEWNDAIYNDIMILKRELIDLMIGEGITKFILIGENVLNFHASDDSYYEEWFNDIEDGWIVGLNFREHVIKEFADNHIDYYINFGEYLNYFPWRTLKPKQLFHHIEEHMQRRLT
>NZ_CP049246.1|WP_103907956.1|1267548_1268946_-|class-II-fumarate-hydratase
MSFRIEKDTMGEVQVPADKYWGAQTERSRNNFKIGPAASMPHEIIEGFAYLKKAAAYANCELGVLPQEKRDAIAAVCDEILAGKLDDQFPLVIWQTGSGTQSNMNVNEVVANRAQVLAGGKIGEGEPVLKANDDVNKSQSSNDTFPTGMHIAAYKAVVEVTIPGVEKLRDTLKKKSDEFMNVVKIGRTHLMDATPLTLGQELSGYVAQLNYGIKAVKNTLAHLSELALGGTAVGTGLNTPKGYDVLVAKYIAEFTGLPFVTAENKFEALAAHDAIVETHGALKQLAVALNKIANDIRMLASGPRSGIGEILIPENEPGSSIMPGKVNPTQCEALTMVAAQVMGNDVAITIGGTQGHYELNVFKPVMAANFLQSARLIGDACVSFEEHCAIGIEPNYDRIKQLVDNSLMLVTALNTKIGYYKAAEIAQTAHKNNSTLKETAIKLGYVTAEEFDEWVKPEEMVGSLK
>NZ_CP049246.1|WP_103906699.1|1287829_1288450_+|response-regulator-transcription-factor
MDPIKVAIIDDNILCRQLLMLQLAAIETIEIEVVFQTDTLVGIHDRLSTDTKIDLFLLDIMMPEIDGIAGIGILKEMFPRIPIFMVSDVQDLAVIQQCIVAGAQAFIPKGSSVSQLMRTLIGILMNKEHHICPKLTKSIYQGIHAQSALHIDLSVDELELVDQVFQGKSLEVISEILERPFCYVQSMILEVLRKMKLPTNACYLAG
>NZ_CP049246.1|WP_103906700.1|1288600_1289662_+|efflux-RND-transporter-periplasmic-adaptor-subunit
MKRTSIIVIVISVLIVAGLVFYRIHTNKEKEEKQNGPAGPRTAAKVYGKVIQGQPFSDFLSLSGAIEADEQIEIHTEISGIVESINFSEGGRVSQGQVLLRINDAELQAQLAQAQTRNNLAAENERRAKLLLEKEAISQEEYDIASADFRTAQSQIQLIRAQLSKTVVKAPFSGTIGLRNISKGSYVTPTLNIAQLVNTNRLKVSFSIPEKYASKVRVNNQIKFNVQGDSSVYTARIYATEPAVEANTRTLLVKAMTSSPSGRLIPGTFANIVFPLETLDDGLLVPAEALIPVQNGKKLFVMRNGLASEVMVETGARTEADVLITSGIQPGDTVLTSGVMSLRNNVPVQVNLR
>NZ_CP049246.1|WP_103906701.1|1289672_1292750_+|efflux-RND-transporter-permease-subunit
MSLSTLSIKRPVLTIVMNILLILFGIIGYTFLGIREFPSIDPAQISVRTNYAGANADIIESQITEPLEKSINSIDGIRNISSSSNQGSSNITIEFNLGKDLEEAANDVRDKVSQALRSLPQDIDAPPVVSKADADSEPIITMTMQSSTKNVLELSDYAENVISQRLQTIPGVSSVQIWGQRKYAMRLWIDPVRLASYGLTVLDVRSALTTQNVELPSGKLTGANTELAIKTIGNLATEEEFNDIIIRSDNNRIVRLSDVGNAALEAENFETKMSDSGYPMVSLAIIPQPGTNYLEIADQFYKEYDKLQQELPEGFELNIAIDNTLFVKKAVFEVLETLVIAIVLVVIIIYIFFRNWSIAFRPLIDIPVSLIATFFIMYLCGFSINVLTLLAIVLATGLVVDDGIVVTENIFKKVEEGMSPIEAAIKGSNEIFFAVISISITLAAVFLPVIFLEGFVGRLFREFGVVIGAAVLISAFVSLTLTPMLNAYLMKGGEQTRSKFYTRTEKYFELMNTEYAGALKGFLRFKWLSFATIAVCFLLIYFFYMLLPKETAPYDDRSYISLRATAPEGVSYDYMDRFMTDLTMLINDSVPEKKVSLVITSPGFGSASSNSGFVRLGLVQPEERERSQQEIADHLSKLVRGYSEGRVSVSQQPTISVNRRGGMPIQYIIQAPNFQKLEEKIPEFMEELAKDKTFSMTDVNLKFNKPEVYVNIDREKAQTLGVSVLDVAQVLQMSLSGQRFGYFMMNGKQYQVMGQFDRKDRSTPMDLAAIYVKNNRGELIQLDNIVDIEERSSPPQLFHNNRYMSATVSAGLAPGKSMGDGIDAMEAVKAKVLDETFTTDLGGESRDFVESGSNTMFAFGLAVILIFLILAAQFESFIDPIIIIITVPMAVAGAMFSLWLFGQTWNIFSQIGTIMLIGLVTKNGILIVEFANQLREEGYSKYDAVLHASEARLRPILMTSLTIALGALPIALSLGAASTSRVGMGVVIVGGTMFALVLTLFVIPAFYLMMSREKKVHPELKEIEE
>NZ_CP049246.1|WP_103906702.1|1292751_1294056_+|TolC-family-protein
MKKTISILYIWLCGFAVCSAQGLLTVKDAVQIALENNYEIKLSQNDLRIAEENTTPGNAGMLPNVTGNFSQNNSVMNSSQVQASGETRSLSNAKNNNMSYGVSIGWTIFDGLAMFSRYDQLKELKKQGEYELKRTILTKVSDVISTYYTIVEQQNLLHAIDSNINISKERLKTAENRFMIGKASRLEVLNVQVNLNEDESSRLRQANVVKNLKINLNSLMARDLAEEFDVEREVEYDDTLIFGELLEKAKVYNPDLQIIAINKRIAELELKRIKGGRYPTIRLNTGYNFSESESSLGFVSSSNSRGLNYGVTASINIFDGFNQRRNERVAQIAIDNADLMIDQQDLLIRTAMSTAYETYQTNLSLARLEENNAQIARQNLNITMEKYRIGTISAVEFRDAQENFINAVSRFNSSRLQAKLSELQLKEMIGNINL
>NZ_CP049246.1|WP_103906703.1|1294320_1295730_+|Gfo/Idh/MocA-family-oxidoreductase
MNNSRRDFLKKASILSSVAITLPSLQNEAFAAPNFNMSGFAAPKIDKVKVAIIGLGMRGPGAVDRISYIEGAEIVALCDKHADRVTKAQTILTKKGLKEAKAYSGEDGWKTMLKNEELDLVYICTPWEYHAPMAIAAMKAGAHAATEVPIGLTISEIWEVVKTSEATKKHCMMLENCCYDFFEMLTLNMTRQGMFGELVHAEGAYIHDLLDLNFNKKGYDNMWRLRENIKMNGNLYPTHGIGPVAQCMNINYGDKMNHLVAMQSNDFMMADRAKELAAQDDFYKEFVGKRYRGNMDTTLIKTEKGKTIMIQHDVTSPRPYSRIHLLSGTKGFAQKYPKEGIAFGHSFVKPEELKALYEKYTPELVKFIGEQAKQVGGHGGMDFMMDWRMIDCLRNGLPLDQSVYDGASWSAIVPLSVDSVAKNSRTVEIPDFTRGNWKTNKPHDMTLNGGGNTKIRAKVESKDVQLNVG
>NZ_CP049246.1|WP_103906704.1|1295893_1296961_+|formylglycine-generating-enzyme-family-protein
MIINRPFHILFLLLLSLGLSAQVPTQSAIDSLTCHDVPVPGRRTLLQQDKPVASVSEGNGDMVLIKGGAFRMGSQHFADAQPVHDVVVSDFYMDVHEVTNDQFAAFVEATGYVTVAERPLDPKDFPGVDTSILVPGSAVFRSPAKTAGLNNHLQWWEYVPGASWRHPEGPDSNLEGRGDHPVTQIAYADAEAYAAWAGKRLPTEAEWEYAAKGGKHTDEEYYWGKEKLIQGKWMANIFQGRFPVDNTKEDDFENTAPVKSFPPNPYGLYDMEGNVWEWCADYYRADYYADSPRINPRGPSTAHDPQEPGLVKRVQKGGSFLCTDQYCERYKAGSRGKGEVNSPTNNVGFRCVKDL
>NZ_CP049246.1|WP_103906705.1|1297446_1300599_+|TonB-dependent-receptor
MKQKLLLLFVAFVFLSSYAFGQSREITGRVTSAADSRPLAGVTVLVQGTNQGTQTNANGAFEITVPSADSRLVFSYVGYQNQVITVGSRAQINVELVSDDETLDEVVVTGYLVQSKKSFTGSSANVTGDKVANRPLQSFTQGLTGQASGVNVVQPSGVLNNPPVVRVRGLSSLSLNSFPLVVVDGIPVSTSDVSQNSAANNPLGDINPEDIESVNILKDAASTAIYGSRAGAGVLVITTKRGKSGDAKFGYDGWVGTSSAVRLPELLNAAQYIQHKNQAIANARAVNPGLPQGSYPSEGGFFETKDENGNVVDTRWYDYVYQNAISHNHNLNVSGGTEKTSYFFSGNVSDQQGILVNNKFMRRALRANVDHKITDWFKLGSSITYTNSENSSPNSGSVPGAAFNTSGLGRIAVVQAPNVSPYLPNGDYSVNGASIGKGANVLAPNYPNPLPIIDLDKNLSETNRLFANIHADINILKDLKFSSNYTWDLRNTNNEQFWNPINGDGLGYGGYAYNNSSKANNWIFMNNLVYNKRWNDHNFVVLVGHESQLTRIDDWGAVRTGLTDRYFNQFQGGYKNNLPGGNGISEHAFESYLSSINYDYAGKYYITGNFRRDGNSALAKKNRWGNFGGASIGWTISEENFFKDGGLGKVFSNMRFKASWGRVGNGNMPILYGAYNLYTSGVYGQDGYVFFNQAGNDDLKWESSSQTNVGVDFGLFDNRLTAEVNYYNKNIDNMILAVPQAPSKGVPGNSILMNVGSMFNRGFEFSLNYRAISNDNFTWNTNLNFATNKNEVVKLYEGRPIISTTAALETTSITQEGMSAAQIYAVRTAGVNPENGRRIFINKNGEQVQYQHLAPAGTPAYSYLDGRPAASIADQAVALGNTLPTWFGGFNNNFQYKNFDMALNFTFSGGNYIYNGSRAGLLDQRIWNNSTEVLEAWSETNKGGSIPRPIYGDNISNGSAFAIEENVEKGDFLRLQTATLGYRLPKNLIERAKFSNVRLYVSVNNAFLITKYTGVDPEISSNGNSNLASGVERNSIPNGRTFTFGVNIGL
>NZ_CP049246.1|WP_103906706.1|1300611_1302063_+|RagB/SusD-family-nutrient-uptake-outer-membrane-protein
MKNTFKNIYRFSKVALAIALLAASTSCGKDFLDRNSELDIPEEQISAEALRVEGQVNGLYASLKNGALYGGRYLIYNDIRGEEFLNRGGNNVTGYSVYQFSNDPSDSYVAGFWIQAYVTINRVNIFLDNISKVSDDIVPAEKKAQYISEAKFIRAISYYTLVQLFAKPYAADNGASQGVPLRLTPEKSVDNNAAQRATVKAIYDQILKDLNEAEPTAVANYGDAYRRGTRVHKNTVIALKTRVYLAMKNFPKVIEEANKIVSPNAPFTATSGVPHKLLEKIESVFADKTSDERILSFPFELTNIPGTQNQLSYYYNMGNIEYYLNKGTTGIYANPNWPETDARKSALTGVASGFTILKKYTDVGTYLDWVPAIRYAEVLLNLAEAEAEVGDQGRALALLKAIRNRSDAAYTFPAFASRSALVDAILLERRIELLGEGFRAPDLQRRNSPINSVGAGRLVQPNDDHYVFPIPLRELIDNVDINK
>NZ_CP049246.1|WP_103906707.1|1302130_1304950_-|carbamoyl-phosphate-synthase-large-subunit
MPRNTSINSVLIIGSGPIVIGQACEFDYSGSQAALSLKEEGISVSIINSNPATIMTDNVVADHVYLLPLTCESIEQILQERQIDAVLPTMGGQTALNLCIEASNRGIWDKYNVQVIGVDVAAIEKTENREEFRQLMVDIGVGVATSKIANSFLEGKEAAQIIGFPLVIRPSYTLAGTGGGFVHKKEDFDAALNRGLHASPTHEVLVEQAVLGWKEFELELLRDTNDNVIIICTIENFDPMGIHTGDSITVAPGMTLSDKCYQDMRNQAIKMMRSIGNFAGGCNVQFSVNPENEEIIAIEINPRVSRSSALASKATGYPIAKIAAKLAIGYNLDELQNQITKNTSAYFEPTLDYVIVKVPRFNFDKFKGANKELGLQMKAVGEVMAIGRTFIEALQKAAQSLETGRAGLGADGRQSRNLEEIMHSLEHPSADRLFHIKDAFELGVPLESIRKATLIDKWFLVQIQELVQLEGELRRYQLNNIPRDFFMTLKQKGYSDVQIAWLLGNTTEDEVYARRKELGIQRVYKMVDTCAAEFPAHTPYYYSTFEDENESVSSDRKKIIVLGSGPNRIGQGIEFDYSCVHGLLAAKECGYEAIMVNCNPETVSTDFNMADKLYFEPVFWEHVREIIELEKPVGVIVQLGGQTALKMAEKLEEIGVKIIGTNFSNMDLAEDRGSFSDLLKDLDIPYPKYGVATSAEEAIQVANEVGYPVLVRPSYVLGGQGMSIVINDEDLEKAVVNLLKNLPGNHILIDHFLDRAEEAESDSICDGEDVHIIGMMEHIEPAGIHSGDSSAVLPPFSLSENVQNKMEEYTVKLAKALNVRGLLNIQFAIKDENVYVIEANPRASRTVPFIAKAYDVPYINIATKVMLGENKLSDFTIERKLKGYAIKEPVFSFSKFPEVDKQLGPEMKSTGEAIRFIDDLNDPHFRELYNKKSMFLNAQ
>NZ_CP049246.1|WP_103906708.1|1305162_1307415_-|family-20-glycosylhydrolase
MNTKLLICLAFIFCFPLVVSAQQTNIDIIPRPTKSLLQEGQLSLAAPLNLYYVAEFSEVKDLILNIQGIQIGEQELVKKLKKQHSNGIRLFKAMDFDHIPEAGYLLEIDGSGVLIKAHNPSGMISGVQSLLQLTLLNKGQHLPFARIEDSPRFPYRGLHLDVSRNFMPFTFLKKYIDLMALYKFNHFHWHLTDGAGWRLEIKKYPELTQKAAWRTHSTWKDWWNNGRQYVDQGSPNASGGYYTQEQARELVAYAAKRGIQIIPEIEMPAHSEEVLAVYPELSCTGKPYTQGELCLGNEGTYTFLKNVLDEVMTIFPSTYIHIGGDEADKSHWKTCPKCQALKQKEGLKSEEELQSYAVRQMDKYLQSKGRKLIGWDEILQGGLSEGATVMSWRGEKGGIEAANAGHDVIMTPGGYLYFDTYQTDPRTQPEALGGFVPLEKVYSYDPIPEDIAEDKRKHILGAQANVWTEYMNTYQHVEYMAFPRALALSEVVWTSPENKSWKDFKKRLQSHYPVLQKLEVNYYRPSYNVISTVAYDSLQAKNTVTFASEQFVPNIKYTIDGSDPNASSTTYNLPIELAKTATVKAASFLDSTRVSPIETVELDMHKAIGKEVIYNRPWEGYPAQGKSTLTNGTKGGLSYQDGQWQGFINNFDVTVDFERREEIASVALRFMQVPGPGVYFPGEFKVQVSDNGKTYRDLGTVINQVGTTDPALKFQVFTVKPNKPVMARYIRIKATNPMKGYLFADEIVIY

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Crispr_ID: NZ_CP049246_7

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP049246_7

1329680-1329773

Orphan

Consensus_repeat	Method
GGCCACCACATATCACCCTCACTGTC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP049246_7

>merge|NZ_CP049246|7|1329680-1329773|CRISPRCasFinder
GGCCACCACATATCACCCTCACTGTCACATATCTCATATCTCAAATCTCTCATCTATCTCTCGTATCGGGCCACCACATATCACCCTCACTGTC

>NZ_CP049246|7|7|1329680-1329773|CRISPRCasFinder
GGCCACCACATATCACCCTCACTGTC	ACATATCTCATATCTCAAATCTCTCATCTATCTCTCGTATCG
GGCCACCACATATCACCCTCACTGTC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP049246.1\|WP_103906720.1\|1319354_1322639_-\|SusC/RagA-family-TonB-linked-outer-membrane-protein	unknown	unknown	gnl\|CDD\|274948
NZ_CP049246.1\|WP_103906725.1\|1326043_1326565_-\|DUF4833-domain-containing-protein	unknown	unknown	gnl\|CDD\|374374
NZ_CP049246.1\|WP_103906730.1\|1332578_1332995_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP049246.1\|WP_103906718.1\|1315712_1317743_+\|excinuclease-ABC-subunit-UvrB	unknown	unknown	gnl\|CDD\|235395
NZ_CP049246.1\|WP_103906732.1\|1334625_1335126_-\|IPExxxVDY-family-protein	unknown	unknown	gnl\|CDD\|380206
NZ_CP049246.1\|WP_103906733.1\|1335656_1336910_+\|beta-ketoacyl-ACP-synthase-II	unknown	unknown	gnl\|CDD\|274452
NZ_CP049246.1\|WP_103906721.1\|1322716_1323649_-\|DUF4974-domain-containing-protein	unknown	unknown	gnl\|CDD\|226235
NZ_CP049246.1\|WP_079643602.1\|1335392_1335629_+\|acyl-carrier-protein	unknown	unknown	gnl\|CDD\|179197
NZ_CP049246.1\|WP_103906719.1\|1317799_1319335_-\|SusD/RagB-family-nutrient-binding-outer-membrane-lipoprotein	unknown	unknown	gnl\|CDD\|378943
NZ_CP049246.1\|WP_103906735.1\|1337868_1339248_+\|histidine--tRNA-ligase	unknown	unknown	gnl\|CDD\|234586
NZ_CP049246.1\|WP_103906736.1\|1339571_1340567_+\|pyruvate-dehydrogenase-(acetyl-transferring)-E1-component-subunit-alpha	unknown	unknown	gnl\|CDD\|274473
NZ_CP049246.1\|WP_103906728.1\|1329864_1330554_-\|response-regulator-transcription-factor	unknown	unknown	gnl\|CDD\|223816
NZ_CP049246.1\|WP_103906716.1\|1314374_1314848_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|377295
NZ_CP049246.1\|WP_103906731.1\|1333082_1334516_-\|pyruvate-kinase	unknown	unknown	gnl\|CDD\|223545
NZ_CP049246.1\|WP_103906726.1\|1326630_1326810_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP049246.1\|WP_103906722.1\|1323629_1324238_-\|sigma-70-family-RNA-polymerase-sigma-factor	unknown	unknown	gnl\|CDD\|274376
NZ_CP049246.1\|WP_103906727.1\|1326957_1329267_-\|5-methyltetrahydropteroyltriglutamate---homocysteine-S-methyltransferase	unknown	unknown	gnl\|CDD\|235367
NZ_CP049246.1\|WP_103906729.1\|1330575_1332450_-\|HAMP-domain-containing-histidine-kinase	unknown	unknown	gnl\|CDD\|223715
NZ_CP049246.1\|WP_103906717.1\|1314950_1315595_-\|uracil-phosphoribosyltransferase	unknown	unknown	gnl\|CDD\|234653
NZ_CP049246.1\|WP_103906734.1\|1336990_1337731_+\|ribonuclease-III	unknown	unknown	gnl\|CDD\|274024

Protein	Function_ID	Function_description	E-value
NZ_CP049246.1\|WP_103906720.1\|1319354_1322639_-\|SusC/RagA-family-TonB-linked-outer-membrane-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].	2.97042e-112
NZ_CP049246.1\|WP_103906725.1\|1326043_1326565_-\|DUF4833-domain-containing-protein	gnl\|CDD\|374374	pfam16117, DUF4833, Domain of unknown function (DUF4833). This family consists of uncharacterized proteins around 170 residues in length and is mainly found in various Parabacteroides and Bacteroides species. The function of this family is unknown.	9.02365e-35
NZ_CP049246.1\|WP_103906722.1\|1323629_1324238_-\|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.	1.41101e-35
NZ_CP049246.1\|WP_103906732.1\|1334625_1335126_-\|IPExxxVDY-family-protein	gnl\|CDD\|380206	NF033205, IPExxxVDY, IPExxxVDY family protein. This protein family is uncharacterized. Member proteins average about 160 amino acids in size, and feature two widely separated invariant Asn residues, as well as the larger (though less invariant) motif for which it is named. Members are found primarily in the Flavobacteriia branch of the Bacteroidetes.	7.06458e-23
NZ_CP049246.1\|WP_103906733.1\|1335656_1336910_+\|beta-ketoacyl-ACP-synthase-II	gnl\|CDD\|274452	TIGR03150, fabF, beta-ketoacyl-acyl-carrier-protein synthase II. 3-oxoacyl-[acyl-carrier-protein] synthase 2 (KAS-II, FabF) is involved in the condensation step of fatty acid biosynthesis in which the malonyl donor group is decarboxylated and the resulting carbanion used to attack and extend the acyl group attached to the acyl carrier protein. Most genomes encoding fatty acid biosynthesis contain a number of condensing enzymes, often of all three types: 1, 2 and 3. Synthase 2 is mechanistically related to synthase 1 (KAS-I, FabB) containing a number of absolutely conserved catalytic residues in common. This model is based primarily on genes which are found in apparent operons with other essential genes of fatty acid biosynthesis (GenProp0681). The large gap between the trusted cutoff and the noise cutoff contains many genes which are not found adjacent to genes of the fatty acid pathway in genomes that often also contain a better hit to this model. These genes may be involved in other processes such as polyketide biosyntheses. Some genomes contain more than one above-trusted hit to this model which may result from recent paralogous expansions. Second hits to this model which are not next to other fatty acid biosynthesis genes may be involved in other processes. FabB sequences should fall well below the noise cutoff of this model. [Fatty acid and phospholipid metabolism, Biosynthesis].	0
NZ_CP049246.1\|WP_103906721.1\|1322716_1323649_-\|DUF4974-domain-containing-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].	8.3838e-23
NZ_CP049246.1\|WP_079643602.1\|1335392_1335629_+\|acyl-carrier-protein	gnl\|CDD\|179197	PRK00982, acpP, acyl carrier protein; Provisional.	1.47975e-34
NZ_CP049246.1\|WP_103906719.1\|1317799_1319335_-\|SusD/RagB-family-nutrient-binding-outer-membrane-lipoprotein	gnl\|CDD\|378943	pfam12771, SusD-like_2, Starch-binding associating with outer membrane. SusD is a secreted starch-binding protein with an N-terminal lipid tail that allows it to associate with the outer membrane.	4.61654e-39
NZ_CP049246.1\|WP_103906735.1\|1337868_1339248_+\|histidine--tRNA-ligase	gnl\|CDD\|234586	PRK00037, hisS, histidyl-tRNA synthetase; Reviewed.	6.46473e-140
NZ_CP049246.1\|WP_103906736.1\|1339571_1340567_+\|pyruvate-dehydrogenase-(acetyl-transferring)-E1-component-subunit-alpha	gnl\|CDD\|274473	TIGR03182, Pyruvate_dehydrogenase_E1_component_subunit_alpha, pyruvate dehydrogenase E1 component, alpha subunit. Members of this protein family are the alpha subunit of the E1 component of pyruvate dehydrogenase (PDH). This model represents one branch of a larger family that E1-alpha proteins from 2-oxoisovalerate dehydrogenase, acetoin dehydrogenase, another PDH clade, etc. [Energy metabolism, Pyruvate dehydrogenase].	0
NZ_CP049246.1\|WP_103906728.1\|1329864_1330554_-\|response-regulator-transcription-factor	gnl\|CDD\|223816	COG0745, OmpR, Response regulators consisting of a CheY-like receiver domain and a winged-helix DNA-binding domain [Signal transduction mechanisms / Transcription].	1.16101e-67
NZ_CP049246.1\|WP_103906716.1\|1314374_1314848_-\|hypothetical-protein	gnl\|CDD\|377295	pfam04308, RNaseH_like, Ribonuclease H-like. RNaseH_like is a family of uncharacterized eubacterial proteins that are distant homologs of Ribonuclease H-like. The family maintains all the core secondary structure elements of the RNase H-like fold and shares several conserved, presumably active site residues with RNase HI. This finding suggests that it functions as a nuclease.	5.5958e-43
NZ_CP049246.1\|WP_103906731.1\|1333082_1334516_-\|pyruvate-kinase	gnl\|CDD\|223545	COG0469, PykF, Pyruvate kinase [Carbohydrate transport and metabolism].	0
NZ_CP049246.1\|WP_103906718.1\|1315712_1317743_+\|excinuclease-ABC-subunit-UvrB	gnl\|CDD\|235395	PRK05298, PRK05298, excinuclease ABC subunit UvrB.	0
NZ_CP049246.1\|WP_103906727.1\|1326957_1329267_-\|5-methyltetrahydropteroyltriglutamate---homocysteine-S-methyltransferase	gnl\|CDD\|235367	PRK05222, PRK05222, 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; Provisional.	0
NZ_CP049246.1\|WP_103906729.1\|1330575_1332450_-\|HAMP-domain-containing-histidine-kinase	gnl\|CDD\|223715	COG0642, BaeS, Signal transduction histidine kinase [Signal transduction mechanisms].	1.71865e-40
NZ_CP049246.1\|WP_103906717.1\|1314950_1315595_-\|uracil-phosphoribosyltransferase	gnl\|CDD\|234653	PRK00129, upp, uracil phosphoribosyltransferase; Reviewed.	1.36709e-79
NZ_CP049246.1\|WP_103906734.1\|1336990_1337731_+\|ribonuclease-III	gnl\|CDD\|274024	TIGR02191, Ribonuclease_3, ribonuclease III, bacterial. This family consists of bacterial examples of ribonuclease III. This enzyme cleaves double-stranded rRNA. It is involved in processing ribosomal RNA precursors. It is found even in minimal genones such as Mycoplasma genitalium and Buchnera aphidicola, and in some cases has been shown to be an essential gene. These bacterial proteins contain a double-stranded RNA binding motif (pfam00035) and a ribonuclease III domain (pfam00636). Eukaryotic homologs tend to be much longer proteins with additional domains, localized to the nucleus, and not included in this family. [Transcription, RNA processing].	8.74905e-61

>NZ_CP049246.1|WP_103906727.1|1326957_1329267_-|5-methyltetrahydropteroyltriglutamate---homocysteine-S-methyltransferase
MLLTNNLGYPRVGAFRELKKANEAYWAKKISAEELLQAGLKIRESNWNTQKENGIELIPSNDFSFYDQVLDLSLTVGAIPARYNSLLNKIDRQYNLDLYFAMARGFQEGGVDVTAMEMTKWFDTNYHYIVPEFVKDQEFKLTSEKFLNEYNEAKKLGIETKPVLIGPITYLLLGKEKEAGFNRIDLIDKLLPVYEEILGKLADAGAKYVQIDEPFLALDIDDATKALYPEVFEKLAAAAKGIKLIVATYFEALRDNEDIAVNLPVHALHLDLVRGENQLDTILAKVPANLTLSLGVVEGRNIWKNDYENSLKKIKQAVDALGKDRVWIAPSSSLLHVPFDLDNENNEESLPAEVKNWLAFAKQKLAEVRDLAVLAEGDVDAETQKRFEANKEAAESRRTSPLIHKPEVKNRVSNITDEDAKRTSTFNARKEAQQAKFNLPGFATTTIGSFPQTKDVRKWRADLKKGAITQEQYDKEIAEETERTIRLQEELDIDVLVHGEFERNDMVEYFGEQLAGYAFTQNGWVQSYGSRCVKPPIIFGDVYRPEDMTVRWSAYAQSLTNRPVKGMLTGPVTILQWSFVRNDQPRSTTTYQIALAILDEVQALEKAGIKIIQIDEPAIREGLPLRKADQQAYLDWAVRSFRVSSSNVEDDTQIHTHMCYSEFNDIIQDIAAMDADVITIETSRSQMELLDAFADFKYPNDIGPGVYDIHSPRVPSTEEMVNLLRKAKAVVPAEQLWVNPDCGLKTRAWPETKAALESMVEAAKILRAE
>NZ_CP049246.1|WP_103906726.1|1326630_1326810_-|hypothetical-protein
MNNRLLGFLGVALASMLFSSCNLIEGIFKAGMWWGIILVVGAVALVIWLFSKMFGGRRD
>NZ_CP049246.1|WP_103906725.1|1326043_1326565_-|DUF4833-domain-containing-protein
MIRITCFIILMFLAGLPIIAQEGYPEPSDKNGLLFYIQHNRGKNTFFYSLNYRGKHQLDQDDPIKVQRELYDEDGAIKPLSAVQRAFAYGISTKKRQHGYEAAIVSMPSQKLYLFTPAHKPAYVETTVNGKSIRLKRIFIKQKDGTSGLGTKVDYILFYGTHNNKAVIEKLIP
>NZ_CP049246.1|WP_103906722.1|1323629_1324238_-|sigma-70-family-RNA-polymerase-sigma-factor
MNDHPFNFALFYKENKNQIYNYAVYHLKDKDAAADIVQEAFLRLWNQKEKLDAQQHIKAYLYSICKNLVFDELKQNNRYSQYAHYIQQAGTPSENSTEDQQNYSELWSLYQEAIANLPLKRQQIFRMSRQSFLSNDDIAVELQLSKNTVKDQIVKSNRYIKDFILRNSQSIPKKIFSLLIVLSSPNTVYILKTYILNGFKPL
>NZ_CP049246.1|WP_103906721.1|1322716_1323649_-|DUF4974-domain-containing-protein
MDSSRFSYLYRRYLANQCTESELKEFLELLKDQDEPANLLDPEEFNQQFDLQHQLPEDQSEAIFNRITQPKKHTWKLYTTVAGIAALLLSIICASLFLLKSPESQYKIFTNTTEDILRIALEDGSVILLRPQAVLTQSHAFQSEPFRKVKLQGEAFFIVAKDPSRPFQVQSESETSIQVYGTRFNLKFTPSAKEVVLTEGSLGMKHGTQEVRLNPQEKAYITADYPHIQKTAVDTMKYMAWTEHQLYFTDEPLHEVLKTLKGHYPEQSLQLPKQFQGLRFTGYLPDNNLPESIQILESTFKNYNLVINKN
>NZ_CP049246.1|WP_103906720.1|1319354_1322639_-|SusC/RagA-family-TonB-linked-outer-membrane-protein
MDLIAFQDRSMIELIQHLEGKFNVRFNYESNLKHVKIKNDFQNNRIQKADLPNFIKDVTFDQVEAEIVGQNAYILKVKAKPAQPRTGNAPSNARTTSALQQVVKGKIVDQETGAALQGVTVRIKGTEVAGQTDANGQFQLHSGETNPTLVITTLGYNRLEAVAGDNMTYSLTSSDQSIEEVVVTALGIKREQKALGYAVQDIKGDQLQKVKGVDVGTTLTGRIAGLRVNNSTEFNAMPTISLRGMSALLVIDGVAYENLNLRDVPVDNIANISVLKGSTAAALYGSKGAGGAIMITTKKGLNKKGTEINVNSNNMFFAGHLALPSVQSAYSAGEGGKYNTNDYVWGDKLDIGRKYEQWNPISKQMELAELTSRGKNNFQNFLEPGIISNNSVSFTNQGEYGSIRTSINHVYNKGQYPNQTLNMTNISVSGETKISEKISLESRFGYNRSFAPNDYGAGYGNQGFIYNILVWSGPEYDLSQYKDYWLVKDQKQNWHYNAWYDNPYLSAHEKLTSKLHNKLNAAVTLNYKFSDWGKVMLRSGYDYYGTTQEQTNPQGIYGTRGGFSGYHSNGKYWTRKLDGFATNNDLIFTANKTFGDFTIEGLAGAAVSYVRDNSIWASTVNGLAIPGFYSLNNSIDPTTTRESKTKNMLNSVYGRASLSWRNAIFVEATGRNDWSSALPKETRSFFYPSLSGSVILSDLLPDYKPSWLTMLKARGSWAVSKQVLDPYVINQAYNISSNAWDGLTMAGYPSTIKDYSISPTQRDLTEIGVDMAFLNNRIYANYTRYYRLLHNRSIETTISSGTGFNKRLINTAEQLMTKGHEITIGGAAIKKQDFQWDVVANLSQNLEFFHQLDPEYSADALYIKKGLRTDYYTVRDYERSPDGQVVHNSAGMPVSANYAAQLFGYSAPKWFWGLSNQFTYKDFGLSFSLDGRVGGLSYSNMNARLWQTGAHPDSDSKERYEEVVNSNKTFIGNGVRIVSGSVSYDKYGQVIKDDRVFAANDTKVSYENYWKSAYSGRQNIWDETFIKLREVSLNYYLPKETAERFKAKRASVGITGQNLFLWTKEYKFSDPDRGAEDLNSPSIRYVGFNLNLTF
>NZ_CP049246.1|WP_103906719.1|1317799_1319335_-|SusD/RagB-family-nutrient-binding-outer-membrane-lipoprotein
MKMKNLYTFLLIGASTLALGSCSKFEEINTNPETTNVVTPAMIATRVIVNMANQPSQKAFMMPYLLNKNIVWTEFVESYQYNGGFNSGQLNFTSINDLASMVKFAPTEKLAKSYEGLMYFSRALKFFNTTMDLGDIPYAEALKGESDKNYFPKYDTQKDVLLGVLKELELADKAFSEGENFSGDPIYKGNTTSWRKLTNSFMLHVLIQLSKKESDADLNIKSRFRTIVSNKPIFASNSDNYELKRANKSGQLYPFYKVGNNFTIYPIISSEIIEPLKSREDRRLFFYANPSEKRIAEGKSPAAFDAYAGIDPSLPFDVVTSIKNTKDFSKLNNRYLDIPTGEPTQQLSYAQLCLVIAEAATRGWIADQPVDWYKKGIQASMEFIQTNTPNAEGYTHGMPLSNDYIASHVQKMGSKFPTATEARIEEIITEKYLASFLQSEFMTYYDYRRTGFPKWKINPSTSLNSEAPTKIPVRWKYPAVENNYNSQHLDEAVKRQFNGTDDINQLIWLLK
>NZ_CP049246.1|WP_103906718.1|1315712_1317743_+|excinuclease-ABC-subunit-UvrB
MKFQLTSEYRPTGDQPSAIQQLVTGVDQGEVYQTLLGVTGSGKTFTVANVIQETQKPTLILSHNKTLAAQLYGEFKQFFPDNAVNYFVSYYDYYQPEAFIASSNTYIEKDLAINEEIEKLRLATTSALMSGRRDVIVVSSVSCIYGMGNPEDFSRSIFRFGVGTTISRNAFLHKLVEILYARTTAEFKRGTFRVKGDTIDVYPAYKDTAYRISFFGDDIDELSEIDPVSGKTLEKHETLALFPANLFVTPKEKFTQSIWQIQDELVMRKAQLENDGKMLEAKRLEERVNYDLEMMRELGYCSGIENYSRFFDGRQPGMRPFCLLDYFPDDYLLVIDESHVTIPQLRAMYGGDRSRKISLVEHGFRLPAALDNRPLNFPEFESLTNQTIYVSATPGDYELQQTEGVFVEQVIRPTGLLDPVVEVRPAINQVDDFLEEVDKTIKEGGRILATTLTKRMAEELTKYMTRLNIKVRYIHSEVKTLERVEILRGLRLGEFDVLVGVNLLREGLDLPEVTLVAILDADKEGFLRSERSLIQTIGRAARNDKGRVIMYADKMTDSMRITIEETDRRRDKQIAYNQEHGITPRTVGKTKEEILEQTSVANFNGEAKIYVEPEPGATVAADPLIEYMSEKDMKKAIETVRKRMEKAAKEMEFLEAAKLRDEMFALEKAFDDKFGK
>NZ_CP049246.1|WP_103906717.1|1314950_1315595_-|uracil-phosphoribosyltransferase
MATILTKQNTIANHFLAELRNVNVQQDRMRFRRNLERLGEIMAYEISKTFEYAQVEVDTPLGVAETSLILNQPVIATIIRAGLPFHQGFLNYFDGADSGFIAAYRHTKKSGEFEVHKKYQNCPNLDDKIVIVADPMLATGRSLVLCCKDLLSDYDIKELHIATVIASEEGLQHVKAFLPEAHVWVGAVDNELTSKSYIVPGLGDAGDLAYGNKE
>NZ_CP049246.1|WP_103906716.1|1314374_1314848_-|hypothetical-protein
MEWQKYNGETIKLPIWSAVEETLIREKDAGNKLKVYIGTDSQVKRGVVEFATVIVFLREHRGGFMFIHKDRKTHNMTIKERMLLEVQHSIETAYELCPLLDQYQIDLEVHADINTNPNFQSNTALKEAMGYILGMGFIFKAKPESFASTNCANKLVQ
>NZ_CP049246.1|WP_103906728.1|1329864_1330554_-|response-regulator-transcription-factor
MNQKILLAEDDPNLGELLKDYLELKGKFDVVLCVDGQEAMDAFRKDEFDLCILDIMMPKKDGFSLGKDIRKINQTIPIIYATAKGMMEDKTQAFELGGDDYITKPFRVEELLLRINALLKRAAKDKEEEVSDKFEIGDYFFDYTSQIISYKGQQQKLSTKEAELLRLLCLKKNDVLTREEALIKIWHDDNYFTGRSMDVFLSKLRKYLKEDPNVEIVNVHGKGYKLLVS
>NZ_CP049246.1|WP_103906729.1|1330575_1332450_-|HAMP-domain-containing-histidine-kinase
MKKRSIALIIGLMSIALIGVMAMQYYFVRESFHKESKLFDEEVKASLSAVANKIERKEIYDFARQQERENQKKFRADQERLQKNEKLLALQLQYQDSIKILQRLAFLHTQNFNSLRTQLNQQFPAVEINNEFFETYIRRKEYRHLVRVTLQQEFTPDNTIAEFTNIEATRALKPVPAKDDSTRFLIPIFPVNSVVAADFKISTLPPEVNKRILSKATELEGKLQKLRTQKLGGAHTLFDSIAILGGKKSSVVADVARGMELAKRPLAERINGPYSLKLLAKELNERGVNSSFVMEIKDSKSSPAVFQGVYQFGEEDLKEVKNPTLYTARLFQGDQGQSPGELSIYFPNKGGIIAETMGYWLFPTILALLALLIGCFAYTLSIIFKQKKISEMKTDFINNMTHEFKTPVATIMIASESLKDPEISADGKRVSKLANIIYDENVRLGSHIERVLNIARLEKENLKIERVNVHINTIAHAVLESMRLQLEKADGILNVNLEATNDLVIGDELHLSNVMFNLVDNAIKYAKDKPEITFRTFNRGNQIVISVADKGMGMTKDQAEKIFDQFYRIPTGNIHNVKGFGLGLSYVNDIIRRLNGKITVKSEKDKGTQFEVTLPLKNASKEVA
>NZ_CP049246.1|WP_103906730.1|1332578_1332995_+|hypothetical-protein
MKVFSLLVLLMMVWCFSSSAQNKEKKSEKESTKAAKTPALRDSSIFPNYKDSLVIDIVPQKRKDVPFPNITGKNQDDGSIAIPNAGKKPLLQGQDDSVILRKDLPGDKSVPMKGTERLDRKQRGNAIDTLKTEKIIKK
>NZ_CP049246.1|WP_103906731.1|1333082_1334516_-|pyruvate-kinase
MDKLKKRTKIVATLGPASSKKDVLTRMIAKGVDVCRLNFSHGSQEDHLKVINTINEINAEHPFNVGILADLQGPKIRIGKVKEGGAILVNGSELEITTHELIGDEKQIYITYENFPNDVKEGEIILLDDGKLQLRVLSTNHKDTVKCEVVHGGILTSRKGVNLPNTKVSIPSLTEEDLDNLNFALDHGADWIAMSFVRSAEDIHQCKEIIKEKGSHARVIAKIEKPEAIENIDAIIEATDAIMVARGDLGVELPMEEVPGLQKIIAQKCRDLSKPVIIATQMLESMITTPRPTRAEVNDVANSVIDGADAVMLSGETSVGEFPEIVIETMAKVITHVEATSYPYYSEKQTLGTVAVTRIPDAICSSSIFLAEKTNASAIAVMTSSGYTAMEIASYRPDADIYVFTGNKTLLRTLSLVWGAQAFMYEKYESTDGTIQDVNKLLRENHLVEPGQIVINTSSTPLHEKGRTNTIRVSEVK
>NZ_CP049246.1|WP_103906732.1|1334625_1335126_-|IPExxxVDY-family-protein
MSKITFKLETDFDLELDFVLIGISSVLRDYRLCHFINKHTGLQFVYGKEDYLDHNGHEKEKPKDELDYHIIYETKKNKPTVQHHYNIFRYHNQTFEFEFYLLSNRSIEGAALIPEILSFDYFLMVKHFIDQEDLDALLENIKAIPEVLLVKEIDPTILKSKENLIF
>NZ_CP049246.1|WP_079643602.1|1335392_1335629_+|acyl-carrier-protein
MSDIASRVKAIIVEKLGVDENEVTPEASFTNDLGADSLDTVELIMEFEKEFNVAIPDDQAENISTVGQAIAYLEKNVN
>NZ_CP049246.1|WP_103906733.1|1335656_1336910_+|beta-ketoacyl-ACP-synthase-II
MELKRVVVTGLGALTPIGNTVPEYWDGLVNGVSGAAPITHFDASKFKTQFACEVKGFDPHDFMDRKEARKLDPFVQYAIASTDEAVKDAGLEFDKLDRTRIGVIWGSGIGGLTTFSEEVATFSKGDGTPRFNPFFIPKMLIDLAPGHISMRHGLQGPNFSAVSACASATNAMIDAFTYIRSGRADIIITGGSEATINEAGIGGFNAMHALSTRNDDPKTASRPFDKDRDGFVSGEGSGAIILESLEHALARGAKIYAEVVGGGMSADAYHITASHPEGQGAKLAMTMAIKDAGMDFSDIDYINVHGTSTPVGDVSETKAIVDLFGEHAYNLNISSTKSMTGHLLGAAGAVEAIASILAVKNDIVPPTINHFTDDPEIDNRLNFTFNKAQERVVNAALSNTFGFGGHNATVIVKKYNG
>NZ_CP049246.1|WP_103906734.1|1336990_1337731_+|ribonuclease-III
MAIAQVYNLYLSPNRQYVRRLKNLLGFVPGNIRLYQMAFRHKSVAVMIKDGVKNSNERLEFLGDAVLGSVVAELLFKLYPYKDEGFLTEMRSKIVSRANLNQLSRKLGFNEMIEFDARMISYPNKQGSLLGDAFEALIGAVYLDKGYTFTREFLLSRIIKPHVDIHTLEVTETNFKSRLIEWCQHTGKEISFVLVDNPEGESNKMFSVVAVVDGEECGLGRDFNKKSAEKIAAEKACEYLKIFDGE
>NZ_CP049246.1|WP_103906735.1|1337868_1339248_+|histidine--tRNA-ligase
MASIKPSLAKGTRDFSPVEMDKRNHIFNTLKAIFSKYGYSEIQTPTFENLQTLTGKYGDEGDRLIFKILNSGDYLGKAPEELLSAKNSASLISHISEKALRYDLTVPFARYVVMHQNDIALPFKRFQIQPVWRADRPQRGRYREFYQCDVDVVGSESLLNEAEFILIYHEALTAFGLKDFNIKLNNRKILSGIAEVVGKPDLIVDMTVAIDKLDKIGLDGVNKELLERGFTQDDLATLEPIIALSGSNTEKIAAMKSVLSNSTVGLEGVAELEEVFAYLTKFGRADLLEYVVEVDITLARGLNYYTGCIFEVKTNEVQMGSIGGGGRYDDLTGMFGLKGLTGVGVSFGADRIYDVLNELDLFPKEGSARTKLLIVNFDSGLESFTLPLLNQLRAADIAVELYPSAVKLKKQMSYADAKQIPYVLLVGDEEVNSGELSLKNMQTGAQEKIRTAELIEKLK
>NZ_CP049246.1|WP_103906736.1|1339571_1340567_+|pyruvate-dehydrogenase-(acetyl-transferring)-E1-component-subunit-alpha
MSSTPITKETYLEWYESMLLMRKFEEKSGQLYGQQKIRGFCHLYIGQEAVVAGTMSVIKPEDSLITAYRDHAHAIAKGVSADACMAELFGKATGCSKGKGGSMHFFSKEHKFMGGHGIVGGQIPLGAGIAFAEKYLGTDNVNICYMGDGAVRQGAFNETLNMAMLWKLPVIFVCENNGYAMGTSVKRTTNMQDIYKMGLGFDMPSAPVDGMDVVAVHNAMDEAVQRARAGEGPTFLEIRTYRYKGHSMSDPAKYRTKEELEEYKERDPIIAVKHAIVENKYADQAWFDEVEAKVKKIVDDSVKFAEESPYPDASEIYKDVYVQEDYPFVMD

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Crispr_ID: NZ_CP049246_8

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP049246_8

1488866-1489009

Orphan

Consensus_repeat	Method
GTCTAACTACTTAATTCTAACTACTACAAACTGTAACAAAAA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP049246_8

>merge|NZ_CP049246|8|1488866-1489009|CRISPRCasFinder
GTCTAACTACTTAATTCTAACTACTACAAACTGTAACAAAAAGGGTGGGCGAGGTGCAAAATTTGGCTAAAGAGATAAGTGTACTTTGCAATTCCGCCCTAGGTCTAACTACTTAATTCTAACTACTACATACTGTAACAAAAA

>NZ_CP049246|8|8|1488866-1489009|CRISPRCasFinder
GTCTAACTACTTAATTCTAACTACTACAAACTGTAACAAAAA	GGGTGGGCGAGGTGCAAAATTTGGCTAAAGAGATAAGTGTACTTTGCAATTCCGCCCTAG
GTCTAACTACTTAATTCTAACTACTACATACTGTAACAAAAA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP049246.1\|WP_160003759.1\|1477068_1478022_+\|siderophore-ABC-transporter-substrate-binding-protein	unknown	unknown	gnl\|CDD\|238560
NZ_CP049246.1\|WP_103906871.1\|1489039_1489684_-\|outer-membrane-lipoprotein-carrier-protein-LolA	unknown	unknown	gnl\|CDD\|319983
NZ_CP049246.1\|WP_103906868.1\|1486211_1486931_+\|CoA-transferase-subunit-A	unknown	unknown	gnl\|CDD\|224702
NZ_CP049246.1\|WP_103906865.1\|1481652_1483272_+\|peptidase-M14	unknown	unknown	gnl\|CDD\|349476
NZ_CP049246.1\|WP_103906875.1\|1494663_1495347_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP049246.1\|WP_103906872.1\|1489683_1492305_-\|DNA-translocase-FtsK	unknown	unknown	gnl\|CDD\|224588
NZ_CP049246.1\|WP_103906874.1\|1493290_1494574_-\|tyrosine--tRNA-ligase	unknown	unknown	gnl\|CDD\|235645
NZ_CP049246.1\|WP_103906877.1\|1497181_1499122_-\|KUP/HAK/KT-family-potassium-transporter	unknown	unknown	gnl\|CDD\|376906
NZ_CP049246.1\|WP_103906876.1\|1495390_1497091_+\|amino-acid-permease	unknown	unknown	gnl\|CDD\|129987
NZ_CP049246.1\|WP_103906878.1\|1499329_1499755_+\|T9SS-type-A-sorting-domain-containing-protein	unknown	unknown	gnl\|CDD\|275036
NZ_CP049246.1\|WP_103906879.1\|1499903_1501193_-\|citrate-synthase	unknown	unknown	gnl\|CDD\|99867
NZ_CP049246.1\|WP_103906866.1\|1483283_1485065_+\|peptidase-M14	unknown	unknown	gnl\|CDD\|349476
NZ_CP049246.1\|WP_103906864.1\|1479756_1481292_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP049246.1\|WP_103906873.1\|1492529_1493228_+\|DUF4397-domain-containing-protein	unknown	unknown	gnl\|CDD\|379570
NZ_CP049246.1\|WP_103906870.1\|1488108_1488738_+\|CoA-transferase-subunit-B	unknown	unknown	gnl\|CDD\|188219
NZ_CP049246.1\|WP_103906880.1\|1501506_1501869_+\|transcriptional-regulator	unknown	unknown	gnl\|CDD\|367747
NZ_CP049246.1\|WP_103906869.1\|1486920_1488105_+\|acetyl-CoA-C-acyltransferase	unknown	unknown	gnl\|CDD\|238383
NZ_CP049246.1\|WP_146060640.1\|1485141_1485732_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP049246.1\|WP_103906862.1\|1478026_1478836_+\|siderophore-interacting-protein	unknown	unknown	gnl\|CDD\|99790
NZ_CP049246.1\|WP_103906863.1\|1478843_1479773_-\|hypothetical-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_CP049246.1\|WP_160003759.1\|1477068_1478022_+\|siderophore-ABC-transporter-substrate-binding-protein	gnl\|CDD\|238560	cd01140, FatB, Siderophore binding protein FatB. These proteins have been shown to function as ABC-type initial receptors in the siderophore-mediated iron uptake in some eubacterial species. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.	1.09065e-103
NZ_CP049246.1\|WP_103906871.1\|1489039_1489684_-\|outer-membrane-lipoprotein-carrier-protein-LolA	gnl\|CDD\|319983	cd16325, LolA, LolA, a periplasmic chaperone. This family contains periplasmic molecular chaperone LolA which binds to outer-membrane specific lipoproteins and transports them from inner membrane to outer membrane (OM) through LolB, a lipoprotein anchored to outer membranes. There are five Lol proteins (LolA, LolB, LolC, LolD, and LolE) involved in the sorting and membrane localization of lipoprotein and are highly conserved in Gram-negative bacteria. LolA accepts OM-specific lipoproteins that are released from the inner membrane by the LolCDE complex and transfers them to the OM receptor LolB. Studies have shown that hydrophobic surface patches large enough to accommodate acyl chains of the OM lipoproteins and the structural flexibility of LolA are important factors for its role as a periplasmic chaperone.	4.67419e-21
NZ_CP049246.1\|WP_103906868.1\|1486211_1486931_+\|CoA-transferase-subunit-A	gnl\|CDD\|224702	COG1788, AtoD, Acyl CoA:acetate/3-ketoacid CoA transferase, alpha subunit [Lipid metabolism].	1.38035e-109
NZ_CP049246.1\|WP_103906865.1\|1481652_1483272_+\|peptidase-M14	gnl\|CDD\|349476	cd06905, M14-like, Peptidase M14-like domain; uncharacterized subfamily. A functionally uncharacterized subgroup of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavages. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism.	7.6396e-87
NZ_CP049246.1\|WP_103906872.1\|1489683_1492305_-\|DNA-translocase-FtsK	gnl\|CDD\|224588	COG1674, FtsK, DNA segregation ATPase FtsK/SpoIIIE and related proteins [Cell division and chromosome partitioning].	9.36021e-129
NZ_CP049246.1\|WP_103906877.1\|1497181_1499122_-\|KUP/HAK/KT-family-potassium-transporter	gnl\|CDD\|376906	pfam02705, K_trans, K+ potassium transporter. This is a family of K+ potassium transporters that are conserved across phyla, having both bacterial (KUP), yeast (HAK), and plant (AtKT) sequences as members.	0
NZ_CP049246.1\|WP_103906876.1\|1495390_1497091_+\|amino-acid-permease	gnl\|CDD\|129987	TIGR00909, putative_amino_acid_transporter, amino acid transporter. [Transport and binding proteins, Amino acids, peptides and amines].	1.79722e-95
NZ_CP049246.1\|WP_103906878.1\|1499329_1499755_+\|T9SS-type-A-sorting-domain-containing-protein	gnl\|CDD\|275036	TIGR04183, hypothetical_protein, Por secretion system C-terminal sorting domain. Species that include Porphyromonas gingivalis, Fibrobacter succinogenes, Flavobacterium johnsoniae, Cytophaga hutchinsonii, Gramella forsetii, Prevotella intermedia, and Salinibacter ruber average twenty or more copies of a C-terminal domain, represented by this model, associated with sorting to the outer membrane and covalent modification.	0.00040361
NZ_CP049246.1\|WP_103906879.1\|1499903_1501193_-\|citrate-synthase	gnl\|CDD\|99867	cd06114, EcCS_like, Escherichia coli (Ec) citrate synthase (CS) GltA_like. CS catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). Some type II CSs including EcCS are strongly and specifically inhibited by NADH through an allosteric mechanism. Included in this group is an NADH-insensitive type II Acetobacter acetii CS which has retained many of the residues used by EcCS for NADH binding.	0
NZ_CP049246.1\|WP_103906866.1\|1483283_1485065_+\|peptidase-M14	gnl\|CDD\|349476	cd06905, M14-like, Peptidase M14-like domain; uncharacterized subfamily. A functionally uncharacterized subgroup of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavages. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism.	8.02677e-147
NZ_CP049246.1\|WP_103906874.1\|1493290_1494574_-\|tyrosine--tRNA-ligase	gnl\|CDD\|235645	PRK05912, PRK05912, tyrosyl-tRNA synthetase; Validated.	0
NZ_CP049246.1\|WP_103906873.1\|1492529_1493228_+\|DUF4397-domain-containing-protein	gnl\|CDD\|379570	pfam14344, DUF4397, Domain of unknown function (DUF4397). This presumed domain is functionally uncharacterized. This domain family is found in bacteria, archaea and eukaryotes, and is approximately 120 amino acids in length.	2.04538e-07
NZ_CP049246.1\|WP_103906870.1\|1488108_1488738_+\|CoA-transferase-subunit-B	gnl\|CDD\|188219	TIGR02428, 3-oxoadipate_CoA-transferase_subunit_B, 3-oxoacid CoA-transferase, B subunit. Various members of this family are characterized as the B subunits of succinyl-CoA:3-ketoacid-CoA transferase (EC 2.8.3.5), beta-ketoadipate:succinyl-CoA transferase (EC 2.8.3.6), acetyl-CoA:acetoacetate CoA transferase (EC 2.8.3.8), and butyrate-acetoacetate CoA-transferase (EC 2.8.3.9). This represents a very distinct clade with strong sequence conservation within the larger family defined by pfam01144. The A subunit represents a different clade in pfam01144.	8.5185e-118
NZ_CP049246.1\|WP_103906880.1\|1501506_1501869_+\|transcriptional-regulator	gnl\|CDD\|367747	pfam03965, Penicillinase_R, Penicillinase repressor. The penicillinase repressor negatively regulates expression of the penicillinase gene. The N-terminal region of this protein is involved in operator recognition, while the C-terminal is responsible for dimerization of the protein.	2.51236e-24
NZ_CP049246.1\|WP_103906869.1\|1486920_1488105_+\|acetyl-CoA-C-acyltransferase	gnl\|CDD\|238383	cd00751, thiolase, Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA, a 2-step reaction involving a covalent intermediate formed with a catalytic cysteine. They are found in prokaryotes and eukaryotes (cytosol, microbodies and mitochondria). There are 2 functional different classes: thiolase-I (3-ketoacyl-CoA thiolase) and thiolase-II (acetoacetyl-CoA thiolase). Thiolase-I can cleave longer fatty acid molecules and plays an important role in the beta-oxidative degradation of fatty acids. Thiolase-II has a high substrate specificity. Although it can cleave acetoacyl-CoA, its main function is the synthesis of acetoacyl-CoA from two molecules of acetyl-CoA, which gives it importance in several biosynthetic pathways.	0
NZ_CP049246.1\|WP_103906862.1\|1478026_1478836_+\|siderophore-interacting-protein	gnl\|CDD\|99790	cd06193, siderophore_interacting, Siderophore interacting proteins share the domain structure of the ferredoxin reductase like family. Siderophores are produced in various bacteria (and some plants) to extract iron from hosts. Binding constants are high, so iron can be pilfered from transferrin and lactoferrin for bacterial uptake, contributing to pathogen virulence. Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and has a variety of physiological functions including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation in a variety of organisms. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one-electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and two electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).	6.84941e-74

>NZ_CP049246.1|WP_103906870.1|1488108_1488738_+|CoA-transferase-subunit-B
MLDKFGIAKRIAKEVKDGYYVNLGIGIPTLVANYIPEGINVVLQSENGLLGMGPFPLEGEEDADYINAGKQTITTLPGSAFFDSAMSFGMIRARRVDLTILGAMEVSENGDIANWKIPGKMVKGMGGAMDLVASAENIIVAMQHVNKAGESKLLPSCTLPLTGVRCVKKIVTELGVFEIVPEGGFKVLELHEGVSLDQVRQSTAGKLVY
>NZ_CP049246.1|WP_103906869.1|1486920_1488105_+|acetyl-CoA-C-acyltransferase
MSNNKKVYIVAAKRTAMGSFGGAISSVSATKLGAAAISGALDSLELGNYEVDEVYMGSVLQANLGQAPARQASKFAGLPDHVPATTINKVCASGMKAVSIAAQQILLGDAKVVVAGGMESMSQVPYYDSAARWGAKFGHQQLEDGLLKDGLTDVYSDQAMGNCGELCAEKYELSREDQDEYAIQSYTRSKIAWESGKFAGEVVPVEVKTRKGVEEFSEDEEYKNINFDKVGQLRPSFKADGTITAANASTLSDGAAALVLMSGEKVAELGLTPLAEVVAYADAEQSPEWFTTTPAIATQKVLQKAGLTIDDIDYFEFNEAFSVVALANAKILEISSSKINVYGGAVALGHPLGCSGARILVTLISVLKQENGTLGLAAICNGGGGASAMILKKC
>NZ_CP049246.1|WP_103906868.1|1486211_1486931_+|CoA-transferase-subunit-A
MIDKSVSNAKEAIQDIADGMTISLGGFGLCGIPENLIAALLEKGVKDLTCISNNAGVDDFGLGLLLQHKQVKKMIASYVGENAEFERQMLSGELEVELIPQGTLATRLMAGGYGMPVIYTPAGVGTEVAEGKESRTFTFHGVEKEYLMEYAFEPDYALVKAWKGDRDGNLVYRGTAQNFNHAVAMCGKITIAEVEELVEPGELDPNHIHTPGIFINKIFQGENYEKRIEQRTVRQKDEQ
>NZ_CP049246.1|WP_146060640.1|1485141_1485732_-|hypothetical-protein
MTRLLAIILFFWVLVPSVSGQTLQQKLMTSSLDSQFVVLNLQSRSQDKDFKIIRKTNLDIIRKNVRDSLNTYKKQIATLRGDASSSEGNILGLQDSVKSLSAALSAEQQKTDSISFLGIQFSKSSYHTMVWVIIIVLAAALFGILAAFRKAKVDTTESKNTVDELQEELQTLRKKSMEREQLLKRQLLDEQLKRNS
>NZ_CP049246.1|WP_103906866.1|1483283_1485065_+|peptidase-M14
MKFTQSILAMALAFSLSTAIAQNKKDDVSREIAGLRAVGSPSNPKVPMNWSRYHDLKQMEQFYRDLQKAYPNLIKYESIGKSFEGRDIFVLTVTDFNQGKAEQKPAMWIDGNIHANELQGSEISMYTAWYLVENYNAVPFIKELLKDKVFYIAPTINPDSREYFIYNPNTMHSSRTGRRPFDNDGDGLVAEDLYDDLDKDGEIVMMRRKSKTGRYKVDPDNPNRMVMVKPGEVGEYELLGFEGIDNDGDGLVNEDITGTYDPNRDWGWNWQPNYVQGGALYYPGTLPETQAVKKFIYAHPNIAGAQSYHNYGGMILRGPGAAEDERFYSRKDVQVYDALGKTGEKMLPGYNYIVIHKDLYTVFGGEIDFLALTRGIFTFSNELMTTYKLFNEKAEGGMRQSDEYYEFDRLLMFGDAYVPWKEFDHPQYGKIEIGGAKKNYTRNHPGFLLMEDAHRNAAFTIYHAYHLPKLELMESSITPLGGNLYEVNATIWNTRIIPTHSDHDVKHRIERPNHIRLEGAKVVTGMQVINKDFNETREQKYKPEQIEVNSIDGMSAVQVRWIVRGNPNAAKLIVDSPKGGYQEFQLKETAGKS
>NZ_CP049246.1|WP_103906865.1|1481652_1483272_+|peptidase-M14
MKYVMLLLISCSMPFFAQAQWNYPSYDALKKQFNTLSSHSSVEMASIGKSYGGEEIPMLKIQKDKLSRPTLLIVAGVDGRHPAGVLQSLRIVQEIVGKPQGELESLLSEKSIWVIPVLNPDAYKRNINSGRWHAGNGRAIDNDRDGRLDEDPDVDLNKDGVISQMRVKSPAGQYKVHPLHPSVLVQADRSKGESGQYELFMEGMDTDHDGQYGEDPSAGVNIDRNFTFDYPFFESETGDYAASEPETRAFMDLLFDQPQVAAVLHLGMQNNLSVAEPFDQRKASERIVKSWSKNDVQVAAMVSKLYNDAVKSQGEAPKLPAGKGNLSTTAYYHAGKFSFVTPGWWIPANSDTSKNVQRVPNGKELDRLVNWVNNKGVQGAVLPWTKIDHPDFPGQEVEVGGVVSAFLNNPPIDHLEGPAKLHTEFVLQLAKSLATLEFSTPKVTALGDDIHRIEIRLYNTGAMPTYPEIADRIKHVSKMKAILDMQKNQSFLSGKRLQLYPALQPGDALSLSWLVKGKGTVKLTVGCPTAGEKTVDIKL
>NZ_CP049246.1|WP_103906864.1|1479756_1481292_-|hypothetical-protein
MNQNLNFLFLFLLLLTTSCKKEFSQISKDTSPRYIGQDEFKELGYGYDILEEIGSPKAVRGKILRIEDLHEANHKTIEFKPLDYQDGYLLSGETSSAYKKLLSNDLNIYAKTIFKIAEATLTAGFKKNTRDSNYYSYATFDKLILKNKISFVGDMRMLKSYIEPNFVRDCETLAPAELVNTYGTHVVLNFMNGAKLHFAYRSRANHSNKNQTVKAGLKATITTLFAGTTFNYDGSYTKEESSSNSEAELYYKTYGGDPTKSLEESISLSNPKTTKINTSNWQSSVTNNNSQIVKINKNGLIPIYEFIEDHEKRAKVKDYILYSYLKIFKTDTNLELFSTGDILGAGHTLDDIESAIMIFPDRPRIIKGSINTYNQTSNERMNTILREVNSSNSIQLFNKRISTFRYFTFGSMHGLSNFSSTPILNALSDIDKIEINNSAYDESHYKVERKLDLIKFQNKIYVRFYEKPQDKPETTTIYPIYDEKAISFYNFNKNRINQVKSISGYIVGPYF
>NZ_CP049246.1|WP_103906863.1|1478843_1479773_-|hypothetical-protein
MGPISNISHHLREKNDYFLRWYKKSLFLYVVTFCASATTVSAQYLQKESTSYQNFSKIIQNENLKWSIAGNENGLSPNILSELSWKNVYSGSKYALGLKLKDISYEFSYSELISYKGTALDQDFKSDNKTDIIYSKELFSSGSKKSDLTFEVSHKNFMRNFYIGITKVNSTNLLFHKNSELISSYHFKKNGIIISFKDIVSLNNLEFSTVFSISPNKYFAQAQWAERTNLNQNPSFIHKSFGLDFKSSMSIHYLIFPSVHTGIKTETYMSKGFKGVDYLFYKNGNIAKTQFNGSQNKYFNFGLSVLFKI
>NZ_CP049246.1|WP_103906862.1|1478026_1478836_+|siderophore-interacting-protein
MEKPKISKYVFKVTAKENITPHYIRIKLKSDEDIEFDQCTPGANNKIFIPPSGTREVQFSTFDPEKGEWVMPDDAIKPIVRTYTHRAIDPETKEITIDFVNHGDNGPASAWARNAVLDDQLGVAMKIRPTVHVGEADHYLLIADSTAIPVLCCILESLPEDASGRCIVEVATPEDKHPEVQHPGFEVTWLVNPHPEKGSALAETARACAIDPDKKYFAYIAAEYSTVRDLRQYFKEELGWGAKDFYAFSYWKSGTAEDKSAQDRREERG
>NZ_CP049246.1|WP_160003759.1|1477068_1478022_+|siderophore-ABC-transporter-substrate-binding-protein
MIKKFLKTSSSLFVLVMGLQLLLSCQSSDKQAGKTAGQDTLQVSHKLGNTVLVKNPERVVVLDIGALETMDALGVKPIGIPKKFVPAYLKDLLDDPNIADVGSVIEPDFEAIAALKPQLILLSTRQERFYEELQEIAPAVFIGTDNKNYLPSFEKNVQLIGRIFEKQNDAQEQLNALETKIKQAQAKYSQDPNKALFLIFNNGKFSAFGQGSRFGFIHDVLGIKPVLDLQDESVHGQRVSNELIAESNPDYLFIVDRNAAVLGKVSSKEDVENKLIKQTNAYKQGKTFYLNPNVWFISGGGLTSVNMMVDDIVNLIQ
>NZ_CP049246.1|WP_103906871.1|1489039_1489684_-|outer-membrane-lipoprotein-carrier-protein-LolA
MMKKLLFVCIAFLAATTGFAQDKAAKALLDEVSRKYDGYSTIQSDFSFKATQKNGESYNDKGQLFLNKGANKYKINLPTQELISDGKSVWSVLKEDKEVQVSEADNSGQSIGPNNIFTFYRDGYNYVSSTDESAGKVGKLTVIDLSPADTKSNYAKIKLRINKNKHIHDVTIFDKSGAKYTYTINGLYVNSPIADAAFQFQKTKYPGFELVDLR
>NZ_CP049246.1|WP_103906872.1|1489683_1492305_-|DNA-translocase-FtsK
MAKLNTFKNSSGSTGTKKAKNTTLSYQKRSRTKSFDQFNFSEGQKKALKILGLFLLILAGLFTVAFVSYLFTWQADQSYIAQSNGGWSTLMKTTEEINDEAVETPVVENKLGKFGALLANQFMYEWFGIASFLFILVIFVIGYKFLYKRSILPVWKTIIYSAVSIIILSVTLGFAQDFISNTPHILEGKFGFWTNQILKSQIGVIGTAGLLIFIILTALVLIYNLDLKFSFQSLRNSNGDEEYDEEDEEEDLATTNQAHQNHINKVRDNTAQVATHTYNHVEEEVIEEEEEGDVDNIGLKTEPVEDNTVSLPLNTIKPNTNFGQNNQEIELTIDPPAPQEKEVVAEPALTVAKVIEEKPITANDLVEKFGEYDPKLDLSGYQYPTLDLLKDYGTGKITINQQELEANKNKIVETLRNYSIEIEHIKATIGPTVTLYEIIPKPGVRISKIKNLEDDIALSLAALGIRIIAPMPGKGTIGIEVPNSSPEMVSMRSILATEKYQKTDMDLPIALGKTISNEVYIADLAKMPHLLVAGATGQGKSVGINAILTSLLYKKHPAELKFVLVDPKKVELSLFKKIERHFLAKLPNEDEAIITDTKKVINTLNSLCIEMDQRYDLLKNAQVRNLKEYNVKFINRRLNPEEGHRFLPFIVLIIDEFADLMMTAGKEVETPIARLAQLARAVGIHLVIATQRPSVNIITGTIKANFPARLAFRVLSKVDSRTILDSGGADQLIGRGDMLLATGSDLIRIQCAFVDTPEVDQVSDFIGSQRGYPSAHLLPEYVGEDGGSDVSDFDPDDRDQLFEEAARLIVMHQQGSTSLIQRKLKLGYNRAGRIIDQLEAAGIVGPFEGSKAREVLYPDEYSLEQYLETLRKD
>NZ_CP049246.1|WP_103906873.1|1492529_1493228_+|DUF4397-domain-containing-protein
MSIPKYIISFTILVFCLITSSCSKDNALDELDAPGSFAGVSAFNAIGGSDSLELMIAGQVVNRDGEIFSEGTNLAYRTVFPGEQAIELKSFSPNAIYAKGKHHFLGSKFYSIFFWGKGSQDYYVSEDDILQPKDGFAKIRFVNLVQGLKVKLDYKNQSSVQSHSFTTPISNFVEVKQGANMELSVSSADSKLAAVEEKVWLQNQAIYTFVIYSVLNKETKQPELKLQQIKLP
>NZ_CP049246.1|WP_103906874.1|1493290_1494574_-|tyrosine--tRNA-ligase
MNFVEELRWRGMLQDIMPGTEELLNKEQVAGYIGFDPTGDSLHVGHLTQIMTLIHFQHAGHKPIALVGGATGMIGDPSFKSAERNLLDEATLKHNVASLKNQLVKFLEFGEGETDAKMVNNYDWFKDFSFLEFIRDVGKLITVNYMMAKDSVKKRLEGENGLSFTEFSYQLIQGYDFYYLWKNHGCKVQMGGSDQWGNIVTGSEIVRRQEQGTVFGLTTQLIKKSDGQKFGKTESGAVWLDAKKTSPYKYYQFWLNATDDDAKNWIKIFTLKPKEEIDAIIAEHDQAPHMRLVQKALAKDITIRTHSEQDYETAVKTSEFLFGNGTLDFLSNLDHEAVLEVFDGVPQFEIAKDKLAAGINILDLLAVDSQVFPSKGEARKMLQGGGVSLNREKLNDIEMTVNTDQLINNKYLIVQRGKKNYYLITVH
>NZ_CP049246.1|WP_103906875.1|1494663_1495347_+|hypothetical-protein
MNFLSHFYFERFATHPERVVGSLLPDLLKNFDKSYTFHPQRFEEQLFTHPLGVELSEGWYRHVEVDKLFHSSTYFIDHSHYLRKELDPVIADLPIRGTFLAHIAIELILDHLLIKHELVNVSRLYENLANVNRTVLKNYLITIGVPDVDGFLTFYDKFIAWRYIFEYKDLEQISKPLINISKRIWQFEVTADVHERMTAVLLSYTEERMHDFKDVYAYIQDNLTYLS
>NZ_CP049246.1|WP_103906876.1|1495390_1497091_+|amino-acid-permease
MANRLFRKKSVDQILSDAEHGGSGLAKVLGVRDLVSLGIAAIVGAGIFSTIGLASYNGGPAVSLLFVFVAFACVFTALSYAQFASTVPVSGSAYTYAYVAFGELFAWIIGWALVLEYAVSNMVVAISWSQYFVSMLEGFGIHLPKWLTMAPGYALDAHQKFLEVGLDKMESIDKVALQAYETAPRILDMPIIFDLPAGLITFFVTWLVYIGIKESRKASNFMVLVKVGIILAVILGGIFFVKPENWVPFAPNGLGGVMSGVAAVFFAFIGFDSISTTAEECKNPQRDLPRAMIYCLLICAVLYVAITLVLTGMVNYTELNVKDPLAYVFQYVGFDHMAGIISVTSVIAITSALLVFQLAQPRIWMTMSRDGLLWKKFATIHPKYKTPSFATIVTGIVVAVPALFFKMDFFVDLTSVGTFFAFILVCCGVLYMDASGLSKRSKFKVPYVNGKYIVGIGFIIGVILVYQFSGETVSHWMEMGSANILLHKSLVIFFWLTWLVLSYLSFKHNFSLLPVMGILINLYLMSELGASNWIIFILWLLAGLVIYFGYGYKHSKLRNREEEKTV
>NZ_CP049246.1|WP_103906877.1|1497181_1499122_-|KUP/HAK/KT-family-potassium-transporter
MSSDHKHNLNKLSWGGLLISLGIIFGDIGTSPLYVFKAIFNKGEIQELMIYGGLSCIFWTLTLQTTVKYVLITLNADNKGEGGILSLYSLVRKKAKWLIIPAIIGGSTLLADGMITPAITISSAIEGLVIKTPNFPTIPVVVLIISFLFIIQRFGTNIVGRVFGPLMMIWFTTIGVLGVSYLGHSPDIWKSLNPYYAYQLLATYPDAWFILGAIFLCTTGAEALYSDMGHVGKSNIRISWIYVKIMLILNYFGQGAWLLEHNGLLLGETNPFYAIMPDWFVIWGVTIATIAAVIASQAMISGSFTLIAEAVRLNIWPKVAIRYPSDHKGQIYVPSVNLILYLGCMLVILVFRESSNMEAAYGLAINLTFIMTTILMTVFMIRKRINAVLIGLFATVYTIIEVAFLVGNISKIAHGGWLTLLLAMSLFIVMYSWYGARKIKNRFVKFVNIRDYFPILSELSEDKSVPLFASHLVYLTSANNLYEVESKITYSIINKKAKRADVYWLVHVDVMDNPHTREYKVTQLIPGKLIRIDFHLGFREEQKISLLFRKVVEDMVKNGEINITSNYETLKKHNIPGDFNFVVLEKVISKTHFLKWNEKIITEIYKILKKLSLSEEKGFGLDSSFVTLERVPLTIPNTEEVKLTRL
>NZ_CP049246.1|WP_103906878.1|1499329_1499755_+|T9SS-type-A-sorting-domain-containing-protein
MKLELRKISRLAVCNLCLCLGLAGYAQASSLSTSTSSTVTAFDFSADKPEENEKLINNVKVFYNGIADQVAVQFKLSKSSTVSIRVMDALGNEVLSLHNGSLEAGVQNLQFETHQKLTDGFYFVRVSSGSETIVKRISVRN
>NZ_CP049246.1|WP_103906879.1|1499903_1501193_-|citrate-synthase
MSETASINLNGTTFDFPVITGTENEKAIDISKLRDQSGYITLDPGFKNTGSTKSAITFLDGEKGVLTYRGYAIEDLADKSTFLEVAYLLIYGELPTKDVLEKFRADIRSQMMIHEDMKNFFAGFPSKSHPMGQLSCLVGALSAFYPESLNPNQTDEEENKMIINLLAKMPTIVSWIQKKSLGHPVVYPKNNFGYIENFLNMIFGEVNQEKTFDPVVIDAMHKLLILHADHEQNCSTSTVRMVGSSNANMYASISAGINALWGPLHGGANQAVIEMLEAIKNDGGDADKYLAKAKDKNDPFRLMGFGHRVYKNFDPRAKIIKKACDDVLEKLGVQDPVLDIAKRLEEAALSDQYFIDRKLYPNVDFYSGIIYRALGFNSDMFTVLFALGRLPGWIAQWKEMRDNKEPIGRPRQVYIGENLRQYVPIADRK
>NZ_CP049246.1|WP_103906880.1|1501506_1501869_+|transcriptional-regulator
MEKLTLQEEEAMLSIWQLNGGFVREILENLKDGQMPYTTLASTIRNLEKKGYVKAVKYANAKRYEPMVSAEEYKAKFMNSFVGDYFKNSYKEMVSFFVKEEKLSSEELEEIMSMIKNQKS

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Crispr_ID: NZ_CP049246_9

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP049246_9

1784810-1785022

Orphan

Consensus_repeat	Method
ACGCTGGCGCAAGAGTTGTGCGGCTGCCTGTGTGTTGGAT	PILER-CR

2 spacers

The CRISPR arrays of NZ_CP049246_9

>merge|NZ_CP049246|9|1784810-1785022|PILER-CR
ACGCTGGCGCAAGAGTTGTGCGGCTGCCTGTGTGTTGGATCTCTTGTGCCTCGAAATCTTCCCCCTTTTTTAATCCCAAGCCACCCGCTAGCGCAAGAGTTGTGCGGATTTCATGCGCAGCTGTTGTTTTGTGCCTACGGCATGTTTTTTTGCCCTTTTTTTAATATCGAGCCACGCTGGCGCAAGAGTTGTGCGGCTGCCTGTGTGTTGGAT

>NZ_CP049246|9|1|1784810-1785022|PILER-CR
ACGCTGGCGCAAGAGTTGTGCGGCTGCCTGTGTGTTGGAT	CTCTTGTGCCTCGAAATCTTCCCCCTTTTTTAATCCCAAGCCAC
CCGCTAGCGCAAGAGTTGTGCGGATTTCATGCGCAGCTGT	TGTTTTGTGCCTACGGCATGTTTTTTTGCCCTTTTTTTAATATCGAGCCACGCTGGCGCAAGAGTT
GTGCGGCTGCCTGTGTGTTGGAT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP049246.1\|WP_103907079.1\|1780876_1781638_-\|SDR-family-NAD(P)-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|187604
NZ_CP049246.1\|WP_103907092.1\|1795379_1795802_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP049246.1\|WP_103907087.1\|1790358_1791099_+\|DUF4290-domain-containing-protein	unknown	unknown	gnl\|CDD\|379482
NZ_CP049246.1\|WP_103907085.1\|1787213_1787843_+\|chloramphenicol-acetyltransferase	unknown	unknown	gnl\|CDD\|215002
NZ_CP049246.1\|WP_146060646.1\|1794878_1795316_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP049246.1\|WP_103907083.1\|1785095_1785779_-\|M15-family-metallopeptidase	unknown	unknown	gnl\|CDD\|350616
NZ_CP049246.1\|WP_103907075.1\|1776175_1777693_+\|SusD/RagB-family-nutrient-binding-outer-membrane-lipoprotein	unknown	unknown	gnl\|CDD\|378943
NZ_CP049246.1\|WP_103907084.1\|1785986_1787123_+\|TlpA-family-protein-disulfide-reductase	unknown	unknown	gnl\|CDD\|239264
NZ_CP049246.1\|WP_103907077.1\|1779962_1780409_-\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|225064
NZ_CP049246.1\|WP_103907082.1\|1782797_1784393_+\|replicative-DNA-helicase	unknown	unknown	gnl\|CDD\|273206
NZ_CP049246.1\|WP_164527204.1\|1777711_1779235_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP049246.1\|WP_103907090.1\|1794092_1794854_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP049246.1\|WP_103907088.1\|1791222_1792548_+\|UDP-N-acetylglucosamine-1-carboxyvinyltransferase	unknown	unknown	gnl\|CDD\|236486
NZ_CP049246.1\|WP_103907080.1\|1781659_1782397_-\|bifunctional-demethylmenaquinone-methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol-methylase-UbiE	unknown	unknown	gnl\|CDD\|234689
NZ_CP049246.1\|WP_103907089.1\|1792649_1793282_+\|YceI-family-protein	unknown	unknown	gnl\|CDD\|377274
NZ_CP049246.1\|WP_103907074.1\|1772921_1776164_+\|SusC/RagA-family-TonB-linked-outer-membrane-protein	unknown	unknown	gnl\|CDD\|274948
NZ_CP049246.1\|WP_103907078.1\|1780419_1780869_-\|GatB/YqeY-domain-containing-protein	unknown	unknown	gnl\|CDD\|370480
NZ_CP049246.1\|WP_103907076.1\|1779452_1779869_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP049246.1\|WP_103907086.1\|1788019_1790302_+\|UvrD-helicase-domain-containing-protein	unknown	unknown	gnl\|CDD\|273429
NZ_CP049246.1\|WP_103907073.1\|1771373_1772339_+\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|379189

Protein	Function_ID	Function_description	E-value
NZ_CP049246.1\|WP_103907079.1\|1780876_1781638_-\|SDR-family-NAD(P)-dependent-oxidoreductase	gnl\|CDD\|187604	cd05346, SDR_c5, classical (c) SDR, subgroup 5. These proteins are members of the classical SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. 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.	4.0535e-126
NZ_CP049246.1\|WP_103907087.1\|1790358_1791099_+\|DUF4290-domain-containing-protein	gnl\|CDD\|379482	pfam14123, DUF4290, Domain of unknown function (DUF4290). This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 200 and 221 amino acids in length. There are two conserved sequence motifs: EYGR and KLWD.	9.88526e-100
NZ_CP049246.1\|WP_103907085.1\|1787213_1787843_+\|chloramphenicol-acetyltransferase	gnl\|CDD\|215002	smart01059, CAT, Chloramphenicol acetyltransferase. Chloramphenicol acetyltransferase (CAT).catalyzes the acetyl-CoA dependent acetylation of chloramphenicol (Cm), an antibiotic which inhibits prokaryotic peptidyltransferase activity. Acetylation of Cm by CAT inactivates the antibiotic. A histidine residue, located in the C-terminal section of the enzyme, plays a central role in its catalytic mechanism. There is a second family of CAT. evolutionary unrelated to the main family described above. These CAT belong to the bacterial hexapeptide-repeat containing-transferases family (see ). The crystal structure of the type III enzyme from Escherichia coli with chloramphenicol bound has been determined. CAT is a trimer of identical subunits (monomer Mr 25,000) and the trimeric structure is stabilised by a number of hydrogen bonds, some of which result in the extension of a beta-sheet across the subunit interface. Chloramphenicol binds in a deep pocket located at the boundary between adjacent subunits of the trimer, such that the majority of residues forming the binding pocket belong to one subunit while the catalytically essential histidine belongs to the adjacent subunit. His195 is appropriately positioned to act as a general base catalyst in the reaction, and the required tautomeric stabilisation is provided by an unusual interaction with a main-chain carbonyl oxygen.	3.72075e-76
NZ_CP049246.1\|WP_103907083.1\|1785095_1785779_-\|M15-family-metallopeptidase	gnl\|CDD\|350616	cd14817, D-Ala-D-Ala_dipeptidase_VanX, D-Ala-D-Ala dipeptidase VanX. D-Ala-D-Ala dipeptidase (also known as D-alanyl-D-alanine dipeptidase vanX; VanX; EC 3.4.13.22) is a Zn2+-dependent enzyme that mediates resistance to the antibiotic vancomycin in Enterococci and other bacteria (both Gram-positive and Gram-negative). It is part of a gene cluster that affects cell-wall biosynthesis. The operon triggers the termination of peptidoglycan precursors by D-Ala-(R)-lactate instead of D-Ala-D-Ala dipeptides. The enzyme is stereospecific, as L-Ala-L-Ala, D-Ala-L-Ala and L-Ala-D-Ala are not substrates. It belongs in the MEROPS peptidase family M15, subfamily D.	1.01333e-126
NZ_CP049246.1\|WP_103907075.1\|1776175_1777693_+\|SusD/RagB-family-nutrient-binding-outer-membrane-lipoprotein	gnl\|CDD\|378943	pfam12771, SusD-like_2, Starch-binding associating with outer membrane. SusD is a secreted starch-binding protein with an N-terminal lipid tail that allows it to associate with the outer membrane.	3.71775e-92
NZ_CP049246.1\|WP_103907084.1\|1785986_1787123_+\|TlpA-family-protein-disulfide-reductase	gnl\|CDD\|239264	cd02966, TlpA_like_family, TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are bacterial protein disulfide reductases with important roles in cytochrome maturation. They are membrane-anchored proteins with a soluble TRX domain containing a CXXC motif located in the periplasm. The TRX domains of this family contain an insert, approximately 25 residues in length, which correspond to an extra alpha helix and a beta strand when compared with TRX. TlpA catalyzes an essential reaction in the biogenesis of cytochrome aa3, while ResA and DsbE are essential proteins in cytochrome c maturation. Also included in this family are proteins containing a TlpA-like TRX domain with domain architectures similar to E. coli DipZ protein, and the N-terminal TRX domain of PilB protein from Neisseria which acts as a disulfide reductase that can recylce methionine sulfoxide reductases.	2.55851e-15
NZ_CP049246.1\|WP_103907077.1\|1779962_1780409_-\|GNAT-family-N-acetyltransferase	gnl\|CDD\|225064	COG2153, ElaA, Predicted acyltransferase [General function prediction only].	3.16485e-57
NZ_CP049246.1\|WP_103907082.1\|1782797_1784393_+\|replicative-DNA-helicase	gnl\|CDD\|273206	TIGR00665, DnaB, replicative DNA helicase. This model describes the helicase DnaB, a homohexameric protein required for DNA replication. The homohexamer can form a ring around a single strand of DNA near a replication fork. An intein of > 400 residues is found at a conserved location in DnaB of Synechocystis PCC6803, Rhodothermus marinus (both experimentally confirmed), and Mycobacterium tuberculosis. The intein removes itself by a self-splicing reaction. The seed alignment contains inteins so that the model built from the seed alignment will model a low cost at common intein insertion sites. [DNA metabolism, DNA replication, recombination, and repair].	0
NZ_CP049246.1\|WP_103907088.1\|1791222_1792548_+\|UDP-N-acetylglucosamine-1-carboxyvinyltransferase	gnl\|CDD\|236486	PRK09369, PRK09369, UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated.	0
NZ_CP049246.1\|WP_103907080.1\|1781659_1782397_-\|bifunctional-demethylmenaquinone-methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol-methylase-UbiE	gnl\|CDD\|234689	PRK00216, ubiE, bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE.	4.86815e-103
NZ_CP049246.1\|WP_103907089.1\|1792649_1793282_+\|YceI-family-protein	gnl\|CDD\|377274	pfam04264, YceI, YceI-like domain. E. coli YceI is a base-induced periplasmic protein. The recent structure of a member of this family shows that it binds to poly-isoprenoid. The structure consists of an extended, eight-stranded, antiparallel beta-barrel that resembles the lipocalin fold.	2.24685e-31
NZ_CP049246.1\|WP_103907074.1\|1772921_1776164_+\|SusC/RagA-family-TonB-linked-outer-membrane-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].	7.47636e-149
NZ_CP049246.1\|WP_103907078.1\|1780419_1780869_-\|GatB/YqeY-domain-containing-protein	gnl\|CDD\|370480	pfam09424, YqeY, Yqey-like protein. The function of this domain found in the YqeY protein is uncertain.	5.96116e-48
NZ_CP049246.1\|WP_103907086.1\|1788019_1790302_+\|UvrD-helicase-domain-containing-protein	gnl\|CDD\|273429	TIGR01073, ATP-dependent_DNA_helicase_PcrA, ATP-dependent DNA helicase PcrA. Designed to identify pcrA members of the uvrD/rep subfamily. [DNA metabolism, DNA replication, recombination, and repair].	0
NZ_CP049246.1\|WP_103907073.1\|1771373_1772339_+\|GNAT-family-N-acetyltransferase	gnl\|CDD\|379189	pfam13444, Acetyltransf_5, Acetyltransferase (GNAT) domain. This family contains proteins with N-acetyltransferase functions.	1.0812e-10

>NZ_CP049246.1|WP_103907082.1|1782797_1784393_+|replicative-DNA-helicase
MSLENEFTNSGSGQPSRASFNKKRTSLNNLVSGLGKLPPQALDLEEAVLGALMLEKNALSEVIDILKPDSFYKEAHQKIFEAIFSLFQKTSPIDILTVVAELRQMGALEMVGGAYYITQLTDRVVSAANIEYHARIISQKYIQRELIKVSTEIINSSYDETSDIFDLLDHAEKSLFDIAQNNLRRDSRKMDDIMREAISSLELLRDRTDGLTGIPSGLTALDRMTSGWQPSDLVIIAARPAMGKTAFVLSVARNAAVDHNRPVAVFSLEMSSVQLVNRLIAGETEIEQEKLKKGNLADHEWQQLHSRIGRLTEAPLIIDDTPALNVFEFRAKCRRLKAQYDIQMVIVDYLQLMHGKSEGKGGGNREQEIGSISRALKSVAKELNIPVLALSQLSRAVESRPGNSKRPMLSDLRESGSIEQDADMVLFLYRPEYYGLTEDEEGRPTAGVGEVIIAKHRNGETGIVPLRFVGKYVKFVDLEDDFSGMSADTGSFQDFGTGMGSAMQPSNNFGDFGRGITMPSRMNDMPDDAPF
>NZ_CP049246.1|WP_103907080.1|1781659_1782397_-|bifunctional-demethylmenaquinone-methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol-methylase-UbiE
MSNDSSTVKPYNQQDGKKEQVADMFNNISKTYDMLNRFMTMGIDTIWRKKAIRSLAPLKPQYILDVATGTGDFAIDSIKILNPKKIIGVDISQGMLDVAKEKIAKKGLQDQFEVTLGDSENLPFADDTFDAVTVAFGVRNFENLEKGLSDIRRVLKPGGKAIVLELSNPTAFPIKQLFNIYFHKITPAMGKLISKDNRAYEYLPESVAKFPDGERFAAITKQVGFSKCTVRPQTFGFCTIYECDK
>NZ_CP049246.1|WP_103907079.1|1780876_1781638_-|SDR-family-NAD(P)-dependent-oxidoreductase
MRTVLITGASSGIGAACALELAREHKYRFLLCARRLDRLETLVQQLLAIDPAVETHTFKLDVRNADEVESQLGNLPAAWQQVDILINNAGLSQGLDPIQDGKIGDWDRMIDTNVKGLLYVTKYVVPMMANSEQPHIINLGSIAGKEVYPNGNVYCATKHAVDALTKAMRIDLLAQGIKVTSIDPGMVETEFSEVRFNGDKDRAKAVYHGLTPLSGQDIAEIVSFVLSRPKHVNINDLLVMPTAQANGTLVIRK
>NZ_CP049246.1|WP_103907078.1|1780419_1780869_-|GatB/YqeY-domain-containing-protein
MSLETQINQDIKAAMIAKDTIRLRGLRAIKAAILLANTEKGHAEELTEDGEIKVLQKLVKQRKESAEIYQQQDRKDLYTIEIEEMQVIEEYLPKQLEREEIENVVRGIIAETGASSIKDMGKVMGAANQKLAGQADGRTISEVVKSLLS
>NZ_CP049246.1|WP_103907077.1|1779962_1780409_-|GNAT-family-N-acetyltransferase
MEWRSKSFSALSALELYKILQVRIDVFMLEQDCLYPECDDKDQQSTHLFGWQDDTCVAYARLLPPEVSYPGCSSIGRVVVHPDYRSHKYGKELMERAIAIQKQQFPGMPIRISAQEYLHKFYTDLGFIVESEVYLEDNIPHQEMALYF
>NZ_CP049246.1|WP_103907076.1|1779452_1779869_-|hypothetical-protein
MKYSLYFFLIFLGSCKPEPYKPTTNEFLYNNKTNYTVDLIRYITINGSANSYSYGYKINKGESIRINQQQEEFLLASVLDSVEIIFDNTKKVVFRKNDEQSNPNLWDVSPVRTSSYTLQENDEVASYIIDNKIFDLAK
>NZ_CP049246.1|WP_164527204.1|1777711_1779235_+|hypothetical-protein
MKKLITKILGAVAGISLLIGCTEGNYPGGQISPYIGIYDVRTLYKGSPVDLNLESLGGSEKITAVVISDHSGNNLPSDLLIVQDKRRLDFLRGIAIPLGSAAKDYVPGDSVIININGGVLDRVDGILQIKNIGADRVEKVASNREVITTVTNTSKLIERPNDFESTMVAIVKGGFSYTPKPGQVLSGEQQINDGFGLITLNTDPKSKLANLPQYKMANYYGIVFTKLEGDSLVPYHRMRIEKDLVELKSVYKTPKVIITGWSNDPKGSDANNEYFQFIATEDIDFSKTPMSVVTSNNANASTPTGVPVNGWATGDMRTYKFNLTSGFAKKGSIFYVGGSNKLIMSTGSTSIKEANWILAYDYTKNAGFDFGKATSNLLANSGNAYGIAIFDGTTVTKESIPEDVVWVATGGSLTNNTNGYRITNNDFYDIIHPLNLKEQPFYRAGSNTNAHTYNTPADAGYFNYMGGEFNLTLGRWTKARAKYAPTLTKESKLAEIEDPLYLTKLVE
>NZ_CP049246.1|WP_103907075.1|1776175_1777693_+|SusD/RagB-family-nutrient-binding-outer-membrane-lipoprotein
MKIKNILLLLLGITFLTSCDKDFVEMNINPTTQDKALPHMFMNNALINAVTYNMNRNRNFNNELMQVTVSIGDGDGKVFRYDFRRSWSDYTWNNHYLNMSNIKDIHKTASEELNYNRSYQGVSLILQAWVYSILTDTYGDIPYTQSTLGRDSLLFEPKFDLQKDIYVDLLNKLDTANTLLKANDLMETGSDPIYKGAPDKWRKFGNSLYLRLLLRIVHKPEVQEHALAKIKEILETNASNYPIIASNEESAILRWTGVDDFKSPFMATRVQDFRASAISEFFMDFLRDTNDPRINIPEYGTSGINRWGIAPVSGSFVGVPSGYAAGTEDYSKMSYFYSADQNKGVNSLQVEPLTGMIMNFSEVEFIKSEAMLKGYISGDPKTPFYSGIESNIRLWIPEWKSNAKDHLVASDIDWNDADTFEQKMERIHKQKYLALFLVDNQQWFEYRRTGHPVLPKGPGLQNNGEMPARMAYPVYVQSSNPTSYKEAIARQGADEINTKVWWQKP
>NZ_CP049246.1|WP_103907074.1|1772921_1776164_+|SusC/RagA-family-TonB-linked-outer-membrane-protein
MYRSSKKLSKVGILLIMGMAMQGTATGSVPYYPVETHVVQEQINVRITVKDQETGTALSGVNMLVDGKAIGFTNDSGVFQGTVTKGTTIRLRMIGYTQTSITVERETYAVGLNSLDESIDEVVVTALGIKREEKALGYATTTVKGEQLTDAMSSNWMDALSGKVAGLNLMRSNAGPVGSTKIILRGESNLTDNNEALIVVDGVVVNGGSGRRSSLGSDSPYGTSSDNMPVDYGSGMDDINPDDIESVTVLKGPGAAALYGSRAANGAVIITTKTGTKKERGIGVTINSNTSFESMNRSPELQYEYGQGTGGAAHYSMGSSIDGGSTSGTSSAYGPKFDGQNFFQLDPTTQKVGLERTPWRAYDGKQGVNGFFDVGRTFTNSVSIDGNTDKTSARFSATNVQNKWIVPNTGYKRNTFSLAVNSKVSEKLTINTKVSYNNRWSDNLPGTGYGNQSLMYWYIFWQPSANIEWLRDYWVKGEEQRKIFYPYSTYPENPYAISYEFINANNRHTFTGNAQASYQFTKELSLQVRAAMDFSAENRNQNRPYDAGSKLAEGSFRTQSIFSRETNADFLLRYAKKLNDDFDFSATVGGATLNNEYRRDDMTSDGLTYPGIYNHGNAKYGIKTQQLNERFQTNSFYGLFTAAYKEFLFLDFTGRMDWTSTLAAVKDPDKKLNFFYPSVNASFVISEVAEMPSFINFAKVRASVAGTGSGVTKPYMTNFAYQKPPNLVGGGNIMNPTGLVNPMILPLKTSSYEVGMDVRMFRKRVNLDVALYKANTFSQHLNRIVDASSGVSRYLINLGEVQNSGVEVALNTDQIKKDSGFNWSSMLTYTSNKNEIKQLADSSIVLQQRSVGSGQIVGFVGGSLGDLYGLGYERAPDGQIIYDESTGYAKITKEVIYLGNTIPKGKMSLGNNFSYKGIRLNVLFDAQWGGVAHSLTHYKLAEQGKTVNTLPGRYSGLIGNGVIQNADGSFRPNDVIATNVDEYYRSHYGADNAEGSTFATDFLKFREARLDYTFNRNVVKRLGINRATIGVYGRDLFIWTKWPAFDPEFGTLDGSDIVKGFEIAQFPSTRTFGFNLVVGF
>NZ_CP049246.1|WP_103907073.1|1771373_1772339_+|GNAT-family-N-acetyltransferase
MQEIIEPVDRELIKKELTPEAFVRYTNNGSNEVYLVNYHTAPNIMREIGRLRELTFRGAGGGTGLPLDIDENDTAAHNYDQLIAWNPEDEEVIAGYRVIKCDHSIAENGDIHLSTAHYFEFSDKFKEEFLPYTIELGRSWVQPKYQPAVDNRKGIFSLDNLWDGLGALVLMNPEVKYLFGKVTMYPHYNEEARDLLIYFMNHYFPDRDNLVEPVKELYLGYKTDISKYQGIFDGLDYKEGYKILNAKIRELGENIPPLINTYMNLSPTMRVFGTARNNEFGEVEETGILISLDDVYPVKKERHMSTFERDRHYGQRPVKVR
>NZ_CP049246.1|WP_103907083.1|1785095_1785779_-|M15-family-metallopeptidase
MKRNLFLYSLIFSLLFVSCGVQRQSIPDLFVDLKKAIPTLAIDLRYHGDHNFVGRPIRGYEGNRIYLSKAAAIALASAQRELAAENLGFKVFDAYRPQQAVDHFKEWASAIADTVAKQEFYPDVDKRDLFNLGYIAEKSGHSRGSTIDLTLIDLRDGKELDMGSGFDYFGERSHHDYQGITAVQKANRKKLRHIMEKHGFKSIAEEWWHYTLINEPNKEVYYDFPIR
>NZ_CP049246.1|WP_103907084.1|1785986_1787123_+|TlpA-family-protein-disulfide-reductase
MSISRYILLGFIWFLTVPNSNAQQLEEVLRPFLNFKTLSYTGNLVEKGVLDDKLYRNTIKASFDYSGKDSVQKVHKKAYAAWRDANKLITLDYSDSTYKVKERNEYTGPIDDSFLERIKRTANKYPTFLKEIPKRDSVLDGKTYYLYEFTPYDSVSNNKRFYETTKLLVDKKTFVPALYRFEFATTLMDNVTYVTYFVDQYLHNIRINDPNFKDISDMTLPANFKTYVPKKRLPMLVEGTDVPSLSFLDQEQQPLDLTNFKGKVILLNISLVACPHSVNSVKMLNDFHHTYGDQNLVIISVYPVDAAEDVQNMVAKFNIEYPYYQNTKNTQVQLKEFQTLGYPAFYVIDKNAKIKAGFEGYSDEIAKKIKAKIEQSIL
>NZ_CP049246.1|WP_103907085.1|1787213_1787843_+|chloramphenicol-acetyltransferase
MKQRIDQSTWERKEHYAFFSKFDEPIYGVTVPVDCTKAYQTAKEKGVSFFMYYLYRALQAFNAIENFRLRIYEGEVYLYDVTHASTTMLREDKTFGFTYIDYHPDEQVFLEGALSEIARVKANSGLELRDVEPNMVQCSALPWLDFTGLSHARSFSRIDSCPKISFGKLVDEAGAKRMNISIHVHHGLVDGYHIGLFVEKFQQLLDGVA
>NZ_CP049246.1|WP_103907086.1|1788019_1790302_+|UvrD-helicase-domain-containing-protein
MDYLAGLNPSQRAAVEQIKGPVMIVAGAGSGKTRVITYRVAHLIRQGVDPFNILVLTFTNKAAKEMRERIMKVVGAEAKNIWMGTFHSIFARILRVEAELIGYPKNFTIYDTDDTKSLLRAILKELNLDDKLYNVNHVYGRISSAKNNLISPQEYNKNEAIMAEDIANGRGQLGQIYMTYAQRCYRAGAMDFDDLLFKTNVLLNKYPDVLHKYQHQFKYLMVDEYQDTNFSQYLIVKRLAAVNENICVVGDDAQSIYAFRGANIQNILNFQKDYPDVKVFKLEQNYRSTKMIVNAANSIIANNKNQLEKNVFSDNEDGEKIKVARAFSDNEEGKIVAEAISQEKALKSLNYKDFAILYRTNAQSRSLEEALRKLNVPYKLYGGTSFYQRKEIKDLIAYFRLTFNPNDEEALKRVINYPRRGIGDTTVEKIMVAADQQQLRLWDVVANAQMFLDGRSAASVSNFGLMIQSFQATAKTNTAFDTAMHIAQHSGILKDLYEDKSVEGLARYENIQELLNGIKEFSEREDLEEKGLDIFMQDIALLTNDDNDKDPNADTVSLMTIHASKGLEFPVVFIVGLEENLFPSQLSLNSRSELEEERRLFYVAVTRAEKKLHLSYATSRYRWGTLNNCEPSRFLDELNPSTLDLDFNPRTAMASNDDFGSERVKWQRKEESSGDMFSKPKPKVIKTTSILPKAHKPTEGFAPSDTSGLQVGMEVEHERFGFGKVINLEGNKPDVKATIFFKELGQKQLLLKFAKLRIVN
>NZ_CP049246.1|WP_103907087.1|1790358_1791099_+|DUF4290-domain-containing-protein
MIFDYNSTRPKLILAEYGRNVQNMVDYICSLPDREERNRLAQVVIDMMGVLNPHLRDVSDFKHKLWDHLYIISDFKIDVDSPYPIPTKENIHHKPEPLKYPNHNIRFKHYGYTVEEMIGKAMSTQNEEARQKMALSIANFMKMAYLTWNKDAVSDDQILNDLRVLSSGALTLPADTVLTKLDFKTPPPGSRTKPATGSGSNQQQNKKQNNSNFRDQKGAGGRKPSNSNYGGGHGGHSNYNNKMKKK
>NZ_CP049246.1|WP_103907088.1|1791222_1792548_+|UDP-N-acetylglucosamine-1-carboxyvinyltransferase
MNAFEINGGKPLKGEIVPQGAKNEALQIISAVLLTEEKITISNIPDIKDVNKLIDLLAAMGVTVNRVSEDTYEFEAKDINIDYFQSEEFKKKGGSLRGSIMIVGPLLARFGKAAIPKPGGDKIGRRRLDTHFLGFEKLGAKFIYDAENHFFNVDASELQGTYILMDEASVTGTANIVMAAVLAKGTTTIYNAACEPYLQQLCKMLNRMGANISGIGSNLLTIEGVERLGGTTHRMLPDMIEIGSFIGLAAMTGSEITIKDVCFKELGIIPSVFSRLGIKFELRGDDIFIPAQDSYEIDTFIDGSILTISDAPWPGFTPDLLSIVLVTAIQAKGNVLIHQKMFESRLFFVDKLIDMGAQIILCDPHRATVIGLNKQNKLRGIEMTSPDIRAGVSLLIAALSAQGKSVIYNIEQIERGYQHIEERLKALGADIRRVDVQPSGN
>NZ_CP049246.1|WP_103907089.1|1792649_1793282_+|YceI-family-protein
MKKITLLSAIAALVLASCAGNPEGKKAETKDSVVVTQSEVVGTTFNVDTAASKVVWTGTKVTGKHTGTVNIKSGSLTVDNGALTAGNVVLDMTSISSTDLEGEYKEKLDGHLKADDFFGVATHPEASFTITEIKPGATANDITVSGNLIIKGVSKNITFDAKVVEATDATIKATANFNITRADWGVSYEGKSDDLISKEINFDINLVANK
>NZ_CP049246.1|WP_103907090.1|1794092_1794854_+|hypothetical-protein
MKSLTTLLIFLCGITFSHAQVKNPASSKPLFDEGITWTTKEENGKIGFGYTDSEWVWAIKPTFDKIASGAQFLSKQKYATMTLKGNQTLNPKNCGVRSHQSNIAIIDRKGNILIEGKTGESFKLIPNSSYAIKLINGQGDASKGCEAFIINIETGKTVHQLQANYSDITYNEHYVNLWGNEGIKLFYNFDGTVYQNDTPFYLPIRKEFKTKKYNTFLAYAEKSRVFNENVTGFFFGYGDNFKIVKENWVNMSK
>NZ_CP049246.1|WP_146060646.1|1794878_1795316_+|hypothetical-protein
MKTKTIMTAILLLFGLISLAQKMEYKTIQDLEDGEKVSDIYIIDLKAKTLKVRFEDGVNIEYKIDAYTKKENQEDEDVYGEDRGVKFTEHLIELEDKKVTPDQLLRTIAYIKLMVPENQYAAKFRKILHVRYHGLTSFYYSVTEN
>NZ_CP049246.1|WP_103907092.1|1795379_1795802_+|hypothetical-protein
MSAFNIFRKKEGKPLPPAYQVGQEWNYHTRPGEENSTLKILKIETYKEYGTIVHIAFSGVCIKNPKYPNGVLEEVLHLPVAEDALRNSTTTLKNDRVSLPNYELGYVRWKAAFDEQQAGHFGIPLREAIQWLEDGTYEVK

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Crispr_ID: NZ_CP049246_10

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP049246_10

1980115-1980206

Orphan

Consensus_repeat	Method
ACCCTCACGCTGGCGCACGAGTTGTG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP049246_10

>merge|NZ_CP049246|10|1980115-1980206|CRISPRCasFinder
ACCCTCACGCTGGCGCACGAGTTGTGGGGGAGGGATGTGCGGTGGATCTCTTGTGCCTTGGATGGAACCCTCACGCTGGCGCAAGAGTTGTG

>NZ_CP049246|10|9|1980115-1980206|CRISPRCasFinder
ACCCTCACGCTGGCGCACGAGTTGTG	GGGGAGGGATGTGCGGTGGATCTCTTGTGCCTTGGATGGA
ACCCTCACGCTGGCGCAAGAGTTGTG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP049246.1\|WP_164527207.1\|1982986_1983781_-\|murein-L,D-transpeptidase-catalytic-domain-family-protein	unknown	unknown	gnl\|CDD\|379310
NZ_CP049246.1\|WP_160003822.1\|1985018_1985429_+\|NUDIX-domain-containing-protein	unknown	unknown	gnl\|CDD\|240046
NZ_CP049246.1\|WP_103907519.1\|1977481_1978006_+\|lipocalin-like-domain-containing-protein	unknown	unknown	gnl\|CDD\|372819
NZ_CP049246.1\|WP_103907513.1\|1971352_1971889_-\|lipocalin	unknown	unknown	gnl\|CDD\|381213
NZ_CP049246.1\|WP_103907514.1\|1972438_1973230_+\|S1/P1-nuclease	unknown	unknown	gnl\|CDD\|211382
NZ_CP049246.1\|WP_103907870.1\|1992091_1993381_+\|Gfo/Idh/MocA-family-oxidoreductase	unknown	unknown	gnl\|CDD\|223745
NZ_CP049246.1\|WP_103907869.1\|1989043_1991956_-\|copper-translocating-P-type-ATPase	unknown	unknown	gnl\|CDD\|319783
NZ_CP049246.1\|WP_103907527.1\|1972031_1972433_+\|DUF4268-domain-containing-protein	unknown	unknown	gnl\|CDD\|379461
NZ_CP049246.1\|WP_103907867.1\|1987344_1988538_+\|MFS-transporter	unknown	unknown	gnl\|CDD\|340882
NZ_CP049246.1\|WP_103907520.1\|1978098_1980009_+\|amidophosphoribosyltransferase	unknown	unknown	gnl\|CDD\|273461
NZ_CP049246.1\|WP_103907518.1\|1976525_1976858_-\|YegP-family-protein	unknown	unknown	gnl\|CDD\|377831
NZ_CP049246.1\|WP_164527198.1\|1981271_1982153_-\|IS3-family-transposase	unknown	unknown	gnl\|CDD\|222853
NZ_CP049246.1\|WP_103907866.1\|1986459_1987044_-\|Crp/Fnr-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|223736
NZ_CP049246.1\|WP_103907516.1\|1973662_1974310_-\|DUF45-domain-containing-protein	unknown	unknown	gnl\|CDD\|307807
NZ_CP049246.1\|WP_103907517.1\|1974450_1976454_+\|M13-family-metallopeptidase	unknown	unknown	gnl\|CDD\|341056
NZ_CP049246.1\|WP_103907868.1\|1988553_1988973_+\|RidA-family-protein	unknown	unknown	gnl\|CDD\|100004
NZ_CP049246.1\|WP_103907863.1\|1983849_1984881_-\|L,D-transpeptidase	unknown	unknown	gnl\|CDD\|377115
NZ_CP049246.1\|WP_103907515.1\|1973304_1973673_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP049246.1\|WP_103907528.1\|1976936_1977317_-\|zinc-chelation-protein-SecC	unknown	unknown	gnl\|CDD\|380015
NZ_CP049246.1\|WP_103907865.1\|1985545_1986139_-\|porin-family-protein	unknown	unknown	gnl\|CDD\|379226

Protein	Function_ID	Function_description	E-value
NZ_CP049246.1\|WP_164527207.1\|1982986_1983781_-\|murein-L,D-transpeptidase-catalytic-domain-family-protein	gnl\|CDD\|379310	pfam13645, YkuD_2, L,D-transpeptidase catalytic domain. This family is related to pfam03734.	3.3944e-96
NZ_CP049246.1\|WP_160003822.1\|1985018_1985429_+\|NUDIX-domain-containing-protein	gnl\|CDD\|240046	cd04690, Nudix_Hydrolase_31, Members of the Nudix hydrolase superfamily catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+, for their activity and contain a highly conserved 23-residue nudix motif (GX5EX7REUXEEXGU, where U = I, L or V), which functions as a metal binding and catalytic site. Substrates of nudix hydrolases include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the nudix hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance & "house-cleaning" enzymes. Substrate specificity is used to define families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required.	7.72745e-31
NZ_CP049246.1\|WP_103907519.1\|1977481_1978006_+\|lipocalin-like-domain-containing-protein	gnl\|CDD\|372819	pfam13924, Lipocalin_5, Lipocalin-like domain. This family includes domains distantly related to lipocalins. However, they do contain the important GXW motif in the first strand. The protein in this family include aln5, which is involved in biosynthesis of alnumycin. The family also includes the ZFK protein from Trypanosoma brucei which is a protein kinase. This domain is at the C-terminus of that protein. The domain is also found as the C-terminal domain in StiJ a protein involved in producing stigmatellin. This domain has been assumed to catalyze a final cyclisation reaction.	7.00126e-39
NZ_CP049246.1\|WP_103907513.1\|1971352_1971889_-\|lipocalin	gnl\|CDD\|381213	cd19438, lipocalin_Blc-like, bacterial lipocalin Blc, Arabidopsis thaliana temperature-induced lipocalin-1, and similar proteins. Escherichia coli bacterial lipocalin (Blc, also known as YjeL) is an outer membrane lipoprotein involved in the storage or transport of lipids necessary for membrane maintenance under stressful conditions. Blc has a binding preference for lysophospholipids. This group includes eukaryotic lipocalins such as Arabidopsis thaliana temperature-induced lipocalin-1 (TIL) which is involved in thermotolerance, oxidative, salt, drought and high light stress tolerance, and is needed for seed longevity by ensuring polyunsaturated lipids integrity. This group belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development.	6.58317e-61
NZ_CP049246.1\|WP_103907514.1\|1972438_1973230_+\|S1/P1-nuclease	gnl\|CDD\|211382	cd11010, S1-P1_nuclease, S1/P1 nucleases and related enzymes. This family summarizes both S1 and P1 nucleases (EC:3.1.30.1) which cleave RNA and single stranded DNA with no base specificity. S1 nuclease is more active on DNA than RNA. Its reaction products are oligonucleotides or single nucleotides with 5' phosphoryl groups. Although its primary substrate is single-stranded, it may also introduce single-stranded breaks in double-stranded DNA or RNA, or DNA-RNA hybrids. It is used as a reagent in nuclease protection assays and in removing single stranded tails from DNA molecules to create blunt ended molecules and opening hairpin loops generated during synthesis of double stranded cDNA. P1 nuclease cleaves its substrate at every position yielding nucleoside 5' monophosphates, and it does not recognize or act on double-stranded DNA. It is useful at removing single stranded strands hanging off the end of double stranded DNA and at completely cleaving melted DNA for simple DNA composition analysis.	1.10106e-70
NZ_CP049246.1\|WP_103907870.1\|1992091_1993381_+\|Gfo/Idh/MocA-family-oxidoreductase	gnl\|CDD\|223745	COG0673, MviM, Predicted dehydrogenases and related proteins [General function prediction only].	2.72582e-39
NZ_CP049246.1\|WP_103907869.1\|1989043_1991956_-\|copper-translocating-P-type-ATPase	gnl\|CDD\|319783	cd02094, P-type_ATPase_Cu-like, P-type heavy metal-transporting ATPase, similar to human copper-transporting ATPases, ATP7A and ATP7B. The mammalian copper-transporting P-type ATPases, ATP7A and ATP7B are key molecules required for the regulation and maintenance of copper homeostasis. Menkes and Wilson diseases are caused by mutation in ATP7A and ATP7B respectively. This subfamily includes other copper-transporting ATPases such as: Bacillus subtilis CopA , Archeaoglobus fulgidus CopA, and Saccharomyces cerevisiae Ccc2p. This subclass of P-type ATPase is also referred to as CPx-type ATPases because their amino acid sequences contain a characteristic CPC or CPH motif associated with a stretch of hydrophobic amino acids and N-terminal ion-binding sequences. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.	0
NZ_CP049246.1\|WP_103907527.1\|1972031_1972433_+\|DUF4268-domain-containing-protein	gnl\|CDD\|379461	pfam14088, DUF4268, Domain of unknown function (DUF4268). This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria and archaea. Proteins in this family are typically between 151 and 387 amino acids in length.	2.22262e-29
NZ_CP049246.1\|WP_103907867.1\|1987344_1988538_+\|MFS-transporter	gnl\|CDD\|340882	cd17324, MFS_NepI_like, Purine ribonucleoside efflux pump NepI and similar transporters of the Major Facilitator Superfamily. This family is composed of purine efflux pumps such as Escherichia coli NepI and Bacillus subtilis PbuE, sugar efflux transporters such as Corynebacterium glutamicum arabinose efflux permease, multidrug resistance (MDR) transporters such as Streptomyces lividans chloramphenicol resistance protein (CmlR), and similar proteins. NepI and PbuE are involved in the efflux of purine ribonucleosides such as guanosine, adenosine and inosine, as well as purine bases like guanine, adenine, and hypoxanthine, and purine base analogs. They play a role in the maintenance of cellular purine base pools, as well as in protecting the cells and conferring resistance against toxic purine base analogs such as 6-mercaptopurine. 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. The NepI-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.	5.15251e-70
NZ_CP049246.1\|WP_103907520.1\|1978098_1980009_+\|amidophosphoribosyltransferase	gnl\|CDD\|273461	TIGR01134, purF, amidophosphoribosyltransferase. Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) amidotransferase. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis].	2.6591e-40
NZ_CP049246.1\|WP_103907518.1\|1976525_1976858_-\|YegP-family-protein	gnl\|CDD\|377831	pfam07411, DUF1508, Domain of unknown function (DUF1508). This family represents a series of bacterial domains of unknown function of around 50 residues in length. Members of this family are often found as tandem repeats and in some cases represent the whole protein. All member proteins are described as being hypothetical.	2.24106e-22
NZ_CP049246.1\|WP_164527198.1\|1981271_1982153_-\|IS3-family-transposase	gnl\|CDD\|222853	PHA02517, PHA02517, putative transposase OrfB; Reviewed.	1.88139e-47
NZ_CP049246.1\|WP_103907866.1\|1986459_1987044_-\|Crp/Fnr-family-transcriptional-regulator	gnl\|CDD\|223736	COG0664, Crp, cAMP-binding proteins - catabolite gene activator and regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms].	5.03164e-11
NZ_CP049246.1\|WP_103907516.1\|1973662_1974310_-\|DUF45-domain-containing-protein	gnl\|CDD\|307807	pfam01863, DUF45, Protein of unknown function DUF45. This protein has no known function. Members are found in some archaebacteria, as well as Helicobacter pylori. The proteins are 190-240 amino acids long, with the C-terminus being the most conserved region, containing three conserved histidines. This motif is similar to that found in Zinc proteases, suggesting that this family may also be proteases.	0.0022942
NZ_CP049246.1\|WP_103907517.1\|1974450_1976454_+\|M13-family-metallopeptidase	gnl\|CDD\|341056	cd08662, M13, Peptidase family M13 includes neprilysin and endothelin-converting enzyme I. The M13 family of metallopeptidases includes neprilysin (neutral endopeptidase, NEP, enkephalinase, CD10, CALLA, EC 3.4.24.11), endothelin-converting enzyme I (ECE-1, EC 3.4.24.71), erythrocyte surface antigen KELL (ECE-3), phosphate-regulating gene on the X chromosome (PHEX), soluble secreted endopeptidase (SEP), and damage-induced neuronal endopeptidase (DINE)/X-converting enzyme (XCE). Proteins in this family fulfill a broad range of physiological roles due to the greater variation in the active site's S2' subsite allowing substrate specificity. NEP is expressed in a variety of tissues including kidney and brain, and is involved in many physiological and pathological processes, including blood pressure and inflammatory response. It degrades a wide array of substrates such as substance P, enkephalins, cholecystokinin, neurotensin and somatostatin. It is an important enzyme in the regulation of amyloid-beta (Abeta) protein that forms amyloid plaques that are associated with Alzeimers disease (AD). ECE-1 catalyzes the final rate-limiting step in the biosynthesis of endothelins via post-translational conversion of the biologically inactive big endothelins. Like NEP, it also hydrolyzes bradykinin, substance P, neurotensin, and Abeta. Endothelin-1 overproduction has been implicated in various diseases including stroke, asthma, hypertension, and cardiac and renal failure. Kell is a homolog of NEP and constitutes a major antigen on human erythrocytes; it preferentially cleaves big endothelin-3 to produce bioactive endothelin-3, but is also known to cleave substance P and neurokinin A. PHEX forms a complex interaction with fibroblast growth factor 23 (FGF23) and matrix extracellular phosphoglycoprotein, causing bone mineralization. A loss-of-function mutation in PHEX disrupts this interaction leading to hypophosphatemic rickets; X-linked hypophosphatemic (XLH) rickets is the most common form of metabolic rickets. ECEL1 is a brain metalloprotease which plays a critical role in the nervous regulation of the respiratory system, while DINE is abundantly expressed in the hypothalamus and its expression responds to nerve injury. A majority of these M13 proteases are prime therapeutic targets for selective inhibition.	0
NZ_CP049246.1\|WP_103907868.1\|1988553_1988973_+\|RidA-family-protein	gnl\|CDD\|100004	cd00448, YjgF_YER057c_UK114_family, YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site.	2.09471e-23
NZ_CP049246.1\|WP_103907863.1\|1983849_1984881_-\|L,D-transpeptidase	gnl\|CDD\|377115	pfam03734, YkuD, L,D-transpeptidase catalytic domain. This family of proteins are found in a range of bacteria. It has been shown that this domain can act as an L,D-transpeptidase that gives rise to an alternative pathway for peptidoglycan cross-linking. This gives bacteria resistance to beta-lactam antibiotics that inhibit PBPs which usually carry out the cross-linking reaction. The conserved region contains a conserved histidine and cysteine, with the cysteine thought to be an active site residue. Several members of this family contain peptidoglycan binding domains. The molecular structure of YkuD protein shows this domain has a novel tertiary fold consisting of a beta-sandwich with two mixed sheets, one containing five strands and the other, six strands. The two beta-sheets form a cradle capped by an alpha-helix. This family was formerly called the ErfK/YbiS/YcfS/YnhG family, but is now named after the first protein of known structure.	3.44338e-11
NZ_CP049246.1\|WP_103907528.1\|1976936_1977317_-\|zinc-chelation-protein-SecC	gnl\|CDD\|380015	pfam17775, UPF0225, UPF0225 domain. This entry represents an NTF2-like domain found in bacterial proteins.	4.20726e-43
NZ_CP049246.1\|WP_103907865.1\|1985545_1986139_-\|porin-family-protein	gnl\|CDD\|379226	pfam13505, OMP_b-brl, Outer membrane protein beta-barrel domain. This domain is found in a wide range of outer membrane proteins. This domain assumes a membrane bound beta-barrel fold.	0.000135698

>NZ_CP049246.1|WP_103907520.1|1978098_1980009_+|amidophosphoribosyltransferase
MSDAIKHECGIALIRLLKPLSYYQEKYGTPYYGINKLYLLMEKQHNRGQDGAGIATIKFDVKPGNRYISRYRAMGSSAVSEIFEYVQKKFAAVNKAYPEESKDTQWLKDNVSFTGEVLLGHLRYGTHGKNSIESCHPFLRQNNWMSRNLVVAGNFNMTNVDELLQQLYDLGQHPKEQADTVTVLEKIGHFLDEENQKLFDQFKQEGLSNIEISAQIAKNLDVAKILTRSAKTWDGGYTIAGIFGHGDAFVMRDPAGIRPAFYYQDDEILVVASERPVIQTAFNVPLGSVKEIKPGHALIAKKDGTVTEEMFRQPVEQKSCSFERIYFSRGSDADIYQERKALGKLLIPQVLKSIDKDIKNTVFSFIPNTAEVSYYGMMDGVNEYVRACQKDALLNRADKISDEELNDVLEMRPRFEKLNVKDAKLRTFITQDADRQDMVQHVYDTTYGIVRDHEDTIVAIDDSIVRGTTLKQSILTILDRLNPKKIVIVSSAPQIRYPDCYGIDMSRMSEFVAFEAAISLLRKNGLAHVIDEVYQKCLASVTLPSEQVENYVKAIYEPFTDDQISQEIGRIIKPHHLKADVDVIFQTLDNLHIACPNHKGDWYFSGDYPTPGGNKVVNRAYMNWMEGKNVRAYFSS
>NZ_CP049246.1|WP_103907519.1|1977481_1978006_+|lipocalin-like-domain-containing-protein
MTTLKNELVGTWQLLSYIEVPIKGADSKFPMGQSPKGILIYGADGHMSVQISNAERNKYQSEDRYLASGEEIQEQVKGFIAFAGTYQIDSSNATVLYSISTSSFPNWEGQVQERKLDFEGDILYLKSVEPILSDGEYVNSYMTWRRVEKEEFLSRRERYLEITQSRQVKSQFED
>NZ_CP049246.1|WP_103907528.1|1976936_1977317_-|zinc-chelation-protein-SecC
MSANCLCGSSLPYVSCCEIVHQDARAALSAEALMRSRYTAFALQLIDFLYDTFHPSTRRFQDKKAIAQWSRENHWQGLEILRATENTVEFKAHYIDQQGNPAVHHEKSRFQKTQGTWYYVDGKELQ
>NZ_CP049246.1|WP_103907518.1|1976525_1976858_-|YegP-family-protein
MGKFVISLRKNGEFQFNLKASNGQVILSSEGYTTKAACENGIASVKKNAPDVKRFDKLTAKNGKFYFNLKAGNGQIIGTSEMYESEAGRTNGMKSVQENAPEANVDDTTL
>NZ_CP049246.1|WP_103907517.1|1974450_1976454_+|M13-family-metallopeptidase
MKQYVLAAALLASSVYVFGQEQHAINPSYMDKSVRPQDDFYNYVNGNWMKTVEIPSDKARWGSFDELRENTDEATLQILKESLDTKFDKGTDGQKIADLYKSYVDFDTRNKLGIAPIQQQLQDIDKISNMKELYDYFLKYAEIGGNPFFGGYVYAHMKNSNMNAVYLGGGGLGLGRSYYQKEDAKNTETLGNYQQYINSLYNKVEPKTRDLKGPKVVAFEKLIASNLKTVEEQRDAQKRYNPVAVNDLGKMVKNMDVQKYLQTMGFKADTVIIGELKYYQNLDKIVNQENLPVIKEYLKFHIMDDATGYLTKELDELSFDFYGKKLRGQKEQRALDKRGLEFVNGNVGELLGKLYVKDNFPAEAKAACEELVKYLIKSFDVHINNLAWMSPATKEKALEKLSKFTVKIGYPDKWKDYSTLTVGNSLIENVHNIQRWSFRENLAKQGKPVDKSEWGMSPQTVNAYYSPLFNEIVFPAAILQKPFYDYKADPAVNFGGIGAVIGHELSHGFDDSGSQYDGNGNLNNWWTAEDKAKFEAAADALVAQFESYEPVPGVFVNGRFTLGENIGDLGGSSVAFDALQMYLKDKGNPGLIDGYTQDQRFFLSWATIWRTKTTDEFVVNQVKTDPHSPAQYRAVGPIINLDAFHKAFDTKEGDKLYVPKDKRIVIW
>NZ_CP049246.1|WP_103907516.1|1973662_1974310_-|DUF45-domain-containing-protein
MFIEIEGTYYELVGTSEAGIRIARTGAQKNIIYAQPGISMDEIKAYIRQFGKEQAADPTEDEERLSFFTLELFDKKYNVRLLPDSYQKPFIKKELILAGANLFRRRERSKIEEDIRSQLFEQTILDLVGSWEEELGILVAQVSFRKLSRSHYTMQQDLKQLTFSKHNVLLSRRLNEYIVAMAMTDLVDPTLQTSTFWNSHFPDWRQLEKYLNYGS
>NZ_CP049246.1|WP_103907515.1|1973304_1973673_-|hypothetical-protein
MEAKEFEFNIPISQEQIGSLEIEPQTLLDFIPAAQTDKLKDFVFDALGNKDGSPEVGNLKVAKFKFDKAKNKGSFRLKFDIDRRYCCSDTESCSSDYVDFVFTTAGKNMLAKGNYFDWTLNN
>NZ_CP049246.1|WP_103907514.1|1972438_1973230_+|S1/P1-nuclease
MKIVGRVMLFFMLLSFSQQAFAWGMTGHRVISEIAEKHLSRKAKRNIERLIGHQKIAYWSNWADFIKSSPDTLLLKTGSWHFLNTLGNLTHAQFLVELQNSPEQNLYKAYKRVRQDVVNKELTLEQRQQAFYFMVHLLGDAHQPMHVSRAEDLGGNRIPVTFFGREGNIHRIWDSDLVDNEKYSYSEYARVLDYEKYFYKQYTNSTFEDWLYESHQLANIIYDDVAKNNKLSYDYIFRFKEPMENALLKAGLRLAKELNEVFG
>NZ_CP049246.1|WP_103907527.1|1972031_1972433_+|DUF4268-domain-containing-protein
MAPVPSADGEKVTWVNYKTGIRNLYFRMDASNKVAQIGIVIADSDAGIRALIFEQFQEYRTVLHAELGEEWIWDAEYYDEYGKATARIYTEIRGSSIFNQQDWPALISFFKPRIMALDSFWSTAQYGFEMFKY
>NZ_CP049246.1|WP_103907513.1|1971352_1971889_-|lipocalin
MDKKKTLITLSAVALGSVIYNYLRPVRSEVEVIHNFDLEKYLGTWYEIARLDFFWEKDLKDVTATYSKNEDGSLKVENSGVHIRTGKQKTSIGKAKLLGAPNEAALKVSFFGPFYSGYNIVRLDEDYQDALVFGDDLDHMWILSREKTISQTRKELYLAYAEACGYDINKLTWTIQEA
>NZ_CP049246.1|WP_164527198.1|1981271_1982153_-|IS3-family-transposase
MGIRLICGLFGRTRHAYYDRQWRVQDVGLKDEIILQHVLRIRSEQKRIGTRKLLHMLAGPLQEHGIRIGRDYLFALMREHSLQIRVRKRKAVTTDSRHWMKKYRNLIKELAVERPEQVWVSDITYVQLNRRWGYLSLVTDAYSRKIVGWAFRGDLSAQGCIDALQMALQQRQYPGKGLIHHSDRGSQYCSKGYVDILRTNGIGVSMTENGDPYENAIAERVNGILKAEFDLYASQSGLRETTRKIRENIRVYNNLRPHASCDYLTPEQAHMRSGALRKRWRPKKYPIVQKEFV
>NZ_CP049246.1|WP_164527207.1|1982986_1983781_-|murein-L,D-transpeptidase-catalytic-domain-family-protein
MNKLLLISLWALATSSFTGDLNNHKIAAPKEIKQTKVEVELTKDPVRALYDEMHLAGTIKWEAFEEAMQGYNQLNPKNKNIITIIDFTLPSTEKRMYVLDLKGKKMLYHSLVSHGRNSGEKFATSFSNKHGSFQSSLGFYFAEETYMGGNGYSLRLDGLEKGINDQARPRAVVVHGADYASANVIKSTGRLGRSYGCPALPREVTKPIINTIKGGSLMYIYAGNKQYLASTKMIKKGPVLTDNKTLIATQHDEVETGSGKATLN
>NZ_CP049246.1|WP_103907863.1|1983849_1984881_-|L,D-transpeptidase
MRKYAFWSVLCALLITASCKITTKNTDTAAEKRKQDSLEQIKKAEEAEKARPRTAADIKLEKDLQYDQHTLEETYPYKDTTRQFQLEKIKEKLAFVENFQRAPHTYGVLQNYKNRNGESPVVENFVRNAYKRVSDTLGTERYQSAPLYREENSEKPSIYGRDGSLVSLESSDTLKMVKVNGISFEGSWFVPKRYVKNIGEDLKITHVNFVDVTNQNILTVERTGENEWKIRSMNPATSGLHKPPHQMETPVGIFMVQEQKPKMFYFGDGTKTIEGFAPYASRFTNGGYIHGVPVNNPKGKIVEYSWSLGTTPRSHMCVRNASSHAKFVYDTSKPYQALVIVID
>NZ_CP049246.1|WP_160003822.1|1985018_1985429_+|NUDIX-domain-containing-protein
MKLKNYIEIAVCIITNDRNELLTVRKTGSTYYQLPGGKLEPQESAMATLLRELREELNLEFEESDFRLVKIHEADAVNERGMRVRGHVFRCARPIPMSLSANAELEEVRWVGPEEVDAVKLANLLRQVAIPEWLRH
>NZ_CP049246.1|WP_103907865.1|1985545_1986139_-|porin-family-protein
MKKILLTLSAVAVLGFAANAQTEKGKFMLGGQVNYDGHNVKDSDFKINSLSIVPNVGYFVADNIAVGLGLGYQWTKAENNENSSETGSAFQLAPFGRMYSNNAGPVKFFGQLSVPMSWGERKINDDKVSTISNYGVELAPGIAFFPTSNIGIEFKVKGLYFQSSTDKAEATDIETTTNSYGLNANSLAPTVGVTFHF
>NZ_CP049246.1|WP_103907866.1|1986459_1987044_-|Crp/Fnr-family-transcriptional-regulator
MEKLRTAMEDLIQTKMPDSDWDFFQSKLIYKEFPKKHRLLDAGQTERYLSFTLKGIIRFFIPNPESETTVFFAFDGWFTSVYDSFVTQRPSYYAAEILEPTAMLRISYADLQEVYAKTSVGNLIGRKASETLFVLKTQREISLVNLTAEQRYLQLLKEQPQYIQQIPQKHLASYIGITPQALSRIKNRTATSKD
>NZ_CP049246.1|WP_103907867.1|1987344_1988538_+|MFS-transporter
MEKVAHPKLSKSLLWLMTVVSGVVVANNYYNQPLLAEIANEFQVSEAAASRITVLTQLGYACGLLMIIPLGDKLFRKRLILVDLIFVMLALIWMALSDAIWMMAAASFLIGFSSVIPQLFVPMVADLSDEENRSSNIGMVMSGLLMGILLSRFIGGIVGDVWGWRSIYWGAAVMMVLSWGFIYRMLPEMKPNFKGNYGSLMKSVWDLARTQPILQLAAFRGAMSFASLCVVFTTLAFHLEQPPFEAGPSVAGSFGLIGAAGALAAAFVGRLNQHWSRNKIIAISLFLLLISWFFIYFLGNYYIGLVIGIVMIDLGLQASHIMNQSDYFAIKTPATSRLNTVYMVSYFIGGSFGSWVGGQAWSAAGWTGVCLVGVLFAVLGLVAHLLFANRLQKKVSP
>NZ_CP049246.1|WP_103907868.1|1988553_1988973_+|RidA-family-protein
MKETGVKHINPTGIFDPTPFAFCHSVQVPSQANLVFISGQSGGVGEGHLLAEDFASQVKSALENLQIVLKAHAATVAHVVKITVLIVDHNPQKMEIWTSMAKEFWKGYDLPVSTLIPVPTLALPGMLIEVDAIAAVSEY
>NZ_CP049246.1|WP_103907869.1|1989043_1991956_-|copper-translocating-P-type-ATPase
MKHHHIYKVSGMTCNGCRTNVEKKLNEIPGVEAQVNLEKEEAMIHAEREISLAQLQEKLKELGGHYHIEEVKDEHATEQTVEQVFAVEGMTCNGCRTNVEKKLNELEGVHASVNLEKGEATVHAERGIDLPAMQQKLDELGGHYTIANKHGDSHSHDHHAHQHAQEPEISESGQYICPMFCEGKDKVYTEPGRCPVCNMHLRPVEKVDFNAPSHQEHQQHKPVVNANNAGKYYCPMMCEGDKVYDKFGSCPVCGMNLEKIPETTLKVEYTCPMHPEIVQDHPGDCPICGMELVPNQVTQEDDQHYRDLLRKLWISVACTVPVFILSMGDMLPGQPVSKVIPYSVNAWLQLLLTLPVVFYTCWMFFQRAWTSFKTWNLNMFSLIGLGAAAAFVFSLLAFFFPQLFPAELKGHHGEVHLYFESVVVILTLVLLGQVMEAKAHSKTNSAIKELIKLSPAEAILVENGKDRKIAIHDVKAGNILRVRAGDKVPVDGVVTEGNSSIDESMITGEPIPVEKDVNDKVIGGTINGNHELLIKAEKIGSETLLSQIIQLVNTASRSQPPIQKLTDKISKIFVPAVIGIAVITFVLWYISGVPNSLAMAFTNLLAVLIVACPCALGLATPMSVMVGIGKGAKNGILVKNSEALEKMEKADVLIVDKTGTITAGKPSVSEVISGNTQFKENDILQIAASVNKNSTHPLAQAMLDKAQEQNISLLDVTKFENISGKGVKGNIHHMSALLGTPRLMKEQNVAISPDEQGQIEELQKKGNSVSVLAIDGKFAGLVAAFDALKDSSIEVLKRFKDEGVEVYMFTGDNQNTADIVAKKAGIEHAKGGLLPEDKLNGIKELQAQGKKVIMVGDGINDAPALTQADVGIAMGTGTDVAIQSAEITLIKGDLTGVHKAYKLSKAMIGNIKQNLWLAFLYNVIGIPIAAGILYPSFGILMSPMIAAAAMSLSSVSVILNSIRLNTVKLD
>NZ_CP049246.1|WP_103907870.1|1992091_1993381_+|Gfo/Idh/MocA-family-oxidoreductase
MSISRRDFIFKSAMLIPALHMGSVFAKHSAEQPLRVGAIGIKGMGWADLKSIIHLPQVTCTAICDIDDAVITERLQNLKDLGQNPKVYKDYRELVNDPQVDAVIIGTPDHWHCLMLVDACKAGKAVYVEKPIGNSIAECNVMLEAKNKYNSIVQVGQWQRSQKHFRDAIDFVHSGKLGKVRLVKAWAYLGWKKRVPMKPDAQVPPGVDYQSWLGPAKIRPFNPNRFHYDFRWFWDYAGGLMTDWGVHLLDYALLGMQVSDPKSIMAAGGKFAYPEDAGDTPDTLTTVYEFEGFNIQWEHATSISGGPYGREHGIAFIGNNGTLVLDRNGWEVIPEFDRMAAVPYQKKVDSGLDLHMKNFVEAIRAKNPALLNAPLEVGAHIAKCAQMGNIAYRTGKKIYWEKEKQRFNEPEANKLLAAAYHNGYRLPRV

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Crispr_ID: NZ_CP049246_11

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP049246_11

2658550-2658670

Orphan

Consensus_repeat	Method
GTGGATCTCTTGTGCCTCAAAATCTCCCCCCTTTT	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP049246_11

>merge|NZ_CP049246|11|2658550-2658670|CRISPRCasFinder
GTGGATCTCTTGTGCCTCAAAATCTCCCCCCTTTTTTAATCCCAAGCCACCCGCTGGCGCAAGAGTTGTGCGGCAGGCCAAGTGTGGTGGATCTCTTGTGCCTCAAAATCTTCCCCCTTTT

>NZ_CP049246|11|10|2658550-2658670|CRISPRCasFinder
GTGGATCTCTTGTGCCTCAAAATCTCCCCCCTTTT	TTAATCCCAAGCCACCCGCTGGCGCAAGAGTTGTGCGGCAGGCCAAGTGTG
GTGGATCTCTTGTGCCTCAAAATCTTCCCCCTTTT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP049246.1\|WP_103906399.1\|2662180_2663203_+\|Holliday-junction-branch-migration-DNA-helicase-RuvB	unknown	unknown	gnl\|CDD\|234619
NZ_CP049246.1\|WP_103906394.1\|2668619_2669159_+\|methyltransferase-domain-containing-protein	unknown	unknown	gnl\|CDD\|223813
NZ_CP049246.1\|WP_103906393.1\|2669155_2669620_+\|pantetheine-phosphate-adenylyltransferase	unknown	unknown	gnl\|CDD\|234674
NZ_CP049246.1\|WP_103906396.1\|2666344_2667769_-\|AAA-family-ATPase	unknown	unknown	gnl\|CDD\|350691
NZ_CP049246.1\|WP_160003735.1\|2653703_2654999_+\|peptidase-S13	unknown	unknown	gnl\|CDD\|224938
NZ_CP049246.1\|WP_103906451.1\|2651883_2653590_+\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	unknown	unknown	gnl\|CDD\|369630
NZ_CP049246.1\|WP_103906411.1\|2644701_2645895_-\|proline-dehydrogenase	unknown	unknown	gnl\|CDD\|215366
NZ_CP049246.1\|WP_103906401.1\|2659634_2661218_+\|peptide-MFS-transporter	unknown	unknown	gnl\|CDD\|225646
NZ_CP049246.1\|WP_103906410.1\|2645989_2646196_+\|RNA-binding-S4-domain-containing-protein	unknown	unknown	gnl\|CDD\|379097
NZ_CP049246.1\|WP_103906395.1\|2667843_2668632_+\|DUF3822-family-protein	unknown	unknown	gnl\|CDD\|378980
NZ_CP049246.1\|WP_103906392.1\|2669640_2670951_-\|DEAD/DEAH-box-helicase	unknown	unknown	gnl\|CDD\|223587
NZ_CP049246.1\|WP_103906452.1\|2646280_2647345_+\|3-dehydroquinate-synthase	unknown	unknown	gnl\|CDD\|341474
NZ_CP049246.1\|WP_103906397.1\|2663768_2666258_-\|S9-family-peptidase	unknown	unknown	gnl\|CDD\|366374
NZ_CP049246.1\|WP_103906408.1\|2648590_2651860_+\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|274948
NZ_CP049246.1\|WP_103906400.1\|2661399_2662134_+\|polyprenol-monophosphomannose-synthase	unknown	unknown	gnl\|CDD\|133062
NZ_CP049246.1\|WP_103906404.1\|2657110_2657989_+\|sugar-phosphate-isomerase/epimerase	unknown	unknown	gnl\|CDD\|366542
NZ_CP049246.1\|WP_103906405.1\|2656355_2657087_+\|(Fe-S)-binding-protein	unknown	unknown	gnl\|CDD\|223325
NZ_CP049246.1\|WP_103906406.1\|2655039_2656359_+\|MFS-transporter	unknown	unknown	gnl\|CDD\|341035
NZ_CP049246.1\|WP_103906398.1\|2663215_2663767_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP049246.1\|WP_103906409.1\|2647348_2648074_+\|ThuA-domain-containing-protein	unknown	unknown	gnl\|CDD\|377643

Protein	Function_ID	Function_description	E-value
NZ_CP049246.1\|WP_103906399.1\|2662180_2663203_+\|Holliday-junction-branch-migration-DNA-helicase-RuvB	gnl\|CDD\|234619	PRK00080, ruvB, Holliday junction branch migration DNA helicase RuvB.	0
NZ_CP049246.1\|WP_103906394.1\|2668619_2669159_+\|methyltransferase-domain-containing-protein	gnl\|CDD\|223813	COG0742, COG0742, N6-adenine-specific methylase [DNA replication, recombination, and repair].	1.52871e-48
NZ_CP049246.1\|WP_103906393.1\|2669155_2669620_+\|pantetheine-phosphate-adenylyltransferase	gnl\|CDD\|234674	PRK00168, coaD, phosphopantetheine adenylyltransferase; Provisional.	4.91652e-65
NZ_CP049246.1\|WP_160003735.1\|2653703_2654999_+\|peptidase-S13	gnl\|CDD\|224938	COG2027, DacB, D-alanyl-D-alanine carboxypeptidase (penicillin-binding protein 4) [Cell envelope biogenesis, outer membrane].	2.43641e-31
NZ_CP049246.1\|WP_103906451.1\|2651883_2653590_+\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	gnl\|CDD\|369630	pfam07980, SusD_RagB, SusD family. This domain is found in bacterial cell surface proteins such SusD and SusD-like proteins, as as well RagB, outer membrane surface receptor antigen. Bacteroidetes, one of the two dominant bacterial phyla in the human gut, are Gram-negative saccharolytic microorganisms that utilize a diverse array of glycans. Hence, they express starch-utilization system (Sus) for glycan uptake. SusD has 551 amino acids, and is almost entirely alpha-helical, with 22 alpha-helices, eight of which form 4 tetra-trico peptide repeats (TPRs: helix-turn-helix motifs involved in protein-protein interactions). The four TPRs pack together to create a right-handed super-helix. This is predicted to mediate the formation of SusD and SusC porin complex at the cell surface. The interaction between SusC and TPR1/TPR2 region of SusD is predicted to be of functional importance since it allows SusD to be in position for oligosaccharide capture from other Sus lipoproteins and delivery of these glycans to the SusC porin. The non-TPR containing portion of SusD is where starch binding occurs. The binding site is a shallow surface cavity located on top of TPR1. SusD homologs such as SusD-like proteins have a critical role in carbohydrate acquisition. Both SusD and its homologs, contain about 15-20 residues at the N-terminus that might be a flexible linker region, anchoring the protein to the membrane and the glycan-binding domain. Other homologs to SusD have been examined in Porphyromonas gingivalis such as RagB, an immunodominant outer-membrane surface receptor antigen. Structural characterization of RagB shows substantial similarity with Bacteroides thetaiotaomicron SusD (i.e alpha-helices and TPR regions). Based on this structural similarity, functional studies suggest that, RagB binding of glycans occurs at pockets on the molecular surface that are distinct from those of SusD.	1.18695e-40
NZ_CP049246.1\|WP_103906411.1\|2644701_2645895_-\|proline-dehydrogenase	gnl\|CDD\|215366	PLN02681, PLN02681, proline dehydrogenase.	2.30962e-107
NZ_CP049246.1\|WP_103906401.1\|2659634_2661218_+\|peptide-MFS-transporter	gnl\|CDD\|225646	COG3104, PTR2, Dipeptide/tripeptide permease [Amino acid transport and metabolism].	1.86863e-107
NZ_CP049246.1\|WP_103906410.1\|2645989_2646196_+\|RNA-binding-S4-domain-containing-protein	gnl\|CDD\|379097	pfam13275, S4_2, S4 domain. The S4 domain is a small domain consisting of 60-65 amino acid residues that was detected in the bacterial ribosomal protein S4.	4.25155e-23
NZ_CP049246.1\|WP_103906395.1\|2667843_2668632_+\|DUF3822-family-protein	gnl\|CDD\|378980	pfam12864, DUF3822, Protein of unknown function (DUF3822). This is a family of uncharacterized bacterial proteins. However, structural-similarity searches indicate the family takes on an actin-like ATPase fold.	5.57392e-19
NZ_CP049246.1\|WP_103906392.1\|2669640_2670951_-\|DEAD/DEAH-box-helicase	gnl\|CDD\|223587	COG0513, SrmB, Superfamily II DNA and RNA helicases [DNA replication, recombination, and repair / Transcription / Translation, ribosomal structure and biogenesis].	8.0502e-84
NZ_CP049246.1\|WP_103906452.1\|2646280_2647345_+\|3-dehydroquinate-synthase	gnl\|CDD\|341474	cd08195, DHQS, Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway for aromatic compounds synthesis. Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway, which involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds, is found in bacteria, microbial eukaryotes, and plants, but not in mammals. Therefore, enzymes of this pathway are attractive targets for the development of non-toxic antimicrobial compounds, herbicides and anti-parasitic agents. The activity of DHQS requires nicotinamide adenine dinucleotide (NAD) as cofactor. A single active site in DHQS catalyzes five sequential reactions involving alcohol oxidation, phosphate elimination, carbonyl reduction, ring opening, and intramolecular aldol condensation. The binding of substrates and ligands induces domain conformational changes. In some fungi and protozoa, this domain is fused with the other four domains in shikimate pathway and forms a penta-domain AROM protein, which catalyzes steps 2-6 in the shikimate pathway.	5.46062e-151
NZ_CP049246.1\|WP_103906397.1\|2663768_2666258_-\|S9-family-peptidase	gnl\|CDD\|366374	pfam00930, DPPIV_N, Dipeptidyl peptidase IV (DPP IV) N-terminal region. This family is an alignment of the region to the N-terminal side of the active site. The Prosite motif does not correspond to this Pfam entry.	2.17881e-35
NZ_CP049246.1\|WP_103906408.1\|2648590_2651860_+\|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_CP049246.1\|WP_103906400.1\|2661399_2662134_+\|polyprenol-monophosphomannose-synthase	gnl\|CDD\|133062	cd06442, DPM1_like, DPM1_like represents putative enzymes similar to eukaryotic DPM1. Proteins similar to eukaryotic DPM1, including enzymes from bacteria and archaea; 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. This protein family belongs to Glycosyltransferase 2 superfamily.	4.16569e-92
NZ_CP049246.1\|WP_103906404.1\|2657110_2657989_+\|sugar-phosphate-isomerase/epimerase	gnl\|CDD\|366542	pfam01261, AP_endonuc_2, Xylose isomerase-like TIM barrel. This TIM alpha/beta barrel structure is found in xylose isomerase and in endonuclease IV (EC:3.1.21.2). This domain is also found in the N termini of bacterial myo-inositol catabolism proteins. These are involved in the myo-inositol catabolism pathway, and is required for growth on myo-inositol in Rhizobium leguminosarum bv. viciae.	3.49379e-16
NZ_CP049246.1\|WP_103906405.1\|2656355_2657087_+\|(Fe-S)-binding-protein	gnl\|CDD\|223325	COG0247, GlpC, Fe-S oxidoreductase [Energy production and conversion].	1.29178e-47
NZ_CP049246.1\|WP_103906406.1\|2655039_2656359_+\|MFS-transporter	gnl\|CDD\|341035	cd17482, MFS_YxiO_like, Bacillus subtilis YxiO, Listeria monocytogenes BtlA, and similar transporters of the Major Facilitator Superfamily. This family is composed of Bacillus subtilis MFS-type transporter YxiO, and similar proteins including Listeria monocytogenes BtlA. The function of B. subtilis YxiO is still unknown, and L. monocytogenes BtlA is a putative secondary transporter involved in bile tolerance and general stress resistance. This 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.	1.06285e-99
NZ_CP049246.1\|WP_103906396.1\|2666344_2667769_-\|AAA-family-ATPase	gnl\|CDD\|350691	cd17933, DEXSc_RecD-like, DEXS-box helicase domain of RecD and similar proteins. RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.	9.91006e-35
NZ_CP049246.1\|WP_103906409.1\|2647348_2648074_+\|ThuA-domain-containing-protein	gnl\|CDD\|377643	pfam06283, ThuA, Trehalose utilisation. This family consists of several bacterial ThuA like proteins. ThuA appears to be involved in utilisation of trehalose. The thuA and thuB genes form part of the trehalose/sucrose transport operon thuEFGKAB, which is located on the pSymB megaplasmid. The thuA and thuB genes are induced in vitro by trehalose but not by sucrose and the extent of its induction depends on the concentration of trehalose available in the medium.	1.2937e-100

>NZ_CP049246.1|WP_103906404.1|2657110_2657989_+|sugar-phosphate-isomerase/epimerase
MNSRREFLRNLGLITAGATLAPSLDVFAAKKDWFEISLAEWSLHRTLYKGDLKNIDFPEFTAKTFGIYGVEYVNQFFKDKAKDMTYLKDLNNRAKDNGVKNVLIMIDGEGNLGDRDEAKRVEAVENHYKWIDAAHFLGCHAVRVNAAGKGTKEEVKEQVVKSLSTLADYGKKGKISVVVENHGGISSHGDWLADVLKSVGKKNCGSLPDFGNFYEYDRYQGVKELMPYAKGVSAKSHAFDANGNDTGIDYAKMMAIVKEAGYKGYVGIEFEGDKISEVEGIKLTKALLEKFK
>NZ_CP049246.1|WP_103906405.1|2656355_2657087_+|(Fe-S)-binding-protein
MNKVELFIPCFIDQLYPETAFNTVKLLEKAGCEVVYNTEQTCCGQPSYNAGFWDEAKIIGQKFLGDFNVEHPIVSPSASCVGMVRGGYDDLFTNSIEHNTCRSIQRNIFEISDFLVNVLQKEYFGAELVGTAVYHDSCSALRECKIKEEPRRLLSHVGGLDLVEMRGQETCCGFGGSFAVKFEGISAAMAEQKVLSAMEVKADYIISTDSSCLLQLQAYIEKHQLPIKTMHLVDVLTSGWANI
>NZ_CP049246.1|WP_103906406.1|2655039_2656359_+|MFS-transporter
MKVFKKNDKRLIRSWSMFDWANSAYNLVINSTIFPVYYTAITANKDTGDTVSFFGIELVNTALSNFSLSIAYLLMALGLPFISAYSDAAGKRKFFMKLFTYVGAFACMGMFFFKLETLEWGIVCFALAAIGYIGGVAFNNSYLPIIATPDQQDRVSAQGFAYGYVGCVTLQLICFVFVFKPEWFGIVDPSLPARISFLLVGLWWILFAQIPFRYLPKNRPTIGSEKMPFFQKVKNEFNTVLAEIKKIDAIRRFLPAYFFYAMGVQTLLIVAAAFGEKELQLGSSKLIASILLIQIVAIGGAYIMSVLAKRFGNIKVLIVVVFFWVMICCFSYFLNNEYQFYGMAFAVGLLMGGIQSLSRSTYSRLIPEHIEDTTSFFSFYDVTEKIAIVVGLFTFAFIEQITHNIRYSALFLSVFFLIGFFLLFRVLKFNKLQIIQNNK
>NZ_CP049246.1|WP_160003735.1|2653703_2654999_+|peptidase-S13
MKNILTALGLFAFLTVHAQIDQDLNQQLQKSNILNKHYYGFSLYDINNQSFVFNYNPEKHFTPASNTKVFTLYTSLKLIGDSIPGLAYEERGDSLIFWGTGDPTFLHTRLDNGKVYNFLKNSNKKLFYATANTQEPSYRNGWSIEDYEFYYQPEVSVFPIYGNVIQFREVNGKLSLMPSHFDKEVVQLSDTTTRYRIHRALENNRLEINELPLPKGYVNEKPFRPSDTLLVKLLEDTLHQEVQLINLPLLANHKIVYSLPTKDVLREMMLPSDNFLAEQLNMIASFLKYRAFKTEDLRAYMMKEYYSKLPDTIELRDGSGLSSYNKITPRSMVQLLLWINNEVRDEAAKLKLFPAGGLEGTLKGVYPTPGGKAFVWAKTGTINSVHCQSGYIQTKKGNRYAYSFLNNNYMGSSGPVRREMVRIITHIYENY
>NZ_CP049246.1|WP_103906451.1|2651883_2653590_+|RagB/SusD-family-nutrient-uptake-outer-membrane-protein
MMKRNKLMILLGAGMLLVSSCGKEFLQKLPQGQLSEPQVGNKDGVEGALVGAYSILNGNVSGTWGNYSSAPSQWLFGEVASDNAHKGSFLDDQSPMNMIEAYNVISTNDNLSQMWQVYFEGVMRCNNTLRLLANDQASTKEITAERALQIQAECKMLRAHYYFMLWRVFRNVPIITEDISTEDAQTVKNDKDVLPLIEEDLKFAVANLPATKINNEFGRMDKNAAKAYLGKLYLYQKKYGDALGLFKEVMAGKDIVGMPFWNNFDVTTENGPEVVMVSKHAINSNGSADNANVGDMLGGLYGSSPVGCCGFYQPTIDLVNAYKVDAKGLPLLDDSYRTNPYLSDKGVAANATYTLNVKLRFDPRLDYTVGRRGVEYLDYGIMPGNGWIRDANYAGPFVGIKTMIPRSQFPTQAAPGENYLTGLDVNIIRLADVWLMAAECEVELGNLAGAMKYVNDIRKRAANLEPKKTATGVNAADYDVKPYTSFPSPDYARKAVRFERRLELAMEGHRFYDLVRWGIAKQTIEAYSAFEGQHLSSYLNLKFDPADEYYPIPQAEIDRSNGALTQKK
>NZ_CP049246.1|WP_103906408.1|2648590_2651860_+|TonB-dependent-receptor
MGKSMKFQGNPFSKRVLKNSLLISMGVLSLQTAIAAESTIWNRIATHPLYAIQTPVKGRIVDKATQQPIIGATIKVVGKTSSTSSDASGNFEIDAQANDVLEVTYVGFVTARYTVTSVTQNAVISLDEDSSNLEEVVVTGYGAQRKKDLTGAVAVVNVSELKSQPAGSAVEALQGRATGVQIVNDGAPGSTPQIRIRGYSTVRNNEPLYVIDGVPFEGKLSWLNQNDIESMQVLKDASAASIYGARANNGVVIITTKSGKEGRTTIAFDAYAGVGVPNKSTFPKMLTPQQVLDFDNRLNGTNLTLPEYLVAGGNSDHKITPEDLDMSKYNYFAKDRSGFYQITKANHAGTNWFNELSQNAPIQSYQLSASGGSETAQYAFSGGFLDQKGSLIHSGFRRYNVRNNAQFNAFNKKLRFGENVSYAYTEGFGMGVNPNTAGGYQGEGSVLGFAYRIQNIIPVYDEGGNFAGSWGEGHGNGQNPVAMAYRAKDNMNRSNFFFGNAFAEYDIIDGLTFRSNFGLRYENYNGVSYTYPNPEFSEGGFNNGMSEYHGFTTEWTWTNTVNYKPKLGEDHVLNIMLGTEAIKNRNRGIDGSRNGYFIMNSLDYLYLNAGSTNFNNNGSGSISSMFSLMGKVDYSYKDRYLLSLIGRRDGSSNFGVNNLYGVFPGISGAWRISQEEFAQGAEWLTDLKLRAGYGVTGNQSIPAFQYLNRYVSSLTQSSYPMNSTAINGIWQSDYANPDIKWEQVKSVNVGLDFTVLNGDLDGSIDWFNKTTTDMLFLVPLPAAAVGRAASPYQNIGDMSNKGIEFSLGYHYGQRQEKPFTLDLSASFSRYVNKVVSLAPTIDHVNYGVFRSMETSILQKGQPFGSFYGYQVAGIYQSEDDVANSPSYENARPGGLKYADLNNNGEIDPGDRTIIGNPHPDFVYSLNINANYKNFDLLMFFYGSQGNDLYEATRYFTDFGVFKGQKSARLLNEWSPTNTGSDIPSLPSPEQNPSAMEYVTSSYYIQDGSFLKLKNLQLGYNLPTQKIFGENTSFNRLRVYLGVTNVFTITKYEGLDPEVSATPSDYPALGVDFGVYPQARQYTFGLSLGF
>NZ_CP049246.1|WP_103906409.1|2647348_2648074_+|ThuA-domain-containing-protein
MRKLITLTLLILIGVSASFATYAKNPKKVLLFTKTAAFRHDNIEEGVQVIKKLYKENGIDVFHTEDAGIFLADSLKNFDAVLFFSTTGNILDEAQKNAFQKFLKSGKGFMGIHAATDTEHEWPWYGQLVGGYFASHPAVQEAKINVLNRKHPATKHLPKEWFHKDEWYDFSDVKPGLNILMTLDESSYKNGKMGDFHPIAWYQVFEGIKMFYTGLGHTKESFQDANFQKQILGGIKYVLGK
>NZ_CP049246.1|WP_103906452.1|2646280_2647345_+|3-dehydroquinate-synthase
MKKITSLGYDVVFDDSLSELQLFLVDHDYSQLLILVDRNTNDHCLPVIQAAIPDIVDYDIIEVDPGEENKNIDFCIGVWKTMLDFGADRKALMLNLGGGVVTDMGGFAASTYKRGIDFIHIPTTLLSQVDASVGGKTGIDLDNVKNIIGTFSQPQAVFISNKFLETLDDRQMRSGFAEVIKHGLIQDKSLFERCKTVVLPNLPEDMVYESVQIKNKVITEDPTEKGLRKILNFGHTIGHAIEGYSLVSDNNPLLHGEAIAIGMVCEAYISNKVNGLPDQELKEISDFLMALYPAYDYNTAVYPEFIELMRNDKKNESNKLGFALLNTIGDCAYNNYVEEDLIIESLDYYKSLIN
>NZ_CP049246.1|WP_103906410.1|2645989_2646196_+|RNA-binding-S4-domain-containing-protein
MQTFTLKGEFIQLIQLLKVMNWVEHGAMAQWAVEEGLVKYNGEVDYRKRLKVKVGDMVEFDGNKVKII
>NZ_CP049246.1|WP_103906411.1|2644701_2645895_-|proline-dehydrogenase
MDIASPLKLDFNNTEIAFSGKSDKDLNKAYWLFKMVASNALIKIGTPITTFSLNIGLPITGIIKNTIYKQFCGGESIADCSRAIQDLGKGHVTTILDYSVEGEESEASFDATCAEILRTVDAAKANPLISFCVFKPTGLGRFDLLAKIDAKETLTATEQEEYKRLMDRCDRICKACHDAGIPVLVDAEHSWIQDTIDDIAREMMEKYNQEKPIVYNTYQLYRHDKLASLKADFAYAKTQDFHLGAKIVRGAYMEIERERAKEKGYPSPIQPDKPASDTDYNQAIHFCLDNIDRIGLMAGTHNEQSCRILAEELERRNIPHNTPNVFFAQLLGMSDNLSFNLAAAGYNVAKYMPYGPVKAVMPYLFRRAQENTSVGGQTGRELSLIMKELKRRKSARK
>NZ_CP049246.1|WP_103906401.1|2659634_2661218_+|peptide-MFS-transporter
MNQENDQDLVQHLEKQGVETKMVMGHPASLFVLFFTEMWERFSYYGMRALLTVFLITEIAKGGWGWNNSDAMQLYAWYTGLVYLTPLIGGMIADKLTGYRKAILWGALIMTLGHASMAFEQTSPTFFYIGLVLMILGNGMFKPNISSMVGQLYPDTSKKKDAGYTIFYMGINSGAFLGMLLCGYIGEKVGWHYGFGLAGVFMFFGMVQFYFAQKIFGVIGEEPGTKHAPSEHVHNLVEEDQTPKNVVRDRLVVVAVLMIASIFFFFAFEQAGGSMTIFAKDYTQRVLSGEAGTIFKWVDAALTIFPILIVTYVLFQLSTQIYSKYPMTVIATAISFAIIWGLGLWKVNREFSQDVTEVTVSWFQILNSFFIVTLASSFSKLWEKVWNPSGPVKFAFGLILVAVGFVALAYGSMSIPQGAKTASVSMIWLILAYFFHTTGELCLSPVGLSYVSKLSPKKFAGLLFGLWFTASAIANFIAGMTGSYIDMITEKYSMTVFFLIIAALPVAVAILLLLFNGKLKKMMHGIN
>NZ_CP049246.1|WP_103906400.1|2661399_2662134_+|polyprenol-monophosphomannose-synthase
MSDSLVIIPTYNEKENIERIIRKVFSLEVDFDILIVDDGSPDGTAEIVKQLQSIEFVGRLHIEERKGKLGLGTAYIHGFKWALARNYAFIFEMDADFSHNPDDLIRLRDSCKYKGADMTIGSRYIKGVNVVNWPMNRVLMSYFASAYVRLITRIDIQDATAGFVCFRREVLETIPLEKIKFVGYAFQIEMKFTAIQYGFNVVEIPIIFTDRTLGTSKMSTKIFKEAFFGVIQMKLGSLFKKYNR
>NZ_CP049246.1|WP_103906399.1|2662180_2663203_+|Holliday-junction-branch-migration-DNA-helicase-RuvB
MNEHLDPNPDRLSPTEKDLERVLRPQTFEDFTGQAKILENLSIFVKAAKLRGEALDHVLLHGPPGLGKTTLSHIIANEMGVGIKITSGPVLDKPGDLAGLLTGLDEGDILFIDEIHRLSPLVEEYLYSAMEDFKIDIMLETGPNARSVQISLNPFTLVGATTRSGLLTAPLRARFGINSRLQYYDSKLLTDIVMRSAAIIHVPISEEGAYEIARRSRGTPRIANALLRRTRDFAQIKGNGSIDKAIAQFALNALNVDEHGLDEMDNRILSTIIDKFKGGPVGLKTIATAVGEDEGTIEEVYEPFLIQEGYLMRTSRGRECTELAFKHLGKNYFNKGNTLF
>NZ_CP049246.1|WP_103906398.1|2663215_2663767_-|hypothetical-protein
MTNKNAKTIQEALMYIGASDLNTDLLQIVSLEDLLAMNMDRKNPRLAFRTAWAVEHILLKHTDLLAQVYPTMLSQYNQLENWSCLRSYTKLIMWMLGRENKSISLTESEQESILDKTFSIVEDPECPVAVLVNGLDILFLLSLEMKWLRTELRMLVEFHLEKEATPALKSRGSMLLKKLTKLN
>NZ_CP049246.1|WP_103906397.1|2663768_2666258_-|S9-family-peptidase
MKYYFLGLCLLIGSYATAQEPSTLAKPNYQLAAKYSPAKLSKMIFSTEVNPNWINFGDKFWYEYNSPKGKKWYLVDPKTRKKSELFDHAEMASRITSIVKNPFDAQHLDIRNLRFMENENLIRFEVQSTKDTVKTKEEIKKLTNKNDTLKKKLFYFEYNLSNKNLRELSEDSKDKSRLFWANFNPDTTKVFYAKDYNLYWMDYANFQKAQKDEKDSTIVEHQITTDGVQYYAWGGDEYSSTTGDKKSLDEEKKKRKPVWINWSPNGRYFTLTRKDNRELSALWVINNVAAQRPTLETYKYLMPGELDSTETELHIFDASTLKSRQVPVAAFKNQTISSWNADRNKNSYKGKHYINYWLGNDEEFYIARSSRDLKRIDILAVNVATGQPRTVIEERSNVYLDVKKPYLINNGNQLIHWSQRDGWGHFYLYNKNGALVNQITNGAYHCDELSSYNEATGTLYFKANGLEKNIDPYYSFFYSVNKNGGNVKLLTPGNFDHQVTSSESGNYFIDNFSRVNTAPVSNLYNGNGQLVMKLEETDLSNLLASGYKFPEPFTVKAGDGITDLYGVMYKPFDFDSTKTYPIIEYVYPGPQTEAVNKSFGRSMDRIDRLAQMGFIVVSVGNRGGHPSRSKWYHTYGYGNLRDYGLEDKKVVAEQLANRYSFIDINRVGITGHSGGGFMSTAAMLVYPDFFKVAVSGAGNHENNIYNRWWSERHHGVKEVVNAKGDTTFSYQIQKNTELAKNLKGHLLLVTGDIDNNVHPANTIRMVDALIRANKRFDFLLLPGQRHAFGDMTEYFFWRMADYFSQHLLGASAMNEVDIMEMNREKPMGK
>NZ_CP049246.1|WP_103906396.1|2666344_2667769_-|AAA-family-ATPase
MQIKNTLIQQFSHAPTEQQIEVFSQLASFLMTFRSDSCFILKGYAGTGKTSIIGALVKTLPKLMKRSVLLAPTGRAAKVMSAYSGRNALTIHKKIYRKKNAASLDMDFSLGDNSHENTLFIVDEASMLSNEGVTMFSQGLLHDLIRYVQSGENCSLMLVGDIAQLPPVGLEDSPALNPEYMNGEFGLDIFTYELTDVVRQDKHSGILYNATKIRNEIRLDEEFAEYSYPKFVTKGFHDIFRMNGDRLIEGLHYAYDKFGINNSMVICRSNKSANLYNKHIRNQILFREEEITGGDLIMVVRNNYYWLQENDEKSTGFIANGDMAVVKKVSNIHDMHGFRFADLYLEFMDNNEGDAIRCRVLLDSLYVDSANLPYEQQKELYNSIAEDYADIGTKKDRMDAIKKDPYYNALQIKFAYAITCHKAQGGQWPLVFVDQGYMVDEMLNTEFMRWLYTAITRATQELFLVNFNEKFYPH
>NZ_CP049246.1|WP_103906395.1|2667843_2668632_+|DUF3822-family-protein
MNYTAKQFHLHYISQYTLIVKANYEYDMLYVLDAEGQILVYMKFESMEPSEEALKLLSLPFQQVFVSVPSQNLTFIPQDLYQEEDLDAYRDFMENPSAAIETEHLDFLQIQALYQYDVLLSHRWKTLFPSAVFIPEFKLNLLQARPYIPLKGEVVGVVFNNSTTDIFLFVNGQFKFYNTFEILSDDDLSYFILNVFDNFQLKDKVTKALVSGVDLEDSVLRKLDNYAHELVYIKASHPAKANEALEEEVSSLYLLDLPTCAS
>NZ_CP049246.1|WP_103906394.1|2668619_2669159_+|methyltransferase-domain-containing-protein
MRIIGGKAAGLRLNPPQNLPVRPTTDIAKEALFNILNNRLDFDELTCLDLFAGTGNISFELASRHAVKVDAVDQHGKCVIYITDTAKKLNLEQIKARKADVFKYIKSAKESYDLIFADPPYDLGQLPMLPKIILEGDLLKPGGLLIVEHPSNRKMVDHPHFQETRQYGNSSFSFYTLPS
>NZ_CP049246.1|WP_103906393.1|2669155_2669620_+|pantetheine-phosphate-adenylyltransferase
MKIAVFPGSFDPYTIAHHDLIERALPLFDKIYIAIGVNSSKVGLMDTDSRKEAITALYQEVPQVEVSFYTGLTVDFCRSVGANFILRGIRNGADLDYENIIAQNNLILAPDIETYFLVSRSGKAHISSTIVRDIWKNKGDISHLVPEAILDFIK
>NZ_CP049246.1|WP_103906392.1|2669640_2670951_-|DEAD/DEAH-box-helicase
MQKLSTYLDNLKIEALNPMQEQVMDQFVNGRDFVLLSPTGSGKTLAFSLLVHKLLLESNKTGVQSLIVVPTRELALQIETVIKQMDPHVNVACIYGGNNNQLEKDKLKQQPPIVIGTPGRIIYHIERVPDLLVNCETLVLDEFDKSLELGFQDQLSFIIAACRFVKHKILTSATDMEELPEFLALNNPVKLDYFDGDKLRPDLSYYKVISSTKLKLESLFKLICKIGNERVLVFCNHREAVEHISDILEGKGIDSIPYHGGLEQFVRELTITKIKNGSQNILVTTDLAARGLDIPEMNHVIHYQFPYKDEDFIHRNGRAGRNGQKGYIYGILTEEDRAAKFLDHAETITLDEFYPLPEPPAYRTLRISAGKKQKVNKIDIVGYILNLPDIDKDDLGVIVVKAHDSYIAVKQEVAAKVAKTGSNGKIKGNKVRINLI

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Crispr_ID: NZ_CP049246_12

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP049246_12

3180538-3180691

Orphan

Consensus_repeat	Method
CCAGCGGGCGTTAATAAAATGCCAAAGGCACAAGAGACCCAACCCACA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP049246_12

>merge|NZ_CP049246|12|3180538-3180691|CRISPRCasFinder
CCAGCGGGCGTTAATAAAATGCCAAAGGCACAAGAGACCCAACCCACAGGCCCAACCGCACAACTCTTGCGCCAGCCTAAATAAACCCTACCGCTCAATCCATACTCCAGCGGGCGTTAATAAAATGCCAAAGGCACAAGAGACCCAAACCACA

>NZ_CP049246|12|11|3180538-3180691|CRISPRCasFinder
CCAGCGGGCGTTAATAAAATGCCAAAGGCACAAGAGACCCAACCCACA	GGCCCAACCGCACAACTCTTGCGCCAGCCTAAATAAACCCTACCGCTCAATCCATACT
CCAGCGGGCGTTAATAAAATGCCAAAGGCACAAGAGACCCAAACCACA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP049246.1\|WP_103905151.1\|3193019_3193919_-\|helix-turn-helix-transcriptional-regulator	unknown	unknown	gnl\|CDD\|197666
NZ_CP049246.1\|WP_103905165.1\|3170949_3171597_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP049246.1\|WP_103905156.1\|3184268_3185261_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|235906
NZ_CP049246.1\|WP_103905155.1\|3186003_3187710_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP049246.1\|WP_103905161.1\|3176459_3176903_-\|carboxymuconolactone-decarboxylase-family-protein	unknown	unknown	gnl\|CDD\|225039
NZ_CP049246.1\|WP_103905154.1\|3187736_3191792_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP049246.1\|WP_103905158.1\|3181384_3182236_+\|ATP-phosphoribosyltransferase	unknown	unknown	gnl\|CDD\|234781
NZ_CP049246.1\|WP_103905152.1\|3192240_3192450_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP049246.1\|WP_103905163.1\|3174793_3175273_+\|Lrp/AsnC-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224439
NZ_CP049246.1\|WP_103905168.1\|3165889_3166717_-\|DUF4249-domain-containing-protein	unknown	unknown	gnl\|CDD\|379442
NZ_CP049246.1\|WP_103905150.1\|3194135_3195119_+\|aldo/keto-reductase	unknown	unknown	gnl\|CDD\|381304
NZ_CP049246.1\|WP_103905162.1\|3175278_3176409_+\|EamA-family-transporter	unknown	unknown	gnl\|CDD\|183067
NZ_CP049246.1\|WP_103905166.1\|3170012_3170888_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP049246.1\|WP_103905385.1\|3166720_3169006_-\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|238657
NZ_CP049246.1\|WP_103905157.1\|3182235_3183528_+\|histidinol-dehydrogenase	unknown	unknown	gnl\|CDD\|376389
NZ_CP049246.1\|WP_103905159.1\|3180758_3181067_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP049246.1\|WP_103905167.1\|3169186_3170005_-\|esterase-family-protein	unknown	unknown	gnl\|CDD\|223700
NZ_CP049246.1\|WP_103905160.1\|3177144_3179715_+\|carboxypeptidase-like-regulatory-domain-containing-protein	unknown	unknown	gnl\|CDD\|372685
NZ_CP049246.1\|WP_103905164.1\|3171643_3174481_-\|FAD-binding-oxidoreductase	unknown	unknown	gnl\|CDD\|223354
NZ_CP049246.1\|WP_103905153.1\|3191992_3192283_-\|JAB-domain-containing-protein	unknown	unknown	gnl\|CDD\|163702

Protein	Function_ID	Function_description	E-value
NZ_CP049246.1\|WP_103905151.1\|3193019_3193919_-\|helix-turn-helix-transcriptional-regulator	gnl\|CDD\|197666	smart00342, HTH_ARAC, helix_turn_helix, arabinose operon control protein.	6.52349e-20
NZ_CP049246.1\|WP_103905156.1\|3184268_3185261_-\|hypothetical-protein	gnl\|CDD\|235906	PRK07003, PRK07003, DNA polymerase III subunit gamma/tau.	1.44782e-08
NZ_CP049246.1\|WP_103905150.1\|3194135_3195119_+\|aldo/keto-reductase	gnl\|CDD\|381304	cd19078, AKR_AKR13C1_2, AKR13C family of aldo-keto reductase (AKR). The AKR13C family includes Helicobacter pyroli aldehyde reductase (AKR13C1) and Thermotoga maritima aldo-keto reductase (AKR13C2). Aldehyde reductase (EC 1.1.1.21), also called aldose reductase, is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides.	0
NZ_CP049246.1\|WP_103905158.1\|3181384_3182236_+\|ATP-phosphoribosyltransferase	gnl\|CDD\|234781	PRK00489, hisG, ATP phosphoribosyltransferase; Reviewed.	4.80401e-133
NZ_CP049246.1\|WP_103905161.1\|3176459_3176903_-\|carboxymuconolactone-decarboxylase-family-protein	gnl\|CDD\|225039	COG2128, COG2128, Uncharacterized conserved protein [Function unknown].	9.70655e-30
NZ_CP049246.1\|WP_103905168.1\|3165889_3166717_-\|DUF4249-domain-containing-protein	gnl\|CDD\|379442	pfam14054, DUF4249, Domain of unknown function (DUF4249). This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 279 and 365 amino acids in length. There are two completely conserved residues (C and G) that may be functionally important.	1.90865e-38
NZ_CP049246.1\|WP_103905162.1\|3175278_3176409_+\|EamA-family-transporter	gnl\|CDD\|183067	PRK11272, PRK11272, putative DMT superfamily transporter inner membrane protein; Provisional.	2.61007e-48
NZ_CP049246.1\|WP_103905385.1\|3166720_3169006_-\|TonB-dependent-receptor	gnl\|CDD\|238657	cd01347, ligand_gated_channel, TonB dependent/Ligand-Gated channels are created by a monomeric 22 strand (22,24) anti-parallel beta-barrel. Ligands apparently bind to the large extracellular loops. The N-terminal 150-200 residues form a plug from the periplasmic end of barrel. Energy (proton-motive force) and TonB-dependent conformational alteration of channel (parts of plug, and loops 7 and 8) allow passage of ligand. FepA residues 12-18 form the TonB box, which mediates the interaction with the TonB-containing inner membrane complex. TonB preferentially interacts with ligand-bound receptors. Transport thru the channel may resemble passage thru an air lock. In this model, ligand binding leads to closure of the extracellular end of pore, then a TonB-mediated signal facillitates opening of the interior side of pore, deforming the N-terminal plug and allowing passage of the ligand to the periplasm. Such a mechanism would prevent the free diffusion of small molecules thru the pore.	2.54005e-21
NZ_CP049246.1\|WP_103905157.1\|3182235_3183528_+\|histidinol-dehydrogenase	gnl\|CDD\|376389	pfam00815, Histidinol_dh, Histidinol dehydrogenase.	0
NZ_CP049246.1\|WP_103905164.1\|3171643_3174481_-\|FAD-binding-oxidoreductase	gnl\|CDD\|223354	COG0277, GlcD, FAD/FMN-containing dehydrogenases [Energy production and conversion].	1.19371e-75
NZ_CP049246.1\|WP_103905167.1\|3169186_3170005_-\|esterase-family-protein	gnl\|CDD\|223700	COG0627, COG0627, Predicted esterase [General function prediction only].	1.6207e-36
NZ_CP049246.1\|WP_103905160.1\|3177144_3179715_+\|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.	1.15661e-13
NZ_CP049246.1\|WP_103905163.1\|3174793_3175273_+\|Lrp/AsnC-family-transcriptional-regulator	gnl\|CDD\|224439	COG1522, Lrp, Transcriptional regulators [Transcription].	1.56643e-31
NZ_CP049246.1\|WP_103905153.1\|3191992_3192283_-\|JAB-domain-containing-protein	gnl\|CDD\|163702	cd08071, MPN_DUF2466, Mov34/MPN/PAD-1 family. Mov34 DUF2466 (also known as DNA repair protein RadC) domain of unknown function contains the signature JAB1/MPN/Mov34 metalloenzyme (JAMM) motif, EXnHS/THX7SXXD, which is involved in zinc ion coordination and provides the active site for isopeptidase activity. However, to date, the name RadC has been misleading and no function has been determined.	2.55183e-37

>NZ_CP049246.1|WP_103905160.1|3177144_3179715_+|carboxypeptidase-like-regulatory-domain-containing-protein
MKTPLLHWIFTLGLLLIFQSSYAQQYITIKGRVINADNSEPIPYASIKVVGAAKEIGASSNDKGEYTLSIPSTYQKIRISSVGFDSEEYPVSTEKEQYIRVMLFPANSIEEVVVKAPKRVKYSNKNNPAVELIRKVVEHRDQNRLTGQKYAEFDQYEKISLGLSNLNDKFKNRKVFKKYQFLFEEADSVKEGGNYVLPAYMEEKFSKVYYRKDPNAKKQYILAERKAEFDPKFVDNDGLSTYFNRLYDEVEIYDNNINILTNQFLSPIANSAPTFYRFYITDTVKNKDETLVELSFFPRNKNDLLFKGKLYVTLDGNYAVKAAEMTVADEINLNFVRDLDIQLGFSKTNDNKYYLTKSSLGIDFALTGKGKGIKGKRVVLIDKYQNGMERPDSIYNVPDQFVVIPEEAPEQKEESYWATLRPEPLSRSEAIIYNNIDSLQKMPSFRTFMDLSALILSGYKQAGPVEIGPVNTFYSYNPIEGFRLRVGGRTTEQLSKRFYVEGYGAYGFEDKKWKYFAAATYSLNNKSIYKFPQHYLRVSASYDTKIPGQNLEFVQEDNVLLSFKRGENKSYLYNEVYRVDYKVEFSNNLSMNAGLGMWKQTPAGVLQFALPQDDGSLVPINNLNSTEFNVGIRYAPHEEFYQGKLYRTPIFNKYPILNFNYTAGIKDLFGGEHNYHNFSLGVFKRFYLSQLGYADVNVDGTYIAGSNLPFPVLNIHRANQTYAYQLQSYNLMNFMEFISDHHASINVQYYMNGFIFNKIPLLNKLKLREVFSFKGVYGGLRDENNPSYNPDVYAWQTNGDGDRMSFTFGSEPYMEASAGVANIFKVLRVDVVKRLNYLDNPNAPEWGIRARIKFDF
>NZ_CP049246.1|WP_103905161.1|3176459_3176903_-|carboxymuconolactone-decarboxylase-family-protein
MSTRMNVQELEPKAYEVLFAMERYLANTDVSYALRELIKIRVSQINKCAYCLEMHTKDARKAGETEQRIYALSAWEESPLFSDEERAVLKFTEEVTHISQEGVREETFQSVKKYFSDNQVAQLIVAIGQINFWNRIAVTTRMQHKHV
>NZ_CP049246.1|WP_103905162.1|3175278_3176409_+|EamA-family-transporter
MVKSANPAASTVIFAYLVVYIVWGSTFFFIEKALHAFPPFVLGSIRFIIAGTLLMGYCWLKGYKLYIKKPVRDAATVGFLLLFVDMAAIIWSEQYISSAIVSILSAATAIWFIILDKPKWKENFSSIPTLLGLILGFLGVVMLFAEQIFGAEAAGANSDKKLTAMIVMTLGTIGWTVGSLISKYSKNSDKKKAEEETAQPKEEEDLNVMVKTAWQMVVAGTTFTLVALLNGEYKTFDFQAVPTEYWGAMIYLALMGSILAFSCYIYLLQVRPATEVSTYAYVNPIVALILVHFFTDHIVSRMQIIGLAVVLFSVLLMNWNLYRNSDLVKNYKRRRKIKKLRDMAPKSSIPRIVEVAEFGKKKEKKSKEDKNPETEQ
>NZ_CP049246.1|WP_103905163.1|3174793_3175273_+|Lrp/AsnC-family-transcriptional-regulator
MAKLEISLDQIDLQIIRIMQDNARTNNADIARELGMAPSAILERVKKLEQKEVILQYNARINPAALDQKMLSFIFIKTQDIIGVQKVGLLLAEIPEVLEVHDIAGEDGYLIKVRTNDSAGLVDLMRNSLSKIEGIISTRTTIVLETVKEDNKLVIPNKD
>NZ_CP049246.1|WP_103905164.1|3171643_3174481_-|FAD-binding-oxidoreductase
MRMAYATDASVYQEIPLAVCIPHNVEDLKILIRFARENGVTLIPRTAGTSLAGQVVGDGIVVDVSRAFNQILEVNAEEGWAIVQPGVIRDDLNAYLRPYGLMFGPETSTASRAMIGGMIGNNSSGLHSIVWGDTRQNLIAAQVLLDDESEVTFEALDEAAYFSKLTASGREGEIYRGINTLLANKENQEAIHAGFPKSDITRRNTGYALDLLSNTDNPFNMCNLLAGSEGTIGIVTSAKIKLMPLPPKEIGLVCIHFSDMVECMRGNVIALKHRPEASELVDKYILDFTVGHPTYQYNRFFIEGDPEALLIVEFRADDLADIMRQAEGLIAELKALGLGYAYPVITGTEQTNLVWDVRKAGLGLIRNLPGDSQPVNLIEDCAVSPEDLPAYVYDVQQLLSEQGVHASYYAHAGAGELHIEPFINLKTEAGRKQFRTILERTTDLVLKYNGSLSGEHGDGRLRGEFIGKVLGDKVYQLLLEVKDIFDPNQVFNARKIVNTPAMDTHLRYDQVYDGKKIGTYFDFTKQESILRLAEKCSGSGDCRKTEITGGTMCPSFMATRDEKDTTRARANMLRQFLTNSTKTNRFDHDEIKEVMDLCLSCKGCKTECPSSVDIAKMKAEFLQHYYDANGSPFRAKVIANFTQSQKLGAMVAPIYNFFATNGLTSSVIKSVVGFAPGRSLPKVSGTTFSQWVNKQKVEQKKRKVYLFSDEFTNYNDTEIGITAYKLLTALGYEVHVPKLSESGRTYLSKGFVKKAKELANKNVDLVADQISAETPLLGIEPSAIITFRDEYPDLVDAPKREKAIQLGQHALMIDEFLVREIEAGRIHPEQFTSEPQKIKLHGHCYQKAFKLVDYTKRLLSFPSNYEVEVIPSGCCGMAGSFGYEKEHFEVSQKVAELVLFPTLRKTGPEYLVAAAGTSCRHQIKDGLQRKSFHPVEIIYAALLKK
>NZ_CP049246.1|WP_103905165.1|3170949_3171597_-|hypothetical-protein
MKKITTYTLLASALVWMSACGNSNQSNTSTADSTGTAVTSAGLPPLVNSASGDINKFFFDLNEVGQTDSSVLYTAHSLYNSDTVGFQVEVMKNIPAGVAGDGRPDGEKGFVEGGVKFSSIGVPSDNFVKSLGTIFNLPTDGKMSSKTLLPLIFSSNNKPVDLSTQGTYSFKYFFRNGTGREAEMFGVLDTYKKSFELSEKDSTYRINIISSFEGK
>NZ_CP049246.1|WP_103905166.1|3170012_3170888_-|hypothetical-protein
MQRTHFLVLFIALLLSFGAAAQNPMPTTRTSHGKIQAPELDELSGIVASMNNPGSFWVHNDSGDKARFFLIDSTAQLQRTFYLEGIQAIDMEDIAWVQRNGVNYLILADIGDNLGRRQDIRLYLVKEPKLAESKTVDTIRAAAIETKVLQYPGKARDSEALFVDPLDNKLYMVSKREFQSALYTADIFGQERSSYQLREVLKFPFTFITAADMAMDRRAVLMKNLTTIFYWPIGDQEPLIKALAKPSVTLQYDPEPQGEAITFSREGEGFFTISERPFGLDSYLYHYHTKP
>NZ_CP049246.1|WP_103905167.1|3169186_3170005_-|esterase-family-protein
MKTTVSAFLLSLFFSFVHAAKVDTLAIPSAAMGKSIKTVIIQPEGGSAKELPTLYLLHGYSGNYSNWVNNVPAVKTLADQMQMVIVCPDGGFGSWYWDSPNDKNFQYETFVAKELVSYVNKNYPVANDRNKRGITGLSMGGHGALYLAIRHQDIFGAAGSTAGGVDIRPFPNNWDMSKRLGEYAEHADLWNTHTVMEMTHLIKPKSLTLFIDCGTEDFFYDVNCKLHEKLDYMNIPHRFLSMPGAHNWDYWKKSILYQLTFFNDFFNSSKAA
>NZ_CP049246.1|WP_103905385.1|3166720_3169006_-|TonB-dependent-receptor
MQVLPAHAQERLTISGYIKDAGTGENLIGAVLRIKDQNLSTYSNNYGFYSISILAGTYQLEVSYQGYRTAVEEMTLSENTRKNFELLSNENSIEEIVVSGKKENGNVSSAQMGNLKFSMEEMKNIPVIFGEKDVLKTIQLLPGVASGGEGSSSFFVRGGAGDQNLILLDEATVYNASHLLGFFSTFNSDAIKDASLYKGGIPAQYGGRISSVMDISMLDGNSKQFSMEGGIGLIASRLKLEGPIVKDRSSFMVSGRRTYADMFLKFSNDETAKKSKLYFYDLNMKMNYKLNDRNTIYLSGYFGKDDLGYGDLFSFDWGNATATVRWNSVINSKLFSNTSLIYSDFTYNVNVDNDNSAFTIASKIQNWNLKQDFSYYANNNSTIRFGVNLLHQQIKPASLDAIEGSEVNSIAVDDRQGIEAAAYVSHEWKPFERLSMIYGLRLNDFMVMGPGTFYEFDQDGEPTKESYYGSVVAKHYFNLEPRLSLSYLLNDNNSIKASYNRIAQNLHQLTNTTASLPTDQYVVSSLNIKPQIADQVALGYFRNFQNNTYELAVETYYKYMDNQIDFRNGADLQANKYLEGDLLYGIGRSYGVEFLVRKNKGKLTGWVGYTLARSERQFDQINNGDWFSARQDRTHDVSVVGVYQLTKKWALGATFVYNTGNAITFPSGKYQVDGETMFYYTERNGYRMPDYHRLDLSATYEPHKEKKRFQSSWAFGIYNAYNRKNAYIIDFRENEQNPNITEAYKIALFGIIPSVTWNFKF
>NZ_CP049246.1|WP_103905168.1|3165889_3166717_-|DUF4249-domain-containing-protein
MRLFKIILLCAVVFSFSSCEELIDVDLNSADPKIVIVADINNSGNVHEVFVSRTVNFDVDRPSDPVENAAVQVRSGAGQVYVFLHQGDGRYVNTNMQLGIAETYSLSVTVDGEEYKSETSMPEYVEVDSIGVTKENIFNETYYFVNLKFQDPPGQANYFKYTVSVNEEKFKFDSATSDKFNDGKLVTHQIGSGGNDEIQLGDKLVVRRQAITKPVYTYWSEYMMTNPGSAAPGNPTSNISNGALGYFSVANVRDYSIDIQDETVSEEIESESASQ
>NZ_CP049246.1|WP_103905159.1|3180758_3181067_-|hypothetical-protein
MNNSSKNELWGIVKPIVAYGSLALNLALIGSCLPFAYTNEKNEDAQMAFYKLWPFDYYVLAFIAIFLGIFSCIYFARAKGVWPKIWLVIQILLVHLFAWGLL
>NZ_CP049246.1|WP_103905158.1|3181384_3182236_+|ATP-phosphoribosyltransferase
MKNLKIAIQKSGRLNEKSVLLLKNCGLDFENYKSSLITTVSNFNLEILFLRDDDIPGYVEEGIADLGIVGENVIDETQAKVQYLQRLGFGRCTLKLAIPKDSSIDRLEDLNGKSIATSYPNILQNFLTEYKINADIQTISGSVEIAPGLGLSDAICDIVSTGGTLKSNGLKPFCDVRNSEAILIGREGLEENPIICELLQRIQSVLRAKETKYVVLNVEKKNLTQITELLHGVKSPTVVPLAEEGWVAVHTVISEDDFWDKINKLKAAGAQGIVVMPIEKIIM
>NZ_CP049246.1|WP_103905157.1|3182235_3183528_+|histidinol-dehydrogenase
MLNTYIYADLTPEKMADLLDRNTDPNHAIQDTVLSIIEDVKQHGDAALKSYAKQFDKVELEKLYLDSDDIDNLAMTISRDQMRALEIAFQNIHKFHQTQLKRERTVETMPGVKCWREVRPIEKVGLYIPGGSAVLPSTLLMLGVPARIAGCKEIVVCSPPQNNGKINGFVAYCLKLLKIDKIYLVGGAQAVAAMAFGTQSIPKVNKIFGPGNQFVTKAKGIIQGMTDVSIDMPAGPSEVLVIADETANPAYVAADLLAQAEHGIDSQAVLVTTSSQLADQVNQELKAQLDVLPRKELAAKAIENSYTVITENIQEAMDFSNRYAPEHLIIESDDWKPLINKVQNAGSVFLGHLTPESAGDYASGTNHTLPTSGYARSYSGVSVDSFVKKITFQHITEQGLEQIGSTVEILAELEGLQAHKNAVSIRKKKQ
>NZ_CP049246.1|WP_103905156.1|3184268_3185261_-|hypothetical-protein
MAEETKSTTPTTGTDQTDNSTPKTTAAAKKPATGTRTTTAAKASGSDSNVEAAASPVRARKSASPSGTAAKTAAGTAKSTPASGTAAAKTPAAKTTAAKAPARTASTATKSGTAAKSTTAASANKSTASAQKPAVKSTASTGAQTAGSTSAKPAASTATKSPSATAAKTASKPAAKTAARPAAKPAAKPASKQEATTAPEQKTTAPASVENTSTPESKLKKEASYKEEVPTKKKVKEDKKAVKENKKSDKKANAKKKVVEAKSEVKKDKEKARKADRKNDKKVVAKVKDTKAAKKSAKKDSKVMKKLKNAFTEIYNKIVGDDKDKKKRKK
>NZ_CP049246.1|WP_103905155.1|3186003_3187710_-|hypothetical-protein
MSLETKSKALKEIVSTYNTEWFLGDISFLMKNIGRAQDQLGKLSSPLRQLYYLAGLNVSSNPANGTDIQYDPEKWEQIVALLNEIEAEYHKLFFTENPEEITEEWKRMRQVAMPSFLSYFNQGPLNFEEQVVNWIKDLFFPMDDILQNDTGLITQDFIQFYENIDQLNQRNFQAFSTNKALLRPNWKEYTKVEVGVIDGVPDFIREMGEKDMHLYTFMADHGIMDRFYPEELVSETLTIEKVQKILHLLSTKREEKDFLYYTETKPGNPLYEKPIVSIDEKMYQVFEVKQVIHAIEILLEKVTTTTTENKTKYVDVKGKLLEKNIVELFSNFFGADFKLYQGYYVDGCEQDILFLWKKYAFIIEAKGYSLREPFRNPEKAFVRIKDDFDACIGYGYKQTRRVEEKFINQEPLKITDKNGNLIEEIDTTQIEEDFSIIVNLKTFGQIQCDLSALIQLEKDDDIFPWVVRLDDLEVFLLTLMARKQKPEKLVEFLLMRELLHGKLICTDELEVCGAFLNKKLNQKQINYADTIATTPDLADIFDEQYRKTMGFKNEKYLYEKQSGKFMFY
>NZ_CP049246.1|WP_103905154.1|3187736_3191792_-|hypothetical-protein
MSVIAALRGYRTQFLYSLHYILSSLSNDLIFRLEGEEDLDILDENGQLLYSIQLKNLGQPITLSGILSDHKTSFIKRFLAKYSEAIPILVSYGDISQELKNWEKHKDTISEKEKKTLKKYKITADEWKLVKSKTQFIEINEEKIADEIEKLIKSNFPEVDPIPTIGFLLNWLQFIAEKQQPITTKDFYSKIQDFAIYITERVAIYNQYGVVLKPLHKVSTENTDQMLLEKEFYNATLTRYEHILLGLDVNREKHLETINDELKENNTIILKGASGQGKTTLLYSYVHNYVNDWLSYELNIQQDPVTTQQSIQAIASISKKLEVPTIFVINVNPNSTDWLQIIKESAHLNHIRFLVAIRNEDWYKASAVGVEFEHKEIDLSLSQEEAKIIYTKLNERNKIIQFTDFEQAWIQIGDDAPLLEFVYSITQGNSLQNKLKQQIQQLRNESDQGCNPQIEFLRIVSLADSLGAKIDVSKLDSNVDYQFIIEKLENEYLVKKSLDRKYIQGLHLIRSQKLVEILFDEFTTYKEEYAYKCISLIDEKNLYLFLLQMFHLEILSPDQFIADLNSKVIIRNWSAYASILKSFIWLGSKSYVENNRKVIDECRTICGGAWTMFTDFMFGSNYDRNGMLDLLKVDDDRREKINDINRRLLPNQNVFNLATEAINQIDFPKEAPSTVFGWKSFGEALFWLKNIPNRKEKLSLIDDSKFESAFRNMDSKSLSKLMLGMYSYSVELDAIRKKYVDIFIEQIKKEFDVIHLSVDENEVNVHYIIDILKNDVERSTNDFIVGVLDIIRTALPDKKQFNSQGYGHRLQTLAVDYDDTHKTMPIENIPLEEWVNINSTIIKLYEYQLRPEDWNEYRNQLNQWEGIIKEKINEFNISFEQLFKGSVNYMPVVPIMQNMLFERSESIKEPKSITEPLGIYGGKKRGTINENEREQRNKKLQSKYELFFKSVSDFKGDIESFIQQSGGTLYSKAKLKTDEAHTHDENTERLSQINLYNAIEKLQIYNSQYNNILGNIDIKHHSKIETNTLFTTASIWKDFLNDNSKGERSAKRIFKLKSDFENKIIKDFKQVSKANSFSIRYINNKTTNDKPIIIIDGVSPFWMLMGYKEAYQIIQQTIDNPEYTSLKYLMLQFWFSNFYFIQTIQNKSLNNQWNEVRLYNIKDKLFEELSFINSISQPIEVKIIENLNIEGWSNLYPEFNDITKATEAYGKLLLLADHFYDLRLFDEIELMESDQEKLKQYIQRIGLELQQSFQAVLDSLVEWINMFPFDEDSYVNSDEEQEYFKAMINIKDHIFPEPKGDEEDYQLIMNMEIVSKWVERLKICTESWGIFILLLYGKYIDKFNSIDSSAR
>NZ_CP049246.1|WP_103905153.1|3191992_3192283_-|JAB-domain-containing-protein
MFQYKLDVIGYRKIADGGLDTVMVDIRLIMSSVLLCNATRIAVAHNHPSGTMRPSASDRSLTNKIIEAGKVLDIQLLDHIVMTTNSYYSFRDEGEF
>NZ_CP049246.1|WP_103905152.1|3192240_3192450_-|hypothetical-protein
MKKNFIANELKLSYHRNQKLSIDDFKCINNSKLMDRIFRMIWDLEEFEIRESFYALYFNTNWTLSDTVK
>NZ_CP049246.1|WP_103905151.1|3193019_3193919_-|helix-turn-helix-transcriptional-regulator
MEEIINFKSIREYNNFNNNETLHPLVSVVDLSKADPRKLSKLRYEFYTVFFKEIKCGDLRYGLKNYDYEEGTLIFLAPGQVIGENGTEFYQPQGTALVFHPELLYGTSLAREIANYTFFSYSASEALHLSEQERKVIMDCLNKIKHELVHSIDKHTKKLIVSNIELFLDYCQRFYDRQFITRENVNKGILEKFEEILNTYFQSEEPQQNGLPTVAYFADQLFLSANYFGDLVKKETGKTAQEYIQNKLIEIAKEKIYDSNKTINEIAFELGFKYPQHFSRLFKNRVGYTPNEYRNVNLN
>NZ_CP049246.1|WP_103905150.1|3194135_3195119_+|aldo/keto-reductase
MENRILGNSGLEVSALGLGCMGLSFGYGPATDQKEAIKLIRTAFESGISFFDTAECYGPFTNETLLGEALEPFRNEVVIATKFGFEDGDSKKGLDSSPSRIRKVAESSLQRLRTDRIDLFYQHRTDPNIPIEEVAGTIRDLIAEGKIKHWGLSEAGTETIRRAHAEQPLAALQSEYSLFCREPEKEIIPTLEELGIGFVPFSPLGKGFLTGAINETTKFDPTDFRNIVPRFSEENRKANQALVDLLKTIASEKEGTPAQVALAWLLAQKPWIAPIPGTTKLHRLKENIGAITIELDAKDLQQINLAASAITIHGERYPAALQNRVGK

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Crispr_ID: NZ_CP049246_13

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP049246_13

3518196-3518327

Orphan

Consensus_repeat	Method
TGTTTTAGTATTGAGATGTGAGATATGAGATGTGAGATAGAAAACGT	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP049246_13

>merge|NZ_CP049246|13|3518196-3518327|CRISPRCasFinder
TGTTTTAGTATTGAGATGTGAGATATGAGATGTGAGATAGAAAACGTGCTATTTGTGTTTCTGGCCACATTTATCAGCTACATCTTGTTTTAGTATTGAGATGTGAGATGTGAGATGTGAGATAGAAAACGT

>NZ_CP049246|13|12|3518196-3518327|CRISPRCasFinder
TGTTTTAGTATTGAGATGTGAGATATGAGATGTGAGATAGAAAACGT	GCTATTTGTGTTTCTGGCCACATTTATCAGCTACATCT
TGTTTTAGTATTGAGATGTGAGATGTGAGATGTGAGATAGAAAACGT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP049246.1\|WP_103906096.1\|3523606_3524902_+\|DUF389-domain-containing-protein	unknown	unknown	gnl\|CDD\|377221
NZ_CP049246.1\|WP_103906082.1\|3507748_3508474_+\|HesA/MoeB/ThiF-family-protein	unknown	unknown	gnl\|CDD\|238386
NZ_CP049246.1\|WP_103906087.1\|3514549_3515452_-\|helix-turn-helix-transcriptional-regulator	unknown	unknown	gnl\|CDD\|225117
NZ_CP049246.1\|WP_103906186.1\|3512252_3512828_-\|HupE/UreJ-family-protein	unknown	unknown	gnl\|CDD\|379373
NZ_CP049246.1\|WP_103906085.1\|3509901_3512256_-\|M1-family-metallopeptidase	unknown	unknown	gnl\|CDD\|341067
NZ_CP049246.1\|WP_103906086.1\|3512938_3513445_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP049246.1\|WP_103906097.1\|3524974_3526144_-\|Na+/H+-antiporter-NhaA	unknown	unknown	gnl\|CDD\|377746
NZ_CP049246.1\|WP_103906083.1\|3508559_3509213_+\|TetR/AcrR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224228
NZ_CP049246.1\|WP_103906093.1\|3520933_3521269_-\|L-rhamnose-mutarotase	unknown	unknown	gnl\|CDD\|377501
NZ_CP049246.1\|WP_103906100.1\|3529626_3530094_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP049246.1\|WP_103906095.1\|3522665_3523505_+\|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|380381
NZ_CP049246.1\|WP_103906090.1\|3517335_3518193_-\|fumarylacetoacetate-hydrolase-family-protein	unknown	unknown	gnl\|CDD\|223257
NZ_CP049246.1\|WP_103906091.1\|3518464_3519229_-\|glucose-1-dehydrogenase	unknown	unknown	gnl\|CDD\|235506
NZ_CP049246.1\|WP_103906089.1\|3516493_3517324_-\|amidohydrolase-family-protein	unknown	unknown	gnl\|CDD\|226145
NZ_CP049246.1\|WP_103906088.1\|3515696_3516488_-\|SDR-family-oxidoreductase	unknown	unknown	gnl\|CDD\|181508
NZ_CP049246.1\|WP_103906099.1\|3527932_3529408_-\|IMP-dehydrogenase	unknown	unknown	gnl\|CDD\|376340
NZ_CP049246.1\|WP_103906098.1\|3526150_3527581_-\|alanine:cation-symporter-family-protein	unknown	unknown	gnl\|CDD\|376500
NZ_CP049246.1\|WP_103906094.1\|3521282_3522533_-\|L-fucose:H+-symporter-permease	unknown	unknown	gnl\|CDD\|340952
NZ_CP049246.1\|WP_103906092.1\|3519263_3520928_-\|altronate-dehydratase	unknown	unknown	gnl\|CDD\|377287
NZ_CP049246.1\|WP_160003708.1\|3509305_3509860_+\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|224584

Protein	Function_ID	Function_description	E-value
NZ_CP049246.1\|WP_103906096.1\|3523606_3524902_+\|DUF389-domain-containing-protein	gnl\|CDD\|377221	pfam04087, DUF389, Domain of unknown function (DUF389). Family of hypothetical bacterial proteins with an undetermined function.	1.54438e-61
NZ_CP049246.1\|WP_103906087.1\|3514549_3515452_-\|helix-turn-helix-transcriptional-regulator	gnl\|CDD\|225117	COG2207, AraC, AraC-type DNA-binding domain-containing proteins [Transcription].	1.68102e-23
NZ_CP049246.1\|WP_103906186.1\|3512252_3512828_-\|HupE/UreJ-family-protein	gnl\|CDD\|379373	pfam13795, HupE_UreJ_2, HupE / UreJ protein. These proteins contain many conserved histidines that may be involved in nickel binding.	1.07845e-56
NZ_CP049246.1\|WP_103906085.1\|3509901_3512256_-\|M1-family-metallopeptidase	gnl\|CDD\|341067	cd09604, M1_APN_like, Peptidase M1 family similar to aminopeptidase N catalytic domain. This family contains bacterial M1 peptidases with smilarity to the catalytic domain of aminopeptidase N (APN; CD13; alanyl aminopeptidase; EC 3.4.11.2), a type II integral membrane protease belonging to the M1 gluzincin family. APN preferentially cleaves neutral amino acids from the N-terminus of oligopeptides and, in higher eukaryotes, is present in a variety of human tissues and cell types (leukocyte, fibroblast, endothelial and epithelial cells). APN expression is dysregulated in inflammatory diseases such as chronic pain, rheumatoid arthritis, multiple sclerosis, systemic sclerosis, systemic lupus erythematosus, polymyositis/dermatomyosytis and pulmonary sarcoidosis, and is enhanced in tumor cells such as melanoma, renal, prostate, pancreas, colon, gastric and thyroid cancers. It is predominantly expressed on stem cells and on cells of the granulocytic and monocytic lineages at distinct stages of differentiation, thus considered a marker of differentiation. Thus, APN inhibition may lead to the development of anti-cancer and anti-inflammatory drugs. APNs are also present in many pathogenic bacteria and represent potential drug targets. Some APNs have been used commercially, such as one from Lactococcus lactis used in the food industry. APN also serves as a receptor for coronaviruses, although the virus receptor interaction site seems to be distinct from the enzymatic site and aminopeptidase activity is not necessary for viral infection. APNs have also been extensively studied as putative Cry toxin receptors. Cry1 proteins are pore-forming toxins that bind to the midgut epithelial cell membrane of susceptible insect larvae, causing extensive damage. Several different toxins, including Cry1Aa, Cry1Ab, Cry1Ac, Cry1Ba, Cry1Ca and Cry1Fa, have been shown to bind to APNs; however, a direct role of APN in cytotoxicity has been yet to be firmly established.	2.92978e-136
NZ_CP049246.1\|WP_103906083.1\|3508559_3509213_+\|TetR/AcrR-family-transcriptional-regulator	gnl\|CDD\|224228	COG1309, AcrR, Transcriptional regulator [Transcription].	4.85355e-09
NZ_CP049246.1\|WP_103906097.1\|3524974_3526144_-\|Na+/H+-antiporter-NhaA	gnl\|CDD\|377746	pfam06965, Na_H_antiport_1, Na+/H+ antiporter 1. This family contains a number of bacterial Na+/H+ antiporter 1 proteins. These are integral membrane proteins that catalyze the exchange of H+ for Na+ in a manner that is highly dependent on the pH.	0
NZ_CP049246.1\|WP_103906082.1\|3507748_3508474_+\|HesA/MoeB/ThiF-family-protein	gnl\|CDD\|238386	cd00757, ThiF_MoeB_HesA_family, ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis family. The common reaction mechanism catalyzed by MoeB and ThiF, like other E1 enzymes, begins with a nucleophilic attack of the C-terminal carboxylate of MoaD and ThiS, respectively, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of MoaD and ThiS. MoeB, as the MPT synthase (MoaE/MoaD complex) sulfurase, is involved in the biosynthesis of the molybdenum cofactor, a derivative of the tricyclic pterin, molybdopterin (MPT). ThiF catalyzes the adenylation of ThiS, as part of the biosynthesis pathway of thiamin pyrophosphate (vitamin B1). .	6.00268e-105
NZ_CP049246.1\|WP_103906093.1\|3520933_3521269_-\|L-rhamnose-mutarotase	gnl\|CDD\|377501	pfam05336, rhaM, L-rhamnose mutarotase. This family contains L-rhamnose mutarotase which is a glycosyl hydrolase that converts the monosaccharide L-rhamnopyranose from the alpha to the beta stereoisomer. In Escherichia coli this enzyme is the product of the rhaM gene (also known as yiiL). The tertiary structure has been solved, in complex with L-rhamnose, and the catalytic mechanism determined. His22 is the proton donor. The enzyme naturally exists as a dimer.	2.29283e-31
NZ_CP049246.1\|WP_103906095.1\|3522665_3523505_+\|helix-turn-helix-domain-containing-protein	gnl\|CDD\|380381	cd06976, cupin_MtlR-like_N, AraC/XylS family transcriptional regulators similar to MtlR, N-terminal cupin domain. MtlR is a Pseudomonas fluorescens protein that acts as a transcriptional regulator of the mannitol utilization genes. It has an N-terminal cupin domain (represented by this alignment) and a C-terminal AraC/XylS family helix-turn-helix (HTH) DNA-binding domain. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.	2.71775e-28
NZ_CP049246.1\|WP_103906090.1\|3517335_3518193_-\|fumarylacetoacetate-hydrolase-family-protein	gnl\|CDD\|223257	COG0179, MhpD, 2-keto-4-pentenoate hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase (catechol pathway) [Secondary metabolites biosynthesis, transport, and catabolism].	7.70371e-100
NZ_CP049246.1\|WP_103906091.1\|3518464_3519229_-\|glucose-1-dehydrogenase	gnl\|CDD\|235506	PRK05565, fabG, 3-ketoacyl-(acyl-carrier-protein) reductase; Provisional.	7.52534e-77
NZ_CP049246.1\|WP_103906089.1\|3516493_3517324_-\|amidohydrolase-family-protein	gnl\|CDD\|226145	COG3618, COG3618, Predicted metal-dependent hydrolase of the TIM-barrel fold [General function prediction only].	1.14666e-44
NZ_CP049246.1\|WP_103906088.1\|3515696_3516488_-\|SDR-family-oxidoreductase	gnl\|CDD\|181508	PRK08628, PRK08628, SDR family oxidoreductase.	6.35141e-164
NZ_CP049246.1\|WP_103906099.1\|3527932_3529408_-\|IMP-dehydrogenase	gnl\|CDD\|376340	pfam00478, IMPDH, IMP dehydrogenase / GMP reductase domain. This family is involved in biosynthesis of guanosine nucleotide. Members of this family contain a TIM barrel structure. In the inosine monophosphate dehydrogenases 2 CBS domains pfam00571 are inserted in the TIM barrel. This family is a member of the common phosphate binding site TIM barrel family.	0
NZ_CP049246.1\|WP_103906098.1\|3526150_3527581_-\|alanine:cation-symporter-family-protein	gnl\|CDD\|376500	pfam01235, Na_Ala_symp, Sodium:alanine symporter family.	0
NZ_CP049246.1\|WP_103906094.1\|3521282_3522533_-\|L-fucose:H+-symporter-permease	gnl\|CDD\|340952	cd17394, MFS_FucP_like, Fucose permease and similar proteins of the Major Facilitator Superfamily of transporters. This subfamily is composed of L-fucose permease (also called L-fucose-proton symporter) and similar proteins such as glucose/galactose transporter and N-acetyl glucosamine transporter NagP. L-fucose permease facilitates the uptake of L-fucose across the boundary membrane with the concomitant transport of protons into the cell; it can also transport L-galactose and D-arabinose. Glucose/galactose transporter functions in the uptake of of glucose and galactose. The FucP-like subfamily belongs to the bacterial fucose permease, eukaryotic Major facilitator superfamily domain-containing protein 4 (FucP/MFSD4) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	5.55651e-133
NZ_CP049246.1\|WP_103906092.1\|3519263_3520928_-\|altronate-dehydratase	gnl\|CDD\|377287	pfam04295, GD_AH_C, D-galactarate dehydratase / Altronate hydrolase, C-terminus. Family members include the C termini of D-galactarate dehydratase (EC:4.2.1.42) which is thought to catalyze the reaction D-galactarate = 5-keto-4-deoxy-D-glucarate + H2O, and altronate hydrolase (altronic acid hydratase, EC:4.2.1.7), which catalyzes D-altronate = 2-keto-2-deoxygluconate + H2O. As purified, both enzymes are catalytically inactive in the absence of added Fe2+, Mn2+, and beta-mercaptoethanol. Synergistic activation of altronate hydrolase activity is seen in the presence of both iron and manganese ions, suggesting that the enzyme may have two ion binding sites. Mn2+ appears to be part of the enzyme active centre, but the function of the single bound Fe2+ ion is unknown. The hydratase has no Fe-S core.	0
NZ_CP049246.1\|WP_160003708.1\|3509305_3509860_+\|GNAT-family-N-acetyltransferase	gnl\|CDD\|224584	COG1670, RimL, Acetyltransferases, including N-acetylases of ribosomal proteins [Translation, ribosomal structure and biogenesis].	3.17257e-27

>NZ_CP049246.1|WP_103906090.1|3517335_3518193_-|fumarylacetoacetate-hydrolase-family-protein
MKLIRFGEPGKEKIGVQLDGKNYDVSAFGGDYNEEFFAESGLARLEEFVKANEGKLIEIPAGTRLGAPFTRPSKIVCIGLNYKDHAAETGAQIPVEPVIFMKASTALVGPNDNVVIPKNSVKTDWEVEFCIVIGKKASYVDEANALDYVAGYVLHNDVSEREFQIERGGTWDKGKGCDTFAPMGPFMATADEIPDVNNVRLWLKVNGETYQDGNTSNLIFNIPFVVSYVSQFMTLLPGDVISTGTPAGVGLGFNPPIYLKPGDVIELGADYLGEQRQEVVAYKPQ
>NZ_CP049246.1|WP_103906089.1|3516493_3517324_-|amidohydrolase-family-protein
MRIDAHQHFWLFDQERDAWITAAMERIQRNFLPNDISMTLKENGFDGVVAVQASQSLQENRFLLELAQVYKLIKGIVGWVDLRSPEVEQQLAQFADQDLIKGYRHVVEGEEDPDFLHRDEFLRGIAALTEHGYTYDLLIRPWHYESTLKCVAANPQQAFMLDHIAKPPIKTQEFSAWAAFIEKLASFSNVHCKVSGLGTEADWKHWKLDHFTEYLEHVFGCFGKGRLVFGSDWPVCLLAGEYSDSLNIVEHHLRDFSSEELAGFWGDNAVKFYGLK
>NZ_CP049246.1|WP_103906088.1|3515696_3516488_-|SDR-family-oxidoreductase
MNLNLTDKIILVTGGAKGIGKGIVESLAREDAIPVIIGRKQADNLRVQAEIEEKGGKAFSVAAELSKPDECRKAVDAVLAEFGRIDGLVNNAGLNDGIGLEHGSYEGFVEALHNTLIHYYLMAQYCLPELKKNKGAILNISSKTAETGQGGTSGYAAANGGRNALTREWAVELLPYGIRVNSVIVAECMTPQYEKWIKTLPNPEETLDKITSRIPLENRMTTVEEIADMSVFLLSDRSSHTTGQLIHVDGGYVHLDRALINDQ
>NZ_CP049246.1|WP_103906087.1|3514549_3515452_-|helix-turn-helix-transcriptional-regulator
MEALKTKEARYPIEFTAPAFGAGSFYIQEDLRDEFYSHYHRHKEIQISYILKGRGSVVIGNLIQPFFENEIYILKANDPHVFIKEGNPEDKVHVVHVFVAFDKLAPLFNLQELQPMQDFFSTMNSSKKVIQQHAGKIKHIFASLMKEEGMAKLMQVLKIFDFLLAHEQDMISLYSGLPGSNFNDKVGVRINDVLRYSLENYNREITIDEVAKLIHMTPSAFCKYFKKHTMKTYVTFLNEIRIEKACQLLINRSTENISEVAYQCGFNTVVHFNRVFKHILRSSPSEFIHKHSAGMAHVVN
>NZ_CP049246.1|WP_103906086.1|3512938_3513445_+|hypothetical-protein
MNIRKTAFCLTVLGLLLSIAAWAHPFYVSITSIDYTVEKKQIEVSCRIFQDDLEKAIKNQLKVGVDVIKPKDREATNRAIATYIKQNFRITANGKPKDLTFLGYEIDNDVAWCYFKAPQEENIKELKVINQLLYQDFKTQANILHVTVNKKRKSTKLDNPKRSAEFVF
>NZ_CP049246.1|WP_103906186.1|3512252_3512828_-|HupE/UreJ-family-protein
MSDFSIYFQLGWQHILDLNGYDHILFVLVLCCSYTLKDWKRILWLVTAFTVGHSITLALAAFQIVRVDMSWVEFLIPVTILATALYNLPKRRKQRNAAVLYGMTLFFGLIHGLGFSNYLQSLLGQEASIVLPLLSFNLGLEFGQLIIVFFLILLSELMLKIFSVSNRDWSFFLSSAVIGISFIMALERIPL
>NZ_CP049246.1|WP_103906085.1|3509901_3512256_-|M1-family-metallopeptidase
MKKYSHLIKSFGTGLLMATVAITHAQNNPGSNHGNKFEQLGSLLSDPNIFRTASGAPGSMYWQQKADYVIDVEIDEVNQVLKGSETITYTNNSPDPLQYLWVQLDENEHADNAESKKFDQSKLREKMSLEQLKAMVPEKKGYGVNIHKVTDGSGKALDYTINYTMMRIDLPVSLKPGAKMTLKIDWDYKITDRMVENGRGGYEHFAKDDNYLYTITQWFPRMAVYSDFQGWQNKQFTGRGEFALVFGDYKVNITVPADHIVGATGECQNYGQVLNATQLSRWKQAQTAKEPIEIVTLDDAKKAMGQKSSAKKTWVYSAKNVRDFAFVSSRRLVWDAMKVNEGIEGNQPMAMSYYGPEAYPLYRRYSTKVVAHTLKTYSKFSIPYPYPVAISVEAANGMEYPMICFNYGRADEDGTYSEAVKYGMIGVIIHEVGHNFFPMIVNSDERQWTWMDEGLNTFLQFLTEQEWDKDFPSRRGPAHRIVDYMQLPKDQLEPIMTNSENIVQFGPNAYAKPATALNILRETIMGRELFDYAFKEYARRWEFKHPTPADFFRTMEDASAVDLDWFWRGWFFGTDPVEISLEHVTQYRMSGSDPKKTQAERKAAFDKDLNTITRQRNLEENMAFLVDKDTSLLDFYNKWDRFAVRPADEASYQQFYNGLSEKEKDIFNGKTSFYELNFKNNGGLVMPLIIQWTFTDGSTEIDRIPAYIWRMDEHEVTKVFAKTKQVASIQLDPFRETADIDEGNNSWPRSAQPSRFEIFQNNGRAARGQSTEGNPMKAAKQQQR
>NZ_CP049246.1|WP_160003708.1|3509305_3509860_+|GNAT-family-N-acetyltransferase
MNRKIPIDKDLSLKAVVASDAIKMYKIIDSQRKYLGEWLPFVQFTNKLDDSKGFIEIAIKHREMKRDYVYKICYKDKMIGLIGTKEIDYLNRNTEIGYWLSEEHQGKGFMTKSVHALIQALFSEVKLERIQICCAVGNEKSIAIPNRLGFKQEGIKRNGEWAGNLQFRDLIVFSLLRSDQQGTT
>NZ_CP049246.1|WP_103906083.1|3508559_3509213_+|TetR/AcrR-family-transcriptional-regulator
MKEGKSASPKTRKVTSGPLREKERTMNRIVNAVGKVLKKKGYPGLTIANIALEAKVDRKLIYTYFGNLDNLVDLFISKRDYWKTKAKTSIDKLLAQDHISQEEMESLLIGQFNSVMSDATLQRILQWELSQHSESLRRLADEREVVGEQLIQKLEKNITNSDSDIRALLALQTAGLYYLALHANSNGSTFCGLDLHKEEDRERIFQALKRLLKAEIG
>NZ_CP049246.1|WP_103906082.1|3507748_3508474_+|HesA/MoeB/ThiF-family-protein
MQEEQMHRDTKFLRYSRQIFMEEVSILGQKNIAAAKILIVGAGGLGSPIIQYLAAAGVGTLGIVDFDDLELHNLNRQVIHSEQGIGKNKANNAKVFVENLNSSIKVIPYTVRLDAETIPEIAAGYDLIIDGSDNFETRYLVNDFAVQAGIPLVYGSIFAFEGQVAVFNLKGSKHLRDLFPEPPHPEDIQTCDQYGVLGPLPGVVGSLMAMMALKICIGMEVKINQLTLINLQDWTFTTVGY
>NZ_CP049246.1|WP_103906091.1|3518464_3519229_-|glucose-1-dehydrogenase
MSKLEGKVAVVTGGGSGIGRAISTLFAQEGAWVHILDLNPQGAEEVQQEIEDLGGKCSVHTCNVSDQEEVLAVVASIGRIDVLVNNAGIAHVGDVEHCSPADFDKVFQVNVKGAYNALFAVIPVMKANGGGAILNLASIAAWVGITDRFAYSMSKGAIFAMSLSVARDYMQDNIRCNSISPARVHTPFVDGFIAKNYPGKETEMFEKLSQSQPIGRMAQPAEIAKLALFLCSDDAGFITGNDYPIDGGFIKLNN
>NZ_CP049246.1|WP_103906092.1|3519263_3520928_-|altronate-dehydratase
MEKERLDYLQIHPKDNVLVALRDLPQGQVVNFQGATFPLRRAVAAKHKFTITAMPKDSEIYMYGVLVGKVNADLEQGELLDVDNLRHAADDFKLGNRKLEWVQPDISAFKDKTFNGFHRSNGTVGTANYWLVIPLVFCENRNVLTLKSALEEKLGYRVESKDYSNEVDELIARYQAGASTEELLAVDLSASVANAKANRLFPQVDGVKFLNHDMGCGGTRMDSDALCGLLAGYITHPNVAGATVLSLGCQHAQASILRAEIQRRDPHFNKPLYIFEQQFEGTEQELMQKAIKATFAGLAEANTLQRKPAGLDKLCIGLECGGSDGFSGISANPALGYLSDMMVTLGGSVILAEFPELCGVEQELSDRCIDEPTAEKFIHLMRTYNAKAEADGSGFYMNPSPGNIRDGLITDAIKSAGAAKKGGNSPVAAVVDYPELANGPGLNLLCTPGNDVESTTAEVAAGANVVLFTTGLGTPTGNPISPVIKVASNTKVFEKMNDAIDLNCGTIIDGEETIEEAAHRILDYVIAVASGEVQAKAVKLGQDDFIPWRRGVSL
>NZ_CP049246.1|WP_103906093.1|3520933_3521269_-|L-rhamnose-mutarotase
MGNRKCAMALDLVDDAGLIAEYEKYHREIPQAIHNSITAAGVVHMEIFRFANRLFMLMEVDDSFSFERKAEMDAANADVQAWEALMWKFQQAIPGAKPGEKWVFMDKIFEL
>NZ_CP049246.1|WP_103906094.1|3521282_3522533_-|L-fucose:H+-symporter-permease
MTKTRNTVAIILITSLFFFWGFIHNLDPILIAHLRSAFSLTHLQASLVDSAVFVAYLFMGIPAGIIMKKYGYKVGILVGLILFAVGCFLFVPAANTMSYAFFLSALFIVACGITILETAANPYMTVLGDPNTATQRLNFAQSFNGLAAFVAPIVGGALILSEEPLTAEQVAALSDADRLAYIQAETAMVKGPYVVLGLIILAVALLFFFIKLPEFRDKEEGSGGFLKAFRHKNVAWAVVAQFFYVGAQVCILSFLIVFAVEVSGIEAKDAKVYAGVAGLLFMLGRFVGTYLMRSIAPSRLLFIFALIATALTFVCIFGSGKTTLYAMVAVAFFMSIMFPTIFAIGVEGIGADTKSASSLIIMSIVGGAIIPPVFGYISDFTGHMQYGYFAVVVCFLVVALFAFQQKAKLKEMNSVA
>NZ_CP049246.1|WP_103906095.1|3522665_3523505_+|helix-turn-helix-domain-containing-protein
MIIKQLAVPKSGDHSFQFRQDLYPRHQSIWHYHDEIELIHVIRGSGTVFIGDRIKGFQAGNTVMIPSHVPHYWLFDEDLPGEEDPIDCIVIHFLKDFGSSNFLKAPELSGVRTLLDRSTRGMFIEDAERLTERFKAVLSNTGLEKLFSLFSLLQRLPAEEPSYLISENYAILNQSDDQARMNNLMSYIRENYKHKIKLLDLAKVADMTENSFCRYFKQRTGKTPVQFINELRIAHACFQLRNKPMPLKEICYDSGFNNFVSFHKTFKSITGTTPTQFRE
>NZ_CP049246.1|WP_103906096.1|3523606_3524902_+|DUF389-domain-containing-protein
MNKLYRFLNLHFGEEAKDKVLENVTASISFRGANVWILACAIAVASVGLNVNSTAVIIGAMLISPLMGPIVGAGFALGVYDFDLLKKSIKNLAIATVVSLFVSFLYFLLSPFKEAQSELLARTAPNIYDVLIAFFGGLAGVIALTRVEKGNPIPGVAIATALMPPLCTAGYGLAIGNFSYFGGALYLYTINCFFICISTFLIVKLLKYPKVKFVDKAREKKITRTITTLILVMLIPSFYLAYQLLQEKKYSQNVDNFIQQEFTNKGYTLIYENTHFNSRPKKIEVAFLDKKFSNAEKEDLNQKLATYQIEGTELVIRQDSTDLKRDILAEISKQSRNVSESDVTIQNLRKELASYTFSDQELISEINILFPELAPYSIGKQLVVVNPDSSFHQNIVTYTSGEAIPAAELSKLKTWLETKLNSKNVRIIRAQ
>NZ_CP049246.1|WP_103906097.1|3524974_3526144_-|Na+/H+-antiporter-NhaA
MANLINLNVFKDFFKSSNAGGILLFICVIISMIIANTPLAPALQNFLDSRWGYESESIHLNYSILLWINDGLMAIFFLLVGLEIKREIVEGELSSPKKASLPILCAIGGAAVPALVYLSLNAGQETASGWGIPMATDIAFALAVINLLGNRVPSSLKIFLAALAIVDDLIAILVIAFFYSSGIEVSYLLYALGGMVILILMNRFNVLNPYLYLIPGVFIWYFIHHSGIHATIAGVLVAMTIPTNDTDVESPLERLEHALVKPVNFIIIPLFAFANTNITLENEMLAGLTAPLGLGITLGLLIGKPVGILLTSYICTKLKLSSLPEGSTWRHILGVGLLAGIGFTMSIFIAILSFKDPLFVSEAKLSILITSLLAGVIGYFFLNSKKQYN
>NZ_CP049246.1|WP_103906098.1|3526150_3527581_-|alanine:cation-symporter-family-protein
MQEIIDKIYSIIWSDALVYLCLLAGVYFSIRFKFPQIMYLREMIRLLFKGGSSEKGISSFQAFSLAISGRVGTGNIAGVATAIGMGGPGAVFWMWIIAFLGSSSAIIEATLGQLYKEVKDGQYRGGPAYYILKGLKSKVFAWTFAIVTIISTGFLLPNVQSNSIAIAMKSAFDIPAFAVGIALIILLGFIIIGGVKRISKVAEFVVPFMAGIYILMAIIIIGMNIQQVPAVFKLIFQSAFSIDATFGGIVGAAISWGVKRGIYSNEAGQGTAPHAAAAAEVSHPIKQGLVQGFSVYVDTLFVCTATALMILFTGQYNVANPTGGFLVENLPQVEAGPEFTQYAVSQHFPGFGSAFIAIALMFFAFTTIMAYYYIAETNVSFIAKQKNRKVLIWVLRVMILGSVYMGCISSAKMAWDLGDIGVGMMAWLNLIAIILLHNKVLRLFKDYNTQLKQGIDPVYINKDLPSGDIWNKKTSI
>NZ_CP049246.1|WP_103906099.1|3527932_3529408_-|IMP-dehydrogenase
MQLDPQKFVQEGLTYDDVLLIPAYSEILPRDVDTSTYLTKKIKLNIPLVSAAMDTVTGADLAIAIAQAGGIGMLHKNMTIAEQAAEVRKVKRSESGMIQDPVTLLENATVGDAFQIMKEHKIGGIPVINLENKLVGIVTNRDLRFQKDMARPISELMTKTNLVVAPEGTDLIKAEEILQNHKIEKLPVVDTNGILKGLITFKDIQKYKHYPNAAKDEHGRLLVGAAVGVTHDTLDRVDALVKAGVDVITIDTAHGHSLGVINKLKEVKAAYPDLQVIVGNIATGDAAKMLADAGADAVKVGIGPGSICTTRIIAGVGVPQLYAVYEVAKALKGTGVPLIADGGIKQTGDIAKAIAAGANTIMAGSLFAGVEEAPGETILLEGRKFKSYRGMGSVEAMEKGSKDRYFQDVEDDIKKLVPEGIVGRVPYKGTLAEVVYQYIGGLRASMGYCGAATIEKLQEAKFVRITGAGLRESHPHNIQITKEAPNYNSRG
>NZ_CP049246.1|WP_103906100.1|3529626_3530094_+|hypothetical-protein
MKKTLLSLAAAAALVFGFNEAKAQTPYKTAIGLAIDLGDGATLFGPQIKHSFGGANAGQAQVLFGDNFTAIGADYSYNQQFAGTNGLGWYVGVGPQIGFGGDLTWFSIRPQAGLEYKIPSAPIAFHFDWKPNWNLSHDTDFNAARFSLGFKFTLR

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Crispr_ID: NZ_CP049246_14

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP049246_14

3990853-3990957

Orphan

Consensus_repeat	Method
TCACCCCCACTGTCTCACATCTCACATCTCAAATCT	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP049246_14

>merge|NZ_CP049246|14|3990853-3990957|CRISPRCasFinder
TCACCCCCACTGTCTCACATCTCACATCTCAAATCTAATCCTCATATTATTCCTTTCCAGCGTCCAATTTCACCCCCACTGTCTCACATCTCACATCTCAAATCT

>NZ_CP049246|14|13|3990853-3990957|CRISPRCasFinder
TCACCCCCACTGTCTCACATCTCACATCTCAAATCT	AATCCTCATATTATTCCTTTCCAGCGTCCAATT
TCACCCCCACTGTCTCACATCTCACATCTCAAATCT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP049246.1\|WP_103905860.1\|3992421_3992976_+\|NifU-family-protein	unknown	unknown	gnl\|CDD\|378032
NZ_CP049246.1\|WP_103905855.1\|3984351_3985962_+\|CTP-synthase	unknown	unknown	gnl\|CDD\|235437
NZ_CP049246.1\|WP_146060599.1\|3995781_3996720_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP049246.1\|WP_103905854.1\|3983080_3984070_-\|aldo/keto-reductase	unknown	unknown	gnl\|CDD\|381369
NZ_CP049246.1\|WP_103905859.1\|3990999_3992349_+\|adenylosuccinate-lyase	unknown	unknown	gnl\|CDD\|236452
NZ_CP049246.1\|WP_103905861.1\|3993337_3994186_+\|transketolase	unknown	unknown	gnl\|CDD\|238970
NZ_CP049246.1\|WP_103905857.1\|3988722_3990072_-\|acyl-CoA-dehydrogenase	unknown	unknown	gnl\|CDD\|173840
NZ_CP049246.1\|WP_103905863.1\|3995201_3995747_+\|RNA-polymerase-sigma-factor	unknown	unknown	gnl\|CDD\|224511
NZ_CP049246.1\|WP_103905866.1\|3997203_3998391_+\|aspartate-aminotransferase-family-protein	unknown	unknown	gnl\|CDD\|99735
NZ_CP049246.1\|WP_103905856.1\|3985999_3987811_+\|membrane-protein-insertase-YidC	unknown	unknown	gnl\|CDD\|234942
NZ_CP049246.1\|WP_103905853.1\|3982658_3983003_+\|50S-ribosomal-protein-L19	unknown	unknown	gnl\|CDD\|235418
NZ_CP049246.1\|WP_103905868.1\|3999288_4000473_-\|class-I-SAM-dependent-rRNA-methyltransferase	unknown	unknown	gnl\|CDD\|224017
NZ_CP049246.1\|WP_103905850.1\|3977221_3979627_+\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|369481
NZ_CP049246.1\|WP_103905849.1\|3976076_3977174_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP049246.1\|WP_103905867.1\|3998433_3999189_+\|SGNH/GDSL-hydrolase-family-protein	unknown	unknown	gnl\|CDD\|238872
NZ_CP049246.1\|WP_103905862.1\|3994242_3995196_+\|transketolase-family-protein	unknown	unknown	gnl\|CDD\|226467
NZ_CP049246.1\|WP_103905852.1\|3980633_3981164_-\|HXXEE-domain-containing-protein	unknown	unknown	gnl\|CDD\|379370
NZ_CP049246.1\|WP_103905930.1\|3981302_3981842_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP049246.1\|WP_103905858.1\|3990309_3990528_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP049246.1\|WP_103905865.1\|3996719_3997148_+\|hypothetical-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_CP049246.1\|WP_103905868.1\|3999288_4000473_-\|class-I-SAM-dependent-rRNA-methyltransferase	gnl\|CDD\|224017	COG1092, COG1092, Predicted SAM-dependent methyltransferases [General function prediction only].	4.6503e-135
NZ_CP049246.1\|WP_103905855.1\|3984351_3985962_+\|CTP-synthase	gnl\|CDD\|235437	PRK05380, pyrG, CTP synthetase; Validated.	0
NZ_CP049246.1\|WP_103905866.1\|3997203_3998391_+\|aspartate-aminotransferase-family-protein	gnl\|CDD\|99735	cd00610, OAT_like, Acetyl ornithine aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to ornithine aminotransferase, acetylornithine aminotransferase, alanine-glyoxylate aminotransferase, dialkylglycine decarboxylase, 4-aminobutyrate aminotransferase, beta-alanine-pyruvate aminotransferase, adenosylmethionine-8-amino-7-oxononanoate aminotransferase, and glutamate-1-semialdehyde 2,1-aminomutase. All the enzymes belonging to this family act on basic amino acids and their derivatives are involved in transamination or decarboxylation.	1.07107e-142
NZ_CP049246.1\|WP_103905857.1\|3988722_3990072_-\|acyl-CoA-dehydrogenase	gnl\|CDD\|173840	cd01151, GCD, Glutaryl-CoA dehydrogenase. Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, which catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and carbon dioxide in the catabolism of lysine, hydroxylysine, and tryptophan. It uses electron transfer flavoprotein (ETF) as an electron acceptor. GCD is a homotetramer. GCD deficiency leads to a severe neurological disorder in humans.	4.51454e-161
NZ_CP049246.1\|WP_103905853.1\|3982658_3983003_+\|50S-ribosomal-protein-L19	gnl\|CDD\|235418	PRK05338, rplS, 50S ribosomal protein L19; Provisional.	4.36171e-59
NZ_CP049246.1\|WP_103905861.1\|3993337_3994186_+\|transketolase	gnl\|CDD\|238970	cd02012, TPP_TK, Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK catalyzes the transfer of a two-carbon unit from ketose phosphates to aldose phosphates. In heterotrophic organisms, TK provides a link between glycolysis and the pentose phosphate pathway and provides precursors for nucleotide, aromatic amino acid and vitamin biosynthesis. In addition, the enzyme plays a central role in the Calvin cycle in plants. Typically, TKs are homodimers. They require TPP and divalent cations, such as magnesium ions, for activity.	4.51725e-126
NZ_CP049246.1\|WP_103905859.1\|3990999_3992349_+\|adenylosuccinate-lyase	gnl\|CDD\|236452	PRK09285, PRK09285, adenylosuccinate lyase; Provisional.	0
NZ_CP049246.1\|WP_103905863.1\|3995201_3995747_+\|RNA-polymerase-sigma-factor	gnl\|CDD\|224511	COG1595, RpoE, DNA-directed RNA polymerase specialized sigma subunit, sigma24 homolog [Transcription].	2.28648e-41
NZ_CP049246.1\|WP_103905850.1\|3977221_3979627_+\|TonB-dependent-receptor	gnl\|CDD\|369481	pfam07715, Plug, TonB-dependent Receptor Plug Domain. The Plug domain has been shown to be an independently folding subunit of the TonB-dependent receptors. It acts as the channel gate, blocking the pore until the channel is bound by ligand. At this point it under goes conformational changes opens the channel.	3.24315e-19
NZ_CP049246.1\|WP_103905860.1\|3992421_3992976_+\|NifU-family-protein	gnl\|CDD\|378032	pfam08712, Nfu_N, Scaffold protein Nfu/NifU N terminal. This domain is found at the N-terminus of NifU and NifU related proteins, and in the human Nfu protein. Both of these proteins are thought to be involved in the the assembly of iron-sulphur clusters.	8.97413e-30
NZ_CP049246.1\|WP_103905854.1\|3983080_3984070_-\|aldo/keto-reductase	gnl\|CDD\|381369	cd19143, AKR_AKR6C1_2, AKR6C family of aldo-keto reductase (AKR). Voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa are founding members of aldo-keto reductase family 6 member C1 (AKR6C1) and C2 (AKR6C2), respectively. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.	0
NZ_CP049246.1\|WP_103905867.1\|3998433_3999189_+\|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.	2.13953e-45
NZ_CP049246.1\|WP_103905862.1\|3994242_3995196_+\|transketolase-family-protein	gnl\|CDD\|226467	COG3958, COG3958, Transketolase, C-terminal subunit [Carbohydrate transport and metabolism].	7.11754e-133
NZ_CP049246.1\|WP_103905852.1\|3980633_3981164_-\|HXXEE-domain-containing-protein	gnl\|CDD\|379370	pfam13787, HXXEE, Protein of unknown function with HXXEE motif. This domain contains an HXXEE motif, another conserved histidine and a YXPG motif. Its function is unknown.	1.77772e-19
NZ_CP049246.1\|WP_103905856.1\|3985999_3987811_+\|membrane-protein-insertase-YidC	gnl\|CDD\|234942	PRK01318, PRK01318, membrane protein insertase; Provisional.	1.30673e-114

>NZ_CP049246.1|WP_103905858.1|3990309_3990528_+|hypothetical-protein
MKNLFKFGFLGLALTIAVASCNNAETKTEATADSLSNAVDSTTEVVADSIENVADSVRATGDSISDSLKNVQ
>NZ_CP049246.1|WP_103905857.1|3988722_3990072_-|acyl-CoA-dehydrogenase
MFDKAKNILKLLKSVDFEQLEKISKKVDLAQVLGAVSKMDENQLNMAMKMLTGSKKKKDPPPINADFYDVSAKLSETDRALQMKVRTFLETEIKPLVNKYWLHDEFPFEIIPKLRELNVCGYVYEGYGCAGGTSLMDGIIASEFGRVDPSIATFLGVQSGLAMGSIYMCGSEEQKNEWLPKMQQLEKIGAFGLTEPLVGSATAGGLTTTCKRDGDNWVLNGQKKWIGNSTFSDITIIWARDLDDQQVKGFIVRKENPGFAVEKIKGKMALRIVQNGLITLTDCVVPDSDRLPHANSFKDTAKVLQMTRAGVAWMAVGCARGAYENALDYTIKREQFGKPIASFQLIQNHLVEMLSNLTAMQTLVFRLSELQDDDKLRDEHASLAKVFCTLRMRDIVSKAREVMGGNGILLEYNVARFLADAEAIYSYEGTKEINSLIVGRSITGFSAFV
>NZ_CP049246.1|WP_103905856.1|3985999_3987811_+|membrane-protein-insertase-YidC
MDRNNILGFILIFAILGGSFFLLKPSEDEIKKEQLHQDSIKRANEGLPPLSDSLKKANVQPAVSDSVLLTQPFGAASRGTDQIVSLENELIKVNVSSKGGRVKSVELKGETNFDGSNLILFDGDNNKFGLEFNVPGKAVKTNDLYFQAQGGNISVAGQDAKSLTMRLSYAPDKYIDYVYTLKGNDYNVQFDIKTVGISSLLDVNSKKALLNWETTLTQKERNVKSEREKSSIFYKEVDGDVDHLSETSDDDEVIENKLAWIAFKQHFFSSILTSKEGFTNAELKSTFMTTDGVVKNYRATSEIALTSDAQHGFSFFFGPNKYKTLKAEGNDFSKIINMGWGPMGWINKFITVPIFDFLDGFNMNYGIVILILTLFLKLLMFPLTYKSYQSMGKMRVLKPQLDEIKAKVGDDNPMLLQQEQMKLYKQAGVNPLGGCLPLLLQMPFTLAFFFFFPNLFELRGESFLWVKDLSTYDAPITFAPIFGVDHISFMCILMTLTTLLTTWYNNSTSGAVNNQMKYIGYIMPLIFFFVLNSFPAGLNYYYFLSAVLTFLTQVLIRQFVNDDKILASIEANKKKPQGEKKQSSFQKKMEEMMRQQQANKDKK
>NZ_CP049246.1|WP_103905855.1|3984351_3985962_+|CTP-synthase
MTKYIFVTGGVTSSLGKGIIAASLAKLLQARGLKVTIQKFDPYINIDPGTLNPYEHGECYVTEDGAETDLDLGHYERFLNVPTSQANNVTTGRIYSHVIEQERAGAYLGKTVQVVPHITDEIKRRMLLLGQSGEYDIVITELGGTVGDIESLPFIEAVRQLRWELGNNDSLVIHLTLVPYLAAAGELKTKPTQHSVKTLLEYGVQPDILVCRTEHKLNNDIRKKLALFCNVNINAVVESIDAPTIYDVPLNMLKEQLDKTVLAKLKLSTKNDPDLENWKSFLGKLKNPTGEVNIGLVGKYVELPDAYKSIAEAFIHAGATNETRVKVKYIAAESVNQENVGEKLKGLDGVLVAPGFGERGLEGKLETIRFVRENKVPFFGICLGMQCSVIEFGRNVLGLKGANSFEMDEKTPHPVINLMEEQKNIKNMGGTMRLGAYDCEIKKGTKAFGIYGKSKISERHRHRYEFNNEYLKDYEKAGMIASGINPTTGLVEIVELKDHPFFVAGQFHPELKSTVVNPHPLFVSFVAAALANKKSQ
>NZ_CP049246.1|WP_103905854.1|3983080_3984070_-|aldo/keto-reductase
MEYRRMGKSGLQLSALSFGSWVTFARQTDDQINERLMAQAYEAGVNFFDNAEVYSAGKSEEMMGRVLKKMNWDRTSYVLSSKAFFGWRGEANKPNQHGLSRKHLMEACHEALTRLQVDYLDLYYCHRPDKNVPIEEVVRTMNTLIQQGKILYWGTSEWSAAEIVEAHMVAKEAGLEGPAVEQPEYNLFNRRKVEVDYAPIFRNIGMGTTIWSPLASGLLTGKYNDGIPEGSRLSLEGYEWLRDKAMAKERLAGVKALGEYAEELGVSLATLSIAWCISNPNVTTAILGATKESQLAENLKALDVLPLLTPEVKVRIDEIMGTQPVDSQH
>NZ_CP049246.1|WP_103905853.1|3982658_3983003_+|50S-ribosomal-protein-L19
MDLVKFVEEQAVVKNENPAFKAGDTISVHYKIREGNKERVQVYQGVVIQLNSEGTNATFTVRKISNGIGVERIFPVNSPNIQKIEVNSVGKVRRAKLFYLRGLTGKAARIKAKR
>NZ_CP049246.1|WP_103905930.1|3981302_3981842_-|hypothetical-protein
MNHHEQIEIPLSKRKMILTLLGACVFVVLGGLFVLNPQKFTSIIMRNPIVILISGIASILFFGIVGISIFRKLLDKKPGLIINHEGVNDNSSGVSAGFIPWSDIREIKVSHVFNQKFLLFIVNNPEDYLDKIKNPLKRSAMKMNYKSYGSPISISSTVLQTNFDDLSKVLVEKLKTYKQ
>NZ_CP049246.1|WP_103905852.1|3980633_3981164_-|HXXEE-domain-containing-protein
MELKILVLIFPIIFMIHDFEEIIFFKKWILRNENELTRRFPKIANKFLPHFKNISTSSFALGVAEEFLIVSIISVFAIMNEDFKLWYGIFIGFFIHIIIHIIQWIIYRKYIPSIVTSFLVLPYCFYTLEKLNESKLLELSDKILWGVIGFVIVILNLLLVHKLIAKFEKMQQIKDQ
>NZ_CP049246.1|WP_103905850.1|3977221_3979627_+|TonB-dependent-receptor
MQKLKCILLLTGCFALPLLSRSQERSAKDSLANLKIEGIDILGHRLLRSNLVKIDHRTLQDIQAHTLGETVSHISGVQNSYFGPFAGAPVIRSLSGNRIKVMSNGLGINDLSGNSPNFNMGIDMDNVESITVHKGSAAVLYGGRAIGGALNVEGRTIPKKMDSVAFNARVQLEGSTNNGFKQAFQAQGNNKKNWAWHVSGSHMKIDKIRIPGNTKPDFVYDPKVIAFDSFLQGMAQLHVDAGHKLNTTIFPYLSQYVLDQFAQGNTDLSEEDKYTFKETYYDREDQMEKPNPRNDAFIPGQDPEKDRSIAYVNSIADYVKPEKGLIPNSHAQQYTFQAGTSYIRKDFFLGVGYETQFSKYGIPGYWTFHTPQHNHGHAGHTHPVTYLPINMKSISNRLKLASQYQVDQLGLSSIKLDYSGQFGSDRELLDIYQANTFETKRHALRMEIEQQPFHILSGTTGVDFAQADISGKGGLRYMPNSLSRELGLFTMQKLTYQFATLALGYRHDQVKRKAFPDAAYQTGRGMAGGEFRERDFHLNQFSGSLKFNITDIAFLEGHFNHSERAPEVNELYSGNNHFAILIEENGDDRLNKETANGIELNGGLNLKNLKISLGWYNTHYNDYLYLAHTGISRGMNFIVKEWRAADTEVQGFEGDASYILRFGDKRSWEFGGYFDLVKNENRSEDEMRDHYDGAYMPNMPTSRFGLSSKVNYGAIYFYVALDRYLEQRFLGKNLSVEPAMPAYSLLSARISYSGKLMKQKVEYHIAGNNLLNQEARPQNSWLKYVSPLPGANISFGVNVLL
>NZ_CP049246.1|WP_103905849.1|3976076_3977174_+|hypothetical-protein
MRLYIKPLSPLFCATLILYLFLSSCKKTEHVPQVDLVIPTDLSIPYGNDTTIHISSPTGNSDKITYSLAFDEATKNIKLHNGNLLQTLEKAVTLHQEKGDLKIQTGLLFPNGATSVSSDVIIPEIYRVKVIAKSNTGNILKEEDLSFKILPGKITFQDVDQTSANAFTYRLFSNKETFIALDSTVKIPEGSQLQLPKSAASTGIKISDNQLVFPSSTGNLSNLEEKSYTVEPALIKDGFPVASRKLKVTFIPQIKFFYGSYYPEYDITVKTPLLNISLYGGFQSQKPVFYPEKYRSSFSIVKIEKDGEPFEDTDKLFAIKADLGIITVKTNKTLQAGQYKIYTKAVLTTGMVLFTDLTLAMKEGD
>NZ_CP049246.1|WP_103905859.1|3990999_3992349_+|adenylosuccinate-lyase
MTLSPLTAITPIDGRYYNNTKDLSNYFSEFALIKYRVLVEVEYFIALCGSGIPQLSHFDGSLNNKLRDLYRNFSLEDAQWIKDTEKVTNHDVKAVEYFLKNEFEKLGLSDSLEFIHFGLTSQDINNTAIPHSWKDALQEVYNPAITELVDELKKLSTEWENVSMLARTHGQPASPTRLGKEIKVFIERIEKQLELLKSIPFSAKFGGATGNFNAHFVAYPNHDWVAFGNSFVNETLGLDRSQTTTQIEHYDNFAASCDNLKRINNIIIDLCRDVWTYISMDYFKQKITAGQIGSSAMPHKVNPIDFENAEGNLGLANAVLEHLAAKLPISRLQRDLTDSTVLRNIGVPFAYTLIAIKSTLRGLRKLILNEAAFQADLENNWAVVAEAIQTILRREGYPKPYEALKDLTRTNAHVTQATIASFVDGLAVSDEVKAEIKAISPSNYTGVKL
>NZ_CP049246.1|WP_103905860.1|3992421_3992976_+|NifU-family-protein
MATINVYTESTPNPATMKFLVNKLLINGSLDYPDKEKAQESAFARELFKFNFVNGVFFASNFVTITKTEDAEWSDIEALLKEFVKGAVESELAVKPVEHSEEVVFEGSDVEVKIQQVLHDYVRPAVEQDGGAIAYKSFDSGIVTVELRGSCSGCPSSTITLKAGIEGLLKRMVPEVEEVVANAM
>NZ_CP049246.1|WP_103905861.1|3993337_3994186_+|transketolase
MSADINKLEQIASQVRRDIVRMVHACQSGHPGGSLGCTDYFVALYFHAMKHDPSFNMDGIGEDLFFLSNGHISPVFYSTLARAGYFPVSELSTFRKINSRLQGHPTTHEHLPGIRVASGSLGQGLSVALGAAQAKKLNKDNSLVYVLMGDGELQEGQVWEAAMYAPHNKMDNIIAAVDYNRAQIDGSTDEVLNLGNLRAKWEAFGWDVLEVDNGNDMTAVIAGLDEAKSRTGKGKPVIILLHTEMGSGVDFMMGSHKWHGVAPNDEQLETALNQIPRTIGDY
>NZ_CP049246.1|WP_103905862.1|3994242_3995196_+|transketolase-family-protein
MKKYTYTESKDTRSGFGAGLLEAGQKNENVVALCADLIGSLKMNDFIKAFPERFFQIGIAEANMMGIAAGLTIGGKIPFTGTFANFSTGRVYDQIRQSIAYSGKNVKICASHAGLTLGEDGATHQILEDIGLMKMLPGMTVINPCDYNQTKAATIALVEHEGPVYLRFGRPVVPNFTPADQKFEIGKAIMLNEGTDVTIVATGHLVWEAIQAGEELEKLGISAEIINIHTIKPLDDEAILKSVTKTGCIVTAEEHNRLGGLGDSVAQLLAKQLPTPQEYVAVDDSFGESGTPAQLMEKYGLNAANIVNAVRKVITRK
>NZ_CP049246.1|WP_103905863.1|3995201_3995747_+|RNA-polymerase-sigma-factor
MEDSLIIAKFADESTREEAFRLLLKKYQQKIYWHVRRMVIDHDDADDVVQDIFIKVWRNLEKFREDSQLYTWLYRIATNECITFLNKKKQKQSVSLDDESSAYLSDSLADGAYFNGDKAQMKLQQALLTLPDKQRLVFNMKYFEDMKYEEISNVLGTSVGALKASYHLAVKKIENFFASND
>NZ_CP049246.1|WP_146060599.1|3995781_3996720_+|hypothetical-protein
MKENNTYHENLEGNNLPNSLRVNPFIVPKNYFEELADRTLFLARLDQLSTAGKVSGFSVPEDFFKNQASQLISQIKIDQIDAAAFTVPANYFDQLGEQVLGQVKIDGLQDEADVPAGYFEQLSSRIMDRIQEEEEVAFSLELQDTGFTVPEGYFDAAEEEILANVAVEELQGLVKSDGFTVPNSYFDQLSNNILEQVQDKKVISLPSREERKEKTPAKRGKVYAWFTTAAAACVAAVIGLSVYNGAENKPMEVEPVALNDIPEEEIINYLSSYSDASDLEYIAEYIYQPEETKGVGTGIDEDVLEDYLNYTL
>NZ_CP049246.1|WP_103905865.1|3996719_3997148_+|hypothetical-protein
MMVRLKHIISMICLICLAFVANGQSRQERFEAIERQKVAFISKQLRLTPAEAQRFFPLYNQYSNEIRAVKSKKSRGANRPERGNSFRSGDVIEYDAQEVNIKKEYRSKFADVIGQSRASQFFSVEQEFIELLYKELNSRNKH
>NZ_CP049246.1|WP_103905866.1|3997203_3998391_+|aspartate-aminotransferase-family-protein
MINNRALFLQNTAQTSDSPRLLEIERAEGIYLYGPQGEKYMDLVSGFNVSNIGHRHPRVLQAIEEQLAKFMHVTVYGEFVQAPQVMFATELLAVLPESFGSVYFTNSGAEAVEGSMKIAKKFTGRREIIAAREAYHGSTQGALSLIGNDAYREAYAPLLPDISFIDYNSQTDLAAITERTAAVIVEAIQGEAGVRVPTATYMKALREKCTETGALLIFDEIQTGFGRTGKLFAFEHFGIVPDILMLAKGIGGGMPLGAFVAPKEIMDVIKANPMLGHITTFGGHPVSCASARASLQVIQEENLVPAVEAKAALFRSELAIPQIREIRGLGLMMCLQLDNFDQVYQVSNYCASKGLIIDWYLHCETALRIAPPLTITEDEIREACKIIREAIAKFC
>NZ_CP049246.1|WP_103905867.1|3998433_3999189_+|SGNH/GDSL-hydrolase-family-protein
MNDRRDFLKKSLLTLGAAGLTGSLAQAFNFSTGAKAKISIKKGDVILFQGDSITDAGRKRDNLNPNDSNAFGNGYAFMAASTLLNKHADKDLKVYNRGISGNRVPDLLGRWQTDALELKPTILSIMIGVNDFWRTKDRGAVNTPEQYKAQYKELLDKTVSALPGVKLILIEPFGVNNVKHVKDDWYPEFPKYQQVVKELAQEYKAVFLPYQQVFDQALKRNANGAHWTTDGVHTTMAGANLMAEAWLNLVS
>NZ_CP049246.1|WP_103905868.1|3999288_4000473_-|class-I-SAM-dependent-rRNA-methyltransferase
MKKIILNKGKDKAAWQLHPWVFSGAIKSTVDHPKNGDIVAVFNNEDEFIAYGMYNAKSRVAVRLLEWDPSKEINEQWWRARVAKAVNKRLALLNEENDTLRLIFAEADFLPGLIADKYADYISIQVHAAGTESVKDIIVDELVQLLHPKGIYERSDLKSREYEGLPDSNGKRYGEVPPEFVEIVENGIHYQVNIVEGQKSGFYCDQRENRAITARYAKDKKVLDCFCYSGGFTLNAFRQGAQSVTSVDSSALAIETLKSNVQKNGFAADKHSAVQSDVNKYLRELGEQGEKFDLIVLDPPKYAPSRSTLEKASRAYKDLNRRGLLLLNSGGILATFSCSGAMDIETFKQVIAWAALDAGKEIQYIYQFCQPEDHPVRASFPEGEYLKGLLVRVV

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Crispr_ID: NZ_CP049246_15

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP049246_15

4017132-4017262

Orphan

Consensus_repeat	Method
GCTGGCGCAAGAGTTGTGCGGCAGGCCTGTGCGGTGGATCTCTTGTG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP049246_15

>merge|NZ_CP049246|15|4017132-4017262|CRISPRCasFinder
GCTGGCGCAAGAGTTGTGCGGCAGGCCTGTGCGGTGGATCTCTTGTGCCTGAAAACCTTACCCTTTTTATTCAATGCGCACAACGCTGGCGCAAGAGTTGTGCGGCAGGCCTGTGCGGTGGATCTCTTGTG

>NZ_CP049246|15|14|4017132-4017262|CRISPRCasFinder
GCTGGCGCAAGAGTTGTGCGGCAGGCCTGTGCGGTGGATCTCTTGTG	CCTGAAAACCTTACCCTTTTTATTCAATGCGCACAAC
GCTGGCGCAAGAGTTGTGCGGCAGGCCTGTGCGGTGGATCTCTTGTG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP049246.1\|WP_103905881.1\|4015708_4016545_+\|elongation-factor-Ts	unknown	unknown	gnl\|CDD\|236491
NZ_CP049246.1\|WP_103905932.1\|4024108_4024414_+\|helix-turn-helix-transcriptional-regulator	unknown	unknown	gnl\|CDD\|238045
NZ_CP049246.1\|WP_103905883.1\|4019164_4019908_+\|SDR-family-oxidoreductase	unknown	unknown	gnl\|CDD\|235506
NZ_CP049246.1\|WP_103905888.1\|4024500_4026030_-\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	unknown	unknown	gnl\|CDD\|369630
NZ_CP049246.1\|WP_103905931.1\|4011003_4011774_-\|DUF4292-domain-containing-protein	unknown	unknown	gnl\|CDD\|372917
NZ_CP049246.1\|WP_103905887.1\|4023465_4023969_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP049246.1\|WP_160003685.1\|4007710_4009162_-\|lytic-transglycosylase-domain-containing-protein	unknown	unknown	gnl\|CDD\|381615
NZ_CP049246.1\|WP_093098741.1\|4013835_4014279_+\|50S-ribosomal-protein-L13	unknown	unknown	gnl\|CDD\|181703
NZ_CP049246.1\|WP_103905889.1\|4026042_4029135_-\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|274948
NZ_CP049246.1\|WP_103905880.1\|4014695_4015502_+\|30S-ribosomal-protein-S2	unknown	unknown	gnl\|CDD\|235396
NZ_CP049246.1\|WP_103905884.1\|4020035_4020884_+\|methylated-DNA--[protein]-cysteine-S-methyltransferase	unknown	unknown	gnl\|CDD\|185333
NZ_CP049246.1\|WP_103905879.1\|4014290_4014677_+\|30S-ribosomal-protein-S9	unknown	unknown	gnl\|CDD\|376328
NZ_CP049246.1\|WP_103905874.1\|4007157_4007673_+\|phosphoribosyltransferase	unknown	unknown	gnl\|CDD\|235365
NZ_CP049246.1\|WP_103905886.1\|4021642_4023232_+\|ABC-F-family-ATP-binding-cassette-domain-containing-protein	unknown	unknown	gnl\|CDD\|223562
NZ_CP049246.1\|WP_103905877.1\|4009616_4010894_-\|peptidoglycan-DD-metalloendopeptidase-family-protein	unknown	unknown	gnl\|CDD\|227278
NZ_CP049246.1\|WP_103905882.1\|4017956_4019033_+\|AI-2E-family-transporter	unknown	unknown	gnl\|CDD\|223701
NZ_CP049246.1\|WP_103905885.1\|4020887_4021490_+\|alpha-ketoglutarate-dependent-dioxygenase-AlkB	unknown	unknown	gnl\|CDD\|225687
NZ_CP049246.1\|WP_103905933.1\|4029570_4029876_-\|N-acetyltransferase	unknown	unknown	gnl\|CDD\|379642
NZ_CP049246.1\|WP_103905876.1\|4009313_4009541_-\|twin-arginine-translocase-TatA/TatE-family-subunit	unknown	unknown	gnl\|CDD\|224739
NZ_CP049246.1\|WP_103905878.1\|4011763_4013470_-\|tetratricopeptide-repeat-protein	unknown	unknown	gnl\|CDD\|274350

Protein	Function_ID	Function_description	E-value
NZ_CP049246.1\|WP_103905881.1\|4015708_4016545_+\|elongation-factor-Ts	gnl\|CDD\|236491	PRK09377, tsf, elongation factor Ts; Provisional.	2.21524e-125
NZ_CP049246.1\|WP_103905932.1\|4024108_4024414_+\|helix-turn-helix-transcriptional-regulator	gnl\|CDD\|238045	cd00093, HTH_XRE, Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the xenobiotic response element family of transcriptional regulators.	0.000453797
NZ_CP049246.1\|WP_103905883.1\|4019164_4019908_+\|SDR-family-oxidoreductase	gnl\|CDD\|235506	PRK05565, fabG, 3-ketoacyl-(acyl-carrier-protein) reductase; Provisional.	9.4431e-84
NZ_CP049246.1\|WP_103905888.1\|4024500_4026030_-\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	gnl\|CDD\|369630	pfam07980, SusD_RagB, SusD family. This domain is found in bacterial cell surface proteins such SusD and SusD-like proteins, as as well RagB, outer membrane surface receptor antigen. Bacteroidetes, one of the two dominant bacterial phyla in the human gut, are Gram-negative saccharolytic microorganisms that utilize a diverse array of glycans. Hence, they express starch-utilization system (Sus) for glycan uptake. SusD has 551 amino acids, and is almost entirely alpha-helical, with 22 alpha-helices, eight of which form 4 tetra-trico peptide repeats (TPRs: helix-turn-helix motifs involved in protein-protein interactions). The four TPRs pack together to create a right-handed super-helix. This is predicted to mediate the formation of SusD and SusC porin complex at the cell surface. The interaction between SusC and TPR1/TPR2 region of SusD is predicted to be of functional importance since it allows SusD to be in position for oligosaccharide capture from other Sus lipoproteins and delivery of these glycans to the SusC porin. The non-TPR containing portion of SusD is where starch binding occurs. The binding site is a shallow surface cavity located on top of TPR1. SusD homologs such as SusD-like proteins have a critical role in carbohydrate acquisition. Both SusD and its homologs, contain about 15-20 residues at the N-terminus that might be a flexible linker region, anchoring the protein to the membrane and the glycan-binding domain. Other homologs to SusD have been examined in Porphyromonas gingivalis such as RagB, an immunodominant outer-membrane surface receptor antigen. Structural characterization of RagB shows substantial similarity with Bacteroides thetaiotaomicron SusD (i.e alpha-helices and TPR regions). Based on this structural similarity, functional studies suggest that, RagB binding of glycans occurs at pockets on the molecular surface that are distinct from those of SusD.	3.16312e-24
NZ_CP049246.1\|WP_103905931.1\|4011003_4011774_-\|DUF4292-domain-containing-protein	gnl\|CDD\|372917	pfam14125, DUF4292, Domain of unknown function (DUF4292). This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 243 and 287 amino acids in length.	9.03242e-37
NZ_CP049246.1\|WP_103905889.1\|4026042_4029135_-\|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_CP049246.1\|WP_160003685.1\|4007710_4009162_-\|lytic-transglycosylase-domain-containing-protein	gnl\|CDD\|381615	cd16894, MltD-like, Membrane-bound lytic murein transglycosylase D and similar proteins. Lytic transglycosylases (LT) catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc). Membrane-bound lytic murein transglycosylase D protein (MltD) family members may have one or more small LysM domains, which may contribute to peptidoglycan binding. Unlike the similar "goose-type" lysozymes, LTs also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, as well as the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL).	8.1768e-57
NZ_CP049246.1\|WP_093098741.1\|4013835_4014279_+\|50S-ribosomal-protein-L13	gnl\|CDD\|181703	PRK09216, rplM, 50S ribosomal protein L13; Reviewed.	3.51256e-96
NZ_CP049246.1\|WP_103905880.1\|4014695_4015502_+\|30S-ribosomal-protein-S2	gnl\|CDD\|235396	PRK05299, rpsB, 30S ribosomal protein S2; Provisional.	3.01901e-145
NZ_CP049246.1\|WP_103905884.1\|4020035_4020884_+\|methylated-DNA--[protein]-cysteine-S-methyltransferase	gnl\|CDD\|185333	PRK15435, PRK15435, bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada.	5.69283e-55
NZ_CP049246.1\|WP_103905879.1\|4014290_4014677_+\|30S-ribosomal-protein-S9	gnl\|CDD\|376328	pfam00380, Ribosomal_S9, Ribosomal protein S9/S16. This family includes small ribosomal subunit S9 from prokaryotes and S16 from eukaryotes.	5.51073e-65
NZ_CP049246.1\|WP_103905874.1\|4007157_4007673_+\|phosphoribosyltransferase	gnl\|CDD\|235365	PRK05205, PRK05205, bifunctional pyr operon transcriptional regulator/uracil phosphoribosyltransferase PyrR.	6.99324e-27
NZ_CP049246.1\|WP_103905886.1\|4021642_4023232_+\|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].	9.69061e-107
NZ_CP049246.1\|WP_103905877.1\|4009616_4010894_-\|peptidoglycan-DD-metalloendopeptidase-family-protein	gnl\|CDD\|227278	COG4942, COG4942, Membrane-bound metallopeptidase [Cell division and chromosome partitioning].	9.53522e-36
NZ_CP049246.1\|WP_103905882.1\|4017956_4019033_+\|AI-2E-family-transporter	gnl\|CDD\|223701	COG0628, yhhT, Predicted permease, member of the PurR regulon [General function prediction only].	3.80729e-28
NZ_CP049246.1\|WP_103905885.1\|4020887_4021490_+\|alpha-ketoglutarate-dependent-dioxygenase-AlkB	gnl\|CDD\|225687	COG3145, AlkB, Alkylated DNA repair protein [DNA replication, recombination, and repair].	8.07996e-27
NZ_CP049246.1\|WP_103905933.1\|4029570_4029876_-\|N-acetyltransferase	gnl\|CDD\|379642	pfam14542, Acetyltransf_CG, GCN5-related N-acetyl-transferase. This family of GCN5-related N-acetyl-transferases bind both CoA and acetyl-CoA. They are characterized by highly conserved glycine, a cysteine residue in the acetyl-CoA binding site near the acetyl group, their small size compared with other GNATs and a lack of of an obvious substrate-binding site. It is proposed that they transfer an acetyl group from acetyl-CoA to one or more unidentified aliphatic amines via an acetyl (cysteine) enzyme intermediate. The substrate might be another macromolecule.	7.84559e-24
NZ_CP049246.1\|WP_103905876.1\|4009313_4009541_-\|twin-arginine-translocase-TatA/TatE-family-subunit	gnl\|CDD\|224739	COG1826, TatA, Sec-independent protein secretion pathway components [Intracellular trafficking and secretion].	6.79089e-15
NZ_CP049246.1\|WP_103905878.1\|4011763_4013470_-\|tetratricopeptide-repeat-protein	gnl\|CDD\|274350	TIGR02917, TPR_domain_protein, putative PEP-CTERM system TPR-repeat lipoprotein. This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.	1.58004e-25

>NZ_CP049246.1|WP_103905881.1|4015708_4016545_+|elongation-factor-Ts
MSVQISASDVNKLRQQTGAGMMDCKKALVEANGDFEAAVDYLRKKGAKVAASRQDRDSNEGVIIAKAAADGKSGIVVEVNCETDFVAKNADFVAFAESVADAALANNPATLDELKAIELNGTKIADQLIEQTGKIGEKIDVSKFETISADKVVAYIHGNYRLGVLVGLSEDAAGADEAGKDVAMQIAAMNPVAIDKDGVDSKTIERELEIAKEQIRAEGKPEEMVEKIAAGKLNKFYKESTLLNQEFVKDSSKTIAQFLDSVSKGLTVTAFKRVQLGA
>NZ_CP049246.1|WP_103905880.1|4014695_4015502_+|30S-ribosomal-protein-S2
MARTTYQELLDAGVHFGHLTRKWDPKMAKYIFMERNGIHIIDLNKTLTKLEEAASAIKQIVKSGRKVLFVATKKQAKEIIAEQAKAVNMPFVTERWLGGMLTNFATVRKSIKKMSNIDKMQKDGTYDVLSKKEKLMIQRERIKLENLLGGIADLNRLPAALFIIDVKKEHIAVAEAMKLNIPTFAMVDTNSDPTNIDFPIPANDDATKSISLIASVIGKAITEGLEERKRDKEEDAEKEAAAAKAAVDNGEATEAAPGKRTRKAKDVE
>NZ_CP049246.1|WP_103905879.1|4014290_4014677_+|30S-ribosomal-protein-S9
MSTTNTSGRRKTAVARIYLTAGNGNITVNSKDYKVYFPTLPLQYIVTQSLLVAESLANFDINVNVQGGGVKGQAEAVRLAIAKALVELNPEVKPALRAKGLMTRDDRMVERKKPGRRKARRRFQFSKR
>NZ_CP049246.1|WP_093098741.1|4013835_4014279_+|50S-ribosomal-protein-L13
MNTLSYKTVSANKNTVNKEWIVVDAEGEILGRLASEIAKVIRGKHKPSFTPHVDCGDNVIVINADKVRLTGNKLGDKVYVRYTGYPGGQRFVSPKELMAKHPERIIEKAVRGMLPKNRLGRQLFKNLYVYAGTEHKHEAQNPKPVKF
>NZ_CP049246.1|WP_103905878.1|4011763_4013470_-|tetratricopeptide-repeat-protein
MRRSQWFKPLMLGVLLVAGQSLFAQELKDDKGYKDQLAAIETKLKSGDISNALQSIEETLQKYPKGAEVYYAKSLLYAQARNFDVALPAAIEAVKISPENILFNNHLLELYKSQGNFDAAVALLDDFMKLHPNNPQLYREKIMLQHTGKQSADALKTYDVAKEKFGETDTLDVLKAEILMDLKKPKEAQALLLPWRQKKSPIRQVYSTLSYIYIDENKPKDAVLVLEDGLQASKDDLLYLDMADANMALNKKIPAFDNIKKAFLSESVTYMDKHRVMSNLVNNNKDFTMDQLQDLAGVLILKHPGIAESHMFKGDVLWIRGALDEAKSLYLTAVSITPQNVEAWRKLVNVDLANNDLDQAIVDGNEALKHNPGNVIITYFVGMAHMMKKDTDQARKYLESALDQSANQNDFVKSMVYGGLGDLYHEIKMESASDVAYEEAIKLDSNNVTALNNAAYYLSLRKENLDKAAEYAKRANEVEPNSGTFQDTYAWVLFQQGKYAEALTWIEKAIKNSQPSGVLYEHYGDILMKVGKGKEAIKQWEKALTFADGSTVDKEKIKKKISEKKYID
>NZ_CP049246.1|WP_103905931.1|4011003_4011774_-|DUF4292-domain-containing-protein
MLTKLSLLMAVLVVLYSCGSKKQASKPADVVTTEKGKDLVSTYELNNLNFITFDGRAKAKMEFGNDSKNVTLNVRMERDKAIWISVTALLGIEAVRILITPDSVKIMNRLNSEYISKPFSYIYNYTNPGISFRMLQDILVGNISTEMLRTDQLQVATSDADVQVIGVKDGLTFHYGVNKQNRPFIFNLMEIGKDTKMEATYSDYAVIDGHNFPQRFTLNIEGNGVKVASDMLYNKSEFNKTVELPFTIPSRYKAIN
>NZ_CP049246.1|WP_103905877.1|4009616_4010894_-|peptidoglycan-DD-metalloendopeptidase-family-protein
MDFKKIALSIFSLLFFVGLSFGQSSLELKKQRERIDREIAELQKVLSAKTREKLLSQKEVAALSKQLDLRENKISTINSELRIINQNINSNNKIVDKLKAELEKMRQDYEKMILFAFRNKNAYNKMMFIFASKDFNQAFRRVKYLQQFTDARKVKVAEIEGTKKQIELKIAQLEQDKKTQQALLKEQEAERNTIAKDRAAHSQELNQLAREERTFRGQLTKKQQEKKRLDAAIKTAIAREVEAARRAEEARRKKLAEEAAKKAGTTVAEAEKKIEKKTGSSVLNNSPEATKLSAGFSSNRGRLPWPVGQGSVVRNYGSVTVERGVRDFYDYIRIRTSDGAPVKTVFEGTVLQVINIGSYAVVVQHGEYLTAYSNLKSVSVRKGQKISTGTVIGSADSDPEVGYSYIDLSVYKGTTSMNPSSWIAR
>NZ_CP049246.1|WP_103905876.1|4009313_4009541_-|twin-arginine-translocase-TatA/TatE-family-subunit
MYTSGLLFIGTNEIIIIVVIVLLLFGGKKIPELMRGLGRGVKEFKEGQKDGPDAENNANTTTTTTTNNDTVNNQR
>NZ_CP049246.1|WP_160003685.1|4007710_4009162_-|lytic-transglycosylase-domain-containing-protein
MNKKISFLVTIGLGVCGFGHAQEITVDPSQFTETFQTSVLDQITQDKERTHMMLDSVKQVAGNGVQFTDEDVNIAQRIQRLQKTIPLEYNARVKAYLDKYISRNYKPYMEKLLGLSSYYFPIYDQIFQEQGIPLEARYLSVVESSLDPHTVSTSGAVGPWQFIYGTAKVYNLNMDSYYDERKDVYSSTYAVASYLKEAYDEFNDWVLALASYNCGRGCVRRAIVRSGLRNPSYWELSPFLPKETQNYIPKYIAMTYVLNHAELYGLNPKEHELQAGNKVLMLDKSVNLASLANALTCSSDLIKQLNPAYKKGVVQATPEKPRRLVIPYNESMSDSLIYAALNNQANPAVQQAIAVLEDEREHRVVRGETLQSIAKKYNVSVQNLMAWNNLTSRSAIVGRTIAVAKPLDEKLTKNVIAANRAKAEKTERAAPSYVSYTVKRGDTLSGIADKHRGATVTKIKADNNIRGSHLKIGQKLKIYKGKS
>NZ_CP049246.1|WP_103905874.1|4007157_4007673_+|phosphoribosyltransferase
MSSKKTLILNKDQIRQKSRRIAYQIIEDNFDEPAIVLVGIADRGYVFAQRLQKLLAEIAPDKSIELLRVNIQKSKRSLESSTDANIDIAKNKVVILIDDVLNSGRTLAYGLGVFLNVPLKRMRTAVLIDRSHHQFPVFSDYYGLKLSTILKEHVEVQLEEYDNTEDAAYLS
>NZ_CP049246.1|WP_103905882.1|4017956_4019033_+|AI-2E-family-transporter
MRIKQINNNSINQIMLILIIILVCILIFHNLFYYLPGFLGAITLYVLYRNSYFKLTEQRRWNKVLTSLMFILLSIVFIVLPIWALVDYLVPQITSFLNNTDKIVSQFNLLKEYMADKPFLKDIDMSDEALLAMLQRMTKYVPSILNSVAEVMINIIVTLFVLYFMQVYARQMESYISSGVPFSPKSKQELWKEFDSMVRSNAIGIPILGFFQGLVAVLGYWIFGVDNFILMGMLTGIASIVPVLGTMTIYVPLGIITLASGETGNGIGILLFGFLLIGSIDNILRFTILKTLGNVPPLITVFGVLLGLKLFGMLGLIFGPLILSSVGVLIKVYSNEYGKGPSILLDQHDSGDHPPFSK
>NZ_CP049246.1|WP_103905883.1|4019164_4019908_+|SDR-family-oxidoreductase
MKQLEDKVAIVTGGASGIGKAIVELFVKEGAKVVVADLNESLGNDLINSLGEGNVIFIKADASSPEDNKKIVDAAIENFGQLHIAVNNAGIGGESNPVGDLSLEGWKKVIDINLNGVFYGMHYQLPEMLRSGGSIINMASILGQVGFANSSAYVAAKHGVVGLTKSAGWEYATKGVRVNAIGPGFIATPLIDENLDQDTLKYLETQHAFQRLGKPEEVAELALWLASDKSSFVTGAYYPVDGGYLAK
>NZ_CP049246.1|WP_103905884.1|4020035_4020884_+|methylated-DNA--[protein]-cysteine-S-methyltransferase
MEKTQQQLNYERVASAIQYIQDNFQHTPSLEEIAEHVHLSPFHFHRLFSDWAGTSPKKFLQYTQVSFAKRLLKEEQRSLFDTHMITGMSSTSRLHDLFIQIEGMTPAEYKQGGDGLEIAYSFQQTPFGKCLIASTDKGICFMAFVDDAQESLADLRKNFAKATLHEQETALHKEALALFTNEGNDLKAIKLHLKGTPFQLKVWQALLQIPLGEISSYKAIAEKIEQPTASRAVGTAIGQNPIAFLIPCHRVLQSSGGIGGYRWKPIRKSAMLGWEFAQTDKQ
>NZ_CP049246.1|WP_103905885.1|4020887_4021490_+|alpha-ketoglutarate-dependent-dioxygenase-AlkB
MKLFNTAEPERNLLPYGGSVHYYGVICDRQQHYYDRLLHNIDWKNDQAVIFGKHIETKRKVAWYGDRRFEYTYSNIQKIALPWTEDLLELKALVERTSGETFNSCLLNLYHDGSEGMAWHSDGEKDLKKHGAIASFTLGAERKFAFKHKETKEKIDILLEDGSLLIMKDATQDNWLHRLPPTKVAHGPRINLTFRTIENG
>NZ_CP049246.1|WP_103905886.1|4021642_4023232_+|ABC-F-family-ATP-binding-cassette-domain-containing-protein
MVILQNATYIHPNKDILFHDLNLVLNPQDKLALIGNNGTGKSTLLQIIAGRLPLSSGQLQVGSTPYYIPQLLDSYNDRTIAEALGIATKLQAFLAILDGEATPENMAELNDDWTIEDRSRQALEHWQLHGIDLNQKLGTLSGGQKTKVFLAGIDIQQPDLILMDEPSNHLDYLARELLYDFIRETNKSLLIVSHDRTLLNILPEIAEMSKSGITRYGGNYAFYAEQKGIALSALDHDVKAKEKELRKAKEKEREALERQNKLNARGKKKQEKAGIPKILMGGLKNKAEGSSSKLKGIHQDKISGIKERLQDLRTHLPEIDQMKFGFQQSGLHLGKTLIEADAINYQINGKNLWSSDLSFQINYGDRYALKGMNGSGKTTLIKLLLGEYLPTTGTLKRAPINAIYVDQDYSLIKSNLSIYEMAQSFNTAALQEHEVKIRLNRFLFGKETWDKSCTFLSGGERMRLLLCCLNIASQAPDLIVLDEPTNNIDIQNITILTSAIQSYQGTLIVVSHDQYFLEEVEVTKEIALF
>NZ_CP049246.1|WP_103905887.1|4023465_4023969_+|hypothetical-protein
MKFKFLLLICFAFLIGCKEEDMSPIEGDLNKALLEKNIWKNEVDVDEQFTDNSDAQKYMRVSTISFTGSHYSQTVSKHSSSLQGVPPDSSYTEFWGEYELSGADSILTLHYKIHSDMAERWIPNSDSLVFQTRFKIISLTEQELAIKPLLDSLKTSYSPVMTYKAVK
>NZ_CP049246.1|WP_103905932.1|4024108_4024414_+|helix-turn-helix-transcriptional-regulator
MLLISPAKAQAKIAESIRKRRLAMELTQEGLSERSGVPLPTLRKFEQKGNISLTALVKLLMIVGGLEDVLTALTPEKRQFNTIEEVLKASTVRERQRGKKK
>NZ_CP049246.1|WP_103905888.1|4024500_4026030_-|RagB/SusD-family-nutrient-uptake-outer-membrane-protein
MQNIKKFTLLGLAVASLFGSCNKELDIIPEGAPAKVNFWKTEADAVSASNALYALYDSEEGFYGRGLFWFINASDDMVTGRANAQADNMKNFNRAYLGGGYTEGNWSGRFTIIKLANDILRYVPAIDMNKEVKNRVLGEAYFNSAMMNFELAAHYGDDRQGVPIVTVENMDQKEAVPRAKNNMENYNHAISQYKKAAQLLPFFDTYKEEDRGRAHKVAAWGYLAKTYLYMKDYKNAELYADSVINFGKRDLEAKYKDVFTVARNYGSEYIWSVTSSAAGPDGWGSLLPGVMLTNGGWGKYNGWGYYLPTKELYDAYESGDVRREATILKPGDKFRFFGEERTFDPPTAALSDYQFNKYMEPFSYADPVGRFLSPNGDHPTTALNVPLMRFAEILLIKAEAAIQQRGAGSGDKQLNMIRQRAGLQARSGQSLSDLKNQRRCELAGEFADRHRDLVRWGDAEAAYAKPLHDSKGKEIWPARKFNPKANHIWLVPQREIDNSKGIIKQNEGW
>NZ_CP049246.1|WP_103905889.1|4026042_4029135_-|TonB-dependent-receptor
MKKNFVWIAAMLCCQVGVHAQLSAETFRPGMPVKHLSQQQITGSVKDANGQPLVGISVRNTASGETVQTDGQGTFSLKANIGDVLHISSVGYMAQDLTIDQRGQYSILLQEDTQTLSEVVVVGYGKQSRSTVTGSVASVGLDRASSRSMNNLGEVLQGKAPGVVVTNEGGDPTSKPRINIRGLGGINGEQPLYVVDGSIYSGVPMLNPNDIASISVLKDAAASIYGARASGGVILVTTKSGRKAPISIDVDAKQGFQSVWKKPQPLNAVQKAMIANQAADNAGVNRNPAYDAAKYPDGQVTRTNWVDEIIQNGYMQDYNIALDGGNEHSTLYSSFNYRKSEGILLNTYSERYNFRINAKHDIKPWLTIGENLYLNYDNGNGAATGDGYTGAIISAIYYPTNVPVYDKSGAFSGLPAEYGPGAYGDVINPVAYLKRLDIDNPMYSLVVNPYVEVKLIEGLKFRSNFSMTQGFNNFKQFTTRVPEIGKPSLSNRLTLTNTRSSDVLAEQTLTYTLDRGDHHFDALGGFNFQKINSRYNQIVGINFVSEDPALRYIVNADETLTPQDGFQQSTLVSYLARLNYNYKEKYMLSLIGRRDGSSLVAKKNRFQNYGSAALAWSLKKEDFLQDVAWLSDLKIRASYGVLGNLGSLDPFAVNPLLVRSQIFLGDAPKRVTYLAETRWANEDLTWAKSKQTNVGLDLGFMNNRLSIIADYFIKDIDNMIMELPLPGTTGLQTQIVNGGSVQDRGFELGIQYQSKNEGAFQYGIGGSLTSVKNEIKSLAGDVQTQPVNSRFRGTLNPVVLQVGESLYSYKVVETDGIFQSEEEVKAHALNGQLIQPYAQPGDFRFKDANKDGKIDADDRVFVGNAYPSFSYGLNFNASYHGFDLNLFFQGVQGNKLFNGMKFTTLNAGAGQQYNLLEGVLDAWTPENKTNDLPRVSLRDNNKNFSETSDFYVEDGSYLRLKNLTLGYTLPAGLTERMRLNKVRLYVTGNNVFTLTKYSGFDPEVGMDSFGMDSGRYPQARAFIFGLNIGF
>NZ_CP049246.1|WP_103905933.1|4029570_4029876_-|N-acetyltransferase
MNTQIMKIINNEENLQFEYAEGDEIARLEYRFYKKDIALMHTVVPESMAGKGVATALAERAFAFAKEKNKKVMVYCPFVAKYVKKHPELRDQIDRDYHPNL

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Self-targeting detection

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_ID	Protospacer_location	Mismatch	Identity
NZ_CP049246_9	9.1\|1784850\|44\|NZ_CP049246\|PILER-CR	1784850-1784893	44	NZ_CP049246.1	2658179-2658222	1	0.977

1. spacer 9.1|1784850|44|NZ_CP049246|PILER-CR matches to position: 2658179-2658222, mismatch: 1, identity: 0.977

ctcttgtgcctcgaaatcttcccccttttttaatcccaagccac	CRISPR spacer
ctcttgtgccttgaaatcttcccccttttttaatcccaagccac	Protospacer
***********.********************************

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

2805973 : 2814385

Megavirus(16.67%)

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_103906275.1\|2805973_2807245_+	adenylosuccinate synthase	G5CQQ4	Megavirus	2.4e-65	34.4
WP_103906274.1\|2807250_2808534_+	anthranilate synthase component I family protein	S4VT78	Pandoravirus	2.6e-43	42.1
WP_103906273.1\|2808673_2809678_+	aspartate--ammonia ligase	A0A1C9C5F0	Heterosigma_akashiwo_virus	1.5e-57	41.0
WP_103906272.1\|2809748_2811143_+	GIY-YIG nuclease family protein	I6R9X8	Croceibacter_phage	2.7e-09	29.8
WP_103906271.1\|2811128_2812199_-	DNA polymerase IV	NA	NA	NA	NA
WP_103906270.1\|2812358_2813234_+	carbon-nitrogen hydrolase	M1IKC7	Paramecium_bursaria_Chlorella_virus	1.1e-58	44.0
WP_103906269.1\|2813311_2814385_+	agmatine deiminase family protein	M1HES8	Acanthocystis_turfacea_Chlorella_virus	1.1e-50	31.5

Anti-CRISPR protein detection

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

Overview of predicted results

Overview of the results

Cas Category Instructions

Results visualization

1. NZ_CP049246

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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