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_CP034279	Streptomyces ficellus strain NRRL 8067 chromosome, complete genome	13 crisprs	DEDDh,DinG,csa3,cas3,WYL,cas14k,cas4	0	2	0	0

Cas Category Instructions

Results visualization

1. NZ_CP034279

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CRISPR-Cas detection and classification

Crispr_ID: NZ_CP034279_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP034279_1

1043327-1043431

Orphan

Consensus_repeat	Method
GGTCCGGTCGAGCCGGTACGCGGACCC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP034279_1

>merge|NZ_CP034279|1|1043327-1043431|CRISPRCasFinder
GGTCCGGTCGAGCCGGTACGCGGACCCTGCGGCCGGGTGGGCGCCACGGCCGGCGCGGTGCCGGGCGCCGGGGAGACGGGTCCGGTCGAGCCGGTGCGCGGACCC

>NZ_CP034279|1|1|1043327-1043431|CRISPRCasFinder
GGTCCGGTCGAGCCGGTACGCGGACCC	TGCGGCCGGGTGGGCGCCACGGCCGGCGCGGTGCCGGGCGCCGGGGAGACG
GGTCCGGTCGAGCCGGTGCGCGGACCC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP034279.1\|WP_156691420.1\|1042518_1043271_+\|MerR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|197716
NZ_CP034279.1\|WP_156691426.1\|1051602_1051911_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|367663
NZ_CP034279.1\|WP_156691427.1\|1053350_1053767_+\|SsgA-family-sporulation/cell-division-regulator	unknown	unknown	gnl\|CDD\|377399
NZ_CP034279.1\|WP_156691419.1\|1041419_1042448_+\|cation-diffusion-facilitator-family-transporter	unknown	unknown	gnl\|CDD\|223131
NZ_CP034279.1\|WP_156691425.1\|1050831_1051521_-\|endonuclease-V	unknown	unknown	gnl\|CDD\|377374
NZ_CP034279.1\|WP_156691412.1\|1030476_1031544_+\|substrate-binding-domain-containing-protein	unknown	unknown	gnl\|CDD\|224525
NZ_CP034279.1\|WP_156691413.1\|1031555_1034339_-\|glycoside-hydrolase	unknown	unknown	gnl\|CDD\|227785
NZ_CP034279.1\|WP_156691421.1\|1043638_1045810_-\|3-hydroxyacyl-CoA-dehydrogenase	unknown	unknown	gnl\|CDD\|236864
NZ_CP034279.1\|WP_156691416.1\|1037062_1037902_+\|ABC-transporter-permease-subunit	unknown	unknown	gnl\|CDD\|223472
NZ_CP034279.1\|WP_156696203.1\|1051964_1053020_-\|oxidoreductase	unknown	unknown	gnl\|CDD\|226855
NZ_CP034279.1\|WP_156691414.1\|1034579_1035950_+\|extracellular-solute-binding-protein	unknown	unknown	gnl\|CDD\|270303
NZ_CP034279.1\|WP_156691417.1\|1037972_1039343_+\|beta-glucosidase	unknown	unknown	gnl\|CDD\|274539
NZ_CP034279.1\|WP_156696201.1\|1040363_1041341_+\|sphingomyelin-phosphodiesterase	unknown	unknown	gnl\|CDD\|132436
NZ_CP034279.1\|WP_156691428.1\|1053995_1055630_+\|ATP-binding-cassette-domain-containing-protein	unknown	unknown	gnl\|CDD\|223562
NZ_CP034279.1\|WP_156696202.1\|1048227_1049382_-\|CoA-transferase	unknown	unknown	gnl\|CDD\|224717
NZ_CP034279.1\|WP_156691424.1\|1049595_1050786_+\|saccharopine-dehydrogenase	unknown	unknown	gnl\|CDD\|225807
NZ_CP034279.1\|WP_156691422.1\|1045851_1047066_-\|acetyl-CoA-C-acetyltransferase	unknown	unknown	gnl\|CDD\|236197
NZ_CP034279.1\|WP_156691415.1\|1036100_1037066_+\|ABC-transporter-permease-subunit	unknown	unknown	gnl\|CDD\|224096
NZ_CP034279.1\|WP_156691423.1\|1047088_1048231_-\|acyl-CoA-dehydrogenase	unknown	unknown	gnl\|CDD\|173849
NZ_CP034279.1\|WP_156691418.1\|1039314_1040208_-\|DUF2236-domain-containing-protein	unknown	unknown	gnl\|CDD\|378343

Protein	Function_ID	Function_description	E-value
NZ_CP034279.1\|WP_156691420.1\|1042518_1043271_+\|MerR-family-transcriptional-regulator	gnl\|CDD\|197716	smart00422, HTH_MERR, helix_turn_helix, mercury resistance.	8.85648e-18
NZ_CP034279.1\|WP_156691426.1\|1051602_1051911_+\|hypothetical-protein	gnl\|CDD\|367663	pfam03795, YCII, YCII-related domain. The majority of proteins in this family consist of a single copy of this domain, though it is also found as a repeat. A strongly conserved histidine and a aspartate suggest that the domain has an enzymatic function. This family also now includes the family formerly known as the DGPF domain (COG3795). Although its function is unknown it is found fused to a sigma-70 factor family domain in CC_1329. Suggesting that this domain plays a role in transcription initiation (Bateman A per. obs.). This domain is named after the most conserved motif in the alignment.	2.42406e-17
NZ_CP034279.1\|WP_156691427.1\|1053350_1053767_+\|SsgA-family-sporulation/cell-division-regulator	gnl\|CDD\|377399	pfam04686, SsgA, Streptomyces sporulation and cell division protein, SsgA. The precise function of SsgA is unknown. It has been found to be essential for spore formation, and to stimulate cell division.	9.88314e-33
NZ_CP034279.1\|WP_156691419.1\|1041419_1042448_+\|cation-diffusion-facilitator-family-transporter	gnl\|CDD\|223131	COG0053, MMT1, Predicted Co/Zn/Cd cation transporters [Inorganic ion transport and metabolism].	1.12167e-78
NZ_CP034279.1\|WP_156691425.1\|1050831_1051521_-\|endonuclease-V	gnl\|CDD\|377374	pfam04493, Endonuclease_5, Endonuclease V. Endonuclease V is specific for single-stranded DNA or for duplex DNA that contains uracil or that is damaged by a variety of agents.	8.27754e-101
NZ_CP034279.1\|WP_156691412.1\|1030476_1031544_+\|substrate-binding-domain-containing-protein	gnl\|CDD\|224525	COG1609, PurR, Transcriptional regulators [Transcription].	8.12502e-97
NZ_CP034279.1\|WP_156691413.1\|1031555_1034339_-\|glycoside-hydrolase	gnl\|CDD\|227785	COG5498, ACF2, Predicted glycosyl hydrolase [Cell envelope biogenesis, outer membrane].	4.75703e-81
NZ_CP034279.1\|WP_156691421.1\|1043638_1045810_-\|3-hydroxyacyl-CoA-dehydrogenase	gnl\|CDD\|236864	PRK11154, fadJ, fatty acid oxidation complex subunit alpha FadJ.	2.30983e-156
NZ_CP034279.1\|WP_156691416.1\|1037062_1037902_+\|ABC-transporter-permease-subunit	gnl\|CDD\|223472	COG0395, UgpE, ABC-type sugar transport system, permease component [Carbohydrate transport and metabolism].	3.30382e-81
NZ_CP034279.1\|WP_156696203.1\|1051964_1053020_-\|oxidoreductase	gnl\|CDD\|226855	COG4447, COG4447, Uncharacterized protein related to plant photosystem II stability/assembly factor [General function prediction only].	2.68913e-21
NZ_CP034279.1\|WP_156691414.1\|1034579_1035950_+\|extracellular-solute-binding-protein	gnl\|CDD\|270303	cd13585, PBP2_TMBP_like, The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and similar oligosaccharides; possess type 2 periplasmic binding fold. This family includes the periplasmic trehalose/maltose-binding component of an ABC transport system and related proteins from archaea and bacteria. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is 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. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.	1.57272e-34
NZ_CP034279.1\|WP_156691417.1\|1037972_1039343_+\|beta-glucosidase	gnl\|CDD\|274539	TIGR03356, BGL, beta-galactosidase.	0
NZ_CP034279.1\|WP_156696201.1\|1040363_1041341_+\|sphingomyelin-phosphodiesterase	gnl\|CDD\|132436	TIGR03395, Sphingomyelinase_C, sphingomyelin phosphodiesterase. Members of this family are bacterial proteins that act as sphingomyelin phosphodiesterase (EC 3.1.4.12), also called sphingomyelinase. Some members of this family have been shown to act as hemolysins. [Cellular processes, Pathogenesis].	3.14271e-113
NZ_CP034279.1\|WP_156691428.1\|1053995_1055630_+\|ATP-binding-cassette-domain-containing-protein	gnl\|CDD\|223562	COG0488, Uup, ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only].	6.25657e-125
NZ_CP034279.1\|WP_156696202.1\|1048227_1049382_-\|CoA-transferase	gnl\|CDD\|224717	COG1804, CaiB, Predicted acyl-CoA transferases/carnitine dehydratase [Energy production and conversion].	2.37246e-108
NZ_CP034279.1\|WP_156691424.1\|1049595_1050786_+\|saccharopine-dehydrogenase	gnl\|CDD\|225807	COG3268, COG3268, Uncharacterized conserved protein [Function unknown].	3.08986e-59
NZ_CP034279.1\|WP_156691422.1\|1045851_1047066_-\|acetyl-CoA-C-acetyltransferase	gnl\|CDD\|236197	PRK08242, PRK08242, acetyl-CoA C-acetyltransferase.	0
NZ_CP034279.1\|WP_156691415.1\|1036100_1037066_+\|ABC-transporter-permease-subunit	gnl\|CDD\|224096	COG1175, UgpA, ABC-type sugar transport systems, permease components [Carbohydrate transport and metabolism].	8.34996e-82
NZ_CP034279.1\|WP_156691423.1\|1047088_1048231_-\|acyl-CoA-dehydrogenase	gnl\|CDD\|173849	cd01160, LCAD, Long chain acyl-CoA dehydrogenase. LCAD is an acyl-CoA dehydrogenases (ACAD), which is found in the mitochondria of eukaryotes and in some prokaryotes. It catalyzes the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of LCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. LCAD acts as a homodimer.	0
NZ_CP034279.1\|WP_156691418.1\|1039314_1040208_-\|DUF2236-domain-containing-protein	gnl\|CDD\|378343	pfam09995, DUF2236, Uncharacterized protein conserved in bacteria (DUF2236). This domain, found in various hypothetical bacterial proteins, has no known function. This family contains a highly conserved arginine and histidine that may be active site residues for an as yet unknown catalytic activity.	8.66105e-54

>NZ_CP034279.1|WP_156691420.1|1042518_1043271_+|MerR-family-transcriptional-regulator
MGTEATEPAESEERQPTLTVDELAARAGVTVRTIRFYGTRGLLPPPVIGPRRVGHYGPEHLSRLALIEELQHQGMTLAAIERYVEQLPPDLSAHDLAIHRALVATWAPDAPEEMSRAELERRAGRALGDEDVDRLAAMDVVARTGAGDTFRVDPGLLRLGLRLLDVPIAHETILASRTVLVEHTRSAAQELTRLFRDEVWGPYRERESDPEHVAAMKSLSAHMQPLVVQALVTAFQRSLKEELRAAFRAE
>NZ_CP034279.1|WP_156691419.1|1041419_1042448_+|cation-diffusion-facilitator-family-transporter
MTGQGHHHGEHRGRHHGHHHPHKHHHHHGERIDAALEGSAAGLRTLWFSFAVLAATTGVQAVVAALSGSVALLGDTVHNATDALTALPLALAFVLGRRAATRRYTYGFGRAEDLAGVFVVMVIAASAAFAGYEAVGRLLDPRDVDHLPAVAAAGLVGFAGNEWVARARIRTGRAIGSAALVADGLHARTDGFTSLAVLLGAGGAALGWWWADPLVGLVITAAILVVLRGAAREVWHRLMDAVDPALVDRAEHVLSHVEGVRGVGTVRMRWLGHALRAETSVVVDPSLTVVQAHAVAVAAEHALLHQVPRLAGATVHIDHAHPADADPHAALAHHSSRIDGRP
>NZ_CP034279.1|WP_156696201.1|1040363_1041341_+|sphingomyelin-phosphodiesterase
MQRAALSATLSAALTVVAVAAAGPAASAGTGAGTPALKVLSYNAFLFSKTLYPNWGQDHRAGAIPEASFFGGQDVVVLQEAFDNASSDALMRNAAARYPYQTPVMGRSKSGWDATSGAYSATTPEDGGVTVLSKWPIVRKEQYVYKDACGADWYSNKGFVYAVLNVDGARVHMVGTHAQSTDPGCDGGEAAAVRSRQFRAMDAFLDAKNIPASEQVLVAGDFNVDSHSGEYASMLSDAGLVDADARTGHPYSFDTQDNSIAAERYPDDPREDLDHVLHRAGHARPAGWTNRVVKEQSAPWTVSSWGKRYTYTNLSDHYPVVASAQ
>NZ_CP034279.1|WP_156691418.1|1039314_1040208_-|DUF2236-domain-containing-protein
MSTAPAPHDPPPPPPGGVLWSLAGDLRGLLMLPAAFTLQVAHPAVGAGVDEHSVFRTDPWGRGERSLRSLQLWVYGGEAAAEEGRRLRALHAGIRGTDTRGRRYHALTPANYAWVHATGFPVYHHAARYLIRPLTAAQERQLYAEWLQVGRVLGIHDRDMPQTIEEFWPYHRKVLAEEIEATAVARELVAADTPLPPFDRGPLPMRLIVRALWPLLLPAFARFRRFLTVGLMPPDARAAMGLEWTDEQERRLRRFGRLVRAVVPVLPERLRYLPLARRARARHREEQRLTRADRPGR
>NZ_CP034279.1|WP_156691417.1|1037972_1039343_+|beta-glucosidase
MDELTFPAGFRWGTATAAYQIEGAADEDGRTPSIWDTFSRTPGRVRNGDTGDIAADHYHRMAEDVALMKDLGVTDYRFSVAWPRVQPTGRGPAVQKGLDFYRRLVDELRAADIRPVATLYHWDLPQELEDAGGWPHRDTAERFAEYAGHVAAALGDRVATWTTLNEPWCVAFLGYASGVHAPGRTEAAASLRAAHHLNLAHGRAVQALRAALPRTAEVSLTLNVHALRALSGSEADRDALRRVDAVGNRIFLDPVFHGRLPEDLVADTAALTDWSFVRDGDLEVTATPVDSLGVNYYSPAVVGAGTSEAPSPWPGTEPHVRFVPAPGPRTAMDWPVDADGLYELLARLRDELPGTPLMVTENGAAYDDYADPSGEVHDPERVAYLRAHLAGVHRALADGVDVRGYFLWSLLDNFEWAYGYGKRFGIVHVDFASQRRTPKDSARWYADVIARGGLRG
>NZ_CP034279.1|WP_156691416.1|1037062_1037902_+|ABC-transporter-permease-subunit
MSARRAGRTLHGGRVAYAILVLAVLVSAFPFYWTIVAASRSNADLAKVPPSLLPGPNLIRNVEAVMEEADIGKALLNSLIVSGSITVGTVLCCTLAGFAFAKLRFRGRGALLAITVGTMMIPPQLGVIPLFMLIAELGWVNQLQSVILPGLVSAFGVFFMRQFLVQALPDELIEAARVDGASSARIFWSIVVPIARPGMAVLGLLTFMAAWNDFFWPIVALSSQNPTVQVALRQLGGGYVHDQSVIMAGTLLGTLPVLLVFGLLGRQIVGGIMQGAVKG
>NZ_CP034279.1|WP_156691415.1|1036100_1037066_+|ABC-transporter-permease-subunit
MKGRTVTLTAPAGSAAARRRPSAARRAWRTVSPYAYLTPFFTLFAAFGLFPLLYTAFVSLYRVELQTPGDMEWRGLGNYAALFTDEFFWISLRNTFTIGVISTVPQLVMALGLAHLLNYRLRGRTFFRTAMLLPYATSVAAATLVFAQLFGRDFGLVNYVLGVVGIGPVDWQTNTVASQIAVSTIVIWRWTGYNALIYLAGMQSIPSELYEAAEMDGASRWRQFFHVTLPGLRPTIVFTAVVSTIGATQLFGEPLLFEGSVSGGISHQYQTLGLYMYEQGWGFFHLGRAAAIAWVMFLLILVLVGVNALVMRRRSRKEAGR
>NZ_CP034279.1|WP_156691414.1|1034579_1035950_+|extracellular-solute-binding-protein
MPNARATGTPRTPAAQAAVHAGTAVRTGAAVRTRAVVRAGAAVLAGVLLAACGSGASGGASDGTVTLTVDLFGSFGYKEAGLYAEYEKLHPGIKIKQTDTEDEQDYWKSLQTRLAGGGGLADVQAIEVGRIASVTQAQPDKFEDLTRYGADKLKGEFAEAKWSAATTEDGRVLGLGTDVGPEAMCYRTDLFKQAGLPTDRAELARRWATWDGYLELGKQYQAKAPAKSAWLDSVGSLFTIMIGQEEERYYDASGKLIYESNPAVKTAWDTATEAADEGLSAKLDQWSPQWNQAFAAGSFATIPCPAWMLGYIKGQAGEAGKGKWDIAKLPGGAGNWGGSYLSVPRAAKHKKEAYELIQWLTAPEQQARLFEKQGNFPSSTGAIAKVADAKDPYFSGAPIGQIFGDAAKAAPVQVLGVHDKNVADQITNALSEVERKGTSPDKAWSNAKKGVENVTG
>NZ_CP034279.1|WP_156691413.1|1031555_1034339_-|glycoside-hydrolase
MPSPRTRPAALLLATTLAALGLTATTATPAAAATVPVGAGGYSDTRPPGTSGPTTNTGTPVTPKLTPAAQGKPVPTNDWWSSLAFQRYGDNPWSTPMYGHPLTYQATAAGLDVGYPTTPAIVGDGRQYEYAHKRDLTLGLTGLNSPDTKADAWSDWTVTPYWSDGTRTLRTTIGHGSPFVYAKGTGGDARITTATAPTVFADQGNVLGITVSGHHYALFAPTGADWTVSGSTLTAGLGGRDYFSVAVMPSPDALATYRTYAYSFVTGSKAEWSYTGGTVRATYTLTTQPQEGTQTGTLQALYRHQWLHTTDALTPYTYVSPRGTMKVRASTSFTTSQRAAAVLPALPKSSGVDAARLRGYLTEAANAADPFQGATDTYWTGKALGRLAQLVPLAEQAGETATRDKLLGLIKGRLQDWFTAGGANEFSYDRTWRTLTGYPASYGSDTELNDHHFHYSYYVYAAAIVAQYDPAWATGSAWGGMVKTLVRDAANPSRTDSAFPFLRGFDVYAGHSWASGHQGFAAGNNQESSSESTNLSAGLVLWGSATGDTALRDLGVYLLTTEAEAIAQYWFDADQQVFPASFGHETAGMVWGSGAAYATWWTANPEEIHGINVLPVTGGSLHLGGEKAAVRRNVAEMERENGGPAVEWRDILWEFQSFADPAAARAKWDVGHASYTPEAGESKAHTYHWLTTLDALGAPDATVSGDIPTSAAFTKGTVRTYAAHNHGSTARTVTFSDGAKLTVPARSTATGTGTGGPGPDPDPDPGPGTGDTFQLRTGGTLTTATGATAGSDTIASAGGANHDGTPHQPLVYEAKGVNGTLKPGGATAFRLQVDAGTTVGLGQQARVSYDLTGDGTFDRTETYHYFATDPVPGWEEYGQARGLRSATGTLGDLKGGTVRLEVWHAIGSGTARLQTGTDRSVLVIPYA
>NZ_CP034279.1|WP_156691412.1|1030476_1031544_+|substrate-binding-domain-containing-protein
MSRKPDPAPGSRPTLEAVAARAGVSRATASRVVNGGAGVRPPLVDKVRRAVEELGYVPNHAARTLVTRRNGAVAVIIAEPEFRIFSDPFFEQQVRGISRELTAHDSQLVLLWVEGPGDYDRIGRYLGGGHVDGALAFSVHNDDGLPSIIGRAQVPAVFGGRPGWPGASGTPGGPAVPYVDADNRGGAREAVRHLLSLGRERVAHIAGPRDLTSAMDRVDGYRDVLLDADPGLIAQGDFTEESGARAMAELLARRPDLDAVFAASDLMASGALRVLRERGLRVPEDVALVGFDDMTSISEATDPPLTTVRQDVEGMGRLMVRLLMRVLNGQETEPGTGSAPGSVITPTELVRRASA
>NZ_CP034279.1|WP_156691421.1|1043638_1045810_-|3-hydroxyacyl-CoA-dehydrogenase
MSQSTTIRWEQDETGVVTLVLDDPDQSANTMNQAFRTSIAAVADRAEAEKDSIRGFVYTSAKKTFFAGGDLKDMMKAGPADARQIFEAGMEMKRALRRIETLGKPVVACLNGAALGGGYEIALASHHRIALDAPGSKIGLPEVTLGLLPGGGGVTRTVRLMGIADALLKVLLQGTQYSPRRALENGLVHEVATTPEEMAAKARAFIDAHPESQQPWDAPGYRIPGGTPAHPKFAANLPAFPANLKKQINGAPYPAPRNILAAAVEGSQVDFETALTIESRYFTELVTGQTAKNMIQAFFFDLQAVNSGASRPRGVEPRKVRRVAVLGAGMMGAGIAYSCARAGIEVVLKDVSAEAAEKGKAYSAKLLDKALSRGRTTEAQRDELLARITPTADPADLAGCDAVIEAVFEDTALKHKVFQEIQEIVEPDALLCSNTSTLPITLLSEGVDRPADFIGLHFFSPVDKMPLVEIIRGERSGDEALARAFDLVRQINKTPIVVNDSRGFFTSRVIGQFINEGVAMVGEGVDPASVEQAAAQAGYPAKVLSLMDELTLTLPRKIRNESRRAIEEAGGTWTEHPAEAVIDRMVDEFGRPGRSGGAGFYDYDETGGRTGLWPGLREHFAGEGATVPFEDMKERMLFSEALDTVRCLEEGVLTSVADANIGSIMGIGFPAWTGGVLQYVNGYEGGLPGFVARARELAERYGERFQPPALLVEKAERGERFGD
>NZ_CP034279.1|WP_156691422.1|1045851_1047066_-|acetyl-CoA-C-acetyltransferase
MSTEAYVYDAIRTPRGRGKANGALHGTKPIDLVVGLIHELRGRFPGLDPAAIDDIVLGVVEPVGDQGSDIARIAAIAAGLPDTVAGVQENRFCASGLEAVNMAAMKVRSGWEDLVLAGGVESMSRVPMASDGGAWFADPMTNWDTNFVPQGIGADLIATLGGYTRRDVDEYAALSQERAAAAWKDGRFDRSVVPVKDRAGLVVLDHDEHMRPGTTADSLASLKPSFAAVGEMGGFDAVALQKYHWVEKIDHVHHAGNSSGIVDGAALVAIGNKEVGERYGITPRARVVSVAVSGSEPTIMLTGPAPASRKALAKAGLTADDIDLVEINEAFAAVVLRFAADMGLPLDKVNVNGGAIAMGHPLGATGAMILGTLVDELERQDKRYGLATLCVGGGMGIATVVERV
>NZ_CP034279.1|WP_156691423.1|1047088_1048231_-|acyl-CoA-dehydrogenase
MKRRIFEAEHDAFRETVRTFLAKEVLPHYEQWEKDGIVSREAWLAAGRQGLLGIAVPEEYGGGGNTDFRYSAVLAEEFTRAGAPGLAIGLHNDIIGPYLTSLGTDEQKRRWLPGFCTGEIITAIAMTEPGAGSDLQGIRTTAEDRGDHWLLNGSKTFISNGILADLVVVVAKTTPEGGAHGLSLLVVERGADGFERGRNLDKIGQKSQDTAELFFHDVRVPKENLLGELNGAFVHLMTNLAQERLNIAVAGIAAAEHLLEITTAYVKEREAFGRPLARLQHIRFEIAEMATECAVTRAFLDRCVVDHANGELDAVHASMAKWWATELQKRVADRCLQLHGGYGYMAEYPVAKAFTDGRIQTIYGGTTEIMKEIIGRSLLG
>NZ_CP034279.1|WP_156696202.1|1048227_1049382_-|CoA-transferase
MRVVELAGIGPGPFAAMLLGDLGADVVRVDRPGGAGLAIDPAYDLTNRNKRSVLVDLKADGGPDRVLDLVERADVLIEGYRPGVAERLGVGPEECLARNPKLVYGRMTGWGQDGPLAQRAGHDIAYIAVTGTLSMIGRADEPPTVPANLVGDYAGGSLYLVVGVLAALHHAREEGGGGQVVDAAITDGAAHLATMIHGMMAAGGWQDRRGANLLDGGCPFYGTYETADGQYMAVGALEQRFYDEFVRLLGIEDTAPARKDFDRWDDLRAAVAARFKDRTRAEWTAVFEGSDACVAPVLSLREAPAHPHLAARATFTDHGGITQPAPAPRFSATPGSVTRPPARPGAGTDEVARDWDVPSLRTDDARSQDARTEDARSDNDRGTG
>NZ_CP034279.1|WP_156691424.1|1049595_1050786_+|saccharopine-dehydrogenase
METRDGTERTYDVVLFGATGFVGELTARYLATHAPATCRWALAGRSLDKLERLRDRLAAEHPRCADLPLVTADAADRDSMRTLAKSARVVATTVGPYVWYGEPLVAACAEAGTDYVDLTGEPEFVDLMYVRHDARARETGARIVHACGFDSVPHDLGVYFTVAQLPGDVPLAVDGFVRSNAFFSGGTFASALTAMARGRHMARAARERRLHEPRLVGRRARAPLAAPRFSRETGAWALPLPTLDASVVARSAAALPQYGPDFRYRHYAAVRTLPMALGGTAAMGGLFALAQVPPARRWLMDRYEAGQGPDEERRARSWFTVRFVGEGGGRRVFTEVSGGDPGYDETAKMLAESALSLAFDDLPKTAGQLTTAVAMGDALLERLTRAGIRFRVADSR
>NZ_CP034279.1|WP_156691425.1|1050831_1051521_-|endonuclease-V
MTIIEIPADWPADEAEALAVQDELRGRVVLDEPGPAPGTGLVTGVDVAYDDERDLVAAAAVVLDARTLTVVEEATAVGRVSFPYVPGLLAFREVPTVLAALAALRGGPGLVVCDGYGRAHPRRFGLASHLGVLTGLPVIGVAKNPFTFTYEQPARERGAAAPLVADGEEVGRALRTREGVKPVFVSAGHRVTLDNACAHTLHLTPRYRIPETTRHADALCRRALKAITA
>NZ_CP034279.1|WP_156691426.1|1051602_1051911_+|hypothetical-protein
MFVLELTYTGPLERVDKLLADHVAWLDGHYASGLFLASGRKEPRDGGIILADGEDRARIEEVTATDPFVTAGVCAYRVTEFIATRTAPELARYRRPLPAAPH
>NZ_CP034279.1|WP_156696203.1|1051964_1053020_-|oxidoreductase
MPAGSTTTAPGRAAPRATGPSWRLKETGAQARFRGLAAVSRSTAWVAGSGGTVLRTGDGGRSWRNVSPAGATGLEFRDIEAFDGRRAVVLAIGEGEASRILRTDDGGASWTESFRNPDPRAFYDCVTFFDSRHGLAMSDPVDGRYRILSTGDGGRSWTVLPTAGMPEALPGEAGFAASGQCLVSSGPRDVWLATGGGATARVLHSSDRGRNWTVAESTIPAGDPVRGVFALAFRDRTHGIAVGGDYRTGQPSPRAGAVSRDGGRTWRQAHTPPPAYRSGVAWLPHSRSAALAVGPTGTDLTTDGGRTWRTVDTGSYDTVDCAAGPAYGPPSSRASGCWAAGEKGRVARLER
>NZ_CP034279.1|WP_156691427.1|1053350_1053767_+|SsgA-family-sporulation/cell-division-regulator
MSTVIEQALQARLVASSPQRETVAATLRYDRRNPFAVQMAFPAPATLEGIDVSWEFSRELLAAGVDEPAGLGDVRVRPFGYDRTVVEFHAPEGVAMVHIRTSEVRRFLERARHLVPEGREHEFLDLDQDLAQLMRDAC
>NZ_CP034279.1|WP_156691428.1|1053995_1055630_+|ATP-binding-cassette-domain-containing-protein
MSTFPTSITCTDLSFAWPDGTPVLEDFQLAVGPGRTGLIGLNGSGKSTLLKLIAGELAPTDGTIRTAGEIGYLPQNATLDTALRVDQALGIAATRAALHAIEGGDASEEHFTAIGDDWDVEERARATLDQLGLGHIGLDRTIGEVSGGECVLLRLAALLLARPDVLLLDEPTNNLDLSARRRLYAAVSSWSGVLVVVSHDRELLELVDQIADLRDGEVTWYGGAYSAYEEALAAEQEAAERMVRVAEADVQRQKRELADAHVKLARRKRYGQKMFDSKREPKIVMNARKRAAQESAGKHRTMHTQKLAEAKERLDEAVEAVRDDDEIRIELPFTAVPPGRDVLLLRDLELRYGARVGGEWELRGPERIALVGRNGAGKTTLLRTVAGELDPVAGEVVAQVPLRFLPQRLDVLDDDLSVVDNVARFAPEATNNRIRARLARFLFRGAKADQPAGTLSGGERFRAALAALLLAEPAPQLLMLDEPTNNLDMASVAKLTAALDAYEGALIVASHDVPFLESIGITRWLLLEGGELRATTAEEVLAGP

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Crispr_ID: NZ_CP034279_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP034279_2

1581285-1581379

Orphan

Consensus_repeat	Method
CCCGCCACCGCCGCCGGCGCGGCAC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP034279_2

>merge|NZ_CP034279|2|1581285-1581379|CRISPRCasFinder
CCCGCCACCGCCGCCGGCGCGGCACCACGGGGACGTGGTGGGCGCCGGGGCGGGGCGGCCGTGACGCTCGCCCACCACCGCCGCCGGCGCGGCAC

>NZ_CP034279|2|2|1581285-1581379|CRISPRCasFinder
CCCGCCACCGCCGCCGGCGCGGCAC	CACGGGGACGTGGTGGGCGCCGGGGCGGGGCGGCCGTGACGCTCG
CCCACCACCGCCGCCGGCGCGGCAC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP034279.1\|WP_156691845.1\|1587074_1587545_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP034279.1\|WP_156691838.1\|1577235_1578699_-\|amino-acid-permease	unknown	unknown	gnl\|CDD\|129987
NZ_CP034279.1\|WP_156691837.1\|1575588_1576416_-\|enoyl-CoA-hydratase-family-protein	unknown	unknown	gnl\|CDD\|181329
NZ_CP034279.1\|WP_156691832.1\|1569205_1569604_-\|RidA-family-protein	unknown	unknown	gnl\|CDD\|100004
NZ_CP034279.1\|WP_156691834.1\|1570815_1572447_+\|AMP-binding-protein	unknown	unknown	gnl\|CDD\|341268
NZ_CP034279.1\|WP_156691847.1\|1588047_1589214_-\|ATP-binding-protein	unknown	unknown	unknown
NZ_CP034279.1\|WP_156691840.1\|1579969_1581208_-\|arginine-deiminase	unknown	unknown	gnl\|CDD\|234949
NZ_CP034279.1\|WP_156691839.1\|1578856_1579873_-\|ornithine-carbamoyltransferase	unknown	unknown	gnl\|CDD\|179366
NZ_CP034279.1\|WP_156691848.1\|1589288_1589687_-\|cell-division-protein-SepF	unknown	unknown	gnl\|CDD\|377370
NZ_CP034279.1\|WP_156691835.1\|1572456_1573284_+\|PaaX-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|225864
NZ_CP034279.1\|WP_156696252.1\|1576907_1577264_+\|ATP-binding-protein	unknown	unknown	gnl\|CDD\|340413
NZ_CP034279.1\|WP_156691841.1\|1581454_1584004_-\|polynucleotide-kinase-phosphatase	unknown	unknown	gnl\|CDD\|274963
NZ_CP034279.1\|WP_156691846.1\|1587670_1588051_-\|nucleotide-pyrophosphohydrolase	unknown	unknown	gnl\|CDD\|212144
NZ_CP034279.1\|WP_156691843.1\|1585543_1586467_-\|TIGR03560-family-F420-dependent-LLM-class-oxidoreductase	unknown	unknown	gnl\|CDD\|274648
NZ_CP034279.1\|WP_156691842.1\|1584000_1585467_-\|3'-terminal-RNA-ribose-2'-O-methyltransferase-Hen1	unknown	unknown	gnl\|CDD\|274962
NZ_CP034279.1\|WP_167536350.1\|1573252_1575592_-\|bifunctional-salicylyl-CoA-5-hydroxylase/oxidoreductase	unknown	unknown	gnl\|CDD\|236203
NZ_CP034279.1\|WP_156691833.1\|1569600_1570719_-\|acyl-CoA-dehydrogenase	unknown	unknown	gnl\|CDD\|173847
NZ_CP034279.1\|WP_156691849.1\|1590021_1591287_+\|extracellular-solute-binding-protein	unknown	unknown	gnl\|CDD\|270303
NZ_CP034279.1\|WP_156691844.1\|1586692_1586902_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP034279.1\|WP_156696253.1\|1591514_1592429_+\|ABC-transporter-permease-subunit	unknown	unknown	gnl\|CDD\|224096

Protein	Function_ID	Function_description	E-value
NZ_CP034279.1\|WP_156691838.1\|1577235_1578699_-\|amino-acid-permease	gnl\|CDD\|129987	TIGR00909, putative_amino_acid_transporter, amino acid transporter. [Transport and binding proteins, Amino acids, peptides and amines].	2.03675e-130
NZ_CP034279.1\|WP_156691837.1\|1575588_1576416_-\|enoyl-CoA-hydratase-family-protein	gnl\|CDD\|181329	PRK08258, PRK08258, enoyl-CoA hydratase family protein.	1.598e-142
NZ_CP034279.1\|WP_156691832.1\|1569205_1569604_-\|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.	1.86797e-24
NZ_CP034279.1\|WP_156691834.1\|1570815_1572447_+\|AMP-binding-protein	gnl\|CDD\|341268	cd05958, ABCL, 2-aminobenzoate-CoA ligase (ABCL). ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.	0
NZ_CP034279.1\|WP_156691840.1\|1579969_1581208_-\|arginine-deiminase	gnl\|CDD\|234949	PRK01388, PRK01388, arginine deiminase; Provisional.	0
NZ_CP034279.1\|WP_156691839.1\|1578856_1579873_-\|ornithine-carbamoyltransferase	gnl\|CDD\|179366	PRK02102, PRK02102, ornithine carbamoyltransferase; Validated.	0
NZ_CP034279.1\|WP_156691848.1\|1589288_1589687_-\|cell-division-protein-SepF	gnl\|CDD\|377370	pfam04472, SepF, Cell division protein SepF. SepF accumulates at the cell division site in an FtsZ-dependent manner and is required for proper septum formation. Mutants are viable but the formation of the septum is much slower and occurs with a very abnormal morphology. This family also includes archaeal related proteins of unknown function.	6.43657e-22
NZ_CP034279.1\|WP_156691835.1\|1572456_1573284_+\|PaaX-family-transcriptional-regulator	gnl\|CDD\|225864	COG3327, PaaX, Phenylacetic acid-responsive transcriptional repressor [Transcription].	4.19958e-40
NZ_CP034279.1\|WP_156696252.1\|1576907_1577264_+\|ATP-binding-protein	gnl\|CDD\|340413	cd16936, HATPase_RsbW-like, Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase involved in regulating sigma-B during stress in Bacilli, and related domains. This family includes histidine kinase-like ATPase (HATPase) domain of RsbW, an anti sigma-B factor as well as a serine-protein kinase involved in regulating sigma-B during stress in Bacilli. The alternative sigma factor sigma-B is an important regulator of the general stress response of Bacillus cereus and B. subtilis. RsbW is an anti-sigma factor while RsbV is an anti-sigma factor antagonist (anti-anti-sigma factor). RsbW can also act as a kinase on RsbV. In a partner-switching mechanism, RsbW, RsbV, and sigma-B participate as follows: in non-stressed cells, sigma-B is present in an inactive form complexed with RsbW; in this form, sigma-B is unable to bind to RNA polymerase. Under stress, RsbV binds to RsbW, forming an RsbV-RsbW complex, and sigma-B is released to bind to RNA polymerase. RsbW may then act as a kinase on RsbV, phosphorylating a serine residue; RsbW is then released to bind to sigma-B, hence blocking its ability to bind RNA polymerase. A phosphatase then dephosphorylates RsbV so that it can again form a complex with RsbW, leading to the release of sigma-B.	3.02205e-20
NZ_CP034279.1\|WP_156691841.1\|1581454_1584004_-\|polynucleotide-kinase-phosphatase	gnl\|CDD\|274963	TIGR04075, Ser/Thr_phosphatase_family_protein, polynucleotide kinase-phosphatase. Members of this protein family are the bacterial polynucleotide kinase-phosphatase (Pnkp) whose genes occur paired with genes for the 3' terminal RNA ribose 2'-O-methyltransferase Hen1. All members of the seed alignment belong to a cassette with the Hen1. The pair acts in bacterial RNA repair. This enzyme performs end-healing reactions on broken RNA, preparing from the RNA ligase to close the break. The working hypothesis is that the combination of Pnkp (RNA repair) and Hen1 (RNA modification) serves to first repair RNA damage from ribotoxins and then perform a modification that prevents the damage from recurring. [Transcription, RNA processing].	0
NZ_CP034279.1\|WP_156691846.1\|1587670_1588051_-\|nucleotide-pyrophosphohydrolase	gnl\|CDD\|212144	cd11537, NTP-PPase_RS21-C6_like, Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in mouse RS21-C6 protein and its homologs. RS21-C6 proteins, highly expressed in all vertebrate genomes and green plants, act as house-cleaning enzymes, removing 5-methyl dCTP (m5dCTP) in order to prevent gene silencing. They show significant sequence similarity to the dimeric 2-deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTP pyrophosphatase or dUTPase) and NTP-PPase MazG proteins. However, unlike typical tandem-domain MazG proteins, RS21-C6 contains a single MazG-like domain and functions as a tetramer (a dimer of dimers) with a typical four-helical bundle. Divalent ions, such as Mg2+, are required for its pyrophosphatase activity. This family also includes a pyrophosphatase from Archaeoglobus fulgidus (Af1178). Although its biological role remains unclear, Af1178 shows significant sequence similarity to the mouse RS21-C6 protein.	1.32635e-40
NZ_CP034279.1\|WP_156691843.1\|1585543_1586467_-\|TIGR03560-family-F420-dependent-LLM-class-oxidoreductase	gnl\|CDD\|274648	TIGR03560, F420_Rv1855c, probable F420-dependent oxidoreductase, Rv1855c family. Coenzyme F420 has a limited phylogenetic distribution, including methanogenic archaea, Mycobacterium tuberculosis and related species, Colwellia psychrerythraea 34H, Rhodopseudomonas palustris HaA2, and others. Partial phylogenetic profiling identifies protein subfamilies, within the larger family called luciferase-like monooxygenanases (pfam00296), that appear only in F420-positive genomes and are likely to be F420-dependent. This model describes one such subfamily, exemplified by Rv1855c from Mycobacterium tuberculosis. [Unknown function, Enzymes of unknown specificity].	2.29093e-112
NZ_CP034279.1\|WP_156691842.1\|1584000_1585467_-\|3'-terminal-RNA-ribose-2'-O-methyltransferase-Hen1	gnl\|CDD\|274962	TIGR04074, Methyltransferase_type_12, 3' terminal RNA ribose 2'-O-methyltransferase Hen1. Members of this protein family are bacterial Hen1, a 3' terminal RNA ribose 2'-O-methyltransferase that acts in bacterial RNA repair. All members of the seed alignment belong to a cassette with the RNA repair enzyme polynucleotide kinase-phosphatase (Pnkp). Chemically similar Hen1 in eukaryotes acts instead on small regulatory RNAs. [Transcription, RNA processing, Protein synthesis, tRNA and rRNA base modification].	0
NZ_CP034279.1\|WP_167536350.1\|1573252_1575592_-\|bifunctional-salicylyl-CoA-5-hydroxylase/oxidoreductase	gnl\|CDD\|236203	PRK08255, PRK08255, bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase.	0
NZ_CP034279.1\|WP_156691833.1\|1569600_1570719_-\|acyl-CoA-dehydrogenase	gnl\|CDD\|173847	cd01158, SCAD_SBCAD, Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA dehydrogenases. Short chain acyl-CoA dehydrogenase (SCAD). SCAD is a mitochondrial beta-oxidation enzyme. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of SCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. This subgroup also contains the eukaryotic short/branched chain acyl-CoA dehydrogenase(SBCAD), the bacterial butyryl-CoA dehydorgenase(BCAD) and 2-methylbutyryl-CoA dehydrogenase, which is involved in isoleucine catabolism. These enzymes are homotetramers.	9.90752e-97
NZ_CP034279.1\|WP_156691849.1\|1590021_1591287_+\|extracellular-solute-binding-protein	gnl\|CDD\|270303	cd13585, PBP2_TMBP_like, The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and similar oligosaccharides; possess type 2 periplasmic binding fold. This family includes the periplasmic trehalose/maltose-binding component of an ABC transport system and related proteins from archaea and bacteria. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is 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. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.	4.42311e-70
NZ_CP034279.1\|WP_156696253.1\|1591514_1592429_+\|ABC-transporter-permease-subunit	gnl\|CDD\|224096	COG1175, UgpA, ABC-type sugar transport systems, permease components [Carbohydrate transport and metabolism].	3.29523e-93

>NZ_CP034279.1|WP_156691840.1|1579969_1581208_-|arginine-deiminase
MGFHVDSETGRLRRVILHRPDLELKRLTPSNKDALLFDDVLWVRRARQEHDGFADVLRDRGVEVHLVGDLLSEALEVPAARDLVLDRVFDEKEYGPLATGHIRAVFDAMDTATLVEVLIGGMTKRDFLAGHAEPTSVRFHVMDLDDFLVPPLPNHLFTRDTSAWIYDGVSINAMRWPARQRETVHFEAIYKHHPLFTGPEAGPFHHWSEGQDDYPSTIEGGDVLVIGRGAVLIGMSERTTPQAVEMLARGLFAAGSARTIVALDMPKSRAFMHLDTVMTMVAHDTFTQYAGLGMLRSYTIEPGDGHRALKVTDHPPQHMHSAIAAALDLPAIRVLTATQDVHAAEREQWDDGCNVLAVEPGVVVAYERNVTTNTHLRKEGIEVIEIPGSELGRGRGGPRCMSCPVMREADPG
>NZ_CP034279.1|WP_156691839.1|1578856_1579873_-|ornithine-carbamoyltransferase
MATDLTGRHFLKELDFTAEEFRSLLDLAAELKAAKRAGTEERRLRGRNIALIFEKSSTRTRCAFEVAAADQGASTTYLDPAGSHIGKKESARDTARVLGRMFDAIEFRGDAQATVEELAAHAGVPVYNGLTDDWHPTQMLADVLTMTEHTDKPLETIAFAYLGDGRYNMGNSYLVTGALLGMDVRIVAPRSYWPADGVVARARELAETSGARVTLTEDIAEGVRGADFVATDVWVSMGEPQEVWDERIGALAPYAVTMDVLRATGNPDVRFLHCLPAFHDLGTAVGREIHERHGLTELEVSDEVFESEHSVVFDEAENRLHTIKAVMVATLAGPGGAA
>NZ_CP034279.1|WP_156691838.1|1577235_1578699_-|amino-acid-permease
MRPTGPPRIKTPAQLIADSGADLEGHGLKRTMGLFQLVCFGVGAIVGTGIFVGLSDSVAEAGPAVVVSFILAAITCIFTAFSFAELGSAIPVSGSSYSFAYATLGERVAFLVGWCLLLEYGVSVSAVAVGWGQYLNELLDSLVGWQLPEALAGPPGDGGTVNIPAVIVIGLAAVLLVRGIRESARATAVMAIVKILILVLFCAIAFRAYQSDNLTPFATHGLAGVTSGASVAFFSYIGFDAITTAGEEVKNPRKNIPLAIMICIGIVTLLYCLVAVAAIGALSADEVADQPAALSLIVDRVTESGVGGGIIAFGAVVAIASVVLAVMYGQTRILMSMSRDGLIPHVFEKISPKTSTPVANTWIVAGVFAVPAAVVPLDVVLNLTTIGTLAIMVAVNIAVIALRRRYPDTESGFRVPLYPLSPVLGVAMCLYLIWGTGWTTWVQFAVFLVVGVLVYALYGRRHSRLGRDLARGEAADGGVTGPAGPGA
>NZ_CP034279.1|WP_156696252.1|1576907_1577264_+|ATP-binding-protein
MARALIRTALADLDASAYRDTAELLTAELVANAVEHTAGKGPIELVVRRLAGGCRVEVHDRDPEPPGDLTTWDDTPPDPWQEHGRGLLLIRALSAACGHRRTDGGKAVWFTLPDLRAP
>NZ_CP034279.1|WP_156691837.1|1575588_1576416_-|enoyl-CoA-hydratase-family-protein
MSPFISSAPRTQEWRHLRLAIDDGVATVTFARPAKLNALTFGAYADLRDLLAELSRERAVRALVLAGEGRGFCSGGDVDDIIGATLSMDTAQLLDFNRMTGQVVRALREAPFPVIAAVHGVAAGAGAVLALAADFRIADPSARFAFLFTKVGLSGGDMGAAYLLPRVVGLGHATRLLMLGEPVRAPEAERIGLISELTEEGAADTRAAELARRLADGPALAHAQTKALLTAELDMPLAASVELDAATQALLMNGEDYAEFHAAFTEKRPPKWRGR
>NZ_CP034279.1|WP_167536350.1|1573252_1575592_-|bifunctional-salicylyl-CoA-5-hydroxylase/oxidoreductase
MSRRAPGAPRRDPRPGRALRVAVVGGGPGGLYAAALLKRLDPDRDITVWERNAPDDTFGFGVVLSDETLGGIEHADPAVYAALQAEFVRWDDIDIVHRGRVLTSGGHGFAALGRRRLLEILHERCAALGVRLRFRTEAPPAAELAASHDLVIAADGVHSRTREAHADVFEPHLTTHRCRYIWLAADFAFDAFRFEIAETEHGVMQLHGYPFSASASTVIVEMREEVWRAAGFDELDEQESVARCAKIFAEALQGRPLASNHSSWTAFRTVVTGRWSHGNVVLLGDAAHTAHFSIGSGTKLAVEDALALAACVQEQPGLPEALAAYEAERRPVVESTQRAAAASLRWFEDLAGHLDQPPRQFAFNLLTRSRRVTHDNLRLRDPRFTDAVERDFGCPPGTPPMFTPFRLRGLTLRNRVVVSPMDMYSAVDGVPGDFHLVHLGGRALGGAGLVMTEMVCVSPEGRITPGCAGLWTPGQAAAWRRVTDFVHHQSPGTAIGVQLGHSGRKGSTRLMWEGIDQPLDSGNWPLVAASPLPYRPGVNQVPHELHRAALTDIREQFAAAARRAARADFDLLELHCAHGYLLSGFLSPLTNRRTDAYGGSLAARLRFPLEVFDAVRAAWPGERPMTVRISATDWAPGGTTAEEAVEIARAFAEHGADAIDVSTGQVVPDERPEYGRSYQTPYADRIRNALKVPVIAVGAISSWDDVNSLLLAGRADLCALARPHLYDPHWTLHAAADQGYEGPGAPWPLPYRAGSRKPPTGRTDAPKPRLSLTPRPPRP
>NZ_CP034279.1|WP_156691835.1|1572456_1573284_+|PaaX-family-transcriptional-regulator
MAEQHTPRSLIVSLYGAYGRTPDNAPLPVAELIRLLAALGVDAPSVRSSVSRLKRRGLLEPRRTSDGAAGYALSGDARQLLDDGDRRIYAAGEPHEDEGWVLAVFSVPEAERHKRHLLRSRLARLGFGTAAPGVWIAPAALYEETRHTLQRLQLDPYVDLFRGEHLGFPATAEAVGRWWDLAAIAKLYEEFLDLHEPVLRAWSTREPSPEEAYRDYLLALDSWRRLPYADPGLPAALLPAGWPGGRAATVFGGLHGLLRDRGEEYVRAGAGGASD
>NZ_CP034279.1|WP_156691834.1|1570815_1572447_+|AMP-binding-protein
MELTPSAHRDTFARDHLPPREQWPELLFDLPGLRYPDRLNCGRELLDRTVERFGASRPVFRDGAGQVWTYGELRTRVDRIAHTLTHDLGVVPGNRVLLRGPTTPWLAACWLAVMKAGAVAVTVLAGARAGELAVMCEMARVSHALCDVRAVDDLVKAEVPGLRVTAYGGDGPDDLLHLAARHRGPYEAVDTAADDVALIAFTSGTTGRPKGCMHFHRDVLAVADTFSEHVLRPGPDDLFAGSPPLGFTFGLGGLVIFPMRAGASALLLEQAGPRQLLAAVAEHRVTVLFTAPTAYRVMLDELDGHDTTSLRRCVSAGENLPEATWRAWFDRTGLRLINGIGATELLHIFVSAADAAIRPGTTGTPVPGWHARVVDDCGEPVPDGQEGLLAVRGPVGCRYLADPRQAEYVRHGWNVTGDTYVREPDGYLRYVARADDMIISAGYNIAGPQVEEALLAHPDVLEAAVVGRPDEVRGQVVVAYTVLRDGLPRDETTAEELRAFVKDRLVPYKCPRRIVFLDALPRTATGKLQRFRLRAEDTPRTRP
>NZ_CP034279.1|WP_156691833.1|1569600_1570719_-|acyl-CoA-dehydrogenase
MPVFSLDPEQTARCAELRATAAERLRPLADKGEPGHVNRPLVAALGELGLIGRLFDAGALDLCLMRESLAQACTEAETALALQGLGAHPVAASGTAAHRARWLPEVTAGRAVAAFALSEPDAGSDAAALALEAVPVSEGGGWRLAGEKRWISNAPEADFYTVFARTTPGAGARGVTAFLVPADRPGLTGSPLDMLSPHPIGSLLFDGVPVWPEDVLGEVDRGFRVAMTTLNRFRPSVGAFAVGMAQAALDATLAHTAGRRAFGGPLKDLQAVAHQVAEMATRTEAARLLVYAAAAAYDEGAPDVPQRAAMAKLLATETAQYVVDAAVQLHGARALQRGHLLEHLYREVRAPRIYEGATEVQRTIIAKELYAS
>NZ_CP034279.1|WP_156691832.1|1569205_1569604_-|RidA-family-protein
MSLERLNPAELSPPTGFSHAVTATGSRLVFLAGQTALDGSGRVVGETLPEQFETALGNLLAALKAAGGTPADLARVTVYATDVADYRERAPELGRVWRRLAGRDYPAMAVIGATRLWDEQALVELDGFAVLD
>NZ_CP034279.1|WP_156691841.1|1581454_1584004_-|polynucleotide-kinase-phosphatase
MTGTTTTGEHRVLPVTDLSLVVLVGATGSGKSTFARKHFKPTEVVSSDFCRGLVADDENDQSASGDAFDLLHTIVGKRLAAGRLTVVDATSVQQESRRQLVRLAREHDVLPIAIVLDMPEEVCAERNAARPDRAHLPRHVIQRHRRELRRSLRGLEREGFRKVHVLRSVAEAESAEVVLEKRYNDLRHLTGPFDIIGDIHGCSSELETLLAKLGYVDGTHPEGRTAVFVGDLVDRGPDSPGVLRRVMGMVASGDALCVPGNHENKLGRWLKGRQVQRTHGLAETIAQLEGESEEFRTRVREFIDGLVSHYVLDEGRLVVCHAGLPEKYHGRTSGRVRSHALYGDTTGETDEFGLPVRYPWAEDYRGRAAVVYGHTPVPSTSWINNTICLDTGAVFGGRMTALRWPERELVDVPAEKVWYEPVKPLATDAPGGHQGRPLDLADVHGRRVVETRYAGHVAVREENAAAALEVMSRFAVDPRLLAYLPPTMAPTPTSREEGFLEHPAEAFAQYCSDGVERVVCEEKHMGSRAVALVFRDADAARERFGVEGATGALHTRTGRPFFTDGALTELVLDRLRRAIDAAGLWDELTTDWLLLDGELMPWSLKASGLLRSQYAAVGAASGAVFPPVLAALESAVGRDVDVTGLLGRQRERAADAAAFTEAYRRYCWDTEGLDGVRFAPFQILAGQGRLLAGVPHDEQLAWLDRLVEHDPSGLLQGTRRLLVDTGDDASVRAGTDWWLELTGSGGEGMVVKPLGALVRDAKGRLVQPGVKVRGREYLRIIYGPEYTRPDNLARLRERHLGHKRSLALREYALGLEALARLADGEPLWRVHEAVFAVLALESEPVDPRL
>NZ_CP034279.1|WP_156691842.1|1584000_1585467_-|3'-terminal-RNA-ribose-2'-O-methyltransferase-Hen1
MFLTISTTGSPRRPATDLGFLLHKHPGKAQAFSTSYGTAHVFYPEASAERCTAALLLEVDPVALVRRGRGKGRGGAPDAALAQYVNDRPYAASSLLAVALSSVFGSALRGVCAALPERAGERLPLRIEIPALPARGGADLVRALFGPLGWTSVDAEPVALDERFPHWGASRYVRLVLEGDLRLADALRHLYVLLPVLDDAKHYWVSPDEVDKLLRAGEGWLAGHPEHALITSRYLSRRRGLTRQAMERLELVRLAEADDLDVEDVDNAVDDAPDTEDRPVPLAEQRCAAILAALRASGATRVLDLGCGEGRLVQALLKDVRFTDIVGVDVSVRALTVAARRLRLERMGERQAGRVRLLQGSLTYTDKRLTGYDAAVLSEVIEHVDLERLPALEYAVFGSARPATVIVTTPNVEYNVRWETLPAGHVRHGDHRFEWTRAEFRTWARSVGERHGYGVEFVSVGPDDPEVGPPTQMAVFTAATTTKEEKAA
>NZ_CP034279.1|WP_156691843.1|1585543_1586467_-|TIGR03560-family-F420-dependent-LLM-class-oxidoreductase
MDLRIFTEPQQGADYDTLLTVAKATEDLGFDAFFRSDHYLRMGSGDGLPGPTDAWITLAGLARETRRIRLGTLMTAGTFRLPGVLAIQVAQVDRMSGGRVELGLGAGWFEEEHRAYGIPFPKEKIGRLEEQLAIVTGLWATETGRTFSYDGTYYQLTDSPALPKPAQAKVPVLVGGLGAQRTPRLAARYADEFNVPFASLEDSERQFGRVRAAAEEAGRKPDDLVYSNALIVCVGKDDAEVARRAAAVGREVEELKENGLAGSPDEVVEKIGRYAAIGASRIYLQVLDLDDLDHLELISSRVMSQLD
>NZ_CP034279.1|WP_156691844.1|1586692_1586902_+|hypothetical-protein
MSQEAVPDQVAPEQPKGLLQQMEELMAALTADLTRLDADLQSSADRLPPPDAAPVSPPAPAQGTGSTAP
>NZ_CP034279.1|WP_156691845.1|1587074_1587545_-|hypothetical-protein
MEAERLIATGRRALADSRVALDIVGEAWQAQLLAQAIGSHVARTGPPELRGEARGLSETGSRGGASPGRPARALRLTHIADVRATLINLGALLGEVGIALVGVACATDEEGLYWQCIEAIDAADEAGDRVREMVRRLAVRERARPPDTAGSSAGPA
>NZ_CP034279.1|WP_156691846.1|1587670_1588051_-|nucleotide-pyrophosphohydrolase
MTELDVQGLQRRLAEFAASREWQPYHTPKNLAAALSVEAAELLEIFQWLTPEEAARVMDDPETAHRVADEVADVLAYLLQFCGSLGVDPLAALSAKIDRNEVRFPVGRPPGRAARASNEPDRHSTE
>NZ_CP034279.1|WP_156691847.1|1588047_1589214_-|ATP-binding-protein
MHATRPSTSLPSSVAPARPAVTELRLSAYKSHRGAAFRLGPVTLFAGASGTGKSSALQAYEALALLAAGVPLAAAFPEPAGCVPERAEADAEGRRGFRIGCTVDGPAGPVRLDLAVQAEPVLRIAGERLTDGDGRTLLTTALRDPGRGTVQAEWHTAGSVPVTRAPLPGDRLGTALLPLRVAGKTEGQRHVLAAAEQVVVALRSVFPCDPQPQRMRTPVVAGDGRLRRGCDNLAEVLHRTRTGCPRRHARLAAVARSGCAGPVSALDVEELADGTVRAVLGRGGDGGTPVERLGEGELRFLALALVLLTGPGVLSMDMAAEVPHAMQTLTVLADGFDRGLDRRQIRELAALAAQICADGHIRLVGTVGEAGARAARGRTGVTVVDLNP
>NZ_CP034279.1|WP_156691848.1|1589288_1589687_-|cell-division-protein-SepF
MSRYERYDVTDEQWEGLAQVVPLRGRNEWPSRVDHSTIPQDYEAAEQRRMVVLRVQVFADAREVAEYLVAQIPVLLDLTAADTDVAKRILDFSSGVVFGLGSGMHRVDRNVFLLAPAGTEVEGAAAAAVPHS
>NZ_CP034279.1|WP_156691849.1|1590021_1591287_+|extracellular-solute-binding-protein
MKTGFKRATVPLAILTLTALTAAGCNSADSGAGSNRVTVWMYPVIMDPKANAAYWDGIEKGFEAAHKNVDLAIEQLPWENRDQKLATAFGSGKGPDVVLLGPDQIPQFQANGAVQPVDRAMEKSRAAFRPTALEAMTQDGKVYAAPIYHTVTSTLYNKKLLDKAGIKEPPATWDALRAAAPKLKQAGVATLDYSASNEASLNMSFYPLLWQAGGKVFDESGKKTAFNSPEGVEALTFLVDLYKSGGVPRSALTNANLFTDHALGKGQVAMGYTNTPSDAVLAGTAWGKENVIVGPALKGPSKQVCFGMPGGLGINARTKNLAGAEKFVAFMTEPAQIASMGKAGGFFSPRTDVAVASDNPFAKEYEAALAHTFPGEPHPAARQLMALITPEIQAALTGKKTPEQALAAAAGEGDDLLARQR
>NZ_CP034279.1|WP_156696253.1|1591514_1592429_+|ABC-transporter-permease-subunit
MPPGGPGSGPGGRRWSPVRRREALVGLAFVGPMLALFLVFRFGPTLGAAFLSLTDYRLSGEWDFIGAANYTRLLQDDLFWESLGVTAVYTALYVPMTVLLALGTAVLLHRTLWLRGFFRGLFFLPYVTSIVLAAVIWKWIYEVEDGLLNTALGALGLGPVDFLGADSLVLPSIAAASAWKGFGYSMLILLAGLQSIPREVAEAATIDGASAWQRFRWVTLPLLRPVLFFVLVIEAIQAFQVFDAMYVMTAGGPVRASYSLVYFLYDSGFKFFDFGYASAIGLVLFLIVLVFSLIQRRLIGREED

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Crispr_ID: NZ_CP034279_3

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP034279_3

2306906-2306992

Orphan

Consensus_repeat	Method
CGGTCGCGCTGACGGTCCCGGCGG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP034279_3

>merge|NZ_CP034279|3|2306906-2306992|CRISPRCasFinder
CGGTCGCGCTGGCGGTCGCGCTGACGGTCCCGGCGGTCGCCGCGGTCGCCGCCGCGGTCACCACGGTCGCGCTGGCGGTCCCGGCGG

>NZ_CP034279|3|3|2306906-2306992|CRISPRCasFinder
CGGTCGCGCTGGCGGTCGCGCTGA	CGGTCCCGGCGGTCGCCGCGGTCGCCGCCGCGGTCACCA
CGGTCGCGCTGGCGGTCCCGGCGG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP034279.1\|WP_156696308.1\|2317464_2319006_-\|DUF3987-domain-containing-protein	unknown	unknown	gnl\|CDD\|379041
NZ_CP034279.1\|WP_156692307.1\|2298387_2299026_-\|protein-tyrosine-phosphatase	unknown	unknown	gnl\|CDD\|319972
NZ_CP034279.1\|WP_156692317.1\|2314309_2314837_-\|response-regulator	unknown	unknown	gnl\|CDD\|381093
NZ_CP034279.1\|WP_156692314.1\|2309329_2310388_-\|threonine-synthase	unknown	unknown	gnl\|CDD\|236013
NZ_CP034279.1\|WP_156692306.1\|2296997_2298284_-\|serine-hydroxymethyltransferase	unknown	unknown	gnl\|CDD\|234571
NZ_CP034279.1\|WP_156692305.1\|2295569_2296892_-\|undecaprenyl/decaprenyl-phosphate-alpha-N-acetylglucosaminyl-1-phosphate-transferase	unknown	unknown	gnl\|CDD\|133463
NZ_CP034279.1\|WP_156692310.1\|2301825_2302044_-\|50S-ribosomal-protein-L31	unknown	unknown	gnl\|CDD\|234576
NZ_CP034279.1\|WP_156696305.1\|2299698_2300523_-\|peptide-chain-release-factor-N(5)-glutamine-methyltransferase	unknown	unknown	gnl\|CDD\|236467
NZ_CP034279.1\|WP_156692318.1\|2315483_2316965_-\|tyrosine-type-recombinase/integrase	unknown	unknown	gnl\|CDD\|271189
NZ_CP034279.1\|WP_156692316.1\|2313180_2314227_-\|arginine--tRNA-ligase	unknown	unknown	gnl\|CDD\|234964
NZ_CP034279.1\|WP_156696306.1\|2303548_2305237_-\|trypsin-like-serine-protease	unknown	unknown	gnl\|CDD\|214473
NZ_CP034279.1\|WP_156692308.1\|2299022_2299670_-\|threonylcarbamoyl-AMP-synthase	unknown	unknown	gnl\|CDD\|223088
NZ_CP034279.1\|WP_156692311.1\|2302176_2303274_-\|LytR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|367673
NZ_CP034279.1\|WP_167536477.1\|2316961_2317132_-\|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|225848
NZ_CP034279.1\|WP_156692315.1\|2311781_2313173_-\|diaminopimelate-decarboxylase	unknown	unknown	gnl\|CDD\|273415
NZ_CP034279.1\|WP_156692320.1\|2319017_2319950_-\|DNA-primase	unknown	unknown	gnl\|CDD\|378140
NZ_CP034279.1\|WP_167536358.1\|2310394_2311687_-\|homoserine-dehydrogenase	unknown	unknown	gnl\|CDD\|235783
NZ_CP034279.1\|WP_156692313.1\|2308032_2308950_-\|homoserine-kinase	unknown	unknown	gnl\|CDD\|234920
NZ_CP034279.1\|WP_156692304.1\|2294869_2295307_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP034279.1\|WP_156692309.1\|2300641_2301721_-\|peptide-chain-release-factor-1	unknown	unknown	gnl\|CDD\|234801

Protein	Function_ID	Function_description	E-value
NZ_CP034279.1\|WP_156696308.1\|2317464_2319006_-\|DUF3987-domain-containing-protein	gnl\|CDD\|379041	pfam13148, DUF3987, Protein of unknown function (DUF3987). A family of uncharacterized proteins found by clustering human gut metagenomic sequences.	3.25884e-115
NZ_CP034279.1\|WP_156692307.1\|2298387_2299026_-\|protein-tyrosine-phosphatase	gnl\|CDD\|319972	cd16344, LMWPAP, low molecular weight protein arginine phosphatase. Low molecular weight protein arginine phosphatases are part of the low molecular weight phosphatase (LMWP) family. They share a highly conserved active site motif (V/I)CXGNTCRS. It has been shown that the conserved threonine, which in many LMWPTPs is an isoleucine, confers specificity to phosphoarginine over phosphotyrosine.	2.28275e-24
NZ_CP034279.1\|WP_156692317.1\|2314309_2314837_-\|response-regulator	gnl\|CDD\|381093	cd17538, REC_D1_PleD-like, first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar domains. PleD contains a REC domain (D1) with the phosphorylatable aspartate, a REC-like adaptor domain (D2), and the enzymatic diguanylate cyclase (DGC) domain, also called the GGDEF domain according to a conserved sequence motif, as its output domain. The GGDEF-containing PleD response regulators are global regulators of cell metabolism in some important human pathogens. This model describes D1 of PleD and similar domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.	1.10408e-34
NZ_CP034279.1\|WP_156692314.1\|2309329_2310388_-\|threonine-synthase	gnl\|CDD\|236013	PRK07409, PRK07409, threonine synthase; Validated.	0
NZ_CP034279.1\|WP_156692306.1\|2296997_2298284_-\|serine-hydroxymethyltransferase	gnl\|CDD\|234571	PRK00011, glyA, serine hydroxymethyltransferase; Reviewed.	0
NZ_CP034279.1\|WP_156692305.1\|2295569_2296892_-\|undecaprenyl/decaprenyl-phosphate-alpha-N-acetylglucosaminyl-1-phosphate-transferase	gnl\|CDD\|133463	cd06853, GT_WecA_like, This subfamily contains Escherichia coli WecA, Bacillus subtilis TagO and related proteins. WecA is an UDP-N-acetylglucosamine (GlcNAc):undecaprenyl-phosphate (Und-P) GlcNAc-1-phosphate transferase that catalyzes the formation of a phosphodiester bond between a membrane-associated undecaprenyl-phosphate molecule and N-acetylglucosamine 1-phosphate, which is usually donated by a soluble UDP-N-acetylglucosamine precursor. WecA participates in the biosynthesis of O antigen LPS in many enteric bacteria and is also involved in the biosynthesis of enterobacterial common antigen. A conserved short sequence motif and a conserved arginine at a cytosolic loop of this integral membrane protein were shown to be critical in recognition of substrate UDP-N-acetylglucosamine.	1.46124e-89
NZ_CP034279.1\|WP_156692310.1\|2301825_2302044_-\|50S-ribosomal-protein-L31	gnl\|CDD\|234576	PRK00019, rpmE, 50S ribosomal protein L31; Reviewed.	7.8188e-40
NZ_CP034279.1\|WP_156696305.1\|2299698_2300523_-\|peptide-chain-release-factor-N(5)-glutamine-methyltransferase	gnl\|CDD\|236467	PRK09328, PRK09328, N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional.	3.81045e-107
NZ_CP034279.1\|WP_156692318.1\|2315483_2316965_-\|tyrosine-type-recombinase/integrase	gnl\|CDD\|271189	cd01189, INT_ICEBs1_C_like, C-terminal catalytic domain of integrases from bacterial phages and conjugate transposons. This family of tyrosine based site-specific integrases is has origins in bacterial phages and conjugate transposons. One member is the integrase from Bacillus subtilis conjugative transposon ICEBs1. ICEBs1 can be excised and transfered to various recipients in response to DNA damage or high concentrations of potential mating partners. The family belongs to the superfamily of DNA breaking-rejoining enzymes, which share the same fold in their catalytic domain and the overall reaction mechanism. The catalytic domain contains six conserved active site residues. Their overall reaction mechanism involves cleavage of a single strand of a DNA duplex by nucleophilic attack of a conserved tyrosine to give a 3' phosphotyrosyl protein-DNA adduct. In the second rejoining step, a terminal 5' hydroxyl attacks the covalent adduct to release the enzyme and generate duplex DNA.	1.70006e-14
NZ_CP034279.1\|WP_156692316.1\|2313180_2314227_-\|arginine--tRNA-ligase	gnl\|CDD\|234964	PRK01611, argS, arginyl-tRNA synthetase; Reviewed.	1.07562e-22
NZ_CP034279.1\|WP_156696306.1\|2303548_2305237_-\|trypsin-like-serine-protease	gnl\|CDD\|214473	smart00020, Tryp_SPc, Trypsin-like serine protease. Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.	6.88113e-62
NZ_CP034279.1\|WP_156692308.1\|2299022_2299670_-\|threonylcarbamoyl-AMP-synthase	gnl\|CDD\|223088	COG0009, SUA5, Putative translation factor (SUA5) [Translation, ribosomal structure and biogenesis].	1.22466e-66
NZ_CP034279.1\|WP_156692311.1\|2302176_2303274_-\|LytR-family-transcriptional-regulator	gnl\|CDD\|367673	pfam03816, LytR_cpsA_psr, Cell envelope-related transcriptional attenuator domain.	9.278e-63
NZ_CP034279.1\|WP_167536477.1\|2316961_2317132_-\|helix-turn-helix-domain-containing-protein	gnl\|CDD\|225848	COG3311, AlpA, Predicted transcriptional regulator [Transcription].	1.09605e-05
NZ_CP034279.1\|WP_156692320.1\|2319017_2319950_-\|DNA-primase	gnl\|CDD\|378140	pfam09250, Prim-Pol, Bifunctional DNA primase/polymerase, N-terminal. Members of this family adopt a structure consisting of a core of antiparallel beta sheets. They are found in various bacterial hypothetical proteins, and have been shown to harbour both primase and polymerase activities.	1.81743e-44
NZ_CP034279.1\|WP_167536358.1\|2310394_2311687_-\|homoserine-dehydrogenase	gnl\|CDD\|235783	PRK06349, PRK06349, homoserine dehydrogenase; Provisional.	0
NZ_CP034279.1\|WP_156692313.1\|2308032_2308950_-\|homoserine-kinase	gnl\|CDD\|234920	PRK01212, PRK01212, homoserine kinase; Provisional.	1.40893e-103
NZ_CP034279.1\|WP_156692315.1\|2311781_2313173_-\|diaminopimelate-decarboxylase	gnl\|CDD\|273415	TIGR01048, Diaminopimelate_decarboxylase, diaminopimelate decarboxylase. This family consists of diaminopimelate decarboxylase, an enzyme which catalyzes the conversion of diaminopimelic acid into lysine during the last step of lysine biosynthesis. [Amino acid biosynthesis, Aspartate family].	1.20398e-166
NZ_CP034279.1\|WP_156692309.1\|2300641_2301721_-\|peptide-chain-release-factor-1	gnl\|CDD\|234801	PRK00591, prfA, peptide chain release factor 1; Validated.	0

>NZ_CP034279.1|WP_156696306.1|2303548_2305237_-|trypsin-like-serine-protease
MAAVVALVGTGIAVSGSDSAEADEAPRMSALPSPEQTESQQELAENVADAMQADVKSSRPLVKQPDDSVESAAPSARIIGGQTTTISTAPWMAQLHFFDSTGAGYFCGGAVIAPTKILTAAHCVKGIKWYAPENAVVVGTDQLPTGKDLHGGEAFGVSRQWHHPQYDDYSLDNDVAVLTLNRPTTVKPLPLAQPSDGALYQSGLDGKVYGWGRTSSTNPNSASPTLKVADADIVSDTNCAAAYPDGFVKGHMLCAGAAPTGSDETSETTCNGDSGGPLVVGGKLVGVVSWGDENCSAEGKYGVYAKLSTYSAPVQARTDDANLNRDHTADLLARRTSDSTLFGWTSKVTSMSRTLNLGKQSAINLITQGDLNRDGAQDLLYRYTNGDVFWSYGTATPKLIAKAWGKHKAILTPGDVTGDELPDMVAVDSAGVMRVYPGRGNGGFNAPVSVGSGWGKFSMIRGHGDFTNDGKADIFARDTTGKTYLYKGTGVATKPWAAPVLVGAFGSMNALATTGDVNSDGVADVLARDTAGKMWLYPGNGKGGFLARKDFGSGWQAYNLFG
>NZ_CP034279.1|WP_156692311.1|2302176_2303274_-|LytR-family-transcriptional-regulator
MAEQGSKTSRIRATGRRRRQSGKGRKALTVAAWSAAGLVLVGGCGFGYVYFTLNGNIESVDINAALRDDDRPQDVDNGSMDILVLGSDSRSGANGEYGRDEGAARSDTAMILHVYEGHKKASVVSVPRDTIIERPDCTDKSGGSVPGQRKAMFNTAYEVGGPACAVKTVEKMSGIRMDHYIEVDFSGFKKLIDELGGVEITTTKPIKDKSSHLDLPVGTHTLGGEQALGLVRTRKGVGDGSDLGRIQLQQAFMKAFIEQAKSVGVFTSPKKLWNLADTATKAIKPDSELDSVKELSDFAGGLKQLGADDVHMITLPVRYDPADLNRVVPLKNQSQQVWAALKADRPIPASATKDAATGSAAGVVK
>NZ_CP034279.1|WP_156692310.1|2301825_2302044_-|50S-ribosomal-protein-L31
MKREIHPEYVETQVSCTCGASFTTRSTIQSGAIRAEVCSECHPFYTGKQKILDTGGRVARFEARFGKKAAAK
>NZ_CP034279.1|WP_156692309.1|2300641_2301721_-|peptide-chain-release-factor-1
MFEAVEELIGEHADLEKKLADPSVHADQANARKLNKRYAELTPIVTTYRSWKQTGEDIETAREFAATDPDFAAEVKELEKQREELTDKLRLLLVPRDPSDDKDVILEVKAGAGGDESALFAGDLLRMYLRYAERVGWKTEIIDATESELGGYKDVQVAVKTKGGNGATEPGQGVWARLKYEGGVHRVQRVPATESQGRIHTSAAGVLVTPEAEEIDVEIHANDLRVDVYRSSGPGGQSVNTTDSAVRITHLPTGIVASCQNEKSQLQNKEQAMRILRSRLLAAAQEEAEKNAADARRSQVRTVDRSEKIRTYNFPENRISDHRVGFKAYNLDQVLDGELDPVIQACVDADSAAKLAAAQ
>NZ_CP034279.1|WP_156696305.1|2299698_2300523_-|peptide-chain-release-factor-N(5)-glutamine-methyltransferase
MAQATQRLADAGVPSPRFDAEELAAFVHGVKRGELHNVKDADFDARYWETVARREAREPLQHITGRAFFRYLELQVGPGVFVPRPETESVVGWAIDAVRAMDVVEPLIVDLCSGSGAIALAMAQEVPRSRVHAVELSEDALVWTRKNAEGSRVTVHQGDALTALPELDGQVDLVISNPPYIPLTEWEYVAPEARDHDPEMALFSGEDGLDTIRGIERTAHRLLRPGGLVVIEHADTQGGQVPWIFNEEAGWADAADHPDLNNRPRFATARKATP
>NZ_CP034279.1|WP_156692308.1|2299022_2299670_-|threonylcarbamoyl-AMP-synthase
MARRYDCNDATDRTTGLREAASAVRRGELVVLPTDTVYGIGADAFSGEAVADLLEAKGRGRNMPTPVLIGSPNTLHGLVTDFSEQAWELVDAFWPGALTLVARHQPSLQWDLGDTRGTVAIRMPLHPVAIELLTEVGPMAVSSANLTGHPAPEDCDAAQGMLGDSVSVYLDGGPTPGIVPSSIVDVTGEVPVLLRAGALSVDELRKVVPDLEVAN
>NZ_CP034279.1|WP_156692307.1|2298387_2299026_-|protein-tyrosine-phosphatase
MTAPEGRGIGTDNAFRILHVSTGNVCRSPITERLTRHALCDRLGDPMGGGLIVESAGTWGHEGAPMEANAEIVLADFGADASGFVGRELLDEHVIRADLVLTATRDHRAQVISMGHSAGLRTFTLKEFTRLVRAIDPATLPDPRDDGMVERARALVRAAAALRGWLLAPSADADEVNDPYGAPITFFRSVGDEINQALDPVVTALTGVPTRH
>NZ_CP034279.1|WP_156692306.1|2296997_2298284_-|serine-hydroxymethyltransferase
MPVTAAAEVRTTRDAYEADADVLRRRDPEIADVLAGEGARQADGLQLIAAENFASPAVLAALGSPLANKYAEGYPGARHHGGCEYADAAERIAVRRATELFGAEHANVQAHSGSSAVLAAYAALLRPGDTVLAMGLAYGGHLTHGSPANFSGRWFDFVPYGVDAESGLIDYEQVRALAHEHRPKAVVCGSISYPRHIDYAAFREIADEVGACLIADAAHPIGLVAGGAAPSPVPYADVVCATTHKVLRGPRGGLLLCGAELAERVDRAVFPFTQGGAQMHTIAAKAVAFGEASTPAFTAYTHQVVVNARALADALAQEGFAVTTGGTDTHLITADPAPLGVDGRVARARLAAAGIVLDTCALPYGDGRGIRLGTAAVTTQGMTAPDMERIAALFSAALRQEDPEAAGTAGNVRGEVRELADRFPPYRG
>NZ_CP034279.1|WP_156692305.1|2295569_2296892_-|undecaprenyl/decaprenyl-phosphate-alpha-N-acetylglucosaminyl-1-phosphate-transferase
MRDYLLTLCVTAAVTYLLTGPVRKFAIAAGAMPEIRARDVHREPTPRLGGIAMFFGLCAGLLVADHLSNLNSVFELSNEPRALLSGAALIWLIGVLDDKFEIDALIKLGGQMIAAGVMVMQGLTILWLPIPGVGTVALTQWQGTLLTVALVVITINAVNFVDGLDGLAAGMVCIAAAAFFLYAYRIWYGFTIEAAAPATLFAVILMGMCLGFLPHNMHPARIFMGDSGSMLIGLVLAASAISITGQVDPDALKIFEGSTREATHAALPVFIPLLLPLTIIAIPVADLVLAIVRRTWNGQSPFAADRGHLHHRLLEIGHSHSRAVLIMYFWSALIAFGTLAYSVHSASMWIVLVIVALSAIGLVLLLLPRFTPRAPRWAESFVPPRYRRRAVRPAEPEQAPGSSSETGDEEPVPVPAGVNGATALSALPELHDRRKAGTRG
>NZ_CP034279.1|WP_156692304.1|2294869_2295307_-|hypothetical-protein
MPSTDVRTLLHTAVPTLVAGAIATVVSGVVAGGQGAIGAVVGTLVVVLFMGIGLVVLQRTAKSLPQLFQAMGLMLYVAELLLLFMFMALFKNTTLFEFKAFAFTIVGATLVWVAAQARAHMKAKILYVDDPSDKGSKPEKTGPSA
>NZ_CP034279.1|WP_156692313.1|2308032_2308950_-|homoserine-kinase
MAGPAFRAAAVRVRVPATSANLGPGFDALGLSLGLYDDVVVRVADSGLHIDIAGEGAEALPRDESHLLVRSLRTAFDLLGGQPRGLEVVCANRIPHGRGLGSSSAAICAGIVAARAVTIGGDARLDDAALLELATEIEGHPDNVAACLLGGFTLAWTEGGAARAIRMDPADSIVPVVFVPGKPVLTETARGLLPRTVPHVDAAVNAGRAALLVEALTRRPELLLAATEDRLHQEYRAPAMPESVALVNRLRADGVPAVISGAGPTVLALAEDGTADKVARLAGEGWAANRLALDGPGASVLPLAP
>NZ_CP034279.1|WP_156692314.1|2309329_2310388_-|threonine-synthase
MTHQWRGIIEEYRDRLPVTDTTPVVTLREGGTPLVPAQVLSERTGCEVHLKVEGANPTGSFKDRGMTMAITRAKEEGAQAVICASTGNTSASAAAYAVRAGMVSAVLVPQGKIALGKMGQALVHGAKILQVDGNFDDCLTLARALSDNYPVALVNSVNPVRIEGQKTAAFEIVDMLGDAPDIHVLPVGNAGNITAYWKGYTEYAADAVSTRTPRMWGFQASGSAPIVRGEVVKDPSTIATAIRIGNPASWNHALAARDESGGFIDEVTDREILRAYRLLASQEGVFVEPASAASVAGLLKAAEQGKVDRGQKIVCTVTGNGLKDPDWAVAGAPQPVTVPVDAATAAERLGLA
>NZ_CP034279.1|WP_167536358.1|2310394_2311687_-|homoserine-dehydrogenase
MMRTRPLKVALLGCGVVGSEVARIMTTHADDLAARIGAPVELAGVAVRRPSKVREGIPAELITTDATALVKRGDIDVVVEVIGGIEPARTLITTAFEHGASVVSANKALLAQEGQSLYAAAEQHGRDLYYEAAVAGAIPLIRPLRESLAGDKVNRVLGIVNGTTNFILDKMDTSGAGYSEALDEATALGYAEADPTADVEGFDAAAKAAILAGIAFHTRVRLDDVYREGMTEVTAADFASAKRMGCTIKLLAICERAADGGSVTARVHPAMIPLSHPLASVRGAYNAVFVEADAAGQLMFYGPGAGGSPTASAVLGDLVAVCRNRLNEATGPGESAYTQLPVSPMGDVVTRYHISLDVADKPGVLAQVATVFAEHGVSIDTVRQQGKDGEADLVVVTHRAPDAALSGTVEALRKLDTVRGVASIMRVEGE
>NZ_CP034279.1|WP_156692315.1|2311781_2313173_-|diaminopimelate-decarboxylase
MSRSAHPAGPRHADVLPEGHYAAPPADLNRLDEKVWARTVTRDGDGVLTVGGISVTDLAEEFGTPAYFLDEADFRARCRAWAEAFGPDADVFYAGKAFLSRAVVRWLKEEGLNLDVCSGGELSTALDAGMPAERIAFHGNNKSPEEIERAVRAGVGRIVLDSFQEIARVAHIAQGLGTRQKVQIRVTVGVEAHTHEFIATAHEDQKFGIALAGGEAAEAVRRALKLDGLELIGIHSHIGSQIFDTSGFEVAAHRVVGLLKQVRDEHGVELPEIDLGGGLGIAYTSDDDPREPHEIAKALSDIVTRECAAAGLATPRISVEPGRAVVGPTAFTLYEVGTVKPLAGLRTYVSVDGGMSDNIRTALYDAEYSVSLVSRTSDAEPMLSRVVGKHCESGDIVVKDAFLPADLAPGDLIAVPATGAYCRSMASNYNHALRPPVVAVKDGEARVIVRRETEEDLLRLDVG
>NZ_CP034279.1|WP_156692316.1|2313180_2314227_-|arginine--tRNA-ligase
MTPADLSLTVQDAVRRAVGEGALRALTRVPERVKVERPRPGGSGDWATNAALQLAREAGMEPLGVARVLKPRIAEADGIARVEITGPGFLNITLAGRSRRALVRDVLDARERYGHGTALEGRAFRLSHPGDVRATVWADAVRGLLAAQGADVHDGAAETLTLRPVPVTYDVLALGPDAARWALLRPAAHDRALGPDGLLTQSEANGLFTVRYAHSRARALLRNAAQLGMSPAYDDEAPLDAQTAYKDEARPGVTPPHQNDAPASRLLTALGDHPAVLEAAARHRAPDRVARHLEVTADALLGFQHTVLPLGDEKPSAAHRSRLALAEAAGTVLAGGLALLGISAPDYL
>NZ_CP034279.1|WP_156692317.1|2314309_2314837_-|response-regulator
MYGWRGGWGRPCGAEVGKTRTQGWDSTYSRVVSGVSGRVLVVDDNRVIRQLIRVNLELEGFEVVTAADGAECLDVVHHVRPDVVTLDVVMPRLDGLRTAERLREDPRTRHLPVAIVSACTQYEVESGLAAGVDAFLAKPFEPADLVRLVRGLRHREIAPPLDGRRGAGHAGSAWS
>NZ_CP034279.1|WP_156692318.1|2315483_2316965_-|tyrosine-type-recombinase/integrase
MNHRNTNRTGSPDGGGPSGQEHNLSTDVRVWNVSKVRSKKAPYQLRWKVAGKVKTASFTTVALADTRRSELRQAMRKGEAFDVVTGLPESELRAAIARESQRPDPSWWDFCREYMNARWRTTAAKTREGLADSLATVALALMGEGAKAPTLEEVRLAMRWAVVPAHRGEEPPPELEAACTWLSNRSLPLSALTDPKVLRDVQYRLSFKLDDAPAAGETYKRRRRGFNTAMEYAIESGYLDENPLAKVKRSGSQANDTVDPRVLVNPTQGMELLTAVSYVGSVHRNRGRRLMAFFACQLYAALRPAEAVGLREKDCYLPERGWGTLTLRETRPVSGKKWTDSGQRHDKRGLKSREAKADRPVPIPPLLVMMLRDHIKEFSTAKDGRLFANERGGVLGTSSYWRVWQEARPIALPPDKVDSPLAHRPYDLRHTCITNWLNAGVPVAEVARRAGNSPEVIHRRYEGCIDGHEELNNKKIEAAMGWREGQDEPSKRG
>NZ_CP034279.1|WP_167536477.1|2316961_2317132_-|helix-turn-helix-domain-containing-protein
MLSIPQVIEEIGVPRATFYRWRQLRKGPRAIKLPNGAVRIRRSELDRWIATLEEAA
>NZ_CP034279.1|WP_156696308.1|2317464_2319006_-|DUF3987-domain-containing-protein
MDSSELWAFFDAQDAPEGTGEAPWEEPIPLTARRELPAFPTEVFPAWLGDYVRAVAEETQTPVDMAGALALAVLGTAAGGRAVVQVRGRWREPTNVFVVVALPPGNRKSAVFNLMANPLYRCEALLVTQSAGRIVEAEITARLAKEVAESAAAKAARGADADKRDELVAEAISLAQAAESVTVPAKPRLLADDATPEVIASLLAEQGGRLSVMSAEGGIFDIIAGRYSGTPNLDVFLRGQAGDRLRVDRRGREEFIEAPALTMGLTVQPGVLEDIGRIKGADERGLLARFLYSLPKSLVGYRKVLTEPIPDAVAATYEEHVTALTMSLTDWTDPAVLQLSPEAGDVLVAFEKRQEPRLRERGGDLAHVQNWANKLGGATCRLAGLLHLAAHPSNGHTEPISADTMRAAVKLTDYFTGHALAVFDLMGADHTAARAHAVLEVLRAQQWSEVSKRDLMVKLSRAEFPTVADLDPALNLLEDHGYIRCQPVQRSGGRGRPPSPRYLIHPQLADPTA
>NZ_CP034279.1|WP_156692320.1|2319017_2319950_-|DNA-primase
MTPNATTALLRAALAAAERGWPVFPLRPGDKRPAGHPERDCPRTGRCESGHRTPEQRATLDPQHITACWQAAPYNVGIATGPAQLVVVDLDIPKDEADTAPSEWAGLGAADGLDVFAVLCERAGERLPTETFTVRTRRGGQHLYFTAPSEKRLRSTGGSLGWKVDTRAWGGYVVAAGSIVGGAPYEIIHDAPAAPLPAWLSDLLTRKPAPAPMPLSELSARMRNATAYSTTALRGELEKVLSARQGGRNRAVYFAAYALARLIRTGDLTEADVTGELMSAGQSIGLPAAECRTAIRSGLARGGAVEVSAA

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Crispr_ID: NZ_CP034279_4

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP034279_4

2552822-2553020

Orphan

Consensus_repeat	Method
TCGTCGAGGCCGCCCCCGAGGCCGAGGCCACGGAGACCAAGCCCCGCCG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP034279_4

>merge|NZ_CP034279|4|2552822-2553020|CRISPRCasFinder
TCGTCGAGGCCGCCCCCGAGGCCGAGGCCACGGAGACCAAGCCCCGCCGCCGTACCCGCAAGGCCGCCGAGCCGATCGTCGAGGCCGCCCCCGAGGCCGAGGCCACGGAGACCAAGCCCCGCCGACGCACCCGCAAGGCCGCCGAACCGGTCGTCGACGCCACCCCGGAGGCCGAGGCCACGGAGACCAAGCCGCGCCG

>NZ_CP034279|4|4|2552822-2553020|CRISPRCasFinder
TCGTCGAGGCCGCCCCCGAGGCCGAGGCCACGGAGACCAAGCCCCGCCG	CCGTACCCGCAAGGCCGCCGAGCCGATCGTCGAGGCCGCCCCCGAGGCCGAGGCCACGGAGACCAAGCCCCGCCGACGCACCCGCAAGGCCGCCGAACCGG
TCGTCGACGCCACCCCGGAGGCCGAGGCCACGGAGACCAAGCCGCGCCG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP034279.1\|WP_156692512.1\|2559543_2560134_-\|suppressor-of-fused-domain-protein	unknown	unknown	gnl\|CDD\|377450
NZ_CP034279.1\|WP_156692510.1\|2557504_2558143_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP034279.1\|WP_156692511.1\|2558310_2559537_+\|MFS-transporter	unknown	unknown	gnl\|CDD\|341027
NZ_CP034279.1\|WP_156692505.1\|2553325_2554207_+\|alpha/beta-fold-hydrolase	unknown	unknown	gnl\|CDD\|366166
NZ_CP034279.1\|WP_156692496.1\|2543259_2545239_-\|DUF3492-domain-containing-protein	unknown	unknown	gnl\|CDD\|340841
NZ_CP034279.1\|WP_156692502.1\|2549722_2549989_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP034279.1\|WP_156692500.1\|2548564_2549206_+\|TetR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224228
NZ_CP034279.1\|WP_156692513.1\|2560583_2561717_+\|magnesium-transporter-CorA	unknown	unknown	gnl\|CDD\|213364
NZ_CP034279.1\|WP_156692503.1\|2550049_2550796_-\|tRNA-2-methylthio-N6-isopentenyl-adenosine(37)-hydroxylase-MiaE-like-protein	unknown	unknown	gnl\|CDD\|205967
NZ_CP034279.1\|WP_156692509.1\|2556474_2557347_-\|PHP-domain-containing-protein	unknown	unknown	gnl\|CDD\|223686
NZ_CP034279.1\|WP_156692495.1\|2541992_2543267_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP034279.1\|WP_156692506.1\|2554191_2555112_-\|NYN-domain-containing-protein	unknown	unknown	gnl\|CDD\|350289
NZ_CP034279.1\|WP_156692514.1\|2561796_2562303_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP034279.1\|WP_156692498.1\|2546985_2548038_-\|alpha/beta-fold-hydrolase	unknown	unknown	gnl\|CDD\|223669
NZ_CP034279.1\|WP_156692508.1\|2555537_2556143_-\|NAAT-family-transporter	unknown	unknown	gnl\|CDD\|225006
NZ_CP034279.1\|WP_156692497.1\|2545435_2546977_-\|DUF3152-domain-containing-protein	unknown	unknown	gnl\|CDD\|371483
NZ_CP034279.1\|WP_156692499.1\|2548191_2548419_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP034279.1\|WP_156692494.1\|2540891_2541878_-\|NAD-dependent-epimerase/dehydratase-family-protein	unknown	unknown	gnl\|CDD\|366597
NZ_CP034279.1\|WP_167536368.1\|2549291_2549519_+\|DUF3107-family-protein	unknown	unknown	gnl\|CDD\|378634
NZ_CP034279.1\|WP_156692507.1\|2555286_2555439_+\|hypothetical-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_CP034279.1\|WP_156692511.1\|2558310_2559537_+\|MFS-transporter	gnl\|CDD\|341027	cd17474, MFS_YfmO_like, Bacillus subtilis multidrug efflux protein YfmO and similar transporters of the Major Facilitator Superfamily. This family is composed of Bacillus subtilis multidrug efflux protein YfmO, bacillibactin exporter YmfD/YmfE, uncharacterized MFS-type transporter YvmA, and similar proteins. YfmO acts to efflux copper or a copper complex, and could contribute to copper resistance. YmfD/YmfE is involved in secretion of bacillibactin. The YfmO-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.	4.10085e-94
NZ_CP034279.1\|WP_156692505.1\|2553325_2554207_+\|alpha/beta-fold-hydrolase	gnl\|CDD\|366166	pfam00561, Abhydrolase_1, alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes.	9.43977e-18
NZ_CP034279.1\|WP_156692496.1\|2543259_2545239_-\|DUF3492-domain-containing-protein	gnl\|CDD\|340841	cd03813, GT4-like, glycosyltransferase family 4 proteins. This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria, while some of them are also found in Archaea and eukaryotes.	1.12621e-151
NZ_CP034279.1\|WP_156692500.1\|2548564_2549206_+\|TetR-family-transcriptional-regulator	gnl\|CDD\|224228	COG1309, AcrR, Transcriptional regulator [Transcription].	2.26122e-15
NZ_CP034279.1\|WP_156692513.1\|2560583_2561717_+\|magnesium-transporter-CorA	gnl\|CDD\|213364	cd12830, MtCorA-like, Mycobacterium tuberculosis CorA-like subfamily. This bacterial subfamily belongs to the Thermotoga maritima CorA (TmCorA)-like family of the MIT superfamily of essential membrane proteins involved in transporting divalent cations (uptake or efflux) across membranes. This subfamily includes the Mg2+ transporter Mycobacterium tuberculosis CorA (which also transports Co2+). Thermotoga maritima CorA forms funnel-shaped homopentamers, the tip of the funnel is formed from two C-terminal transmembrane (TM) helices from each monomer, and the large opening of the funnel from the N-terminal cytoplasmic domains. The GMN signature motif of the MIT superfamily occurs just after TM1, mutation within this motif is known to abolish Mg2+ transport by a related protein, Saccharomyces cerevisiae Alr1p. Natural variants in this signature sequence may be associated with the transport of different divalent cations. The functional diversity of the MIT superfamily may also be due to minor structural differences regulating gating, substrate selection, and transport.	9.40848e-172
NZ_CP034279.1\|WP_156692503.1\|2550049_2550796_-\|tRNA-2-methylthio-N6-isopentenyl-adenosine(37)-hydroxylase-MiaE-like-protein	gnl\|CDD\|205967	pfam13794, MiaE_2, tRNA-(MS[2]IO[6]A)-hydroxylase (MiaE)-like.	1.93784e-87
NZ_CP034279.1\|WP_156692509.1\|2556474_2557347_-\|PHP-domain-containing-protein	gnl\|CDD\|223686	COG0613, COG0613, Predicted metal-dependent phosphoesterases (PHP family) [General function prediction only].	7.67586e-45
NZ_CP034279.1\|WP_156692512.1\|2559543_2560134_-\|suppressor-of-fused-domain-protein	gnl\|CDD\|377450	pfam05076, SUFU, Suppressor of fused protein (SUFU). SUFU, encoding the human orthologue of Drosophila suppressor of fused, appears to have a conserved role in the repression of Hedgehog signaling. SUFU exerts its repressor role by physically interacting with GLI proteins in both the cytoplasm and the nucleus. SUFU has been found to be a tumor-suppressor gene that predisposes individuals to medulloblastoma by modulating the SHH signaling pathway. Genomic contextual analysis of bacterial SUFU versions revealed that they are immunity proteins against diverse nuclease toxins in polymorphic toxin systems.	9.77221e-32
NZ_CP034279.1\|WP_156692506.1\|2554191_2555112_-\|NYN-domain-containing-protein	gnl\|CDD\|350289	cd18722, PIN_NicB-like, LabA-like PIN domain of Pseudomonas putida S16 NicB and related proteins. Curiously NicB from Pseudomonas putida S16 is described as a putative NADH-dependent hydroxylase involved in the microbial degradation of nicotine. This subfamily also includes the uncharacterized CPP15 (plasmid) protein from Campylobacter jejuni. This subfamily belongs to LabA-like PIN domain family which includes Synechococcus elongatus PCC 7942 LabA, human ZNF451, uncharacterized Bacillus subtilis YqxD and Escherichia coli YaiI, and the N-terminal domain of a well-conserved group of mainly bacterial proteins with no defined function, which contain a C-terminal LabA_like_C domain. Curiously, a gene labeled NicB from Pseudomonas putida S16, which is described as a putative NADH-dependent hydroxylase involved in the microbial degradation of nicotine also falls into the LabA-like PIN family. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons.	6.65213e-06
NZ_CP034279.1\|WP_156692498.1\|2546985_2548038_-\|alpha/beta-fold-hydrolase	gnl\|CDD\|223669	COG0596, MhpC, Predicted hydrolases or acyltransferases (alpha/beta hydrolase superfamily) [General function prediction only].	1.8016e-27
NZ_CP034279.1\|WP_156692508.1\|2555537_2556143_-\|NAAT-family-transporter	gnl\|CDD\|225006	COG2095, MarC, Multiple antibiotic transporter [Intracellular trafficking and secretion].	1.55527e-41
NZ_CP034279.1\|WP_156692497.1\|2545435_2546977_-\|DUF3152-domain-containing-protein	gnl\|CDD\|371483	pfam11350, DUF3152, Protein of unknown function (DUF3152). Some members in this family of proteins are annotated as membrane proteins however this cannot be confirmed. Currently there is no known function.	2.52532e-55
NZ_CP034279.1\|WP_156692494.1\|2540891_2541878_-\|NAD-dependent-epimerase/dehydratase-family-protein	gnl\|CDD\|366597	pfam01370, Epimerase, NAD dependent epimerase/dehydratase family. This family of proteins utilize NAD as a cofactor. The proteins in this family use nucleotide-sugar substrates for a variety of chemical reactions.	1.99916e-41
NZ_CP034279.1\|WP_167536368.1\|2549291_2549519_+\|DUF3107-family-protein	gnl\|CDD\|378634	pfam11305, DUF3107, Protein of unknown function (DUF3107). Some members in this family of proteins are annotated as ATP-binding proteins however this cannot be confirmed. Currently no function is known.	6.35451e-37

>NZ_CP034279.1|WP_156692503.1|2550049_2550796_-|tRNA-2-methylthio-N6-isopentenyl-adenosine(37)-hydroxylase-MiaE-like-protein
METPDNAAASAAATEEPTGIAAQNWAAASAEPQYRAAVVDLLGALAYGELAAFERLAEDAKLAPTLADKAELAKMASAEFHHFERLRDRLTAIDAEPTAAMEPFAKALDDFHRQTAPSDWLEGLVKAYVGDSIASDFYREVAVRLDSDTRALVLAVLDDTGHGNFAVEKVRAAIEADPRVGGRLALWARRLMGEALSQAQRVVAERDALSTMLVGGVADGFDLAAVGEMFSRITKAHTKRMAALGLAA
>NZ_CP034279.1|WP_156692502.1|2549722_2549989_+|hypothetical-protein
MFWEAFGSVVLGFALSWAAAHRLTDRLPSRRVVLGAGVLGALFGSLITHAALGPGYALGTLLGAVAVAAVVLSLLLRPTRRLRRATQT
>NZ_CP034279.1|WP_167536368.1|2549291_2549519_+|DUF3107-family-protein
MEVKIGVQHAPREIALESGQSAEEVERAVADALAGTSQLLSLTDDKGRKVLVPADRIAYVEIGEPAKPRVGFGAL
>NZ_CP034279.1|WP_156692500.1|2548564_2549206_+|TetR-family-transcriptional-regulator
MTAIEQTEAARPRGTRLPRRARRNQLLGAAQEVFVAQGYHAAAMDDIAERAGVSKPVLYQHFPGKLELYLALLDQHCESLLQAVRTALASTTDNKLRVAATMDAYFAYVEDEGGAFRLVFESDLTNEPAVRERVERVSLQCAEAISDVIAEDTGLSKDESMLLAVGLGGVSQVVARYWLSSESTIPREKAVQLLTSLAWRGIAGFPLHGSESH
>NZ_CP034279.1|WP_156692499.1|2548191_2548419_+|hypothetical-protein
MTVDPTDPETFETTENGEASVALDEETPEADAAEQHRELQQHGDDPLTRVDPAVANPADAAEQTRVVDQDEDDYR
>NZ_CP034279.1|WP_156692498.1|2546985_2548038_-|alpha/beta-fold-hydrolase
MSSTELPESIAATAAGPRVSAVRIAEGERLRCVTLPGLTLNVRYRPSDRTGLPPALYVHGLGGSSQNWSAVMPLLEDVVDGEAVDLPGFGDSPPPDDGNYSVTAHTRAVIRMLDAGDRGPVHLIANSLGGAVATRLAAVRPDLVATLTLISPALPELRAQRGAWPTALLALPGVASLFTRMTRDWTAEQRVRGVLSLCYGDPGRVTDEGFRNAVEEMERRLRLPYFWDAMARSARGIVDAYTLGGQQGLWRQAERVLAPTLLVYGGRDQLVSFRMARRAAAAFRDSRLLTLPDAGHVAMMEYPETVAQAVRELIHETGHGSHRTGHGKSRETGHGKTHEADHETDHENRS
>NZ_CP034279.1|WP_156692497.1|2545435_2546977_-|DUF3152-domain-containing-protein
MGRHSRKGPAPQGSDQARGAVREGARAGGRRRKNSAAPAEPQHHQGTPPAGAQQPVRGGHPEHSEQGGGRGEGRYGDWHGVPVRPTGPTGPTRPAGSTRPESPAGPGGPVGAAGPMRPPGPSDATVRTGPMRPVGPVNPSHRTSPSGPSGDPSASGPATGVGAGARIPGPRREFVEAFDDSGYGHPPRGTGHAGGGRPGQGPVSAPGEAGTPGASGSGGYEEPDGDRKTGRPGGAGKGRTFTGIAAAAVTTVLAVVVAGQVTGAGADATDARPPGEAAGRADGGAAEGGAGAARSDRSDQRAAPPGAAPPAARPTYAQLMAKRFPLDPKLKGTGAFAAVPGVDKAPGKGDKVRYRIDVEKGLALDSTLFARAVHDTLNDERSWAHNGAMTFERVSSGEADFVITLASPGTTGVWCAKSDLDTTVDNVSCDSAATERVMINAYRWAQGSATYGPDAMLAYRQMLINHEVGHRLGHNHVNCRTPGALAPVMQQQTKSLAVEGIECRPNPWVFPGG
>NZ_CP034279.1|WP_156692496.1|2543259_2545239_-|DUF3492-domain-containing-protein
MRIGLLTEGGYPYTTGESRLWCDRLVRGLAQHEFDVYALSRSARQEDAGWVPLPPQVQRVRTAPLWGREDDGCAGRGGRGRRAGRAYGRRERRRFATCFAELAAAVCRTPEAPSPDAAPRDAGSPGAGTADGTPRGTDLAAGAGAGTGPGTGSTTGFAEGLYGLADLGREHGGLSAALRSQDAVRLLESACRAGGVRRGVHGATLPDHLAFAARVERALRPLSLDWYGEDGLGAVDLCHAASGGTAALPGLLAKRFFGVPLLVTEYGVQLRAHYLSAADASLSAPVRALLAAFHGCLAAEVYRQAAVITPGNTHTRRWQEKCGADRAKLRTVYPGMEAERFAAVGESGDGGDPRTLMWVGRIEPTKDLVGLLHAFADVRRAEPEARLRIVSTPSRDAESATYRTHCEGLAAQLFPDEATDAHAVGDNPVSFEDLGSPYAPDLAHAYAAAGVVVLSSVVEGFPLGLVEAMLCGRATVSTDVGAVVEVIGGTGLVVPPRNPRALADACLSLLRDPARRERLGAAARARALELFTVEQNLAAFRGIYLELISQAPVHRDAEGVGADGEPLPFAHPAEAYVPGHWTGRGSGGATTPAWAAAEQGAAPGAYTATATRPGAPTPPPPAAAPPAPVPAAAVDSIPVVASLPVAASFPIAGKVDGHV
>NZ_CP034279.1|WP_156692495.1|2541992_2543267_-|hypothetical-protein
MSDGGTPAPGSRAPGAAPGALPARSTHAWRSHAEALLSKPAPGPADTPTTLGDGAGRERAGGGGPVARRGPADPVKALLHRHRELCERAVDPLEIAAGLEAHGVTDRTAARFRHRDVFSLAEELYARVPRGDDGTRARSAASAPGADGPWSARTTLLALLPGAVGALTVAGLAVTDGPLWAAVGVAGALALAVALTAGRTAAGTHPAAGAHTAAGTRAWTGFLLLYALFGDGLLEQLVAGGPDGPWPVDAPPLLGLALAALPADGCARLYAARARRRLADSRGLADFAARSRPLLLGAVALYTTVLAGLLALVGAALGHGSVSGGALALGVLLFLARLLAVHGFPGGAAAGLLGACAVEALACASVLAARLPGCDRLARPVEAALAGWGPGAVPTLACGGAALALLAYATAVLARASAHADTTT
>NZ_CP034279.1|WP_156692494.1|2540891_2541878_-|NAD-dependent-epimerase/dehydratase-family-protein
MRVLLLGANGFIGRYVADRLLADPAVHLTALGRGDDADVRFDLAGGSPGALTRFLDAVHPGVVINCAGTTRGGARELTRHNTVAVATVCEALRRSGCGARMVQVGCASEYGPSQPGSSTAEDAVPRPGGPYGVSKLAATELVLGSGLDAVVLRVFSPVGPGTPAGSPLGRLAEAMRRAMQTGDGELKLGGLGVQRDFVDVRDVARAVHAASLSAAQGIVNIGTGRAVRLRDAAAVLARVAGYAGSLHEQDAPGGRPALSAVGAMASIGAQRGESGPEHLAPAPHPYPDGCGSWQQADVRTARDRLGWRPRINLEESLADIWMEAACRI
>NZ_CP034279.1|WP_156692505.1|2553325_2554207_+|alpha/beta-fold-hydrolase
MSRPPTFTPPRCARAYALVTSRGEFAVLDAVPADGTEPKGTALLLPGFTGSKEDFIAMLEPLADAGYRAVAVDGRGQYETPGPADQQAYSQDELARDVLAQAAVLGAGRVHLLGHSLGGQIARAAVLLDATPFASLTLMSSGPAQVAPSQQDKIKLLSDALAVMSMDQVWDAMRALDPPEDADEAGGNREDLRRRWLLHNPAQLLATGRGLTVEPDRVDELAALRPPLPVHVISGVRDDTWPVPLLDAMAGRLAAYRTRVEGAEHSPNTDRPVETALAVARFWNACAERQSRD
>NZ_CP034279.1|WP_156692506.1|2554191_2555112_-|NYN-domain-containing-protein
MNDDPGTTPAPTLTELGARLERTNELLERMLAEVAKTPSTHAIFVDAGYVHAAAGLLVAGTEDRRSFDLDAEGLIEAFIDKARTIFADSRLLRVYWYDGARRRIHTPGQQAIAELPDVKVRLGNLNANNQQKGVDSLIRSDLESLARHRAISDAALVGGDEDLVSAVEAAQGYGARVHLWGIEAAEGRNQAEPLLWEVDSTRTFDLDFCRPYVTRRPVTTYESEGEPPPSRDEVRALGARIAATWLAERGTDAMAELLPGHPYLPGPVDQELLVEAERLLSRSLRGHAVLRRSLRDGFWQHLQSRL
>NZ_CP034279.1|WP_156692507.1|2555286_2555439_+|hypothetical-protein
MRFEILRLDDVDGTPVDTTVVDAASVNRIVQQAASIGQRIWIRPAGTSAS
>NZ_CP034279.1|WP_156692508.1|2555537_2556143_-|NAAT-family-transporter
MFDVAVFGSLFLTLFVIMDPPGITPIFLALTSGRATKVQRRMAWQAVAVAFGVITVFGILGQQILAYLHVSVPALMIAGGLLLLLIALDLLTGKTDEPKQTKDVNVALVPLGMPLLAGPGAIVSVILAVQHAEGVSGQVSVWAAIVAMHVVLWLTMRYSLLIIRVIKDGGVVLVTRLAGMMLSAIAVQQIINGVTQVVQGS
>NZ_CP034279.1|WP_156692509.1|2556474_2557347_-|PHP-domain-containing-protein
MRIDLHTHSTASDGTDTPAELVRAAAAAGLDVVALTDHDTTRGHAEAKAALAHLDRELTLVTGAELSCRIDGTGMHMLAYLFDPDEPELARERELVRDDRVPRAHAMVGKLQELGVPITWERVAGIAGDGSVGRPHIAEALVELGVVPSVSDAFTPQWLADGGRAYVDKHELDPFLAIRLVKAAGGVTVFAHPGAAKRGRTVPESVIADLAAYGLDGIEVDHMDHDEATRARLRGLAADLGLLVTGSSDYHGTRKTCGLGDHTTDPEIYGEITRRATGAFPVMGTGGTRA
>NZ_CP034279.1|WP_156692510.1|2557504_2558143_-|hypothetical-protein
MRGEPSCPKCGGRVRAPGLFSDSWQCDLHGAVQPLQPVIPPSVEALGVVTHRARVPVWMPWPLPVGWLFTGVAYAGDDRSGGRATVVACSGPGPLGGVGELLLVAEELGVGLGARYAGIDGPDPGPHMCTGTRPQAKVHAAGRPTPLWHVSDAPEDRAVFAGEARGLWLWAVVWPEKSGLLMYDELVLTDLREAGSEVELLPCGALSPRLLG
>NZ_CP034279.1|WP_156692511.1|2558310_2559537_+|MFS-transporter
MREKDPFDEGAGSILRQPRAVWATAGASVVAFMGIGLVDPILPSIAQGLHATPSQVSLLFTSYFLITAVAMLVTGFVSSRVGGRRTLLAGLALVIVFAALSGTSGSVGELVGFRAGWGLGNALFVSTSLAVIVGAAAGGSAAAILLYESALGLGMACGPLVGAVLGDASWRYPFFGTAALMAIGFLCIAAFLKDQPRPARKTSLLDPLRALGHGGLASVAASAFFYNYAFFTVLAFTPFVLDMTPYRSGAVFFAWGVLLAVFSVLVAPRLQERFGSLRVLGASLLLLAADVVVLGYGDHTTAVVCTVLSGAFIGVNNTVFTELALGVSDAPRPVASAGYNFVRWFAAAAAPWLAPRIEEWSDVHLPFVVAGASAAVGAGIVVARRRSLTREAEEHRAPEAGSPALAAN
>NZ_CP034279.1|WP_156692512.1|2559543_2560134_-|suppressor-of-fused-domain-protein
MGEVLALVEARLRTALGEPDARAAVTFLGTDRIEVLRFADAEAGLVRYATLGMSAQPMTDPTAALADPVKGPRAELVLSVRAGLADTDKALRPLAVLAASPQVEGVVVAPGASLDTGEPLWPGAPFTSVLVAEPGGLVEDLELDAPMDPVRFLPLLPMTPNEAAWKRVHGAQALQERWLTAGTDLRDPLRGSVTLA
>NZ_CP034279.1|WP_156692513.1|2560583_2561717_+|magnesium-transporter-CorA
MSMIRDLRAAVRPSLRKSSSPYNTYNSYDATRDPSTSTAVVDCAVYRDGRRLKDDTTDACLTPREAMRQVREGGGFAWIGLHEPTEAEFAGIAAEFGLHPLAVEDAVHAHQRPKLERYDDTLFTVFKTIHYVDHAELTATSEVVETGEVMCFTGRDFVITVRHGGQGSLRNLRHRMEGEPELLEKGPSAVLHAIADHVVDGYIAVADAVQIDIDQIEIDVFSPPTKGSTRGADTGRIYQLKREVLEFKRAVSPLLRPMQLLSERPMRLVDPDIQKYFRDVADHLARVQEQVIGFDELLNSILQANLAQATVAQNEDMRKITSWAAIVAVPTAVCGVYGMNFDHMPELHWKYGYPMVLTGIIGICFAIHRTLKRNGWL
>NZ_CP034279.1|WP_156692514.1|2561796_2562303_+|hypothetical-protein
MTDATLEQALVEEATKKSGLIWVRGGGPARALWHVWLDGAAHVVGDGPGEQPLPGLPDGSTAEVTVRSKDKGGRLVAWTAGVTELAPGSEPWDAAVAELKGKRLNAPDAETMTDRWARECRVLRLTPQGATTAHPDGSLAAVPLPTPVTTRRPVPAALPRLLLKRRGR

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Crispr_ID: NZ_CP034279_5

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP034279_5

2807845-2807929

Orphan

Consensus_repeat	Method
GGCGACCTCGACGCAGCTGTCGCCG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP034279_5

>merge|NZ_CP034279|5|2807845-2807929|CRISPRCasFinder
GGCGACCTCGACGCAGCTGTCGCCGGAACCGCCGCTGTAGCTGGACTTGTGCCAGGAGAGGGCGACTTCGACGCAGCTGTCGCCG

>NZ_CP034279|5|5|2807845-2807929|CRISPRCasFinder
GGCGACCTCGACGCAGCTGTCGCCG	GAACCGCCGCTGTAGCTGGACTTGTGCCAGGAGAG
GGCGACTTCGACGCAGCTGTCGCCG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP034279.1\|WP_156692707.1\|2800120_2800990_+\|L,D-transpeptidase-family-protein	unknown	unknown	gnl\|CDD\|341130
NZ_CP034279.1\|WP_156692721.1\|2815016_2816771_+\|succinate-dehydrogenase-flavoprotein-subunit	unknown	unknown	gnl\|CDD\|236185
NZ_CP034279.1\|WP_156692708.1\|2801199_2802336_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|235906
NZ_CP034279.1\|WP_156696356.1\|2808965_2810006_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP034279.1\|WP_156692720.1\|2814514_2814994_+\|succinate-dehydrogenase	unknown	unknown	gnl\|CDD\|239580
NZ_CP034279.1\|WP_156692722.1\|2816770_2817529_+\|succinate-dehydrogenase-iron-sulfur-subunit	unknown	unknown	gnl\|CDD\|235652
NZ_CP034279.1\|WP_156692709.1\|2802335_2803142_-\|sigma-70-family-RNA-polymerase-sigma-factor	unknown	unknown	gnl\|CDD\|224511
NZ_CP034279.1\|WP_156692718.1\|2813402_2813990_+\|2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline-decarboxylase	unknown	unknown	gnl\|CDD\|184333
NZ_CP034279.1\|WP_156692710.1\|2804083_2805136_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|236766
NZ_CP034279.1\|WP_156692715.1\|2810160_2810661_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP034279.1\|WP_156692704.1\|2796727_2797552_-\|MerR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|133382
NZ_CP034279.1\|WP_156692714.1\|2807975_2808800_-\|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|379262
NZ_CP034279.1\|WP_156692711.1\|2805684_2806449_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|237171
NZ_CP034279.1\|WP_156692712.1\|2806445_2807006_-\|sigma-70-family-RNA-polymerase-sigma-factor	unknown	unknown	gnl\|CDD\|131997
NZ_CP034279.1\|WP_156692706.1\|2798354_2799935_-\|methylmalonyl-CoA-mutase	unknown	unknown	gnl\|CDD\|376584
NZ_CP034279.1\|WP_156692716.1\|2810718_2811534_-\|DUF4328-domain-containing-protein	unknown	unknown	gnl\|CDD\|379508
NZ_CP034279.1\|WP_156692719.1\|2814125_2814506_+\|succinate-dehydrogenase,-cytochrome-b556-subunit	unknown	unknown	gnl\|CDD\|239581
NZ_CP034279.1\|WP_156692717.1\|2811619_2813257_-\|family-20-glycosylhydrolase	unknown	unknown	gnl\|CDD\|119334
NZ_CP034279.1\|WP_156696355.1\|2807098_2807686_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP034279.1\|WP_156692705.1\|2797612_2798272_-\|leucine-efflux-protein-LeuE	unknown	unknown	gnl\|CDD\|236807

Protein	Function_ID	Function_description	E-value
NZ_CP034279.1\|WP_156692707.1\|2800120_2800990_+\|L,D-transpeptidase-family-protein	gnl\|CDD\|341130	cd16913, YkuD_like, L,D-transpeptidases/carboxypeptidases similar to Bacillus YkuD. Members of the YkuD-like family of proteins are found in a range of bacteria. The best studied member Bacillus YkuD has been shown to act as an L,D-transpeptidase that gives rise to an alternative pathway for peptidoglycan cross-linking. Another member Helicobacter pylori Csd6 functions as an L,D-carboxypeptidase and regulates helical cell shape and motility. The conserved region contains a conserved histidine and cysteine, with the cysteine thought to be an active site residue.	1.98387e-22
NZ_CP034279.1\|WP_156692721.1\|2815016_2816771_+\|succinate-dehydrogenase-flavoprotein-subunit	gnl\|CDD\|236185	PRK08205, sdhA, succinate dehydrogenase flavoprotein subunit; Reviewed.	0
NZ_CP034279.1\|WP_156692708.1\|2801199_2802336_-\|hypothetical-protein	gnl\|CDD\|235906	PRK07003, PRK07003, DNA polymerase III subunit gamma/tau.	2.88753e-05
NZ_CP034279.1\|WP_156692719.1\|2814125_2814506_+\|succinate-dehydrogenase,-cytochrome-b556-subunit	gnl\|CDD\|239581	cd03501, SQR_TypeA_SdhC_like, Succinate:quinone oxidoreductase (SQR) Type A subfamily, Succinate dehydrogenase C (SdhC)-like subunit; SQR catalyzes the oxidation of succinate to fumarate coupled to the reduction of quinone to quinol. Members of this subfamily reduce low potential quinones such as menaquinone and thermoplasmaquinone. SQR is also called succinate dehydrogenase or Complex II, and is part of the citric acid cycle and the aerobic respiratory chain. SQR is composed of a flavoprotein catalytic subunit, an iron-sulfur protein and one or two hydrophobic transmembrane subunits. Members of this subfamily are similar to the Thermoplasma acidophilum SQR and are classified as Type A because they contain two transmembrane subunits as well as two heme groups. Although there are no structures available for this subfamily, the presence of two hemes has been proven spectroscopically for T. acidophilum. The two membrane anchor subunits are similar to the SdhD and SdhC subunits of bacterial SQRs, which contain heme and quinone binding sites. The two-electron oxidation of succinate in the flavoprotein active site is coupled to the two-electron reduction of quinone in the membrane anchor subunits via electron transport through FAD and three iron-sulfur centers. The reversible reduction of quinone is an essential feature of respiration, allowing transfer of electrons between respiratory complexes.	5.4416e-41
NZ_CP034279.1\|WP_156692720.1\|2814514_2814994_+\|succinate-dehydrogenase	gnl\|CDD\|239580	cd03500, SQR_TypeA_SdhD_like, Succinate:quinone oxidoreductase (SQR) Type A subfamily, Succinate dehydrogenase D (SdhD)-like subunit; SQR catalyzes the oxidation of succinate to fumarate coupled to the reduction of quinone to quinol. Members of this subfamily reduce low potential quinones such as menaquinone and thermoplasmaquinone. SQR is also called succinate dehydrogenase or Complex II, and is part of the citric acid cycle and the aerobic respiratory chain. SQR is composed of a flavoprotein catalytic subunit, an iron-sulfur protein and one or two hydrophobic transmembrane subunits. Members of this subfamily are similar to the Thermoplasma acidophilum SQR and are classified as Type A because they contain two transmembrane subunits as well as two heme groups. Although there are no structures available for this subfamily, the presence of two hemes has been proven spectroscopically for T. acidophilum. The two membrane anchor subunits are similar to the SdhD and SdhC subunits of bacterial SQRs, which contain heme and quinone binding sites. The two-electron oxidation of succinate in the flavoprotein active site is coupled to the two-electron reduction of quinone in the membrane anchor subunits via electron transport through FAD and three iron-sulfur centers. The reversible reduction of quinone is an essential feature of respiration, allowing transfer of electrons between respiratory complexes.	7.33791e-45
NZ_CP034279.1\|WP_156692722.1\|2816770_2817529_+\|succinate-dehydrogenase-iron-sulfur-subunit	gnl\|CDD\|235652	PRK05950, sdhB, succinate dehydrogenase iron-sulfur subunit; Reviewed.	2.76352e-146
NZ_CP034279.1\|WP_156692709.1\|2802335_2803142_-\|sigma-70-family-RNA-polymerase-sigma-factor	gnl\|CDD\|224511	COG1595, RpoE, DNA-directed RNA polymerase specialized sigma subunit, sigma24 homolog [Transcription].	2.64495e-32
NZ_CP034279.1\|WP_156692718.1\|2813402_2813990_+\|2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline-decarboxylase	gnl\|CDD\|184333	PRK13798, PRK13798, putative OHCU decarboxylase; Provisional.	1.0468e-38
NZ_CP034279.1\|WP_156692710.1\|2804083_2805136_+\|hypothetical-protein	gnl\|CDD\|236766	PRK10811, rne, ribonuclease E; Reviewed.	0.00349253
NZ_CP034279.1\|WP_156692704.1\|2796727_2797552_-\|MerR-family-transcriptional-regulator	gnl\|CDD\|133382	cd01107, HTH_BmrR, Helix-Turn-Helix DNA binding domain of the BmrR transcription regulator. Helix-turn-helix (HTH) multidrug-efflux transporter transcription regulator, BmrR and YdfL of Bacillus subtilis, and related proteins; N-terminal domain. Bmr is a membrane protein which causes the efflux of a variety of toxic substances and antibiotics. BmrR is comprised of two distinct domains that harbor a regulatory (effector-binding) site and an active (DNA-binding) site. The conserved N-terminal domain contains a winged HTH motif that mediates DNA binding, while the C-terminal domain binds coactivating, toxic compounds. BmrR shares the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements.	7.41221e-43
NZ_CP034279.1\|WP_156692714.1\|2807975_2808800_-\|helix-turn-helix-domain-containing-protein	gnl\|CDD\|379262	pfam13560, HTH_31, Helix-turn-helix domain. This domain is a helix-turn-helix domain that probably binds to DNA.	3.00372e-06
NZ_CP034279.1\|WP_156692711.1\|2805684_2806449_-\|hypothetical-protein	gnl\|CDD\|237171	PRK12678, PRK12678, transcription termination factor Rho; Provisional.	2.41563e-07
NZ_CP034279.1\|WP_156692712.1\|2806445_2807006_-\|sigma-70-family-RNA-polymerase-sigma-factor	gnl\|CDD\|131997	TIGR02952, RNA_polymerase_sigma-70_factor_ECF_subfamily, RNA polymerase sigma-70 factor, TIGR02952 family. This group of sigma factors are members of the sigma-70 family (TIGR02937). They and appear by homology, tree building, bidirectional best hits and one-to-a-genome distribution, to represent a conserved family. This family is found in a limited number of Gram-positive bacterial lineages.	9.18363e-28
NZ_CP034279.1\|WP_156692706.1\|2798354_2799935_-\|methylmalonyl-CoA-mutase	gnl\|CDD\|376584	pfam01642, MM_CoA_mutase, Methylmalonyl-CoA mutase. The enzyme methylmalonyl-CoA mutase is a member of a class of enzymes that uses coenzyme B12 (adenosylcobalamin) as a cofactor. The enzyme induces the formation of an adenosyl radical from the cofactor. This radical then initiates a free-radical rearrangement of its substrate, succinyl-CoA, to methylmalonyl-CoA.	0
NZ_CP034279.1\|WP_156692716.1\|2810718_2811534_-\|DUF4328-domain-containing-protein	gnl\|CDD\|379508	pfam14219, DUF4328, Domain of unknown function (DUF4328). This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 218 and 342 amino acids in length.	1.73594e-29
NZ_CP034279.1\|WP_156692717.1\|2811619_2813257_-\|family-20-glycosylhydrolase	gnl\|CDD\|119334	cd06564, GH20_DspB_LnbB-like, Glycosyl hydrolase family 20 (GH20) catalytic domain of dispersin B (DspB), lacto-N-biosidase (LnbB) and related proteins. Dispersin B is a soluble beta-N-acetylglucosamidase found in bacteria that hydrolyzes the beta-1,6-linkages of PGA (poly-beta-(1,6)-N-acetylglucosamine), a major component of the extracellular polysaccharide matrix. Lacto-N-biosidase hydrolyzes lacto-N-biose (LNB) type I oligosaccharides at the nonreducing terminus to produce lacto-N-biose as part of the GNB/LNB (galacto-N-biose/lacto-N-biose I) degradation pathway. The lacto-N-biosidase from Bifidobacterium bifidum has this GH20 domain, a carbohydrate binding module 32, and a bacterial immunoglobulin-like domain 2, as well as a YSIRK signal peptide and a G5 membrane anchor at the N and C termini, respectively. 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.	4.88126e-81
NZ_CP034279.1\|WP_156692705.1\|2797612_2798272_-\|leucine-efflux-protein-LeuE	gnl\|CDD\|236807	PRK10958, PRK10958, leucine export protein LeuE; Provisional.	9.48589e-104

>NZ_CP034279.1|WP_156696355.1|2807098_2807686_-|hypothetical-protein
MVSTLRRADGGADWDAKAGSLEWTCWETVEHLADDLFAYAAQLGPERPPLDGPVPFLWEPRRPGGPANVTYADRKAGPAGLLQVLEACGAMLAAMVRVTPAEVRAHHVFGASDAEGFAAMGVVETLVHAHDVTQGLGLPWDPPPELCRRVLRRLFPDAPTATPAWATLLWATGRGGLPGRERLTSWRWYGAANGG
>NZ_CP034279.1|WP_156692712.1|2806445_2807006_-|sigma-70-family-RNA-polymerase-sigma-factor
MGAYDTELGAAVERAQRGDEVAFARAYRLVHPGLLGYVRGLVGDDAEDVAAEAWLEIARDLGRFRGDGAGFRGWTATIARNRALDHLRKQRRSPRTATLEQDVLDLPDAQDTAGAALESLSTAHVLAMVRGLPPDQAEAVLLRVVVGLDGPATARVLGKRPGAVRTAAYRGLRKLAGRLAQGGARG
>NZ_CP034279.1|WP_156692711.1|2805684_2806449_-|hypothetical-protein
MRRDRKRLRDGDAADRDTAVRAALLAALVPGGEADPAGEERAVAAFRAARDEGRHAGARGLGRQGDWRPGRERRRRRSLRAGAMGLAATVLLGGVAVAAQSGAIRSPFGGGGGGAAPEPRPSVTSTPPDVTGAPDATRAPGGEPQGPGPSRQHPTTTPSDRPGDHKDGDDERAKGRETNGKKNHGRDQDQDRGGSHNDKGWAHRHDKDRDTGRDREKAKDHSREKDPDRDRGTGQQKGRVGPGQDREHDRGRGR
>NZ_CP034279.1|WP_156692710.1|2804083_2805136_+|hypothetical-protein
MTAPAAAQPVAVDAEPRLPAVLSESVEDATVQARSVQAHWTPERIKNALANPLQAPADDLPSDETSAETSGSDLPEITASAEAVLPADHKAAVDARAAQAAAVPKAKEVASPQAWPNRVVGKLLFQVPGKGDASCSATVIASKTKNAVWTAAHCLHKGSGGANGFYKSFIFLPGYHEDTYPSGWWYHKRVIVPDTWGKSGDLRSSDMGALVMASGEPAYGNLQDEVGAWGYQFSDATDHADVHSMGYPSDGYGRPNKDFHYGSTMMYCRGKTIDAGNLNPLDNRLRLTCDMGHGSSGGPMASAYNSGKPKIVGVNSHRDADKNGKWTKPYMYSSNHGKVAVAVIDLVNKG
>NZ_CP034279.1|WP_156692709.1|2802335_2803142_-|sigma-70-family-RNA-polymerase-sigma-factor
MDVMPFDHVACCCAPGVATAVTSRDDEQVVGVLGDDAELTTAVLAAQDGDEDAFRAVYRAVHPRLLGYIRTLVGDADAEDVASESWLQIARDLDRFSGDADRFRGWAARIARNRALDHLRMRGRRPSIGGDETELAEKPAESDTADEAMEALATGRTMDLIAQLPQDQAEAVILRVVVGLDAKSAAKTLGKRPGAVRTAAHRGLKRLAELMDADAAPGAGPAGVESAGGAGGTLSAALGVVPPQPKRRAVSGVRTGVTQWRSRTQKDM
>NZ_CP034279.1|WP_156692708.1|2801199_2802336_-|hypothetical-protein
MADERDEWLDHDAAENLLRGEPVGPVADHARERARKVERALDALRATAHPAAGGLPGEEAALAAFRQARAEKAAGAAAAGAAATGTAGAATASGGAGVAGVPEVGTVRTRPGPRRRMRWGRPVRWGLAASVAGLAVGGVAVGAGTGVLPVLGGDSEPLPAASVSAAASDEPEAAGPTGGTDAGTPGTPEEPGAVPPSASATPGPGTDREPGRPDPEGSGDSGTTGGTVGEPGGDLGEVTGGGSGSASAGVSGSSGDGRGDTWLARTAQDCRDYRDGRLDLDRRERLADEAKGVALIKILCDRVLAAEEHQQGGSPGSGSSGSGGGAPGGGGHGTGAGGGSGGDGEGRGDGDGSDTARPSASWRPLAPALTVRRTGLAF
>NZ_CP034279.1|WP_156692707.1|2800120_2800990_+|L,D-transpeptidase-family-protein
MHRTSVIRRAALAAAAVATALAATGCAGQAVGAAGGPASASSTPSGAPASGDATASPSSAASAAGGAAPAASAPASPDAAKVLMAEGTETEQVRELQARLRQLGHFHRSPTAFYGSMTGKAVSAFQEKQGLPATAKVDGTTWAKLTAASRTPTAGELRPPTTNELDKPDERCMTGRVLCISKESRTLAWMVDGKVVSAMDVRFGSENTPTREGIFKVDRKEREWESTLYHTSMPYSMFFSGGQAVHYSSDFKARGYNGGSHGCVNVRDMDRLAAVFGQVKVGDKVVVHW
>NZ_CP034279.1|WP_156692706.1|2798354_2799935_-|methylmalonyl-CoA-mutase
MARESESGLPIEPVYGPDALSGWDHDEKLGDPGSYPFTRGVYPSMYTGRPWTMRQYAGFGTAVESNARYQQLIANGTMGLSVAFDLPTQMGHDSDAPIAHGEVGKVGVAIDSIDDMRVLLGGIPLDKVSTSMTINAPAALLLLLYQLVGEEQGVPADRLTGTIQNDVLKEYIARGTYIFPPKPSLRLIADIFKYCRAEIPKWNTISISGYHMAEAGASPAQEIAFTLANGIEYVRTAVAAGMDVDDFAPRLSFFFVARTTILEEVAKFRAARRIWARVMRDEFGAKNPKSMMLRFHTQTAGVQLTAQQPEVNLVRVAVQGLAAVLGGTQSLHTNSFDEAIALPTDKSARLALRTQQVLAYETDVTATVDPFAGSYVVERMTDDVEEAAVALMARVEDLGGAVDAIERGFQKNEIERSAYRVAQETDSGERVVVGVNRFQLDEEEPYEPLRVDPAIEAQQAERLAGLRAGRDQEAVDSALAALKKAAEGTDNVLYPMKDALRARATVGEVCNALREVWGTYVPTDAF
>NZ_CP034279.1|WP_156692705.1|2797612_2798272_-|leucine-efflux-protein-LeuE
MLGVTDLPTYLAGLALIILLPGPNSLYVLSVAARRGVRTGYAAASGVWCGDTVLMTLSAAGVASLLQANALLFGIVKFAGAGYLTWLAVGMLRAAWLLWRTRRERVAEEPGEAAPAPAAERPFRRAFVISLLNPKAILFFIAFFVQFVDPAYQYPALSFVVLGALAQAASVLYLTVLIFTGTHLAAAFRRRRRLSAGATSAAGALFLGFAVKLSLTSTA
>NZ_CP034279.1|WP_156692704.1|2796727_2797552_-|MerR-family-transcriptional-regulator
MFTIGDFARHGRVSVRMLRHYDAVGLLRPAHVDPHSGYRYYEAGQLARLNRVIALKDLGFTLDQVGSILDEEVGAEELRGMLRLRQAELESAMSEAAARLAQVGARLRAIESEGHMSTQDVVVKSVPGARLAVLKGTAAGFGPDQIGPVIGPLYQELCARLAAAGALECGGPGIAYYEDAPAGDGSIVVHAGMTLPAGVTVPDVEIVELPGIDQAATVVHRGPMEALLPTIQTLATWIDTNGYRSAGYSRELYLEWSQDPARWVTEIQEPIVPA
>NZ_CP034279.1|WP_156692714.1|2807975_2808800_-|helix-turn-helix-domain-containing-protein
MTEGITEPERSESLKTFGAVLQAFRENARHTQETLAPELGYSVHYLASVEQGRRFPTREFVERAEETLDAFGALRKASRHLTRKPGLAIWFQKWALLEASAITLDTYEPRVLPGLLQTEAYARTLFRGQLPPLSDEQVEAQLLARLERQRLLRDRPNTAYSFILEEHLFHHRVGGTEVTRELLDHVLEVVQLRNVEVQVLPLGRGHHAGLGGPIQLAETPEHEWLAYCEAQRGGQFIAESKEISVLQMRYGKLRAQALTPDDSKGLLSQLRGAL
>NZ_CP034279.1|WP_156696356.1|2808965_2810006_-|hypothetical-protein
MAGSAACGTVEQLSAGKKLDRAFEKLGKEKTLSFELDLDTDAASLKALDAKSEPEPGEELPDEAADLLSGAKISFTVESTKPIEKSGEKDYVGMAMKVTTPDGDLAEFRQVGDWGYIRTDPKALEKISGEPMPDSKELPPEAGAFKDVLEGKWVKFNTKEMEKAGGQGAGTPSPEPTLDAKTQEKLLDSLREVVSREVEFTTGKSEDGTEHITAVAPFRTLITELIGEIRPLAKDLPPGMELPTDKDLKDAPNAKVTADFALKNGELKEVRVDLAKLAEDAKVKKFGLVLRLGEGQKPTAPAGATELDLEGFLGGFAGPSMDEEGFDETATDPEGFPVEGFPEDAA
>NZ_CP034279.1|WP_156692715.1|2810160_2810661_-|hypothetical-protein
MSHSVQQLIAHAGERGLAASALACLDRCLPLLDPAPDDLLRPLWRGVAEGGAGWADGLAEVRGLVADVEGDAVLVRKMLGAAPSDWDATALRPWAEMCSAAALELHERLGGGPLVDGEERRQAQILEYLETTASDDPPAGLRPVLDVSAEGRRVLRAVVSRRERSA
>NZ_CP034279.1|WP_156692716.1|2810718_2811534_-|DUF4328-domain-containing-protein
MLCTNCGLNTVSTREGLCGVCAVTAPGAPAAPPGVTGSRGGTFLQSPVGLGRAVVVLLCAVAAVDLFAVFTDLRLYGFVSDLAAGTWEGMEEEAERADLLLEWGGRLQVLGIVATGVVFIIWLHRVRKNAAVFAPDVVTSGAGWAIGGWFVPIANLFMPRRIARESWRASTRHPHGAPEKGERATVLNTWWTLWLLTMFTGRAAGALYDRAETVDELVRAARMYVVADTVSTAAALCAALFVHRLTTMQHAKALRGPGPVVAEPMVSSHTQ
>NZ_CP034279.1|WP_156692717.1|2811619_2813257_-|family-20-glycosylhydrolase
MDGGKRVNRHSTGGLVAVAVLSLTVAGCGDGDGADRGTSAPGTATTPAATSPAPETSPDPSPTRTYPLSTAPATIPAVREHEPARGPGWKPGAGSAVVVAKGSGALADEARLLAGELKTAYRGEAAARPGDVELALNTGQAGGPESYTLTTRDGKVRISAPDEAGAFYGTRTVKQALRSGGTVPEGVVRDRPAKPQRGLNLDIARKHFDAAWIEDRLRDMADLKLNQLVLHFSDDQGFRIASTSHPEVVSKDHLTTAQVRRIIALANRLHIDVVPEVDSPGHLGAVLRAHPQLQLRNVQGAPRQGAIDISKPESARIVDDLIREYAALFPGPWFHVGADEYQALTVRDPAASYPQLARAARQEFGANATVEDLATGWLNDRAAVANAAKKKAKAWNDGFFAGGTVTANKNIEVEYWTGKEIGAREPVSYLAEGRKVVNLNDEYLYYVLGEPNEFTYPTGRRIYEEWTPRVLRGSSAAPERYAGQILGGRFAVWCDLADAQTQAQVADGIRMPLRATAQKLWDPATPELTWQQFQALANKLGSTGA
>NZ_CP034279.1|WP_156692718.1|2813402_2813990_+|2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline-decarboxylase
MAGDSNAAAARARAIPAPGRAGHASGGPAVRTPEGLAAFNAAPAGAAEAALLACCGSRGWARRVAAHRPYPTLDALLAAADEAGYDLHGEDLDEALADETSADLPPGTPAAAHTAWEAAQSQYESRFHHAFVICLDGHRPAEQLNQALSAIHTRMSHPPEKERAIAADELRRLARARLSRLIGRADTVGSPSVPV
>NZ_CP034279.1|WP_156692719.1|2814125_2814506_+|succinate-dehydrogenase,-cytochrome-b556-subunit
MPAGTLYRGREGMWSWVAHRVTGVLIFFFLFVHVLDTALVRVSPEAYDEVVATYKTPIVALLEYGLVAAILFHALNGLRVIAVDFWSKGPRYQKQMLWTVMGIWFVLMVGALYPVLGHAVREVFGS
>NZ_CP034279.1|WP_156692720.1|2814514_2814994_+|succinate-dehydrogenase
MSTDLTKSAVGPVEGVGLYDADNPAPVIEPPRKRTGKTPKSTRGNFEMAAWLFMRLSGIVLVVLVIGHLLIQLVLDGGVSKIGFAFVAGRWASPFWQVWDLLMLWLAMLHGANGLRTVINDYAERPNTRLWLKGLLYTATVFTILLGTLVIFTFDPNIR
>NZ_CP034279.1|WP_156692721.1|2815016_2816771_+|succinate-dehydrogenase-flavoprotein-subunit
MKIHKYDTVIVGAGGAGMRAAIEATKRSRTAVLTKLYPTRSHTGAAQGGMAAALANVEEDNWEWHTFDTVKGGDYLVDQDAAEILAKEAIDAVLDLEKMGLPFNRTPGGTIDQRRFGGHSRNHGEAPVRRSCYAADRTGHMILQTLYQNCVKEGVEFFNEFYVLDQLITEVDGVKKSAGVVAYELATGEIHVFQAKAVIYASGGTGKFFKVTSNAHTLTGDGQAACYRRGLPLEDMEFFQFHPTGIWRMGILLTEGARGEGGILRNKDGERFMEKYAPVMKDLASRDVVSRSIYTEIREGRGCGPEGDHVYLDLTHLPPEQLDAKLPDITEFARTYLGIEPYTDPIPIQPTAHYAMGGIPTNVEGEVLSDNTTVVPGLYAAGEVACVSVHGANRLGTNSLLDINVFGKRAGIAAAEYSAKADYVELPENPASFVQEQVERLRNSTGSERVSVLRKELQETMDANVMVFRTEQTIKTAVEKIAELRERYLNVSVQDKGKRFNTDLLEAIELGNLLDLAEVMAVSALARKESRGGHYREDYPNRDDVNFMRHTMAYREVGADGSETVRLDYKPVVQTRYQPMERKY
>NZ_CP034279.1|WP_156692722.1|2816770_2817529_+|succinate-dehydrogenase-iron-sulfur-subunit
MATPTLEKREAGFADSPYITATFRIRRFNPEVSEHAVWEDFQIEIDPKERVLDALHKIKWDVDGSLTFRRSCAHGICGSDAMRINGKNRLACKTLIKDINPEKPITVEAIKGLTVLKDLVVDMEPFFQAYRDVMPFLITTGNEPTRERLQSAEDRERFDDTTKCILCAACTSSCPVFWNDGQYFGPAAIVNAHRFIFDSRDEAGEQRLEILNDKDGVWRCRTTFNCTDACPRGIEVTKAIQEVKRALITRRF

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Crispr_ID: NZ_CP034279_6

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP034279_6

2956051-2956202

Orphan

Consensus_repeat	Method
AGCAACCGTGCGTCAGACGCGGCGGCGCTTCGGCGGACGGCAGCCGT	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP034279_6

>merge|NZ_CP034279|6|2956051-2956202|CRISPRCasFinder
AGCAACCGTGCGTCAGACGCGGCGGCGCTTCGGCGGACGGCAGCCGTGCTGCGAATTCCCGGGGGACGACCCCCGGACCCCCAGCAGACCGCCGACCCGCCCGTCAGCAGCCGTGCGTCAGACGCGGCGGCGCTTCGGCGGACGGCAGCCGT

>NZ_CP034279|6|6|2956051-2956202|CRISPRCasFinder
AGCAACCGTGCGTCAGACGCGGCGGCGCTTCGGCGGACGGCAGCCGT	GCTGCGAATTCCCGGGGGACGACCCCCGGACCCCCAGCAGACCGCCGACCCGCCCGTC
AGCAGCCGTGCGTCAGACGCGGCGGCGCTTCGGCGGACGGCAGCCGT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP034279.1\|WP_156692822.1\|2948168_2949527_-\|phosphoglucosamine-mutase	unknown	unknown	gnl\|CDD\|237672
NZ_CP034279.1\|WP_064069940.1\|2954352_2954841_-\|50S-ribosomal-protein-L17	unknown	unknown	gnl\|CDD\|235522
NZ_CP034279.1\|WP_041130781.1\|2961621_2961804_-\|50S-ribosomal-protein-L30	unknown	unknown	gnl\|CDD\|180163
NZ_CP034279.1\|WP_003956442.1\|2957374_2957596_-\|translation-initiation-factor-IF-1	unknown	unknown	gnl\|CDD\|178954
NZ_CP034279.1\|WP_156692827.1\|2956638_2957019_-\|30S-ribosomal-protein-S13	unknown	unknown	gnl\|CDD\|235358
NZ_CP034279.1\|WP_031076680.1\|2962452_2962836_-\|50S-ribosomal-protein-L18	unknown	unknown	gnl\|CDD\|235524
NZ_CP034279.1\|WP_031076704.1\|2949638_2950157_-\|30S-ribosomal-protein-S9	unknown	unknown	gnl\|CDD\|178888
NZ_CP034279.1\|WP_156692824.1\|2950870_2952493_-\|ATP-binding-cassette-domain-containing-protein	unknown	unknown	gnl\|CDD\|223562
NZ_CP034279.1\|WP_156692825.1\|2952548_2953433_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP034279.1\|WP_003956430.1\|2954921_2955944_-\|DNA-directed-RNA-polymerase-subunit-alpha	unknown	unknown	gnl\|CDD\|235359
NZ_CP034279.1\|WP_156692826.1\|2953394_2954261_-\|tRNA-pseudouridine(38-40)-synthase-TruA	unknown	unknown	gnl\|CDD\|234577
NZ_CP034279.1\|WP_156692828.1\|2957793_2958645_-\|type-I-methionyl-aminopeptidase	unknown	unknown	gnl\|CDD\|235576
NZ_CP034279.1\|WP_126886732.1\|2961164_2961620_-\|50S-ribosomal-protein-L15	unknown	unknown	gnl\|CDD\|235523
NZ_CP034279.1\|WP_156692820.1\|2946128_2947130_+\|type-I-pantothenate-kinase	unknown	unknown	gnl\|CDD\|235466
NZ_CP034279.1\|WP_156692821.1\|2947159_2948101_+\|DUF389-domain-containing-protein	unknown	unknown	gnl\|CDD\|129372
NZ_CP034279.1\|WP_156692830.1\|2959420_2960740_-\|preprotein-translocase-subunit-SecY	unknown	unknown	gnl\|CDD\|236412
NZ_CP034279.1\|WP_156692829.1\|2958761_2959421_-\|adenylate-kinase	unknown	unknown	gnl\|CDD\|234711
NZ_CP034279.1\|WP_003956441.1\|2957203_2957317_-\|50S-ribosomal-protein-L36	unknown	unknown	gnl\|CDD\|179039
NZ_CP034279.1\|WP_156692823.1\|2950201_2950645_-\|50S-ribosomal-protein-L13	unknown	unknown	gnl\|CDD\|181703
NZ_CP034279.1\|WP_128554712.1\|2961803_2962409_-\|30S-ribosomal-protein-S5	unknown	unknown	gnl\|CDD\|234790

Protein	Function_ID	Function_description	E-value
NZ_CP034279.1\|WP_156692822.1\|2948168_2949527_-\|phosphoglucosamine-mutase	gnl\|CDD\|237672	PRK14318, glmM, phosphoglucosamine mutase; Provisional.	0
NZ_CP034279.1\|WP_064069940.1\|2954352_2954841_-\|50S-ribosomal-protein-L17	gnl\|CDD\|235522	PRK05591, rplQ, 50S ribosomal protein L17; Validated.	3.09394e-62
NZ_CP034279.1\|WP_041130781.1\|2961621_2961804_-\|50S-ribosomal-protein-L30	gnl\|CDD\|180163	PRK05611, rpmD, 50S ribosomal protein L30; Reviewed.	9.43347e-27
NZ_CP034279.1\|WP_003956442.1\|2957374_2957596_-\|translation-initiation-factor-IF-1	gnl\|CDD\|178954	PRK00276, infA, translation initiation factor IF-1; Validated.	7.62048e-47
NZ_CP034279.1\|WP_156692827.1\|2956638_2957019_-\|30S-ribosomal-protein-S13	gnl\|CDD\|235358	PRK05179, rpsM, 30S ribosomal protein S13; Validated.	1.04719e-74
NZ_CP034279.1\|WP_031076680.1\|2962452_2962836_-\|50S-ribosomal-protein-L18	gnl\|CDD\|235524	PRK05593, rplR, 50S ribosomal protein L18; Reviewed.	2.96731e-54
NZ_CP034279.1\|WP_031076704.1\|2949638_2950157_-\|30S-ribosomal-protein-S9	gnl\|CDD\|178888	PRK00132, rpsI, 30S ribosomal protein S9; Reviewed.	1.08082e-73
NZ_CP034279.1\|WP_156692824.1\|2950870_2952493_-\|ATP-binding-cassette-domain-containing-protein	gnl\|CDD\|223562	COG0488, Uup, ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only].	7.28265e-94
NZ_CP034279.1\|WP_156692828.1\|2957793_2958645_-\|type-I-methionyl-aminopeptidase	gnl\|CDD\|235576	PRK05716, PRK05716, methionine aminopeptidase; Validated.	3.58136e-123
NZ_CP034279.1\|WP_003956430.1\|2954921_2955944_-\|DNA-directed-RNA-polymerase-subunit-alpha	gnl\|CDD\|235359	PRK05182, PRK05182, DNA-directed RNA polymerase subunit alpha; Provisional.	0
NZ_CP034279.1\|WP_156692826.1\|2953394_2954261_-\|tRNA-pseudouridine(38-40)-synthase-TruA	gnl\|CDD\|234577	PRK00021, truA, tRNA pseudouridine(38-40) synthase TruA.	3.45028e-106
NZ_CP034279.1\|WP_156692829.1\|2958761_2959421_-\|adenylate-kinase	gnl\|CDD\|234711	PRK00279, adk, adenylate kinase; Reviewed.	3.43365e-134
NZ_CP034279.1\|WP_126886732.1\|2961164_2961620_-\|50S-ribosomal-protein-L15	gnl\|CDD\|235523	PRK05592, rplO, 50S ribosomal protein L15; Reviewed.	3.66585e-68
NZ_CP034279.1\|WP_156692820.1\|2946128_2947130_+\|type-I-pantothenate-kinase	gnl\|CDD\|235466	PRK05439, PRK05439, pantothenate kinase; Provisional.	0
NZ_CP034279.1\|WP_156692821.1\|2947159_2948101_+\|DUF389-domain-containing-protein	gnl\|CDD\|129372	TIGR00271, Uncharacterized_protein_MJ0678, uncharacterized hydrophobic domain. This domain is in a family of archaeal proteins that includes AF0785 of Archaeoglobus fulgidus and in several eubacterial proteins, including the much longer protein sll1151 from Synechocystis PCC6803.	1.13258e-54
NZ_CP034279.1\|WP_156692830.1\|2959420_2960740_-\|preprotein-translocase-subunit-SecY	gnl\|CDD\|236412	PRK09204, secY, preprotein translocase subunit SecY; Reviewed.	0
NZ_CP034279.1\|WP_003956441.1\|2957203_2957317_-\|50S-ribosomal-protein-L36	gnl\|CDD\|179039	PRK00465, rpmJ, 50S ribosomal protein L36; Reviewed.	3.28149e-12
NZ_CP034279.1\|WP_156692823.1\|2950201_2950645_-\|50S-ribosomal-protein-L13	gnl\|CDD\|181703	PRK09216, rplM, 50S ribosomal protein L13; Reviewed.	1.75709e-100
NZ_CP034279.1\|WP_128554712.1\|2961803_2962409_-\|30S-ribosomal-protein-S5	gnl\|CDD\|234790	PRK00550, rpsE, 30S ribosomal protein S5; Validated.	3.91293e-92

>NZ_CP034279.1|WP_003956430.1|2954921_2955944_-|DNA-directed-RNA-polymerase-subunit-alpha
MLIAQRPSLTEEVVDEYRSRFVIEPLEPGFGYTLGNSLRRTLLSSIPGAAVTSIRIDGVLHEFTTVPGVKEDVTDLILNIKQLVVSSEHDEPVVMYLRKQGPGLVTAADIAPPAGVEVHNPDLVLATLNGKGKLEMELTVERGRGYVSAVQNKQVGQEIGRIPVDSIYSPVLKVTYKVEATRVEQRTDFDKLIVDVETKQAMRPRDAMASAGKTLVELFGLARELNIDAEGIDMGPSPTDAALAADLALPIEELELTVRSYNCLKREGIHSVGELVARSEADLLDIRNFGAKSIDEVKAKLAGMGLALKDSPPGFDPTAAADAFGADDDADAGFVETEQY
>NZ_CP034279.1|WP_064069940.1|2954352_2954841_-|50S-ribosomal-protein-L17
MPKPAKGARLGGSAAHEKLLLANLAKSLFEHGRITTTEAKARRLRPVAERLITKAKKGDIHNRRLVLQTITDKGIVHTLFTEIAPRYAERPGGYTRITKIGNRRGDNAPMAVIELVEGEIAKKATVAEAEAATKRAVKESDEAAKAEDTKADEAPAEESKDA
>NZ_CP034279.1|WP_156692826.1|2953394_2954261_-|tRNA-pseudouridine(38-40)-synthase-TruA
MSDEVEPGFVRVRLDLSYDGKDFHGWAKQAGGQRTVQGDIEDALRTVTRSSETYELTVAGRTDAGVHARGQVAHVDLPEAVWAEHRDKLLRRLAGRLAHDVRVWRVEEAPSGFNARFSAIWRRYAYRVTDTPGGVDPLLRGHILWHDWPLDVDAMNAAAEALVGEHDFAAYCKKREGATTIRTLQELRWERLPSGVLEATVKADAFCHNMVRSLVGALLFVGDGHRPADWPGKVLAAGVRDSAVHVVRPHGLTLEEVGYPADELLAARNLEARNKRSLPSGGRSGGCC
>NZ_CP034279.1|WP_156692825.1|2952548_2953433_+|hypothetical-protein
MSFGGPQWPQQPHDPYQQHQQPTAQTPDWSALAEASAARTRRKRLLLIGGAALATALVGTLIATAIVSANKKGDDGANLADTTSAAPELPTDTAKPQPSFSSVAPPPPPDPMDFISSAAKDKAPIGPDTLFPGKKLTMGDRVHRKGATASTTDCGSAAEDGLGAVLERNGCTRVIRATYERDGVAVTVGVALFDTEAAALKAKEQAVGSVVPLAGSGVKGFCQSQTVCLRRTNTLGRYAYFTQAGFTSGKKVTTGEKAVYKASDDLAAFTFNQIYARGRTQASAAATAPAAGGQ
>NZ_CP034279.1|WP_156692824.1|2950870_2952493_-|ATP-binding-cassette-domain-containing-protein
MGHVEVAHVEYFLPDGRALLGDVSFRVGEGAVVALVGANGAGKTTLLRLISGDLQPHGGTVTVSGGLGVMPQFVGSVRDERSVRDLLVSVAPARIREAAAAVDAAEHLIMTVDDEAAQMAYAQALSDWAEARGYEAETVWDMCTMAALGVPYEKAQFREVRTLSGGEQKRLVLEALLRGPEEVLLLDEPDNYLDVPGKRWLEERLGETRKTVLFVSHDRELLARAAEKIVAVEPGPAGSDVWVHGGGFATFHEARRERFARFEELKRRWEEKHAQLKKLVVNLRQAASVSHEMASRYAAAQTRLRKFEEAGPPPEPPREQDIRMRLRGGRTGVRAVTCAGLELAGLMKPFDLEVFYGERVAVLGSNGSGKSHFLRLLAGDASVAYTGSFKLGARVVPGHFAQTHAHPELLGRTLVDILWTEHARDRGGAMSVLRRYELERQGDQVFDRLSGGQQARFQILLLELAGTTALLLDEPTDNLDLESAEALQVGLEAYEGTVLAVTHDRWFARAFDRYLVFGSDGVVRETPEPVWDERRVERAR
>NZ_CP034279.1|WP_156692823.1|2950201_2950645_-|50S-ribosomal-protein-L13
MRTYSPKPGDVTRQWHIIDAQDVVLGRLATTAANLLRGKHKPVYAPHMDMGDFVIIINADKVHLSGNKRTQKMAYRHSGYPGGLRSVRYDELLDKNPEKAVEKAIKGMIPKNSLGRQMLSKLKVYAGENHPHAAQQPVPFEITQVAQ
>NZ_CP034279.1|WP_031076704.1|2949638_2950157_-|30S-ribosomal-protein-S9
MAETTVENPIEGEETYAEVTTFESEVPVEGEYTSESLASRFGEPQPAAGLGRRKNAIARVRIVPGTGKWKINGRTLEDYFPNKVHQQEVNEPFKVLELDNRYDVIARISGGGVSGQAGALRLGVARALNEADVDNNRGPLKKAGFLSRDDRAVERKKAGLKKARKAPQYSKR
>NZ_CP034279.1|WP_156692822.1|2948168_2949527_-|phosphoglucosamine-mutase
MGRLFGTDGVRGVANADLTAELALGLSVAAAHVLAEAGTFEGHRPTAVVGRDPRASGEFLEAAVVAGLASAGVDVMRVGVLPTPAVAFLTGALGADLGVMLSASHNAMPDNGIKFFARGGHKLADELEDRIESVYEQHRTGEPWDRPTGAGVGRVADYQEGFDQYVAHLLSVLPNRLDGLKIVLDEAHGAASGVSPAAFQQAGAEVITIGATPDGLNINDGCGSTHLGMLKAAVVEHGADLGIAHDGDADRCLAVDHTGAEVDGDQILAVLALAMREAGTLRGDTVVATVMSNLGFKLAMEREGLQLVQTAVGDRYVLESMKEHGYALGGEQSGHVIVLDHATTGDGTLTGLMLAARVAATGRSLADLAGVMERLPQVLINVKDVDKSRVKTSAELGTAVADAERRLGSTGRVLLRPSGTEPLVRVMVEAADIEQARSVAGELADVVKSALG
>NZ_CP034279.1|WP_156692821.1|2947159_2948101_+|DUF389-domain-containing-protein
MLHLRLIVPADRTDEVVAAIEKTVGTTHLVVVPGAARDPVGDLVLCDVAREAGDELISGLRALGLDRDGSIAVEDIGLSLSERANQAEEDAPGEGADAVLWEQLQDATHEESTLSVTYVAFLTLATMIAACGVVLDNAILVVGAMAVGPEFGPLAGVCTALVQRRPRLAGRSLVALLVGFAAAMGLTVLFSLGMNATGLFTEDMLHGDRPNTGFVYAPDWFSFVVGLLAGAAGTLSLTSAKSGALVGVAISVTTVPAAANAAVALAYGDLGQTRGSVEQLLLNLLAIVLAGTLTLLAQKFFWARQRRRGPVKA
>NZ_CP034279.1|WP_156692820.1|2946128_2947130_+|type-I-pantothenate-kinase
MACVITSPPRSAAAHRRAEATPYVDLTRAEWSALREKTPLPLTADEVERLRGLGDVIDLDEVRDIYLPLSRLLNLYVGATANLRGALNTFLGDVGQKSAQRGTPFVIGVAGSVAVGKSTVARLLQALLARWPEHPRVELVTTDGFLLPMKELQARGLMSRKGFPESYDRRALTRFVADIKAGKDEVTAPVYSHLIYDIVPGRRLTVRRPDILIVEGLNVLQPALPGKDGRTRVGLADYFDFSVYVDARPEDIEAWYLNRFRKLRATAFQDPSSYFRKYTQVSEEEALDYARTMWRTINKVNLLENVAPTRGRATLVVRKGPDHKVQRLSLRKL
>NZ_CP034279.1|WP_156692827.1|2956638_2957019_-|30S-ribosomal-protein-S13
MARVSGVDIPREKRVEIALTYVFGIGRTRSKEILASTGVNPNTRVRDLSEEDLVKIREYVDANLRTEGDLRREIQGDIRRKIEIQCYQGIRHRRGLPVHGQRTSTNARTRKGPRRAIAGKKKPGKK
>NZ_CP034279.1|WP_003956441.1|2957203_2957317_-|50S-ribosomal-protein-L36
MKVKPSVKKICDKCKVIRRHGRVMVICDNLRHKQRQG
>NZ_CP034279.1|WP_003956442.1|2957374_2957596_-|translation-initiation-factor-IF-1
MAKKQGAIEIEGTVIESLPNAMFKVELQNGHKVLAHISGKMRMHYIRILPDDRVVVELSPYDLTRGRIVYRYK
>NZ_CP034279.1|WP_156692828.1|2957793_2958645_-|type-I-methionyl-aminopeptidase
MVQIKTPEQIAKMREAGLVVAAIHAATREAAVPGATTKDLDEVARKVIADHGAKSNFLGYGGFPATICTSVNEVVVHGIPSDDVVLKDGDIISIDCGAIVDGWHGDAAYTAFVGSGHAPELIELSRVTEESMWAGIAAMRNGNRLMDISRAIESYIRRQPRPSTGEHSLGKFGIIEDYGGHGIGTEMHMDPHLLNYVTRKRGKGPKLVPGFCLAIEPMVSLGTPRTEVLEDDWTVITTDGTWSSHWEHSVALTEEGPLVLTSPDGGKAKLAELGVTAAPDPLA
>NZ_CP034279.1|WP_156692829.1|2958761_2959421_-|adenylate-kinase
MRIVLVGPPGAGKGTQAAFLAKNLSIPHISTGDLFRANISQGTELGLKAKSYMDAGELVPDEVTIGMAKDRMEHPDAVNGFLLDGFPRNVSQAEALDVMLRAGNMKLDAVLDLEVPEDEVVKRIAGRRLCRNNDKHVFHVTYTPPKTEGVCDVCGGELYQRGDDSEETVRRRLEVYHTQTEPIIDYYKAQGLVVTISALGKVDEVTGRAMAALRGEQAA
>NZ_CP034279.1|WP_156692830.1|2959420_2960740_-|preprotein-translocase-subunit-SecY
MLTAFARAFKTPDLRKKLLFTLGIIVIYRLGAHIPVPGVDYQSVQQCVDEASKGGNSLLGLVNLFSGGALLQITIFALGIMPYITASIILQLLTVVIPRLEALKKEGQAGTAKITQYTRYLTIALAILQGTGLVATARTGALFSGCTVAGQVVPDRSIFVTILMVITMTAGTAVVMWLGELVTDRGIGNGMSILMFISIAAGFPGALWAIKVSGKLAQGWIEFGTVILIGFVMVALVVFVEQAQRRIPVQYAKRMIGRRSYGGTSTYIPLKVNQAGVIPVIFASSLLYIPALIAQFSSGTSGWKTWIEAHFVKGDHPYYITVYFLLIVFFAFFYVAISFNPEEVADNMKKYGGFIPGIRAGRPTAEYLSYVLNRITWPGSLYLGLIALVPTMALAGFGGANANFPFGGTSILIIVGVGLETVKQIESQLQQRNYEGFLR
>NZ_CP034279.1|WP_126886732.1|2961164_2961620_-|50S-ribosomal-protein-L15
MAEQNPLKVHNLRPAPGAKTAKTRVGRGEASKGKTAGRGTKGTKARYQVPERFEGGQMPLHMRLPKLKGFKNPFRTEYQVVNLDKLAALYPQGGEVTVADLVDKGAVRKNSLVKVLGQGEISVALQVTVDAVSGSAKEKITAAGGTVTELV
>NZ_CP034279.1|WP_041130781.1|2961621_2961804_-|50S-ribosomal-protein-L30
MARLKVTQTKSYIGSKQNHRDTLRSLGLKRLGDVVVKEDRPEFRGMVHTVRHLVTVEEVD
>NZ_CP034279.1|WP_128554712.1|2961803_2962409_-|30S-ribosomal-protein-S5
MAGPQRRGSGAGGGERRDRKGRDGGAAAAEKTAYVERVVAINRVAKVVKGGRRFSFTALVVVGDGDGTVGVGYGKAKEVPAAIAKGVEEAKKHFFKVPRIQGTIPHPIQGEKAAGVVLLKPASPGTGVIAGGPVRAVLECAGVHDILSKSLGSDNAINIVHATVAALQGLQRPEEIAARRGLPLEDVAPAALLRARAGAGA
>NZ_CP034279.1|WP_031076680.1|2962452_2962836_-|50S-ribosomal-protein-L18
MAYGVKIAKGKAYKGAALKRRHIRIRKKIAGTTERPRLVVTRSNRGITAQVIDDIAGHTLASASTLDASIRGGEGDKSAKAKQVGQLVAERAKAAGIEAVVFDRGGNQYAGRIAALADAAREAGLKF

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Crispr_ID: NZ_CP034279_7

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP034279_7

3298660-3298757

Unclear

Consensus_repeat	Method
CGAGCCGACCCCGCAGCCGACCG	CRISPRCasFinder

1 spacers

cas3

The CRISPR arrays of NZ_CP034279_7

>merge|NZ_CP034279|7|3298660-3298757|CRISPRCasFinder
CGAGCCGACCCCGCAGCCGACCGGGCGTCGCCGACCCGGCGCGCGGAGCCCCACCGCTCCGGGCCACCGGGAGCACGAGCCGACACCGCAGCCGACCG

>NZ_CP034279|7|7|3298660-3298757|CRISPRCasFinder
CGAGCCGACCCCGCAGCCGACCG	GGCGTCGCCGACCCGGCGCGCGGAGCCCCACCGCTCCGGGCCACCGGGAGCA
CGAGCCGACACCGCAGCCGACCG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP034279.1\|WP_156693110.1\|3305513_3307991_+\|DEAD/DEAH-box-helicase	cas3	mkCas0139_cas3_CAS-I	gnl\|CDD\|274800
NZ_CP034279.1\|WP_003967428.1\|3305080_3305434_-\|STAS-domain-containing-protein	unknown	unknown	gnl\|CDD\|132914
NZ_CP034279.1\|WP_156693101.1\|3286618_3288025_+\|tyrosine-type-recombinase/integrase	unknown	unknown	gnl\|CDD\|271189
NZ_CP034279.1\|WP_156693104.1\|3291250_3294475_-\|dTMP-kinase	unknown	unknown	gnl\|CDD\|234814
NZ_CP034279.1\|WP_156693102.1\|3288218_3289775_-\|alpha/beta-fold-hydrolase	unknown	unknown	gnl\|CDD\|312032
NZ_CP034279.1\|WP_156693108.1\|3301411_3303802_-\|sodium-translocating-pyrophosphatase	unknown	unknown	gnl\|CDD\|234827
NZ_CP034279.1\|WP_156693100.1\|3286350_3286554_+\|excisionase-family-DNA-binding-protein	unknown	unknown	gnl\|CDD\|378935
NZ_CP034279.1\|WP_156693098.1\|3283560_3284421_+\|DNA-primase	unknown	unknown	gnl\|CDD\|214927
NZ_CP034279.1\|WP_156693105.1\|3294935_3297824_-\|type-I-DNA-topoisomerase	unknown	unknown	gnl\|CDD\|236048
NZ_CP034279.1\|WP_156696392.1\|3307932_3308265_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|274799
NZ_CP034279.1\|WP_156693099.1\|3284424_3285897_+\|ATP-binding-protein	unknown	unknown	gnl\|CDD\|226967
NZ_CP034279.1\|WP_156693097.1\|3282399_3283425_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP034279.1\|WP_156693103.1\|3289877_3291083_-\|DNA-polymerase-III-subunit-delta'	unknown	unknown	gnl\|CDD\|236134
NZ_CP034279.1\|WP_156696393.1\|3308970_3309192_-\|DUF4244-domain-containing-protein	unknown	unknown	gnl\|CDD\|379429
NZ_CP034279.1\|WP_156693106.1\|3298868_3300383_-\|methyltransferase	unknown	unknown	gnl\|CDD\|225443
NZ_CP034279.1\|WP_156696391.1\|3298149_3298347_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP034279.1\|WP_156693111.1\|3308618_3308984_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|377921
NZ_CP034279.1\|WP_156696394.1\|3309230_3309923_-\|type-II-secretion-protein-F	unknown	unknown	gnl\|CDD\|366122
NZ_CP034279.1\|WP_156693109.1\|3304037_3304496_-\|ATP-binding-protein	unknown	unknown	gnl\|CDD\|379279
NZ_CP034279.1\|WP_156693107.1\|3300488_3301154_-\|small-secreted-protein	unknown	unknown	gnl\|CDD\|341072

Protein	Function_ID	Function_description	E-value
NZ_CP034279.1\|WP_156693110.1\|3305513_3307991_+\|DEAD/DEAH-box-helicase	gnl\|CDD\|274800	TIGR03817, DECH_helic, helicase/secretion neighborhood putative DEAH-box helicase. A conserved gene neighborhood widely spread in the Actinobacteria contains this uncharacterized DEAH-box family helicase encoded convergently towards an operon of genes for protein homologous to type II secretion and pilus formation proteins. The context suggests that this helicase may play a role in conjugal transfer of DNA.	0
NZ_CP034279.1\|WP_003967428.1\|3305080_3305434_-\|STAS-domain-containing-protein	gnl\|CDD\|132914	cd07043, STAS_anti-anti-sigma_factors, Sulphate Transporter and Anti-Sigma factor antagonist) domain of anti-anti-sigma factors, key regulators of anti-sigma factors by phosphorylation. Anti-anti-sigma factors play an important role in the regulation of several sigma factors and their corresponding anti-sigma factors. Upon dephosphorylation they bind the anti-sigma factor and induce the release of the sigma factor from the anti-sigma factor. In a feedback mechanism the anti-anti-sigma factor can be inactivated via phosphorylation by the anti-sigma factor. Well studied examples from Bacillus subtilis are SpoIIAA (regulating sigmaF and sigmaC which play an important role in sporulation) and RsbV (regulating sigmaB involved in the general stress response). The STAS domain is also found in the C- terminal region of sulphate transporters and stressosomes.	4.53055e-33
NZ_CP034279.1\|WP_156693101.1\|3286618_3288025_+\|tyrosine-type-recombinase/integrase	gnl\|CDD\|271189	cd01189, INT_ICEBs1_C_like, C-terminal catalytic domain of integrases from bacterial phages and conjugate transposons. This family of tyrosine based site-specific integrases is has origins in bacterial phages and conjugate transposons. One member is the integrase from Bacillus subtilis conjugative transposon ICEBs1. ICEBs1 can be excised and transfered to various recipients in response to DNA damage or high concentrations of potential mating partners. The family belongs to the superfamily of DNA breaking-rejoining enzymes, which share the same fold in their catalytic domain and the overall reaction mechanism. The catalytic domain contains six conserved active site residues. Their overall reaction mechanism involves cleavage of a single strand of a DNA duplex by nucleophilic attack of a conserved tyrosine to give a 3' phosphotyrosyl protein-DNA adduct. In the second rejoining step, a terminal 5' hydroxyl attacks the covalent adduct to release the enzyme and generate duplex DNA.	2.01821e-17
NZ_CP034279.1\|WP_156693104.1\|3291250_3294475_-\|dTMP-kinase	gnl\|CDD\|234814	PRK00698, tmk, thymidylate kinase; Validated.	4.8301e-81
NZ_CP034279.1\|WP_156693102.1\|3288218_3289775_-\|alpha/beta-fold-hydrolase	gnl\|CDD\|312032	pfam08386, Abhydrolase_4, TAP-like protein. This is a family of putative bacterial peptidases and hydrolases that bear similarity to a tripeptidyl aminopeptidase isolated from Streptomyces lividans. A member of this family is thought to be involved in the C-terminal processing of propionicin F, a bacteriocidin characterized from Propionibacterium freudenreichii.	2.15623e-33
NZ_CP034279.1\|WP_156693108.1\|3301411_3303802_-\|sodium-translocating-pyrophosphatase	gnl\|CDD\|234827	PRK00733, hppA, membrane-bound proton-translocating pyrophosphatase; Validated.	0
NZ_CP034279.1\|WP_156693100.1\|3286350_3286554_+\|excisionase-family-DNA-binding-protein	gnl\|CDD\|378935	pfam12728, HTH_17, Helix-turn-helix domain. This domain is a DNA-binding helix-turn-helix domain.	5.62323e-13
NZ_CP034279.1\|WP_156693098.1\|3283560_3284421_+\|DNA-primase	gnl\|CDD\|214927	smart00943, Prim-Pol, Bifunctional DNA primase/polymerase, N-terminal. Members of this family adopt a structure consisting of a core of antiparallel beta sheets. They are found in various bacterial hypothetical proteins, and have been shown to harbour both primase and polymerase activities.	4.31747e-15
NZ_CP034279.1\|WP_156693105.1\|3294935_3297824_-\|type-I-DNA-topoisomerase	gnl\|CDD\|236048	PRK07561, PRK07561, DNA topoisomerase I subunit omega; Validated.	0
NZ_CP034279.1\|WP_156693111.1\|3308618_3308984_-\|hypothetical-protein	gnl\|CDD\|377921	pfam07811, TadE, TadE-like protein. The members of this family are similar to a region of the protein product of the bacterial tadE locus. In various bacterial species, the tad locus is closely linked to flp-like genes, which encode proteins required for the production of pili involved in adherence to surfaces. It is thought that the tad loci encode proteins that act to assemble or export an Flp pilus in various bacteria. All tad loci but TadA have putative transmembrane regions, and in fact the region in question is this family has a high proportion of hydrophobic amino acid residues.	0.00128091
NZ_CP034279.1\|WP_156693099.1\|3284424_3285897_+\|ATP-binding-protein	gnl\|CDD\|226967	COG4608, AppF, ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism].	0.000969084
NZ_CP034279.1\|WP_156696392.1\|3307932_3308265_-\|hypothetical-protein	gnl\|CDD\|274799	TIGR03816, tadE_like_DECH, helicase/secretion neighborhood TadE-like protein. Members of this small, highly hydrophobic protein family occur in a pilus/secretion-like region that usually is next to an uncharacterized DEAH-box helicase, in Actinobacteria. Members show sequence similarity to the TadE-like family described by pfam07811. The function is unknown. [Unknown function, General].	3.19153e-07
NZ_CP034279.1\|WP_156693103.1\|3289877_3291083_-\|DNA-polymerase-III-subunit-delta'	gnl\|CDD\|236134	PRK07940, PRK07940, DNA polymerase III subunit delta'; Validated.	0
NZ_CP034279.1\|WP_156696393.1\|3308970_3309192_-\|DUF4244-domain-containing-protein	gnl\|CDD\|379429	pfam14029, DUF4244, Protein of unknown function (DUF4244). This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 66 and 95 amino acids in length. There is a conserved EYA sequence motif.	1.0688e-16
NZ_CP034279.1\|WP_156693106.1\|3298868_3300383_-\|methyltransferase	gnl\|CDD\|225443	COG2890, HemK, Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis].	5.60138e-19
NZ_CP034279.1\|WP_156696394.1\|3309230_3309923_-\|type-II-secretion-protein-F	gnl\|CDD\|366122	pfam00482, T2SSF, Type II secretion system (T2SS), protein F. The original family covered both the regions found by the current model. The splitting of the family has allowed the related FlaJ_arch (archaeal FlaJ family) to be merged with it. Proteins with this domain in form a platform for the machiney of the Type II secretion system, as well as the Type 4 pili and the archaeal flagella. This domain seems to show some similarity to PF00664 but this may just be due to similarities in the TM helices (personal obs: C Yeats).	4.09152e-13
NZ_CP034279.1\|WP_156693109.1\|3304037_3304496_-\|ATP-binding-protein	gnl\|CDD\|379279	pfam13581, HATPase_c_2, Histidine kinase-like ATPase domain.	6.21532e-28
NZ_CP034279.1\|WP_156693107.1\|3300488_3301154_-\|small-secreted-protein	gnl\|CDD\|341072	cd09609, M3B_PepF, Peptidase family M3B, oligopeptidase F (PepF). Peptidase family M3B oligopeptidase F (PepF; Pz-peptidase B; EC 3.4.24.-) is mostly bacterial and is similar to oligoendopeptidase F from Lactococcus lactis. This enzyme hydrolyzes peptides containing between 7 and 17 amino acids with fairly broad specificity. The PepF gene is duplicated in L. lactis on the plasmid that bears it, while a shortened second copy is found in Bacillus subtilis. Most bacterial PepFs are cytoplasmic endopeptidases; however, the Bacillus amyloliquefaciens PepF oligopeptidase is a secreted protein and may facilitate the process of sporulation. Specifically, the yjbG gene encoding the homolog of the PepF1 and PepF2 oligoendopeptidases of Lactococcus lactis has been identified in Bacillus subtilis as an inhibitor of sporulation initiation when over-expressed from a multicopy plasmid.	0.00217073

>NZ_CP034279.1|WP_156696391.1|3298149_3298347_-|hypothetical-protein
MESGPAIFAGVAFTLFGAGLLLWTGTRALHRAPVALGVSPVAAITFATSLGAAFVVLGLWCFGRV
>NZ_CP034279.1|WP_156693105.1|3294935_3297824_-|type-I-DNA-topoisomerase
MSPTSETAQGGRRLVIVESPAKAKTIKGYLGPGYVVEASVGHIRDLPNGAAEVPEKYTGEVRRLGVDVEHDFQPIYVVNADKKAQVRKLKEQLAESDELFLATDEDREGEAIAWHLLEVLKPKVPVHRMVFHEITKDAIQAAVANPRELNKRMVDAQETRRILDRLYGYEVSPVLWKKVMPRLSAGRVQSVATRLVVERERERIAFRSASYWDLTGTFATGRTGDASDPSNIVARLATVDGRRVAQGRDFGPDGQLKASSGQVLHLDEANARALAAALADTSFAVRSVESKPYRRSPYAPFRTTTLQQEASRKLGFGAKATMQIAQKLYENGFITYMRTDSTILSDTAVTAARAQVTQLYGADYLPDSPRVYAGKVKNAQEAHEAIRPSGDRFRTPAETGLTGDQFKLYELIWKRTVASQMKDAVGNSVTVKIGGRASDGRDAEFSASGKTITFHGFMKAYVEGADDPNAELDDRERRLPQVAQGDALSAEEITADGHATKPPARYTEASLVKELEEREIGRPSTYASIIGTILDRGYVFKKGTALVPSFLSFAVVNLLEKHFGRLVDYDFTAKMEDDLDRIARGEAQAVPWLKRFYFGEGDGATGGAAEAGNGDGDHLGGLKELVTDLGAIDAREISSFPVGNGIVLRVGRYGPYIERGEKDAEGHQRADVPEDLAPDELSVELAEELLAKPSGDFELGTDPATGHQIVAKDGRYGPYVTEVLPEGTPKTGKNAVKPRTASLFKSMTLDTVTLEDALRLMSLPRVVGTDAEGVEITAQNGRYGPYLKKGTDSRSLENEEQLFNITLEEALAIYAQPKQRGRAAAKPPLKELGTDPVSERPVVVKDGRFGPYVTDGETNATLRTGDSVEEITPERGYELLAEKRAKGPAKKTAKKTAAKKAPAKKTTAKKTAAKKTAAKKTTTAKSAAATKTAAKKTTTAKSAAAKKTTAKKTTASRTTSDD
>NZ_CP034279.1|WP_156693104.1|3291250_3294475_-|dTMP-kinase
MTRAEQPTVLSPTSDSDAALAADSRERAVRALLRTPPLRRLWSAQLVGGIGDALALLVLVLLALQAAVVEGAFGGGYRGAAFAVAAVFGVRILSTLLFGAVLLGPLTTLTGPKGPLDRRWTMVGADGVRVALLVIAPLWIDWTPDKALGFLLGTVFLAGVAERFWTVAKEAAAPALLPAQPPEGAAVRPLPDQMDALRRLSLRTGFAAVPGAAAALLIATLVGNVLATGVDWFSGHQAALGSYVAAGLFAASVSVLYFLELPDAQTPRPRSPLEGLRRPSTGNGVDKGRTGAIPLLVLACTAVAGAIASATAVAVLHARDLGGGPVTFALLVLALIGGTALGIRGARSVLPALSRRRLLALAITVTGVALLALGLVPDTATVLFIALGAGFSAGVAANTGHVLLDQETEEYRRPRLTEHLQAVVRVTIALGALAAPLLAAAIGPHRLANGDFVFAHGGAAFTLMLVGALLLPVAALVLAKTDDRSGVPLRRDLRDALRGGDPEQAPSKSGFFIALEGGDGAGKSTQVEALADWIRAKGHEVVVTREPGATPIGKRLRSILLDVSSAGLSNRAEALLYAADRAEHVDSLVRPALERGAIVISDRYIDSSVAYQGAGRDLSPTEIARISRWATSGLVPHLTVLLDVSPETARERFTEAPDRLESEPAEFHRRVRAGFLALAAADPGRYLVVDAGQEPESVTTVVRHRLDQMLPLSEAEVKAMEAARKAAEEEARRKAEEAAARKAEEERLERERQEQLAKLRAEEEERKRREEEEARQREAERQAEEARRRAEEARRLAEEERRRREAEEKTRREEQERLRQLKEEQERLRAEAEARRLEKQRKAEEALLRAEEARRLAEAAAAASAAASVAASATETVSGTETTVPTPVVDPLVNPDQETQEVPAPRVNMRKDDEETTLLPPVRDADPAGRPPRPAPADDETTLLRPVRDTGTGADTGTGAGASAIDETAVLPPVRQQDPHQGAADETAVLPPVRDAGTAGRVPPGFFRDEEPDRPGGAERTRELPQVDEQGTPRRRSDWAEETPLDDLPTLADELLGPHDEEDGRGRGRGGRRT
>NZ_CP034279.1|WP_156693103.1|3289877_3291083_-|DNA-polymerase-III-subunit-delta'
MPVWDDLVGQERVQEQLRAAARDADALVTADASGTAPPDASKMTHAWLFTGPPGSGRTTAARAFAAALQCVSPDRALGGEPGCGFCDGCHTALVGTHADVSTVAAVGTQILVDDMRDTVRKSFTSPANGRWQVILVEDAERLNEKSANAVLKAVEEPAPRTVWLLCAPSIEDVLPTIRSRCRHLTLRTPPVEAVADVLIRRDGIEPEVAHAAARATQGHIDHARRLATDERARARRATVLKLPLRVEDVGGCLKAAQELIDAASEDAKEVAEGTDVKETEELKAALGGAPGGRMPRGTAGAMKELEDKQKRRRTRTQRDSLDLALGELTSFYRDVLALQLGSATALANVDVRDALERTARDSTPERTLRRIEAVLACREAMDRNVAPLLAVEAMTMALRAG
>NZ_CP034279.1|WP_156693102.1|3288218_3289775_-|alpha/beta-fold-hydrolase
MDSRRLFRTSRLIRTSAVSLSVFGLLLAGCSDSGSTPAASAPASASIASPEQLKAFYDQRLTWRACGVAGFECATMKAPLDYADPDGEQIKLAVSRVKATGPGKRLGSLLVNPGGPGGSAVGYLQGYAGIGYPAPVRARYDMVAVDPRGVARSEPVRCLDGPQMDVYTQVDQTPDDSGEKDRLAASFKDFAAGCQKRSGRILPHVSTVESARDMDILRAVLGDKRLNYVGASYGTFLGATYAELFPSRTGRLVLDGAMDPSLPTAELNRDQTAGFETAFQSFAADCVKRSDCPLGTGSPAAAADRLKAFFAELDAAPVPTGESRQLGEALATTGVIAAMYDESAWPQLREALTRAMGGEGSALLALADSYYERETDGTYSNLMYANAAVNCLDQPPAFTGPAQAAAAVPSFEKASPVFGEGLAWASLNCAYWPTEATGSAHRIEARGAAPIVVVGTTRDPATPYKWAKALAAQLSSGTLLTYDGDGHTAYGRGSDCVDTAINTYLLDGTVPPAGKRCR
>NZ_CP034279.1|WP_156693101.1|3286618_3288025_+|tyrosine-type-recombinase/integrase
MSPRKPNMESSIYFGADGWWHGRVTMGVKSDGGPDRRHRRARTEAEIKRKVKELERQRDQGRAPAAGRKPTVTAWMETYLTDIASLKLKPRSLDDYWSKTRNDIIPGVGKHRIDKLQPEHLERIYRAMLDAGHAPSHVVKVHRILSRALKIAHRRRIVGENVATLVDPPSIDETEANPFTKEEAKAFLEAAAKRPTFMRWVVGVGMGFRQGETLGLRWSYVDLQAELFRPEWQLQRLTWRHGCDDPHACGGRLHRFEPCPPDCTSHKGYKRGCPKPCAKTCTKHASTCPERKEGGLTFTRPKTKKSRNAVPIPPVFVPFLLDHKARQETAREAAGELWQEHDVVFSRPDGRPLDPRADYEEFKELLKEAGIDDRRLYDGSRHTAGTILNELGVDMPTIMEILRHTQISQTRRYVKGRSHLSKDAMRRMGEFFVSPPAPPSAPNPGPTETRSETTDTRAARSLRRRRIR
>NZ_CP034279.1|WP_156693100.1|3286350_3286554_+|excisionase-family-DNA-binding-protein
MSTAIAAPVDRLLYKPEEAAEALAVSRSTVYELMAEGTLKYIKLGRTRRIRRADLEAYVANLAPLPN
>NZ_CP034279.1|WP_156693099.1|3284424_3285897_+|ATP-binding-protein
MSEDEKTPAREVITDYAQAHFRYFRTADGTVYAQRNGHPVARPIRSQGTTGSHRQELMVGLFRDGVGVFNGTALKEALDLIEALALTEDTQPVHIRVAPGFDGATWLDLGRNDGRSVRIHPTGWDVTVPDPREVCWRRTQLTGELPLPAKDTDGKGIDLLLRLTNFANAETECLAIAWLIGCLGPSVPVPAPFLTGPQGAGKSTAGRMLVRIIEGMSGDLRRAPKDEENLTAAVAAGWVTALDNLSHMPPDLSDAMCCIVTGAENVKRALFTDGDVFRARYRRPMLLTGIDVGVIRPDLAERLLPLRLERPRVRRTEAELWAEYEEVLPVILGSLLDLAVKVRAAEADIPTDLRMADFAHLCAQLDEATGFGSLNAYRASLDDLNDDVIEGDLLAQTVLKHAAGMTPGTEVQMTSSEWLHALTGLYSGEECRPLPKGWPTTGKVLSDRLKRLQPTLAARGVLIDWGRTGSARYIEMTRPAPPAHEQAALH
>NZ_CP034279.1|WP_156693098.1|3283560_3284421_+|DNA-primase
MTQRALIRRDHLSVALELAASGVPVLPLRAGKVPFGNCRVCAKGACGGRPNMKNSGPCKCPGPCHGWAAATTDPHILTSGPWRRAWLRAEAVAYHPGGAGLTVVDLDNADAIAWAREALPATQTVPSTRGEHWLYLGAMQSVNGVRQGVDIKSTMAYARWLGFGTGTMTDLPDAVRALAVKKPSTARPAPHVLAMTARAGTGKCPHRTPVYLERGIAMAEQRITEASSAVHATVYRTFLAVLTTHGRCGCLTDTHVGRLFTAAQAKGESWRHCTDAWANARTALGM
>NZ_CP034279.1|WP_156693097.1|3282399_3283425_-|hypothetical-protein
MTTTVDLVPGLITTREAIAAAYGCGTFQGIEPADDAGKVFVYSDPSAGEEYGYTFDGRAEDDEFGPLYLYTGAGANGDQKPSGRNGSILSHVEKQRELHLFVAHGRVPGGGAMQQRYIGQMVVDPIKPYEVRRAPGQNGVMRSVLVFRFRPAEGTTPAWTEGDKVPAATQTAIEVTDPVNDVPAPVVLPKQSGAKAKKTEQHSTAETVADIPAGQRKVLRREGELVKAFAAHLAAAGHETHSFQITIKGEPGALTPDLYDATDHVLYEAKGLTTRANVRMAIGQLADYRRHIPNSKALRVAVLLPSEPTADVKDLLGEVNVELVYQADEGFAGWPLLSSQP
>NZ_CP034279.1|WP_156693106.1|3298868_3300383_-|methyltransferase
MSTTSLTASLPVPDRADRLRDALLAADFTADGLLELLGAPAYAALARSETVPALRATRADGPLATLVRLFLLQRPVPHDRARAVLPLEEALADGWVVADGGEIRATVDVRPYGGPEGQDWFIVSDLGCAVGGAAGASGRGEGVVLGVGGASTTLAGITVRTPVASALDLGTGSGIQALHAAQHATRVTATDLNPRALEFTRLTLALSGAPEADLRTGSLFEPVASETYDLIVSNPPFVISPGARLTYRDGGMGGDDLCRSLVQRAGERLNDGGFAHFLANWQHVEGEDWQDRLRSWVPRGCDAWIVQREVQDVTQYAELWLRDAGDHQGDPDRYTERYEAWLDEFEQRGTKAVGFGWITLRKSGADEPSVVVEEWPHPVEQPLGETVRAHFARQDYLRTRDDAALLADHFVLAPEVMQEQVGMPGAEDPEHVVLRQNRGMRRATRVDTVGAGFAGVCDGTLSAGRILDAIAQLMGEDPVLLRDRTPQAIRLLVEEGFLEPAPGT
>NZ_CP034279.1|WP_156693107.1|3300488_3301154_-|small-secreted-protein
MNKKLAAALSGGAVLVLALSGCSDDDGGGENKVDAWAKNVCDQAQPQIQKRANAQQAIISTAADGKPADIQAADSKAFQDIADADKALAKAVQDAGVPPVDGGEKLQQDAVKELNATAAAYEGLKKQVDALDPKNQQKFADGLQTVAAGLKKIEKMDQDALAKLQAGQLGQAMAKQPGCRRAEASVPPAKPGPAASDASDASAASGASAPASAGKPSAPAA
>NZ_CP034279.1|WP_156693108.1|3301411_3303802_-|sodium-translocating-pyrophosphatase
MAGLFSTQVSDHPTSLAAAVLTDENRIIVIVIAAVALAALIVAQLLVRQVLAAGEGTTAMKKIAAAVQEGANAYLARQLRTLGIFAVVVFFLLLLLPADNWSQRAGRSLFFLVGALFSAITGYIGMRLAVRANVRVAAAAREATPAPGEPQKDLTTVSHKAMKIAFRTGGVVGMFTVGLGLLGASCVVLVYAADAPKVLEGFGLGAALIAMFMRVGGGIFTKAADVGADLVGKVEQGIPEDDPRNAATIADNVGDNVGDCAGMAADLFESYAVTLVAALILGKAAFGDLGLAFPLIVPAIGVVTAMIGIFAVAPRRADRSGMAAINRGFFISAVISLALVAVAVFVYLPSSYAELEGVTESAISAHGGDPRTLALVAVAIGIVLAALIQQLTGYFTETTRRPVRDIGKSSLTGPATVVLAGISIGLESAVYTALLIGLSVYGAFLLGGASITLALFAVALAGTGLLTTVGVIVAMDTFGPVSDNAQGIAEMSGDVEGAGAQVLTDLDAVGNTTKAITKGIAIATAVLAAAALFGSYRDAIATAVREVEARATEMNLTMDISQPNNLVGLILGAAVVFLFSGLAINAVSRSAGAVVYEVRRQFREHPGIMDHSEKPEYGRVVDICTKDALRELATPGLLAVMAPIAVGFTFGVGALGAYLAGAIGTGTLMAVFLANSGGAWDNAKKLVEDGHHGGKGSESHAATVIGDTVGDPFKDTAGPAINPLLKVMNLVALLIAPAIVQFSYGDDASAGVRAVVATLSILVIIAAVYVSKRRTIAVGDEDDNNTGRVTDKAATL
>NZ_CP034279.1|WP_156693109.1|3304037_3304496_-|ATP-binding-protein
MATVELRFSAQPEHVRTARLVAAAVARRAGVDEAVLDEVRLAVGEACSRAVGLHRSNHVASPIRVVLSEEEKTFSIEVGDEVPGAGVAAADAAGVPGSRSAAPVEEFDDAEGEDEMGLAVITGLVDDVEVSAGEAGGVIRMTWPTTPTTVLP
>NZ_CP034279.1|WP_003967428.1|3305080_3305434_-|STAS-domain-containing-protein
MDLSLSTRNVSGPGGDRTVVEVGGEIDVYTAPKLREQLVELVNDGSYHLVVDMEGVDFLDSTGLGVLVGGLKRVRAHEGSLRLVCNQERILKIFRITGLTKVFPIHTTVDEAVAATD
>NZ_CP034279.1|WP_156693110.1|3305513_3307991_+|DEAD/DEAH-box-helicase
MAFIHLPAAMHDALGALSVTPVTHSVPMAMNHRPSRPPESGETRPTPGTVLDRLATGADRAARITHTEHLPPRAGRHAVWPDRIRPEVINAIRTAGIEHPWAHQAAAAEYALDGESVVIATGTASGKSLAYLAPVLTTLLDGSEAPNGRGATALYLAPTKALAADQRRSVKALAQPLGNRIRPAVYDGDTPVEEREWVRQYANYVLTNPDMLHRGVLPSHPRWSSFLRSLRYVVIDECHTYRGVFGSHVAQVLRRLRRVCARYGSSPVFLLASATAARPAHAAERLTGLPVREVADDASPRGEMVFALWEPPLTELQGEQGAPVRRTATAETADLLTDLTVQGVRSVAFVRSRRGAELISVIAKERLAEVDRSLPARVAAYRGGYLPEERRALERALHSGELLGLAATTALELGIDVSGLDAVVIAGYPGTRASLWQQAGRAGRSGQGALAVLVARDDPLDTFLVHHPEALFRQPVESTVLDPDNPYVLAPHLCAAAAEVPLTDSDLALFGPAVPDLLPQLESAGLLRRRASGWYWTRRERAADLTDIRGEGGSPVQIVEAGTGRLLGTVDESAAHAAVHDGAVHLHMGRTYLVRQLDLKDSVALVEEANPPYSTTARDTTAISVLETDTEIPWGDGRLCYGSVEVTNQVVSYLRRRLITGEVLGETKLDLPPRTLRTRAVWWTVTEDQLDAARVNPEQLGGALHAAEHASIGLLPLFATCDRWDIGGVSVPLHPDTMLPTVFVYDGHPGGAGFAERAFHTAREWLTATRDAIASCECDAGCPSCIQSPKCGNGNDPLHKRGAVRLLTELLRGAPEAPQEAPHVP
>NZ_CP034279.1|WP_156696392.1|3307932_3308265_-|hypothetical-protein
MWAAMAATVLCTVFAVVLALGQAVAARHRAGGAADLAALAAADRALWGTSAACGAAERVARAQATEVVRCTVRGEIAEVTARARFGPYAPVVRARAGPPGALPGLPAAVP
>NZ_CP034279.1|WP_156693111.1|3308618_3308984_-|hypothetical-protein
MPSSEGGGDRGSVTAEAATVLPVLALFTMALVWALMATAAHIQCVDAARAGARAVARSEPRAQAVAAARSAAPDGARVAVDRTGDLWRVRVEAPSPGPGPLRLTLRAEAAALAEDTVGVTP
>NZ_CP034279.1|WP_156696393.1|3308970_3309192_-|DUF4244-domain-containing-protein
MVQAVKARVAWVARAARVRGVGGGRDAGMTTAEYAMGTLAACAFAAVLYKIVTSDVVSGGLQSLIGRALDAQF
>NZ_CP034279.1|WP_156696394.1|3309230_3309923_-|type-II-secretion-protein-F
MLVARRLRARARRRTAALLGTETGRRRTGWPGRCGSWVRRWAAPMGAAAGGWVLVGGVAGLVVGVVSAYGTWKWQRRPRPVTDEDGEAARGLPLAADLLAACLSAGAGPREAAEAVGESLGGPVGDRLAWAAAELRLGGEPDDVWGRFGEIPGARPLARCLERASASGAPAAEAVSRLAAGLRADRARRATARAQRAQVLITAPVGLCFLPAFLAVGVAPVVIGLAGELL

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Crispr_ID: NZ_CP034279_8

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP034279_8

4801719-4801842

Orphan

Consensus_repeat	Method
CCCGTTGTGGGCAATCGTCCGGC	CRISPRCasFinder

2 spacers

The CRISPR arrays of NZ_CP034279_8

>merge|NZ_CP034279|8|4801719-4801842|CRISPRCasFinder
CCCGTCGTGGGCAATCCTCCCGGGACTCCCATCCCCGTTGTGGGCAATCGTCCGGCCGGTCTCGTTGTGGGCAATCGTCCCGGGGGCTCCCTCCCCACCCACCCGTTGTGGGCAATCGTCCCGC

>NZ_CP034279|8|8|4801719-4801842|CRISPRCasFinder
CCCGTCGTGGGCAATCCTCCCGG	GACTCCCATCCCCGTTGTGGGCAATCGTCCGGCCGGT
CTCGTTGTGGGCAATCGTCCCGG	GGGCTCCCTCCCCACCCA
CCCGTTGTGGGCAATCGTCCCGC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP034279.1\|WP_156694266.1\|4793390_4797122_+\|ATP-binding-cassette-domain-containing-protein	unknown	unknown	gnl\|CDD\|224055
NZ_CP034279.1\|WP_156694262.1\|4786278_4787751_-\|PucR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|377939
NZ_CP034279.1\|WP_156694267.1\|4797229_4797577_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP034279.1\|WP_156694280.1\|4812444_4813056_-\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|224584
NZ_CP034279.1\|WP_156694277.1\|4807881_4810107_+\|ATP-dependent-RecD-like-DNA-helicase	unknown	unknown	gnl\|CDD\|273632
NZ_CP034279.1\|WP_156694270.1\|4799741_4801595_-\|glycoside-hydrolase-family-3-protein	unknown	unknown	gnl\|CDD\|366376
NZ_CP034279.1\|WP_156694274.1\|4805223_4806366_+\|DUF993-family-protein	unknown	unknown	gnl\|CDD\|368783
NZ_CP034279.1\|WP_156694279.1\|4812047_4812359_-\|copper-binding-protein	unknown	unknown	gnl\|CDD\|225328
NZ_CP034279.1\|WP_156694265.1\|4792303_4793269_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|379138
NZ_CP034279.1\|WP_156694261.1\|4785580_4786186_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP034279.1\|WP_156694276.1\|4807357_4807792_-\|VOC-family-protein	unknown	unknown	gnl\|CDD\|380093
NZ_CP034279.1\|WP_156694272.1\|4802924_4803974_-\|substrate-binding-domain-containing-protein	unknown	unknown	gnl\|CDD\|224525
NZ_CP034279.1\|WP_156694271.1\|4802079_4802856_-\|TIM-barrel-protein	unknown	unknown	gnl\|CDD\|366542
NZ_CP034279.1\|WP_156694275.1\|4806362_4807175_+\|TIM-barrel-protein	unknown	unknown	gnl\|CDD\|224007
NZ_CP034279.1\|WP_156694263.1\|4789460_4790447_+\|agmatinase	unknown	unknown	gnl\|CDD\|212538
NZ_CP034279.1\|WP_156694264.1\|4790551_4792234_+\|thiamine-pyrophosphate-binding-protein	unknown	unknown	gnl\|CDD\|223107
NZ_CP034279.1\|WP_156694269.1\|4798233_4799670_+\|aminopeptidase	unknown	unknown	gnl\|CDD\|283275
NZ_CP034279.1\|WP_156694273.1\|4804075_4805227_+\|Gfo/Idh/MocA-family-oxidoreductase	unknown	unknown	gnl\|CDD\|223745
NZ_CP034279.1\|WP_156694268.1\|4797678_4798068_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP034279.1\|WP_156694278.1\|4810284_4811574_+\|citrate-synthase	unknown	unknown	gnl\|CDD\|180164

Protein	Function_ID	Function_description	E-value
NZ_CP034279.1\|WP_156694266.1\|4793390_4797122_+\|ATP-binding-cassette-domain-containing-protein	gnl\|CDD\|224055	COG1132, MdlB, ABC-type multidrug transport system, ATPase and permease components [Defense mechanisms].	2.31935e-167
NZ_CP034279.1\|WP_156694262.1\|4786278_4787751_-\|PucR-family-transcriptional-regulator	gnl\|CDD\|377939	pfam07905, PucR, Purine catabolism regulatory protein-like family. The bacterial proteins found in this family are similar to the purine catabolism regulatory protein expressed by Bacillus subtilis (PucR). PucR is thought to be a transcriptional activator involved in the induction of the purine degradation pathway, and may contain a LysR-like DNA-binding domain. It is similar to LysR-type regulators in that it represses its own expression. The other members of this family are also annotated as being putative regulatory proteins.	2.2885e-24
NZ_CP034279.1\|WP_156694277.1\|4807881_4810107_+\|ATP-dependent-RecD-like-DNA-helicase	gnl\|CDD\|273632	TIGR01448, recD_rel, helicase, putative, RecD/TraA family. This model describes a family similar to RecD, the exodeoxyribonuclease V alpha chain of TIGR01447. Members of this family, however, are not found in a context of RecB and RecC and are longer by about 200 amino acids at the amino end. Chlamydia muridarum has both a member of this family and a RecD. [Unknown function, Enzymes of unknown specificity].	0
NZ_CP034279.1\|WP_156694270.1\|4799741_4801595_-\|glycoside-hydrolase-family-3-protein	gnl\|CDD\|366376	pfam00933, Glyco_hydro_3, Glycosyl hydrolase family 3 N terminal domain.	3.70755e-118
NZ_CP034279.1\|WP_156694274.1\|4805223_4806366_+\|DUF993-family-protein	gnl\|CDD\|368783	pfam06187, DUF993, Protein of unknown function (DUF993). This family consists of several hypothetical bacterial proteins of unknown function.	0
NZ_CP034279.1\|WP_156694279.1\|4812047_4812359_-\|copper-binding-protein	gnl\|CDD\|225328	COG2608, CopZ, Copper chaperone [Inorganic ion transport and metabolism].	1.04143e-12
NZ_CP034279.1\|WP_156694280.1\|4812444_4813056_-\|GNAT-family-N-acetyltransferase	gnl\|CDD\|224584	COG1670, RimL, Acetyltransferases, including N-acetylases of ribosomal proteins [Translation, ribosomal structure and biogenesis].	6.53649e-38
NZ_CP034279.1\|WP_156694276.1\|4807357_4807792_-\|VOC-family-protein	gnl\|CDD\|380093	pfam18029, Glyoxalase_6, Glyoxalase-like domain. This entry comprises a diverse set of domains related to the Glyoxalase domain. The exact specificity of these proteins is uncertain.	1.66052e-27
NZ_CP034279.1\|WP_156694272.1\|4802924_4803974_-\|substrate-binding-domain-containing-protein	gnl\|CDD\|224525	COG1609, PurR, Transcriptional regulators [Transcription].	9.10338e-95
NZ_CP034279.1\|WP_156694271.1\|4802079_4802856_-\|TIM-barrel-protein	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.	3.4832e-27
NZ_CP034279.1\|WP_156694275.1\|4806362_4807175_+\|TIM-barrel-protein	gnl\|CDD\|224007	COG1082, IolE, Sugar phosphate isomerases/epimerases [Carbohydrate transport and metabolism].	8.78197e-31
NZ_CP034279.1\|WP_156694263.1\|4789460_4790447_+\|agmatinase	gnl\|CDD\|212538	cd11592, Agmatinase_PAH, Agmatinase-like family includes proclavaminic acid amidinohydrolase. This agmatinase subfamily contains bacterial and fungal/metazoan enzymes, including proclavaminic acid amidinohydrolase (PAH, EC 3.5.3.22) and Pseudomonas aeruginosa guanidinobutyrase (GbuA) and guanidinopropionase (GpuA). PAH hydrolyzes amidinoproclavaminate to yield proclavaminate and urea in clavulanic acid biosynthesis. Clavulanic acid is an effective inhibitor of beta-lactamases and is used in combination with amoxicillin to prevent the beta-lactam rings of the antibiotic from hydrolysis and, thus keeping the antibiotic biologically active. GbuA hydrolyzes 4-guanidinobutyrate (4-GB) into 4-aminobutyrate and urea while GpuA hydrolyzes 3-guanidinopropionate (3-GP) into beta-alanine and urea. Mutation studies show that significant variations in two active site loops in these two enzymes may be important for substrate specificity. This subfamily belongs to the ureohydrolase superfamily, which includes arginase, agmatinase, proclavaminate amidinohydrolase, and formiminoglutamase.	1.82723e-167
NZ_CP034279.1\|WP_156694264.1\|4790551_4792234_+\|thiamine-pyrophosphate-binding-protein	gnl\|CDD\|223107	COG0028, IlvB, Thiamine pyrophosphate-requiring enzymes [acetolactate synthase, pyruvate dehydrogenase (cytochrome), glyoxylate carboligase, phosphonopyruvate decarboxylase] [Amino acid transport and metabolism / Coenzyme metabolism].	1.00147e-140
NZ_CP034279.1\|WP_156694269.1\|4798233_4799670_+\|aminopeptidase	gnl\|CDD\|283275	pfam05576, Peptidase_S37, PS-10 peptidase S37. These serine proteases have been found in Streptomyces species.	0
NZ_CP034279.1\|WP_156694273.1\|4804075_4805227_+\|Gfo/Idh/MocA-family-oxidoreductase	gnl\|CDD\|223745	COG0673, MviM, Predicted dehydrogenases and related proteins [General function prediction only].	5.29845e-49
NZ_CP034279.1\|WP_156694265.1\|4792303_4793269_+\|hypothetical-protein	gnl\|CDD\|379138	pfam13354, Beta-lactamase2, Beta-lactamase enzyme family. This family is closely related to Beta-lactamase, pfam00144, the serine beta-lactamase-like superfamily, which contains the distantly related pfam00905 and PF00768 D-alanyl-D-alanine carboxypeptidase.	1.27291e-11
NZ_CP034279.1\|WP_156694278.1\|4810284_4811574_+\|citrate-synthase	gnl\|CDD\|180164	PRK05614, gltA, citrate synthase.	0

>NZ_CP034279.1|WP_156694270.1|4799741_4801595_-|glycoside-hydrolase-family-3-protein
MHHRATSTDSPSSSPSVPSRRTLLAVTAAAAAAAVSGGAVPAAAAADDRRLKQLVSRMSLEEKVGQLFVMRVYGHSATEPDQADVDANLKEIGVRNAAELIAKYHVGGIIYFSWAHNTRDPHQIADLSNGIQRAALGRPARVPVPVLISTDQEHGIVARIGEPATLMPGAMALGAGGSRSDARRAAQVAGAELAALGIRQNYAPVADVNVNPANPVIGVRSFGAEPGAVAAMVAAQVGGYQRAGVAATSKHFPGHGDTSVDSHYGLPTISHTREQWRTLDAPPFRAAIAAGIDSIMTAHIVVPALDPAEDPATLSRPILTGILREQLGYDGVVVTDSLGMEGVRTKYGDDRVPVLALKAGCDQLLNPPKLDVAFHAVLNAVRGGEISETRVDESILRILRLKVRLGLFRDPYVTHGAVDRTVGTRSHLATADRIAERTTTLLLNEGALLPLRAAERPNLLVVGADVASPSGTTGPPTATLGAALAALGFTTTVLPTGTAPTAAKIDEAVAAAAGKDAVVVGTYNVSASSAQRTLVSRLAATGVPVVTVAIRNPYDIAHLSGQRATLATYSWTDVELRAAARVIAGRARPEGRLPVPVQRADDPARVLYPVGYGLGYG
>NZ_CP034279.1|WP_156694269.1|4798233_4799670_+|aminopeptidase
MRKALTWLLSLVVLIGIMSAAGTATAAGTADRGTTPDSGTTTDIKDRILAIPGMSLVEEKPYPGYRYFVLTYTQPVDHRDRSKGTFQQRLTLLHKDTTRPTVFHTSGYAVSTRPSRAEPTRIVDGNQVSMEYRFFTPSRPQPADWSTLDIWQAASDQHRIFTALKRIYDRKWLSTGASKGGMTATYYERFYPRDMDGVVAYVAPNDVVEKEDSAYDRFFATVSTKECRDRLNALQREALVRRAPLQEKLRTWAAAEGATFTTVGTLDKAYEAVVLDFVWAFWQYSTEADCASIPVAATATDQAVYDTIDAHSGWAAYTDQSLEAYTPYYYQAATELGSPSLRLPHLKGLTRYGYQPARNFVPRDIPMRFKPWVMRDVDTWVRHHGRGMLFVYGGNDPWGAEKFRIDKGARDAYVMTAPGANHGANVEGLTEADRTKATARILAWAGVAPADPSRAAPLKTFDPRLDEREPAKEMTLRP
>NZ_CP034279.1|WP_156694268.1|4797678_4798068_+|hypothetical-protein
MARARRLLVQMLAVLVAAGFLVLGGPGAPRADAAVTACSGRLVKTVKFSTGELRVYKKRQYACALTVAKKPGARRAMSVSIQPRGGRAAVDVGAFTRQAGPVTVYALNRCVRASGTVAGRGGSTGWILC
>NZ_CP034279.1|WP_156694267.1|4797229_4797577_+|hypothetical-protein
MITDPAAFPAPSRPAARVRVRATIAAVAFLPACAVVGFLTLFSERASGCVLEGGDQCVGVPGAFWLHSALAAGLLWCVALFTPDRGGRSRAVRLAAYRVQLGCEAFALFAILSHA
>NZ_CP034279.1|WP_156694266.1|4793390_4797122_+|ATP-binding-cassette-domain-containing-protein
MAAAEQGWARRLSGYAWRYRRNVVLALGSSLAGMAVMALVPLITKVVIDDVIGAKTRSLAVWTGLLLAAAVAVYAATYVRRYYGGRLALDVQHDLRTEMYGTITRLDGRRQDELSTGQVVGRATSDLQLIQGLLFMLPMTIGNILLFLISLVVMAWLSLPLTLVALAVAPALWFIAKRSRTRLHPATWYAQAQAAHVAGVVDGAVTGVRVVKGFGQEEQETGKIRAASRKLFAGRLRTIRLNSRYTPALQAVPALGQVAMLALGGWLATRGQITLGTFVAFSTYLAQLVGPVRMLAMVLTVGQQARAGVERVLELIDTEPGIEDGTKELPADAPASVEFDDVSFAYEDGRPVLDGFSLEIRPGETVAVVGSSGSGKSTVSLLLPRFYDVTHGAVLIGGHDVRELTLDSLRAAIGLVPEDSFLFSDTVRANIAYGKPDATDEEIRAAARAAQADGFIAGLPDGYDTKVGEHGLTLSGGQRQRVALARAILTDPRLLVLDDATSAVDARVEHEIHEALRSVMAGRTTLLIAHRRSTLNLADRIAVLDDGRLSDIGTHDELERRSALYRRLLTDPDELGGVSPGHAVPVTAPQEDRTVREELDAEFDAERGITPALWVRDADAADARSGAGDGATPELLAQVEALPPATDTPAVDEARAVTPEESYGLRRLLRGFGAVLLVSLGLVAVDAGMGLLLPILIRHGIDDGVEQAALGAVWVASGLALATVLVQWVAQTGEIRMTGRTGERVLYALRLKIFAQLQRLGLDYYERELTGRIMTRMTTDVDALSTFLQTGLVTAFVSLVTFFGIMVALVVIDVQLALVVFATLPVLVVGTVFFRRSSVKAYELARERISVVNADLQESVAGLRIVQAFRRERSGRQAFAARSAEYRAARVRGQWLISVYFPFVQLLSSVAAAAVLIVGAGRVEAGTLTTGALVAYLLYIDLFFAPVQQLSQVFDGYQQAAVSLGRMQELLREKTSTAAPAKPLPVPSLRGDIAFEGVSFSYKDDESALTGVDLRIPAGQTVAFVGETGAGKSTLVKLVARFYDPTSGRVTADGADLRDLDLTAYRHRLGVVPQEAYLFAGTVRDAIAYGRPGASDAEVEAAARAVGAHDMIATLDGGYLHEVAERGRNLSAGQRQLIALARAELVDPDVLLLDEATAALDLATEAQVNAATDRLAGRRTTLVVAHRLTTAARADRVVVMDRGRVAEDGTHEELLARDGRYAELWRTFIGEEPAGTGTPAPTG
>NZ_CP034279.1|WP_156694265.1|4792303_4793269_+|hypothetical-protein
MCCVNRLSISRRRRGAVSAAVALGVLLPTAATITPATAAAPAVACTSQKAGLAAKLVKDINAALKGRKSTTAILVNDRVSKTSCVLRPDTQFDSASVVKTTVLATLLWDAQKSKRALTATEKSRATAMITKSDNDATTALWKQLGVTKVKGFLAAAQMTKTVPGSGGYWGLTQITARDQQKLLGLITAKNTVLTDASRAYILDLMNKVVAAQRWGAPAGAPATARIHVKNGWLPRATHAWRVHSIGAFTGTTHNYQLTVLTHDNATMQDGINTIQAVARVVHADLNPGAARSDAFVPPAVPQEAVPAVPGRAAQDLVSAPR
>NZ_CP034279.1|WP_156694264.1|4790551_4792234_+|thiamine-pyrophosphate-binding-protein
MTHDHDLVLRPTTAQTEAALNPPPGRTGGDLVVETLAGLGATTVFGLPGQHALGMFDALRRSKLQYVGLRVENNAGFAADAYGRITGEAAPLLLSTGPGALMSLAALQEAAAASAPVLAIGSQVPAAGLGGGRHGYLHELRDQRASFRDVVKSVHTVRTASQIPSAVAAAWESALTAPHGPVWVEIPQDVLLAETSLPVVTAMDATPEDLPPRPELTALAAHLLANAERPAIIAGGGVVRADASGKLLALAERIGAPVVTTFGGKGAFPWEHPLSLQSWLEDRHTTEFLEDADVLLVVGSGLGELSSNYHTFAPRGRIVQIEADLGKLESNHPALGIHADARLALSALLETVPARHDDTAAERVRTVLDKVRARIEGQDLTLERQVLAAVREALPDDAPSFWDMTILAYWAWSAFDARRPNTMHSAQGAGGLGYGFPAALGAAAADPTRPVLAVSGDGGAMYSIAELATARQYGLNVTWLIVDDGGYGILREYMTDAFGEATGTELARPDFVALAGSFGVPAVTTTRESLAADLANSLAAPGPSVVVLPAVLKMFAPTHL
>NZ_CP034279.1|WP_156694263.1|4789460_4790447_+|agmatinase
MSSSNENVTPRGPVDSSRVPRYAGPATFARLPRLDEVGTADVAVVGVPFDSGVSYRPGARFGGNAIREASRLLRPYNPAQDASPFALAQVADGGDIAVNPFNINEAVETVEAAADDLLGTGARLMTLGGDHTIALPLLRSVAKKHGPVALLHFDAHLDTWDTYFGAEYTHGTPFRRAVEEGILDTEALSHVGTRGPLYGKQDLTDDEKMGFGIVTSADVYRRGADEVADQLRQRIGDRPLYISIDIDCLDPAHAPGTGTPEAGGMTSRELLEILRGLASCNLVSADVVEVAPAYDHAEITSVAASHTAYELTTIMSRQIAAQRASGAK
>NZ_CP034279.1|WP_156694262.1|4786278_4787751_-|PucR-family-transcriptional-regulator
MEEPSMSESAGALPAPPAPPVRLSALLAREDLGLRLLAGPEEADIHWVHTSEMADPFPYLLGGELLMTAGVQLPDPERYVARVVAAGAAALGFGVAPVYDTVPGALAEACARHGLPLLEVPPRTPFTAVGRAVWRLMAEARHRELRRVTEAQQALATAAARPDPVPAVLHALASRLAGRAALYAPDGSEYAAAGPAPEPEVAAALARLARVPHAGSREAGPAEGSGGGAGGPRPASAADTVAGVPLAAYALGGGQGLTLGLAPGRREPGDRTVAGVAVVLLSLLTAPHQGADEATRSAALVRLLLGAGPAEVAPLLGGGPWTVVHARGEGVPPPLGTPLVDVDVREGTVRALLPAGRDAAPHPGWALGVSAPAGPAELAAADLQAARALRRARAAHLPLARHRSGGMGALLDPDEASAYARTLLAPLSEPLRETLRAWLSLHGSWDRTATALGVHRNTVRQRIARCGEALAMDLDDAEARMELWFALRWS
>NZ_CP034279.1|WP_156694261.1|4785580_4786186_+|hypothetical-protein
MNTLRTALATAAAAVLGLAALATAPAQAAAQPAFLAASQMPPSSTPWTATQVFTGVPENGGVLCASYKIPAQNSRYREFSTDLDANGVQVTTVARTEADAVKLVDTLRTSLANCGPLLEQQNPGLKAVSASHGKLAVEEGAWVYSLDTADPQIGATDIHLFSVGRDGRTVTLVRWGQTGDLKDAPLTAFRTTTKTAVNKLH
>NZ_CP034279.1|WP_156694271.1|4802079_4802856_-|TIM-barrel-protein
MKYAFSTLGVPGMPVPDVARLAAGCGYQGVELRAHPEEPVHPGLVSHERRAVVEEFAREGVEILTVAGYARVAEAGDDEPVYEELHRLLYLAADLGASYVRVFPGGGDQDPAEADATAARRLGAAAEIAADLGVRILVETHDSHRTGADVARIVGAVGHKHVGALWDVMHPWSAGERPTATHAVLAPYLGYVQVKDVASTDDPTPLALGAGVLPLAECLALVGDEGWVSWEYEKRWHPGAAELPPLLAAGREHLSTLT
>NZ_CP034279.1|WP_156694272.1|4802924_4803974_-|substrate-binding-domain-containing-protein
MTVTLADVAARARVSPATVSRVLNGNYPVAAATRERVLRAVDELDYVLNGPASALAAATSDLVGILVHDIADPFFGIIAGAAQHAMVEGAPGRAGGEKLAVVCNTGGSPERELTYLTLLQRQRAAAVVLTGGAVDDPEHTAATAAKLARLTNGGTRVVLCGRPPVPGAAVTATLTFDNRGGARRLTEHLLSLGHERIGYVAGPAERTTTRHRLEGHLSAMRDAGLAAGLDRLTAHGSYDRRSGYDATLELLRREPGLTAIAAANDTVALGVCAALRDQGRRVPDDVSVAGFDDLPFSVDAAPALTTVRLPLHEAGARAGRLATGTEAPPPGGVATVGAELVVRSSTARP
>NZ_CP034279.1|WP_156694273.1|4804075_4805227_+|Gfo/Idh/MocA-family-oxidoreductase
MTRRTVRIAMNGVTGRMGHRQHLVRSILAIREQGGLDLGDGRVVWPEPVLVGRREHALRELARRHGLTEWSTDLDAVLADGTVDVYFDAQATSARADAIRKAIAAGKHVYTEKPTATDTAAALDLARLARAAGVRHGVVQDKLFLPGLRKLKRLVDGGFFGEILSVRGEFGYWVFEGDWQEAQRPSWNYRAEDGGGIVVDMFPHWEYVLHELFGRVCGVTAHVTTHVPRRWDEDGKPYAATADDAAYGIFQLESGAVAQINSSWAVRVHRDELVEFQVDGTHGSAVAGLRGCRVQHRSATPKPVWNPDAPVTEAFRDQWQEVPDNAGFDNGFKAQWELFLRHVVLDEPFPWDLLAGARGVQLAELGLKSSAEGRRYDVPELTL
>NZ_CP034279.1|WP_156694274.1|4805223_4806366_+|DUF993-family-protein
MTIRLPHGPYEPRTTPRSFGPTGSPPVSRTVFAAAHVVADPYADVPPGSPAAVDWDATLAFRRHLWAHGLGVAEAMDTAQRGMGLDWAAAAELIRRSAAEARAAGGRIAAGVGTDQLTGPAGRAAVRAAYEEQLALVEDAGAQPVLMASRALAAAATSADDYLDVYTGLLRQASGPVILHWLGPVFDPALDGYWGSADLDTATDTFLKVVAEHPDKVDGIKVSLLDAGREVDLRRRLPEGVRCYTGDDFHYPELIEGDAHGSSHALLGVFDPLGPLAAQAVRVLDAGDKEGFRALLDPTVALSRHLFEAPTRFYKTGVVLLAWLAGHQDHFTVLGGLQSARSLPHLARAYELADRLGLFPDPALAEHRMKALLSVYGGGR
>NZ_CP034279.1|WP_156694275.1|4806362_4807175_+|TIM-barrel-protein
MSDLARFSINQMTVRQLPLPRLVEECVRLGVPGVGLWREPVAEYGLEATAQLVRDAGLAVTTLCRGGFFTTATDLDDNRAAVDEAATLGTDTLVLVSGGLPPGVKDLAAARSRIAGALAELVPYAAGRGVRLAIEPLHPMYAADRCAVSTLDQALALARPFAPSEVGVVVDTYHVWWDDHAPAAVARAGAEGRVHAFQVADWTTPLPAGVLTGRGPLGDGVIDLRAWRERVDASGYTGPIEVELFNDTLWSRDGVDVLEETARRYVEHVL
>NZ_CP034279.1|WP_156694276.1|4807357_4807792_-|VOC-family-protein
MSSIRQFQVTFDCADPERVARFWCEVLGYVLPPPPKGFGTWEDFRSSLPPEERGAWSACVDPSGAGPRLFFQRVPEGKAGKNRVHLDVRVGTGLVGEERLTTLEAEGARLVALGAVRVRLLPADEDNESCLVMQDVEGNEFCLD
>NZ_CP034279.1|WP_156694277.1|4807881_4810107_+|ATP-dependent-RecD-like-DNA-helicase
MSSLSVVEGVLERITYANEENGYTVARVDTGRGGGDLLTVVGSLLGAQPGESLRMEGRWGSHPSYGKQFTVENYTTVLPATVQGIRRYLGSGLIKGIGPRIADRIVEHFGVGTLEVIEQEPARLVEVPGLGPKRTRMIGAAWEEQKAIKEVMVFLQGVGVSTSIAVRIYKKYQDASISVVRNQPYRLAADVWGIGFLTADRIAQAVGIPHDSPDRVKAGLQYALSQSTDQGHCFLPEERLISDAVKLLQVDTGLVIDCLAALAADEEGVVREQVPGPEGQPLTAVYLVPFHRAEVSLAAQLQRLLRTGEDRMPAFRDVAWDKALAWLADRTGADLAPEQEEAVRLALTEKVAVLTGGPGCGKSFTVRSIVELARAKKAKVVLAAPTGRAAKRLAELTGAEASTVHRLLELKPGGDAAYDRDRPLDADLVVVDEASMLDLLLANKLVKAVAPGAHLLLVGDVDQLPSVGAGEVLSDLLAPDGPVPSVRLTRIFRQARQSGVVTNAHRINSGQQPLTSGLPDFFLFVAEETEEAGRLTVDVAARRLPAKFGLDPRRDVQVLAPMHRGPAGAGVLNGLLQQAVTPARPGLAEKRFGGRVFRVGDKVTQIRNNYEKGANGVFNGTVGVVTSLDVDEQRLTVLTDEDEEVPYDFDELDELAHAYAVTIHRSQGSEYPAVVIPVTTGAWMMLQRNLLYTAVTRAKKLVVLVGSRKAIGQAVRTVSAGRRFTSLRHRLKGEVRVGNIT
>NZ_CP034279.1|WP_156694278.1|4810284_4811574_+|citrate-synthase
MSDNSVVLRYADGEYTYPVVESTVGDKGFDIGKLRAQTGLVTLDSGYGNTAAYKSAITYLDGEQGILRYRGYPIEQLAERSTFLEVAYLLINGELPKVDELAAFRNEITQHTLLHEDVKRFFDGFPRDAHPMAMLSSVVSALSTFYQDSHNPFDEKQRHLSTIRLLAKLPTIAAYAYKKSIGHPFVYPRNDLSYVENFLRMTFSVPAQEYELDPVVVSALDKLLILHADHEQNCSTSTVRLVGSSQANMFASVSAGISALWGPLHGGANQSVLEMLQGIKADGGDVDSFIRKVKNKEDGVRLMGFGHRVYKNFDPRAKIIKAAAHDVLSALGKSDELLDIALKLEEHALADDYFVSRNLYPNVDFYTGLIYRAMGFPTEMFTVLFALGRLPGWIAQWHEMIKEPGSRIGRPRQIYTGEVLRDFVPVEGR
>NZ_CP034279.1|WP_156694279.1|4812047_4812359_-|copper-binding-protein
MTAETRTELPQATGSCCSPAGSCHDSAAGAAAGGVTTVYEVRGMTCGHCEGAVTEEVSALAGVTSVTADAGSGLVTVVSETALDEAEVRAAVDEAGYELAGRA
>NZ_CP034279.1|WP_156694280.1|4812444_4813056_-|GNAT-family-N-acetyltransferase
MTDFSSKPTLTGDNVVLRPVTEEDAAVFAEILTDPEVLTLTGTPEDAPPLSPAYLRSWYGSRGDHPDRLDLALVDRTSGEVVGELVLNEWDEPNRSCNFRTLIGPRGRGRGLGTEAIRLLLAHAFEHLHLNRVSLGVFAFNPRAIRVYEKVGFVQEGVEREALLHRGRWIDSLSMSVLAREWAVHRGHPETAHGPGLTGIHTP

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Crispr_ID: NZ_CP034279_9

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP034279_9

5076678-5076782

Orphan

Consensus_repeat	Method
ATCCCCTGTAGCTCAATTGGCAGAGCA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP034279_9

>merge|NZ_CP034279|9|5076678-5076782|CRISPRCasFinder
ATCCCCTGTAGCTCAATTGGCAGAGCAGCCGGCTGTTAACCGGCAGGTTACTGGTTCGAGTCCAGTCGGGGGAGCGCGATCCCCTGTAGCTCAATTGGCAGAGCA

>NZ_CP034279|9|9|5076678-5076782|CRISPRCasFinder
ATCCCCTGTAGCTCAATTGGCAGAGCA	GCCGGCTGTTAACCGGCAGGTTACTGGTTCGAGTCCAGTCGGGGGAGCGCG
ATCCCCTGTAGCTCAATTGGCAGAGCA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP034279.1\|WP_156694522.1\|5063144_5063876_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP034279.1\|WP_156694532.1\|5077145_5077982_-\|class-II-glutamine-amidotransferase	unknown	unknown	gnl\|CDD\|238889
NZ_CP034279.1\|WP_156694530.1\|5074739_5076182_-\|sugar-kinase	unknown	unknown	gnl\|CDD\|198375
NZ_CP034279.1\|WP_156694531.1\|5076203_5076506_-\|YtxH-domain-containing-protein	unknown	unknown	unknown
NZ_CP034279.1\|WP_156694533.1\|5077989_5078409_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP034279.1\|WP_156694526.1\|5067560_5069471_+\|DNA-primase	unknown	unknown	gnl\|CDD\|235551
NZ_CP034279.1\|WP_156694529.1\|5072931_5074665_-\|ATP-binding-cassette-domain-containing-protein	unknown	unknown	gnl\|CDD\|224055
NZ_CP034279.1\|WP_156694541.1\|5087110_5087686_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP034279.1\|WP_156694525.1\|5066179_5067448_+\|FAD-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|170080
NZ_CP034279.1\|WP_156694537.1\|5081455_5082778_-\|acetyl-CoA-carboxylase	unknown	unknown	gnl\|CDD\|223895
NZ_CP034279.1\|WP_156694538.1\|5082770_5084237_-\|AMP-binding-protein	unknown	unknown	gnl\|CDD\|236096
NZ_CP034279.1\|WP_156694524.1\|5064762_5066076_+\|deoxyguanosinetriphosphate-triphosphohydrolase	unknown	unknown	gnl\|CDD\|235098
NZ_CP034279.1\|WP_156694523.1\|5063957_5064725_+\|sirohydrochlorin-chelatase	unknown	unknown	gnl\|CDD\|239507
NZ_CP034279.1\|WP_156694535.1\|5080034_5080448_-\|Ohr-family-peroxiredoxin	unknown	unknown	gnl\|CDD\|274649
NZ_CP034279.1\|WP_156694539.1\|5084416_5085889_-\|GAF-domain-containing-protein	unknown	unknown	gnl\|CDD\|226951
NZ_CP034279.1\|WP_156694536.1\|5080566_5081073_+\|MarR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|197670
NZ_CP034279.1\|WP_156694528.1\|5070979_5072932_-\|ATP-binding-cassette-domain-containing-protein	unknown	unknown	gnl\|CDD\|224055
NZ_CP034279.1\|WP_156694534.1\|5078836_5080045_+\|TIGR00645-family-protein	unknown	unknown	gnl\|CDD\|180607
NZ_CP034279.1\|WP_156694540.1\|5085885_5086929_-\|rod-shape-determining-protein-MreB	unknown	unknown	gnl\|CDD\|336482
NZ_CP034279.1\|WP_156694527.1\|5069540_5070953_+\|sigma-70-family-RNA-polymerase-sigma-factor	unknown	unknown	gnl\|CDD\|235640

Protein	Function_ID	Function_description	E-value
NZ_CP034279.1\|WP_156694539.1\|5084416_5085889_-\|GAF-domain-containing-protein	gnl\|CDD\|226951	COG4585, COG4585, Signal transduction histidine kinase [Signal transduction mechanisms].	1.76793e-14
NZ_CP034279.1\|WP_156694532.1\|5077145_5077982_-\|class-II-glutamine-amidotransferase	gnl\|CDD\|238889	cd01908, YafJ, Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine amidotransferase-like protein of unknown function found in prokaryotes, eukaryotes and archaea. YafJ has a conserved structural fold similar to those of other class II glutamine amidotransferases including glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). The YafJ fold is also somewhat similar to the Ntn (N-terminal nucleophile) hydrolase fold of the proteasomal alpha and beta subunits.	7.6789e-87
NZ_CP034279.1\|WP_156694530.1\|5074739_5076182_-\|sugar-kinase	gnl\|CDD\|198375	cd07809, FGGY_D-XK_1, D-xylulose kinases, subgroup 1; members of the FGGY family of carbohydrate kinases. This subgroup is composed of D-xylulose kinases (XK, also known as xylulokinase; EC 2.7.1.17) from bacteria and eukaryota. They share high sequence similarity with Escherichia coli xylulokinase (EcXK), which catalyzes the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P) and ADP. Some uncharacterized sequences are also included in this subfamily. EcXK exists as a dimer. Each monomer consists of two large domains separated by an open cleft that forms an active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The presence of Mg2+ or Mn2+ might be required for catalytic activity. Members of this subgroup belong to the FGGY family of carbohydrate kinases.	8.09695e-117
NZ_CP034279.1\|WP_156694526.1\|5067560_5069471_+\|DNA-primase	gnl\|CDD\|235551	PRK05667, dnaG, DNA primase; Validated.	0
NZ_CP034279.1\|WP_156694529.1\|5072931_5074665_-\|ATP-binding-cassette-domain-containing-protein	gnl\|CDD\|224055	COG1132, MdlB, ABC-type multidrug transport system, ATPase and permease components [Defense mechanisms].	1.15744e-159
NZ_CP034279.1\|WP_156694535.1\|5080034_5080448_-\|Ohr-family-peroxiredoxin	gnl\|CDD\|274649	TIGR03561, organ_hyd_perox, peroxiredoxin, Ohr subfamily. pfam02566, OsmC-like protein, contains several deeply split clades of homologous proteins. The clade modeled here includes the protein Ohr, or organic hydroperoxide resistance protein. [Cellular processes, Detoxification].	1.54863e-61
NZ_CP034279.1\|WP_156694537.1\|5081455_5082778_-\|acetyl-CoA-carboxylase	gnl\|CDD\|223895	COG0825, AccA, Acetyl-CoA carboxylase alpha subunit [Lipid metabolism].	1.77481e-53
NZ_CP034279.1\|WP_156694538.1\|5082770_5084237_-\|AMP-binding-protein	gnl\|CDD\|236096	PRK07787, PRK07787, acyl-CoA synthetase; Validated.	0
NZ_CP034279.1\|WP_156694524.1\|5064762_5066076_+\|deoxyguanosinetriphosphate-triphosphohydrolase	gnl\|CDD\|235098	PRK03007, PRK03007, deoxyguanosinetriphosphate triphosphohydrolase-like protein; Provisional.	0
NZ_CP034279.1\|WP_156694523.1\|5063957_5064725_+\|sirohydrochlorin-chelatase	gnl\|CDD\|239507	cd03414, CbiX_SirB_C, Sirohydrochlorin cobalt chelatase (CbiX) and sirohydrochlorin iron chelatase (SirB), C-terminal domain. SirB catalyzes the ferro-chelation of sirohydrochlorin to siroheme, the prosthetic group of sulfite and nitrite reductases. CbiX is a cobaltochelatase, responsible for the chelation of Co2+ into sirohydrochlorin, an important step in the vitamin B12 biosynthetic pathway. CbiX often contains a C-terminal histidine-rich region that may be important for metal delivery and/or storage, and may also contain an iron-sulfur center. Both CbiX and SirB are found in a wide range of bacteria.	1.04348e-27
NZ_CP034279.1\|WP_156694525.1\|5066179_5067448_+\|FAD-dependent-oxidoreductase	gnl\|CDD\|170080	PRK09754, PRK09754, phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional.	5.50721e-69
NZ_CP034279.1\|WP_156694536.1\|5080566_5081073_+\|MarR-family-transcriptional-regulator	gnl\|CDD\|197670	smart00347, HTH_MARR, helix_turn_helix multiple antibiotic resistance protein.	9.27989e-22
NZ_CP034279.1\|WP_156694534.1\|5078836_5080045_+\|TIGR00645-family-protein	gnl\|CDD\|180607	PRK06526, PRK06526, transposase; Provisional.	1.26405e-88
NZ_CP034279.1\|WP_156694528.1\|5070979_5072932_-\|ATP-binding-cassette-domain-containing-protein	gnl\|CDD\|224055	COG1132, MdlB, ABC-type multidrug transport system, ATPase and permease components [Defense mechanisms].	0
NZ_CP034279.1\|WP_156694540.1\|5085885_5086929_-\|rod-shape-determining-protein-MreB	gnl\|CDD\|336482	pfam06723, MreB_Mbl, MreB/Mbl protein. This family consists of bacterial MreB and Mbl proteins as well as two related archaeal sequences. MreB is known to be a rod shape-determining protein in bacteria and goes to make up the bacterial cytoskeleton. Genes coding for MreB/Mbl are only found in elongated bacteria, not in coccoid forms. It has been speculated that constituents of the eukaryotic cytoskeleton (tubulin, actin) may have evolved from prokaryotic precursor proteins closely related to today's bacterial proteins FtsZ and MreB/Mbl.	5.94481e-143
NZ_CP034279.1\|WP_156694527.1\|5069540_5070953_+\|sigma-70-family-RNA-polymerase-sigma-factor	gnl\|CDD\|235640	PRK05901, PRK05901, RNA polymerase sigma factor; Provisional.	4.90643e-161

>NZ_CP034279.1|WP_156694531.1|5076203_5076506_-|YtxH-domain-containing-protein
MRYKVTFVVGLALGYVLGTRAGRERYEQLRKSAREFSHNPAVRNAAESAAQTGREVAGKALHTVSDKVGDRMPESVAERVRSLRERSQGNGQDEWGTSNT
>NZ_CP034279.1|WP_156694530.1|5074739_5076182_-|sugar-kinase
MGIVAGLDSSSGFTRIVVCDTETGAVLRQGYAQHPVEPKATEVDPQAWLLSLGEAASGGLLEGVQAIGVSAQQHGLVPLDRQGALVRPALVGNDKRAQVAAADLVEAFGGRQAWAEAVGCVPQSAQPVAKLRWLARTEPEAAARVAMVMQPHDWLVWQLLGRPVRRTTDRGAASGTGYWSAGTGAYRPDLVELALGHQAALPEVLGPAEAAGMTPEGLLISAGTGETMAAALGLGLGVGDAVVSLGASGSVMAVHHEALADPRGMITAFADAAGTHLPVVHTSNAVRALRGTAEMLGLDGGLEELSALALKSTPGASGLVLLPYLEGERTPQLPHTAGTLSGLRRESMKPEHLARAAFEGMLCSLADAMDVLRGRGVEVRRVFLLGAAAELPAVQAAAPAIFGAQVVVPQPADYAALGAARQAAWALGVSQGVLSPQAPPAWQGAAAQVFEPGEEVAVGQAVRQQYMATREQLHPGAFAA
>NZ_CP034279.1|WP_156694529.1|5072931_5074665_-|ATP-binding-cassette-domain-containing-protein
MLRQLLRIHLGPYKRPIALLVALQLLQTCATLYLPTLNADIIDNGVVRGDTGYILRFGALMIAVSVVQVVCNIGAVHLGARTAAALGRDVRAAVFDRVQSFSAREVGHFGAPSLITRTTNDVQQVQMLVLMAFTLMVSAPIMCVGGIVMALGQDVPLSGVLLAVVPVLGVAVTLIVRRMRPLFRTMQERLDTVNRVLREQITGNRVIRAFVKDAYERERFERANAGLTEVSMSTGRLMALMFPTVMTVVNVSSVAVVWFGAHRIDDGAMEIGALTAFLAYLMQIVMAVMMATFMFMMVPRAEVCAERIEEVLRTESSVIPPAAPVRELSRRGHLEVRGADFRYPGAEEPVLRGVDLVARPGETTAIIGSTGSGKSTLLGLVPRLFDVTGGEVLVDGVDVRDLDPAVMARTVGLVPQRPYLFSGTVATNLRYGNPAASDEELWHALEVAQAAAFVRELEGGLDAPVSQGGTNVSGGQRQRLAIARTLVQRPEIYLFDDSFSALDYTTDALLRTALAAETAESTVVIVAQRVSTIRDADRIVVLDEGRVVGVGRHQELMAGNETYREIVLSQLTEAEAA
>NZ_CP034279.1|WP_156694528.1|5070979_5072932_-|ATP-binding-cassette-domain-containing-protein
MAGPAGRMMAAAGGPDQRSMDFKGSSRRLLRQLRPEKATLSVMLAAGVLSVALSVVGPMILGWATDLVFAGVVGREMPAELSKEQAVAGLRADGDGGLADMLSGVDFVPGRGIDFGAVGGVLMAALVVYVVAGLLMLVSTRMSIRVINRTVYRMREDVQAKLERLPLSYFDRAKRGEVLSRATNDIDNISQTMQQTMGQLINSALTIVGVLVMMFWISPLLALVALVTVPVSVVVATRVGKRSQPHFVQQWKSTGRLNAHIEEMYTGHALVKVFGRQGEAAADFREQNEALYEAGFRAQFNSGVMQPLMLFISNINYVLVAVVGGLRVASGTLSIGDVQAFIQYSRQFSMPLTQVASMANLVQSGVASAERIFELLDAQEQEPDAVGAAGRPGGPEEDGRDRGRVALEKVSFRYDPERPLIEDLSLSVEPGQTVAIVGPTGAGKTTLVNLLMRFYEVTGGRILLDGVAVTEMSRDELRSRIGMVLQDTWLFGGTIADNIAYGASREVTREEIEEAARAAHADRFVRTLPDGYDTVIDDEGAGVSAGEKQLITIARAFLSDPVILVLDEATSSVDTRTEVLIQKAMARLAHGRTSFVIAHRLSTIRDADVILVMENGAIVEQGTHEELLAARGAYARLYAAQFAQAVAEVD
>NZ_CP034279.1|WP_156694527.1|5069540_5070953_+|sigma-70-family-RNA-polymerase-sigma-factor
MPESSERGRSTDGGRPTPADPLIEYGTENSGAAAAVPLPHAPEPAAITLEVAPVQTRTPTDIDPATATAIAVPVQGLPTRHPEAGPGAGPDAPTGAAPDAPAGPDLDPLTDPVLDPVLDTATDPVLDPVPDVVPVLPPDAVPDAEPDDAGQTATGRSRTASAEAAGSGPSADLFRQYLREIGRIPLLTAAEEVELARRVEAGLFAEEKLARTPDPDSQLALDLDRLVVMGRMAKRRLIEANLRLVVSVAKRYVGRGLTMLDLVQEGNLGLIRAVEKFDYARGYKFSTYATWWIRQAMSRALADQARTIRVPVHVVELINRVVRVQRRMLQERGCEPTHDEVAAHLDLAPERVGEVLRLAQEPISLHAPVGEEDDVALGDLIEDGDAASPVESAAFLLLREHLEAVLSTLGERERKVVQLRYGLADGRPRTLEEIGRIFGVTRERIRQIESKTLNKLRDHAFADQLRGYLD
>NZ_CP034279.1|WP_156694526.1|5067560_5069471_+|DNA-primase
MAGGRINDDDVKAVRDAVPIDAVVSEYLQLRSAGGGNLKGLCPFHDEKSPSFQVSPSKGLFHCFGCQEGGDTIAFVMKIDHLSFSETVERLAAKAGITLRYEEGGYNPGHQRGERIRLIEAHKAAAQFYAEQLDGAEAEIGRKFLAERGFDQAAAQHFGVGYSPAGWDHLTRHLRGKGFSDKELLVSGLAQESRRNPIDRFRGRLMWPIRDVGGDVVGFGARKLRDDDNGPKYLNTPETPIYKKSQVLYGIDLAKKDIAKSSRAVVVEGYTDVMACHLAGVTTAIATCGTAFGGDHIKILRRLLMDNGSARVIFTFDGDAAGQKAALRAFEDDQKFAAETYIAIAPDGMDPCELRLAKGDDAVADLVEPRTPLFEFALRQIVNRYDLETPAGRAAALDEAAPIVARIKNIASQHEVAVQLAGMLGILDTQFVVKRVAQFARWARDRGGRGPAPATQARPPAAAPAPHAPAAPSGPALNLRSPAHRTERELLKLALQYPALVSPAFDAYGADEFTAPPYAAVRQTIADAGGAEQGISNAAEYLARVRDAAPDDRVRALVTELAVEVIHGRTVDETYAGDQLVQVRLRAVDRRIRDVTGSLTRLGTHADPDHLAAVQNELWVLQQYAQSLRNNGADAL
>NZ_CP034279.1|WP_156694525.1|5066179_5067448_+|FAD-dependent-oxidoreductase
MVDADQTFVIVGGGLAGVKAAETLRAEGFTGRVILIGDEVDPPYERPPLSKGYLTGKEPRERAFVHESAWYAEKDVELHLGQPVTAVDRAAKAVRLGDGTTIHYDKLLLATGSEPRRLDIPGTDLAGVHHLRRLAHADRLQGTLAALGRDNGHLVVAGAGWIGLEVAAAARGYGAEVTVVEPDPTPLYRVLGPELGQLFADLHAEHGVRFRFGTHLTQITGQDGMVLAARTDDGDEHPAHAVLVAVGAAPRTDLAENAGLALVDRAHGGGVAVDASLRTSDPDIHAAGDVAAAEHPLLHTRLRVEHWANALNGGPAAARAMLGRDVSYDRVPYFFSDQYDLGMEYSGWAPPGTYDQVVLRGDAGKREFIAFWLKDRRVLAGMNVNVWDVTSDIQALVRSGAPVDPDALADPSTPLTAVLPGP
>NZ_CP034279.1|WP_156694524.1|5064762_5066076_+|deoxyguanosinetriphosphate-triphosphohydrolase
MNGMDGTDGMDGTDGTYDEAATGRWAPEPDKRPGRTAFQRDRARVLHSGALRRLAGKTQVVTPGSRSHAWDPSPRTRLTHSLECAQVGRELGAALGCDPDLVEAACLSHDMGHPPFGHNGEQALNDFAKDCGGFEGNAQSLRLLTRIEPKRFIHLATTGEVVSVGLNLTRATLDAATKYPWPRGAHPTDPDSPKFGVYEDDLPVFAWVREGAPGTRQCFEAQVMDWSDDVAYSVHDFEDGLHAGHVDPNLLLAEPERADIWRVAIGRYVPHDTDPQELEAALDRLMEQEWWPHGYDGSAIAQARLKDATSQLIGRFCLAAEAATRRAYGTGRLTRYGAELVVPRETRHECAVLKAVADRYVMQRAEQEALRADQRIVLGELAEALTARAPEGLDPQFRALFDTAPDDRARKRVIVDQIASLTDASARALHSRLTHRG
>NZ_CP034279.1|WP_156694523.1|5063957_5064725_+|sirohydrochlorin-chelatase
MTEQPHPPTLVAVAHGSRDPRALATVNALLDRVRELRPTLPVRLGHIELNAPLLTDTLAAHPPGDAVLVPLLLSRGHHVKHDLPRAAATAPHLRVRVAAPLGPHPLLVEALLARLTEAGWRTAHGTDRATGVVLAAAGSRDPDSAADTRRTARLLSERLGGVPVVPAYASAASPTVPEALRALTARGRHRIAVASCFTAPGLFAARTAAAAPWIAAAPLGAHPALARLVLHRYDQATATPAPAPSTTAEPQLVTA
>NZ_CP034279.1|WP_156694522.1|5063144_5063876_+|hypothetical-protein
MSTPGLWARAAARNNAAWCDTMCRAHGLGPGDLTGRVWTHPRRTPPYYPDAVTLVPGTPAHEVLDAIDLRTPGCSVKDGFATLDLTPHGFRPLFDAQWIHRPATPPGDTAADTVPWEPVRTAAALADWETAWSDGADPMNLFRPALLDDPATTVLAGHAPDGRTVAGAVVTLSATPDAGPVVGVSNVFATGPGADPWPGCLAAIARRWPGTPVVGYEHGDDLTAALRHGFTTTGTLRVWVAAP
>NZ_CP034279.1|WP_156694532.1|5077145_5077982_-|class-II-glutamine-amidotransferase
MCRWLAYSGTPLLLEGILYRPAHSLIDQSLHSRMGVETTNGDGFGIGWYAQDTDLDAPAVVRDVGPAWNNRNLREIAKTVRSPLFFAHIRASTGTAVQQTNCHPFRHGRWLWMHNGAIADFHLLRRELCLAVEPGLFADIEGSTDSEVMFYLALTLGLEEDPPGAVARMAGLVERTGRAHGVDHPLQMTIALTDGVSIWAFRYSTERRSRSLFYSSRVDSLRALHPDLTFLRDISDETRLVVSEPLGDLPGAWHEVPEHTYGVVRPGADDLRPFAPAA
>NZ_CP034279.1|WP_156694533.1|5077989_5078409_-|hypothetical-protein
MSTHVQHDRKSQGFASGLVVFSAVMMVVAGVLDLFRGIMGVARDDVFVTTPNYIFKFDLTSWGWIHLIFGALAIIVGMGLFKPSMWARVAGVALASLLLIANFLSIPYYPLWSIVAIAMYGFIIWALCTVRPDSGGRGV
>NZ_CP034279.1|WP_156694534.1|5078836_5080045_+|TIGR00645-family-protein
MTTLGCALFATRWLQAPLYFGLVAAQGVYVYKFFNELWHLIHHVISGHADETHVMLAVLKLVDVVMIANLLIMVIVGGYETFVSRIGLQGHRDQPEWLSHVNSNVLKVKLATAIVGISSVHLLQMFVDVHHTPRHDLLWGTVIHMAFIASAAILAYMSGPMAAHEAKAHALHETRHAEPRTVTIPAQRDGGAAHHDEAPEAGSGAEERIEAAGFPARKVLETFDDGHLRAPDPQVIARLGKADFVARKANVVLLGGPGTGKTHLAVALGVRACQAGHQVLFATAAEWGTRLSDAKAAGRLRAELARLDAYPVLIVDEVGYVPFEPEVANLFFQLVSHRYERASLIVTGNRPLGRWDEVFGDSATASATVDRLAHHAEVVTLDADSYRTRRLEGAGVGGWVTR
>NZ_CP034279.1|WP_156694535.1|5080034_5080448_-|Ohr-family-peroxiredoxin
MDALYTAVATANGREGRAVSSDGQIDLPLGFPQALGGNGQGTNPEQLFAAGYAACFASAMGAIGRQEKIDVKDASVTAEVSIGKDTDGGFGLAVVMRVELPDHLQGEPGRDLLEKTHAYCPYSKATRGNIQVELVIE
>NZ_CP034279.1|WP_156694536.1|5080566_5081073_+|MarR-family-transcriptional-regulator
MDTLGTKVADGTARDEDFLRLDHQICFSLHAATRAFNSVYRTALKDLGLTYPQYLVMLVLWERGELPVKQIGEHLRLDSGTLSPLLKRLEAAGYVERRRSAEDERSVTARPTPAGTALRERALGVPRRIATATGMTLDEVRELRARLNELTTALDAAGPLAEGCVTED
>NZ_CP034279.1|WP_156694537.1|5081455_5082778_-|acetyl-CoA-carboxylase
MAERLSARAAIGLLTDAFEDHAPPDRACAPDGPLAWEGYDASRARAAERTGEAESVVYGTARVGDRSCAVLAFEFGFLGGSLGERAGDRLEAAYRLAREERVPLLSLVATGGSRMQEGMVALTQLQRVARESVLLREAGLPHLTVLRDPATGGGWATVGAGADVILALPGAQVGFAGSRVRPADADPAAYTAEGQLAAGHVDAVVRPEELRGTVTRWVTALTSPAAQAPPPAALSSGPLPASGWDAVRQARDPGRPRAEAYLNAYFTDRLPLAGDRCGGTDPGMLCGIGLRADGRAVAYVAQCGTATRPAGYRTAARVIRLADRLGVPVLTLVDTPGAANDAEAERAGAGAAIADAFTAVAAARVPVTTLLIGEGGSGGALALAAPDNTWATRDSYFSVIAPELAAAILKRPPQDAPHTAEQLRLRPQDLVELGVVRGIV
>NZ_CP034279.1|WP_156694538.1|5082770_5084237_-|AMP-binding-protein
MSSLFPALDAPDAGAGRPALRFADRSLTYGELRAAARSLAVRLDGAERVAVWATPTLETSVAVVAALLAGVPAVPLNPRTGERELTHIVTDSRPALVLASPEDGLPHALSGLDRLDVTVDSAESAPVGRPPAEPDDPEAPALIVYTSGTTGPPKGAVLPRRAVASTLDALADAWAWTSADVLVHALPLFHVHGLILGVLGPLRHGGSVRHLGRFTTGGVARELAAGGTMLFGVPTMYHRIAEALDDDPQLAKALAGARLLVSGSAALPLHDHERIAALTGRRVIERYGMTETLMNTSVRADDVEPRTGSVGVPLPGVELRLVDEEDGTEIAAYDGETVGEIQVRGPNLFTGYLNRPDATAAAFDGTWFRTGDMAVRAGDGSVRIVGRRATDLIKSGGYKIGAGEIENALLDHPGVREAAVTGEPDPDLGERIVAWVVPADPTAPPSEAELADHVAAQLAPHKRPRTVRYLDVLPRNDMGKIMKRSLHG
>NZ_CP034279.1|WP_156694539.1|5084416_5085889_-|GAF-domain-containing-protein
MTGRGLPALLGAVLDVGTDLELRATLQHLVEHAAALTDARTASLVVLDPEQGRPTDRYTTGTAGNDDRSDRGDEHDLAVPVRVHTEVFGRLHLTGKRGGPFTGEDLATLRVLASQAGIAIGNARLYETARQRERWIEGAAAVTTALLTGGAAADALVTVAERARLLAGAAAGVVLQPTGEGGMEIVAASTPHDPDDLLGTTIAPGSPVLEQLLGGEPVFIDDSATDPRMTTPVRTRFGPSMMLPLQSGGKLIGTLALPRRRGGLPYTAVERLLASQFASQAALALVLADAQADRERLAVYEDRDRIARDLHDLVVQRLFATEMMLEATRRRASGAAADLLDRAVDELDSTIQEVRTAIFALQQPPVDAPRSLRGRVLRETGGAAVLLGFRPSVHFTGAVDALVTDPVADRLLTALRGALVAAHRREGLTAVDVEVDATATLPDGRPGIRLTVTDDGAGGATVTWRSPREVGPRDALDGGPGSPAAPPPPT
>NZ_CP034279.1|WP_156694540.1|5085885_5086929_-|rod-shape-determining-protein-MreB
MTVSLEQLRRCHVAVDLGAARTRVFVKGVGLVVDEPSVAAVNTRTGALIAVGEFAEKMTGRTPDYIRVVRPVSGGSVVDIDMAQRMLRHLLGEKLRRQLRRKPMLRAAACTPHDSDPLAQRATIETLVGLGARRVELVDTLIAAAVGCGLPVEQPTATMILVCGAATTQVAVLSLGAIVTAERIPVGGNAIDHAVIQYLRHQHELMLPSQSVRPLQLALHGNGLTPHGPASTEIHGRDVATGLARSVLVDTAAVRQALHTPLTAVLDGIGKVLRDCPPDLVADLVDRGIMMVGGSALLPGLDQMLRNATGMPVHIAERPDVCAVLGLGAMLEGRIEPLTLNPLAEAE
>NZ_CP034279.1|WP_156694541.1|5087110_5087686_-|hypothetical-protein
MKGTGTPSAPFGPPDFQLVLLRRMADHQPGLVEDARRELGASIADMREANRRWQAMTRSPRSRGALARYRSVLGEPESRTRRTVGDLECDALLWPVPLWPGLRFEVLAAPGGGPVWNEWLVRAPGAAGPELRTVADLRPWTCTVDEVARAFPPARPLEGTAPTRWRLAFTPPGGGEPCTAEFTWGLLQRLL

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Crispr_ID: NZ_CP034279_10

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP034279_10

5139471-5139545

Orphan

Consensus_repeat	Method
CTGCGGGTAGCCGTAGGCGGGCTG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP034279_10

>merge|NZ_CP034279|10|5139471-5139545|CRISPRCasFinder
CTGCGGGTAGCCGTAGGCGGGCTGCCCGGACCCGGGCTGTGCCGGACCGTCCTGCGGGTAGCCGTAGCCGGGCTG

>NZ_CP034279|10|10|5139471-5139545|CRISPRCasFinder
CTGCGGGTAGCCGTAGGCGGGCTG	CCCGGACCCGGGCTGTGCCGGACCGTC
CTGCGGGTAGCCGTAGCCGGGCTG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP034279.1\|WP_156694577.1\|5129610_5130060_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|377188
NZ_CP034279.1\|WP_156694581.1\|5134587_5135019_+\|DUF3052-family-protein	unknown	unknown	gnl\|CDD\|378615
NZ_CP034279.1\|WP_156694593.1\|5146156_5147500_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|224117
NZ_CP034279.1\|WP_156694589.1\|5141704_5144251_+\|phosphoribosyltransferase	unknown	unknown	gnl\|CDD\|378594
NZ_CP034279.1\|WP_156694595.1\|5148691_5149822_-\|tyrosine-type-recombinase/integrase	unknown	unknown	gnl\|CDD\|271189
NZ_CP034279.1\|WP_156694594.1\|5147574_5148339_-\|DUF4097-family-beta-strand-repeat-protein	unknown	unknown	gnl\|CDD\|372574
NZ_CP034279.1\|WP_156694583.1\|5135721_5136297_+\|chemical-damaging-agent-resistance-protein-C	unknown	unknown	gnl\|CDD\|376767
NZ_CP034279.1\|WP_156694578.1\|5130079_5130388_+\|small-hydrophobic-protein	unknown	unknown	unknown
NZ_CP034279.1\|WP_156694597.1\|5150033_5151434_-\|replication-initiation-protein	unknown	unknown	unknown
NZ_CP034279.1\|WP_156694585.1\|5137335_5138460_+\|DUF475-domain-containing-protein	unknown	unknown	gnl\|CDD\|237583
NZ_CP034279.1\|WP_156694586.1\|5138618_5139362_+\|Tellurium-resistance	unknown	unknown	gnl\|CDD\|226595
NZ_CP034279.1\|WP_156694579.1\|5130533_5131340_-\|two-pore-domain-potassium-channel-family-protein	unknown	unknown	gnl\|CDD\|369572
NZ_CP034279.1\|WP_156694591.1\|5145043_5145655_-\|DedA-family-protein	unknown	unknown	gnl\|CDD\|223659
NZ_CP034279.1\|WP_156694588.1\|5140544_5141708_+\|HpcH/HpaI-aldolase/citrate-lyase-family-protein	unknown	unknown	gnl\|CDD\|379744
NZ_CP034279.1\|WP_156694584.1\|5136676_5137252_+\|chemical-damaging-agent-resistance-protein-C	unknown	unknown	gnl\|CDD\|376767
NZ_CP034279.1\|WP_156694582.1\|5135123_5135609_+\|redoxin-domain-containing-protein	unknown	unknown	gnl\|CDD\|239316
NZ_CP034279.1\|WP_156694592.1\|5145916_5146135_-\|zinc-ribbon-domain-containing-protein	unknown	unknown	gnl\|CDD\|274226
NZ_CP034279.1\|WP_156694596.1\|5149821_5150037_-\|excisionase-family-DNA-binding-protein	unknown	unknown	gnl\|CDD\|200128
NZ_CP034279.1\|WP_156694590.1\|5144247_5145075_+\|HAD-family-hydrolase	unknown	unknown	gnl\|CDD\|319822
NZ_CP034279.1\|WP_156694580.1\|5131403_5134136_-\|pyruvate-dehydrogenase-(acetyl-transferring),-homodimeric-type	unknown	unknown	gnl\|CDD\|236500

Protein	Function_ID	Function_description	E-value
NZ_CP034279.1\|WP_156694577.1\|5129610_5130060_+\|hypothetical-protein	gnl\|CDD\|377188	pfam03995, Inhibitor_I36, Peptidase inhibitor family I36. This domain is currently only found in a small set of S. coelicolor secreted proteins. There are four conserved cysteines that probably form two disulphide bonds. Proteins 2SCK31.15C and SCO3675 also have probable beta-propellers at their C-termini. This family includes Streptomyces nigrescens SmpI, a known peptidase inhibitor of known structure. This protein has a crystallin like fold pfam00030 and is distantly related by sequence. It is not known whether other members of this family are peptidase inhibitors.	6.53356e-05
NZ_CP034279.1\|WP_156694590.1\|5144247_5145075_+\|HAD-family-hydrolase	gnl\|CDD\|319822	cd07520, HAD_like, uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily. The haloacid dehalogenase-like (HAD) hydrolases are a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members include 2-L-haloalkanoic acid dehalogenase (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. Members are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.	1.12684e-10
NZ_CP034279.1\|WP_156694593.1\|5146156_5147500_-\|hypothetical-protein	gnl\|CDD\|224117	COG1196, Smc, Chromosome segregation ATPases [Cell division and chromosome partitioning].	0.00489891
NZ_CP034279.1\|WP_156694589.1\|5141704_5144251_+\|phosphoribosyltransferase	gnl\|CDD\|378594	pfam11202, PRTase_1, Phosphoribosyl transferase (PRTase). This PRTase family is fused to a C-terminal RNA binding Pelota domain, pfam01248. These genes are found in the biosynthetic operon associated with the Ter stress response operon and are predicted to be involved in the biosynthesis of a ribo-nucleoside involved in stress response.	1.30616e-150
NZ_CP034279.1\|WP_156694595.1\|5148691_5149822_-\|tyrosine-type-recombinase/integrase	gnl\|CDD\|271189	cd01189, INT_ICEBs1_C_like, C-terminal catalytic domain of integrases from bacterial phages and conjugate transposons. This family of tyrosine based site-specific integrases is has origins in bacterial phages and conjugate transposons. One member is the integrase from Bacillus subtilis conjugative transposon ICEBs1. ICEBs1 can be excised and transfered to various recipients in response to DNA damage or high concentrations of potential mating partners. The family belongs to the superfamily of DNA breaking-rejoining enzymes, which share the same fold in their catalytic domain and the overall reaction mechanism. The catalytic domain contains six conserved active site residues. Their overall reaction mechanism involves cleavage of a single strand of a DNA duplex by nucleophilic attack of a conserved tyrosine to give a 3' phosphotyrosyl protein-DNA adduct. In the second rejoining step, a terminal 5' hydroxyl attacks the covalent adduct to release the enzyme and generate duplex DNA.	1.83598e-30
NZ_CP034279.1\|WP_156694594.1\|5147574_5148339_-\|DUF4097-family-beta-strand-repeat-protein	gnl\|CDD\|372574	pfam13349, DUF4097, Putative adhesin. This has a putative all-beta structure with a twenty-residue repeat with a highly conserved repeating GD, gly-asp, motif. It may form part of a bacterial adhesin.	1.71531e-09
NZ_CP034279.1\|WP_156694583.1\|5135721_5136297_+\|chemical-damaging-agent-resistance-protein-C	gnl\|CDD\|376767	pfam02342, TerD, TerD domain. The TerD domain is found in TerD family proteins that include the paralogous TerD, TerA, TerE, TerF and TerZ proteins It is found in a stress response operon with TerB and TerC. TerD has a maximum of two calcium-binding sites depending on the conservation of aspartates. It has various fusions to nuclease domains, RNA binding domains, ubiquitin related domains, and metal binding domains. The ter gene products lie at the centre of membrane-linked metal recognition complexes with regulatory ramifications encompassing phosphorylation-dependent signal transduction, RNA-dependent regulation, biosynthesis of nucleoside-like metabolites and DNA processing linked to novel pathways.	1.32001e-121
NZ_CP034279.1\|WP_156694581.1\|5134587_5135019_+\|DUF3052-family-protein	gnl\|CDD\|378615	pfam11253, DUF3052, Protein of unknown function (DUF3052). This family of proteins with unknown function appears to be restricted to Actinobacteria.	2.16739e-67
NZ_CP034279.1\|WP_156694585.1\|5137335_5138460_+\|DUF475-domain-containing-protein	gnl\|CDD\|237583	PRK14013, PRK14013, hypothetical protein; Provisional.	5.60355e-173
NZ_CP034279.1\|WP_156694586.1\|5138618_5139362_+\|Tellurium-resistance	gnl\|CDD\|226595	COG4110, COG4110, Uncharacterized protein involved in stress response [General function prediction only].	7.71192e-52
NZ_CP034279.1\|WP_156694579.1\|5130533_5131340_-\|two-pore-domain-potassium-channel-family-protein	gnl\|CDD\|369572	pfam07885, Ion_trans_2, Ion channel. This family includes the two membrane helix type ion channels found in bacteria.	2.63047e-15
NZ_CP034279.1\|WP_156694591.1\|5145043_5145655_-\|DedA-family-protein	gnl\|CDD\|223659	COG0586, DedA, Uncharacterized membrane-associated protein [Function unknown].	2.39268e-40
NZ_CP034279.1\|WP_156694588.1\|5140544_5141708_+\|HpcH/HpaI-aldolase/citrate-lyase-family-protein	gnl\|CDD\|379744	pfam15617, C-C_Bond_Lyase, C-C_Bond_Lyase of the TIM-Barrel fold. This family of TIM-Barrel fold C-C bond lyase is related to citrate-lyase. These genes are found in the biosynthetic operon, with other enzymatic domains, associated with the Ter stress response operon and are predicted to be involved in the biosynthesis of a ribo-nucleoside involved in stress response.	5.11474e-165
NZ_CP034279.1\|WP_156694584.1\|5136676_5137252_+\|chemical-damaging-agent-resistance-protein-C	gnl\|CDD\|376767	pfam02342, TerD, TerD domain. The TerD domain is found in TerD family proteins that include the paralogous TerD, TerA, TerE, TerF and TerZ proteins It is found in a stress response operon with TerB and TerC. TerD has a maximum of two calcium-binding sites depending on the conservation of aspartates. It has various fusions to nuclease domains, RNA binding domains, ubiquitin related domains, and metal binding domains. The ter gene products lie at the centre of membrane-linked metal recognition complexes with regulatory ramifications encompassing phosphorylation-dependent signal transduction, RNA-dependent regulation, biosynthesis of nucleoside-like metabolites and DNA processing linked to novel pathways.	2.66352e-120
NZ_CP034279.1\|WP_156694582.1\|5135123_5135609_+\|redoxin-domain-containing-protein	gnl\|CDD\|239316	cd03018, PRX_AhpE_like, Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium tuberculosis AhpE. AhpE is described as a 1-cys PRX because of the absence of a resolving cysteine. The structure and sequence of AhpE, however, show greater similarity to 2-cys PRXs than 1-cys PRXs. PRXs are thiol-specific antioxidant (TSA) proteins that confer a protective role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either thioredoxin, glutathione, trypanothione and AhpF. The first step of catalysis is the nucleophilic attack by the peroxidatic cysteine on the peroxide leading to the formation of a cysteine sulfenic acid intermediate. The absence of a resolving cysteine suggests that functional AhpE is regenerated by an external reductant. The solution behavior and crystal structure of AhpE show that it forms dimers and octamers.	1.23104e-76
NZ_CP034279.1\|WP_156694596.1\|5149821_5150037_-\|excisionase-family-DNA-binding-protein	gnl\|CDD\|200128	TIGR01764, Probable_excisionase, DNA binding domain, excisionase family. An excisionase, or Xis protein, is a small protein that binds and promotes excisive recombination; it is not enzymatically active. This model represents a number of putative excisionases and related proteins from temperate phage, plasmids, and transposons, as well as DNA binding domains of other proteins, such as a DNA modification methylase. This model identifies mostly small proteins and N-terminal regions of large proteins, but some proteins appear to have two copies. This domain appears similar, in both sequence and predicted secondary structure (PSIPRED) to the MerR family of transcriptional regulators (pfam00376). [Unknown function, General].	8.20245e-12
NZ_CP034279.1\|WP_156694592.1\|5145916_5146135_-\|zinc-ribbon-domain-containing-protein	gnl\|CDD\|274226	TIGR02605, CxxC_CxxC_SSSS, putative regulatory protein, FmdB family. This model represents a region of about 50 amino acids found in a number of small proteins in a wide range of bacteria. The region begins usually with the initiator Met and contains two CxxC motifs separated by 17 amino acids. One member of this family is has been noted as a putative regulatory protein, designated FmdB (SP:Q50229, ). Most members of this family have a C-terminal region containing highly degenerate sequence, such as SSTSESTKSSGSSGSSGSSESKASGSTEKSTSSTTAAAAV in Mycobacterium tuberculosis and VAVGGSAPAPSPAPRAGGGGGGCCGGGCCG in Streptomyces avermitilis. These low complexity regions, which are not included in the model, resemble low-complexity C-terminal regions of some heterocycle-containing bacteriocin precursors. [Regulatory functions, DNA interactions].	1.81791e-11
NZ_CP034279.1\|WP_156694580.1\|5131403_5134136_-\|pyruvate-dehydrogenase-(acetyl-transferring),-homodimeric-type	gnl\|CDD\|236500	PRK09405, aceE, pyruvate dehydrogenase subunit E1; Reviewed.	0

>NZ_CP034279.1|WP_156694586.1|5138618_5139362_+|Tellurium-resistance
MAFWDSLLRNNNAAQFDSGSASSNAIDLTKRRPSVSLTKQGAATGNLRVNLSWRMRTSDIEGRSRHSGRLLRHPLKLFKPDVVQAHTQGVVNVDLDIGCLYEMKDGTKGVVQPLGSFFGDLNSAPYVKLSGDDRFGAPSGETIFVNLDHRDAIKRLLFFVYIYDQTPAFDRTHATMTLYPSNGPRIEIELDERAPQARSCAVFMLENVKDELVVRREVRFVYGFQAELDRLYGWGLQWGRGFKAGKV
>NZ_CP034279.1|WP_156694585.1|5137335_5138460_+|DUF475-domain-containing-protein
MVLKTFGWSFAVTALGLAFAAWQWGWEAFGIVLILSILEISLSFDNAVVNAGILKKMNAFWQKIFLTIGILIAVFGMRLVFPVVIVAISAQVGPIEAVQLAMDNPSRYEDLVTDAHAAIAAFGGMFLLMIFLDFMFEDREHKWLSWLERPAAKLGKVDMLSVCIALIVLLITAMTFATQAHTSTGHADKSATVLLSGVAGLVTYLIVGGLSGYFEDKLEEEEEREHEEEEKAKKEGKPVSAVGLAGKAAFFLFLYLEVLDASFSFDGVIGAFAITNHIFWMALGLGIGAMYVRSLTVYLVRQGTLDDYVYLEHGAHYAIGALAVILLITIQHEISEIITGLVGVFLIAASFLSSVRRNKALAAAGEEDKTHVSV
>NZ_CP034279.1|WP_156694584.1|5136676_5137252_+|chemical-damaging-agent-resistance-protein-C
MGVTLAKGGNVSLSKAAPNLTQVLVGLGWDARSTTGAPFDLDASALLCQNGRVLGDEWFVFYNNLTSPDGSVEHTGDNLTGEGEGDDESLIVDLPRVPAHVDKIIFPVSIHEADNRGQTFGQVSNAFIRVVNQADGQELARYDLSEDASTETAMIFGELYRYGGEWKFRAVGQGYASGLRGIALDFGVNVS
>NZ_CP034279.1|WP_156694583.1|5135721_5136297_+|chemical-damaging-agent-resistance-protein-C
MGVSLSKGGNVSLTKEAPGLTAVTVGLGWDVRTTTGTDFDLDASAILVSAEGKVRNDQDFVFFNNLKSADGSVEHTGDNLTGEGEGDDEQVKVDLANVPADVAKILFPVSIYDAETRQQSFGQVRNAFIRVVNQAGGAEIARYDLSEDASTETAMVFGELYRNGAEWKFRAVGQGYASGLRGIAQDFGVNV
>NZ_CP034279.1|WP_156694582.1|5135123_5135609_+|redoxin-domain-containing-protein
MAIEAIETTAPVQAGTKAPDFELKDNHGRTVSLADFRGEKNVVLLFYPFAFTGVCTGELCALRDELPTFVNDDTQLLAVSNDSIHTLRVFAEQEGLEYPLLSDFWPHGEVSRAYGVFDEEKGCAVRGTFIIDKEGVVRWTVVNGLPDARDLNEYVAALDTL
>NZ_CP034279.1|WP_156694581.1|5134587_5135019_+|DUF3052-family-protein
MSATADHAEERTNPAAKLGFEPGQVVQEIGYDDDVEQELREGIEALIGQDLVDEDYDDVADVVLLWFRDDDGDLTDALVDAIGLIDEGGQIWLMTPKTGRDGYIEPSDINEAAQTAGLSQTRSINAGKDWTGSRLVTPKTAKR
>NZ_CP034279.1|WP_156694580.1|5131403_5134136_-|pyruvate-dehydrogenase-(acetyl-transferring),-homodimeric-type
MASGSDRNPIIIGGLPSQVPDFDPEETQEWLDSLDAAVDERGRERARYLMLRLIERAREKRVAVPEMRSTDYVNTIATKDEPFFPGNEEIERKVLNATRWNAAVMVSRAQRPGIGVGGHIATFASSASLYDVGFNHFFRGKDEGDGGDQIFFQGHASPGVYARAFLLDRLTEAQLDAFRQEKSKFPNGLSSYPHPRLMPDFWEFPTVSMGLGPIGAIYQARMNRYMEARGIADTSKSQVWAFLGDGEMDEPESLGQLSIAAREGLDNLTFVVNCNLQRLDGPVRGNGKIIQELESQFRGAGWNVIKLVWDRSWDPLLAQDRDGILVNKLNTTPDGQFQTYATETGAYIRDHFFGDDQRLRAMVENMSDDQILHLGRGGHDHKKIFAAYKAAVEHKGQPTVILAQTVKGWTLGPNFEGRNATHQMKKLTVDDLKGFRDRLHIPITDQQLESGVPPYYHPGRDSEEIQYMHDRRKGLGGYVPTRVVRAKPLALPDDKTYAAVKKGSGQQSIATTMAFVRLLKDLMRDKEIGKRFVLIAPDEYRTFGMDSFFPSAKIYNPLGQQYEAVDRELLLAYKESPTGQMLHDGISEAGCTASLIAAGSAYATHGEPLIPVYVFYSMFGFQRTGDQFWQMADQLARGFVLGATAGRTTLTGEGLQHADGHSQLLASTNPACVAYDPAFGFEIAHIVKDGLRRMYGENAEDVFYYLTVYNEPIQHPAEPADVDVDGIVKGIHRFKAGEAGAIPAQILASGVAVPWALEAQRILADEWNVRADVWSATSWNELRREAVEVERHNLLHPEEEQQVPFVTRKLSGAEGPFVAVSDWMRSVPDQISRWVPGTYTSLGADGFGFADTRGAARRYFHIDAQSVVLAVLTELARDGKVDRSVLKQAVDRYQLLDVSAADPGAAGGDA
>NZ_CP034279.1|WP_156694579.1|5130533_5131340_-|two-pore-domain-potassium-channel-family-protein
MKERWEARTQTPLLALALAFAVAYAVPIVAPDAERWVHTSCTAVEWVVWGAFALDYVIRLALAPSRWHFVRSHPLDLLAVLLPLVQPLRLLRLVSTLLLVGRRARMASQIRLTTYVAGSVAGLLMFGSLAVLHVERDAPDGNIKTLGDAVWWSFTTMTTVGYGDHAPTTGLGRLLAVGLMLSGIALLGVVTANIAAWFISRFERDDAAERRQAALLEALTLEVRELRAEVGRLSPGATEVVSAPATSGPATSGPVVPAPPRTDPEMAP
>NZ_CP034279.1|WP_156694578.1|5130079_5130388_+|small-hydrophobic-protein
MGSFGYTSRSRRSPRSRGRTWSRTGPDRATLGIVGLVCAVAGLFVLGIVLGPVAIVCGWLGMGRRWASNHLPALVAFVLGAIDTVLALVWLAGAGTPGNGVL
>NZ_CP034279.1|WP_156694577.1|5129610_5130060_+|hypothetical-protein
MRSTTVVRSAVLTLACAAALTAGASATTALGAAVPVAAVPVGAVPVTAKSAATAPRLGPCDAGQLCLWAKEGFRGARHTYELAGVDIESCVPLPAGTAAVALANRTGRPVTTYQSAECGETGEFETYPGGGTWVPQSPYRVRAFKVWEN
>NZ_CP034279.1|WP_156694588.1|5140544_5141708_+|HpcH/HpaI-aldolase/citrate-lyase-family-protein
MRHFGHIPATARSGLFHREPCEFTADSPARVLGAALGATLYSPATRPRLADDVMKQVGRGVVSMVLCLEDSIDDGEVAEAEENLVRHFADLHERDGEPPLLFIRVRRAEQMADLVRRLGPSARLLSGFVLPKFTEERGGPFMEALTVAENICERRLFAMPVLESPELLHLETRYETLAGIGRIVDKYRDRVLALRLGVTDFCSAYGLRRSPEMTAYDVHIVAGVIADVVNVLGRSDGTGFTITGPVWEYFRLQERIFKPQLRRSPFMEQRADELRTALIEHDLDGLLREIELDRANGLLGKTCIHPSHVLPVHALSVVSHEEFSDAEDILRPERGGGGVLRSAYTNKMNEVKPHRAWAERTLRRAEVFGVAKEDVGFVELLAAGLVK
>NZ_CP034279.1|WP_156694589.1|5141704_5144251_+|phosphoribosyltransferase
MSHETPGRIPGESENVVVWSGTWVSERLGVELTGDRRLPELLGLALRRNPKRAHLLVSNVLGKHVPQSPGVVWRSGYDLGVRVRQLLGPADAERAVVLGYAETATGLGHSVADGVGSAPYLHSTRRPVPGVAPAGGFEEAHSHATSHLLLPEDPALLAGTGPLVLVDDEFSTGNTVLNTVRDLHSRHPRERYVIVALVDMRSAADQDRFAAFAAEIGARVDLVTLAAGTVRLPDGVLARGQALVAEYEAAAATRGAGTTPAAPAAPAPPVRRVRLGWPDGVPDGGRHGFTPAHRARLDAALPAMAERLADALGLPDGAPGGEGAAAPRLLVLGCEELMYAPLALGVALERHGGAEVRFSTTTRSPVLPVDDPGYAIRTRLVFPAHDAPADGPGDRYAYNVAGAGFDAVVAVVDSAADTPALHAPDGLLAQLAAHIPHVLLAVVPSYVPASRVPVPHVPASHVPAERPSMLPEPLRGPAFSSYAPEEVGWLLQDLSDVELEAPTEEREEAIQHGGAHYAESLPVEYQPSDRYQALFHAALDTSAARIARAVGTVTETVLAERSPRPVLVSLARAGTPVGVLMRRWALHRHGLDLPHYAVSIVRGRGIDANALRWLAAHHDPADVVFVDGWTGKGAITRELAAALQDFPGFDPEIAVLADPGSCVRTYGTREDFLIPSACLNSTVSGLISRTVLRADLVGPDDYHGAKFYRELAGADVSNDFLTAITSHFDDVTALVDADVKELSATDRTPTWAGWAAVERISQEYGIHDVNLVKPGVGETTRVLLRRVPWKILAQRGAGADLDHVRLLAEQRGVPVEEVDDLHYTCVGLIHPKYTRGATGADGKAVANR
>NZ_CP034279.1|WP_156694590.1|5144247_5145075_+|HAD-family-hydrolase
MTTALTTLVASDLDRTLIYSAAALGLTMPDAEAPRLLCVETYQHKPLSYMTETAAALLTELPRHAVFVPATTRTREQYQRIRLPGPPARYAICANGGHLLVDGVSDPDWRRTVAARLADECASLDEVRTHLLAAADPAWLLKERVAEDLFAYLVVERALMPDGWMKELAAWAAPRGWAVSLQGRKVYAVPQPLTKSAAVREVARRTGADQVLAAGDSLLDADLLLAADRGWRPGHGELAEAGWNAGHVEALEERGVAAGEEILRRFSSAVPPNPA
>NZ_CP034279.1|WP_156694591.1|5145043_5145655_-|DedA-family-protein
MERWINSLMDTLGAPGAGLAIALENLFPPLPSEVILPLAGFASATGRIDLIAALLWTTAGSVVGALALYGVGALLGRERTIAIASKLPLVKVADIERTEAWFGRHGTKAVFFGRMIPIFRSLISVPAGIERMPLPVFLGLTTLGSAIWNTAFVLAGYVLGDNWEQVSHYVSLYSKVVLVVAVAAVVAFVAVRLLKPGSGARRS
>NZ_CP034279.1|WP_156694592.1|5145916_5146135_-|zinc-ribbon-domain-containing-protein
MPRYEYRCRTCGDTFELNRPMAESSAPAACPVGHDDTVKLLSAVAVGGTAKGGAPAPSQGGGGGCCGGGCCG
>NZ_CP034279.1|WP_156694593.1|5146156_5147500_-|hypothetical-protein
MTATRARRYVQDVLALMLLPVPLMVAALPGAFAGGGTRRWFGGRGESQRADAQAAKDAAAAAFYELDTAQRDLRISIETITAVDASPGALRAVDGFAELGRRIDEVSLAYITVVDAYDLDRDDLEASVASRARGELNRAKDDLVRVKGELDRFEQGLGPLLDKAETQLARLAPAVERARAALLSASNALDTVRGSGLRADDLATRLAALGPELTKLNQGAGQHGVAETLQRADQVLRDAEGVRAEAERLPERAAEIDKRLVSLRTRAQALANRASSVDPVLSELRRRFSVACWQDLQHVPEQAAKSVRQAEGKIEEAAKARQEQRWPDATALLSTVRALLNGADEAVSAAGDRLSRLNAVSKDPEVEIQRTRFAIRDAQRLAMAGRNTPDPRHARPLDDSVARLERAIAGLEGRHPDYWHFLTETEAVRATVARAVEMIREDRGGGH
>NZ_CP034279.1|WP_156694594.1|5147574_5148339_-|DUF4097-family-beta-strand-repeat-protein
MGAGRVRAFVVGGVVLGALGLAGCGDAGVEGAPVERKAFGFRGESLVVEAGDSELVLVPADVKDVEVSRQVDGWVVFGEGPDPVWKLEGDRLTLRVECDALASRCGARHEVRVPRGVAVTVEGDNGDVTAEGFETALKVTVDNGGVTVRDGRGPLELRSENGDVRVEGGTARSVVTSSGNGEIRLALGAVPERVEAVNDNGDITVELPGGATRYAVEAGSDNGEVKVGVPTDERSGHVVKARSDNGQVTVRSAN
>NZ_CP034279.1|WP_156694595.1|5148691_5149822_-|tyrosine-type-recombinase/integrase
MANGKGRKRRFGSVRKLPSGRFQARYRGPDGQLRAAPQTFATQTDADRWLVRKEAEIIEGRWQNPDDKIPFGAYADAWFKERDYAATTRERNGSALRLHILPTFRDVNVGDITTPQIRRWRAGLLDSGVGEPTVVKAYQILRAIMHTAVDDGLIQRNPCRIKGAGATKTAERPFLTVAEVFRLADVVPERYRALILLAAFTSLRFGELAALQRHDVDLERRVVSVRRAAAETRTDGLLIKTPKSAAGIRTVAFPASLGEELQAHLSEYSQAGRNGLVFVGPRGGMLRRNNFRRIWLRALAQAGLGDVHFHDLRHTGNTLAATGGATTRELMHRMGHSSVRAALIYQHLVNGRDHKIADHVDRQIRKVQDRNGPSGT
>NZ_CP034279.1|WP_156694596.1|5149821_5150037_-|excisionase-family-DNA-binding-protein
MKDRLMSVAEVAEYLGTTERFPRRLIAERRIVFVKVGRHVRIPESALESFVLANTVSPISPGRGTAYKAVA
>NZ_CP034279.1|WP_156694597.1|5150033_5151434_-|replication-initiation-protein
MTDTATAAGLDPATLSDLLRVAGSPGFDRLTEQIRRTGGCAAPIRLSGGTKLIDPATKTVLHAYTTDNEPGGVLRVACGNRRASRCPACAWTYAGDTYHLIRAGLVGAPDKGTPDTIRDHPRVFATLTAPSFGPVHNRPGNRRCRCGTRHPEDAPELGTPLDPETYDYAGAVLWNNHASELWRYFTIYLRREVARRAGLTQKAAREQSRVSFGKVAEYQKRGAVHFHAVIRFDGPEGPDTPPPAWATLDLLTDAIRAAAARVEVSVPAAPEHGVDQDLVLRWGDQLDVQPIGAFGQGEELTEQAVAAYVAKYATKAAETTGTVDHPVGNKEALVLLGVPDHPRRLMEACMDLDAAYPDRRLRAWAHMLGFRGHFSTKSRRYSTTLGALRQVRADYRAAQQRTALGLPDPDEHPEATVLTVAHWAYAGHGSTPGESWLAANVRRDIQHNREHAREIRAELDLEGAAA

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Crispr_ID: NZ_CP034279_11

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP034279_11

6211014-6211125

Orphan

Consensus_repeat	Method
GGTGCGACGGACGGGGCCGGTGCGGCAGGCGGGGTCGGTG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP034279_11

>merge|NZ_CP034279|11|6211014-6211125|CRISPRCasFinder
GGTGCGGGTGCGCTGGTGGGTGCGACGGACGGGGCCGGTGCGGCAGGCGGGGTCGGTGCGACGGACAGGGCCGGTGCGGCAGGCGGGGCCGGTGCGTCGGACGGGGCCGGTG

>NZ_CP034279|11|11|6211014-6211125|CRISPRCasFinder
GGTGCGGGTGCGCTGGTGGGTGCGACGGACGGGGCCGGTG	CGGCAGGCGGGGTCGGTGCGACGGACAGGGCC
GGTGCGGCAGGCGGGGCCGGTGCGTCGGACGGGGCCGGTG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP034279.1\|WP_156695432.1\|6215621_6216743_+\|glycosyltransferase	unknown	unknown	gnl\|CDD\|340842
NZ_CP034279.1\|WP_156695427.1\|6207666_6208434_-\|glycerophosphodiester-phosphodiesterase	unknown	unknown	gnl\|CDD\|176504
NZ_CP034279.1\|WP_156695422.1\|6201410_6201851_+\|AsnC-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|214628
NZ_CP034279.1\|WP_156695424.1\|6204038_6204848_+\|glycosyltransferase	unknown	unknown	gnl\|CDD\|133062
NZ_CP034279.1\|WP_156695429.1\|6209256_6210759_+\|aminotransferase-class-I/II-fold-pyridoxal-phosphate-dependent-enzyme	unknown	unknown	gnl\|CDD\|224089
NZ_CP034279.1\|WP_156695437.1\|6223397_6224024_-\|5-oxoprolinase-subunit-PxpB	unknown	unknown	gnl\|CDD\|367142
NZ_CP034279.1\|WP_156695426.1\|6206253_6207621_-\|MFS-transporter	unknown	unknown	gnl\|CDD\|341035
NZ_CP034279.1\|WP_156695435.1\|6218948_6222554_+\|5-oxoprolinase	unknown	unknown	gnl\|CDD\|215358
NZ_CP034279.1\|WP_156695431.1\|6213929_6215348_+\|HEAT-repeat-domain-containing-protein	unknown	unknown	unknown
NZ_CP034279.1\|WP_156695436.1\|6222504_6223401_-\|5-oxoprolinase/urea-amidolyase-family-protein	unknown	unknown	gnl\|CDD\|376868
NZ_CP034279.1\|WP_156695421.1\|6200808_6201207_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP034279.1\|WP_156695428.1\|6208430_6209153_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|225239
NZ_CP034279.1\|WP_156695434.1\|6217896_6218952_+\|SGNH/GDSL-hydrolase-family-protein	unknown	unknown	gnl\|CDD\|238870
NZ_CP034279.1\|WP_156695438.1\|6224020_6224785_-\|5-oxoprolinase-subunit-PxpA	unknown	unknown	gnl\|CDD\|377121
NZ_CP034279.1\|WP_156695425.1\|6204894_6205500_+\|FxsA-family-protein	unknown	unknown	gnl\|CDD\|377238
NZ_CP034279.1\|WP_156695423.1\|6201873_6203499_+\|amidohydrolase-family-protein	unknown	unknown	gnl\|CDD\|238625
NZ_CP034279.1\|WP_156695430.1\|6213286_6213679_+\|ankyrin-repeat-domain-containing-protein	unknown	unknown	gnl\|CDD\|293786
NZ_CP034279.1\|WP_073757949.1\|6212750_6212945_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP034279.1\|WP_026278069.1\|6205623_6205998_-\|RNA-polymerase-binding-protein-RbpA	unknown	unknown	gnl\|CDD\|379162
NZ_CP034279.1\|WP_156695433.1\|6216739_6217900_+\|glycosyltransferase	unknown	unknown	gnl\|CDD\|340842

Protein	Function_ID	Function_description	E-value
NZ_CP034279.1\|WP_156695427.1\|6207666_6208434_-\|glycerophosphodiester-phosphodiesterase	gnl\|CDD\|176504	cd08561, GDPD_cytoplasmic_ScUgpQ2_like, Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic phosphodiesterases UgpQ2 and similar proteins. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of uncharacterized cytoplasmic phosphodiesterases which predominantly exist in bacteria. The prototype of this family is a putative cytoplasmic phosphodiesterase encoded by gene ulpQ2 (SCO1419) in the Streptomyces coelicolor genome. It is distantly related to the Escherichia coli cytoplasmic phosphodiesterases UgpQ that catalyzes the hydrolysis of glycerophosphodiesters at the inner side of the cytoplasmic membrane to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols.	1.11352e-83
NZ_CP034279.1\|WP_156695422.1\|6201410_6201851_+\|AsnC-family-transcriptional-regulator	gnl\|CDD\|214628	smart00344, HTH_ASNC, helix_turn_helix ASNC type. AsnC: an autogenously regulated activator of asparagine synthetase A transcription in Escherichia coli).	1.32662e-42
NZ_CP034279.1\|WP_156695424.1\|6204038_6204848_+\|glycosyltransferase	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.	5.81611e-98
NZ_CP034279.1\|WP_156695429.1\|6209256_6210759_+\|aminotransferase-class-I/II-fold-pyridoxal-phosphate-dependent-enzyme	gnl\|CDD\|224089	COG1167, ARO8, Transcriptional regulators containing a DNA-binding HTH domain and an aminotransferase domain (MocR family) and their eukaryotic orthologs [Transcription / Amino acid transport and metabolism].	7.33835e-87
NZ_CP034279.1\|WP_156695437.1\|6223397_6224024_-\|5-oxoprolinase-subunit-PxpB	gnl\|CDD\|367142	pfam02682, CT_C_D, Carboxyltransferase domain, subdomain C and D. Urea carboxylase (UC) catalyzes a two-step, ATP- and biotin-dependent carboxylation reaction of urea. It is composed of biotin carboxylase (BC), carboxyltransferase (CT), and biotin carboxyl carrier protein (BCCP) domains. The CT domain of UC consists of four subdomains, named A, B, C and D. This domain covers the C and D subdomains of the CT domain. This domain covers the whole length of kipI (kinase A inhibitor) from Bacillus subtilis. It can also be found in S. cerevisiae urea amidolyase Dur1,2, which is a multifunctional biotin-dependent enzyme with domains for urea carboxylase and allophanate (urea carboxylate) hydrolase activity.	3.09847e-70
NZ_CP034279.1\|WP_156695426.1\|6206253_6207621_-\|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.	4.11275e-139
NZ_CP034279.1\|WP_156695435.1\|6218948_6222554_+\|5-oxoprolinase	gnl\|CDD\|215358	PLN02666, PLN02666, 5-oxoprolinase.	0
NZ_CP034279.1\|WP_156695436.1\|6222504_6223401_-\|5-oxoprolinase/urea-amidolyase-family-protein	gnl\|CDD\|376868	pfam02626, CT_A_B, Carboxyltransferase domain, subdomain A and B. Urea carboxylase (UC) catalyzes a two-step, ATP- and biotin-dependent carboxylation reaction of urea. It is composed of biotin carboxylase (BC), carboxyltransferase (CT), and biotin carboxyl carrier protein (BCCP) domains. The CT domain of UC consists of four subdomains, named A, B, C and D. This domain covers the A and B subdomains of the CT domain. This domain covers the whole length of KipA (kinase A) from Bacillus subtilis. It can also be found in S. cerevisiae urea amidolyase Dur1,2, which is a multifunctional biotin-dependent enzyme with domains for urea carboxylase and allophanate (urea carboxylate) hydrolase activity.	8.01596e-109
NZ_CP034279.1\|WP_156695432.1\|6215621_6216743_+\|glycosyltransferase	gnl\|CDD\|340842	cd03814, GT4-like, glycosyltransferase family 4 proteins. This family is most closely related to the GT4 family of glycosyltransferases and includes a sequence annotated as alpha-D-mannose-alpha(1-6)phosphatidyl myo-inositol monomannoside transferase from Bacillus halodurans. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.	2.05059e-109
NZ_CP034279.1\|WP_156695428.1\|6208430_6209153_-\|hypothetical-protein	gnl\|CDD\|225239	COG2364, COG2364, Predicted membrane protein [Function unknown].	1.99252e-41
NZ_CP034279.1\|WP_156695434.1\|6217896_6218952_+\|SGNH/GDSL-hydrolase-family-protein	gnl\|CDD\|238870	cd01832, SGNH_hydrolase_like_1, Members of the SGNH-hydrolase superfamily, 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 from other serine hydrolases, but may lack the carboxlic acid. Myxobacterial members of this subfamily have been reported to be involved in adventurous gliding motility.	2.8376e-41
NZ_CP034279.1\|WP_156695438.1\|6224020_6224785_-\|5-oxoprolinase-subunit-PxpA	gnl\|CDD\|377121	pfam03746, LamB_YcsF, LamB/YcsF family. This family includes LamB. The lam locus of Aspergillus nidulans consists of two divergently transcribed genes, lamA and lamB, involved in the utilisation of lactams such as 2-pyrrolidinone. Both genes are under the control of the positive regulatory gene amdR and are subject to carbon and nitrogen metabolite repression. The exact molecular function of the proteins in this family is unknown.	1.48466e-134
NZ_CP034279.1\|WP_156695425.1\|6204894_6205500_+\|FxsA-family-protein	gnl\|CDD\|377238	pfam04186, FxsA, FxsA cytoplasmic membrane protein. This is a bacterial family of cytoplasmic membrane proteins. It includes two transmembrane regions. The molecular function of FxsA is unknown, but in Escherichia coli its over-expression has been shown to alleviate the exclusion of phage T7 in those cells with an F plasmid.	7.53749e-28
NZ_CP034279.1\|WP_156695423.1\|6201873_6203499_+\|amidohydrolase-family-protein	gnl\|CDD\|238625	cd01300, YtcJ_like, YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. The Arabidopsis homolog LAF3 has been identified as a factor required for photochrome A signalling.	1.34056e-108
NZ_CP034279.1\|WP_156695430.1\|6213286_6213679_+\|ankyrin-repeat-domain-containing-protein	gnl\|CDD\|293786	sd00045, ANK, ankyrin repeats. Ankyrin repeats are one of the most abundant repeat motifs, and generally function as scaffolds for protein-protein interactions in processes including cell cycle, transcriptional regulation, signal transduction, vesicular trafficking, and inflammatory response. Although predominantly found in eukaryotic proteins, they are also found in some bacterial and viral proteins. Less is known of their physiological roles in prokaryotes. Some bacterial ANK proteins play key roles in microbial pathogenesis by mimicking or manipulating host function(s). The pathogen Providencia alcalifaciens N-formyltransferase ankyrin repeats function in small molecule binding and allosteric control. Ankyrin-repeat proteins have been associated with a number of human diseases.	4.89479e-15
NZ_CP034279.1\|WP_026278069.1\|6205623_6205998_-\|RNA-polymerase-binding-protein-RbpA	gnl\|CDD\|379162	pfam13397, RbpA, RNA polymerase-binding protein. RbpA is a family bacterial RNA polymerase-binding proteins. RbpA acts as a transcription factor by binding to the sigma subunit of RNA polymerase.	1.69538e-50
NZ_CP034279.1\|WP_156695433.1\|6216739_6217900_+\|glycosyltransferase	gnl\|CDD\|340842	cd03814, GT4-like, glycosyltransferase family 4 proteins. This family is most closely related to the GT4 family of glycosyltransferases and includes a sequence annotated as alpha-D-mannose-alpha(1-6)phosphatidyl myo-inositol monomannoside transferase from Bacillus halodurans. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.	5.30214e-64

>NZ_CP034279.1|WP_156695429.1|6209256_6210759_+|aminotransferase-class-I/II-fold-pyridoxal-phosphate-dependent-enzyme
MAEWTSAVGPAQLARQLNAQQPRPAGPGTRKPPAYRALADGIRLLVLEGRVPVAARLPAERELALALSVSRTTVAAAYEALRAEGFLESRRGAGSWTAVPAGNPLPARGLEPLPPEALGSMIDLGCASLPAPEPWLTRGFQGALEELPPYAHTHGDYPAGLPALRQMLADRYTRRGIPTMPEQIMVTTGAMGAIDAICHLFAGRGERIAVESPSYANILQLMREAGARLVPVAMSEGLEGWDLTRWRQVLRDAAPRLAYVVADFHNPTGALADEDRRRALVDASRSAGTVLVVDETMTELYLEEGLDMPRPVCAFDPAGSTVLTVGSASKAFWAGMRIGWVRAAPDVIRSLVAARAYADLGTPVLEQLGVDWLMRTGGWEEAVALRREQARENRDALVAAVRRELPDWEFEVPRGGLTLWVRTGGLSGSRLAEVGERVGVRVPSGPRFGVDGAFEGYVRLPFTVAGPVADEAAVRLAAATRLVRAGASSGSGESPRTFVA
>NZ_CP034279.1|WP_156695428.1|6208430_6209153_-|hypothetical-protein
MSTTSSTPDTEEATRPASPGPAAARLPRHLPRRLFQLYFGLTLYGVSSAMLVRSGLGLEPWNVLHQGLAERTGLSMGVVLTVLGALILLLWIPLRQKPGLGTVSNVLVIGAAMDGALWLLPDAHGWPAQVLLMAGGVVLNGVATGLYIAARFGPGPRDGLMTGLHRRTGRSIRLIRTTIEVTVVVTGFLLGGSLGVGTVLYALAIGPLAQFFLRVFAVPGQDGGSTVVASRKPGQVILRR
>NZ_CP034279.1|WP_156695427.1|6207666_6208434_-|glycerophosphodiester-phosphodiesterase
MTRVRHPYLDHPSSPIPFAHRGGAADGLENTATAFRRAAAAGYRYFETDVHTTADGRLVAFHDATLDRVTDSRGRIQDLPWSAVRHARVAGTEPLPLFEELMEEFPDARWNVDVKAEPALRPLVETIRRANAWDRVCVGSFNEGRVVRAHRLGGDRLATSYGVRGVLALRLRSYGIPAALRTGAVAAQVPEAQNGVRVVDRRFVRAAHERGLQVHVWTVNDPERMAALLDLGVDGIMTDHLETLRTVLTDRGVWV
>NZ_CP034279.1|WP_156695426.1|6206253_6207621_-|MFS-transporter
MSDAEDARTDDRAAGGATAAERRREQRGWYFYDFACSVYSTSVLTVFVGPYLTSVARAAADADGFVHPLGIPVRAGSVFPYAVSASLVLAVLVMPLAGAAADRTGRKKPLLAVSAYVGAAATAGMFFLDGDRYLLGALLLIVANAALAVSMVLYNAYLPQIATPEERDAVSSRGWAFGYTSGALVLVLDLVLYTGHASFGLSEQEAVRICLASAGLWWGAFTLVPLRRLRDRRVRPGGEGAAGSGWRQLVATLRDMRRHPLTLSFLLAYLVYNDGVQTVISQASIYGSEELGLEQSTLITAVLLVQVLAVAGALGMGRLARLYGAQRTILASLAVWTLILVAGYLLPAGEPVWFYALAAAIGLVLGGSQALSRSLFSHLVPPGKEAEYFSAYEMSDRGLSWLGPLVFGLGYQLTGSYRDAIISLVIFFAAGFVLLARVPVRKAVAAAGNPVPDRI
>NZ_CP034279.1|WP_026278069.1|6205623_6205998_-|RNA-polymerase-binding-protein-RbpA
MSERALRGTRLVVTSYETDRGIDLAPRQAVEYACEKGHRFEMPFSVEAEIPPEWECKVCGSQALLVDGDGPEEKKGKPARTHWDMLMERRTREELEEVLAERLAVLRSGAMNIAVHPRDSRKSA
>NZ_CP034279.1|WP_156695425.1|6204894_6205500_+|FxsA-family-protein
MTTGSPPPTDRKPRSRARSLVPVGVAAWLVLEVWLLTLVAGAAGGLTVLALLVGGAVLGGAVIKRAGRRAFRTLTETLQQQQSGAPSASAGGTDRASAGNGFLMLGGLLLMLPGLISDALGLLLLVPPVRAMAGRYAERTLERRMRAAMPGYGPLGDAFQQAQQARMHRPDGKVVQGEVIRDDTHGRAAYDDEGPRPPLTR
>NZ_CP034279.1|WP_156695424.1|6204038_6204848_+|glycosyltransferase
MNDGGQRRYGPLGRALVIIPTYNEAENIKPIVSRVRAAVPDVDVLVADDNSPDGTGKLADELAAEDDHVHVLHRKGKEGLGAAYLAGFRWGIEHDYGVLVEMDADGSHQPEELPRLLTALKGADLVLGSRWVPGGRVVNWPKSREFLSRGGSTYSRLLLDVPIRDVTGGFRAFRKETLEGLGLDEVASQGYCFQVDLARRAVAAGYHVVEVPITFVERELGDSKMSRDIVVEALWRVTAWGVGSRAERLLGRRPSGPRAAGPAGPADRS
>NZ_CP034279.1|WP_156695423.1|6201873_6203499_+|amidohydrolase-family-protein
MTESEHRTVLLRGGDVHSPADPFATAMVVERGHVAWVGSEGAADAFAAGVDEVIDLEGALVTPAFTDAHVHTTATGLALTGLDLSGARTLAEALERVRAHSAARPADQVLLGHGWDAARWPESRPPSRAELDEATGGRPLYLPRVDVHSAVVTTALLDRVPGVTGLPGYHPDQPLTAAAHHAVRAAAHAAVTPRQRAEAQRAALARAASLGIGTVHECAGPEISDEDDFTGLLALAAEEAGPRVVGYWAEAVSGEKDARRIRELGAIGAAGDLFADGSLGSHTACLHEPYADAPHTGTAHLDAAAVAAHVTACTEAGLQAGFHAIGDAAVSAVVEGVRAAAETVGLARVRAARHRVEHAEMLTPETVAAFAELALTASVQPAFDAAWGGEDGMYAQRLGAERARTLNPYAALLRAGVPLAFGSDSPVTPLDPWGTVRAAAFHRTPEHRISVRAAFTAHTRGGWRATGRDDAGVLVPGAPADYAVWRADELVVQAPDDRVARWSTDPRSGTPGLPDLTPGADLPVCLRTVVSGRTVFVRPNE
>NZ_CP034279.1|WP_156695422.1|6201410_6201851_+|AsnC-family-transcriptional-regulator
MEELDRQIVELLVKDGRMSYTDLGKATGLSTSAVHQRVRRLEQRGVIRGYAAVVDPEAVGLPLTAFISVKPFDPSAPDDIADRLADISEIEACHSVAGEENYILKVRVATPLELEHLLTRIRSQSGVSTRTTVVLSTPYEARPPRV
>NZ_CP034279.1|WP_156695421.1|6200808_6201207_-|hypothetical-protein
MQEPVDSVGSHVDDELDAYDTFEMVRVICPDCSQPIALLADEDALPEHALCPTPWNPFVLTVCSGTGRAAAEARPADESLELQEQDTALLLTLPQGLDWRTQPFSHVGGPGSRPLKMPRPSGRRMPPMRRAA
>NZ_CP034279.1|WP_073757949.1|6212750_6212945_-|hypothetical-protein
MILSISGVVLLGIIVFLFFRKDGLKASHALVCALFGFYLAGTAIAPSITAGGASLASLLGGIKF
>NZ_CP034279.1|WP_156695430.1|6213286_6213679_+|ankyrin-repeat-domain-containing-protein
MSETPDPEVIELASKVFDLARQGDAEALAAYVDAGVPANLTNDKGDCLVMLAAYHGNEDAVTALLARGADPNRVNDRGQTPIAGAVFKGEDGVVRALLAAGADPEAGTPSAVDTARMFGKTHLLELFASR
>NZ_CP034279.1|WP_156695431.1|6213929_6215348_+|HEAT-repeat-domain-containing-protein
MFDPVIAPSGTLLGLLQRGRGDGTLHALAAPRAEALAALNHCVLSDPRQDWQVENRSLYYARLYLDLHGGLEEIEAHLFGADDVLDTEESRTGLALAVLGHLAAYGREDALALLRRYAATGSNWAWALDELALRDDDSGLRGLAAPILARFPATPEGDAELAAAVRDAFEPRPWRLWAEDRRETIGARVRAAREQGSFDRWQRQLRPTGPRPGWSVQAVFEWAQEGLDRGSPLHVPAARCLTAVAGPDDRPLIVEAARGGPDGARCAALHYLAEARDPAVLDLIEAAAVSDSRIVAEAAVAAFERMCGDAAVDRARGWVHRPDPLGASAAGVLACRGDARDATLVLGALREAVRSDGPDAPSLYTLVDGTGRLEVACAAPVLRHIYRETASSQLRGRTARALAATDPSFATGFAVECLWDCEETTREIAALHAETGDVRVAERLRRLAADPAEEDEVQSAVRSRIGPDLPKV
>NZ_CP034279.1|WP_156695432.1|6215621_6216743_+|glycosyltransferase
MRVVIVTESFPPDVNGVAHCALQTARHLAARGHDPLVLAPAVPAGTPDGDAPCPVVRIPSLPLPGYPQVRVALPSRRVAAAIAAHRADLVHLASPFVLGVRGMTVAARLGLPAVAVYQTDLAGYARTYVGAGESAAWRRLRAVHGAADRTLAPSTAAVRDLERHGVARVRLWPRGVDTRRFRPGLRDEALRRELAPGGELLVGYVGRLAPEKRVELLAGVCGLPGVRVVVVGDGPSEGALRAALPGAVFLGRRTGGDLARIFASLDVFVHTGPHETFCQTVQEAMAGGVPVVAPAAGGPLDLVDHGRTGLLVAPHDPDAVRTAVSALAGDPDLRAAYGRTARATVEGRTWAVVGDQLIDHYGEVLRQRTAVAA
>NZ_CP034279.1|WP_156695433.1|6216739_6217900_+|glycosyltransferase
MSLRIVRLANFVTPSSGGLRTALDELGRGYLAAGHEPVLVTPGERESDRLTLQGRVITLPGPALPGTGGYRVLADRGRLRRLLEEIGPDRLEVSDRTTLRWTGEWARRARVPAVMVSHETAHGVLRTWGVPARPAALTADRLNRLSAWAYTRIVCTTEWAEREFVRIGARNVVRAPLGVDLIRYRPQRRRPALRARYAPGADVMLLLCSRLSVEKRPALALDTLAELRARGVRAALVVAGDGPLRGGLERRARGLDVRFLGHVPDREEVAALQATADVCLAPGPAETFGLSALEALACGTPVVASATSALPEVVGDAGAAAEDTPAAFADAVARLLARPEGHRRAEARARAELFGWDRSVAAFLAAHDAPVRSARAPGPSGAEVPA
>NZ_CP034279.1|WP_156695434.1|6217896_6218952_+|SGNH/GDSL-hydrolase-family-protein
MSATVEAPLDGGPLRRKLHARVAPAGGADVPAERATGVRRFAALGDSLTAGVGDPVAGGWRGWAALLADALAAAPDADAVVPSGAGPGADAVAPGGEGAVEFRNLAVCGARARDVAETQLPLALAYRPDVASVVVGVNDTLRSSFDITGFALALDGVCARLAAQGALLLTACLPDPGAVLGLPPPLARPLARRQRQVNAVVHALSARYGAVHLHMADAAWVADRSLWSADRLHPGERGHRTIAARFHALLAERGLAGGAAPAREPGQPPPSRADTLLWLATAGTGWVARRCHDLLPQLLRLAGTEVRHWARGTGARLDLSAEQSLAAALAVVSGPRAVPVPVRASAATMGA
>NZ_CP034279.1|WP_156695435.1|6218948_6222554_+|5-oxoprolinase
MTGRWEFWIDRGGTFTDVVARRPDGRLVTRKLLSHDPDRYRDAAVAGIRLVLGLAADEPVPADRIASVKMGTTVATNALLERRGEPTVLLITEGFRDALRIAYQNRPRIFDRRILLPEAVYERVVEVPERVDARGTVVRPLDLAAVGGLLKAAHGDGFRSAAVVLMHGYAHPGHEVRVAEAARDAGFTQVSCSHEVSPLIKLVPRGDTTVVDAYLSPILRRYVDEVAGELRGVRLMFMQSNGGLREAAHFRGKDAVLSGPAGGVVGMARTSEQAGHRRVIGFDMGGTSTDVSHYAGAFERELGTQVAGVRMRAPMMSIHTVAAGGGSVLHFDGQRYRVGPDSAGADPGPACYRRGGPLTVTDANVMLGRVQPAHFPAVFGPGGDLPLDAEVVRDRFTALAEEVRRHTGTTRSPEEVAAGFLEIAVLNMANAVKKISVQRGHDVTRYALTSFGGAGGQHACAVADALGVDTVLVPPLAGVLSAYGIGLADATAMREQSVEAELDGDVHARVEGICDRLARRTRDELRADGLPDSAISTHARVLVRYAGTDATLPVTLAPAGDMAEEFTAAHRARYGFTMDKPLVVEAVSVEATGRAGAPGPPGAGQPPGKGPPRPRATVAMFVDGERRDTPLYRREDLRPADTVPGPAVVAEADATTVVDDGWQAVATDSGHLLLTRARPRPGRSAVGTDVDPVLLEVFNNLFMAIAEQMGVRLENTAHSVNIKERLDFSCALFDADGNLIANAPHIPVHLGSMGESIKEVLRRNEGAMRPGDVYAINDPYHGGTHLPDVTVVTPVFGPSGDLRFLVASRGHHAEIGGITPGSMPAFSSSVDEEGVLFDNWLLVRDGRLREAETRRLLTEAPHPSRDPDTNLADLRAQIAANEKGIEELDHMVDQFGLDVVHAYMRHVRNNAEESVRRIVATLRDGSCRYETDGGPVIQVAVRVDRERRGAVLDFTGTSPQQPGNVNAPTSVVMAAVLYVFRTLVDDDIPLNSGCLEPLDVRVPDGSMLAPAHPAATVAGNVETSQAVTGALYAALGVQAEGSGTMNNVTFGNDRVQYYETVASGSGAGDGFPGADAVQTHMTNSRLTDPEVLEWRHPVRVDAFAVRDGSGGAGRWRGGEGVVRRIRFLEPMTVALLTGHRRIAPYGMAGGAPGALGENAVERADSTVRRLAGVDVVDVGPGDVLVVTTPGGGGYGTPAAPG
>NZ_CP034279.1|WP_156695436.1|6222504_6223401_-|5-oxoprolinase/urea-amidolyase-family-protein
MTDRALAVVRAGALTTVQDGGRPGYAHLGVPRSGALDPGARDLANRLVGNPADAAVLETTVDGCAVRPRCAVTVAVGGAPCPVTVDGRPASWGAAVRVPAGAVLAVGAAVRGLRSYVAFAGGVAAEPVLGSRSTDLLSGLGPAPLRDGAVLPLGPEPPAPPGHDAVPWPGPPGELVLHVRPGPRDDWFTARALSAFATRAYRVSPASNRIGLRTEGPPLERAVAGELPSEGMVLGAVQVPPDGRPVVFLADHPTTGGYPVVAVVRERDLAAAAQAVPGTPVRFIPVRQASRSRRPRGW
>NZ_CP034279.1|WP_156695437.1|6223397_6224024_-|5-oxoprolinase-subunit-PxpB
MRTLPVGDRALLVEFGSGEETEAFHAELLRRRAAGALPAVTEVVPAARTVLLDGVEAPERLAALVAGWEIEPLHARVDPVVEIPVRYDGPDLPDVAALWGVPPADVATVHSAAEFRVAFCGFAPGFGYLTGLPEAYEVPRRATPRTAVPAGAVAMAGPYTGVYPRSSPGGWQLIGTTDAVLWDPAREPAALLSPGTRVRFVPRGVGAR
>NZ_CP034279.1|WP_156695438.1|6224020_6224785_-|5-oxoprolinase-subunit-PxpA
MTWASIDLNADLGEGFGRWRLTDDEQLLSVVTSANVACGFHAGDAATMRRVCALAAERGVRIGAQVSYRDLAGFGRRSMDVPYEELAAEVAYQIGALEVFARAAGARVSYVKPHGALYNRVVHDDGQAQAVVDGVLLTGERLPLLGLPGSRLHEVAEKAGLPVVTEAFADRAYTAAGTLVPRGEEGAVITDAAAVVERSVAMARFGTVTSRCGRPVAVRARSLCLHGDTPGAVGLARRVRHQLEASGVRVGAFV

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Crispr_ID: NZ_CP034279_12

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP034279_12

6721085-6721182

Orphan

Consensus_repeat	Method
GCGGGACGATTGCCCACAACGGG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP034279_12

>merge|NZ_CP034279|12|6721085-6721182|CRISPRCasFinder
GCGGGACGATTGCCCACAACGGGGGGAGCGGCCCTGCGGGACGATTGCCCACAACGGGGGGTGGGGAGCCGCTCCGCGGGACGATTGCCCACAACGGG

>NZ_CP034279|12|12|6721085-6721182|CRISPRCasFinder
GCGGGACGATTGCCCACAACGGG	GGGAGCGGCCCTGCGGGACGATTGCCCACAACGGGGGGTGGGGAGCCGCTCC
GCGGGACGATTGCCCACAACGGG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP034279.1\|WP_156695829.1\|6712420_6714928_+\|SpoIIE-family-protein-phosphatase	unknown	unknown	gnl\|CDD\|369272
NZ_CP034279.1\|WP_156696672.1\|6711311_6712154_-\|SIS-domain-containing-protein	unknown	unknown	gnl\|CDD\|224651
NZ_CP034279.1\|WP_156695840.1\|6728947_6730042_-\|glutamate--cysteine-ligase	unknown	unknown	gnl\|CDD\|237408
NZ_CP034279.1\|WP_156695835.1\|6722607_6723279_-\|SIS-domain-containing-protein	unknown	unknown	gnl\|CDD\|240139
NZ_CP034279.1\|WP_156695830.1\|6714987_6717357_+\|SpoIIE-family-protein-phosphatase	unknown	unknown	gnl\|CDD\|369272
NZ_CP034279.1\|WP_156695827.1\|6709318_6710317_-\|glycosyltransferase	unknown	unknown	gnl\|CDD\|133030
NZ_CP034279.1\|WP_156695832.1\|6718471_6719206_-\|SDR-family-NAD(P)-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|212491
NZ_CP034279.1\|WP_156695837.1\|6724813_6725779_-\|glycosyltransferase	unknown	unknown	gnl\|CDD\|340831
NZ_CP034279.1\|WP_156695831.1\|6717432_6718470_+\|DNA-topoisomerase-IB	unknown	unknown	gnl\|CDD\|226099
NZ_CP034279.1\|WP_156695836.1\|6723413_6724817_-\|glycosyltransferase	unknown	unknown	gnl\|CDD\|340830
NZ_CP034279.1\|WP_156695834.1\|6721207_6722611_-\|D-glycero-beta-D-manno-heptose-1-phosphate-adenylyltransferase	unknown	unknown	gnl\|CDD\|225425
NZ_CP034279.1\|WP_156695838.1\|6725795_6727463_-\|carbamoyltransferase	unknown	unknown	gnl\|CDD\|225103
NZ_CP034279.1\|WP_156695833.1\|6719400_6720804_+\|MFS-transporter	unknown	unknown	gnl\|CDD\|340863
NZ_CP034279.1\|WP_156695839.1\|6727515_6728484_-\|NAD-dependent-epimerase/dehydratase-family-protein	unknown	unknown	gnl\|CDD\|187541
NZ_CP034279.1\|WP_156695828.1\|6710754_6711009_+\|DUF5133-domain-containing-protein	unknown	unknown	gnl\|CDD\|375043
NZ_CP034279.1\|WP_156695842.1\|6731087_6732095_-\|glycosyltransferase-family-9-protein	unknown	unknown	gnl\|CDD\|340821
NZ_CP034279.1\|WP_156695841.1\|6730137_6731091_-\|glycosyltransferase-family-9-protein	unknown	unknown	gnl\|CDD\|340821
NZ_CP034279.1\|WP_156695825.1\|6707365_6708880_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP034279.1\|WP_156695826.1\|6708854_6709322_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|377229
NZ_CP034279.1\|WP_167536489.1\|6732091_6732658_-\|HAD-IIIA-family-hydrolase	unknown	unknown	gnl\|CDD\|319806

Protein	Function_ID	Function_description	E-value
NZ_CP034279.1\|WP_156695829.1\|6712420_6714928_+\|SpoIIE-family-protein-phosphatase	gnl\|CDD\|369272	pfam07228, SpoIIE, Stage II sporulation protein E (SpoIIE). This family contains a number of bacterial stage II sporulation E proteins (EC:3.1.3.16). These are required for formation of a normal polar septum during sporulation. The N-terminal region is hydrophobic and is expected to contain up to 12 membrane-spanning segments.	2.53616e-52
NZ_CP034279.1\|WP_156696672.1\|6711311_6712154_-\|SIS-domain-containing-protein	gnl\|CDD\|224651	COG1737, RpiR, Transcriptional regulators [Transcription].	1.28722e-38
NZ_CP034279.1\|WP_156695840.1\|6728947_6730042_-\|glutamate--cysteine-ligase	gnl\|CDD\|237408	PRK13517, PRK13517, glutamate--cysteine ligase.	1.9857e-133
NZ_CP034279.1\|WP_156695835.1\|6722607_6723279_-\|SIS-domain-containing-protein	gnl\|CDD\|240139	cd05006, SIS_GmhA, Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose isomerase catalyzes the isomerization of sedoheptulose 7-phosphate into D-glycero-D-mannoheptose 7-phosphate. This is the first step of the biosynthesis of gram-negative bacteria inner core lipopolysaccharide precursor, L-glycero-D-mannoheptose (Gmh).	4.59042e-66
NZ_CP034279.1\|WP_156695830.1\|6714987_6717357_+\|SpoIIE-family-protein-phosphatase	gnl\|CDD\|369272	pfam07228, SpoIIE, Stage II sporulation protein E (SpoIIE). This family contains a number of bacterial stage II sporulation E proteins (EC:3.1.3.16). These are required for formation of a normal polar septum during sporulation. The N-terminal region is hydrophobic and is expected to contain up to 12 membrane-spanning segments.	2.24175e-49
NZ_CP034279.1\|WP_156695827.1\|6709318_6710317_-\|glycosyltransferase	gnl\|CDD\|133030	cd04187, DPM1_like_bac, Bacterial DPM1_like enzymes are related to eukaryotic DPM1. A family of bacterial enzymes related to eukaryotic DPM1; Although the mechanism of eukaryotic enzyme is well studied, the mechanism of the bacterial enzymes is not well understood. The eukaryotic DPM1 is the catalytic subunit of eukaryotic Dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. The enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. This protein family belongs to Glycosyltransferase 2 superfamily.	3.18304e-83
NZ_CP034279.1\|WP_156695832.1\|6718471_6719206_-\|SDR-family-NAD(P)-dependent-oxidoreductase	gnl\|CDD\|212491	cd05233, SDR_c, classical (c) SDRs. 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 prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, 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.	7.31431e-52
NZ_CP034279.1\|WP_156695837.1\|6724813_6725779_-\|glycosyltransferase	gnl\|CDD\|340831	cd03801, GT4_PimA-like, phosphatidyl-myo-inositol mannosyltransferase. This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.	1.51645e-11
NZ_CP034279.1\|WP_156695831.1\|6717432_6718470_+\|DNA-topoisomerase-IB	gnl\|CDD\|226099	COG3569, COG3569, Topoisomerase IB [DNA replication, recombination, and repair].	2.76801e-63
NZ_CP034279.1\|WP_156695836.1\|6723413_6724817_-\|glycosyltransferase	gnl\|CDD\|340830	cd03800, GT4_sucrose_synthase, sucrose-phosphate synthase and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. The sucrose-phosphate synthases in this family may be unique to plants and photosynthetic bacteria. This enzyme catalyzes the synthesis of sucrose 6-phosphate from fructose 6-phosphate and uridine 5'-diphosphate-glucose, a key regulatory step of sucrose metabolism. The activity of this enzyme is regulated by phosphorylation and moderated by the concentration of various metabolites and light.	7.86948e-136
NZ_CP034279.1\|WP_156695834.1\|6721207_6722611_-\|D-glycero-beta-D-manno-heptose-1-phosphate-adenylyltransferase	gnl\|CDD\|225425	COG2870, RfaE, ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell envelope biogenesis, outer membrane].	7.11879e-95
NZ_CP034279.1\|WP_156695838.1\|6725795_6727463_-\|carbamoyltransferase	gnl\|CDD\|225103	COG2192, COG2192, Predicted carbamoyl transferase, NodU family [Posttranslational modification, protein turnover, chaperones].	1.54502e-166
NZ_CP034279.1\|WP_156695833.1\|6719400_6720804_+\|MFS-transporter	gnl\|CDD\|340863	cd06173, MFS_MefA_like, Macrolide efflux protein A and similar proteins of the Major Facilitator Superfamily of transporters. This family is composed of Streptococcus pyogenes macrolide efflux protein A (MefA) and similar transporters, many of which remain uncharacterized. Some members may be multidrug resistance (MDR) transporters, which are drug/H+ antiporters (DHAs) that mediate the efflux of a variety of drugs and toxic compounds, conferring resistance to these compounds. MefA confers resistance to 14-membered macrolides including erythromycin and to 15-membered macrolides. It functions as an efflux pump to regulate intracellular macrolide levels. The MefA-like family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	1.79303e-58
NZ_CP034279.1\|WP_156695839.1\|6727515_6728484_-\|NAD-dependent-epimerase/dehydratase-family-protein	gnl\|CDD\|187541	cd05230, UGD_SDR_e, UDP-glucuronate decarboxylase (UGD) and related proteins, extended (e) SDRs. UGD catalyzes the formation of UDP-xylose from UDP-glucuronate; it is an extended-SDR, and has the characteristic glycine-rich NAD-binding pattern, TGXXGXXG, and active site tetrad. 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.	1.15458e-165
NZ_CP034279.1\|WP_156695828.1\|6710754_6711009_+\|DUF5133-domain-containing-protein	gnl\|CDD\|375043	pfam17196, DUF5133, Protein of unknown function (DUF5133). This protein of unknown function is part of the Borrelidin synthesis genomic cluster. Borrelidin is a polyketide antibiotic.	1.59418e-10
NZ_CP034279.1\|WP_156695842.1\|6731087_6732095_-\|glycosyltransferase-family-9-protein	gnl\|CDD\|340821	cd03789, GT9_LPS_heptosyltransferase, lipopolysaccharide heptosyltransferase and similar proteins. Lipopolysaccharide heptosyltransferase (2.4.99.B6) is involved in the biosynthesis of lipooligosaccharide (LOS). Lipopolysaccharide (LPS) is a major component of the outer membrane of gram-negative bacteria. LPS heptosyltransferase transfers heptose molecules from ADP-heptose to 3-deoxy-D-manno-octulosonic acid (KDO), a part of the inner core component of LPS. This family also contains lipopolysaccharide 1,2-N-acetylglucosaminetransferase EC 2.4.1.56 and belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.	7.88511e-53
NZ_CP034279.1\|WP_156695841.1\|6730137_6731091_-\|glycosyltransferase-family-9-protein	gnl\|CDD\|340821	cd03789, GT9_LPS_heptosyltransferase, lipopolysaccharide heptosyltransferase and similar proteins. Lipopolysaccharide heptosyltransferase (2.4.99.B6) is involved in the biosynthesis of lipooligosaccharide (LOS). Lipopolysaccharide (LPS) is a major component of the outer membrane of gram-negative bacteria. LPS heptosyltransferase transfers heptose molecules from ADP-heptose to 3-deoxy-D-manno-octulosonic acid (KDO), a part of the inner core component of LPS. This family also contains lipopolysaccharide 1,2-N-acetylglucosaminetransferase EC 2.4.1.56 and belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.	3.06488e-48
NZ_CP034279.1\|WP_156695826.1\|6708854_6709322_-\|hypothetical-protein	gnl\|CDD\|377229	pfam04138, GtrA, GtrA-like protein. Members of this family are predicted to be integral membrane proteins with three or four transmembrane spans. They are involved in the synthesis of cell surface polysaccharides. The GtrA family are a subset of this family. GtrA is predicted to be an integral membrane protein with 4 transmembrane spans. It is involved is in O antigen modification by Shigella flexneri bacteriophage X (SfX), but does not determine the specificity of glucosylation. Its function remains unknown, but it may play a role in translocation of undecaprenyl phosphate linked glucose (UndP-Glc) across the cytoplasmic membrane. Another member of this family is a DTDP-glucose-4-keto-6-deoxy-D-glucose reductase, which catalyzes the conversion of dTDP-4-keto-6-deoxy-D-glucose to dTDP-D-fucose, which is involved in the biosynthesis of the serotype-specific polysaccharide antigen of Actinobacillus actinomycetemcomitans Y4 (serotype b). This family also includes the teichoic acid glycosylation protein, GtcA, which is a serotype-specific protein in some Listeria innocua and monocytogenes strains. Its exact function is not known, but it is essential for decoration of cell wall teichoic acids with glucose and galactose.	6.40149e-18
NZ_CP034279.1\|WP_167536489.1\|6732091_6732658_-\|HAD-IIIA-family-hydrolase	gnl\|CDD\|319806	cd07503, HAD_HisB-N, histidinol phosphate phosphatase and related phosphatases. This family includes the N-terminal domain of the Escherichia coli bifunctional enzyme histidinol-phosphate phosphatase/imidazole-glycerol-phosphate dehydratase, HisB. The N-terminal histidinol-phosphate phosphatase domain catalyzes the dephosphorylation of histidinol phosphate, the eight step of L-histidine biosynthesis. This family also includes Escherichia coli GmhB phosphatase which is highly specific for D-glycero-D-manno-heptose-1,7-bisphosphate, it removes the C(7)phosphate and not the C(1)phosphate, and this is the third essential step of lipopolysaccharide heptose biosynthesis. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.	5.28116e-60

>NZ_CP034279.1|WP_156695833.1|6719400_6720804_+|MFS-transporter
MVDAAGTPPTRPAAADRYRWTGRAAQQEPPSPPCSAIRVPRSTVSLSSPHSPWRSLTYRSMRWWSLANLVSNAGTWMQLTVQNLLVLQITGSAAATGLSLSVQAAPGLLMGVAGGAAVDRWPRKLTAAVSQALLGTVAFTTALLIAFDQLNLPALMALAAVTGLIATVDGPACSLLGNDLVRAEDVPSAIGVGSLVSNAGRLAGTGLAGLAVGVFGTGAAYVANGVSFLFVAAVIPFLRPVTHTVTRKAAPADTDDDMSVREGLRFFARRPRLVALAGITGISAIFGRNYGLTLAVLVTGPLAGGAGSFGTVSTVLAVGGIIGAVLGARLRKPSVRLVGTLAAAGALLQVVAGLSPSLAVLLILVLPMAVVESVSDTAGTTVLQTDPPAEMRGRVLGVWGSIKTVWGLAGPPALGLLMELAGARGALVAGGLLIAGAIGAGHLLRRRAPTPVLTPVPAPRPALSTAA
>NZ_CP034279.1|WP_156695832.1|6718471_6719206_-|SDR-family-NAD(P)-dependent-oxidoreductase
MDGVLRGKQALVTGGARGLGASITRRLAGAGASVLVADVRKEQARELCDELAVEGRDARFVELDVRDARAVGEVFRELERDGQAVDVLVNNAAVDVSKPIEHLTAEEVTRVVTTNLLGPMYLCLEAYRRMVARGGGHIVNILSTASNRTWTEAGPYSAGKSGLRAFTHTLFKEAQRDCPGIGVTGVIAGGMETPFILERFPDADVSMLQSPDIVADTVLYALSVPAGSAVSELVVVPRREPSWP
>NZ_CP034279.1|WP_156695831.1|6717432_6718470_+|DNA-topoisomerase-IB
MRLYHSRPTDPGHRRRRHGRGFRYLDPSGNPLRDPAETARIKALVIPPAWQDVWICTRANGHLQAVGTDTAGRRQYLYHPQFRAEQEQAKHEHVLDIAERLPDVRQAVDAHLGDRGLTRRRVLATAVRLLDLGFFRIGSDRYTEVNSSYGLTTLLREHSHCQAGAVVFTYPGKHGRELVQTVADPPTCRSLTALLRRRGGGGDRLFAYWERPAWQDVTGADVNAYLKEQAGVEITAKDFRTWHATVMAAVALAVSQPVARSESARKRAIARAAHEVAGYLGNTPAVCRASYINPRVIELYEEGVTVAATLPRLGDEGVYGVPATQGPTERAVLHMIRTGRPPGKT
>NZ_CP034279.1|WP_156695830.1|6714987_6717357_+|SpoIIE-family-protein-phosphatase
MSAVHAAEGADFRGPLDVTKAATAVLDADGTVVGWGPAAHALLGYPPDEAVGSPIGTFIVDRPGEYDMATPLPGAAQARRQVVHMRRRDGHIVRVATATLPLSHTGKGPARLLAIADADETERWEALQSMLRGLATQSPVGLAIYDTDLRVVWTNHALYEEMGTLQYAGLGPDEMVTHGQVLSDGHPATLTEAMQRVLDTGDTVIELHYSGRPPADPEHDHVWSCSYYRLQDGNGRVLGVCEETVDVTDRYLAQQRLDLLVRAGRRVGTSLDMTRTAQELSSVAVPQFADGVTVDLIDIVLEGDQPAPGSTSTRVVRVWEGPAPDTTPQVIDHPADSLQARCLAAGRPVLENPAHDGPAHSRLAVPLRTDGASLGVVTFRRDHHPDPFEDDDVPLADELVARAAVCIDNARRYTREHAAALTLQRSLLPRKLPRLTGVDVAHRYLPADSSAGVGGDWYDVIALSGTRVGLVVGDVVGHGVRAAATMGRIRTSVRALARLDLPPDELLTRLDELITQDAHEQTAVQAEPDDPALGVTCLYAVYDPVTGRCSMARAGSPLPSVVDPTTGEITHPDVPAGPPLGLGGLPFESAEFTLAEGSLMALFTDGLVQGRDRDRDTELDALHTVLAEHRLPLEELCDRVVTTLLPGPVDDDAALLLVRTRTLDSHEVAAWDLTGEPEVVGRARALATGQVDAWGLDGELSFTTELVVSELVTNAIRYASGPIQLRLIRDRALICEVSDTGHTSPNLRRAAGDDEGGRGLFLIAQMTQQWGTRYTPTGKTIWAEQPIPP
>NZ_CP034279.1|WP_156695829.1|6712420_6714928_+|SpoIIE-family-protein-phosphatase
MPGKSHSNGPGTATGPPDELALELAHATVGAVEATGGFAGGVYLRTDTPELLRLAALAGLPVQLFHPWWNMHVNRPFPVADAYRSGSAIHLADAEDAMRRYPQLMAGLPFPFGSLNEPVTDGSDCYGVLVVIRAATPGRPVETADRRRIRQTAHTLATRLTALATRTPVTWTGPPLNVQLPARTTPPVRGGRFHWDRATGALTLDDTLQTLLAAGRDPDRGRHPATRAHPAPLRLTGLDDLASVLAPEDRYGLWTVARQVTEADGPLTRRIWLRAPDGRPCLLELSGGAGHLHGTLVEPGAGPVVATAADRLPSGVCSLDRLGRITFVSRTAETLLGRGRPELVGRTLWDALPWFGRPAYEDHFRAALLSDEPVHFPAQRDPDAWLSVSLYPGHEGVTMTLTASDQPAYTPGSLVAPGAGLGSPADRASVLYRPVALAIALTEAVTARQVSAVVTEELLPAFGGRQLAIYLLNERKLHLAWETGFPQGFLDRFDGVGLDARLPGVETLTTGRPIFFESMQHLAAAYPGIPMDAHVGARAFLPLIASGRPVGSCILGFDQPRGFSPEERTVLTALAGLIAQALQRARRYDSEAALARGLQSALLPHRLPALPGVDTAGRYLPGTQGMEVGGDWYDVIDTGRGIALVIGDVQGHGVAAAATMGQLRSAVRAFALSGHDPEEVMSGTNRLLIDLDAGQFATCCYILLDTAAGTTHAVRAGHLPPLLRHPDGTTDVVDLPGGVVLGVDAEATYPVTPLRLVPGDVLALYTDGLVEEPGTDIDLGIERLRRALAAVGTGPLAETAEGLIREAGAGDRPDDIALLLAARTPDDAPGPPRTG
>NZ_CP034279.1|WP_156696672.1|6711311_6712154_-|SIS-domain-containing-protein
MDRVMALFGGHRLSPAQRRIAQYMTDHLTEAAFLSITDLAERVGVSQPSVTRFATSLGYSGFPALREALQPIALSAVAGAPETREEIRRNELQAAIDAEIENLEQLRRLVADPGQILDVGRELAGSVPLTILGLRISVSLAEYFAYAARRIHPDVRLVTRGGSVAYDALLQSREAGGTWVLAFAMPRHAHETLSAMRAARRAGLRVALITDLTFGPLVEEADVALTAATGSRLVFDSYAAPGVLSAAVLQAMADANPERTQVRLEGYEQAAEQHNFFLDD
>NZ_CP034279.1|WP_156695828.1|6710754_6711009_+|DUF5133-domain-containing-protein
MLLAHPAVLRELVARYESLCTASQELALAPDLKRRLDDVTYTLCVTTGTRHLDQALAAARARLAATTTVASATVATATAAVTAT
>NZ_CP034279.1|WP_156695827.1|6709318_6710317_-|glycosyltransferase
MVHLSVVVPCFDESEVIDAFHTALVGALEPTGVTFEVAYVDDGSTDRTVDRLRGLAATDARVRFTSFSRNFGKESALLAGMRMARGEVVVLMDADLQHPPALLPRMLELHRHGYDQVIAQRDRTGEGPVRAALSRAYYRLVRRFMDVEIADGAGDFRLLSRRAVDSLLSLPESNRFSKGLFSWIGFDTVSFRYENVERAAGRSKWGGRRLLNYGIDGLLSFNSRPLRLAIHTGLWLFLSALLYALWIIANALLDGVDTPGYATLITAIVGLSGIQLATLGVIGEYVGRIYHESKRRPHYIVRETERSAVVHPDHRHVPDVVLEPAGRARPKP
>NZ_CP034279.1|WP_156695826.1|6708854_6709322_-|hypothetical-protein
MRPPAALRAPAVRQFALFAVIGLANTAVYYVVYASLNVWLPYLAAHAVGYAVSVVGSFLLNSWITLRTRPTWRAFARYPLSGVVNVVGSGLLLHLAVSRLGMDENLAALAAGLLVTPLSFLLARWAITSGAAATRRSASRRPPGEEPVREGASRE
>NZ_CP034279.1|WP_156695825.1|6707365_6708880_+|hypothetical-protein
MAVGASSVTTPPDPGQGPGPGRDKGDGDPRGSATTAWTTGLALLPLGLLAAAAYLGRYVRPSADEWCFLPVVRDEGVSGLVGKFYFTDNGRVGNGLLVGLYAKFPVAGHQWYGLVSGALMLGLLWALTALLLRRTGLGVPRGVPLLVASMITAVFLFATPNTYKTFYWPAASVSHTLAPVLACAAAIPLLRGHGRRGRIAALVVVLLAGVFMGTLSEEASVVALVVLSGVVLCAGLVLTERVRAFARIWALTGMAGVAIGTLVLVTSPGSRNRRERFGAETTSMLAPESLIASLKAFVRILETVLTTWQYAGAVAAGVLLGLLAGRDAAHRADRVLLPGRPLLLTGLGAAAFLVSGYLCTVITYPVFGPRVVTAERTWNDYLLLFVLLLVGAGAFLGRTLRQRGIRTGVVTALAAAVCAVTVAGLAVPLYELGHDMRVRAQKWDHQDRWLRERAAAGAKVLPYKPVSVSAMLEPFSANGTRIWPAGCVADYYHLDKVTRGTRLP
>NZ_CP034279.1|WP_156695834.1|6721207_6722611_-|D-glycero-beta-D-manno-heptose-1-phosphate-adenylyltransferase
MSAYKPLVVVGDVLLDEDIQGVSTRLAPDAPAPVVDVTGDQRRPGGAGLAATLATHGGRDVVLVTALGDDPASEAVRRSLRGRVRVVELPLNGTLPVKTRVLAGGRPLVRIDRGGGDPGEPDAAVRDTLEQAHAVLVADYGRHTAGAVRAHLAAVAPKVPVVWDPHLKGDAPVPGSRIVTPNAAETMALCRGGDDSLRAFAERGADLAERWGVAAVAVTLGERGVLLTRPGAMTPMLVPVPYRADGDACGAGDCFAAATAAALADGALPEEAVQRAVAEAAAFVAAGGAGNPSLWRTPLPVTPREAPDAADPFVLAEQVRARGGTVVATGGCFDLLHAGHVGLLESARRIGDCLIVCVNSDESVERLKGPGRPLNPLPDRVRVLAGLGSVDAVAVFDGDTPAELLGRLRPDVWVKGGDYSAEDLPEAEVLHTWGGQAVVLPYLDGRSTTLLARRAAEAATPIRPPGR
>NZ_CP034279.1|WP_156695835.1|6722607_6723279_-|SIS-domain-containing-protein
MTDPLAPPTLEAAHEHCRALQDALARFRHDHLDRITEWGGHLAAVLPVGGRLLAAGNGGSAAQAQHLTAELVGRYQRERPAFSAISLHAETSSVTAIGNDYGFDQVYARQVAAHGRPGDVLVLLSTSGHSANLIAAAMTARRAGLRVWALTGSRPNPLAEAADEACCVDAGSTATVQETHLVAVHLLCESFDAAVATTVDATAGRPARAAGAAAPVAARRRMS
>NZ_CP034279.1|WP_156695836.1|6723413_6724817_-|glycosyltransferase
MTSLDPLEPDRTAAGDVGGIGEVGDVGDIDTEAEVLEVLDAEARGLGAGDVVGAGPGDGNGNRLSVALVSEHASPLAALGGVDAGGQNVHVARLASALADRGHRVTVFTRRDTRDLPDRVALRPGVEVLHVPAGPPEPIPKDALLPYMAEFGRWMAGEWRARPPDLVHSHYWMSGVATLRAAREARLPFVHTYHALGTVKRRHQKHADTSPAERVDREREVGLGCDRVIATCHDEVYELSRMRIPADKVGVVPCGVDTGQFTPDGPAADRDGGLRYRLLQLGRLVPRKGAAVSITALTRLPDTELLVVGGPPPERLDEDPEVRRLREIARVAGVASRVHFAGGVPPEEVAPLLRSADVVLCPADYEPFGIVPLEAMACGRPVVASAVGGQLDTVADPVTGRLVPPRDPDALARAVGELLADPAQRAACGAAGRRRVLSRYGWAEVAAATEKEYAAVLAARHAVTGVA
>NZ_CP034279.1|WP_156695837.1|6724813_6725779_-|glycosyltransferase
MNILLWHVHGSWTTAFVQGPHTYLVPVTPDRGPDGLGRARTFSWPDSVREVTPEELREEPVDLVVLQRPHELDLAERWLGGRRPGRDVPAVYLEHNAPDGNVPATRHPCADRDDLTLVHVTHFNRLFWDNGATRTEVIEHGIVDPGHQYTGRLARAAIVVNEPVRRGRHTGTDLLPALSEAAPLDVFGMRTEGLAAHLGIPEDRCRSADLPQRDLHAAMAERRLYLHPVRWTSLGLSLLEAMHLGMPVVALATTEAIEAVPAGAGTLSTRPEVLARAARHYLNEPEAAASDGARARQAALERYGLKRFLDDWERVMTEVRA
>NZ_CP034279.1|WP_156695838.1|6725795_6727463_-|carbamoyltransferase
MRILGINALFHDPAAALVIDGRTVAAAEEERFSRRKHGKRPVPFSAWELPEQAAAWCLKRAGLRPQDLDAVAYSYDPELARSAADLGLDDPWDGLRQTYAREAPGFLKAALPGLDPGIVRFVPHHMAHAASGAFAAEGADTSSVLVLDGRGERASHLAARRVHDRLEALHAQELPHSLGLVYEELTEHLGFLRSSDEFKVMALASHGRPRMLPELRRWVYPTGDGGFHATGVPWAELCPRRRPDEAWTQDHADTAASAQAVLEETLLDLVRWLHGQTHDGLLTLAGGVALNCVANARIAREGPFDRVWVQPAAGDAGTALGGALLLAAGGGDDPDPMRGADLGRDWSDAELGAWLKTAAVPFDRPADIAETVAEALADNAIVAWFQGRSEFGPRALGHRSLLAHPGHAGNLERLNDVKGREQFRPVAPMVLAERAGEIFDGVTPSPYMLFVHDVAPEWRERIPAVVHVDGTARIQTVDRRAEPLVARMLTEFERRTGLPVVVNTSLNTAGRPMVDDPRDALECFGSSPVDLLAIGPYAVRRGDFFRSDDTDDASR
>NZ_CP034279.1|WP_156695839.1|6727515_6728484_-|NAD-dependent-epimerase/dehydratase-family-protein
MTTAFSRRWEHAVVTGGAGFVGSHLCHALLDSGSAVTCVDDFSTGRPENISGLLDHPGFTLVRANVSEPFFVDRPPDLVLHFASPASPADYLRLPLHTLETGSLGTRHALALAHRSDARFLLASTSEVYGDPQQHPQNERYWGNVNPVGPRSVYDEAKRFGEALTTAEAEVHGTDAGIVRLFNTYGPRMRGHDGRAVPTFVRQALDGEPLTVTGDGRQTRSLCYIDDTVRGILAAAAHGLRGPVNIGNPTEITMLELARLVIELTGSGSEIRFIERPTDDPAVRCPDITLARDKLEWEPRIDAEEGLRRTIAWFREHADARS
>NZ_CP034279.1|WP_156695840.1|6728947_6730042_-|glutamate--cysteine-ligase
MITIGVEEEYLLLDQDTCLPVPLADQVRTAAGLEPIVDDAEVQSELLQAQVEVATPVCTDLEEVGGHLLRLRHALGTAAEKNGCRIAACATAPYREIAPVPVTQKARYLAMRSQAPQLVAEQLVNGMHVHAAVPDREMGVAVLSRIRVWLPVLVAMSANSPLWDGNDTGFASWRTVIFGRWPVSGPPPRFTSLVDHETRVQSLLDTGIITDTGQLYWQARLSDKYPTVEVRCADVQLRADTAVMFAGIVRGLIATAIRDEKAGLPLPNCTPELLQAANWHAARHGLSGLLVDPTGKARRAGDVLVMLLDHVTPALDDAGDTREVTSLVHRLLQQGTPADQQRRALAEGGLRALADLITSETVAP
>NZ_CP034279.1|WP_156695841.1|6730137_6731091_-|glycosyltransferase-family-9-protein
MRPRLLVLRALGLGDLLAGIPALRALRRAHPAYEIVLAAPEQLAAPANASGAVDRLLPASAPGRAVPAHLDWTGPPPEVAVDLHGNGPPSHRLLQRLRPGRLLAFAHPRTPEIQGPAWTADEHERARWCRLLTWYGIPADPSDLRLPAPATPSPAPGAVVVHPGADSGARRWPAERYAAVVRALRQRGHRVALTGGPGEDELLDRVLDAARTDGVRAFRGGLPFDRLGALFAGASAVVSGDTGIAHLAVAYGTPSVTLFGPVAPGLWGPPPGTRHVVLWHPGPPGDPHGQDPDPQLLRIGPDDVLKALLDHPEVPRP
>NZ_CP034279.1|WP_156695842.1|6731087_6732095_-|glycosyltransferase-family-9-protein
MKALVVRLDSFGDVLLAGPAVRAVAGRADRVTLLCGPRGAPAARLLPGVDEVLVWDAPWAGFTPPPVRRPDIDRLVNRVAAARADTALVLTSFHQSPLPAALLLRMAGIAHIAADSEDAPGSLLDVRHRRAPHAHEAQAALDLAEAAGFPRPAGDDGRLCVRHAPGAPDLTGPAPYVVVHPGASVEARRWSPERCAHAVRLLAGAGHRVVVTGGPDERELTALVAGRDGLDLGGRTQPPQLAAVLAAAGAVVVGNTGPAHLAAAVGTPVVSLFSPVVPAERWGPYGVPHVLLGEQRAPCADSRARQCPVPGHPCLDEVTGEDVAAAVEKLLKGGA
>NZ_CP034279.1|WP_167536489.1|6732091_6732658_-|HAD-IIIA-family-hydrolase
MGRRPVTRPAAVLFDRDDTLVEDVPYNADPRKVRPMPGAHEALRTLRDHGILLGVVSNQSGVGRGLLTEADVRAVNARVDALLGPFDVWVHCPHTPEDGCRCRKPAPGMVLEAAHRLGVPPGHCVVVGDIGADMGAARAAGARGVLVPTARTLPGEVAAAPHVCRDLMSAVRHVLRADRASVSPGSPA

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Crispr_ID: NZ_CP034279_13

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP034279_13

7024760-7024909

Orphan

Consensus_repeat	Method
ACGGCGCGACCGCGCGCGCCGCCGACGACGTGACCGCGC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP034279_13

>merge|NZ_CP034279|13|7024760-7024909|CRISPRCasFinder
ACGGCACCATGACGCGCGCCGATGACGGCGCGACCGCGCGCGCCGCCGACGACGTGACCGCGCGCGCCGACAACGCGACCACGCGTACAGACGACACGACCACGCGTACCAACGGCGCGACCGCGCGCGCCGCCGACGACGCGACCGCGC

>NZ_CP034279|13|13|7024760-7024909|CRISPRCasFinder
ACGGCACCATGACGCGCGCCGATGACGGCGCGACCGCGC	GCGCCGCCGACGACGTGACCGCGCGCGCCGACAACGCGACCACGCGTACAGACGACACGACCACGCGTACCA
ACGGCGCGACCGCGCGCGCCGCCGACGACGCGACCGCGC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP034279.1\|WP_156696072.1\|7020264_7021119_-\|tat-(twin-arginine-translocation)-pathway-signal-sequence	unknown	unknown	unknown
NZ_CP034279.1\|WP_156696083.1\|7031058_7032099_-\|VWA-domain-containing-protein	unknown	unknown	gnl\|CDD\|238119
NZ_CP034279.1\|WP_156696707.1\|7032272_7033613_+\|geranylgeranyl-reductase-family-protein	unknown	unknown	gnl\|CDD\|273936
NZ_CP034279.1\|WP_167536453.1\|7026028_7026409_+\|STAS-domain-containing-protein	unknown	unknown	gnl\|CDD\|132914
NZ_CP034279.1\|WP_156696070.1\|7018301_7019198_+\|SDR-family-NAD(P)-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|235633
NZ_CP034279.1\|WP_156696077.1\|7026467_7027376_-\|allantoinase-PuuE	unknown	unknown	gnl\|CDD\|211797
NZ_CP034279.1\|WP_156696071.1\|7019335_7020247_+\|phenylalanine-4-monooxygenase	unknown	unknown	gnl\|CDD\|238215
NZ_CP034279.1\|WP_156696069.1\|7015747_7016953_+\|SpoIIE-family-protein-phosphatase	unknown	unknown	gnl\|CDD\|369272
NZ_CP034279.1\|WP_156696081.1\|7029851_7030229_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP034279.1\|WP_156696068.1\|7014098_7015751_+\|HAMP-domain-containing-protein	unknown	unknown	gnl\|CDD\|226702
NZ_CP034279.1\|WP_156696073.1\|7021324_7021885_-\|hemerythrin-domain-containing-protein	unknown	unknown	gnl\|CDD\|376622
NZ_CP034279.1\|WP_156696075.1\|7023106_7024726_+\|SpoIIE-family-protein-phosphatase	unknown	unknown	gnl\|CDD\|369272
NZ_CP034279.1\|WP_156696074.1\|7022210_7022627_+\|CBS-domain-containing-protein	unknown	unknown	gnl\|CDD\|341390
NZ_CP034279.1\|WP_156696080.1\|7029520_7029793_+\|DUF3253-domain-containing-protein	unknown	unknown	gnl\|CDD\|371633
NZ_CP034279.1\|WP_156696705.1\|7017720_7018080_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|212140
NZ_CP034279.1\|WP_156696078.1\|7027638_7028382_+\|methyltransferase-domain-containing-protein	unknown	unknown	gnl\|CDD\|379312
NZ_CP034279.1\|WP_156696079.1\|7028527_7029433_-\|NAD-dependent-protein-deacetylase	unknown	unknown	gnl\|CDD\|238700
NZ_CP034279.1\|WP_156696704.1\|7017215_7017668_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|370266
NZ_CP034279.1\|WP_156696082.1\|7030323_7030812_+\|MarR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|197670
NZ_CP034279.1\|WP_156696084.1\|7033630_7034356_-\|methyltransferase-domain-containing-protein	unknown	unknown	gnl\|CDD\|379312

Protein	Function_ID	Function_description	E-value
NZ_CP034279.1\|WP_156696082.1\|7030323_7030812_+\|MarR-family-transcriptional-regulator	gnl\|CDD\|197670	smart00347, HTH_MARR, helix_turn_helix multiple antibiotic resistance protein.	4.35689e-17
NZ_CP034279.1\|WP_156696083.1\|7031058_7032099_-\|VWA-domain-containing-protein	gnl\|CDD\|238119	cd00198, vWFA, Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains.	1.26034e-08
NZ_CP034279.1\|WP_156696707.1\|7032272_7033613_+\|geranylgeranyl-reductase-family-protein	gnl\|CDD\|273936	TIGR02032, Uncharacterized_protein_MJ1520, geranylgeranyl reductase family. This model represents a subfamily which includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll].	1.37295e-64
NZ_CP034279.1\|WP_167536453.1\|7026028_7026409_+\|STAS-domain-containing-protein	gnl\|CDD\|132914	cd07043, STAS_anti-anti-sigma_factors, Sulphate Transporter and Anti-Sigma factor antagonist) domain of anti-anti-sigma factors, key regulators of anti-sigma factors by phosphorylation. Anti-anti-sigma factors play an important role in the regulation of several sigma factors and their corresponding anti-sigma factors. Upon dephosphorylation they bind the anti-sigma factor and induce the release of the sigma factor from the anti-sigma factor. In a feedback mechanism the anti-anti-sigma factor can be inactivated via phosphorylation by the anti-sigma factor. Well studied examples from Bacillus subtilis are SpoIIAA (regulating sigmaF and sigmaC which play an important role in sporulation) and RsbV (regulating sigmaB involved in the general stress response). The STAS domain is also found in the C- terminal region of sulphate transporters and stressosomes.	4.24578e-17
NZ_CP034279.1\|WP_156696070.1\|7018301_7019198_+\|SDR-family-NAD(P)-dependent-oxidoreductase	gnl\|CDD\|235633	PRK05872, PRK05872, short chain dehydrogenase; Provisional.	2.42377e-109
NZ_CP034279.1\|WP_156696077.1\|7026467_7027376_-\|allantoinase-PuuE	gnl\|CDD\|211797	TIGR03212, uraD_N-term-dom, putative urate catabolism protein. This model represents a protein that is predominantly found just upstream of the UraD protein (OHCU decarboxylase) and in a number of instances as a N-terminal fusion with it. UraD itself catalyzes the last step in the catabolism of urate to allantoate. The function of this protein is presently unknown. It shows homology with the pfam01522 polysaccharide deacetylase domain family.	7.94109e-158
NZ_CP034279.1\|WP_156696071.1\|7019335_7020247_+\|phenylalanine-4-monooxygenase	gnl\|CDD\|238215	cd00361, arom_aa_hydroxylase, Biopterin-dependent aromatic amino acid hydroxylase; a family of non-heme, iron(II)-dependent enzymes that includes prokaryotic and eukaryotic phenylalanine-4-hydroxylase (PheOH), eukaryotic tyrosine hydroxylase (TyrOH) and eukaryotic tryptophan hydroxylase (TrpOH). PheOH converts L-phenylalanine to L-tyrosine, an important step in phenylalanine catabolism and neurotransmitter biosynthesis, and is linked to a severe variant of phenylketonuria in humans. TyrOH and TrpOH are involved in the biosynthesis of catecholamine and serotonin, respectively. The eukaryotic enzymes are all homotetramers.	8.70338e-75
NZ_CP034279.1\|WP_156696069.1\|7015747_7016953_+\|SpoIIE-family-protein-phosphatase	gnl\|CDD\|369272	pfam07228, SpoIIE, Stage II sporulation protein E (SpoIIE). This family contains a number of bacterial stage II sporulation E proteins (EC:3.1.3.16). These are required for formation of a normal polar septum during sporulation. The N-terminal region is hydrophobic and is expected to contain up to 12 membrane-spanning segments.	2.65584e-32
NZ_CP034279.1\|WP_156696084.1\|7033630_7034356_-\|methyltransferase-domain-containing-protein	gnl\|CDD\|379312	pfam13649, Methyltransf_25, Methyltransferase domain. This family appears to be a methyltransferase domain.	2.65885e-14
NZ_CP034279.1\|WP_156696068.1\|7014098_7015751_+\|HAMP-domain-containing-protein	gnl\|CDD\|226702	COG4251, COG4251, Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal transduction mechanisms].	6.5148e-75
NZ_CP034279.1\|WP_156696073.1\|7021324_7021885_-\|hemerythrin-domain-containing-protein	gnl\|CDD\|376622	pfam01814, Hemerythrin, Hemerythrin HHE cation binding domain. Iteration of the HHE family found it to be related to Hemerythrin. It also demonstrated that what has been described as a single domain in fact consists of two cation binding domains. Members of this family occur all across nature and are involved in a variety of processes. For instance, in Nereis diversicolor hemerythrin binds Cadmium so as to protect the organism from toxicity. However Hemerythrin is classically described as Oxygen-binding through two attached Fe2+ ions. And the bacterial NorA is a regulator of response to NO, which suggests yet another set-up for its metal ligands. In Staphylococcus aureus the iron-sulfur cluster repair protein ScdA has been noted to be important when the organism switches to living in environments with low oxygen concentrations; perhaps this protein acts as an oxygen store or scavenger.	3.45066e-14
NZ_CP034279.1\|WP_156696075.1\|7023106_7024726_+\|SpoIIE-family-protein-phosphatase	gnl\|CDD\|369272	pfam07228, SpoIIE, Stage II sporulation protein E (SpoIIE). This family contains a number of bacterial stage II sporulation E proteins (EC:3.1.3.16). These are required for formation of a normal polar septum during sporulation. The N-terminal region is hydrophobic and is expected to contain up to 12 membrane-spanning segments.	3.90566e-39
NZ_CP034279.1\|WP_156696074.1\|7022210_7022627_+\|CBS-domain-containing-protein	gnl\|CDD\|341390	cd04622, CBS_pair_HRP1_like, CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds. Mycobacterium tuberculosis adapts to cellular stresses by upregulation of the dormancy survival regulon. Hypoxic response protein 1 (HRP1) is encoded by one of the most strongly upregulated genes in the dormancy survival regulon. HRP1 is a 'CBS-domain-only protein; however unlike other CBS containing proteins it does not appear to bind AMP. The biological function of the protein remains unclear, but is thought to contribute to the modulation of the host immune response. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).	4.49951e-45
NZ_CP034279.1\|WP_156696080.1\|7029520_7029793_+\|DUF3253-domain-containing-protein	gnl\|CDD\|371633	pfam11625, DUF3253, Protein of unknown function (DUF3253). This bacterial family of proteins has no known function.	5.81785e-27
NZ_CP034279.1\|WP_156696705.1\|7017720_7018080_-\|hypothetical-protein	gnl\|CDD\|212140	cd11533, NTP-PPase_Af0060_like, Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in uncharacterized protein from Archaeoglobus fulgidus (Af0060) and its bacterial homologs. This family includes an uncharacterized protein from Archaeoglobus fulgidus (Af0060) and its homologs from bacteria. Although its biological role remains unclear, Af0060 shows high sequence similarity to the dimeric 2-deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTP pyrophosphatase or dUTPase) and NTP-PPase MazG proteins. However, unlike typical tandem-domain MazG proteins, members in this family consist of a single MazG-like domain that contains a well conserved divalent ion-binding motif EXX[E/D].	1.36119e-18
NZ_CP034279.1\|WP_156696078.1\|7027638_7028382_+\|methyltransferase-domain-containing-protein	gnl\|CDD\|379312	pfam13649, Methyltransf_25, Methyltransferase domain. This family appears to be a methyltransferase domain.	5.06815e-26
NZ_CP034279.1\|WP_156696079.1\|7028527_7029433_-\|NAD-dependent-protein-deacetylase	gnl\|CDD\|238700	cd01409, SIRT4, SIRT4: Eukaryotic and prokaryotic group (class2) which includes human sirtuin SIRT4 and several bacterial homologs; and are members of the SIR2 family of proteins, silent information regulator 2 (Sir2) enzymes which catalyze NAD+-dependent protein/histone deacetylation. Sir2 proteins have been shown to regulate gene silencing, DNA repair, metabolic enzymes, and life span.	1.86339e-137
NZ_CP034279.1\|WP_156696704.1\|7017215_7017668_+\|hypothetical-protein	gnl\|CDD\|370266	pfam09056, Phospholip_A2_3, Prokaryotic phospholipase A2. The prokaryotic phospholipase A2 domain is predominantly found in bacterial and fungal phospholipases, as well as various hypothetical and putative proteins. It enables the liberation of fatty acids and lysophospholipid by hydrolysing the 2-ester bond of 1,2-diacyl-3-sn-phosphoglycerides. The domain adopts an alpha-helical secondary structure, consisting of five alpha-helices and two helical segments.	4.89144e-36

>NZ_CP034279.1|WP_156696075.1|7023106_7024726_+|SpoIIE-family-protein-phosphatase
MTSSPARPRTGAVSTVSAATAPCPVVVMDADGRVAELNDAARDLLPAARTGRSLTAPAWLAATRDTPHAVPVSGAVGDRSFSAHPSVLAGGGTAWWLVEDTAYRAAREELEAERERTRFLTDASSALLASLNLNRCMEVTARLATEHLADAAVVVAPTAARKLPIVVCDHRGELTRDTVAEVPDSVPALAEALRGFPPVPSRWIDPASAPDWLIPPGFGDIGSLAVTPLPGHGVPAGALILLRRVPQAAFTDAEEALAGLFAARAGVAMSAARLYAEQNTITDTLMRELLPPTLGHVEGVEYAGGYRPSQDTERVGGDFYDVHPPTEDFPETLAVLGDVAGKGLEAAVLTGKIRNTLHALLPLAGDHAKMLRLLNNAIRSSHHTRFATLVLASVRRDDRDVTVRLTSAGHPAPLIVRRDGTVEEADTGGTLIGVLPSIRSRSSEIRLGPGETCLLFTDGVTEAKGGPLGDSLFGEQRLKRAAAECAGMPAEAVVEHIRMVTSQWIGDGRHDDIAVMAITAPRGAHLSAVDGTTRGRYTA
>NZ_CP034279.1|WP_156696074.1|7022210_7022627_+|CBS-domain-containing-protein
MTTARQIMTEGTECIGAEESVLEAAKKMKQLGVGALPICGTDNKLKGMLTDRDIVVKVLGAGKDPASCKAGELAQGEAVTIGADDDADEILRTMTEHKVRRLPVIDGHDLVGMVAQADVARALPDPKVGDLLQALSTD
>NZ_CP034279.1|WP_156696073.1|7021324_7021885_-|hemerythrin-domain-containing-protein
MGHGGNVIQELTTDHREVDELFARIESLPAGDEQRRELADELTMELIRHAVAEEMYLYPAVRRFVDDGDDLADKEIEDHSEVERMLTDLEGCHPGDARFDALINRLKAAVTTHVADEENRLFPLLAESCSPQSLDELGDKIRSAKKTAPTRPHPAAPDTPPANKLLAPGAGMVDRMRDMLTGRGKG
>NZ_CP034279.1|WP_156696072.1|7020264_7021119_-|tat-(twin-arginine-translocation)-pathway-signal-sequence
MTSRALSLLTATPRRQAGFLACAAGVVLVAFFLAPNALARSSIDTGNVGDAFREGFVSHWASGGRDLPARLDAAVAFWFRFHLVKAGVSALLLAVAVALAVVLGRRYRQLSGGRNRGRTGRVPGALALPRALVLAGVLALFALVALVANLQGAVAPFSSLLPFLTSGGGHGELGATLDEVRQQLAALPAGERSPALAFMVGDFAAYHAVLAVMAALVAVASAGAAAVLFRRLRASRDVRSRRARTCGAAATAVLAAAALVIAVANTTSAADSPRALALFFAGDW
>NZ_CP034279.1|WP_156696071.1|7019335_7020247_+|phenylalanine-4-monooxygenase
MIDWTGLTPLDAHGTLMGRAEEHPGFADPDYVRRRNSIAGLAQGHWVGDPSPAVSYTASEHATWRTVYAALQHPQERFACREVLRARALAPVPADGVPQHEEVSDRLEALTGFRFTLAGGIVPNKRFLGAMADGYFHAVQYVRHPAMPLYTPEPDVLHDVFGHGIHLTDPLFADLYRTVGRAAARVETDDALDLISRVYWFTLEYGVTLEQGRPRAYGAALLSSYGELGRFARADLRPFDLAELARLPYQVAGYQPVLFTVGSLAHLSDLLHGFLDDFDETTRDRYHLPALSERGFMACPPRA
>NZ_CP034279.1|WP_156696070.1|7018301_7019198_+|SDR-family-NAD(P)-dependent-oxidoreductase
MGQSDALRGRTAVVTGAARGLGAALARELANRGMRVALLGLEAERLEKAARPLPVETRCYAVDVTDDEAMRRTAEAVTDDLGAPSVVIANAGVAEGGPFATSDAASWRRVIEVNLIGSAITARSFLPGLLASHGYFLQVASTAAFGSAPMMSAYCASKAGVESFAQSLRAELAHQRIGVGIAYVHWTDTDMIRDADRHTVLRELRAHMPPGARKTYPVQRVASWVAQGVDHKSATVYAPPWLRLVQPLRPLFPYAVTAVSRRALPRLARDSSVEPTGLLGVGGRADWHALRRHRSEHQ
>NZ_CP034279.1|WP_156696705.1|7017720_7018080_-|hypothetical-protein
MHGADGAGGTDRVWGGVQRLRGWLDAEAGSPEAGDVRLLRIFKISEEVGEVAEAVHGALGVNPRKGASHSWGDVEEELADVIVTAMVALATITPRPEDVLDARVRYLVRRALGSGPDVR
>NZ_CP034279.1|WP_156696704.1|7017215_7017668_+|hypothetical-protein
MAGSVSADGTTTAAAAAAPTKAQKLKRLSHLTAASQDAAGDWTVDREKWRTTGSNKYGFNWKTDGCSGASDNPGGFHFWAACARHDFGYRNYKKLNAFTGANKKRVDKTFLYDMNWTCDKQWGPITQAQRKACRKVAKKYYDAVVAFGHL
>NZ_CP034279.1|WP_156696069.1|7015747_7016953_+|SpoIIE-family-protein-phosphatase
MTAATVTGPAAAAGEPTYRILLIEDDLGDALLVEELLYDTGLRYELITRPTLAEARTALAGTAIDCILLDLHLPDVSGIDAVAAVRALAPHTAVIVLTGLSEAQAGTDAMAAGAQDYLVKGKVEADLLYRTVRYAVYRSQTERAGAEAQAARLRAEENARLERGLLPQPILDTSTVTVTSRYLPGASMALLGGDFLDVVEGDEGLLHAVIGDVSGHGPDAAALGVCLRIAWRSLVLGGHRGDDLLHLMERILIAERGTRHMFATCTILTLDQKAATATLHLAGHHEPLLTTPEGTRELTAAHGVALGIAPELRSWPATVLALPATGALTLYTDGLTEGHNGATKERLGVEGLLALIGNQPTADPAAHVDLLIKEANELNAGRHTDDVAVLRLDWGTRPTRP
>NZ_CP034279.1|WP_156696068.1|7014098_7015751_+|HAMP-domain-containing-protein
MTGDEKQPRARGMSAWTTRRWLRMGAAVSLVVLTLLGATGAWVLSRTESISEELVDVRTPALTTAIRLESAILNQETGIRGYGLTGTPEFLGPYRQGLAEERANHARLSRLLRGHPAGLADLKAVRTALSGWQERVARPVAAEPPGSPSRLATERAAEGKEAFDEVRAALRGQQERLRADSARTNDDLMATLVVRNWVFSAIAVLVVVLTALIFEGLRRGINEPLEQLGADARTIAGGDFDHPITPTGPADLRRLSGEIDSMRRRLVRELAFVEEARVRLDAQAADLQRSNAELEQFAYVASHDLQEPLRKVSSFTQLLQRRYGGQLDARADQYIDFAVDGANRMQKLINDLLDFSRVGRLHNAHQSVDLETVLEGTLSALSVGIEEAGATITHDPLPTLVADPTQMGMLWQNLIGNAVKFHRPDEPPKIHVTAAREGELWRFTVTDNGIGIAPEYADKIFVIFQRLHTKDVYSGSGIGLAMCKKIVEFHGGTIGVDTDYRDGARITFTLAPEPAESTGPSALPESDRSQSDRSESERSESDRSDPEPAR
>NZ_CP034279.1|WP_167536453.1|7026028_7026409_+|STAS-domain-containing-protein
MTATPDPDPAVTPPPAGPHTVHLALTGDLDYDAYGEFLQQARAALEGRSDVTDLRLDCREAGLVDSMGLSALLQIHRSAEENGIRFHLDHIGPALRRLMELTGTYEHLTALQQPGPRPGPHPGSGT
>NZ_CP034279.1|WP_156696077.1|7026467_7027376_-|allantoinase-PuuE
MPEHERDLVGYGAEPPHAAWPGGARVAVSLVLNYEEGGEQNVLEGDPASEGYLHEIVGAPPVVGGRDLNVESMFAYGSRAGFWRVHRTLAAHGAPLTVYAVAQALERNPEAARAMAAAGWEVASHGRRWIDYRHVPEDGERADVARSIGTIERLVGRRPVGWYTGRTSPHTRRLVAEEGGFLYDSDDYSDDLPFYVRAAGRPHLVVPYGLDTNDFKFLLVHGFTTAEDMLAYLVDSFDALHAEGADRPRMMSVGLHCRIIGRPGRIRVLDGFLRHVARRGGAWVATREQIARHWLATHPPVR
>NZ_CP034279.1|WP_156696078.1|7027638_7028382_+|methyltransferase-domain-containing-protein
MSVQQYDKIGEAFEGFKSLPLMLHGEVPSLLGMVGDVSGKSVLDLACGTGFYSREFKRRGADEVFGVDISVEMIAAARDRERRDPLGVRYEVGDVTELRALDRRFDIALGVQCLNYAEDVAAMERMCRNIHRNLLPGGRFFVLAQKPDYRFDSATLERYGFRCEPTGEELETGPQVRVTALLDPRPVTIVTSAPRREVYEKCLRAAGFSEVEWVPLEVSEAGIQEFGEDFWADLLANPPLEMLRCRA
>NZ_CP034279.1|WP_156696079.1|7028527_7029433_-|NAD-dependent-protein-deacetylase
MRMRPTLSWTPAEDWPPGTTDPRPVADALSAGGVLVLSGAGLSTESGIPDYRGEGGSLSRHTPMTYQDFTGGARARRRYWARSHLGWRTFGRARPNAGHRAVAAFERHGLLAGVITQNVDGLHQAAGSASVVELHGSLDRVVCLSCGTFGSRRELALRLEEANAGFAPVAAGINPDGDADLTDDQVGDFRVVPCAVCGGILKPDVVFFGEAVPPHRIDHCRSLVREASSLLVLGSSLTVMSGLRFVRQAAEAGKPVLIVNRDPTRGDQHALTRVALPLGATLTTVAERLGVPVDDGTPRTG
>NZ_CP034279.1|WP_156696080.1|7029520_7029793_+|DUF3253-domain-containing-protein
MTDSEQRMDRLLERAILELLERRAPTATICPSDAARAVYSGEGDGWRALMEPARRAARRLVAAGEVEITQGGHPVEPAKARGPIRIRRAR
>NZ_CP034279.1|WP_156696081.1|7029851_7030229_-|hypothetical-protein
MSAHGDVDLGHTVAGWTGTALGLLGLCVTGLAVITVSPPLALAGAGIVAAAAAVTWALHLLGWGKPSGPRPREEWSWKVRDRAVRHGHPDCLGCRMAGRRPMAAAAPEPAALPHPATAPEVVAAR
>NZ_CP034279.1|WP_156696082.1|7030323_7030812_+|MarR-family-transcriptional-regulator
MDGKVRPPATAEQAHAQMDHLIALGIIAQHDVAQRLGLNVTDVTCLGFILEAENLGEPISAGDLAQRAKLTTGAVTGVINRLERAGYAHRQSDPGDRRRVRVVADVSAAARVYEVYEGNYRRIAELFADYSAEEVAVLSDWLTRATDIMRASLEEVRSGGTG
>NZ_CP034279.1|WP_156696083.1|7031058_7032099_-|VWA-domain-containing-protein
MSAVQNYINHVALVLDASSSMSHLSRKVVEVADQQIAYLARRSRELDQETRVTVYVFADTVECVIYDKDVLRMPSLKQLYRAGGMTALLAAALKSQRELAQTAQLYGDHSFLTFILTDGQENASHRCPDASRRSPRELVAAVAEMIDTQKDNWTLAVLVPDQMGKREATQYGFPKENIAIWDATSTQGLEEAGQVIQQATEKFMVGRTQGIRGSRAVFSTGAEAVNKDTVAAAGLTPVEPSQYHLIPVTRAAAIREWVTESGHTYRTGGAFYQLSKLEKIQAQKQIAVLEKATDRVFTGPEARALLGLPDVEVRIKPDHNDDYTIFVQSTSVNRKLVPNTRLLLMN
>NZ_CP034279.1|WP_156696707.1|7032272_7033613_+|geranylgeranyl-reductase-family-protein
MGAADGPSSPGDTHQDGGEAQVLVVGAGPAGSAAALHLARAGVEVVLLEKSGFPRDKVCGDGLTPRGVHQLIRMGIDVNAPGWTRNRGMRWVCSGRQVEIDWPRLGSHPDFGLTRSRHDFDDLLAAHAVGAGARLHTGVRVTAPLTDRAGRITGVTGVAGPEKRPVRYRAPLVVAADGASARTAVLMGLERDPTRTVATAARRYYRSEARSQDPYLELWADLLCSRTGRDLPGYGWVFPLGDGRINVGLGAMPHRSRGAVDLRATMDQWLTRLPQDWGVGEETATCPLRSAALPMGFNRHPQYHRGLLLVGDSAGMVSPWSGEGIGQALEAAEAAAETIALALARPSGTGREHALRQYPAEINRRWGRYYRLGNLAGDLILGRYGYRPILHPRVMASPPLLRTLARLLTHVADEPPRDTVDALLHTLLRAVPRPRPLTRRTPPTRP
>NZ_CP034279.1|WP_156696084.1|7033630_7034356_-|methyltransferase-domain-containing-protein
MSDDIFAEAPASDAPSAPTASSTPSTPSAPSTVDGYAGDPAVREEWDKRYADRQQLWSGQPNGALVAEVAGLAPGRALDVGCGEGADAVWLAREGWDVTALEVSGVALERAAGHARDAGVAVRWVHAALTDAALTPASFDLVSAQYPALLRTSDAVAERALLAAVAPGGVLLVVHHADVDAEQARESGFDPADYVWPSTVVALLDDAWVVEVDEQRPRPAPDGGAGAHHTDDVVLRARRVR

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Self-targeting detection

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_ID	Protospacer_location	Mismatch	Identity

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity
NZ_CP034279_11	11.1\|6211054\|32\|NZ_CP034279\|CRISPRCasFinder	6211054-6211085	32	NZ_AP022611	Mycolicibacterium madagascariense strain JCM 13574 plasmid pJCM13574	175670-175701	8	0.75
NZ_CP034279_3	3.1\|2306930\|39\|NZ_CP034279\|CRISPRCasFinder	2306930-2306968	39	NZ_CP033582	Streptomyces sp. ADI95-16 plasmid pADI95-16a, complete sequence	209631-209669	12	0.692

1. spacer 11.1|6211054|32|NZ_CP034279|CRISPRCasFinder matches to NZ_AP022611 (Mycolicibacterium madagascariense strain JCM 13574 plasmid pJCM13574) position: , mismatch: 8, identity: 0.75

cggcaggcggggtcggtgcgacggacagggcc	CRISPR spacer
cggcaggcgggggcggtgcggcgttaggaccc	Protospacer
************ *******.**   .*. **

2. spacer 3.1|2306930|39|NZ_CP034279|CRISPRCasFinder matches to NZ_CP033582 (Streptomyces sp. ADI95-16 plasmid pADI95-16a, complete sequence) position: , mismatch: 12, identity: 0.692

cggtcccggcggtcgccgcggtcgccgccgcggtcacca	CRISPR spacer
tctccgaggccgtcgccgcggtcgccgccgccgtcgggg	Protospacer
.  .*  *** ******************** ***.  .

Prophage detection

Region	Region Position	Protein_number	Hit_taxonomy	Key_proteins	Att_site	Prophage annotation

Anti-CRISPR protein detection

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