CRISPRimmunity

Overview of predicted results

Overview of the results

Contig_ID	Contig_def	CRISPR array number	Contig Signature genes	Self targeting spacer number	Target MGE spacer number	Prophage number	Anti-CRISPR protein number
NZ_CP023703	Streptomyces galilaeus strain ATCC 14969 chromosome, complete genome	10 crisprs	c2c9_V-U4,csa3,RT,casR,DEDDh,WYL,cas4,Cas9_archaeal,cas3,DinG,Cas14u_CAS-V	0	6	0	0

1. NZ_CP023703

CRISPR-Cas detection and classification

Crispr_ID: NZ_CP023703_1

• CRISPR_ID: NZ_CP023703_1
• CRISPR_location: 842709-842900
• CRISPR_type: Orphan
• Repeat_type: NA
• Spacer_info: 3 spacers

Consensus repeat of NZ_CP023703_1

Consensus_repeat	Method
GCGTTCGCCGCACACACGCGTGCGCGCG	CRISPRCasFinder
GCGTTCGCCGCACACACGCGTGCGCGCGA	PILER-CR

spacers of NZ_CP023703_1

>1.1|842737|30|NZ_CP023703|CRISPRCasFinder
AAGCCTCAGGGGATCGGGTGGCGGGTATAG
>1.2|842795|33|NZ_CP023703|CRISPRCasFinder
TCCCGCTCGAACTCCTCCCGGGGGTATCCCGGC
>1.3|842856|17|NZ_CP023703|CRISPRCasFinder
ACGAACGGCGCGCGCGG
>1.4|842746|29|NZ_CP023703|PILER-CR
AGCCTCAGGGGATCGGGTGGCGGGTATAG
>1.5|842804|32|NZ_CP023703|PILER-CR
CCCGCTCGAACTCCTCCCGGGGGTATCCCGGC

CRISPR arrays and Neighbor proteins around NZ_CP023703_1

CRISPR arrays

The CRISPR arrays of NZ_CP023703_1

>merge|NZ_CP023703|1|842709-842900|CRISPRCasFinder,PILER-CR
CACGCACACGCACACACGCGGGCGCGCGAAGCCTCAGGGGATCGGGTGGCGGGTATAGGCGTTCGCCGCACACACGCGTGCGCGCGTCCCGCTCGAACTCCTCCCGGGGGTATCCCGGCGCGTTCGCCGCACACACGCGTGCGCGCGACGAACGGCGCGCGCGGGCGCCGGGGGCACCCACGCGCGCGTGCC

>NZ_CP023703|1|1|842709-842900|CRISPRCasFinder
CACGCACACGCACACACGCGGGCGCGCG	AAGCCTCAGGGGATCGGGTGGCGGGTATAG
GCGTTCGCCGCACACACGCGTGCGCGCG	TCCCGCTCGAACTCCTCCCGGGGGTATCCCGGC
GCGTTCGCCGCACACACGCGTGCGCGCG	ACGAACGGCGCGCGCGG
GCGCCGGGGGCACCCACGCGCGCGTGCC

>NZ_CP023703|1|1|842717-842856|PILER-CR
CGCACACACGCGGGCGCGCGAAGCCTCAG	GGGATCGGGTGGCGGGTATAGGCGTTCGC
CGCACACACGCGTGCGCGCGTCCCGCTCG	AACTCCTCCCGGGGGTATCCCGGCGCGTTCGC
CGCACACACGCGTGCGCGCGA

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP023703.1|WP_150469748.1|832977_833502_+|PadR-family-transcriptional-regulator	unknown	unknown	gnl|CDD|224609
NZ_CP023703.1|WP_150469762.1|849546_851070_+|aldehyde-dehydrogenase-family-protein	unknown	unknown	gnl|CDD|143434
NZ_CP023703.1|WP_150469766.1|853934_854240_-|HypC/HybG/HupF-family-hydrogenase-formation-chaperone	unknown	unknown	gnl|CDD|376549
NZ_CP023703.1|WP_150469752.1|835882_836065_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP023703.1|WP_150469757.1|842901_844068_-|xylose-isomerase	unknown	unknown	gnl|CDD|237170
NZ_CP023703.1|WP_150469761.1|848071_849340_+|GAF-domain-containing-protein	unknown	unknown	gnl|CDD|225822
NZ_CP023703.1|WP_150469764.1|851738_852818_-|hydrogenase-expression/formation-protein-HypE	unknown	unknown	gnl|CDD|273984
NZ_CP023703.1|WP_150469755.1|840633_841977_+|esterase-like-activity-of-phytase-family-protein	unknown	unknown	gnl|CDD|379191
NZ_CP023703.1|WP_167534835.1|833487_834384_-|DUF2236-domain-containing-protein	unknown	unknown	gnl|CDD|378343
NZ_CP023703.1|WP_150469753.1|836301_839169_+|DEAD/DEAH-box-helicase	unknown	unknown	gnl|CDD|223627
NZ_CP023703.1|WP_150469763.1|851300_851684_+|hypothetical-protein	unknown	unknown	unknown
NZ_CP023703.1|WP_150469765.1|852810_853938_-|hydrogenase-formation-protein-HypD	unknown	unknown	gnl|CDD|237892
NZ_CP023703.1|WP_167534836.1|847388_847955_+|N-acetylmuramoyl-L-alanine-amidase	unknown	unknown	gnl|CDD|376556
NZ_CP023703.1|WP_150469750.1|834500_834833_+|hypothetical-protein	unknown	unknown	unknown
NZ_CP023703.1|WP_150469756.1|842105_842579_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP023703.1|WP_150469758.1|844184_845630_+|xylulokinase	unknown	unknown	gnl|CDD|198375
NZ_CP023703.1|WP_150469759.1|845644_846853_+|ROK-family-protein	unknown	unknown	gnl|CDD|224851
NZ_CP023703.1|WP_150469751.1|834970_835831_+|hypothetical-protein	unknown	unknown	unknown
NZ_CP023703.1|WP_150469747.1|832080_832839_-|alpha/beta-fold-hydrolase	unknown	unknown	gnl|CDD|223669
NZ_CP023703.1|WP_150469754.1|839165_840494_+|SWF-or-SNF-family-helicase	unknown	unknown	gnl|CDD|226729

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
NZ_CP023703.1|WP_150469748.1|832977_833502_+|PadR-family-transcriptional-regulator	gnl|CDD|224609	COG1695, COG1695, Predicted transcriptional regulators [Transcription].	6.16866e-17
NZ_CP023703.1|WP_150469762.1|849546_851070_+|aldehyde-dehydrogenase-family-protein	gnl|CDD|143434	cd07116, ALDH_ACDHII-AcoD, Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like. Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane. These proteins apparently require RpoN factors for expression.	0
NZ_CP023703.1|WP_150469766.1|853934_854240_-|HypC/HybG/HupF-family-hydrogenase-formation-chaperone	gnl|CDD|376549	pfam01455, HupF_HypC, HupF/HypC family.	1.18687e-29
NZ_CP023703.1|WP_150469747.1|832080_832839_-|alpha/beta-fold-hydrolase	gnl|CDD|223669	COG0596, MhpC, Predicted hydrolases or acyltransferases (alpha/beta hydrolase superfamily) [General function prediction only].	1.48023e-18
NZ_CP023703.1|WP_150469757.1|842901_844068_-|xylose-isomerase	gnl|CDD|237170	PRK12677, PRK12677, xylose isomerase; Provisional.	0
NZ_CP023703.1|WP_150469764.1|851738_852818_-|hydrogenase-expression/formation-protein-HypE	gnl|CDD|273984	TIGR02124, Hydrogenase_expression/formation_protein_HypE, hydrogenase expression/formation protein HypE. This family contains HypE (or HupE), a protein required for expression of catalytically active hydrogenase in many systems. It appears to be an accessory protein involved in maturation rather than a regulatory protein involved in expression. HypE shows considerable homology to the thiamine-monophosphate kinase ThiL (TIGR01379) and other enzymes.	1.57242e-171
NZ_CP023703.1|WP_150469755.1|840633_841977_+|esterase-like-activity-of-phytase-family-protein	gnl|CDD|379191	pfam13449, Phytase-like, Esterase-like activity of phytase. This is a repeated domain that carries several highly conserved Glu and Asp residues indicating the likelihood that the domain incorporates the enzymic activity of the PLC-like phospho-diesterase part of the proteins.	7.23682e-44
NZ_CP023703.1|WP_167534835.1|833487_834384_-|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.	2.2465e-11
NZ_CP023703.1|WP_150469753.1|836301_839169_+|DEAD/DEAH-box-helicase	gnl|CDD|223627	COG0553, HepA, Superfamily II DNA/RNA helicases, SNF2 family [Transcription / DNA replication, recombination, and repair].	3.57723e-125
NZ_CP023703.1|WP_150469765.1|852810_853938_-|hydrogenase-formation-protein-HypD	gnl|CDD|237892	PRK15062, PRK15062, hydrogenase isoenzymes formation protein HypD; Provisional.	0
NZ_CP023703.1|WP_150469758.1|844184_845630_+|xylulokinase	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.	0
NZ_CP023703.1|WP_150469759.1|845644_846853_+|ROK-family-protein	gnl|CDD|224851	COG1940, NagC, Transcriptional regulator/sugar kinase [Transcription / Carbohydrate transport and metabolism].	1.63287e-49
NZ_CP023703.1|WP_150469761.1|848071_849340_+|GAF-domain-containing-protein	gnl|CDD|225822	COG3284, AcoR, Transcriptional activator of acetoin/glycerol metabolism [Secondary metabolites biosynthesis, transport, and catabolism / Transcription].	1.12719e-25
NZ_CP023703.1|WP_167534836.1|847388_847955_+|N-acetylmuramoyl-L-alanine-amidase	gnl|CDD|376556	pfam01510, Amidase_2, N-acetylmuramoyl-L-alanine amidase. This family includes zinc amidases that have N-acetylmuramoyl-L-alanine amidase activity EC:3.5.1.28. This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls (preferentially: D-lactyl-L-Ala). The structure is known for the bacteriophage T7 structure and shows that two of the conserved histidines are zinc binding.	2.95588e-38
NZ_CP023703.1|WP_150469754.1|839165_840494_+|SWF-or-SNF-family-helicase	gnl|CDD|226729	COG4279, COG4279, Uncharacterized conserved protein [Function unknown].	2.08673e-31

Protein sequences

>NZ_CP023703.1|WP_150469756.1|842105_842579_-|hypothetical-protein
MAMPPVPPKPPGPPGDTPPPGGFGPPTPDFGPGGGDRPPSGPPPGPSGPSDGPRRRRSLLFAVLALLAAAAVVFAVVLVASGNDDSPDGDPPPGKGSSPAPSLSLPSELPSGFPTELPTQLPSELPSQFPSDLPSDLPTALPSDLESLLPSLAELLP
>NZ_CP023703.1|WP_150469755.1|840633_841977_+|esterase-like-activity-of-phytase-family-protein
MSPHATGRRAVHRSVAAGVPLAVLAALVTAGPASAHTPSGDAHVTRTATLGDIPLGAFSNALLPGTVADDRGVDLGGIGSDIYPAGRKGEYWTVTDRGPNGQIKVDGKKRRTFPVPGFDPAIVRIKVSGDTVKVLASIPLTTSSGRPVTGLPNQAGRDEAPFSHDAATPLSYNPNGLDTEGIVRAADGSFWLVDEYGPSLVHVSARGRVLARYVPEGLNLTGADYPVVEALPEVLLHRKINRGLEGLAQLPGGDLVLAMQSPLSLPDTDAGEASRTVRLLRFSPKKKAVTAEYAYRFDPVEVVDPSEDDTSELKVSSVVAVGGDRLLVEERTDKAARLHLVRLDRKADILGGRWDDEATSPSLEQLADPSASGVPVLSKRLVVDLGTVAGVPGKIEGVALVNRDTLALINDNDFGMTDGTGAFDAQGRLVDSGIETKVTYVRLPKGL
>NZ_CP023703.1|WP_150469754.1|839165_840494_+|SWF-or-SNF-family-helicase
MNAYDSERERTFEALPPAHGRGFAQSWWGRAWLTALEGGALDGEQVRTGRRLARAGAVGAVSVRPGRITAVVQDRDGTGYRADVLLDVLTDAQWDRFLDLTVERAGHVAALLDREMPPHLVEDVETAGIELLPGLGDLEAECGCDAWDHCGHTAALCYQVARLLDQDPFVLLLLRGRAEQSLLADLQARSTAVPTEPEPAPQEGVDAVEAYLAGHVLPPLPAVPELPEQPGVPPTLDTEAPPPGDVEPAALETLAARTAAQAHALLAEAVRGGAERRGPAWALTVGEDAVRLAAGLAGDGDGDGDTDSTRSVLDRLAAGTGRSREQLALAVRAWRTGGVAALAVLEEEWAVEGEALARARAALDTAWEEGERPVLRVRGNRWTVAGPAGQLRLGRDGRWWPYRKERGRWVPAGDAAQDPATALAAVGSEEAEGAEGVAEALS
>NZ_CP023703.1|WP_150469753.1|836301_839169_+|DEAD/DEAH-box-helicase
MQWVSAETPSEIVELARCPAVFVPGVPARTGRVAFWRPDGATAPVPAPGSGSVEDLSVVRPTSAGVELVRVSAVLLPVHEALDVLTRARTVPDAHRAASFWAAAALAALEFTARGLLLPGLSPDDHDAWRVGPLGPDDVEGIRRLAAAMPPEAHALPLTGAPPLRLPDQERLLRAFLDAVADTLPRSPAAPLMTGGPAYAASQPLHVPQLRSWAADVAAGHDAGVRVSLRIEVSGLSPAAPEAVAAFRAVPQVHSVSDPSLVADAAEIWQDAGAGHQAFGPRARMDALLALRRAARAWPALTPLLSAAVPDAVDLLDEEVADLLGEGSRALAAAGVQVHWPRELARTLTARAVVGPPDDVPGPDRSGSDAPSFLSADALLSFSWSFALGGQSLTREELDRLAEANRPLVRLRDQWVLIDPRELRRAQGRQDRKVSPIDALGAALTGSTEVDGRRVEVQPTGWLAALRERLTRPDDQEPVEQPAALDATLRDYQRRGLGWLARNTSLGLGCCLADDMGLGKTITLIALHLHRRTDPSAAGPTLVVCPTSLMGNWQREIERFAPGTPVRRFHGPRRDLADLADAEFVLTTYGTLRLDAGRLGEVPWGLVVADEAQHVKNPYSETARALRSIGARARVALTGTPVENNLSELWAILDWTTPGLLGRLGTFRTRYARAVEAGGDPAAAERLARLVSPFLLRRRKSDPGIAPELPPKTETDRPVFLTKEQTGLYEAVVRETLTAIAEADDMARRGLVVKLLTGLKQICNHPAQYLKEDRPRTAGRSGKLELLDELLDTILAEGAGVLVFTQYVGMARVLERHLAARGVPTQFLHGGTPVAAREAMVARFQDGEVPVFLLSLKAAGTGLNLTRAEHVVHYDRWWNPAVEAQATDRAYRIGQTRPVQVHRLIAEGTIEDRIADMLRRKQRLADAVLGSGEAGFTELSDAELAELVELRGGTR
>NZ_CP023703.1|WP_150469752.1|835882_836065_-|hypothetical-protein
MSKNAKIAAGGVAVGLLLLIWLPWWAALLIMVGVPAAAYLMLDPSQRRRLRRVTRKELGR
>NZ_CP023703.1|WP_150469751.1|834970_835831_+|hypothetical-protein
MAGTEEDAVAAADDALYVLTAVLLTPAKFPSVLGDDYPEACAALGLAPLADGYGLVLGQDGEGARWTVAIDDVSLVAVAIASWDCGMEYDLSPDERTVVAALPGWPLAVAVAAPGVPAPHDPDPEAAGGPALRPPDTTTWGPAQRRLGADEIALQWALWREQIDDAEFAPAGAGSEAAGTTEVDESAEDGEGDNSPAGRGGVRRVLAEVRAYVETPPPLGRVRSSFAPGDARTLRADGPGWSLVARTDDIAFVLLDDEPGEVLPVGRGPELPGLLDALDKMAVRPS
>NZ_CP023703.1|WP_150469750.1|834500_834833_+|hypothetical-protein
MFDSVRGIWGRFLDAARGRARADGEERSAGAPRKSGGKRAPNLFEAAAAYVSACAEDDQERIEEAAGWVSPEALSFGVNELACRAVIALARERDESPRTVARALLGLPSA
>NZ_CP023703.1|WP_167534835.1|833487_834384_-|DUF2236-domain-containing-protein
MKRFERLGRIRRMDPVAQASEIYRLTVAYEFPWDFTRALELALYRTYAVPSIGALLARTAELTDRTQKRYDDTSLLLDAVVEHGFDSDEGRTAVRRINRMHGSYDISDDDMRYVLCTFVVMPKRWIDAYGWRRLSRHEIVASTVHYRTLGHRMGIKDIPSSYEEFEACLDAYEAAHFGWDEGARAVADATLDLVASWYPRPLAPVLRTATLALLDEPLLRAFRYTAPAPTTRALVRRAVRARGRAVRLFPPRRAPHYARQNWEIKSYPEGYRLDELGTRPVSGLRGCPVRHGDGSAVQ
>NZ_CP023703.1|WP_150469748.1|832977_833502_+|PadR-family-transcriptional-regulator
MLELAILGFLYDTPLHGYELRKRISALTGHVRPVAESTLYPAIKRLEKAGLLVRATEPGAVAAPRHVLSLTDEGRSALRRRLTEPDERDITDENRWFTVLAFLRHLDDAPAQAAVLRRRLAFLEEPASFFYDDDRALRAEELDDPFRRGVLTIARATSRAELRWLRATLESLDG
>NZ_CP023703.1|WP_150469747.1|832080_832839_-|alpha/beta-fold-hydrolase
MQQAEFGQGGSRIRWTEAPGEEPARVYVHGLGAASAVYHAHVAARPELAGRRSLFVDLPGHGISDRPQDFGYTLEEHADAVAAALDAAGVTGAELVAHSMGGSVAIVLADRRPDLVARLVVTEANLDAFPPSTAGSSGIASWTEEEFVDGGHARVLEKVGPLWAATMRLADPRGLHRSAVGLRRGSEPVMREILAGLDTIERVYLQGELSGPLDGAEALEAAGVRILTVPAAGHNAMFDNPDAFARAVAADA
>NZ_CP023703.1|WP_150469757.1|842901_844068_-|xylose-isomerase
MSYQPTPDDRFTFGLWTVGWQGRDPFGDATRAALDPVETVQRLAELGAHGVTFHDDDLIPFGSSDSEREAHIKRFRQALDDTGMKVPMATTNLFTHPVFKDGAFTANDRDVRRYALRKTIRNIDLAAELGAKTYVAWGGREGAESGAAKDVRVALDRMKEAFDLLGEYVVEQGYDLRFAIEPKPNEPRGDILLPTVGHALAFIERLERPEMYGVNPEVGHEQMAGLNFPHGIAQALWANKLFHIDLNGQSGIKYDQDLRFGAGDLRSAFWLVDLLETAGYSGPLHFDFKPPRTEDLDGVWASAAGCMRNYLILKERAAAFRNDPEVQQALRDSRLDELAQPTAADGLQGLLADRGAFEDFDTEAAAARGMAFERLDQLAMDHLLGARG
>NZ_CP023703.1|WP_150469758.1|844184_845630_+|xylulokinase
MSAAEGPLVVGVDTSTQSTKVLVVDAATGQVVASGQAPHTVSSGAGRESDPRQWWDALHEALRQCGDAAHEAAAVSIGGQQHGLVTLDERGEPVRPALLWNDVRSAPQARRLTEELGGAKFWAERTGSVPAASFTVTKWAWLAEHEPEALRATKAVRLPHDYLTERLTGEGTTDRGDASGTGWWASGTESYDAEILAHVGLDPALLPRVVRPGEVAGTVRDSHDLPFSKGTLVAAGTGDNAAAALGLGLRPGTPVLSLGTSGTVYAVSKRRPTDPTGTVAGFADAHGDWLPLACTLNCTLAVDRIATLLGLDREAVEPTTALTLLPYLDGERTPNLPNASGLLHGLRHDTTAGQLLQAAYDGAVHSLLGALDLVLDEDADRSAPLLLIGGGARGRAWQQTVRRLSGRPVQIPEAKELVALGAAAQAAGLLTGEDPAAVARRWNTARGPVLDPVERDEAALARIAGVLSDAAPLLERGTDTH
>NZ_CP023703.1|WP_150469759.1|845644_846853_+|ROK-family-protein
MSAPPHEARPTGPGRALPDTQQGMRRRNLARVMHAVSAEGPLSRAAVASHIGLTRAAVSTLVDELIRTGLIEELGPERPGRVGRPGSALAVSGRGPAGIGAEIGVDHLAVCAVDLRGEVRARAVRHGTNRGRAPEPVLRELTGLVRRVVADAEREGLWPAGLAVAVPGLVGRDARTVVRAPNLDWQDVDLGALLPGEFPLTVDNEANFGGLAELWLGAATPRDFLHVSAEIGIGAALVVDGSLLRGTRGFAGELGHVPVHPDGPDCGCGSRGCLEQYAGEEAVLRAAGLELGEDRVGLLARRAADGDEEVRRALREAGTALGVALTGALNLLDPEAVVLGGALAGLAPWLLPSLESELARRTAGPPCPVSVSRLGPEGPLLGAAHSVVRAVLDDPAGVAGRG
>NZ_CP023703.1|WP_167534836.1|847388_847955_+|N-acetylmuramoyl-L-alanine-amidase
MSPRPRKAPTVERTRPLPLLDRRRILKGAALAAVPYALLPSNYTASSRPTTYTVDRVVIHVTQTTYAQALSVFQNPKKRVSAHYVVRSADGHVAQCVREADVAWHAGNWDHNTRSIGIEHEGWVDRPAYFTNALYERSARLTASVCDRYGIPKDRAHIIGHHEVPGTDHTDPGPDWDWVRYVRLVNFA
>NZ_CP023703.1|WP_150469761.1|848071_849340_+|GAF-domain-containing-protein
MTDPWVALEPGADPAERVRVLRRAHDAFTAAGTVPRPVRSVVADSWRRSARAGVGPDGTASVELTDADLGTYRSEHPLTRVMPLFRELMGTFAADGKHLLAVCDAHGRLLWVEGHPATRRQAERMNFVPGARWAETSVGTNAPGTAVALDRPVQVFAAEHFIRRVQPWTCAAAPVHDPRTGQVLGAVDITGGDGLAHPHSLAFVQAVARAAESHLALLAPARPETDPPRLTVLGRDEAWLAAGGRRLRLSRRHSEIMVLLARHPEGLTGDELLCAVYEDESVTPVTLRAELARLRGVLGPGLVASRPYRLTVPVESDIAVVERRLAAGAVTAAVAAYSGPPLPASQAPAVVRLRSRLADSLRAALIAGRDPDLLADWAHSPWGEEDLDVWRALASARPTAAVRARLAALESELAAPASWTRG
>NZ_CP023703.1|WP_150469762.1|849546_851070_+|aldehyde-dehydrogenase-family-protein
MTRYAAPGTEGSIVSYQARYDHFIGGEYVAPARGQYFENPSPVNGLPFTEVARGTAEDVERALDAAHAAAPGWGRTSATERSDILLKIADRMEAYLEPLAVAESWENGKPVRETLAADIPLAIDHFRYFAGAVRGQEGALSEIDEDTVAYHFHEPLGVVAQIIPWNFPILMATWKLAPALAAGNAVVIKPAEQTPVSLHYWMSLVADLLPPGVVNIVNGFGEEAGKPLASSPRVAKIAFTGETATGRLIMQYAAENLKPVTLELGGKSPNIFFDDVWEKDDDLRDKALEGFTMFALNQGEVCTCPSRGLIQRGNYAEFMAAAVARTELIKPGHPLDTDTMIGAQASGDQLTKILSYIDIGRQEGAKILTGGERADYDGELKGGYYVQPTIFEGDNRMRIFQEEIFGPVVSVASFDDFDDAVKIANDTSYGLGAGVWTRDINTAYRAGRAIQAGRVWTNCYHAYPAHAAFGGYKQSGIGRETHKMMLEHYQQTKNLLVSYSPKKLGFF
>NZ_CP023703.1|WP_150469763.1|851300_851684_+|hypothetical-protein
MPKKPRSSEPPHGKGPSRHQGTGQHGWSPDVDETRQQDNPSAHRSFRPEQAGERGKGRSMSPEETKPVPGDTAKSRSASGEKYGDADEKGRRDTGRKGRSQRPSGTKDASATTGVDPQDPPSGRRPG
>NZ_CP023703.1|WP_150469764.1|851738_852818_-|hydrogenase-expression/formation-protein-HypE
MSDTTDLPGPALDVEAWTCPAPLRDRPRVVMGHGGGGVLSAELVQQIFAPAFGGEVLAQMGDAAVLSVGGARLAFSTDSYVVRPLFFPGGSIGDLAVNGTVNDLAMSGARAAYLSCGFILEEGVELDVVTRVSEALGAAARTACVEVATGDTKVVEAGHGDGIYINTAGIGLVPAGVDLRPQRVVPGDVVIVSGAIGVHGVAVMSVREGLEFGVEIKSDCAALGGLVDAMLAVTPDLHVLRDPTRGGLAAALNEIAQASGTGVVIRERDVPVPPAVANACAILGLDPMYIANEGKLVAFVPREHADAVLGVMRAHPLGADSVIIGEAVEGHPGMVVARTGLGGTRVVDLPIGEQLPRIC
>NZ_CP023703.1|WP_150469765.1|852810_853938_-|hydrogenase-formation-protein-HypD
MKYIDEFQDPELARRLLDDIHATVTRPWALMEVCGGQTHSIIRHGIDQLLPDKIELIHGPGCPVCVTPLEVIDKALEIASRPEVIFCSFGDMLRVPATGRDLFQVRGEGGDVRVVYSPLDALRIAQQNPDREVVFFGIGFETTAPPNAMTVHQARKLGIPNFSMLVSHVRVPPAIEAIMSSPSCRVQGFLAAGHVCSVMGMGEYPELAERFRVPIVVTGFEPLDILEGVRRTVRQLERGEHTVDNAYARAVRAEGNAAARAMLEDVFDVTDRAWRGIGVIPQSGWRLAPKYRAYDAEYRFSVEGIRTQEPAECRSGEVLQGLLKPHECEAFGTLCTPRTPLGATMVSSEGACAAYYLYRRLEMPAAKAQEATPVV
>NZ_CP023703.1|WP_150469766.1|853934_854240_-|HypC/HybG/HupF-family-hydrogenase-formation-chaperone
MCLAVPGRVLDIEERDGTRMATVDFGGVVKEVCLEYLPDLQVGEYAIVHVGFALQRLDEESARQTLELFAELGLLQEEFGDAWEMSATEAGVDPVEEVRNQ

Crispr_ID: NZ_CP023703_2

• CRISPR_ID: NZ_CP023703_2
• CRISPR_location: 1198420-1198496
• CRISPR_type: Orphan
• Repeat_type: NA
• Spacer_info: 1 spacers

Consensus repeat of NZ_CP023703_2

Consensus_repeat	Method
TCGTGGCGGTACGCCGACGCTGAC	CRISPRCasFinder

spacers of NZ_CP023703_2

>2.1|1198444|29|NZ_CP023703|CRISPRCasFinder
GGCCGGCGCCGCCAGGCCACGCCCGGCCC

CRISPR arrays and Neighbor proteins around NZ_CP023703_2

CRISPR arrays

The CRISPR arrays of NZ_CP023703_2

>merge|NZ_CP023703|2|1198420-1198496|CRISPRCasFinder
TCGTGGCGGTACGCCGACGCTGACGGCCGGCGCCGCCAGGCCACGCCCGGCCCTCGTGGGGGTACGCCGACGCTGAC

>NZ_CP023703|2|2|1198420-1198496|CRISPRCasFinder
TCGTGGCGGTACGCCGACGCTGAC	GGCCGGCGCCGCCAGGCCACGCCCGGCCC
TCGTGGGGGTACGCCGACGCTGAC

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP023703.1|WP_150470008.1|1196051_1196804_+|5-oxoprolinase-subunit-PxpA	unknown	unknown	gnl|CDD|235446
NZ_CP023703.1|WP_150470002.1|1184100_1185660_+|choline-oxidase	unknown	unknown	gnl|CDD|235000
NZ_CP023703.1|WP_150470019.1|1208584_1209352_+|glycerophosphodiester-phosphodiesterase	unknown	unknown	gnl|CDD|176504
NZ_CP023703.1|WP_150470012.1|1199365_1200733_-|glycosyltransferase	unknown	unknown	gnl|CDD|340842
NZ_CP023703.1|WP_073492896.1|1204426_1204621_+|hypothetical-protein	unknown	unknown	unknown
NZ_CP023703.1|WP_150470015.1|1203770_1204163_-|ankyrin-repeat-domain-containing-protein	unknown	unknown	gnl|CDD|293786
NZ_CP023703.1|WP_150470006.1|1193007_1193712_-|FCD-domain-containing-protein	unknown	unknown	gnl|CDD|224715
NZ_CP023703.1|WP_150470005.1|1191343_1192870_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP023703.1|WP_150470007.1|1193886_1195188_+|MFS-transporter	unknown	unknown	gnl|CDD|340929
NZ_CP023703.1|WP_150470013.1|1200729_1201857_-|glycosyltransferase	unknown	unknown	gnl|CDD|340842
NZ_CP023703.1|WP_150470004.1|1190421_1191297_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP023703.1|WP_150470018.1|1207910_1208588_+|hypothetical-protein	unknown	unknown	gnl|CDD|225239
NZ_CP023703.1|WP_150474402.1|1195223_1196039_+|putative-hydro-lyase	unknown	unknown	gnl|CDD|180100
NZ_CP023703.1|WP_150470001.1|1182521_1184090_+|amino-acid-permease	unknown	unknown	gnl|CDD|132469
NZ_CP023703.1|WP_150470011.1|1198508_1199369_-|SGNH/GDSL-hydrolase-family-protein	unknown	unknown	gnl|CDD|238870
NZ_CP023703.1|WP_150470017.1|1206312_1207812_-|aminotransferase-class-I/II-fold-pyridoxal-phosphate-dependent-enzyme	unknown	unknown	gnl|CDD|224089
NZ_CP023703.1|WP_167534806.1|1204674_1206243_+|hypothetical-protein	unknown	unknown	gnl|CDD|238540
NZ_CP023703.1|WP_150470014.1|1202025_1203447_-|HEAT-repeat-domain-containing-protein	unknown	unknown	unknown
NZ_CP023703.1|WP_150470003.1|1185743_1190357_-|hypothetical-protein	unknown	unknown	gnl|CDD|173412
NZ_CP023703.1|WP_150470009.1|1196800_1197427_+|carboxyltransferase-domain-containing-protein	unknown	unknown	gnl|CDD|367142

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
NZ_CP023703.1|WP_150470008.1|1196051_1196804_+|5-oxoprolinase-subunit-PxpA	gnl|CDD|235446	PRK05406, PRK05406, 5-oxoprolinase subunit PxpA.	2.37901e-133
NZ_CP023703.1|WP_150470002.1|1184100_1185660_+|choline-oxidase	gnl|CDD|235000	PRK02106, PRK02106, choline dehydrogenase; Validated.	1.57383e-152
NZ_CP023703.1|WP_150470019.1|1208584_1209352_+|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.	2.0511e-93
NZ_CP023703.1|WP_150470012.1|1199365_1200733_-|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.	3.42735e-63
NZ_CP023703.1|WP_150470015.1|1203770_1204163_-|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.	3.75471e-18
NZ_CP023703.1|WP_150470006.1|1193007_1193712_-|FCD-domain-containing-protein	gnl|CDD|224715	COG1802, GntR, Transcriptional regulators [Transcription].	3.81856e-35
NZ_CP023703.1|WP_150470007.1|1193886_1195188_+|MFS-transporter	gnl|CDD|340929	cd17371, MFS_MucK, Cis,cis-muconate transport protein and similar proteins of the Major Facilitator Superfamily. This subfamily is composed of Acinetobacter sp. Cis,cis-muconate transport protein (MucK), Escherichia coli putative sialic acid transporter 1, and similar proteins. MucK functions in the uptake of muconate and allows Acinetobacter calcoaceticus ADP1 (BD413) to grow on exogenous cis,cis-muconate as the sole carbon source. The MucK subfamily belongs to the Metazoan Synaptic Vesicle Glycoprotein 2 (SV2) and related small molecule transporter family (SV2-like) of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	6.90797e-141
NZ_CP023703.1|WP_150470013.1|1200729_1201857_-|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.	6.48867e-109
NZ_CP023703.1|WP_150470018.1|1207910_1208588_+|hypothetical-protein	gnl|CDD|225239	COG2364, COG2364, Predicted membrane protein [Function unknown].	3.01862e-43
NZ_CP023703.1|WP_150474402.1|1195223_1196039_+|putative-hydro-lyase	gnl|CDD|180100	PRK05463, PRK05463, putative hydro-lyase.	4.9045e-174
NZ_CP023703.1|WP_150470001.1|1182521_1184090_+|amino-acid-permease	gnl|CDD|132469	TIGR03428, ureacarb_perm, permease, urea carboxylase system. A number of bacteria obtain nitrogen by biotin- and ATP-dependent urea degradation system distinct from urease. The two characterized proteins of this system are the enzymes urea carboxylase and allophanate hydrolase, but other, uncharacterized proteins co-occur as genes encoded nearby in multiple organisms. This family includes predicted permeases of the amino acid permease family, likely to transport either urea or a compound from which urea is derived. It is found so far only Actinobacteria, whereas a number of other species with the urea carboxylase have an adjacent ABC transporter operon.	1.81905e-162
NZ_CP023703.1|WP_150470011.1|1198508_1199369_-|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.	9.63679e-49
NZ_CP023703.1|WP_150470017.1|1206312_1207812_-|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].	9.52583e-90
NZ_CP023703.1|WP_167534806.1|1204674_1206243_+|hypothetical-protein	gnl|CDD|238540	cd01120, RecA-like_NTPases, RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H+ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.	0.00241234
NZ_CP023703.1|WP_150470003.1|1185743_1190357_-|hypothetical-protein	gnl|CDD|173412	PTZ00121, PTZ00121, MAEBL; Provisional.	5.40449e-13
NZ_CP023703.1|WP_150470009.1|1196800_1197427_+|carboxyltransferase-domain-containing-protein	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.	8.01439e-71

Protein sequences

>NZ_CP023703.1|WP_150470009.1|1196800_1197427_+|carboxyltransferase-domain-containing-protein
MRVLPVGEDALLVEVASGEDAQALHAELLRRRAEGSLSVREIVPAARTVLLDGLADPARWAAELTGASVPPAPSRTGAAIELAVRYDGPDLADVAAHWGVSAQEVVRIHAATEFRVAFCGFAPGFGYLTGLPPRYDVPRRATPRTAVPAGSVALAGPYTGVYPRSSPGGWQLIGTTRAVLWDHARVPAALLTPGTRVRFVAVDGAGAV
>NZ_CP023703.1|WP_150470008.1|1196051_1196804_+|5-oxoprolinase-subunit-PxpA
MIDLNADLGEGFGRWELTDDERLLSVVTSANVACGFHAGDAVTMRRVCELAAERGVTIGAQVAYHDLAGFGRRAMDVPPAELAAEVAYQIGALEVFARAAGARVAYVKPHGALYNRVVHDEEQATAVIDGVLLADPALPVLGLPGSRLLEVAGKAGLPAVTEAFADRAYTEEGTLVPRGQDGAVISDPDVVVERSLGLARLGEVDSLAGTRIEVRARSLCLHGDTPGAVELARRVRRRLEESGVRVEAFA
>NZ_CP023703.1|WP_150474402.1|1195223_1196039_+|putative-hydro-lyase
MVQDRPVTLVDEHAHAWSPTTARSRFRDGLTGPTAGVAAGHTQANLISVPADWAYDMLLFCQRNPKPCPVLDVTDAGSWTTVLAEGADLRTDLPRYRVWRDGELVDEPTDVRGYWRDDLVSFLIGCSFTFEWALAGAGVPLRHVEQGRNVPMYVTDRQCRPAGRLHGPLVVSMRPVPPEHLAAAIRESSLLPAVHGSPVHCGDPSGLGIDDLGHPGFGEPVDAEPDDIPVFWACGVTPQAAVMASRPPFALTHAPGQMFLTDARDEQYRVA
>NZ_CP023703.1|WP_150470007.1|1193886_1195188_+|MFS-transporter
MSTTPPPQAPSTATHPPAAERASDDGALAWLRALGPRGRRAFAGAFGGYALDSYDYFTLPLSMVALAAYFGLDSGQTGLFTTVTLVASAVGGALAGVLADRIGRVKALMITVITYAVFTVACGFAPTYETLLLFRALQGLGFGGEWAVGAILVAEYASAQHRGRTLGAIQSSWAVGWGLAAIMYTLVFSVFGDDVAWRVMFWTGALPALLVVWMRRRVQDAPTAVAARERNAGKGSFAAIFRGPLLRTTIFAGLLSTGVQGGYYTLATWVPTYLKSERGLSVVNTGGYLTFLISGAFLGYLTGGYLTDRLGRRRNIWLFAVLSAVCILAYANIPSGADTLLLLLGFPLGFCMSAIFSGFGSYLSELYPTAVRGTGQGFTYNTGRAVGAVFPTTVGFLADSWGVGGALVFGAIGYGIAALALLGLPETRGKELE
>NZ_CP023703.1|WP_150470006.1|1193007_1193712_-|FCD-domain-containing-protein
MAEQLAGLADDRALLGRTSTAERVADILRSRIADGYFPPGTRLSEDSIGGALGVSRNTLREAFRLLTHERLLVHELNRGVFVRVLTVEDVEDIYRTRALVECAVVRGLGKPPYALGNLAEAVEEGQRAARESDWKSLGTANIHFHRELVALAGSERTDELMRSVFAELRLAFHVVDDPRRLHEPYLARNRQILRALEAGDGAEAEKLLAVYLGDSRERIVEVYRRRVGDDPSDG
>NZ_CP023703.1|WP_150470005.1|1191343_1192870_-|hypothetical-protein
MTSPASTDRVPPQLSAGPRPAPGPAADEGLARRLRALACTAPIHDLDARKANLAGEYSVYGMAEIALAAIDLVTLNMDFDTGADHDQIVARLIPRIAAQAPGRQAEEHERVARWVLENLINVGSVDRGFRAVYGTFAPDGTYVRRDYDFKLIEEVPGYGGTVYLRTTDEAVNVLVGALDTDVTSAQIAAEVKLEVLIRRGRLADAQLAAEQARYRTVQYSETLRRALEATRRNVRAVDWLNAVPDMIAEALDHVADRYRHENAILTNIRKARDEIEDAENKRRAAELVDIVKDCIRRHTQLQSRLLEAGPLFRAEQDRQAFATPMTSSGTDLYGHLVVPVLPLPLEQAVRVTDAYFARGTGLRTPVSVRVGDLVDLLLTPPVERENLGAEMPEPDLIATPDDSRFSEEQLAAAKELLDLPADAPRRLSGLLAEARRRDPELPYLVALLAVHAASPAVGTAYRQGEQKLLFAVDDGTELDDSEFGGADLIVGMALLDAAGMAADRTEAA
>NZ_CP023703.1|WP_150470004.1|1190421_1191297_-|hypothetical-protein
MTEYVDRSEPETVAPASAAVTPADAADAARLVAFGLQPRLQPARDQEYADLLRRYREDPPFARLADAVATGLGLIVLEVSPRAGMAVTAAEDSVFAVRMGDYARRTSADSGDRFLHGLAHLAVAAMAFPRPEDLADDGYIGRVSVNGVDAFVRQACRRLEERAEEQGENTDPATDAPGLEAAWRIWVRRSAAGATKDARRLAGSTTGIVGKAVAFLTESGFLQRTGDDNGGTYRTTARYQLQVRDMAASAAMAELLELGIVPVTDGTPTLLPPEESDDLELVAGAGLPFHS
>NZ_CP023703.1|WP_150470003.1|1185743_1190357_-|hypothetical-protein
MYELSRVRLYSIGPAGARYADTVLDLRGVGEVVPDPAPAQAEFFEDEPVGPPRRPAPAGVLFLENGGGKSVLLKLIFSVMLPGHRNTLGGASSGVLRKFLLADDCGHVALEWQHVLTGECVVVGKVSEWRGRQVSNDPRKFAEAWYSFRPGPGLSLDNLPVAESTAVRPSAEGQSGAQGRRRTMKGFRDALTDAGKAYPHLEVHWEEIHDRWIEHLGELGLDPELFRYQREMNADEGEAAGLFAVKKDSDFTDLLLRAVTDTRDTDGLADLVGGFGNKLGRRAELIAERDFTAGSVDLLGRIVEAADTRARAREVHAGAERRTRTLARRLSARGLRERTRAADLAQRVTAAAYAVTHSESARERSALIAAELAFRHASLALAAAEKSAAAQKRELAEARTLHAAWQAAEVSLRQRAAADRVARVSAAIQEAERDAAPALAARAKAAVDLVRALHGAAGSAETLANEEEERSAALQEVGEAAHRDATSAATEAQRARSEAGHLRQRLTEVEQETAEAVRAGWLDDSAPDADPARAALAASDAEKSAVAAWDTAREASRKAAEHAREAASAESRAELTAARAADAATGARRSYEAERGLAEDLAAEERLAELLGVTGASTPRIIPQPRQEDEGDGTGLTPEDLDRYADDLRELLDDTVSSAERQLFDLRTAAADDSRILGALGDGGLLPPGPDVLATVEYLGEHGIPALPGWRYLAQAVDPVDHARVLAARPELVDGVIITDPASHARAREALGEAALLPRSAVAVGTAAALLAPTPAPGTDAGDVFLVPPNPAMHDEHAADEERQALRARAAERDEEIRRLAARLGKDRELSARLSSWRTGCPAGRLTELARTAEEARAFAEESEAELAEARTVRAEADEAAAEAAQARDERQEAAQKARRAADALAGLAFRLRERAGWQVKLRELADEAAESEARAQACLERARAADEDRRAAQRAADDSRRTARALRAERSEIAGAPDDVPEPGPGAPKASLPALREAYRAASQLYEKVGVGADLRAEQARAEGDESAALAELDRLSNKVRTRAEQLLQSPDGSDGPSRQAASARAEELVQLLETRVSTASEHLGRLRGEAERHAPEDGDAHTELPAELQPRDAGHAQALLRTATAELASRTETLAQAREAHAELLDAHRAAEDAAGGFDEIAAMLRDLLREHTPEEEQEAPEPYPGTLEEARGSAAEARRSLRGCAADLSAAEAAVREASDILVRHANSTRYEQVRTPARQQIRELPAAALPEHAQKWADAFAPRLRVLTDELAQLERNRDSIVDRLRGLVESALATLRSAQRLSRLPEGLGEWSGQEFLRIRFEEPDQATLTERLGEVVDEATRAAVKKNSDLRRDGMSLLLRGVGAALQPKGVAVEILKPDAVLRAERVPVGQMGDVFSGGQLLTAAIALYCTMAALRSNDRGRDKHRYAGTLFLDNPIGRANATYLLELQRAVSDALGVQLLYTTGLFDTTALAEFPLVIRLRNDADLRAGLKYISVEEHLRPGLPQVSTGEAGHSEITATRMYKRTAPSTP
>NZ_CP023703.1|WP_150470002.1|1184100_1185660_+|choline-oxidase
MSIDEFDYVVVGGGTAGNVVAARLSEDPAVTVCVLEAGPSDVGDDDILRLDRWMGLLESGYDWDYPVEPQASGNSFLRHARAKVLGGCSSHNSCIAFWAPAEDLDDWAAAGCTGWSAADLFPLYRRLESNDAPGDHHGRTGPVRLRTLKGEDPCGTALLEACAQAGIPTTAFNSGTTVVRGANWFQINSDENNIRQSSSVAYLHPVMGKRPNLEVRTGVRAKKLVLDGRRCVGARYLAPDLIHTRTVRARREVIVSCGSVDSPKLLMLSGIGPAAHLREVGVEVAVDAPGVGENLQDHPEGVIMWEARQPMPATSSQWWEAGIFYDTEPGLDRPDLMFHYGSVPFDMNTARHGFPTSENAFCLTPNVTRARSRGTVRLRTRDYRDKPMVDPRYFTHEHDVRVMTYGLRLARRIASQSALSGWAGAELAPGPDVRTDDELLDYIHKTHNTVYHPSCTVKMGADDDPSAPLDARLRVKGVEGLRVADGSVMPDLVTVNPCVTTMMIGEKCADLLKEDARRL
>NZ_CP023703.1|WP_150470001.1|1182521_1184090_+|amino-acid-permease
MTTTAEPPSDKQGQDDAELAEFGYKPELRRTLGNFHTFAAGISYISILTGTFQLFYFGYGSGGPAYWWSWPMVFVGQFTVALCFAELAARYPVAGSVYNWSKKIGNPHLGWLAGWMMLIASIVSIAAVALAYQLTLPQISSFFQFVGDGTGTYDVATNAVILAAVLILFTTLVNAFGVKLTATINTAGVFIELIATVVLIVLFAAHITRGPQVVMDTQSTGTGYGAGYLGAFLVASLASAYVMYGFDTAASLGEESLDPSRNAPRAIIRAIVASFVLGGLILLLALMSVSSLKGEKLSTDGLQFIVLDVLGPTAGKAMLWCVLIAVTVCALAVHTAAIRLAFAMARDNNLPASSRLARCHPRFQTPVLPTVIIGILALAILVVNIRQPQIFTVVTSIGIIMIYLAYLGVTAPMLVARLRGKWQPAGDGKFSLGRWGLPVNILAVVWGAAMTINLIWPRASVYNATAPFHWYLQWGAVLFVAVIAGGGFAYYWFVQRHKTGVLAEHRLEAPAATAPSPAPAGD
>NZ_CP023703.1|WP_150470011.1|1198508_1199369_-|SGNH/GDSL-hydrolase-family-protein
MRPVRFVALGDSLTEGVGDPVGEGWRGWAALLARGLSAGPEAAVEFTNLAVSGAQTRDVVERQLPDALAQRPGIASVVVGVNDTLRCTFDVHAVAARLDTVYGAFAAQGTVLLTACLPDPGAMLGLPGVLARPLARRQRAVNAVVHALSARYGAVHLHASEGAWLTDRAMWSVDRLHPGERGHRQLAVRFHALLAGAGLATGPAPSPEPEFPAPTRSAGLRWLATAGTGWVARRCTDLLPQLLALAVDETRHRARGTSARLDLRTSAAVSAALAALSVPERQPGAA
>NZ_CP023703.1|WP_150470012.1|1199365_1200733_-|glycosyltransferase
MSAARPLRIVRLANFVAPSSGGLRTALRELGKGYRAAGHDPVLVVPGDRASDRDTEQGRVITLPGPLLPGTGGYRVLTDRRRVARLLEDLAPDRLEVSDRTTLRWTGKWARRARVPAAMVSHETADGVLRTWGLSEGAARRAADSLNIRTAHTYARVVCTTEYAEREFVRIGARNVVRAPLGVDLAERHPTLADTGLRARYARDDQILLVTCTRLSVEKRPGTALDALESLGRRGTRAVLVVAGDGPLRGRLEQRARDRGLPVVFLGHVSDRGLLGALQASADVCLAPGPAETFGLAALEAMACGTPVVASASSALPEVIGVAGATAADHGDAFADAVEALLERPAGERREAARARAECFGWGTAVEAFLAAHDAGVLSGTGVGDDGTVASRSGADVGTVPSRSGADVGTLPSRSGVDVGTLRSRSGADEATVPSRPDVCDGTTPSRPFVVGGLG
>NZ_CP023703.1|WP_150470013.1|1200729_1201857_-|glycosyltransferase
MRVVIVTESFPPDVNGVAHCALQTARHLVDRGHLPLVVAPATAAGPGPDAEAPCPVIRVPSLPLPGYPQVRVALPSRRVAAALVEHRADMVHLASPFILGVRGMAAAARLGIPAVAVYQTDLAGYARTYVHAGEAAAWRRIRSVHAAADLTLAPSSAAFHDLDSHGVPRVKLWPRGVDTVRFRPDLRDDALRRELAPNGEVIVGYVGRLAPEKQVELLAGVCGLDGVRVVVVGDGPSRPGLGEALPGAVFLGRRTGDELARIFASLDVFAHTGPFETFCQTVQEAMASGVPVVAPAAGGPLDLVAHGRTGLLVPARDAGAVRDAVAALAADPARRTAYGDAGRAMVEGRTWAAVGDQLIGHYGDVLAARRLAVAA
>NZ_CP023703.1|WP_150470014.1|1202025_1203447_-|HEAT-repeat-domain-containing-protein
MFDPFIAPSGTLLGLLQRGRGDGTLHALTAPRSEALAALHHCVLRDPRHDWQVENRSLYYARLYLDLGGDLDEIEAHLFDVEDAFDTEENRTGLSLAVLGHLASYGRQDALDLLRRYAASGSNWAWALDELALRDDDAGLRALAAPVLARFATDAEGEAELAAVVRDAFEPRPWRLWAEDPREYVSARVRAAQEAGCFDRWQRQLSPTGPRPGWSVRAVFEWAQQGIERGAALHVPAARCLTAVAGPEDRAEIVRAAEDGTEGARCTALRYLADQDDAQAPDLIEQAVATGSRFVVEAAVDAFERMRSAAAVDRARGWAHRPDALGAAAGRVLACRGTGRDSDLVLGALREAVRGEGCDAPTLWTLVDGAGRLGIACAAPVLRHIYRETASSHLRGRCARALAATDPSFATGFAVECLWDCEETTREIAARHAETGDARVVERLRRLAADPAEEDEVQTAVRSRIGPDAASAM
>NZ_CP023703.1|WP_150470015.1|1203770_1204163_-|ankyrin-repeat-domain-containing-protein
MTEVPDPEVVELATKIFDLARRGQTEELVAYVDAGVPANLTNDRGDSLLMLAAYHGHAEAVRALLARGADADRINDRGQTPLAGAVFKGETDVIKALLEAGADPAAGTPSAVDTARMFAKAELLELFGVQ
>NZ_CP023703.1|WP_073492896.1|1204426_1204621_+|hypothetical-protein
MILSISGVVLLGIIVFLFFRKDGLKASHGVVCALFGFYLASTAIAPSIKAGGESLASLLGGIKF
>NZ_CP023703.1|WP_167534806.1|1204674_1206243_+|hypothetical-protein
MARRPLPRILSTGSAQIARSRELARTAADSATDILHPLITVTRGLRRLASAGRRKWAETPKDRRGPLLFLVASVILVVALVPYGPLLAVITLMAAAAWQGRDRTPPAPDGPDESQTQRLQALYEALMPYFSTAEDPSPLYAHGGEWEKAFPSHEFDGTGRITQLEIRYPAYFPDGEAEARARVEHLLAAKSGRGREYRFAWDEEGNALTVSVLAPLPTDLAAQRFVTAPGETVLGFTDPSQVQRTLPLTHGEERRDVPPVVWRTGVRSTEPHLLAVGQPGSGTSTLLRSVALQALRYGDVLVIDGGGTGEYACLTGRDGVLGVEVGLAGALASLEWAAHETERRLIAANRARQEGHPPPDDTRRPLWILLDRPTAFTHLAEADGRKDPQDLLQVPLRHGRAAQVTVVVAEQFDSLDTLSDAVRQHTRARVVLGPAPAAQLEAVLGVRPHTSPAEHVPAGRGYARLGTGPTHRLQVPATPDPYDEATSDAHRQAVLELLPPRTTPADGENLPVPAEAVAAESS
>NZ_CP023703.1|WP_150470017.1|1206312_1207812_-|aminotransferase-class-I/II-fold-pyridoxal-phosphate-dependent-enzyme
MAQWTSAVGAAQLARLLTSQQDRPAGPGTRRPPAYRALADGVRLLVLEGRVPVAARLPAERELALALSVSRTTVAAAYEALRAEGFLESRRGAGSWTAVPAGNPVPARGLEPLPPEALGSVIDLGCAALPAPEPWLTRAVQGALEELPPYAHTHGDYPAGLPALRAMIAERYTRRGIPTMPEQIMVTTGAMGAIDAICHLFAGRGERIAVESPSYANILQLMREAGARLVPVAMAEGLAGWDMDRWRQVLREAAPRIAYVVADFHNPTGALADEDQRRRLVEAARSAGTVLVADETMTELWLDDDVEMPRPVCGFDPAGSTVITVGSASKAFWAGMRIGWVRAAPDVIRSLVAARAYADLGTPVLEQLAVNWLFSTGGWEQAVELRREQARGNRDALVAAVRRELPEWEFAVPKGGLTLWVRAGGLSGSRLAEAGERVGVRVPSGPRFGVDGAFEGYVRLPFTVGGAVAEEAAARLAAAARIVESGGTVGGESPRTFVA
>NZ_CP023703.1|WP_150470018.1|1207910_1208588_+|hypothetical-protein
MSEPPSPTAPPNRGLPRRLTQLYAGLALYGASSALLVRAGLGLEPWNVLHQGLAELSGLSIGVVSIIVGAAVLLLWIPLRQRPGLGTVSNVFVVGLAMDGTLALLPEAHGLAVRVPLLMAGILLNGAATGLYIAASFGPGPRDGLMTGLHRRTGRSIRLMRTAVEITVVATGFVLGGTIGVGTLLYALSIGPLAQLFLRVFAVPPASGGSTVVATGSPRGAILRP
>NZ_CP023703.1|WP_150470019.1|1208584_1209352_+|glycerophosphodiester-phosphodiesterase
MSTPVRHPYLDHPGPIPFAHRGGAADGLENTVAQFRRAVEAGYRYIETDVHATRDGRLAAFHDATLDRLTDGAGRIADLPWAQVRAARVGGKEPVPLFEELLETFPEVRWNIDVKAEPALHPLLNLIGRANAWDRVCVGSFSEARVLRAQRLAGPRLATSYGTRGVLNLRLRSWGVPAALRRSAVAAQVPEAQSGIQVVDHRFVRSAHARGLKVHVWTINETDRMHRLLDLGVDGIMTDHIDMLRKVMEDRGVWV

Crispr_ID: NZ_CP023703_3

• CRISPR_ID: NZ_CP023703_3
• CRISPR_location: 1805482-1805606
• CRISPR_type: Orphan
• Repeat_type: NA
• Spacer_info: 1 spacers

Consensus repeat of NZ_CP023703_3

Consensus_repeat	Method
CTGGAGCTGACCGGCAAGGAGCTGCGCTCATGA	CRISPRCasFinder

spacers of NZ_CP023703_3

>3.1|1805515|59|NZ_CP023703|CRISPRCasFinder
TTCCAGCCCGCGATGGGACCGGCCGGGGGTCCGGGGGTTGTCCCCCGGAACGGCACAGC

CRISPR arrays and Neighbor proteins around NZ_CP023703_3

CRISPR arrays

The CRISPR arrays of NZ_CP023703_3

>merge|NZ_CP023703|3|1805482-1805606|CRISPRCasFinder
CTGGAGCTGACCGGCAAGGAGCTGCGCTCATGATTCCAGCCCGCGATGGGACCGGCCGGGGGTCCGGGGGTTGTCCCCCGGAACGGCACAGCCTGGAGCTGACCGGCAAGGAGCTTCGCTCATGA

>NZ_CP023703|3|3|1805482-1805606|CRISPRCasFinder
CTGGAGCTGACCGGCAAGGAGCTGCGCTCATGA	TTCCAGCCCGCGATGGGACCGGCCGGGGGTCCGGGGGTTGTCCCCCGGAACGGCACAGC
CTGGAGCTGACCGGCAAGGAGCTTCGCTCATGA

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP023703.1|WP_150470416.1|1811234_1813322_+|transketolase	unknown	unknown	gnl|CDD|223100
NZ_CP023703.1|WP_150470413.1|1806425_1807436_+|heme-A-synthase	unknown	unknown	gnl|CDD|224528
NZ_CP023703.1|WP_086772106.1|1801354_1802776_-|Fe-S-cluster-assembly-protein-SufB	unknown	unknown	gnl|CDD|131035
NZ_CP023703.1|WP_086772107.1|1802772_1803552_-|transcriptional-regulator	unknown	unknown	gnl|CDD|225222
NZ_CP023703.1|WP_150470410.1|1803713_1804511_+|AAC(3)-family-N-acetyltransferase	unknown	unknown	gnl|CDD|376807
NZ_CP023703.1|WP_086767938.1|1808234_1809341_-|amidohydrolase-family-protein	unknown	unknown	gnl|CDD|368185
NZ_CP023703.1|WP_150470407.1|1796041_1796884_+|alpha-L-arabinofuranosidase	unknown	unknown	gnl|CDD|377497
NZ_CP023703.1|WP_086772102.1|1797769_1799026_-|cysteine-desulfurase	unknown	unknown	gnl|CDD|131034
NZ_CP023703.1|WP_150470418.1|1815998_1817105_+|glucose-6-phosphate-dehydrogenase-assembly-protein-OpcA	unknown	unknown	gnl|CDD|213538
NZ_CP023703.1|WP_150470419.1|1817101_1817884_+|6-phosphogluconolactonase	unknown	unknown	gnl|CDD|273494
NZ_CP023703.1|WP_150470408.1|1797272_1797737_-|SUF-system-NifU-family-Fe-S-cluster-assembly-protein	unknown	unknown	gnl|CDD|273918
NZ_CP023703.1|WP_167535026.1|1809867_1810821_-|protoheme-IX-farnesyltransferase	unknown	unknown	gnl|CDD|235293
NZ_CP023703.1|WP_150470409.1|1799022_1799787_-|Fe-S-cluster-assembly-ATPase-SufC	unknown	unknown	gnl|CDD|223473
NZ_CP023703.1|WP_086772104.1|1799794_1800112_-|non-heme-iron-oxygenase-ferredoxin-subunit	unknown	unknown	gnl|CDD|239604
NZ_CP023703.1|WP_086767946.1|1814478_1816002_+|glucose-6-phosphate-dehydrogenase	unknown	unknown	gnl|CDD|235579
NZ_CP023703.1|WP_150470417.1|1813355_1814474_+|transaldolase	unknown	unknown	gnl|CDD|235117
NZ_CP023703.1|WP_086772105.1|1800111_1801293_-|Fe-S-cluster-assembly-protein-SufD	unknown	unknown	gnl|CDD|223791
NZ_CP023703.1|WP_167534852.1|1809415_1809772_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP023703.1|WP_150470414.1|1807437_1808190_-|nucleotidyltransferase	unknown	unknown	unknown
NZ_CP023703.1|WP_086772100.1|1796943_1797276_-|metal-sulfur-cluster-assembly-factor	unknown	unknown	gnl|CDD|225062

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
NZ_CP023703.1|WP_150470416.1|1811234_1813322_+|transketolase	gnl|CDD|223100	COG0021, TktA, Transketolase [Carbohydrate transport and metabolism].	0
NZ_CP023703.1|WP_150470413.1|1806425_1807436_+|heme-A-synthase	gnl|CDD|224528	COG1612, CtaA, Uncharacterized protein required for cytochrome oxidase assembly [Posttranslational modification, protein turnover, chaperones].	9.77289e-26
NZ_CP023703.1|WP_086772106.1|1801354_1802776_-|Fe-S-cluster-assembly-protein-SufB	gnl|CDD|131035	TIGR01980, UPF0051_protein_slr0074, FeS assembly protein SufB. This protein, SufB, forms a cytosolic complex SufBCD. This complex enhances the cysteine desulfurase of SufSE. The system, together with SufA, is believed to act in iron-sulfur cluster formation during oxidative stress. Note that SufC belongs to the family of ABC transporter ATP binding proteins, so this protein, encoded by an adjacent gene, has often been annotated as a transporter component. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other].	0
NZ_CP023703.1|WP_086772107.1|1802772_1803552_-|transcriptional-regulator	gnl|CDD|225222	COG2345, COG2345, Predicted transcriptional regulator [Transcription].	6.2328e-55
NZ_CP023703.1|WP_150470410.1|1803713_1804511_+|AAC(3)-family-N-acetyltransferase	gnl|CDD|376807	pfam02522, Antibiotic_NAT, Aminoglycoside 3-N-acetyltransferase. This family consists of bacterial aminoglycoside 3-N-acetyltransferases EC:2.3.1.81, these catalyze the reaction: Acetyl-Co + a 2-deoxystreptamine antibiotic <=> CoA + N3'-acetyl-2-deoxystreptamine antibiotic. The enzyme can use a range of antibiotics with 2-deoxystreptamine rings as acceptor for its acetyltransferase activity, this inactivates and confers resistance to gentamicin, kanamycin, tobramycin, neomycin and apramycin amongst others.	5.88727e-102
NZ_CP023703.1|WP_150470407.1|1796041_1796884_+|alpha-L-arabinofuranosidase	gnl|CDD|377497	pfam05270, AbfB, Alpha-L-arabinofuranosidase B (ABFB) domain. This family consists of several fungal alpha-L-arabinofuranosidase B proteins. L-Arabinose is a constituent of plant-cell-wall poly-saccharides. It is found in a polymeric form in L-arabinan, in which the backbone is formed by 1,5-a- linked l-arabinose residues that can be branched via 1,2-a- and 1,3-a-linked l-arabinofuranose side chains. AbfB hydrolyzes 1,5-a, 1,3-a and 1,2-a linkages in both oligosaccharides and polysaccharides, which contain terminal non-reducing l-arabinofuranoses in side chains.	7.12366e-45
NZ_CP023703.1|WP_086772102.1|1797769_1799026_-|cysteine-desulfurase	gnl|CDD|131034	TIGR01979, Probable_cysteine_desulfurase, cysteine desulfurases, SufSfamily. This model represents a subfamily of NifS-related cysteine desulfurases involved in FeS cluster formation needed for nitrogen fixation among other vital functions. Many cysteine desulfurases are also active as selenocysteine lyase and/or cysteine sulfinate desulfinase. This subfamily is associated with the six-gene SUF system described in E. coli and Erwinia as an FeS cluster formation system during oxidative stress. The active site Cys is this subfamily resembles GHHC with one or both His conserved. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other].	0
NZ_CP023703.1|WP_150470418.1|1815998_1817105_+|glucose-6-phosphate-dehydrogenase-assembly-protein-OpcA	gnl|CDD|213538	TIGR00534, Putative_OxPP_cycle_protein_OpcA, glucose-6-phosphate dehydrogenase assembly protein OpcA. The opcA gene is found immediately downstream of zwf, the glucose-6-phosphate dehydrogenase (G6PDH) gene, in a number of species, including Mycobacterium tuberculosis, Streptomyces coelicolor, Nostoc punctiforme, and Synechococcus sp. PCC 7942. In the latter, disruption of opcA was shown to block assembly of G6PDH into active oligomeric forms. [Protein fate, Protein folding and stabilization].	2.91626e-98
NZ_CP023703.1|WP_150470419.1|1817101_1817884_+|6-phosphogluconolactonase	gnl|CDD|273494	TIGR01198, 6-phosphogluconolactonase_6PGL., 6-phosphogluconolactonase. This enzyme of the pentose phosphate pathway is often found as a part of a multifunctional protein with [Energy metabolism, Pentose phosphate pathway].	1.93855e-82
NZ_CP023703.1|WP_150470408.1|1797272_1797737_-|SUF-system-NifU-family-Fe-S-cluster-assembly-protein	gnl|CDD|273918	TIGR01994, Iron-sulfur_cluster_assembly_scaffold_protein_IscU, SUF system FeS assembly protein, NifU family. Three iron-sulfur cluster assembly systems are known so far. ISC is broadly distributed while NIF tends to be associated with nitrogenase in nitrogen-fixing bacteria. The most recently described is SUF, believed to be important to maintain the function during aerobic stress of enzymes with labile Fe-S clusters. It is fairly widely distributed. This family represents one of two different proteins proposed to act as a scaffold on which the Fe-S cluster is built and from which it is transferred. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other].	2.84651e-61
NZ_CP023703.1|WP_167535026.1|1809867_1810821_-|protoheme-IX-farnesyltransferase	gnl|CDD|235293	PRK04375, PRK04375, protoheme IX farnesyltransferase; Provisional.	2.31814e-147
NZ_CP023703.1|WP_150470409.1|1799022_1799787_-|Fe-S-cluster-assembly-ATPase-SufC	gnl|CDD|223473	COG0396, sufC, Cysteine desulfurase activator ATPase [Posttranslational modification, protein turnover, chaperones].	1.73821e-143
NZ_CP023703.1|WP_086772104.1|1799794_1800112_-|non-heme-iron-oxygenase-ferredoxin-subunit	gnl|CDD|239604	cd03528, Rieske_RO_ferredoxin, Rieske non-heme iron oxygenase (RO) family, Rieske ferredoxin component; composed of the Rieske ferredoxin component of some three-component RO systems including biphenyl dioxygenase (BPDO) and carbazole 1,9a-dioxygenase (CARDO). The RO family comprise a large class of aromatic ring-hydroxylating dioxygenases found predominantly in microorganisms. These enzymes enable microorganisms to tolerate and even exclusively utilize aromatic compounds for growth. ROs consist of two or three components: reductase, oxygenase, and ferredoxin (in some cases) components. The ferredoxin component contains either a plant-type or Rieske-type [2Fe-2S] cluster. The Rieske ferredoxin component in this family carries an electron from the RO reductase component to the terminal RO oxygenase component. BPDO degrades biphenyls and polychlorinated biphenyls. BPDO ferredoxin (BphF) has structural features consistent with a minimal and perhaps archetypical Rieske protein in that the insertions that give other Rieske proteins unique structural features are missing. CARDO catalyzes dihydroxylation at the C1 and C9a positions of carbazole. Rieske ferredoxins are found as subunits of membrane oxidase complexes, cis-dihydrodiol-forming aromatic dioxygenases, bacterial assimilatory nitrite reductases, and arsenite oxidase. Rieske ferredoxins are also found as soluble electron carriers in bacterial dioxygenase and monooxygenase complexes.	4.51304e-51
NZ_CP023703.1|WP_086767946.1|1814478_1816002_+|glucose-6-phosphate-dehydrogenase	gnl|CDD|235579	PRK05722, PRK05722, glucose-6-phosphate 1-dehydrogenase; Validated.	0
NZ_CP023703.1|WP_150470417.1|1813355_1814474_+|transaldolase	gnl|CDD|235117	PRK03343, PRK03343, transaldolase; Validated.	0
NZ_CP023703.1|WP_086772105.1|1800111_1801293_-|Fe-S-cluster-assembly-protein-SufD	gnl|CDD|223791	COG0719, SufB, Cysteine desulfurase activator SufB [Posttranslational modification, protein turnover, chaperones].	1.00863e-82
NZ_CP023703.1|WP_086767938.1|1808234_1809341_-|amidohydrolase-family-protein	gnl|CDD|368185	pfam04909, Amidohydro_2, Amidohydrolase. These proteins are amidohydrolases that are related to pfam01979.	8.1873e-09
NZ_CP023703.1|WP_086772100.1|1796943_1797276_-|metal-sulfur-cluster-assembly-factor	gnl|CDD|225062	COG2151, PaaD, Predicted metal-sulfur cluster biosynthetic enzyme [General function prediction only].	5.98261e-33

Protein sequences

>NZ_CP023703.1|WP_150470410.1|1803713_1804511_+|AAC(3)-family-N-acetyltransferase
MPTPPPTGPLVTRDTLASDLRTLGVEPGEILLEHSSLSALGWVCGGAVAAVQGLLDALGPDGTLVVPTQSGDLSDPSHWGNPPVPRAWWDTIRATMPAYDPLVTPSRGVGVIPETVRTWPGALRSAHPQTSFAALGPRAAEVTEGHAPDCRLGERSPLARLEALGARVLLLGAGYDTCTSFHLAEYRIPAPRVGSGRPGPEGWEVVSEVSIDADRFDELGHDFERDRPVVRAKVGAADARLFPVADAVAYAERWLPLHRSRAEEV
>NZ_CP023703.1|WP_086772107.1|1802772_1803552_-|transcriptional-regulator
MKNVGEARVTPTGTPQEELATGERSTRNRVARSILDHGPSTVADLAGRLGLTQAAVRRHLDALVADDVVEAREQRVYGARTRGRPAKVFALTDCGRDAFDQSYDKLAADALRFIQERFGGDEAVVAFARARIAEQATGYREAIEAAAPDQRTQALAKALSADGYAATARSAPVGEQLCQHHCPVAHVAEKFPQLCEAETEIFSQLLGTHVQRLATIAHGDGVCTTYIPKISPTADHPADPSTDHAPDIASASTAGRNPA
>NZ_CP023703.1|WP_086772106.1|1801354_1802776_-|Fe-S-cluster-assembly-protein-SufB
MTLPTETAHPELEGLGKYEYGWADSDTAGASAKRGINEDVVRDISSKKNEPEWMTKLRLKGLRLFEKKPMPNWGSDLSGIDFDNIKYFVRSTEKQAESWEDLPEDIKNTYDRLGIPEAEKQRLVAGVAAQYESEVVYHQIREDLEEQGVIFLDTDTALKQHPELFKEYFGTVIPVGDNKFASLNTAVWSGGSFIYVPKGVHVEIPLQAYFRINTENMGQFERTLIIVDEGAYVHYVEGCTAPIYKSDSLHSAVVEIIVKKNARCRYTTIQNWSNNVYNLVTKRAVAYEGATMEWIDGNIGSKVTMKYPAVYLMGEHAKGETLSIAFAGEGQHQDAGSKMVHMAPNTSSNIVSKSVARGGGRTSYRGLVEIGEGAHGSKSNVLCDALLVDTISRSDTYPYVDVREDDVSMGHEATVSKVSDDQLFYLMSRGLTEFEAMAMIVRGFVEPIAKELPMEYALELNRLIELQMEGAVG
>NZ_CP023703.1|WP_086772105.1|1800111_1801293_-|Fe-S-cluster-assembly-protein-SufD
MAEAQNIPVGSTTAGQIAVAAESTVATRMSAPPSFDVADFPVPHGREEEWRFTPLERLRGLHDGTAVATGEGVKVDIDAPEGVVVETVGRDDARLGRAGTPVDRVAAQAYSAFEKAGVVTVPKETVLTEPIRIAVHGQGGVAYGHQVVELGAFAEAVVVIDHTGDAVLAANVDYILGDGAKLTVVSVQDWDDKAVHVGQHNALIGRDATFKSFVVTFGGDLVRLHPRIAYAGTGGEAELFGLYFTDAGQHQEHRLLVDHNTPHCKSNVAYKGALQGDGAHAVWIGDVLIEATAEGTDTYEMNRNLVLTDGARVDSVPNLEIETGEIVGAGHASATGRFDDEQLFYLMARGIAAHDARRLVVRGFFAELVQQIGVDDIEERLLVKIDEELEAAV
>NZ_CP023703.1|WP_086772104.1|1799794_1800112_-|non-heme-iron-oxygenase-ferredoxin-subunit
MAFVRACGLSELEEDTPKRVELDGTPVSVVKTEGEVFAIHDICSHANVSLSEGEVEDCQIECWLHGSAFDLRTGKPSGLPATRPVPVYPVKIEGDDVLVSLTQES
>NZ_CP023703.1|WP_150470409.1|1799022_1799787_-|Fe-S-cluster-assembly-ATPase-SufC
MATLEIRDLHVTVEADNATKEILKGVDLTVKQGETHAIMGPNGSGKSTLAYSLAGHPKYTITGGTVTLDGEDVLEMSVDERARAGLFLAMQYPVEVPGVSVSNFLRTSATAIRGEAPKLRTWVKEVREAMERLNMDPAFAERNVNEGFSGGEKKRHEILQLELLKPKIAILDETDSGLDVDALRVVSEGVNRVRETGEVGTLLITHYTRILRYIKPDHVHVFSAGRIVESGGAELADKLENEGYEVYTKGGASA
>NZ_CP023703.1|WP_086772102.1|1797769_1799026_-|cysteine-desulfurase
MTQLPGLLDTEAIRKDFPILDRMVHDDRKLVYLDNAATSQKPRQVLDALSGYYERYNANVHRGVHVLAEEATALYEGARDKVAEFINAPSRDEVIFTKNASESLNLVANMLGWADEPYRVDAETEIVITEMEHHSNIVPWQLLSQRTGAKLKWFGLTDDGRLDLSNIDEIITEKTKIVSFVLVSNILGTINPVEAIVRRAQEVGALVCIDASQAAPHMPMDVQALQADFVAFTGHKMCGPTGIGVLWGRQELLEDLPPFLGGGEMIETVSMHSSTYAPAPHKFEAGTPPIAQAVGLGAAIDYLSAIGMDKILAHEHAITEYAVKRLGEVPGLRIIGPATAEERGAAISFTLGDIHPHDVGQVLDEQGIAVRVGHHCARPVCLRYGIPATTRASFYLYSTPAEIDALVEGLEHVRNFFG
>NZ_CP023703.1|WP_150470408.1|1797272_1797737_-|SUF-system-NifU-family-Fe-S-cluster-assembly-protein
MKLDSMYQEVILDHYKHPHGRGLRDGDAEVHHVNPTCGDEITLRVKYDGTTIEDVSYEGQGCSISQASASVLNDLLVGKELSEAQKIQETFLELMQSKGRVEPDDAMEEVLEDAIAFAGVSKYPARVKCALLSWMAWKDATAQALGAEAERKTA
>NZ_CP023703.1|WP_086772100.1|1796943_1797276_-|metal-sulfur-cluster-assembly-factor
MSETVEMKPASEDEVREALYDVVDPELGIDVVNLGLIYGIHIDDANIATIDMTLTSAACPLTDVIEDQAKSATDGLVNELRINWVWMPPWGPDKITDDGREQLRALGFNV
>NZ_CP023703.1|WP_150470407.1|1796041_1796884_+|alpha-L-arabinofuranosidase
MPDNKSRPSQERPWENGWAPDTTRAPGTRRLWLAGVLAVATVVACVATISLADKPSDVKSAAGEERTTSDKETSSGLISFASPTVSGSPSASATKGSASPSASASASTSPSPSPSSNGGSSASPSPSGPAAGGGSDPKPVGVRRSMRSINYPNRYWRVGGGQVRLEAAGGSEFREDATFVVVKGLADSSCFTFVTSDGMSLRHRDFVLRPERNDGSALFKQDATFCAVPSSHSSGAIMLESVNYPGRFLRHRNFALRLDAYGYGSNHREDFSFHLVDGLA
>NZ_CP023703.1|WP_150470413.1|1806425_1807436_+|heme-A-synthase
MDGVPNVTRADAVAAVRNPLAFIAARWTPAPRTVQRAALTALVMSVVIVVTGGAVRLTGSGLGCPTWPKCTDDSLTATGAMGFHGAIEFGNRMLTYVLCAAVGWAIIAARSQKPYRRGLTRLGWAQFWVVMSNAVLGGIVVLVGLNPYTVAAHFVATSALIAIAVVMWQRTREGDAQARPLVGKSVQQLVWVLIAATVVLILVGTVVTGAGPHAGDSSEVERMPLDWETVSKVHAVLAWIVVTLTFALWFVLRAVDAPRLPLDRTRDLFVVLLAQGVIGYVQYFTDLPEVLVGLHMLGSALVWIAVLRVLLALRERPEPAVGLPGPATEATVGSRA
>NZ_CP023703.1|WP_150470414.1|1807437_1808190_-|nucleotidyltransferase
MQTDILLDRFLGALAPLDPVAVWAHGSLAGGDYQEGRSDLDLIAVLPGPLRPGTLWRVAVLHQELRADPLAAGLHCSYLTPATAADPARPHLTWAHQELMRRPVTPVTRRELHAFGRVLHGRAPAGLLPEVSDRELGEFVVSDQRDFWRPAVDKARLWTRDVWVDAGLVTFARASVTLRQGRLISKREALAELPGLGAPAEIVEDIRRRRYGEPAPVRPAASEEEWRAHRAESARGWLGPAIDGLVAAHG
>NZ_CP023703.1|WP_086767938.1|1808234_1809341_-|amidohydrolase-family-protein
MIETPSLVDQYCHGVLRTELGLGTFEAQLARTEGPPAPGTTLFDTQTGFAVRRWCPPLLGLEPHCPPARYLARRRELGVLESGRRLLRGSGITTYLVDTGLPGDLTGPDELASAGDAEAREIVRLELLAEQVADTSGTVESFLANLAEAVHGAAATAVAFTSVAGVRHGLALAPEPPGPGEVRGAAGRWLAGRRVGGELSDPVLLRHLLWIAVASGRPLQLHAGLGEPGLRIDRTDPVLLTDFVRATAGLGTDLVLLHGYPYHRHAAHLAGVFPHVYADSGAALVRTGARAATVLAEILELAPFGKILFSSGARGLPELHVVGARLFREALARVLGGWVAQDAWSLTDAQRVAGMVAAGNARRVYGLG
>NZ_CP023703.1|WP_167534852.1|1809415_1809772_-|hypothetical-protein
MADTKQADETADAKQAAKAERTAARLAKRISAFSKEHGGAEGQIAHLGERGARIVLVGEDGGWGDVVAPDMEIAAKAVEKSGITVHEDFDGEFAAKVRTGPYEWSRMAGIQVGGPRNT
>NZ_CP023703.1|WP_167535026.1|1809867_1810821_-|protoheme-IX-farnesyltransferase
MCVTAVESRPAGLIGTKQSPSRRPVGARVMAFVALTKPRIIELLLITTVPVMFLAQQGVPDLGLVLLTCLGGYLSAGGANALNMYIDRDIDALMDRTSQRPLVTGMVSPRECLAFGISLAIGSTLLFGLTVNWLSAWLALGALLFYVVVYTMILKRRTSQNIVWGGIAGCMPVLIGWSAVTDSLSWAPVVLFLVMFFWTPPHYWPLSMKVREDYARVGVPMLPVIASNKVVARQIVIYSWVMVAVSLLLTPLGYTGWFYTTVALAAGGWWLWEAHSLQNRAKAETEGGKLKEMRLFHWSITYVSLLFVAVAVDPFLR
>NZ_CP023703.1|WP_150470416.1|1811234_1813322_+|transketolase
MSTKPTTTDLEWTELDQRAVDTARVLAADAVQRVGNGHPGTAMSLAPAAYTLFQKVMRHDPADADWVGRDRFVLSAGHSSLTLYTQLYLAGFGLELDDLKSFRTWGSKTPGHPEYGHTVGVETTTGPLGQGVANAVGMAMAARYERGLFDPETPQGESPFDHFVYCVAGDGCLQEGISAEASSLAGHQKLGNLVLLWDDNHISIEGDTETAVSEDTVKRYEAYGWHVQRVAPKPDGDLDPHALYDAIEAAKQVTDRPSFIAMRSIIAWPAPNAQNTEAAHGSALGDDEVAATKRVLGFDPEQSFEVSDEVIGHTRQALERGAQAKAEWEKSYQLWRDNNPQRAAEFDRVAAAELPAGWEEKIPVFETGKGVATRAASGKVLQALGAVIPELWGGSADLAGSNNTTIDKTSSFLPADNPLPEASPYGRTIHFGIREHSMAAEMNGIALHGNTRVYGGTFLVFSDYMRNAVRLSALMHLPVTYVWTHDSIGLGEDGPTHQPVEHLAALRAIPGLNVVRPADANETAIAWREILKRYTKVFGKGAPHGLILTRQGVPTYESNEEAAKGGYVLFEASSGTPEVILLATGSEVHVAVEAREQLEADGVPTRVVSMPSVEWFEEQDQGYRDSVLPPSVKARVAVEAGIGLTWHKYVGDAGRIVSLEHFGASADGKVLFREFGFTAENVADKARESLTAAQR
>NZ_CP023703.1|WP_150470417.1|1813355_1814474_+|transaldolase
MTDALKRLSEEGVAIWLDDLSRKRITSGNLAELIDQQHVVGVTTNPSIFQKAISQGDGYDQQVSDLAARKVTVEEAIRMITTADVRDAADILRPVFDATGGQDGRVSIEVDPRLAHHTKATVAEAKQLAWLVDRPNTLIKIPATKAGLPAITEVIGNGISVNVTLIFSLERYREVMEAYLAGLEKAQAKGLDLSLIHSVASFFVSRVDTEIDKRLDALGTDEAKAARGKAGVANARLAYQAYEEVFAGARWDALEKAGANKQRALWASTGVKDPAYRDTMYVVDLVAPNTVNTMPEATLFATEDHGEVTGNTVAGTYEQARAELDAVEKLGISYDDVVQLLEDEGVEKFEASWNDLLKSTEAELQRLAPSEG
>NZ_CP023703.1|WP_086767946.1|1814478_1816002_+|glucose-6-phosphate-dehydrogenase
MSSSNPLRDPADRRLPRIAGPSGLVIFGVTGDLSRKKLMPAVYDLANRGLLPPGFSLVGFARREWANEDFAQEVHDAVKEHARTPFREEVWQQLIQGMRFVQGTFDDDDAFERLRSTIEELDKAQGTGGNFAFYLSVPPGAFPVVIQQLKKHNLADQRGGSWRRAVIEKPFGHDLKSAEELNATVEEVFAPDQVFRIDHYLGKETVQNILALRFANTMFEPIWNRSFVDHVQITMAEDIGIGGRAGYYDGIGAARDVIQNHLLQLMALTAMEEPASFDADALAAEKTKVLGAVRLPKDLGDATVRGQYAAGWQGGAKAVGYLQEEGIDPKSKTDTYAAIKLEVDNRRWAGVPFYLRTGKRLGRRVTEIAVVFQRAPHSPFDHTATEELGKNAIVIRVQPDEGVTVRFGSKVPGTSMEIRDVSMDFAYGESFTESSPEAYERLILDVLLGDSNLFPRTEEVELSWKILDPIEQYWDENGKPAQYQAGTWGPVEADEMLERDGRSWRRP
>NZ_CP023703.1|WP_150470418.1|1815998_1817105_+|glucose-6-phosphate-dehydrogenase-assembly-protein-OpcA
MKIDLTDTTASKINKGLVQGRRAIGTPAVGMVLTLVIVTDEENAYDALKAAGDASREHPSRTLVVIKRVSRSPRDRTKSRLDAEVRVGAEAGTGETVVLRLYGEVAEHAQSVVLPLLLPDAPVVAWWPVNAPLDPAADPLGALAQRRVTDTYAAEQPVRDLTARSRTYTPGDTDLSWTRITPWRSMLAAALDQVTCKVESVEVEGEEFNPSCELLAMWLGDRLDVPVQRSLSGGPGLTAVRLSTDCGPIVLDRADGSLATLSIDGQPDRAVALQRRDTAELIAEELRRLDPDDTYASALRFGVERLNTSDGRSGTGSAPEASADAPEAVAKGAAKGEPVAVPTPVEAAVKVPAKESTAQAPVKKAAAK
>NZ_CP023703.1|WP_150470419.1|1817101_1817884_+|6-phosphogluconolactonase
MSTPQLVVHRDKDLMAQAAAARLITKIVDAQASRGHASVVLTGGRNGNGLLAALAAAPARDAVDWGRLDLWWGDERFLPEGDPDRNVTQAREALLDSVPLDPKRVHAMPASDGVYGSDVEAAAAGYAEELARAAGPENHGSVPTFDVLMLGVGPDTHVASLFPELPAVRETERTVVGVRGAPKPPPTRTTLTLVAIRSAREVWLLAAGEDKAQAAAIALSGAGEIQAPAAGARGRSRTLWLLDSAAASQLPRSLYPPASP

Crispr_ID: NZ_CP023703_4

• CRISPR_ID: NZ_CP023703_4
• CRISPR_location: 4085733-4085838
• CRISPR_type: Orphan
• Repeat_type: NA
• Spacer_info: 1 spacers

Consensus repeat of NZ_CP023703_4

Consensus_repeat	Method
CGGGTTCCGCCCCCGTGCCCTCCGGGTCT	CRISPRCasFinder

spacers of NZ_CP023703_4

>4.1|4085762|48|NZ_CP023703|CRISPRCasFinder
CAAGCCCGGTGCTCTGCTGCTGAGCTACACGCCGATGCGCCGACGTGG

CRISPR arrays and Neighbor proteins around NZ_CP023703_4

CRISPR arrays

The CRISPR arrays of NZ_CP023703_4

>merge|NZ_CP023703|4|4085733-4085838|CRISPRCasFinder
CGGGTTCCGCCCCCGTGCCCTCCGGGTCTCAAGCCCGGTGCTCTGCTGCTGAGCTACACGCCGATGCGCCGACGTGGCGGGTTCCGCCCCCGCGCCCTCCGGGTCT

>NZ_CP023703|4|4|4085733-4085838|CRISPRCasFinder
CGGGTTCCGCCCCCGTGCCCTCCGGGTCT	CAAGCCCGGTGCTCTGCTGCTGAGCTACACGCCGATGCGCCGACGTGG
CGGGTTCCGCCCCCGCGCCCTCCGGGTCT

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP023703.1|WP_150471897.1|4076273_4077878_+|protein-kinase	unknown	unknown	gnl|CDD|270916
NZ_CP023703.1|WP_150471907.1|4091032_4091527_-|hypothetical-protein	unknown	unknown	gnl|CDD|367978
NZ_CP023703.1|WP_150471898.1|4077974_4078973_-|phosphotransferase	unknown	unknown	gnl|CDD|270702
NZ_CP023703.1|WP_150474597.1|4092968_4093163_-|DUF397-domain-containing-protein	unknown	unknown	gnl|CDD|377231
NZ_CP023703.1|WP_150471904.1|4088187_4089090_+|D-alanyl-D-alanine-carboxypeptidase	unknown	unknown	gnl|CDD|224600
NZ_CP023703.1|WP_150471895.1|4072744_4073110_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP023703.1|WP_150471908.1|4091523_4092525_-|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl|CDD|181818
NZ_CP023703.1|WP_150471909.1|4092577_4092964_+|cupin-domain-containing-protein	unknown	unknown	gnl|CDD|380355
NZ_CP023703.1|WP_150471896.1|4074301_4075927_-|protein-kinase	unknown	unknown	gnl|CDD|270916
NZ_CP023703.1|WP_150471900.1|4081756_4083244_+|2-oxo-acid-dehydrogenase-subunit-E2	unknown	unknown	gnl|CDD|237001
NZ_CP023703.1|WP_150471894.1|4071745_4072726_+|zinc-binding-dehydrogenase	unknown	unknown	gnl|CDD|176180
NZ_CP023703.1|WP_150471905.1|4089161_4089986_-|maleylpyruvate-isomerase-family-mycothiol-dependent-enzyme	unknown	unknown	gnl|CDD|274422
NZ_CP023703.1|WP_150474596.1|4073662_4074211_+|DUF2587-domain-containing-protein	unknown	unknown	gnl|CDD|378489
NZ_CP023703.1|WP_150471910.1|4093419_4095183_+|redoxin-domain-containing-protein	unknown	unknown	gnl|CDD|271321
NZ_CP023703.1|WP_150471903.1|4087254_4087929_-|FCD-domain-containing-protein	unknown	unknown	gnl|CDD|224715
NZ_CP023703.1|WP_150471899.1|4079516_4080767_+|pyruvate-dehydrogenase-(acetyl-transferring)-E1-component-subunit-alpha	unknown	unknown	gnl|CDD|213783
NZ_CP023703.1|WP_150471906.1|4090208_4091006_+|carbon-nitrogen-family-hydrolase	unknown	unknown	gnl|CDD|143607
NZ_CP023703.1|WP_150471902.1|4085962_4087258_-|MFS-transporter	unknown	unknown	gnl|CDD|349949
NZ_CP023703.1|WP_150471901.1|4083404_4085720_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP023703.1|WP_073498290.1|4080768_4081746_+|alpha-ketoacid-dehydrogenase-subunit-beta	unknown	unknown	gnl|CDD|223101

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
NZ_CP023703.1|WP_150471897.1|4076273_4077878_+|protein-kinase	gnl|CDD|270916	cd14014, STKc_PknB_like, Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.	2.40297e-121
NZ_CP023703.1|WP_150471907.1|4091032_4091527_-|hypothetical-protein	gnl|CDD|367978	pfam04525, LOR, LURP-one-related. The structure of this family has been solved. It comprises a 12-stranded beta barrel with a central C-terminal alpha helix. This helix is thought to be a transmembrane helix. It is structurally similar to the C-terminal domain of the Tubby protein. In plants it plays a role in defense against pathogens.	1.22311e-29
NZ_CP023703.1|WP_150471898.1|4077974_4078973_-|phosphotransferase	gnl|CDD|270702	cd05153, HomoserineK_II, Type II Homoserine Kinase. This subfamily is composed of unusual homoserine kinases, from a subset of bacteria, which have a Protein Kinase fold. These proteins do not bear any similarity to the GHMP family homoserine kinases present in most bacteria and eukaryotes. Homoserine kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to L-homoserine producing L-homoserine phosphate, an intermediate in the production of the amino acids threonine, methionine, and isoleucine. The Type II homoserine kinase subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).	1.87456e-39
NZ_CP023703.1|WP_150474597.1|4092968_4093163_-|DUF397-domain-containing-protein	gnl|CDD|377231	pfam04149, DUF397, Domain of unknown function (DUF397). The function of this family is unknown.	2.8888e-12
NZ_CP023703.1|WP_150471904.1|4088187_4089090_+|D-alanyl-D-alanine-carboxypeptidase	gnl|CDD|224600	COG1686, DacC, D-alanyl-D-alanine carboxypeptidase [Cell envelope biogenesis, outer membrane].	1.84102e-50
NZ_CP023703.1|WP_150471908.1|4091523_4092525_-|helix-turn-helix-domain-containing-protein	gnl|CDD|181818	PRK09393, ftrA, transcriptional activator FtrA; Provisional.	2.30565e-120
NZ_CP023703.1|WP_150471909.1|4092577_4092964_+|cupin-domain-containing-protein	gnl|CDD|380355	cd02226, cupin_YdbB-like, Bacillus subtilis YdbB and related proteins, cupin domain. This family includes bacterial proteins homologous to YdbB, a Bacillus subtilis protein of unknown function. It also includes protein Nmb1881 From Neisseria meningitidis, also of unknown function. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.	1.99275e-43
NZ_CP023703.1|WP_150471896.1|4074301_4075927_-|protein-kinase	gnl|CDD|270916	cd14014, STKc_PknB_like, Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.	2.08056e-122
NZ_CP023703.1|WP_150471900.1|4081756_4083244_+|2-oxo-acid-dehydrogenase-subunit-E2	gnl|CDD|237001	PRK11856, PRK11856, branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed.	1.41748e-160
NZ_CP023703.1|WP_150471894.1|4071745_4072726_+|zinc-binding-dehydrogenase	gnl|CDD|176180	cd05276, p53_inducible_oxidoreductase, PIG3 p53-inducible quinone oxidoreductase. PIG3 p53-inducible quinone oxidoreductase, a medium chain dehydrogenase/reductase family member, acts in the apoptotic pathway. PIG3 reduces ortho-quinones, but its apoptotic activity has been attributed to oxidative stress generation, since overexpression of PIG3 accumulates reactive oxygen species. PIG3 resembles the MDR family member quinone reductases, which catalyze the reduction of quinone to hydroxyquinone. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.	0
NZ_CP023703.1|WP_150471905.1|4089161_4089986_-|maleylpyruvate-isomerase-family-mycothiol-dependent-enzyme	gnl|CDD|274422	TIGR03083, TIGR03083, uncharacterized Actinobacterial protein TIGR03083. This protein family pulls together several groups of proteins, each very different from the others. They share in common three conserved regions. The first is a region of about 38 amino acids, nearly always at the N-terminus of a protein. This region has a bulky hydrophobic residue, usually Trp, at position 29, and a His residue at position 37 that is invariant, so far, in over 150 instances. The second conserved region has a motif [DE]xxxHxxD. The third conserved region contains a hydrophobic patch and a well-conserved Arg residue. Most examples are found in the Actinobacteria, including the genera Mycobacterium, Corynebacterium, Streptomyces, Nocardia, Frankia, etc. The pattern of near-invariant residues against a backdrop of extreme sequence divergence suggests enzymatic activity and conservation of active site residues.	6.56675e-26
NZ_CP023703.1|WP_150474596.1|4073662_4074211_+|DUF2587-domain-containing-protein	gnl|CDD|378489	pfam10759, DUF2587, Protein of unknown function (DUF2587). This is a bacterial family of proteins with no known function.	9.82504e-93
NZ_CP023703.1|WP_150471910.1|4093419_4095183_+|redoxin-domain-containing-protein	gnl|CDD|271321	cd14951, NHL-2_like, NHL repeat domain of NHL repeat-containing protein 2 and similar proteins. NHL repeat-containing protein 2 (NHLRC2) and related bacterial proteins; members of this eukaryotic and bacterial family are uncharacterized, the NHL repeat domain is found C-terminally of a thioredoxin domain. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.	5.29704e-144
NZ_CP023703.1|WP_073498290.1|4080768_4081746_+|alpha-ketoacid-dehydrogenase-subunit-beta	gnl|CDD|223101	COG0022, AcoB, Pyruvate/2-oxoglutarate dehydrogenase complex, dehydrogenase (E1) component, eukaryotic type, beta subunit [Energy production and conversion].	9.42236e-162
NZ_CP023703.1|WP_150471899.1|4079516_4080767_+|pyruvate-dehydrogenase-(acetyl-transferring)-E1-component-subunit-alpha	gnl|CDD|213783	TIGR03181, PDH_E1_alph_x, pyruvate dehydrogenase E1 component, alpha subunit. Members of this protein family are the alpha subunit of the E1 component of pyruvate dehydrogenase (PDH). This model represents one branch of a larger family that E1-alpha proteins from 2-oxoisovalerate dehydrogenase, acetoin dehydrogenase, another PDH clade, etc. [Energy metabolism, Pyruvate dehydrogenase].	0
NZ_CP023703.1|WP_150471906.1|4090208_4091006_+|carbon-nitrogen-family-hydrolase	gnl|CDD|143607	cd07583, nitrilase_5, Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases). The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.	5.12577e-122
NZ_CP023703.1|WP_150471902.1|4085962_4087258_-|MFS-transporter	gnl|CDD|349949	cd06174, MFS, Major Facilitator Superfamily. The Major Facilitator Superfamily (MFS) is a large and diverse group of secondary transporters that includes uniporters, symporters, and antiporters. MFS proteins facilitate the transport across cytoplasmic or internal membranes of a variety of substrates including ions, sugar phosphates, drugs, neurotransmitters, nucleosides, amino acids, and peptides. They do so using the electrochemical potential of the transported substrates. Uniporters transport a single substrate, while symporters and antiporters transport two substrates in the same or in opposite directions, respectively, across membranes. MFS proteins are typically 400 to 600 amino acids in length, and the majority contain 12 transmembrane alpha helices (TMs) connected by hydrophilic loops. The N- and C-terminal halves of these proteins display weak similarity and may be the result of a gene duplication/fusion event. Based on kinetic studies and the structures of a few bacterial superfamily members, GlpT (glycerol-3-phosphate transporter), LacY (lactose permease), and EmrD (multidrug transporter), MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement. Bacterial members function primarily for nutrient uptake, and as drug-efflux pumps to confer antibiotic resistance. Some MFS proteins have medical significance in humans such as the glucose transporter Glut4, which is impaired in type II diabetes, and glucose-6-phosphate transporter (G6PT), which causes glycogen storage disease when mutated.	1.07556e-33
NZ_CP023703.1|WP_150471903.1|4087254_4087929_-|FCD-domain-containing-protein	gnl|CDD|224715	COG1802, GntR, Transcriptional regulators [Transcription].	7.28836e-42

Protein sequences

>NZ_CP023703.1|WP_150471901.1|4083404_4085720_-|hypothetical-protein
MNHDADQQHLVEANPGYASGQLARALTTARTHQDPETRRRAQDRGRRWRDVLSGMAGGLLTIGSRTPVAGLPAWVTPEVVRGGFATGQPAAGGPLLAHECETARRAGIPENRRDLFAYWLSEEGLGLLHELLDTGRYEVTVPEEAALLTVAWLARAGETDAALDLVEELAPFADRLRFAPQPSDLPAPDPGAVHRRTVGDAVDTLVRRTPSRAVETQREALTVWQPFGDELLALWLETADADGLVLARTPGAGWRERGAALLRRYADLADRHTYCTKHRRPKQNLAILRSALEETVGGRELDARRSGLLRHAVTSMVRRRGLPGSTRLTALRREQAVQAALPSHHALAQLVLRRLAGLPQEVGVAEIAPLLVPVSEDEARETGLPAGAAVPAALRRPVEVALSAPVGTLVERGLVPSAEVLAELVPQLVAVTTAQAYPDEALRTLAAAGYRAFRNRRSLLLLNLERQVRAEELPWVTAVAGQRSAAEAGEESALALRQLGELAVQAFPATVLPNPLVRELSVLAREAELGAPLVEELAADIFMGTFTPKFLAAARVAAELLGGGSLYERYYAVDYRAIRTMAIIEAAEAQTGRNRPRTSPGFAKLCAERAAGSSSGDRYFGSTAANGMVIEQAQILTTHNLATLVHRVGIAPATGWEDLARRSFGTVCRLTARVHGNPRPLTTIKDAAYAWRQMLFHLSLCTGEEQARTLNWVVEEAGRQPGHVTDRLAPALTGLRQVAEGGSADTGAGRRLLGWSTEGHWMREPGSAGGR
>NZ_CP023703.1|WP_150471900.1|4081756_4083244_+|2-oxo-acid-dehydrogenase-subunit-E2
MTTMTEASVREFKMPDVGEGLTEAEILKWYVQPGDTVTDGQVVCEVETAKAAVELPIPYDGVVRELRFPEGTTVDVGMSIIAVDVSGGSAPAAAPEPAPAVEEEPEEPKSQGSGRQPVLVGYGVATSSTKRRPRKSAEIPAQESAPVSAAVQAELNGHGTIPEAAPAPSAPVSAPATAADRPRPLAKPPVRKLAKDLGVDLASVVPSGPDGIITREDVHAAAAAPAQAPARPTAPQPTPATAQVSTAPVTTAAAAPAASYDAGRETRIPVKGVRKATAQAMVGSAFTAPHVTEFVTVDVTRTMKLVEELKGDKDMQGLRVNPLLLIAKALLVAIKRNPDVNASWDEANQEIVRKHYVNLGIAAATPRGLIVPNIKDAHDKTLPQLAEALGELVATAREGRTSPAAMQGGTVTITNVGVFGVDTGTPILNPGESAILAVGAIKLQPWVHKGKVKPRQVTTLALSFDHRLVDGELGSKVLADVAAVLEQPKRLITWG
>NZ_CP023703.1|WP_073498290.1|4080768_4081746_+|alpha-ketoacid-dehydrogenase-subunit-beta
MAEKMALAKAINESLRKALESDPKVLVMGEDVGKLGGVFRVTDGLQKDFGESRVIDTPLAESGIVGTAIGLALRGYRPVVEIQFDGFVFPAYDQIVTQLAKMHARALGKIKMPVVIRIPYGGGIGAVEHHSESPESLFAHVAGLKVVSPSNAGDAYWMMQQAIQSDDPVIFFEPKRRYWDKGEVDPEAIPGPLHKARVVREGTDLTLVAYGPMVKLCQEAAAAAAEEGKNLEVLDLRSVSPLDFDSIQASVEKTRRLVVVHEAPVFFGSGAEIAARITERCFYHLEAPVLRVGGYHAPYPPARLEDEYLPGLDRVLDTVDRALAY
>NZ_CP023703.1|WP_150471899.1|4079516_4080767_+|pyruvate-dehydrogenase-(acetyl-transferring)-E1-component-subunit-alpha
MTVESTAARKPRRSAGGKAGATGTGTGTETAAEATGTGAKRAPRTTRAAARKGTAEPQLVQLLTPEGKRVKNAEYDPYVADVTPDELRGLYRDMVLTRRFDAEATSLQRQGELGLWASLLGQEAAQIGSGRALRDDDYVFPTYREHGVAWCRGVDPANLLGMFRGVNNGGWDPNSNNFHLYTIVIGSQTLHATGYAMGVAKDGADSAVIAYFGDGASSQGDVAESFTFSAVYNAPVVFFCQNNQWAISEPTEKQTRVPLYQRAQGYGFPGVRVDGNDVLGCLAVTKWALERARRGEGPTLVEAYTYRMGAHTTSDDPTRYRHDDERAAWEAKDPILRLRRFLEASNHTDEGFFAELEAESEALGRRVREAVRSMPDPDHFAIFENVYADGHALVDEERAQFAAYQASFADAPEGGN
>NZ_CP023703.1|WP_150471898.1|4077974_4078973_-|phosphotransferase
MNHAPPLGALLRRYAAGSALSCEPVDQGLLNRGYRLRTTRGRYFLKHHFDPDTADPVSIVRQHRATQRLADLGVPVAPPLPGRDGRTVAVVGGHAYALHPWVDGRHRHGAQLTAGACGRLGALLGVVHASLERVMPAHARARATPAESPADTFTLIDDLLARVRRHRPADSFDELARHRLLERRTLLERHADRRPPHSGPVGWVHGDFHPFNVLYRGDAPAAIVDWDRLGVQPRAEEAVRAAAIFFVRPDGTLDLPKARAYARAYRPAAGATPSELAAAVHRVWWERLNDFWMLRWHYERGDTRADPQFPAASALAVWWTQEYDAVCDAFTD
>NZ_CP023703.1|WP_150471897.1|4076273_4077878_+|protein-kinase
MAQQQRAQGPSDPEATGGGMSDAPEMWGNGGLVGDGRYRLTGRLGRGGMAEVFAAEDVRLGRTVAVKLLRADLAEDPVSKARFTREAQSVAGLNHHAIVAVYDSGEDVVGSQSVPYIVMELVEGRTIRDLLLNAEAPGPEQALIIVSGVLEALAYSHQHGIVHRDIKPANVIITDNGAVKVMDFGIARALHGASTTMTQTGMVMGTPQYLSPEQALGKAVDHRSDLYATGCLLYELLSLRPPFTGETPLSVVYQHVQDIPVPPSQTSEGVCPPELDGLVMRSLAKDPDDRFQTAEEMRGLIQYGLQMLYEQGAHTGTWNTGPVGAGTGAGAAAAGFASTTALPHGADGSHTSQIPQPILPRGYGNGDDGGFEGRGNRGSGRGKLWILAVLAVIAIAAGVALALNNRDTGGGKTGTTTSPSATPSASDDQASESPSASPSEESTEDTSEGSTGSNSGSNWTPSYTPSYSPSPSYSSEPSDEPSDPVTSDPVTEEPTGSESSDPGTADGGTGDGGTSEGGGTITGVTGGGSAGDDG
>NZ_CP023703.1|WP_150471896.1|4074301_4075927_-|protein-kinase
MSQDGAQGRYAGRALAGGRYQLRDLLGEGGMASVHLAYDSVLDRQVAVKTLHTELGREQAFRERFRREAQAVAKLTHTNIVSVFDTGEDDVDGLTTPYIVMEYIEGRPLGSVLDEDVRGQGAMPADKALKITADVLAALEISHEMGLVHRDIKPGNVMMTKRGVVKVMDFGIARAMQSGVTSMTQTGMVVGTPQYLSPEQALGRAVDARSDLYSVGIMLFQLVTGRLPFDADSPLAIAYAHVQEEPVAPSSINRALPPAVDALVARALKKNPNERFPNAVAMRDECLRVAASFQPAPPSIVAGTPSQSGSGVGSAVFPPVGQNSQAPVGNVQTPYQPAPTPNPYGTPSTPAPSYGYPQQGYQTPAPAYGHQQGPNTSPAYTMSPQAGGAPGGGRKNSTGALVGSAIVVLATIGALIGTLAANGNDDDKPTDPLTPTASPSQVAGYRGPDTAKTIETSECTEPQEAYNDPDKIRLPDFKFKNIDSVKACFQAAGWTIKEKDLDENTYGDGTVMNQFPSAGTDVDPEDMPEIELSVSTGNPPS
>NZ_CP023703.1|WP_150474596.1|4073662_4074211_+|DUF2587-domain-containing-protein
MEMPRNERSPENAQKILVVGQDGMALGGIDADDDSRETPVTEQVEQPAKVMRIGSMIKQLLEEVRAAPLDEASRVRLKEIHASSVKELEDGLAPELVEELERLSLPFNEDSTPSDAELRIAQAQLVGWLEGLFHGIQTTLFAQQMAARAQLEQMRRALPPGVGGHEDSDDPRAGGRSGGPYL
>NZ_CP023703.1|WP_150471895.1|4072744_4073110_-|hypothetical-protein
MPSASSATPDRAGSRAGEGRIRPGRTGEAAEADPEVRDEETAVAEEEGLGDEDGFGAEPTAEAPREAGLVPSASPHTVRRADAAEEQPVGRMLRILPLGSGLVLIGLGLGLAFVGLRLRRD
>NZ_CP023703.1|WP_150471894.1|4071745_4072726_+|zinc-binding-dehydrogenase
MHAITIPEPGGPEALVWDEVPDPVPGEGEVLVEVVASAVNRADVLQRQGFYNPPPGASPYPGLECSGRIAALGPGVSGWAVGDEVCALLAGGGYAEKVAVPAGQLLPVPEGVDLVRAAALPEVACTVWSNVFMISHLRPGETLLVHGGSSGIGTMAIQLAKAVGATVAVTAGSKEKLERCAELGADILINYREQDFVAEIEQATDGAGADVILDNMGAKYLDRNVRSLAVNGRLAIIGMQGGVKAELNIGLLLGKRAAISATSLRARPLGEKASIVAAVREHVWPLLAAGHVRPVVDRELPMSEAGAAHRVVEESGHVGKVLLVAR
>NZ_CP023703.1|WP_150471902.1|4085962_4087258_-|MFS-transporter
MSNITRPGDPPGGRRAAAVWGIGVSVYFVAVIFRTSLGVAGLDAADRFHVNASALSTFSILQLLVYAGMQIPVGLLVDRLGTKKVLAIGVVLFTAGQLGFAFSPTYGTALASRALLGCGDAMTFISVLRLGSRWFPARRGPLVAQLAGLAGMAGNLVSTLLLARLLHGIGWTPAFAGSSLAGVVVLVLLLVFLKDHPEGHEPEPFPHRGAAYVRRQISASWREPGTRLGLWVHFTTQFPAMVFLLLWGMPFLVEAQDLTRATAGELLTLVVLSNMAVGLVYGQVVARHHEARLPLALGTVGATALVWATTLAYPGDHAPMWLLIVLCAVLGACGPASMLGFDFARPANPPERQGTASGITNMGGFVASMTTLFAVGVLLDATGDDYRIAFSSVFVLQALGVSQILRLRSRAARREKERLVASRVSSVHVPA
>NZ_CP023703.1|WP_150471903.1|4087254_4087929_-|FCD-domain-containing-protein
MSPASAAPAPATVKQPPAADRVYAHVKQGVLDRRYEGGVLLTEGELAEAVGVSRTPVREALLRLEAEGLIKLYPKKGALVLPVSAQEIKDVVETRLLVEEHAARKAVPAPAGLIRRLEELLEQQKAQAAAGDLAGAAVTDRCFHAEIVRSGGNDILSRLYDQLRDRQLRMGVAVMHSHPDRIAKTLAEHEEILQALRSGDAEAAVGIVHRHVGWFSHLARGEVR
>NZ_CP023703.1|WP_150471904.1|4088187_4089090_+|D-alanyl-D-alanine-carboxypeptidase
MITATKGFRVRRAAAVAVTAGAMLSTGVLFAAPAQAVTVPTITAKSGFVMNSATGTALYTKSADTRRLTASTTKIMTAKVVLSQANLNLDAKVTIQKAYSDYIIANNYASNAKLIVGDRVTVRQLLYGLMLPSGCDAAYALADKFGTGTTRAARVKSFIGKMNTMAKSLGMKNTHFDSFDGISRGSNYSSVRDLTLLGRSAMKSATFRGVVKAKSYTARTITKTGATRTMGAWTNTNTLLGWNGTLGIKTGSGTEAKYCLVFAATLNGESVMGAVLTSSSAANRTADVQKLIKFGYAKIS
>NZ_CP023703.1|WP_150471905.1|4089161_4089986_-|maleylpyruvate-isomerase-family-mycothiol-dependent-enzyme
MSLHPTLQSYADAWTHSIEAISELVQPLVEGEWNRRTPCPGWSVRDLVSHVIGLDSEMYGDPRPIHTLPRDLFHVTNDFQRYMEMQVDVRRHHTAPEMTSELELSIIRRNRQLRNENRQPNTMVRGHLGTELTLEESMRNHAFAVWVHEQDLRTALGRPGNLDSPGAHIARDVLLDALPAVVAEKADAPRSSAIVFDVHGPVEFLRTIRVDIQGRGTLETAPALGPAAAFSLDWETYVRLACGRVTPEAVADRVKAEGEPELTAAVLRNFAVTK
>NZ_CP023703.1|WP_150471906.1|4090208_4091006_+|carbon-nitrogen-family-hydrolase
MRASLIQIAVDEGESVESRRERVASLVREQAGVADLVVLPELWTTGAFAYEEFAAEAEPLDGPTHEAMAKAASDAGVWLHAGSIPERDPDGPLYNTSLVFSPSGERAAAYRKIHRFGFDKGEAVLMGAGRDLVTVRLPETTVGVATCYDLRFPELFRGLVDAGAETLVVSAGWPERRRAHWTLLAQARAVENQAFVLACGTAGTHAGVPQAGHSIVVDPWGEVLAEAGPGEEILTVEFDPAKVARTREQFPALKDRVLGLEPPRR
>NZ_CP023703.1|WP_150471907.1|4091032_4091527_-|hypothetical-protein
MRFLVRDRILGFGDDYWIEDEQGNKVFLVDGKAIRLRDTFELKDTRGRVLIDIHQKMFALRDTMVIERDGEPLATIRRKRLSLLRNHYRVSLADGRTVLDVSGKILDREFAVEYDGELLAVISRRWLSVRETYGVDVVRDDADPALLIAVAVCVIHLAEKERED
>NZ_CP023703.1|WP_150471908.1|4091523_4092525_-|helix-turn-helix-domain-containing-protein
MPQGSSQSRPHRVAVIVDEGTNPFEVGVATELFGLPRPELGLDRPPYEVTLCAPTPGVRMNHGFFTLTGVPGLEAVDDADTLVVPGRPDNVVPRGAAVLDAIRRTHARGARILSFCTGSFALAEAGLLDGRRATTHWLWADTFRELHPKVLLEPDVLFVDEGDLLTAAGSAAALDLGLHLWRRDHGAEAANHVSRRLVFAAHRDGGQQQFVERPVPDVPDESLGPLLVWAQERLGEPLTVADLAARAALSPATLHRRFRAQLGTTPLAWLTGERVALACRLIERGEERLDVVAARSGLGTAANLRARVRRETGLSPSAYRRRFGPPAGEAVMA
>NZ_CP023703.1|WP_150471909.1|4092577_4092964_+|cupin-domain-containing-protein
MEPVSLPQALASFTDRWSPRIVTAVNDYDVRVAKAEGEHVWHVHDHTDEFFLVLDGELHISLREPGGERTVVLPRGSVFTVPRGIEHKPYAPVLTEILLFEPTGTSTVGDHHDAVPAHVDATTGHALS
>NZ_CP023703.1|WP_150474597.1|4092968_4093163_-|DUF397-domain-containing-protein
MKSCHWQKSSFSGGGGDTNCLEIAAAPTTLHLRESDTPATTLSPTPTALTALLAAVKAATTSPR
>NZ_CP023703.1|WP_150471910.1|4093419_4095183_+|redoxin-domain-containing-protein
MTDSAPRRVRVRAPELIGKGGWLNTGGKQYSLADLRGRILVLDFWTFCCVNCLHVLDELRALEQKHRDTLVVIGVHSPKFVHEAEHEAVADAVERYGVEHPVLDDPELATWKQYAVRAWPTLVVVDPEGYVVAQHAGEGHVHAIGRLVTELEAEHAAKGTLRRGGGPYVAPQPEPTDLRFPGRAVVLPSGKLLVSDTTRHQLVELAADGETVVRRIGQGSRGSTDSTWVRSRFSEPQGLALLPDGSVVVADTVSHRVRRFDPESGRTTTLAGTGFQWMRGDDTSGPAREVNLSSPWDVAWWEGKVWIAMAGVHQLWTYDPAEGTVRVAAGTANEGLVDGPAAEAWFAQPSGLAATPDRLWVADSETSALRWLDRDGVVHTAVGTGLFDFGHRDGPAGQALLQHPLGVTALADGSVAVSDTYNHALRRYDPATDEVTTLATDLREPSGAVLVGDDIVVVESAHRTQCAPTEVAPGRLRLDVTFPAPAGQKLDTRYGPSTRLLVSATPPELLLTGAGAGAGPDLSRTLELNPAVPEGVLHVSAMAASCDDDSSVEYPACHVHRQDWDVPLILTESGADRLPLVQAGLGA

Crispr_ID: NZ_CP023703_5

• CRISPR_ID: NZ_CP023703_5
• CRISPR_location: 4622021-4622104
• CRISPR_type: Orphan
• Repeat_type: NA
• Spacer_info: 1 spacers

Consensus repeat of NZ_CP023703_5

Consensus_repeat	Method
TTCGAGGCATTCGCCGCCCTCGCC	CRISPRCasFinder

spacers of NZ_CP023703_5

>5.1|4622045|36|NZ_CP023703|CRISPRCasFinder
ACCGCTGTAGGTCGACTTACGCCAGGTGTAGGCGGC

CRISPR arrays and Neighbor proteins around NZ_CP023703_5

CRISPR arrays

The CRISPR arrays of NZ_CP023703_5

>merge|NZ_CP023703|5|4622021-4622104|CRISPRCasFinder
TTCGAGGCATTCGCCGCCCTCGCCACCGCTGTAGGTCGACTTACGCCAGGTGTAGGCGGCTTCCAGGCATTCGCCGCCCTCGCC

>NZ_CP023703|5|5|4622021-4622104|CRISPRCasFinder
TTCGAGGCATTCGCCGCCCTCGCC	ACCGCTGTAGGTCGACTTACGCCAGGTGTAGGCGGC
TTCCAGGCATTCGCCGCCCTCGCC

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP023703.1|WP_086771194.1|4613658_4614114_+|Lrp/AsnC-family-transcriptional-regulator	unknown	unknown	gnl|CDD|214628
NZ_CP023703.1|WP_150472277.1|4626566_4627376_+|hypothetical-protein	unknown	unknown	unknown
NZ_CP023703.1|WP_086770891.1|4623708_4624227_+|SigE-family-RNA-polymerase-sigma-factor	unknown	unknown	gnl|CDD|132028
NZ_CP023703.1|WP_086771193.1|4614182_4615346_+|aminofutalosine-synthase-MqnE	unknown	unknown	gnl|CDD|213851
NZ_CP023703.1|WP_150474633.1|4612877_4613540_+|UbiX-family-flavin-prenyltransferase	unknown	unknown	gnl|CDD|223241
NZ_CP023703.1|WP_150474635.1|4627543_4629283_+|3-oxosteroid-1-dehydrogenase	unknown	unknown	gnl|CDD|236111
NZ_CP023703.1|WP_150472268.1|4617421_4618066_+|TetR-family-transcriptional-regulator	unknown	unknown	gnl|CDD|224228
NZ_CP023703.1|WP_150474634.1|4623168_4623624_+|ATP-binding-protein	unknown	unknown	gnl|CDD|340413
NZ_CP023703.1|WP_150472278.1|4629505_4630150_-|methyltransferase-domain-containing-protein	unknown	unknown	gnl|CDD|379312
NZ_CP023703.1|WP_150472274.1|4624219_4624813_+|hypothetical-protein	unknown	unknown	unknown
NZ_CP023703.1|WP_167535040.1|4624965_4625451_+|hypothetical-protein	unknown	unknown	unknown
NZ_CP023703.1|WP_150472271.1|4621421_4621922_+|hypothetical-protein	unknown	unknown	unknown
NZ_CP023703.1|WP_150472269.1|4618230_4619079_-|hypothetical-protein	unknown	unknown	gnl|CDD|366711
NZ_CP023703.1|WP_150472265.1|4615705_4616365_+|UdgX-family-uracil-DNA-binding-protein	unknown	unknown	gnl|CDD|274850
NZ_CP023703.1|WP_150472270.1|4619462_4621388_+|AMP-binding-protein	unknown	unknown	gnl|CDD|341233
NZ_CP023703.1|WP_150472266.1|4616391_4616916_+|GNAT-family-N-acetyltransferase	unknown	unknown	gnl|CDD|366181
NZ_CP023703.1|WP_150472276.1|4625566_4626262_+|hypothetical-protein	unknown	unknown	unknown
NZ_CP023703.1|WP_150472267.1|4617052_4617352_+|DUF4229-domain-containing-protein	unknown	unknown	gnl|CDD|379415
NZ_CP023703.1|WP_150472279.1|4630199_4630487_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP023703.1|WP_150472273.1|4622145_4623009_-|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl|CDD|238045

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
NZ_CP023703.1|WP_150472278.1|4629505_4630150_-|methyltransferase-domain-containing-protein	gnl|CDD|379312	pfam13649, Methyltransf_25, Methyltransferase domain. This family appears to be a methyltransferase domain.	5.23457e-25
NZ_CP023703.1|WP_086770891.1|4623708_4624227_+|SigE-family-RNA-polymerase-sigma-factor	gnl|CDD|132028	TIGR02983, putative_RNA_polymerase_ECF-subfamily_sigma_factor, RNA polymerase sigma-70 factor, sigma-E family. This group of similar sigma-70 factors includes the sigE factor from Streptomyces coelicolor. The family appears to include a paralagous expansion in the Streptomycetes lineage, while related Actinomycetales have at most two representatives.	3.91266e-38
NZ_CP023703.1|WP_150474633.1|4612877_4613540_+|UbiX-family-flavin-prenyltransferase	gnl|CDD|223241	COG0163, UbiX family flavin prenyltransferase [Coenzyme transport and metabolism].	2.322e-64
NZ_CP023703.1|WP_150474635.1|4627543_4629283_+|3-oxosteroid-1-dehydrogenase	gnl|CDD|236111	PRK07843, PRK07843, 3-oxosteroid 1-dehydrogenase.	0
NZ_CP023703.1|WP_150472267.1|4617052_4617352_+|DUF4229-domain-containing-protein	gnl|CDD|379415	pfam14012, DUF4229, Protein of unknown function (DUF4229). This family of integral membrane proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 95 and 122 amino acids in length.	3.61859e-15
NZ_CP023703.1|WP_150474634.1|4623168_4623624_+|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.	3.81161e-16
NZ_CP023703.1|WP_150472269.1|4618230_4619079_-|hypothetical-protein	gnl|CDD|366711	pfam01575, MaoC_dehydratas, MaoC like domain. The maoC gene is part of a operon with maoA which is involved in the synthesis of monoamine oxidase. The MaoC protein is found to share similarity with a wide variety of enzymes; estradiol 17 beta-dehydrogenase 4, peroxisomal hydratase-dehydrogenase-epimerase, fatty acid synthase beta subunit. Several bacterial proteins that are composed solely of this domain have (R)-specific enoyl-CoA hydratase activity. This domain is also present in the NodN nodulation protein N.	7.13171e-10
NZ_CP023703.1|WP_086771194.1|4613658_4614114_+|Lrp/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).	4.19013e-35
NZ_CP023703.1|WP_086771193.1|4614182_4615346_+|aminofutalosine-synthase-MqnE	gnl|CDD|213851	TIGR03700, mena_SCO4494, putative menaquinone biosynthesis radical SAM enzyme, SCO4494 family. Members of this protein family appear to be involved in menaquinone biosynthesis by an alternate pathway via futalosine, based on close phylogenetic correlation with known markers of the futalosine pathway, gene clustering in many organisms, and paralogy with the SCO4550 protein. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone].	0
NZ_CP023703.1|WP_150472265.1|4615705_4616365_+|UdgX-family-uracil-DNA-binding-protein	gnl|CDD|274850	TIGR03914, SPO1_DNA_polymerase-related_protein, uracil-DNA glycosylase family domain. This model represents a clade within the uracil-DNA glycosylase superfamily. Among characterized proteins, it most closely resembles the Thermus thermophilus uracil-DNA glycosylase TTUDGA, which acts uracil (deamidated cytosine) in both single-stranded DNA and U/G pairs of double-stranded DNA. This domain may occur either as a stand-alone protein or as the C-terminal domain of a fusion with another domain that always pairs with a particular radical-SAM family protein.	5.51285e-79
NZ_CP023703.1|WP_150472270.1|4619462_4621388_+|AMP-binding-protein	gnl|CDD|341233	cd05907, VL_LC_FACS_like, Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases. This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.	0
NZ_CP023703.1|WP_150472266.1|4616391_4616916_+|GNAT-family-N-acetyltransferase	gnl|CDD|366181	pfam00583, Acetyltransf_1, Acetyltransferase (GNAT) family. This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.	2.51755e-10
NZ_CP023703.1|WP_150472268.1|4617421_4618066_+|TetR-family-transcriptional-regulator	gnl|CDD|224228	COG1309, AcrR, Transcriptional regulator [Transcription].	2.53744e-14
NZ_CP023703.1|WP_150472273.1|4622145_4623009_-|helix-turn-helix-domain-containing-protein	gnl|CDD|238045	cd00093, HTH_XRE, Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the xenobiotic response element family of transcriptional regulators.	4.50941e-09

Protein sequences

>NZ_CP023703.1|WP_150472271.1|4621421_4621922_+|hypothetical-protein
MPPVNAIEFFHYPWAESPTYPDYLVWGIRVDGTDLRALVGEATYTLWRAELAGEFDDEAEDEKETAEQVRTQHDGLGVPEFEDHHFRTQGDAVPLLGCSCGIWGCWPLMAKVTVTPTAVTWSAFHQPYREEEWGELALGPYEFPRDAYEAAVCAPLVLSEDPLPLP
>NZ_CP023703.1|WP_150472270.1|4619462_4621388_+|AMP-binding-protein
MSTPYSSSTPAFAGYDAPPALVEPETRRLDGVVREASMPVFARPMTYGSLAELPFDNAGAAPDAVVLSRRDAEGRWADVTAQQFAAEVLAVAKGLIGEGLAPGDRIAIMARTTYEWTLLDFAAWAAGLVTVPVYPTSSVFQTRWILQDSGAVALVTETLGQAAAIGPERDRLPDLQHIWVIEKGHVERLAELGEQHIPESEVEVRRGMLVPDTLATLIYTSGTTGRPKGCALTHGNFFAEVDNAIELLYPVFKSATDDLSVLLFLPMSHVFGRMVAIACIRARVRLGHAPSLKADQLLPDLAAFRPTCLLAIPYMLEKIFNTARAKAEAGGRVSTFDRAVNTAIRYGEAVEAHNAGTGSGPGATLRAGRALYDPLVYRRIRNAMGGRVRHAICGGSPLGRRLAAFYAGAGIEIYEGYGLTETTGASTVTPPMKPRLGTVGWPLPGTKIRIAADGEILIAGDHVLRGYWDPAAGGVVPAAPDGWLATGDIGELDDEGYLTITGRKKELIITSGGKSVAPAPLENWLRSHPLISQAMVLGDGRPYVSALLTLDPDGLTHWRQMNGKHPVPAELLIDDVELNDVLQRAIDEANKLVSRPESIRRFTILPRDFTEAEGHLTPSMKLRRDVIMRDFADEMEGLYGQ
>NZ_CP023703.1|WP_150472269.1|4618230_4619079_-|hypothetical-protein
MTAPPLSASPALGPLLARGALLSPFKRPRPGAAFSGGRLVLPGLRVDLARLAAYERVCGFPTGDDALPITYPHVLGFPLAMRIMSGRGFPLPLLGLVHTSISLTRHRPLPATGTTYELAVHVDRLVPHRRGTEAVVVTELREAGEVVWESESRYLARHRTDGEVPEPAPGSGEPPLPVVDEWRLGADIGRRYGAVSGDRNPIHLSPLTARLFGFPRAIAHGMWTATCCLAAHGTPAAAHVAVDFRAPVLLPGTVAFAAQGRRFELRGTGGDGERVHVRGRVG
>NZ_CP023703.1|WP_150472268.1|4617421_4618066_+|TetR-family-transcriptional-regulator
MGAVKTKRMPRAVREQQMLDAAVETFGRRGYMAASMDEIAELAGVSKPLVYLYLNSKEDLFTACIRREAEALVGAVRAGVDTGLPADRQLWDGLLAFFAHTGRHPHAWSVLHIQARTHGETFAAEAAAMRAEIVAFVTQLIVVAAREAHRDPDLPEREVAGLAEALVGAAESLAAWANTAESVTPRQAAATLMNFAWAGLGNLMTGHPWSPPEP
>NZ_CP023703.1|WP_150472267.1|4617052_4617352_+|DUF4229-domain-containing-protein
MLRYTLMRLGVFVGCLAAVWGLVYLGVFPRGLGDSNGMWIVLLSLVLSAPLSFVLLRKERDRASETVVRRVDRMKAGLESNRSQEDEAADSAHAQGQAS
>NZ_CP023703.1|WP_150472266.1|4616391_4616916_+|GNAT-family-N-acetyltransferase
MALTFTLDPAVTPGLRDGVLDLWTDVSNAGGAVGFVPPVTREAVRPELVRHLVQMAEGRTHLLVGLDETGEVAATAFLTFNTHRLMTHWLWLYTVMVHPRHQGRGYGRDLLTAAAEAARTFDGIDAIRLTCRGGQGLERFYASCGYKEVGRVPDAIRVAPGDDRDDVTMLLPLI
>NZ_CP023703.1|WP_150472265.1|4615705_4616365_+|UdgX-family-uracil-DNA-binding-protein
MTPRTTPAPEDQYTAAPFIPEGPLTLPALREAAVGCEGCPLHRNATRTVFGAGKATARVMLVGEQPGDQEDRQGKPFVGPAGRLLDRALEEAGLDPTDAYVTNAVKHFKFTQAEPRKRRIHKAPTLREMTACAPWLAAELTVVEPELIVVLGATAGKALLGSSFKVTEVRGTVLEREIHGHPERLVPTVHPSSVLRSDDREAAYRGLVGDLEVAARVLS
>NZ_CP023703.1|WP_086771193.1|4614182_4615346_+|aminofutalosine-synthase-MqnE
MDVGLKRELEQKVRAGERLTREDGIALYESDDLAWLGGLAHEVRTRKNGDVVHFNVNRHLNMTNVCTASCAYCSFQRKPGEKDAYTMRIEEAVKLAKAMESENLTELHIVNGLHPNLPWRYYPRSLRELKAALPHVSLKAFTATEIHHFETISGLSASEILDELIDAGLESLTGGGAEIFDWEVRQHIVDHRTHWEDWSRIHRLAHEKGLKTPSTMLYGHIEEPRHRVDHVLRLRELQDETGGFQVFIPLRYQHDFVDMKDGKVRNRLQARTQMATGAEALKTFAVSRLLFDNVPHVKVFWVMHGVQTAQLALQHGADDMDGSVVEYKITHDADNYGTPNKLTREDLLDLIRDAGFRPVERNTRYEIIREYDAPDPARRESPQPMRL
>NZ_CP023703.1|WP_086771194.1|4613658_4614114_+|Lrp/AsnC-family-transcriptional-regulator
MDAVDRQLIQALRENGRASYAELGRLVGLSGPSVTDRINRLEAAGVITGYRATVNAAQLGLGVTALIGISLSDAADHEDVAARMKDLSEIEDCWFIAGDDSFMLKVRANDVDGLEKIIRRLSGTKGVSRTRTTIVLSTKWENRVGELPEEV
>NZ_CP023703.1|WP_150474633.1|4612877_4613540_+|UbiX-family-flavin-prenyltransferase
MPWIVGVSGASGTPYAAAVLRALLAGGESVDLVVSRASRLTLLDETGISFRDAHWRDDLRDWLARGADGKPDTFDVGADLDTDAVRYWGAGDLAAGPSSGSYPAKGMLIVPASTACVAGVALGLSKDLLQRAASVTLKERRTLVVAVRETPLSGQTLRHLVALDDAGASVVPASPAFYAGATHIQDLVDFVAGRVLDSAGVPHGLYRRWTGELGGATRPA
>NZ_CP023703.1|WP_150472273.1|4622145_4623009_-|helix-turn-helix-domain-containing-protein
MQEERERRPETPAEADGTTGLFTALGKMLKRLRERKGLTQKEFGLLVGYGPDAISSMERGVRLIRPEVLEKADAILDAGGMLADAIPEVREAMSRVRTRHPEWYRGYAALEAEAVELHFYANQAMPGLLQTEEYALAVFGQRRPFLSRETIEKRVVDRLSRQQVFDRWPSPIVSYVLEEVLLDRPIGGSSIFKGQLLNLLRVGEMRNVAIQVMPTRLEEHPNLDSAFNLLTPKKHAQVAYTESQGYPRLITDPEEVRKITDRYGIMRAMALPPKDSRALIETKLEEL
>NZ_CP023703.1|WP_150474634.1|4623168_4623624_+|ATP-binding-protein
MSTQRSTPLGELTLRLSSTPRGARLARRMTAQQLDAWGYPHDGDANDTAQHVVAELAANAVTHGRVPGRDFELRLLLLAEGTLRVEVSDTRGDRQLRIVTDPEAEGGRGLVLVAVLARTWGVDERDVGKTVWAELPLRARGERATVPSRVR
>NZ_CP023703.1|WP_086770891.1|4623708_4624227_+|SigE-family-RNA-polymerase-sigma-factor
MDEQAFDAFYAGSVGRLIGQLYAMIGDRGEAQDVVQEAFVRAWEHRARLDEDGAPEAWVRTVAWRLAVSRWRRVRTSLSFARRQGPPPNVPPPDTHHVLLVQALRQIPAAQRRVIVLHHLCDLEVKQVAAETNSPVGTVKAQLSRGRAALARILADTELDPRAGRVSEVEHG
>NZ_CP023703.1|WP_150472274.1|4624219_4624813_+|hypothetical-protein
MADETGLDDHLARLAADGRRFAVPMAAEQIRVRGDRRLRRKRAVRMSGGVLVAAAVAVGGLSLVLSGRGPAPTAAKPTPSLSAPRFVPPTPAPGEEYAVEIGYVYDARVLADGIQVTVKQLRTERGTAVPTGVVHKLTLSPQTPVEVEQVAGGKPGDMRLEELVDRLSGGPRWVFAVDYDGEGRIQSLREAVWLTVE
>NZ_CP023703.1|WP_167535040.1|4624965_4625451_+|hypothetical-protein
MRLLSVVAFGSLALTGCGEGKEPADPTDPTAVAASTGKTPWAGTKQFVTVDKVWAEGGLTYLSVRPAEKKVNTQFDTWEIIPGTGAFTTVTMAKDARVLLTAPVRGDDASGAGRGEPLPASQAEFVTLLTQLDAGTAAGVGYDLSFDGQGRVAKLQSLYRP
>NZ_CP023703.1|WP_150472276.1|4625566_4626262_+|hypothetical-protein
MTNTARRRNTRRWLAVVALGALAVTGCGSQKPADRPESAAAAKPASTSESGDRTDARSQGGTESVAPAESPKKASPSAPAGNAGTRTDGGQKSAEPAAAAKETSASAGQAAFAGTQQFVTIGKAWTEGGLTRLSVRPAEKKVNTQFDTWEIIPGTGPFTTVTMTKDARVLLACPVRDEVAGTSRAEPLPYSPTRFVALLNQMDSGLQDGIGYDLVFDGAGQVTSLKSLYRP
>NZ_CP023703.1|WP_150472277.1|4626566_4627376_+|hypothetical-protein
MRRVRKNLAAFAVTAALVGAGTLAGASSASAATTWQAMDKVCTSYTALDGVTPKGQICAQVQKRVTDTGSVTGWRGRVILSPASGYGMKPTTYHWYTGGALAQVCAGGCTMKTAAWTSTWSPVQTLSSGPYKVQGEFSDGANWDLHASWGMWQTAAEKCATYAAGKVCVRYEVRHYRDIPQERSRLSYAPAGGGHIIPQSIRIGSVIDGVRTSKTLNLCDPSCTTRTSAYSATVTRTTPNPAGTNEYYATGTFKRPNGTTSTLKAAITG
>NZ_CP023703.1|WP_150474635.1|4627543_4629283_+|3-oxosteroid-1-dehydrogenase
MLGAGAGAGLALAAGTQAGAQVTATAAEPPLLGTYDVVVIGSGAAGMTAALTAARRGLSCVVVEKAATFGGSAARSGAGIWIPNNPVILAAGVPDTPAKAAAYLKAVVGPEVAADRQAAFLAHGPAMLSFVMANSPLRFRWMEGYSDYYPELPGGLPGGRSVEPDQLDGNVLGAELARLNPPYMQLPAGMVVFSADYKWLALTAVSVRGAAVAAECLARGTKAALLGQKPLTMGQSLAAGLRAGLLSAGVPVWLSTPLTDLHVEGGRVTGAVVTRDGAAGLVRARRGVVVGSGGFEHNAAMRAQYQRQPIGTEWTVGAKENTGDGIRAGQRVGGSVALMDDAWWGPTIPVPGRPYFCLAERTLPGGLLVDRSGARFVNEAAPYSDVVHTMYDRHPTDPAIPAWLIVDQNYRNRYLFKDVAPTLPLPDDWYSSGAAHKSWTWDGLATAIGVPPAALRATVDRFNSLALRGQDTDFGRGDSVYDHYYTDPAVLPNSCLAPLWLPPFHAFRIVPGDLGTKGGLRTDARARVLRPDDTPIPGLYAAGNASAAVMGHSYAGAGSTIGPAMTFGYLAALDLAGVL
>NZ_CP023703.1|WP_150472278.1|4629505_4630150_-|methyltransferase-domain-containing-protein
MTEASDFLTATRTFYDAIAEDYADHFHDLHAKLPWDRAVFALYAELVGVGGKVADLGCGPGRVTGHLASLGLSMSGLDLSESMLAVARRENPGLRFERGSMLELGHEDGSLDGVVSWYSSIHTPADRLPHLFAEFRRVLKPGGHALLAFQVGEEPRHLEQPWGHPVSLDFHRRTPEGMAGLLAEAGFSVRSRTVRAPEPELDEKVPQAYLVARA
>NZ_CP023703.1|WP_150472279.1|4630199_4630487_-|hypothetical-protein
MENGDGTNGTSDAGGATPAAPLGLAAGLGIGTAVGVALGLTVFDNLGLGLSLGIGLGVAIGAGADAGAGVARKRGETGGTGETGGTPRQAGEAPE

Crispr_ID: NZ_CP023703_6

• CRISPR_ID: NZ_CP023703_6
• CRISPR_location: 4836171-4836310
• CRISPR_type: Orphan
• Repeat_type: NA
• Spacer_info: 1 spacers

Consensus repeat of NZ_CP023703_6

Consensus_repeat	Method
CACACTAGGGGCGGACACTCCGTGAACCATCAGGTGCCTG	CRISPRCasFinder

spacers of NZ_CP023703_6

>6.1|4836211|60|NZ_CP023703|CRISPRCasFinder
CCGCAGTGGCCGCTGCGGTGGGCACCACCTATTTTCGGATGGTGAGCGGCCGCCCCCACA

CRISPR arrays and Neighbor proteins around NZ_CP023703_6

CRISPR arrays

The CRISPR arrays of NZ_CP023703_6

>merge|NZ_CP023703|6|4836171-4836310|CRISPRCasFinder
CACACTAGGGGCGGACACTCCGTGAACCATCAGGTGCCTGCCGCAGTGGCCGCTGCGGTGGGCACCACCTATTTTCGGATGGTGAGCGGCCGCCCCCACACACACTAGGGGCGGACACTCCGTGAACCATCAGGAGCCTG

>NZ_CP023703|6|6|4836171-4836310|CRISPRCasFinder
CACACTAGGGGCGGACACTCCGTGAACCATCAGGTGCCTG	CCGCAGTGGCCGCTGCGGTGGGCACCACCTATTTTCGGATGGTGAGCGGCCGCCCCCACA
CACACTAGGGGCGGACACTCCGTGAACCATCAGGAGCCTG

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP023703.1|WP_150474651.1|4839746_4840892_-|serine-hydrolase	unknown	unknown	gnl|CDD|365903
NZ_CP023703.1|WP_150472394.1|4849892_4851692_+|protein-kinase	unknown	unknown	gnl|CDD|270916
NZ_CP023703.1|WP_150474653.1|4843617_4846137_+|protein-kinase	unknown	unknown	gnl|CDD|270916
NZ_CP023703.1|WP_150472393.1|4848174_4849800_+|protein-kinase	unknown	unknown	gnl|CDD|270916
NZ_CP023703.1|WP_150472391.1|4836414_4837623_-|nucleotide-sugar-dehydrogenase	unknown	unknown	gnl|CDD|223749
NZ_CP023703.1|WP_086770885.1|4829280_4830177_+|LysR-family-transcriptional-regulator	unknown	unknown	gnl|CDD|176115
NZ_CP023703.1|WP_150472392.1|4837926_4839633_+|FAD-dependent-oxidoreductase	unknown	unknown	gnl|CDD|223651
NZ_CP023703.1|WP_150474654.1|4846308_4848084_+|protein-kinase	unknown	unknown	gnl|CDD|270916
NZ_CP023703.1|WP_150472388.1|4826898_4827585_-|SnoaL-like-domain-containing-protein	unknown	unknown	gnl|CDD|377824
NZ_CP023703.1|WP_150472390.1|4830263_4830590_-|WhiB-family-transcriptional-regulator	unknown	unknown	gnl|CDD|376791
NZ_CP023703.1|WP_086770882.1|4832992_4834501_+|IMP-dehydrogenase	unknown	unknown	gnl|CDD|376340
NZ_CP023703.1|WP_150474652.1|4841263_4843402_+|protein-kinase	unknown	unknown	gnl|CDD|270916
NZ_CP023703.1|WP_150472395.1|4851718_4853518_+|protein-kinase	unknown	unknown	gnl|CDD|270916
NZ_CP023703.1|WP_086770883.1|4832162_4832750_+|sigma-70-family-RNA-polymerase-sigma-factor	unknown	unknown	gnl|CDD|236607
NZ_CP023703.1|WP_150472396.1|4853646_4855260_+|aldehyde-dehydrogenase-family-protein	unknown	unknown	gnl|CDD|236501
NZ_CP023703.1|WP_086770881.1|4834627_4835752_+|GuaB3-family-IMP-dehydrogenase-related-protein	unknown	unknown	gnl|CDD|236322
NZ_CP023703.1|WP_150472387.1|4825166_4826792_+|chaperonin-GroEL	unknown	unknown	gnl|CDD|234573
NZ_CP023703.1|WP_086770887.1|4827660_4828434_-|SDR-family-oxidoreductase	unknown	unknown	gnl|CDD|223377
NZ_CP023703.1|WP_150472389.1|4828531_4829200_-|MOSC-domain-containing-protein	unknown	unknown	gnl|CDD|225167
NZ_CP023703.1|WP_003948568.1|4830969_4831581_+|response-regulator-transcription-factor	unknown	unknown	gnl|CDD|225107

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
NZ_CP023703.1|WP_150474651.1|4839746_4840892_-|serine-hydrolase	gnl|CDD|365903	pfam00144, Beta-lactamase, Beta-lactamase. This family appears to be distantly related to pfam00905 and PF00768 D-alanyl-D-alanine carboxypeptidase.	8.93431e-43
NZ_CP023703.1|WP_150472394.1|4849892_4851692_+|protein-kinase	gnl|CDD|270916	cd14014, STKc_PknB_like, Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.	4.63072e-103
NZ_CP023703.1|WP_150474653.1|4843617_4846137_+|protein-kinase	gnl|CDD|270916	cd14014, STKc_PknB_like, Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.	6.13767e-18
NZ_CP023703.1|WP_150472393.1|4848174_4849800_+|protein-kinase	gnl|CDD|270916	cd14014, STKc_PknB_like, Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.	7.05124e-109
NZ_CP023703.1|WP_150472391.1|4836414_4837623_-|nucleotide-sugar-dehydrogenase	gnl|CDD|223749	COG0677, WecC, UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell envelope biogenesis, outer membrane].	7.8035e-127
NZ_CP023703.1|WP_086770885.1|4829280_4830177_+|LysR-family-transcriptional-regulator	gnl|CDD|176115	cd08423, PBP2_LTTR_like_6, The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional regulator, contains the type 2 periplasmic binding fold. LysR-transcriptional regulators comprise the largest family of prokaryotic transcription factor. Homologs of some of LTTRs with similar domain organizations are also found in the archaea and eukaryotic organisms. The LTTRs are composed of two functional domains joined by a linker helix involved in oligomerization: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal substrate-binding domain, which is structurally homologous to the type 2 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcriptional repressor undergoes a conformational change upon substrate binding which in turn changes the DNA binding affinity of the repressor. The genes controlled by the LTTRs have diverse functional roles including amino acid biosynthesis, CO2 fixation, antibiotic resistance, degradation of aromatic compounds, nodule formation of nitrogen-fixing bacteria, and synthesis of virulence factors, to a name a few. This substrate-binding domain shows significant homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.	5.27114e-58
NZ_CP023703.1|WP_150472392.1|4837926_4839633_+|FAD-dependent-oxidoreductase	gnl|CDD|223651	COG0578, GlpA, Glycerol-3-phosphate dehydrogenase [Energy production and conversion].	2.49147e-165
NZ_CP023703.1|WP_150474654.1|4846308_4848084_+|protein-kinase	gnl|CDD|270916	cd14014, STKc_PknB_like, Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.	2.4711e-101
NZ_CP023703.1|WP_150472388.1|4826898_4827585_-|SnoaL-like-domain-containing-protein	gnl|CDD|377824	pfam07366, SnoaL, SnoaL-like polyketide cyclase. This family includes SnoaL a polyketide cyclase involved in nogalamycin biosynthesis. This family was formerly known as DUF1486. The proteins in this family adopt a distorted alpha-beta barrel fold. Structural data together with site-directed mutagenesis experiments have shown that SnoaL has a different mechanism to that of the classical aldolase for catalyzing intramolecular aldol condensation.	1.56833e-30
NZ_CP023703.1|WP_150472390.1|4830263_4830590_-|WhiB-family-transcriptional-regulator	gnl|CDD|376791	pfam02467, Whib, Transcription factor WhiB. WhiB is a putative transcription factor in Actinobacteria, required for differentiation and sporulation.	1.49364e-27
NZ_CP023703.1|WP_086770882.1|4832992_4834501_+|IMP-dehydrogenase	gnl|CDD|376340	pfam00478, IMPDH, IMP dehydrogenase / GMP reductase domain. This family is involved in biosynthesis of guanosine nucleotide. Members of this family contain a TIM barrel structure. In the inosine monophosphate dehydrogenases 2 CBS domains pfam00571 are inserted in the TIM barrel. This family is a member of the common phosphate binding site TIM barrel family.	0
NZ_CP023703.1|WP_150474652.1|4841263_4843402_+|protein-kinase	gnl|CDD|270916	cd14014, STKc_PknB_like, Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.	1.1741e-97
NZ_CP023703.1|WP_150472395.1|4851718_4853518_+|protein-kinase	gnl|CDD|270916	cd14014, STKc_PknB_like, Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.	2.39656e-98
NZ_CP023703.1|WP_086770883.1|4832162_4832750_+|sigma-70-family-RNA-polymerase-sigma-factor	gnl|CDD|236607	PRK09648, PRK09648, RNA polymerase sigma factor ShbA.	1.49928e-89
NZ_CP023703.1|WP_150472396.1|4853646_4855260_+|aldehyde-dehydrogenase-family-protein	gnl|CDD|236501	PRK09407, gabD2, succinic semialdehyde dehydrogenase; Reviewed.	0
NZ_CP023703.1|WP_086770881.1|4834627_4835752_+|GuaB3-family-IMP-dehydrogenase-related-protein	gnl|CDD|236322	PRK08649, PRK08649, GuaB3 family IMP dehydrogenase-related protein.	0
NZ_CP023703.1|WP_150472387.1|4825166_4826792_+|chaperonin-GroEL	gnl|CDD|234573	PRK00013, groEL, chaperonin GroEL; Reviewed.	0
NZ_CP023703.1|WP_086770887.1|4827660_4828434_-|SDR-family-oxidoreductase	gnl|CDD|223377	COG0300, DltE, Short-chain dehydrogenases of various substrate specificities [General function prediction only].	4.75604e-81
NZ_CP023703.1|WP_150472389.1|4828531_4829200_-|MOSC-domain-containing-protein	gnl|CDD|225167	COG2258, COG2258, Uncharacterized protein conserved in bacteria [Function unknown].	5.29808e-59
NZ_CP023703.1|WP_003948568.1|4830969_4831581_+|response-regulator-transcription-factor	gnl|CDD|225107	COG2197, CitB, Response regulator containing a CheY-like receiver domain and an HTH DNA-binding domain [Signal transduction mechanisms / Transcription].	1.73082e-50

Protein sequences

>NZ_CP023703.1|WP_086770881.1|4834627_4835752_+|GuaB3-family-IMP-dehydrogenase-related-protein
MTEIEIGRGKRGRRAYAFDDIAVVPSRRTRDPKEVSIAWQIDAYRFELPFLAAPMDSVVSPATAIRIGELGGLGVLNLEGLWTRYEDPQPLLDEIVGLPVEAATRRLQEIYSAPIKEELIGQRIKEVRDSGVVTAAALSPQRTAQFSKAVVDAGVDIFVIRGTTVSAEHVSGSHEPLNLKQFIYELDVPVIVGGCATYTAALHLMRTGAAGVLVGFGGGAAHTTRNVLGIQVPMATAVADVAAARRDYMDESGGRYVHVIADGGVGWSGDLPKAVACGADAVMMGSPLARATDAPGRGHHWGMEAVNEELPRGQKVDLGTVGTIEEVLAGPSHTPDGSMNFFGALRRAMSTTGYSELKEFQRVEVTVADSVHRR
>NZ_CP023703.1|WP_086770882.1|4832992_4834501_+|IMP-dehydrogenase
MTANVDGVPGKFATLGLTYDDVLLLPGPSDMAPDEIDTASYVSRNVRVNIPLLSAAMDKVTESRMAISMARQGGVGVLHRNLSIADQANQVDLVKRSESGMVTDPITIHPDATLGEADALCAKFRISGVPVTDGNKRLLGIVTNRDMAFETDRTRRVREVMTPMPLVTGKVGISGVEAMELLRRHKIEKLPLVDDEGHLKGLITVKDFVKAEKYPLAAKDSEGRLLVGAAVGVAGDAFERAQALIEAGADFIVVDTAHGHSRLVGDMIAKIKSNHTRVDVIGGNVATRDGAQSLVDAGADAIKVGVGPGSICTTRVVAGIGVPQVTAIYEAALAAKEAGVPVIGDGGLQYSGDIAKALVAGADTVMLGSLLAGCEESPGELLFINGKQFKSYRGMGSLGAMQTRGERKSFSKDRYFQEGVASDEQLIPEGIEGQVPYRGPLSSVVHQLVGGLRQSMFYVGGRTVPELQDNGRFVRITSAGLKESHPHDIQMTVEAPNYSGKK
>NZ_CP023703.1|WP_086770883.1|4832162_4832750_+|sigma-70-family-RNA-polymerase-sigma-factor
MREDEAVRAPGVIGGLVHRAVDGDEQATHDLLAHVHPLALRYCRTRLSRLPGDARHFVEDLAQEVCVAVLLALPRYKDTGRPFEAFVFAIAAHKVADLQRAAMRHPGSTAVPSDEMPERPDDSLGPEERALLSSDAEWAKKLLANLPENQRELLLLRIAVGLTAEETGQMLGMSPGAVRVAQHRALSRLRALAEQ
>NZ_CP023703.1|WP_003948568.1|4830969_4831581_+|response-regulator-transcription-factor
MTSVLVCDDSPLAREALRRAVATVPGVERVTTAANGEEVLRRWGADRSDLILMDVRMPGLGGVETVRRLLSADPGARIIMLTVAEDLDGVALAVAAGARGYLHKDASRAELRATVTQALADPTWRLAPRRLRSAEMGAAPTLTAREIQVLEGMSHGRSNAEIGRELFLSEDTVKTHARRLFKKLGASDRAHAVALGFRWGLVR
>NZ_CP023703.1|WP_150472390.1|4830263_4830590_-|WhiB-family-transcriptional-regulator
MADFSRLPGPNADLWDWQLLAACRGVDSSLFFHPEGERGAARSARENSAKEVCMRCPVRAQCAAHALAVREPYGVWGGLTEDEREELMGRARNRLVSASAGAGGASNT
>NZ_CP023703.1|WP_086770885.1|4829280_4830177_+|LysR-family-transcriptional-regulator
MIEARHLRVLRAVAATGSFSAAGRELGCTQPAVSQQMKALESSVGTPLLVRSGRAMRLTQAGDALVRHAAGILAGLTAAEEEVAAIAGLRAGRVRLVSFPSGSSTLVPTALAALRAAHPGTRVSLEEAEPPESVDKLRDGDCDVALAFRYEDAPGAEEWPDLVVRPLLTDRLVALLPERHRLARADSLAIGELAREPWIAGCPRCRGRLVEVCEAAGFTPRIDFATDDYPAVAGLVGAGLGVAVLPQLAIESVRQRGVRAVTLEPAVRREVVALTLPDLAQVPAVAAMLGQLQRAAAR
>NZ_CP023703.1|WP_150472389.1|4828531_4829200_-|MOSC-domain-containing-protein
MRLLSVNVGRPKAVPYTDQPEGLTGIDKRPVEGPVRVAAPGPKGVAGSGLAGDAVCHLRHHGGDDQAVYAVAREDLDDWERELGRTFADGAFGENLTTTGLDVSGARIGERWRIGPQVVLEVTSGRIPCRTFQGHVGEKGWVRRFTQKAATGAYLRVIVPGEIRAGDAIEIVHLPEHEVTARMEFQATTTHRELLPQLLAAGEALHPEALAAARKYVEKHGG
>NZ_CP023703.1|WP_086770887.1|4827660_4828434_-|SDR-family-oxidoreductase
MTTALITGSTAGIGAAFARRLAADGHDLVLVARDTQRLREQATELHDRHGIEAEVLTADLATDEGIEAVAARLGDRRNPVDLLVNNAGFGNKGRYLDVSMADELKMLKVHCEAVLRLTSAAAEAMRERGRGGVVNVASVAAFVPRGTYGASKAWVVQFTQGAAKDLAGSGVRLMALCPGFVRTEFHERAGMGTDNIPGWMWLDADKLVAAALADLARGKSVSIPDPRYKALMGLVKVTPRALLGGVSSRTGRKYGPQ
>NZ_CP023703.1|WP_150472388.1|4826898_4827585_-|SnoaL-like-domain-containing-protein
MTFVQLIDCRTSRFDEMNRLMDMWVEQTKGKRTATHALVGKDRSDASHFVEIVEFPSYEEAMRNSNLPETDEIFQGMVALCDEMPTFTDLEVVRDEQLNCATAREWFEQAGTIEIDRMFDRVTEDYVEHDPSAEETGLRAAREEFAGWRQAFDFSFRVDDQIAQEDRVCTRWTWTARHKGDYLGIPATGENVTMTGMTWQRFRDGMICEGWWQYDRVGLMEQLGVLGE
>NZ_CP023703.1|WP_150472387.1|4825166_4826792_+|chaperonin-GroEL
MAKILKFDEDARRALERGVNKLADTVKVTIGPKGRNVVIDKKFGAPTITNDGVTIAREVELDDPYENLGAQLVKEVATKTNDIAGDGTTTATVLAQALVREGLKNVAAGASPALLKKGIDAAVKAVSDELLASARPIDEKSDIAAVAGLSAQDSQVGELIAEAMDKVGKDGVITVEESNTFGLELDFTEGMAFDKGYLSPYFVTDQERMEAVLDDPYILINQGKISSIADMLPLLEKVIQTNSSRPLLIIAEDLEGEALSTLVVNKIRGTFNAVAVKAPGFGDRRKAMLQDLAVLTGATVISEEVGLKLDQVGVDVLGSARRVTVTKDDTTVVDGAGKTEDVHGRVAQIKAEIANTDSDWDREKLQERLAKLAGGVCVIKVGAATEVELKEKKHRLEDAISATRAAVEEGIVSGGGSALVHAVKVLEGNLGKTGDEATGVAVVRKAAVEPLRWIAENAGLEGYVITSKVAELDKGQGFNAATGEYGDLVKQGVIDPVKVTRSALENAASIASLLLTTETLVVEKKEEEEPAAGGHSHGHSH
>NZ_CP023703.1|WP_150472391.1|4836414_4837623_-|nucleotide-sugar-dehydrogenase
MPADLAVIGLGPLGLPLAQAAVAAGIPTLGYRTGPEPGSLSPAELRRMLSGGFRPATNPAELGRVRTAVICAPTPRDADGGLDLSQVEAAARTLAGHLRPHTTVILESPVPPGTTEDFLRPLLEEMSGLRAGRDFHLAYSPSRVDPGRRDFTPANTPKVIGGLTPACTESAAAFYGRLTDKVVRARGLREAETVTLLETNFRHVNMALVNEMAVLCNDLGVDLWDVIRCAETKPFGFQAFRPGPGVGGHSVPLDRTGHPGSPLRMVELAQQVNSRMPRYVVQRAATLLNEHGKSARGARVLLLGVTYKADLADRQGTPAQEIAIRLMELGAAVSYHDPHVPSWSVLDRPVPRADSLYEAAADADLTILLQQHRTYDLQGLSVKAQLLLDTRGATPTGAAHRL
>NZ_CP023703.1|WP_150472392.1|4837926_4839633_+|FAD-dependent-oxidoreductase
MRTATLGPAQRAESLAAMAERELDVLVVGGGVVGAGTALDAVTRGLSTGLVEARDWASGTSSRSSKLIHGGLRYLEMLDFVLVREALKERGLLLERLAPHLVKPVPFLYPLQHKGWERLYAGSGVALYDAMSMARAHGRGLPTHRHLSRRHALRVAPALKKDALVGALQYYDAQMDDARYVATLVRTAAAYGAKVANRARVTSFLREGERVVGARVRDAEGGGEYEIRARQVVNATGVWTDDTQAMVGERGQFHVRASKGIHLVVPKDRIHSSTGLILRTEKSVLFVIPWGRHWIVGTTDTDWDLDKAHPAASSADIDYLLEHVNSVLAVPLTRDDVEGVYAGLRPLLAGESDATSKLSREHTVAHPVPGLVVVAGGKYTTYRVMAKDAVDAAVHGLDLRVAECVTEDVPLLGAEGYRALWNARARIAGRTGLHVVRVEHLLNRYGSMAEELLDLIADDPTLGEPLRAADDYLRAEIVYAASHEGARHLDDALTRRTRISIETFDRGTRSAREAAELMAPVLGWDKDQIEREVQHYEKRVEAERESQRQPDDLTADAARLGAPDIVPQ
>NZ_CP023703.1|WP_150474651.1|4839746_4840892_-|serine-hydrolase
MTLLGPTTADAHPAPALLTRTTDASSATHVTDASDATDPAGPTAVPGTAAALLPLLRSRGKAPAAALLAHEEGATRFAESGPDIARSDHFRAGSITKTFLATVVLQLASEQRLSLADPVERYLPGLVRGAGNDGRALTLRSLLTHTSGLYDFARETGGVRPVTPLQAVRIALTHPPADRGRYAYSNTNYVLLGLVVEQVTGRSYATEAERRILDPLALNGTSFPGSRTSLPSPHGRAHGPDGTDVTELDPRVAGAAGELVTTLADLNRFYSALLSGELLPSGRLHEMLDTRTAHGSYGLGLIPARLPCGVTVWGHNGRISGSYVRTAATVDGRHVLTFRVNTTAMADPSLEPALLAAEFCPRTPSNEPVPNGDPAPRHSFE
>NZ_CP023703.1|WP_150474652.1|4841263_4843402_+|protein-kinase
MSEAERAGASRQDKSARLLAGRYRLGDVLGRGGMGTVWRAEDETLGRTVAVKELRFPGNIDDEEKRRLITRTLREAKAIARIRNNSAVTVFDVVEEDDRPWIVMELVEGKSLAEVIREDGVLEPKRAAEVGLAILDVLRSAHREGILHRDVKPSNVLIAEDGRVVLTDFGIAQVEGDPSITSTGMLVGAPSYISPERARGHKPGPAADLWSLGGLLYAAVEGTPPYDKGSAIATLTAVMTEPLDEPKNAGPLRDVIYGLLTKDPVRRLDDAGARAKLNAVLHAPDRRETEAADATKVVPLPMQPDGPGSRAGSSASSSAGSSGGEAAEKLRGALRSVRKAAVAAGAATSAAAGRAKSSNAPGVSGGSGASGASRSLGTQEETRGGAATGAVTSAAAVAATKAEGTAAGRATTTAASASVPVSRSATGAAPGQGGANGGPAPRSSGWPVMTPPDLPPRPVPRAPLTDVVPKRTLVIIAVVVALAVLGTVLALTLGGGEDDPDGAKSGGGSQAVASDSAAADTKDDEDGGARADGSAPESAASGSASGSSSPSSTAAAGGAGSGTSGSGAGAAVTTHESKQGYTIGLPAGWKYQSTSAAGDRFAGPDGQKLLIGWTTTPKDDPVADWENQERSMKRSQYKRVRIEKVDYRGWNTADWEFTYSESGTAYRTIDRGFVVNDHLGHALMHTAKSAAWDGDLRVNTWKTFTETFTPKV
>NZ_CP023703.1|WP_150474653.1|4843617_4846137_+|protein-kinase
MTDRVAGGGIVDEYAGRVLADRYRLPLPPSDEYELTETRAFDTYSGQEVLVRQVPLPEVVEAEVLDAEGLPQGFTARERGARRSVRGTGAEASTRRPADPVVRRAVEAAQAAASIPDHPRLDQVFDVFAEGGSLWVVSELVSARPLAALLAEKPLTPYRAAEVASDVLMALRVLHAHGWVHRNITARTVLVCDDGRVMLTGLAVGAAEEALCGYDPVPVDEEQAQGQAQVQGRAQAQIQAPERQVQQPHLGAVDPEAARRAAIEARAAGGLPAATPEPSGGASGAVARRPVETGGDIRAARAGAIAAYRAGARAAARVHEAQQDGRTALPGARTSADGDTGSGTGIEGAAPSPYVLGSGRAQGPGGVGGTSTGQIADPYGVVGAPAPAALGTGAVPVPAQAGGGPAGTRWDEPSAGASVRRGPATALAAERARQARMAVVGPVTERWAPEQAGPVHENWQLAAPIGPATDLWGLGALLFRAVQGHAPYPEESTAELVQLVCAEPPAFAEECGPLRPVVESLLRQDPTERLDFEELSGWLRSLVRSAPEPEAGTYVVAAPPTDPRRLPIVRRRGELVRRRRAGLPAPHGRHKRGRAEPGRSPRSLGRTLVVVVLLVLAAAVAYAVMFMPKAGEEGTGSAGGAERTGSAGQANPAPDASSEPRPDDGSPDVSPPAASASASGAAETQSGGLPSGFTLRKDAEGFQLAVADGWDRSPKNGRGQVVYTHAGFELIVVPGRDSAAQYGSDPMVYQREKESELQPYRDSSWATASGLRTIQVGGRTSAEGQFTWTGGDGRELFVRNVALLLDGRYHVVQLRGPEAERDEVTRLFEQASASYRYTG
>NZ_CP023703.1|WP_150474654.1|4846308_4848084_+|protein-kinase
MQGLLVAGRYRLVDAIGSGGMGRVWRAHDELLHRAVALKELTAALYVSESDRTVLLARTRAEARAAARINHSAVVTVHDVLEHDGRPWIVMELVEGRSLADAVKQDGRVEPTEAARIGLWVLRALRAAHSAGVLHRDVKPGNVLLADDGRVLLTDFGIAQIDGDTTITRTGEVVGSVDFLAPERIRGHDPGQSSDLWALGATLYTAVEGLSPFRRTSPLSTMQAVVEEEPAVPRYAGPLAPVIAALLRKEPAARPDTDGTERLLAEAAEGRRPDEAQAYIPTQYTGPAGHGTQGGEATGGHPGATTGGAARASGGGTPYPPSGPYAGAASGAHPGAPTVVPAASGTHAQPVAGGPTSLGQTAIGPTGLGPGGPAASQRPPRRRRLRVLALVVVVAALVGGGTAMALQTWGGDGTAQGSGSQSPSPTPTGKGSGPDSWKDIHDPLGFRLSLPPGWERSVFQDDGDLKQIDYSPDGGKHFVRIAIDASPDFDDPYAHQLDLHQQLKRLVDYQKVTLERNTYRDREGARWEYTWTALAKDTDFPGPRHAIEETYISRDGTEYVIYMSSPAKDWARTARQFTSVLQSWREPPSTS
>NZ_CP023703.1|WP_150472393.1|4848174_4849800_+|protein-kinase
MGTEGDDVRVIAGRYRLEARLGRGGMGIVWRATDRLLGRRVAVKELVQDDALSAEQARARRDRTLREARAVAQLSHPHIIVVHDVVEEDERPYIVMELIEGGSLADRIAQRGPIDPREAARIGADLLGALRAAHAAGVLHRDIKPANVLVDSATGRAVLTDFGIAQVAGATTLTETGSFVGSPEYTAPERMSGERTGPASDLWSLGALLCTALSGESPFRRDSLGGILHAVVFADIRTPPQAEPLLPVVRGLLERDPDRRLTAEEAERMLRAFLDTGRTPSGRTGYTPTQADLPHQRPDRPASDPPRRERSTRGVLVAALLVAAMAGAGVSAAALLLDREGNGRDTPSTSAPGVPGAPSGTPGGPGAPGVTDTTSSGTPSDTPSSTPTPSHGRPTAPSGYRVVDDPAGFALAVPEGFTRDPQGERVFYLSPGQVFRLGIKITVPQRGGPLGVMERAAAKGPDTNPGYRDGRVTETTRAGRPAALWQFTWNGFDAAEGARHTYDLCWEDGGRLYDVWVSAPVGKAREAREYFDVAVDTLVPE
>NZ_CP023703.1|WP_150472394.1|4849892_4851692_+|protein-kinase
MSHNGGPGHGADDTTSFVLQPPVLQPSVPQPPASQSPVPQPPVPQPPQPADAQQPARAPQAAHPDNPYAMPAQVAPAPQEPGVGRLIAGRYRLLAKLGHGGMGTVWRAKDETVDREVAVKEPRVPDHLPERERANAFERMRREARAAARLDHPSVVNVHDVAVVDGQPWIVMELIHGRSLGGALEEGTLGVREAARIGLEVLGALEAAHAAGILHRDVKPDNVLLGRHDRVVLTDFGIAQIEGETNLTDTGGFVGSPEFIAPERVLGQRPGPASDLWSLGVVLYAATEGVSPFRRSNTPATLQSVLNAAPAPPAAAQGPLAEAVNGLLEKDPARRPQAAQVRALLERAANPPAPAPTPAPTQVVTAPVVLAPDAQGPIGGWSVRATAGRAGWGLRVGTRLFWTGLGATVVAAAIAAWLVVADPSGGGLPADWRTSAQKDVTATLAVPKDYVLGKPEETDDDHWVSFTDPSGVISVVLAVDRKAEDTGGDIKDSAAAEMYEDNDDFKTNGNYGLDMPKAPKTSPDANAEYQGRPAAENTVAYISTDTQNPLPREMRTLYYKSTAGDMYKLTIAYPGKGDFTKRGQEVAATAIAHLKVDKL
>NZ_CP023703.1|WP_150472395.1|4851718_4853518_+|protein-kinase
MSDDGEREGVNGRTVGGRYRLLERIGSGGMGTVWRARDLLMDREVAVKEPRLPGDPQDEFHRRAAHRLYREVRAAARVDHPSAVSIHDVVVEEGEGLPDGLPWIVMELVRGESLHEVLRRGPLDPAEAARIGLAVLGALRAAHAVGIVHRDVKPANVLLGPHGRVALTDFGIAHIQGEESLTLSGEFVGSLEFIAPERMSGRGAGPTSDLWSLGVLLYAAVEGWSPFRRTTVESTLAAILAADLPEPKQAGPLAPLLVRLLARDPDERPAPAEVAEALEAATLTCWPAPSATDEPTEPQDTARLREFGDDVGTIRIGAEAEPSGEPEEPTGPQPGPQPEPDREPDPDSDPDSDPDPSTEAPSQSTPTPTPTPTPTPTPAPIVEDPAPKATPLLRRPAPLALLAVLVLAGAGLGAPLLMDADSGAATGPTATRGSSPAPSHSTTPTPTPAAWTAHPEPEMGAVLSLPAEYREFARQGGPDEQPRLVVYSAGSVDVRLTQWDRAPGSPLGRAAEAHETWDSYDGDARTQTTRTTFQGHEAVLADTAYSLDTSPTRVMELFVLTDDSRMYELRVDMPKGTAEEKQGTAVFKAARDRLRIDVP
>NZ_CP023703.1|WP_150472396.1|4853646_4855260_+|aldehyde-dehydrogenase-family-protein
MTDSQAPEKTGTNPLAPTPAGARTAADVVTPQLVAQLTKGVVGSGRTANHTPFTGEKLADLPESTPEDVQRAFTAARAAQAVWEQVPVRERAAVLLRFHDLVLQRQGEVLDLIQLETGKARLHAHEEVQAVAVAARHYGRKAPSYLRPKRHAGAMPTLTKVTELRHARGVVGQIAPWNYPLELSVGDALPAFVAGNAVVMKPDTETCLTALWARDLLIEAGLPAEVFQVVIGEGPVVGPEIVRHADYVSFTGSTRTGREVAQGAAARLVGVSLELGGKNAMLVLADADVEKAAAGAVRACFSSAGQLCISIERLYVHESIADAFLERFAARTKAMRLGTSLAYGADMGSLVGERQLETVSRHVEEAVAKGAKVVAGGVARPDVGPYFFEPTILDGVTEPMSVCGEETFGPVVSIYRFTTDDEAVDLANSTPYGLNSSVWTKDGRRGRAVAARLRTGTVNVNEGYAPAYGSVQSPMGGMKDSGLGRRHGSEGILKYTEAQTVAQQRLLPMAPALGMSDEKYAEFMSRSLRLMKAFRFR

Crispr_ID: NZ_CP023703_7

• CRISPR_ID: NZ_CP023703_7
• CRISPR_location: 5133592-5133729
• CRISPR_type: Orphan
• Repeat_type: NA
• Spacer_info: 2 spacers

Consensus repeat of NZ_CP023703_7

Consensus_repeat	Method
CCGAGGAGCCGTCGGAGGAGCCGA	CRISPRCasFinder

spacers of NZ_CP023703_7

>7.1|5133616|33|NZ_CP023703|CRISPRCasFinder
GCACGGCGACCCCGTCGACCAAGCCGCCGAAGA
>7.2|5133673|33|NZ_CP023703|CRISPRCasFinder
CCACCGAGGAGCCCTCGGAGGAGCCGACGACGG

CRISPR arrays and Neighbor proteins around NZ_CP023703_7

CRISPR arrays

The CRISPR arrays of NZ_CP023703_7

>merge|NZ_CP023703|7|5133592-5133729|CRISPRCasFinder
CCGAGGAGCCGTCGGAGGAGCCGAGCACGGCGACCCCGTCGACCAAGCCGCCGAAGACGCAGACGCCGTCGCAGGAACCGACCACCGAGGAGCCCTCGGAGGAGCCGACGACGGGCGAACCGACGACGGGGGAGCCGA

>NZ_CP023703|7|7|5133592-5133729|CRISPRCasFinder
CCGAGGAGCCGTCGGAGGAGCCGA	GCACGGCGACCCCGTCGACCAAGCCGCCGAAGA
CGCAGACGCCGTCGCAGGAACCGA	CCACCGAGGAGCCCTCGGAGGAGCCGACGACGG
GCGAACCGACGACGGGGGAGCCGA

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP023703.1|WP_150472590.1|5136267_5136960_-|DUF402-domain-containing-protein	unknown	unknown	gnl|CDD|377233
NZ_CP023703.1|WP_167534940.1|5138579_5140247_-|fumarate-hydratase	unknown	unknown	gnl|CDD|237955
NZ_CP023703.1|WP_150472593.1|5140427_5141117_+|DUF1707-domain-containing-protein	unknown	unknown	gnl|CDD|377959
NZ_CP023703.1|WP_150472595.1|5143493_5144084_-|malonic-semialdehyde-reductase	unknown	unknown	gnl|CDD|180040
NZ_CP023703.1|WP_150472587.1|5130127_5131063_-|SPFH-domain-containing-protein	unknown	unknown	gnl|CDD|259800
NZ_CP023703.1|WP_150472582.1|5124260_5125163_+|MarR-family-transcriptional-regulator	unknown	unknown	gnl|CDD|237865
NZ_CP023703.1|WP_150472591.1|5137033_5138419_-|aspartate-ammonia-lyase	unknown	unknown	gnl|CDD|234779
NZ_CP023703.1|WP_150472585.1|5129213_5129738_-|PadR-family-transcriptional-regulator	unknown	unknown	gnl|CDD|224609
NZ_CP023703.1|WP_086764670.1|5144234_5144459_-|exodeoxyribonuclease-VII-small-subunit	unknown	unknown	gnl|CDD|179195
NZ_CP023703.1|WP_150472580.1|5121769_5122474_+|transglycosylase-SLT-domain-containing-protein	unknown	unknown	gnl|CDD|366654
NZ_CP023703.1|WP_086764679.1|5141706_5142741_-|class-II-fructose-bisphosphatase	unknown	unknown	gnl|CDD|236536
NZ_CP023703.1|WP_086773312.1|5125291_5125660_+|dynein-regulation-protein-LC7	unknown	unknown	gnl|CDD|214939
NZ_CP023703.1|WP_150472581.1|5122621_5124046_+|AI-2E-family-transporter	unknown	unknown	gnl|CDD|223701
NZ_CP023703.1|WP_150472586.1|5129843_5130182_-|hypothetical-protein	unknown	unknown	gnl|CDD|227214
NZ_CP023703.1|WP_150472583.1|5126191_5128531_-|FtsX-like-permease-family-protein	unknown	unknown	gnl|CDD|225669
NZ_CP023703.1|WP_150472589.1|5133862_5135971_-|SpoIIE-family-protein-phosphatase	unknown	unknown	gnl|CDD|369272
NZ_CP023703.1|WP_086773309.1|5125665_5126094_+|hypothetical-protein	unknown	unknown	unknown
NZ_CP023703.1|WP_150472584.1|5128527_5129217_-|ATP-binding-cassette-domain-containing-protein	unknown	unknown	gnl|CDD|213222
NZ_CP023703.1|WP_086764683.1|5141235_5141610_+|WhiB-family-transcriptional-regulator	unknown	unknown	gnl|CDD|376791
NZ_CP023703.1|WP_150472594.1|5142865_5143393_+|DUF4245-family-protein	unknown	unknown	gnl|CDD|379430

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
NZ_CP023703.1|WP_167534940.1|5138579_5140247_-|fumarate-hydratase	gnl|CDD|237955	PRK15389, PRK15389, fumarate hydratase; Provisional.	0
NZ_CP023703.1|WP_150472593.1|5140427_5141117_+|DUF1707-domain-containing-protein	gnl|CDD|377959	pfam08044, DUF1707, Domain of unknown function (DUF1707). This domain is found in a variety of Actinomycetales proteins. All of the proteins containing this domain are hypothetical and probably membrane bound or associated. Currently, it is unclear to the function of this domain.	1.34289e-19
NZ_CP023703.1|WP_150472595.1|5143493_5144084_-|malonic-semialdehyde-reductase	gnl|CDD|180040	PRK05365, PRK05365, malonic semialdehyde reductase; Provisional.	2.00586e-101
NZ_CP023703.1|WP_150472587.1|5130127_5131063_-|SPFH-domain-containing-protein	gnl|CDD|259800	cd03402, SPFH_like_u2, Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily. This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease, and in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.	8.20718e-130
NZ_CP023703.1|WP_150472582.1|5124260_5125163_+|MarR-family-transcriptional-regulator	gnl|CDD|237865	PRK14951, PRK14951, DNA polymerase III subunits gamma and tau; Provisional.	0.000633141
NZ_CP023703.1|WP_150472591.1|5137033_5138419_-|aspartate-ammonia-lyase	gnl|CDD|234779	PRK00485, fumC, fumarate hydratase; Reviewed.	0
NZ_CP023703.1|WP_150472589.1|5133862_5135971_-|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.	6.28903e-54
NZ_CP023703.1|WP_150472585.1|5129213_5129738_-|PadR-family-transcriptional-regulator	gnl|CDD|224609	COG1695, COG1695, Predicted transcriptional regulators [Transcription].	2.4971e-16
NZ_CP023703.1|WP_086764670.1|5144234_5144459_-|exodeoxyribonuclease-VII-small-subunit	gnl|CDD|179195	PRK00977, PRK00977, exodeoxyribonuclease VII small subunit; Provisional.	1.21333e-18
NZ_CP023703.1|WP_150472580.1|5121769_5122474_+|transglycosylase-SLT-domain-containing-protein	gnl|CDD|366654	pfam01464, SLT, Transglycosylase SLT domain. This family is distantly related to pfam00062. Members are found in phages, type II, type III and type IV secretion systems.	2.78164e-05
NZ_CP023703.1|WP_086764679.1|5141706_5142741_-|class-II-fructose-bisphosphatase	gnl|CDD|236536	PRK09479, glpX, fructose 1,6-bisphosphatase II; Reviewed.	0
NZ_CP023703.1|WP_086773312.1|5125291_5125660_+|dynein-regulation-protein-LC7	gnl|CDD|214939	smart00960, Robl_LC7, Roadblock/LC7 domain. This family includes proteins that are about 100 amino acids long and have been shown to be related. Members of this family of proteins are associated with both flagellar outer arm dynein and Drosophila and rat brain cytoplasmic dynein. It is proposed that roadblock/LC7 family members may modulate specific dynein functions. This family also includes Golgi-associated MP1 adapter protein and MglB from Myxococcus xanthus, a protein involved in gliding motility. However the family also includes members from non-motile bacteria such as Streptomyces coelicolor, suggesting that the protein may play a structural or regulatory role.	7.98681e-10
NZ_CP023703.1|WP_150472581.1|5122621_5124046_+|AI-2E-family-transporter	gnl|CDD|223701	COG0628, yhhT, Predicted permease, member of the PurR regulon [General function prediction only].	1.17502e-57
NZ_CP023703.1|WP_150472586.1|5129843_5130182_-|hypothetical-protein	gnl|CDD|227214	COG4877, COG4877, Uncharacterized protein conserved in bacteria [Function unknown].	2.60296e-15
NZ_CP023703.1|WP_150472583.1|5126191_5128531_-|FtsX-like-permease-family-protein	gnl|CDD|225669	COG3127, COG3127, Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, permease component [Secondary metabolites biosynthesis, transport, and catabolism].	1.88968e-06
NZ_CP023703.1|WP_150472590.1|5136267_5136960_-|DUF402-domain-containing-protein	gnl|CDD|377233	pfam04167, DUF402, Protein of unknown function (DUF402). Family member FomD is a predicted protein from a fosfomycin biosynthesis gene cluster in Streptomyces wedmorensis. Its function is unknown.	8.67457e-17
NZ_CP023703.1|WP_086764683.1|5141235_5141610_+|WhiB-family-transcriptional-regulator	gnl|CDD|376791	pfam02467, Whib, Transcription factor WhiB. WhiB is a putative transcription factor in Actinobacteria, required for differentiation and sporulation.	4.83077e-20
NZ_CP023703.1|WP_150472584.1|5128527_5129217_-|ATP-binding-cassette-domain-containing-protein	gnl|CDD|213222	cd03255, ABC_MJ0796_LolCDE_FtsE, ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and cell division protein. This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. An FtsE null mutants showed filamentous growth and appeared viable on high salt medium only, indicating a role for FtsE in cell division and/or salt transport. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.	1.2955e-96
NZ_CP023703.1|WP_150472594.1|5142865_5143393_+|DUF4245-family-protein	gnl|CDD|379430	pfam14030, DUF4245, Protein of unknown function (DUF4245). This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 188 and 235 amino acids in length.	3.42293e-51

Protein sequences

>NZ_CP023703.1|WP_150472587.1|5130127_5131063_-|SPFH-domain-containing-protein
MSTHDPSATVDTPEMPTPQVREFPARSVGGGLALLSGLVGLLAGAGMIAVATTVTSSGGNAALIVGGILVALTAFLAMCGLNTVAPGEARVVQLFGRYRGTIREDGLRWVNPFTSREKISTRVRNHETAVLKVNDAYGNPIELAAVVVWKVQDTAQASFEVDDFLEFVATQTEAAVRHIAIEYPYDAHEEDGLSLRGNAEEITEKLAVELHARVAAAGVRIIESRFTHLAYAPEIASAMLQRQQAGAVVAARREIVDGAVGMVEAALSRIAEQGIVELDEERKAAMVSNLMVVLCGDRAPQPVLNTGTLYQ
>NZ_CP023703.1|WP_150472586.1|5129843_5130182_-|hypothetical-protein
MRGPGTAAGTEHGDALPVTSPEEGEAPRRRPQQRKQVLLRLDPLVYDALARWASDELRSANAQIEFLLRKALQDAGRLPGGTQPLPRRGRPPGPPGPSGPPGPSGESAPGAP
>NZ_CP023703.1|WP_150472585.1|5129213_5129738_-|PadR-family-transcriptional-regulator
MSIGHTLLGLLESGPRHGYDLKRAFDEKFGHDRPLHYGQVYSTMSRLLKHGLVEVDGIEAGGGPERKRYAITDAGITDVARWLATPEKPEPYLQSTLYTKVVLALLTHRDAADILDTQRSEHLRSMRILTDRKRKGDLADQLICDHALFHLEADLRWLELTAARLDKLREAVTS
>NZ_CP023703.1|WP_150472584.1|5128527_5129217_-|ATP-binding-cassette-domain-containing-protein
MTAPAGSLLAAQDLRKAYGPTLALDGAEFSIHPGEVVAVMGPSGSGKSTLLHCLAGIVPPDSGSITYDGQELATMSDARRSALRRSEFGFVFQFGQLVPELTCVENVALPLRLNGAPRKQAERTALAWMERLEVDDLRGKRPGEVSGGQGQRVAVARSLVTGPRVIFADEPTGALDSLNGERVMDLLTEAARSANAAVVLVTHEARVAAYSDREIVVRDGKSRDMERVV
>NZ_CP023703.1|WP_150472583.1|5126191_5128531_-|FtsX-like-permease-family-protein
MNLRQWGRDLALGFRFAFAGGREGWVRAGLTAVGVGFGVALLLLSTALPNALSARHDREQARQDYRYDLTVPPKADDTLVISHVDTIFRDKDVRGRLVEPEGPRAPLPPGVDRYPGAGEMVVSPALKKLLAADGSALLRERLPYRIVGGIGESGLIGSQELAYFAGASGLAAHMDMWRTVRLTGFGDPTPTREQPDPILVLLNIVVIVALLMPVAVFIAAAVRFGGDRRDRRLAALRLVGSDSRMTRRIAAGEALAGALLGLVLGTAFFLVGRQVAGSVEVMGVSVWPSYLDPSPALATLVAVAVPTAAVLVTLLALRGVVIEPLGVVRAAKPARRRLWWRLLLPVAGLAMLYPMIGQGRDNGDFNKYLVVGGVLLLLVGITALLPWLVETAVGRLGAGGVAWQLAVRRLQLSSGTAARMVNGIAVAVAAAIALQMLFAGVDDQYTEETGQDLRRAQMQVSLPDGTPMAPTVQKFTHTKGVRKVTALSEGYLGDVSWDTENGPNLSAELVVGDCAALREVAKLPSCADGDVFVLEGGEYSADGPAMNRPGRKLYLESYNRLDGGEVTWTVPASVGTARSIVDPAGTRRDGFLMTPGAMPSSIAKTVSGQLYVSVDESVPDVSEHVRNTAAAVDPLSVPDNWTATRTSVRYDSLRTGLLVGALCVLMLIGASLLVSQLEQLRERRKLLSALVAFGTRRRTLTMSVLWQTAIPIGLGLLLASAVGITLGAVLLRMSDTPVVVDWPTVLAMACAGAAVVLAVTLLSLPPLLRLMRPDGLRTE
>NZ_CP023703.1|WP_086773309.1|5125665_5126094_+|hypothetical-protein
MATKRMTPGFSDQVMGLVKALRTDAPDCVASGVVDMSTGMLLSYETVDNHPPEVLDLLAGATLDLFQGRTVVMIEDVFKERRGSSGDNHFFQEILVNSDNLTHLFVRMTEQQDVVAVVVCRKSVNVGMLFAQVRRVVKEYQL
>NZ_CP023703.1|WP_086773312.1|5125291_5125660_+|dynein-regulation-protein-LC7
MRGLREQVTGITDTVVAAADGLLIAADTADSIDPEGLAALAAAGLGLARRTSEATDRGALQRTVTYGSRGCAAFYGVGDTALMVVLGDEGMDVDRLHTATQPTLRRIDLILTDRAAKAPEGV
>NZ_CP023703.1|WP_150472582.1|5124260_5125163_+|MarR-family-transcriptional-regulator
MSGYELLARDLTACGRDGFTGELRASGSPGGTFHLRDGLVVAVESPGAPGPEALLLRSGRIGGEEWAGLVRESDGARWPVAGLVAHGYTGAAQLRVVCVMALQDAAFAVVAGGVDACERAPGEGPPPGAVAVGEPPTPLLAGASRRLAALLALPYPVRPERERPVPTSLSYAAVRLTALQRELLTHADGRRTARDLAFRTGRGVYTVTVEVARMLAEGFLECPRTPAPIPVRLPPGGEGVRRREPAPAPSSPPSPPPAPPSRRPWQPPPLPPPEPARLPRRRPGASGIKEFFRLRDPTGN
>NZ_CP023703.1|WP_150472581.1|5122621_5124046_+|AI-2E-family-transporter
MSRVPGWLGRVGAGLTRMGQRLDERRAETDRESGAVPDPAVPETPVAPAVELPPPAPRPDPAQVVPWGVRVAAEAGWRLLVLAGTVWVLMKVISAVQLVVLAFVVALLLTALLEPTVARLKRLGVPRGPATALTGIFGFVVIGLMGWFVTWQVMENIDNLSDQVQDGIDDLRRWLLNSPFHVTDKQINGIAKNLREAVGANTDEITSAGLEGVTVVVEALTGILLAFFSTLFLLYDGKRIWQWTLKLVPAAARPGVAGAGPRAWATLTAYVRGTVLVALIDAIFIGLGIYFLEVPMAVPLAVFIFLFSFIPLVGAVASGALAVVVALVTQGVFTAVMTLAVVLAVQQIEGHILQPFILGRAVRVHPLAVVLSVACGGMVAGIGGAVVAVPLVAVTNTVVSYLHAYSREPALLTAPKPRGATAVDVAPVKHSARPALEDEAVQADSGGPGAAAPGDGTGRGGGGEEPPNPTHPQG
>NZ_CP023703.1|WP_150472580.1|5121769_5122474_+|transglycosylase-SLT-domain-containing-protein
MLEGNRVSRISVRGFAVASATAVTAVGSVVGVASGSTAQPNDAEATVSDSTTLLADIPVGQQAQVQTASLTQQASVQAIAADEGAKKDAEESARKAAAKTAIAKKEAAEKAAADAKERAEVKAAASRSSSDFPIQNSYTIDQIQAMAQQMVPSGQWQCFSNIVDHESSWNYRAVNPSSGAYGLFQALPAGKYVSAGADWQTNPATQIKWGLNYMNDRYGSPCDAWSFWQSNHWY
>NZ_CP023703.1|WP_150472589.1|5133862_5135971_-|SpoIIE-family-protein-phosphatase
MTEQPTSYERPQGVDPTDARGALLRTQGPAPGATALPSAAAQARTDGTPGTTTPGGPAPRPQGKDPAVSDAEHSQPAAAAEPDAHRPRPAPEAIPPQPGAETRAERPQDTRDRRTGQAPAAGRQPTPMRRDGDRLRFVGAATRRIARGLDLDEIVMGLCRATVPTFSDAILVYLRDPLPVGDERPAADRVVLRLRRTDRIPEEREPEPGFAQLGMPPPETPELLELSAAIAELCEVRPGGALAEVLRGVRPVFADTPAATAALPELLGAESRLDIPGGQRAILAPLRGRRRVIGAAVFIRRPERIPFEADDLLVAAQLATHSALGIDKAVLYDREAYIADELQRTMLPETLPRPTGVRLASRYLPAAETARVGGDWYDAIPLPGSRVALVVGDVMGHSMTSAAIMGQLRTTAQTLAGLDLPPQEVLHHLDEQAQRLGTDRMATCLYAVYDPVSHRITIANAGHPPPILLHLGGRAEVLRVPPGAPIGVGGVDFEAVELDAPAGATLLLYTDGLVESRLRDVATGIEQLREKLAATAQLTGPDHPPPLEALCDEVLDMLGPGDRDDDIALLAARFDGIAPSDVAYWFLEPEDAAPGRARRLARRALERWGMEDMTDSVELLVSEVVTNAVRYATRPVSLRLLRTDVLRCEVGDDVPQLPRLRQARATDEGGRGLYLVNRLARRWGATRLSTGKVVWFELNRGS
>NZ_CP023703.1|WP_150472590.1|5136267_5136960_-|DUF402-domain-containing-protein
MADGGAVRRVGTGGAAGLWRPGDQILWRYRENGGAGIHIARPVTVVRDDEELLAVWLAPGTQCVRPVLADGTPPHQEPLRTRYTKPRTVVPGRWFGTGVLKLARPGEPWSVWLFWEPGWQFKNWYVNFEEPLSRWDGGVDSEDHFLDLCVYPDRSWGWRDEDEFAQAQQDGLMDVSVAERVREAGRSAVEVVRAWGAPFADGWENWRPDPSWAVPLLPEDWDRTPAHLST
>NZ_CP023703.1|WP_150472591.1|5137033_5138419_-|aspartate-ammonia-lyase
MTEYRIEHDSMGEVRVPADAKWRAQTQRAVENFPVSGQRIERAHIEALARIKGAAAKVNAELGVLDKEIAGAIQEAAAEVAGGKWDEQFPVDVFQTGSGTSSNMNTNEVVATLATERLGRDVHPNDHVNASQSSNDVFPSSIHIAATTAVTHDLIPALEHLAASLERKAAEFSDVVKSGRTHLMDATPVTLGQEFGGYAAQVRYGVERLTASLPRLAELPLGGTAVGTGINTPPGFSAAVIEEVARVTGLPLTEARDHFEAQGARDGIVETSGQLRTIAVGLTKIANDLRWMASGPRTGLAEISLPDLQPGSSIMPGKVNPVIPEAVLMVAAQVVGNDATVATAGAAGNFELNVMLPVIAKNVLESIRLLANVSRLLADRTVDGIVADRERAREYAESSPSVVTPLNKYIGYEEAAKVAKKALAERRTIRETVLDGGYVERGDLTLQQLDEALDVLRMTHP
>NZ_CP023703.1|WP_167534940.1|5138579_5140247_-|fumarate-hydratase
MPEFAYTDLLPMGEDTTPYRLVTSEGVSTFEADGRTFLKVEPEALRKLAEEAIHDIQHYLRPAHLAQLRRIIDDPEASGNDKFVALDLLKNANIAAAGVLPMCQDTGTAIVMGKRGQNVLTDGGDESALSRGIYDAYLNLNLRYSQMAPLTMWEEKNTGSNLPAQIELYAADGGAYKFLFMAKGGGSANKSFLYQETKAVLNEASMMKFLEEKIRSLGTAACPPYHLAIVVGGTSAEYALKTAKYASAHYLDEIPAEGSPLGHGFRDKELEEKVFELTQRIGIGAQFGGKYFCHDVRVVRLPRHGASCPVAIAVSCSADRQAVAKITAEGVFLEQLETDPARFLPETTEEHLESDGDVVRIDLNQPMDDILAELTKYPVKTRLSLSGPLVVARDIAHAKIKERLDAGEEMPQYLKDHPVYYAGPAKTPEGYASGSFGPTTAGRMDSYVEQFQAAGGSKVMLAKGNRSAQVTKACDAHGGFYLGSIGGPAARLAQDCIKKVEVVEYEELGMEAVWKIEVEDFPAFIVVDDKGNDFFQDPAPAPTFTSIPVRGPGLA
>NZ_CP023703.1|WP_150472593.1|5140427_5141117_+|DUF1707-domain-containing-protein
MDLQKQTEPPAAVSELRASDADRDRIADILREALAEGRLTAEEHSERVEGVLAAKTVGELDVFVRDLPAAHPRQASPRMPAPNRPTPGAIPADPDDNLVAIFSASVRKGRWRAGRRIHAYAVFGSVEIDLSEALFEYQQVVIKAFSVFGNVEISVPENVSLRGTGGGVLGNFEVDTLDSPDPDAPVIYVDGWSVLGNIEARPKRGKLVADILDRVHRKVDRSMRKHLDR
>NZ_CP023703.1|WP_086764683.1|5141235_5141610_+|WhiB-family-transcriptional-regulator
MLQSPHSSQVAAVPAQRVPARDRDQDAPWHTEAVCRRDEAGLFFAPSKEPTAARLSREEAAKRVCGGCPVMVECREHALLQPEPYGVWGGLTAAERRVVLARRRRRDVELKKATRPADHIAAAG
>NZ_CP023703.1|WP_086764679.1|5141706_5142741_-|class-II-fructose-bisphosphatase
MTENHQLPSELDVPSEAPDRNLALELVRVTEAAAMAAGRWVGRGDKNGADGAAVRAMRTLVSTVSMNGVVVIGEGEKDEAPMLFNGERVGDGTGPEVDIAVDPIDGTTLTAKGMPNAIAVLAATERGAMFDPSAVFYMDKLVTGPEAADFVDIDAPVSVNIRRVAKAKRATPEDVTVVILDRPRHAGIIDEIRQTGARIKLITDGDVAGSILALREGTGVDLLLGVGGTPEGIISACAVKCLGGTIQGKLWPKDDEERQRAIDAGHDLDRVLTTEDLVTGENVFFVATGITDGELLRGVRYRSETAVTDSIVMRSKSGTVRRIDSEHRLSKLRAYSAIDFDRAK
>NZ_CP023703.1|WP_150472594.1|5142865_5143393_+|DUF4245-family-protein
MAGSKGKTQTVRDMVLSLGLIMVAGLVMYFFIPHDDSAAPDVKRVDYRVELLTARRAASYPVAAPEGLSSDWKATSVRFDGAQFDAWHLGFHSPDGEYVAVEQSTEKRARFIDDASQGARETKATEVIGGQTWTRYTGGRYDALVLEGTDGATTVVAGTASFAQLAEMAGALKLA
>NZ_CP023703.1|WP_150472595.1|5143493_5144084_-|malonic-semialdehyde-reductase
MSLALDPAAQDLLFRDAHTANTFTDEPVTEEQVQAIYDLVKFGPTAFNQTPLRVTLVRSPEARERLVQHMAEGNQAKTASAPLVAILAADNEFHEELPTLLPSFPQAKDVFFAERPVRESSATLNAALQAAYFIVGVRAAGLAAGPMTGFDAEGIRKEFLDDDHTPLIVVNIGKPGEGASYPRSPRLAYDQVVTTV
>NZ_CP023703.1|WP_086764670.1|5144234_5144459_-|exodeoxyribonuclease-VII-small-subunit
MTSKTDEALGYEQARDELIEVVRRLEAGGTTLEESLALWERGEELAKVCRRWLEGARARLDAALAEEEGPAEGE

Crispr_ID: NZ_CP023703_8

• CRISPR_ID: NZ_CP023703_8
• CRISPR_location: 6753228-6753332
• CRISPR_type: Orphan
• Repeat_type: NA
• Spacer_info: 1 spacers

Consensus repeat of NZ_CP023703_8

Consensus_repeat	Method
GTCACGCCGGTTCGAATCCGGTCG	CRISPRCasFinder

spacers of NZ_CP023703_8

>8.1|6753252|57|NZ_CP023703|CRISPRCasFinder
TCCGGAGGTGTGCGCGGTCCCGTAGAGCAGAGGCAGCCTCGCCGCCTTCTCAGGGCG

CRISPR arrays and Neighbor proteins around NZ_CP023703_8

CRISPR arrays

The CRISPR arrays of NZ_CP023703_8

>merge|NZ_CP023703|8|6753228-6753332|CRISPRCasFinder
GTCACGCCGGTTCGAATCCGGTCGTCCGGAGGTGTGCGCGGTCCCGTAGAGCAGAGGCAGCCTCGCCGCCTTCTCAGGGCGGGTACGCCGGTTCGAATCCGGTCG

>NZ_CP023703|8|8|6753228-6753332|CRISPRCasFinder
GTCACGCCGGTTCGAATCCGGTCG	TCCGGAGGTGTGCGCGGTCCCGTAGAGCAGAGGCAGCCTCGCCGCCTTCTCAGGGCG
GGTACGCCGGTTCGAATCCGGTCG

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP023703.1|WP_150473655.1|6753376_6754723_+|SDR-family-oxidoreductase	unknown	unknown	gnl|CDD|187586
NZ_CP023703.1|WP_150473661.1|6763810_6764896_+|oxidoreductase	unknown	unknown	gnl|CDD|226855
NZ_CP023703.1|WP_150473648.1|6740051_6741122_-|DUF3048-domain-containing-protein	unknown	unknown	gnl|CDD|378618
NZ_CP023703.1|WP_086771173.1|6763118_6763532_-|SsgA-family-sporulation/cell-division-regulator	unknown	unknown	gnl|CDD|377399
NZ_CP023703.1|WP_150473660.1|6761214_6762837_-|ATP-binding-cassette-domain-containing-protein	unknown	unknown	gnl|CDD|223562
NZ_CP023703.1|WP_150473657.1|6756562_6757969_-|hypothetical-protein	unknown	unknown	gnl|CDD|226382
NZ_CP023703.1|WP_150473652.1|6749764_6750718_+|multicopper-oxidase-domain-containing-protein	unknown	unknown	gnl|CDD|259991
NZ_CP023703.1|WP_086771170.1|6752828_6753110_+|WhiB-family-transcriptional-regulator	unknown	unknown	gnl|CDD|376791
NZ_CP023703.1|WP_150473654.1|6751850_6752642_-|VOC-family-protein	unknown	unknown	gnl|CDD|319911
NZ_CP023703.1|WP_086771175.1|6764944_6765271_+|plasmid-stabilization-protein	unknown	unknown	unknown
NZ_CP023703.1|WP_086771163.1|6741351_6742542_+|glutathione-dependent-formaldehyde-dehydrogenase	unknown	unknown	gnl|CDD|176243
NZ_CP023703.1|WP_150474784.1|6744800_6746981_-|DUF1080-domain-containing-protein	unknown	unknown	gnl|CDD|368908
NZ_CP023703.1|WP_150473651.1|6747025_6749575_-|ThuA-domain-containing-protein	unknown	unknown	gnl|CDD|377643
NZ_CP023703.1|WP_150473650.1|6743748_6744780_+|DNA-polymerase-domain-containing-protein	unknown	unknown	gnl|CDD|240135
NZ_CP023703.1|WP_150473659.1|6760286_6761063_-|N(G),N(G)-dimethylarginine-dimethylaminohydrolase	unknown	unknown	gnl|CDD|224747
NZ_CP023703.1|WP_150473649.1|6742587_6743673_-|ATP-dependent-DNA-ligase	unknown	unknown	gnl|CDD|236191
NZ_CP023703.1|WP_086771171.1|6759080_6760058_-|acyl-ACP-desaturase	unknown	unknown	gnl|CDD|153109
NZ_CP023703.1|WP_150473658.1|6758156_6758996_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP023703.1|WP_150473653.1|6750788_6751838_+|substrate-binding-domain-containing-protein	unknown	unknown	gnl|CDD|224525
NZ_CP023703.1|WP_150473656.1|6754738_6756562_-|AAA-family-ATPase	unknown	unknown	gnl|CDD|223786

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
NZ_CP023703.1|WP_150473655.1|6753376_6754723_+|SDR-family-oxidoreductase	gnl|CDD|187586	cd05325, carb_red_sniffer_like_SDR_c, carbonyl reductase sniffer-like, classical (c) SDRs. Sniffer is an NADPH-dependent carbonyl reductase of the classical SDR family. Studies in Drosophila melanogaster implicate Sniffer in the prevention of neurodegeneration due to aging and oxidative-stress. This subgroup also includes Rhodococcus sp. AD45 IsoH, which is an NAD-dependent 1-hydroxy-2-glutathionyl-2-methyl-3-butene dehydrogenase involved in isoprene metabolism, Aspergillus nidulans StcE encoded by a gene which is part of a proposed sterigmatocystin biosynthesis gene cluster, Bacillus circulans SANK 72073 BtrF encoded by a gene found in the butirosin biosynthesis gene cluster, and Aspergillus parasiticus nor-1 involved in the biosynthesis of aflatoxins. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.	7.07583e-10
NZ_CP023703.1|WP_150473661.1|6763810_6764896_+|oxidoreductase	gnl|CDD|226855	COG4447, COG4447, Uncharacterized protein related to plant photosystem II stability/assembly factor [General function prediction only].	2.37035e-18
NZ_CP023703.1|WP_150473648.1|6740051_6741122_-|DUF3048-domain-containing-protein	gnl|CDD|378618	pfam11258, DUF3048, Protein of unknown function (DUF3048) N-terminal domain. Some members in this bacterial family of proteins are annotated as YerB. However currently no function is known. This entry represents the N-terminal domain.	2.53955e-35
NZ_CP023703.1|WP_086771173.1|6763118_6763532_-|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.	8.2532e-34
NZ_CP023703.1|WP_150473660.1|6761214_6762837_-|ATP-binding-cassette-domain-containing-protein	gnl|CDD|223562	COG0488, Uup, ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only].	1.43323e-122
NZ_CP023703.1|WP_150473657.1|6756562_6757969_-|hypothetical-protein	gnl|CDD|226382	COG3864, COG3864, Uncharacterized protein conserved in bacteria [Function unknown].	1.66291e-10
NZ_CP023703.1|WP_150473652.1|6749764_6750718_+|multicopper-oxidase-domain-containing-protein	gnl|CDD|259991	cd14449, CuRO_1_2DMCO_NIR_like_2, The cupredoxin domain 1 of a two-domain laccase related to nitrite reductase. The two-domain laccase (small laccase) in this family differs significantly from all laccases. It resembles the two domain nitrite reductase in both sequence and structure. It consists of two cupredoxin domains and forms trimers, and hence resembles the quaternary structure of nitrite reductases more than that of large laccases. There are three trinuclear copper clusters in the enzyme localized between domains 1 and 2 of each pair of neighbor chains. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety of organic substrates coupled to the reduction of molecular oxygen to water. It displays broad substrate specificity, catalyzing the oxidation of a wide variety of aromatic, notably phenolic, and inorganic substances. Laccase has been implicated in a wide spectrum of biological activities. This subfamily has lost the type 1 (T1) copper binding site in domain 1 that is present in other two-domain laccases.	5.81593e-69
NZ_CP023703.1|WP_086771170.1|6752828_6753110_+|WhiB-family-transcriptional-regulator	gnl|CDD|376791	pfam02467, Whib, Transcription factor WhiB. WhiB is a putative transcription factor in Actinobacteria, required for differentiation and sporulation.	9.46793e-24
NZ_CP023703.1|WP_150473654.1|6751850_6752642_-|VOC-family-protein	gnl|CDD|319911	cd07247, SgaA_N_like, N-terminal domain of Streptomyces griseus SgaA and similar domains. SgaA suppresses the growth disturbances caused by high osmolarity and a high concentration of A-factor, a microbial hormone, during the early growth phase in Streptomyces griseus. A-factor (2-isocapryloyl-3R-hydroxymethyl-gamma-butyrolactone) controls morphological differentiation and secondary metabolism in Streptomyces griseus. It is a chemical signaling molecule that at a very low concentration acts as a switch for yellow pigment production, aerial mycelium formation, streptomycin production, and streptomycin resistance. The structure and amino acid sequence of SgaA are closely related to a group of antibiotics resistance proteins, including bleomycin resistance protein, mitomycin resistance protein, and fosfomycin resistance proteins. SgaA might also function as a streptomycin resistance protein.	8.14254e-33
NZ_CP023703.1|WP_086771163.1|6741351_6742542_+|glutathione-dependent-formaldehyde-dehydrogenase	gnl|CDD|176243	cd08283, FDH_like_1, Glutathione-dependent formaldehyde dehydrogenase related proteins, child 1. Members identified as glutathione-dependent formaldehyde dehydrogenase(FDH), a member of the zinc-dependent/medium chain alcohol dehydrogenase family. FDH converts formaldehyde and NAD(P) to formate and NAD(P)H. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. MDH family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. Like many zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), these FDHs form dimers, with 4 zinc ions per dimer. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.	0
NZ_CP023703.1|WP_150474784.1|6744800_6746981_-|DUF1080-domain-containing-protein	gnl|CDD|368908	pfam06439, DUF1080, Domain of Unknown Function (DUF1080). This family has structural similarity to an endo-1,3-1,4-beta glucanase belonging to glycoside hydrolase family 16. However, the structure surrounding the active site differs from that of the endo-1,3-1,4-beta glucanase.	1.49522e-32
NZ_CP023703.1|WP_150473651.1|6747025_6749575_-|ThuA-domain-containing-protein	gnl|CDD|377643	pfam06283, ThuA, Trehalose utilisation. This family consists of several bacterial ThuA like proteins. ThuA appears to be involved in utilisation of trehalose. The thuA and thuB genes form part of the trehalose/sucrose transport operon thuEFGKAB, which is located on the pSymB megaplasmid. The thuA and thuB genes are induced in vitro by trehalose but not by sucrose and the extent of its induction depends on the concentration of trehalose available in the medium.	2.83121e-76
NZ_CP023703.1|WP_150473650.1|6743748_6744780_+|DNA-polymerase-domain-containing-protein	gnl|CDD|240135	cd04865, LigD_Pol_like_2, LigD_Pol_like_2: Polymerase (Pol) domain of bacterial LigD proteins similar to Pseudomonas aeruginosa (Pae) LigD, subgroup 2. The LigD Pol domain belongs to the archaeal/eukaryal primase (AEP) superfamily. In prokaryotes, LigD along with Ku is required for non-homologous end joining (NHEJ)-mediated repair of DNA double-strand breaks (DSB). NHEJ-mediated DNA DSB repair is error-prone. It has been suggested that LigD Pol contributes to NHEJ-mediated DNA DSB repair in vivo, by filling in short 5'-overhangs with ribonucleotides; the filled in termini would then be sealed by the associated LigD ligase domain, resulting in short stretches of RNA incorporated into the genomic DNA. The Pol domains of PaeLigD and Mycobacterium tuberculosis (Mt)LigD are stimulated by manganese, are error-prone, and prefer adding rNTPs to dNTPs in vitro; however PaeLigD and MtLigD belong to other subgroups, proteins in this subgroup await functional characterization.	1.17851e-123
NZ_CP023703.1|WP_150473659.1|6760286_6761063_-|N(G),N(G)-dimethylarginine-dimethylaminohydrolase	gnl|CDD|224747	COG1834, COG1834, N-Dimethylarginine dimethylaminohydrolase [Amino acid transport and metabolism].	5.11975e-41
NZ_CP023703.1|WP_150473649.1|6742587_6743673_-|ATP-dependent-DNA-ligase	gnl|CDD|236191	PRK08224, ligC, ATP-dependent DNA ligase; Reviewed.	0
NZ_CP023703.1|WP_086771171.1|6759080_6760058_-|acyl-ACP-desaturase	gnl|CDD|153109	cd01050, Acyl_ACP_Desat, Acyl ACP desaturase, ferritin-like diiron-binding domain. Acyl-Acyl Carrier Protein Desaturase (Acyl_ACP_Desat) is a mu-oxo-bridged diiron-carboxylate enzyme, which belongs to a broad superfamily of ferritin-like proteins and catalyzes the NADPH and O2-dependent formation of a cis-double bond in acyl-ACPs. Acyl-ACP desaturases are found in higher plants and a few bacterial species (Mycobacterium tuberculosis, M. leprae, M. avium and Streptomyces avermitilis, S. coelicolor). In plants, Acyl-ACP desaturase is a plastid-localized, covalently ACP linked, soluble desaturase that introduces the first double bound into saturated fatty acids, resulting in the corresponding monounsaturated fatty acid. Members of this class of soluble desaturases are specific for a particular substrate chain length and introduce the double bond between specific carbon atoms. For example, delta 9 stearoyl-ACP is specific for stearic acid and introduces a double bond between carbon 9 and 10 to yield oleic acid in the ACP-bound form. The enzymatic reaction requires molecular oxygen, NAD(P)H, NAD(P)H ferredoxin oxido-reductase and ferredoxin. The enzyme is active in the homodimeric form; the monomer consists mainly of alpha-helices with the catalytic diiron center buried within a four-helix bundle. Integral membrane fatty acid desaturases that introduce double bonds into fatty acid chains, acyl-CoA desaturases of animals, yeasts, and fungi, and acyl-lipid desaturases of cyanobacteria and higher plants, are distinct from soluble acyl-ACP desaturases, lack diiron centers, and are not included in this CD.	5.06393e-134
NZ_CP023703.1|WP_150473653.1|6750788_6751838_+|substrate-binding-domain-containing-protein	gnl|CDD|224525	COG1609, PurR, Transcriptional regulators [Transcription].	3.35792e-101
NZ_CP023703.1|WP_150473656.1|6754738_6756562_-|AAA-family-ATPase	gnl|CDD|223786	COG0714, COG0714, MoxR-like ATPases [General function prediction only].	5.61448e-05

Protein sequences

>NZ_CP023703.1|WP_086771170.1|6752828_6753110_+|WhiB-family-transcriptional-regulator
MRERFSPHVTILAMPTDTIPTPDLAWQREALCAQTGADFFFPEPGSSVREAKRICGMCEMRTACLDYALAHDERFGVWGGLSEKERLHLRRTN
>NZ_CP023703.1|WP_150473654.1|6751850_6752642_-|VOC-family-protein
MLTTRFVNGAPNWLDIGTTDIDRAAAFYGALFGWRFVSAGPDAGGYGFFQLDGRTAAGGMGSAPEQGPASWTVYFRTADADATCEAAEQAHGRVLFPPMDVMGQGTMAIIVDPAGVPFGVWQPGRLAGLDVAGEPGSLCWVELYTPDIAAAAAFYRSTLGLETSGVAFPGGTYTCVNPAGAGEESMFGGVVPLADDPTEAPHPPYWLPYVEVADVDAVVARAEELGGTVRLGGTDIEGVGRVARLADPDGSRFAVIRSEPRKA
>NZ_CP023703.1|WP_150473653.1|6750788_6751838_+|substrate-binding-domain-containing-protein
MSDTVPRPTLEAVAARAGVSRATVSRVVNGGDGVREPLVERVRQAVEELGYVPNQAARSLVTKRHDAVAVVIAEPETRVFADPFFALQLRGISKELTAHDNQLVLLLTEGRDDHTRVARYLAGGHVDGALVFSLHVDDPLPELIQGAGVPTVFGGRPGWGDGTRDVVYVDSDNRGGARAAVRHLVGLGRTRVAHITGPLDQTSAADRLQGYRDVMGDADPRLVVESDFTPGGGERAMRELLDRCPEVDAVFAANDLTASGVLRVLRERGRRVPEDVAVVGFDDMVPVAEQSDPPLTTVRQDIEEMGRIMTRLLLRSLDRRNTGGAAPDPVRPAPSGEVLPTTLVRRASA
>NZ_CP023703.1|WP_150473652.1|6749764_6750718_+|multicopper-oxidase-domain-containing-protein
MDRRDFNRRVLLGGAAATSLSLVGSETAGARPNTAAAPVGGQVRHLRLYAEKLPDGRFGYGFEKGRATVPGPLIEVNEGDTVHIEFENTLDVAASLHVHGLDYEISSDGTAQNHSDVEPGGTRTYTWRTHAPGRRADGTWRAGSAGYWHYHDHVVGTEHGTGGIRKGLYGPVIVRRAGDVLPDATHTIVFNDMTINNRPAHSGPDFEATVGDRVEFVMITHGEYYHTFHLHGHRWADNRTGTLTGPDDPSQVIDNKIVGPADSFGFQVIAGEGVGAGAWMYHCHVQSHSDMGMVGLFLVRKPDGTIPGYEPHHPHEH
>NZ_CP023703.1|WP_150473651.1|6747025_6749575_-|ThuA-domain-containing-protein
MHLRGLSTRRAKSTERAGSARVAGTARRGVRRRRRARVAAVAAVVVTAGLLSGPAVQARPAPEPPLTTISVTSPPGGPGVNVLVFHGSAAAGEESPVVDAGIEAIEDIGLTGATDQRFAVEATDDASVFTDGPRLSRFHAIVFLTGGGDVLDPEQEAGLEAYMEAGGGFVGLHDAARAEPYSDWFTGLIGARPAANGPTAVQRATVEVGDRRHPAGKDLPVEWKRPDRWPNWTRNPTGTVHTVARVRESTYQPGTSANGADHPISWCRDYDGGRSFYTGMGGTVSAYDETDFRAHLRGALLWTTRLAQADCKATITAHYKAERLTQPNRPGLNDQIGEPHGLVTAPDGRVLYIGRGGADSSQPVITDWSNPDIGKGKGEIHVYDPVTKKVTLAGALTVFGNKGGGDELVKVEEGLLGIELDPRFAQNGWVYLHYTPHSGVDRDKRMAERRVSRFTLDPATNRLDLGSEKVLLKWPVQVHSCCHAGGGMAWDSRGNLYIATGDNNSSGFSDGYSGNNPQPNYKGVSFADARRTAGNTNNLNGKILRIHPEPDGTYTLPEGNLFTGRESAEGGGKTRGEIYVMGVRNPARISVDRQTDVLYAGWVGPDASVPSTTWGPAKYDTFAVITEASNRGWPYCMGNKQPYRDRNLPDPAKPLGWYDCDRPRNESPNNDGLVNLPPVTGNNIWYSPQGGAPDYPRDASGVPSYKQGEARYLLPWLKGGGQAAMNGPLYRYDAASASTAKWPAYWDGKWFVGDFYDADQPRNAVLMNPVTQGAGSLPVHSESLKRIVPVGNDGIRNLMDWRFGPDGALYVLDYGRGFFTSDARSALWRVTYTGGGPTPAVGQLARGTR
>NZ_CP023703.1|WP_150474784.1|6744800_6746981_-|DUF1080-domain-containing-protein
MVLGLQAGPGAARPGQQPVRAVPPATAAQVLTWTAGDDITRYTTAPTTAVAGPATIVFENSAATGNTTGMPHTLTFVTSDPEFNGDVELNILANPNDDMGGRHTAEVTLSPGRYLYHCTIPGHGQMHGILVVSEGSEEDTTAPETSARVSGVQNAQGEYVGSASVAVAATDETGGSGVDRIQYAVDATGDWIPYTAPVVVDRAGGHSIRYRAFDKAGNVSAEKSVAFTVVPPASDDTTPPDTSATVSGELNADGTYVDMATVTVTASDTGSGVDRIQYAVGEATDDWISYTGPVMVHQVGTHTVRYRAVDKAGNASAAKSVTFTVVAAPPRDTTPPVTGVTVEGTRNAAGAYVGHARVTVGASDEGGSGVAAVEYSLDGGPYLAYAAPVVVDRAGTHTVAYRATDRAGNTSAARDVSFTVAAGGGVPAPACPEWDERLTVFVGTVGTGVPNRVTDNRCRINELIEDEREWTSHALFLKHVRTVLDALFRNGVVDEREYDAVLGAAGTSGIGEPGQTEGYRTIMDGSAASLARWEQVGGGSFAPNGDGSITSGTTRAGLGMLWYPQRKYADFSLRLQWRDDAPGTGNANSGLFVRFPWVHGDAEEPRPEWAAIKYGHEVQVLDRPDGDLYKTGSVYGFDRVGLAGAGVTQKGTWNDYEIRVVGQHYSVLRNGVLINEFDNTGGQEFSPPRADDPGTDGRRFASGYVGLQVHGTSDVVSYRDIRIMEL
>NZ_CP023703.1|WP_150473650.1|6743748_6744780_+|DNA-polymerase-domain-containing-protein
MGDAVELEVAGRTVRLSSPDKIFFPERGFTKLDLARYYQAVAPGILRALRDRPTTLERYPDGVTGESFFQKRAPKNMPDWIPRAHITFPSGRSADEMCPTEQAAVLWAAQYGTLTFHPWPVRRSDVDRPDELRIDLDPQPGTDYDDAVHAAHELRAVLEEFGGLRGWPKTSGGRGLHVFVPITPSWTFTQVRRAAIAAGRELERRMPDRVTTKWWKEERGERIFVDYNQTARDRTIASAYSVRPRPHAPVSAPLRWEEVGVAHPVDFDIATMPARYAELGDVHADMDEHAFSLEALLELARRDEHDHGLGDLPYPPEYPKMPGEPRRVQPSRARKDGPAPTTP
>NZ_CP023703.1|WP_150473649.1|6742587_6743673_-|ATP-dependent-DNA-ligase
MDLPVMPPVKPMLAKSVAAIPPGMQYEAKWDGFRAIVFRDGAEVELGSRTGKPLTRYFPELVEALRERVPERCVLDGEIVIAREGRLDFDALTERIHPADSRVRMLAERTPSSFVAFDLLALDDESVLDVPQSDRRALLERALDGVTPPVHLAPSTTDIEVARRWFEEFEGAGLDGVIAKPLTLAYRPDERAMFKIKHERTADVVVAGYRFHKSGPVVGSLLLGLYDDRGALQHVGVSAAFAMKRRAELVEELEPLRMDDVAGHPWAAWAEEAAHESARLPGAPSRWSGKKDLSWVPLRPERVAEVAYDHMENGARFRHTARFRRWRPDRTPESCTYAQLEEPVRYDLAEILGAPPRTAPS
>NZ_CP023703.1|WP_086771163.1|6741351_6742542_+|glutathione-dependent-formaldehyde-dehydrogenase
MKAVTWQGKRDVRVESVPDPTIQEPTDAVIRVTSTGLCGSDLHLYEVLTPFMTPGDILGHEPMGIVEEVGAGVVDLSVGDRVVVPFQIACGDCWMCLNSLPTQCETTQVTAEGMGAALFGYTRLYGAVPGGQAEYLRVPQAQYGPIKVPEGPPDDRFVYLSDVLPTAWQAVAYAGIPEGGSVAVLGLGPIGDMACRVAQVRGAGRVFGVDLVGDRLRRAHARGVETYDLRNFDSEKELVDAIRDETDGRGPDAVIDAVGTEAHGSAAARMIQNASALLPRKVSGPLAERFSVDRLAALHTAIELVRRGGTLSLVGVYGGTADPLPMLTMFDKQLQIRMGQANVRRWSDDILPYLTDEDPLGVDDFATHRIPLSEAPKAYEMFQQKRDGAVKILMTP
>NZ_CP023703.1|WP_150473648.1|6740051_6741122_-|DUF3048-domain-containing-protein
MVEMATVDGATRRRPGRRFWASRGRGPARRGVHPGRGTATASALAAALALTLAAGCTNGPAPADDGRGTDRPASRTDTGTGTAAAVGQVLAVKIDNVRAARPQTGLDAADIVYVEQVEGGLSRLMAVYATRLPKTVGPVRSARESDLELLRQFDRPALAFSGAQGKLLPLIDKEPLEAVTPQDTEDAYYRGTEKASPHNLYLRPHRVLPSAPGEAALTTGFRHGPPPDGGTPTRSRTVRYPSARFTFTWSQERRGWEITTDGAPTVTADGRRLAPPTVVVQYVDVRRSGYHDVLGNHTPYTETVGSGTAEVLRDGRSHDVRWLRPTATDGTRFTTRAGTPVAFAEGQVWVVFAQRP
>NZ_CP023703.1|WP_150473655.1|6753376_6754723_+|SDR-family-oxidoreductase
MDEANGAVSDAEMAVFHEVVGKLKALPVDDPVRLRAEQVAASFARDGRLRRRKARDAEVSAADAAAMAATATGALDRREDAPLDGAGRTGVFHRPRPCYVCKSPYRQVDAFYHRLCPACAADNTARRALSTDLSGRRVLLTGGRVKIGFQLALMMLRDGAELLVTSRFPHDTVRRFHAEPGSAKWRDRLTVLAVDLRDPRQVLGLCEELRTEGEPLDILVNNAAQTVRRPPESYALLAAAEHDALPEGVRRAPGFTPMRMLEGLGGSVCALPASLREADEAGLLPDPSPENSWSARLGALDPAEVLETQLVNALAPALLCDRLLPLLLASPRPCRYVVNVTAVEGRFAVRNKQAGHPHTNMAKAALNMLTRTSAAELAERGVHMCAVDTGWITDENPAPKKARMAGAGFRTPLDIVDGAARVYDPIVRGEAGDPVSGVFLKDYRVAQW
>NZ_CP023703.1|WP_150473656.1|6754738_6756562_-|AAA-family-ATPase
MTPETRQMSIPTTPRQHTGVSRLEGFIDAMIDLGQTGQIFGEHGIGKTATFFSYLARTRPDTTLVYVPAANLTPDDLLVNAPVRDPRSGELVLRQLVMSGLRPGRPFVLLIDDSLQAGDTIQSQLMQVACNWTLGEHDLRALGCVGVFLTDNESLTETSARRGDLALLDRMVTMRITANDTPWRRHLAAKYRPWDLRPVFSLWASLSPALRELLSPRTLDHVLANAREGFPLRWGLPLLDGERLRLAEPGPDGRPGQNRTAEILDRIAQTLGVPNPATVPDPVRQVVRAALRNRWTVLLQGPPGCGKTELVRETVREGLGRDALYFSLPVTNVEDLCAPVPSPDGTLDNLLAVNFTGPEAKAIVWDEYNRPKDKAAFAKLMEITQEWSLAGRRIENLRAQIAVQNPPYHLGRKLLVSRNNIAQATRFTASLEVTPQDIPANEWLLARYGADAETVLEWWKHDIDEEGRAWITKRTLERLIKLHRRGLPLEMATVYLGDGEYAPVPLTALVDRLRGRPVTGLRELARDADVWEARLRHAAEHSAEGGDDSDVVHQILANAELSQLKKHRAVVSRLVAHLPAKLRATYLVGASQQHQTFWTGVFTGMRR
>NZ_CP023703.1|WP_150473657.1|6756562_6757969_-|hypothetical-protein
MGYGEQGRWRAPLVDLADRRALEAYRPADPAVVAQARRLKEAALLDFGLTESAVASWLYAKCHHQIPTTAVDTAAVVASGDGTCLLLYNPDFFVGLGLAGVKFVLFHEARHLVHRHLLADPDLRDDPVFTLAAEVAVNHVALIRLGREDLPLLDGRPTGVDPRKVYDAYTEDLTAHGLEPVTYETFIATDMRVFAELKRMRHPPVPDERLCVHLVAGAVPADQETIDAVTSSALLNSLLAARRGHTGAEQELLDLMGRTEEGSARAARLWGMLGAGVLRGETTRTRTVHWWQRWLVDVLGSKLRDGERLVYPKKRGALLAALGQEPMLARRGPVRDKVLVIAYDTSGSMPGDVVRWLTELVGRIDGVEAHWLSFDAVVMPFVPGERVYGGGGTSFHAVADYVEGRTEVGGRVLDVSPDAVVVLTDGYAPPVTPAEPDKWIWLITEGGTEWPETHTPAMACHRVTTGSR
>NZ_CP023703.1|WP_150473658.1|6758156_6758996_-|hypothetical-protein
MHYSHTVQQALGFLLGLTDEDTALRIRERIALPAPEPDGPEAVQRRLNRVWSWRNVPSSVVLWILEQDDPELNAVVWRHLATDAGLRRAIARGIPFGPDRTQPVRVHRVPGEEPEVPGSYVRHGLVGALREAGTMAAARSAASMVLSRDDWRTVTEADAERPLPGFTRWALSVRPDCPPALRAQFGSHAKFTHRVRTAGVLDGPAGYATEHGPAVGVLEILAMGHLMFPARIGAAEDALRPLVRDHLGDREEAWAVLAQLASTFHGTVPELVATAGAIA
>NZ_CP023703.1|WP_086771171.1|6759080_6760058_-|acyl-ACP-desaturase
MTTTSPHLGSPSAVWTDARLLYALEEVVETELNRHLKVTKDWMPHEYVPWSDARNFPGFFEDGEAWEKGQSKVTEIGRIALVVNLLTEDNLPSYHHEIASLFGRDGAWGTWVHRWTAEEGRHGIVMRDYLLASRAVDPDQLEQFRMVHMSEGFESDNRHSMLHSVAYVAFQELATRVSHRNTGHQSGDPVCDRMLARIATDENLHMVFYRNLLKAAFELAPDLTMQAVRDVVVNFRMPGHGMPGFERAAAQMAIGEIYNMRIHHDDVIQPVLRYLKVLDIEGLDPEGLKAQEELGLYMGGLDAEASKFDEKLAARKARMAARAAG
>NZ_CP023703.1|WP_150473659.1|6760286_6761063_-|N(G),N(G)-dimethylarginine-dimethylaminohydrolase
MPSKKALIRRPSPRLAEGLVTHVERAAVDVDLALEQWEAYGEALRANGWETVEIDPADDCPDSVFVEDTVVMYRNVALIARSGAESRRAETAGVEEAVARLGCSVNWIWEPGTLDGGDVLKDGDTVYVGRGGRTNAAGVQQVREAFEPLGARVVTVPVSRVLHLKSAVTALPDGTVIGHIPKVDRPALFPRFLSVPEEAGGHVVLLGGPRLLISASAPKTTDLLADLGYEPVVVDISEFEKLEGCVTCLSVRLRGLYA
>NZ_CP023703.1|WP_150473660.1|6761214_6762837_-|ATP-binding-cassette-domain-containing-protein
MSSSITCTSLSFAWPDGTPVLDGLDVAFGPGLTGLVGVNGSGKSTLLKLIAGELTPSDGTVRTAGEIGYLPQNVTLDTSLRVDEALGIAARRAALHAIEAGDVREKHFETLGDDWDVEERALATLGELGLAAIGLDRTIGEVSGGESVLLRLAALLLRRPDILLLDEPTNNLDLYARRRLYAAVAAWPGVMVVVSHDRELLELVDQIADLRAGEVAWYGGNYSAYEEALTTEQEAAERMVRVAESDLRKQKRELSDAQMKLARRKRYGQKMWDQKREPKIVMGARKRAAQESAGKHRILHEERLAEARERLDEAALAVRDDAEIRVDLPYTAVPPGRDVLSLLDLRLAYGARVEGGFDLRGPERVALVGRNGAGKTTLLRTIAGELAPVAGEVHAHVPLRFLPQRLDVLDDGLTVAENVARFAPDATDNRIRARLARFLFRGGRADQKAATLSGGERFRATLAALMLAEPAPQLLLLDEPTNNLDMASVRQLTSALESYEGALIVASHDLPFLESIGITRWLLLDGELRPTSAQELADPV
>NZ_CP023703.1|WP_086771173.1|6763118_6763532_-|SsgA-family-sporulation/cell-division-regulator
MSIVIEQPVEARLVAAAPRMQSIPATLHYDRRDPFAVRMTFPAPATLEGVDVCWTFARDLLTAGLHDAEGDGDVRVRPYGYDRTVLEFHAPEGTAIVHVHSAEIRRFLQATGELVPAGLEHLQLDLDHDLAELMRDA
>NZ_CP023703.1|WP_150473661.1|6763810_6764896_+|oxidoreductase
MRRAGRTVAAGAACAAALAVLTAVPAQAGETGRPGGHEPAWAPKDTGTPTVRFRGLAAVDRDTAWVAGTQGTVLRTTDGGANWRNVSPPGAAGLQFRDVEAFDARRAVVLAIGEGEASRVYRTDDGGATWTESFRNTDTRAFYDCMTFFDRRHGLAMSDPVDGRFRILSTSDGGRSWTVLPDAGMPAALPGEAGFAASGQCLVSAGSRDVWLATGGAERARVLHSADRGLTWTVTDAPIPAGDPARGVFGLAFRDRTHGLAVGGDYRADQPSPSAAAATGDAGRTWRPAGTPPPAYRSGVAWLPHSRTAALAVGPTGTDLTTDAGRTWRTVDTGSYDTVDCTPDRGCWAAGEQGRVARLER
>NZ_CP023703.1|WP_086771175.1|6764944_6765271_+|plasmid-stabilization-protein
MPRGSSPKRERQYEHIKESAQERGESAGRAKEIASRTVNKERARSGESKTASRTSTQDMSSGERGGRRSGKGSQGPTYDQLYEEAKRRDIHGRSDMNKSQLQRALGKD

Crispr_ID: NZ_CP023703_9

• CRISPR_ID: NZ_CP023703_9
• CRISPR_location: 7067100-7067273
• CRISPR_type: Orphan
• Repeat_type: NA
• Spacer_info: 4 spacers

Consensus repeat of NZ_CP023703_9

Consensus_repeat	Method
NNNNGGCAACAACNNCGG	CRT

spacers of NZ_CP023703_9

>9.1|7067118|21|NZ_CP023703|CRT
GGGCGGAAACAACAACGGCGG
>9.2|7067157|18|NZ_CP023703|CRT
TGGCGGTAACGGCAACAA
>9.3|7067193|27|NZ_CP023703|CRT
TAGCAACAACGGCAACAACGGTGGGAA
>9.4|7067238|18|NZ_CP023703|CRT
CAACAACGGCGGCAACAA

CRISPR arrays and Neighbor proteins around NZ_CP023703_9

CRISPR arrays

The CRISPR arrays of NZ_CP023703_9

>merge|NZ_CP023703|9|7067100-7067273|CRT
TCCGGGCAACAACAACTGGGGCGGAAACAACAACGGCGGTAACGGCAACAACAACGGTGGCGGTAACGGCAACAACAATGGCAACAACGGCGGTAGCAACAACGGCAACAACGGTGGGAACAACGGCAACAACGGCGGCAACAACGGCGGCAACAACGGCGGCAACAACGGCGG

>NZ_CP023703|9|1|7067100-7067273|CRT
TCCGGGCAACAACAACTG	GGGCGGAAACAACAACGGCGG
TAACGGCAACAACAACGG	TGGCGGTAACGGCAACAA
CAATGGCAACAACGGCGG	TAGCAACAACGGCAACAACGGTGGGAA
CAACGGCAACAACGGCGG	CAACAACGGCGGCAACAA
CGGCGGCAACAACGGCGG

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP023703.1|WP_150473828.1|7078865_7079615_+|succinate-dehydrogenase/fumarate-reductase-iron-sulfur-subunit	unknown	unknown	gnl|CDD|181038
NZ_CP023703.1|WP_150473820.1|7064827_7065670_+|polysaccharide-deacetylase-family-protein	unknown	unknown	gnl|CDD|213022
NZ_CP023703.1|WP_150473826.1|7075208_7076093_-|LysR-family-transcriptional-regulator	unknown	unknown	gnl|CDD|183051
NZ_CP023703.1|WP_150473816.1|7057805_7059893_+|SpoIIE-family-protein-phosphatase	unknown	unknown	gnl|CDD|369272
NZ_CP023703.1|WP_150473825.1|7074504_7074891_+|DUF4440-domain-containing-protein	unknown	unknown	gnl|CDD|227327
NZ_CP023703.1|WP_150473815.1|7056262_7057684_-|lipase-maturation-factor-family-protein	unknown	unknown	gnl|CDD|369070
NZ_CP023703.1|WP_150473818.1|7063052_7064183_+|CapA-family-protein	unknown	unknown	gnl|CDD|214858
NZ_CP023703.1|WP_086772019.1|7061622_7062135_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP023703.1|WP_150473823.1|7068564_7069329_-|DUF4239-domain-containing-protein	unknown	unknown	gnl|CDD|372881
NZ_CP023703.1|WP_150474810.1|7076212_7076884_+|succinate-dehydrogenase	unknown	unknown	gnl|CDD|131101
NZ_CP023703.1|WP_150473821.1|7065933_7066605_-|class-F-sortase	unknown	unknown	gnl|CDD|320678
NZ_CP023703.1|WP_086772020.1|7062284_7062830_-|sigma-70-family-RNA-polymerase-sigma-factor	unknown	unknown	gnl|CDD|236605
NZ_CP023703.1|WP_086770801.1|7070272_7071244_+|hypothetical-protein	unknown	unknown	gnl|CDD|226765
NZ_CP023703.1|WP_150473827.1|7076886_7078869_+|fumarate-reductase/succinate-dehydrogenase-flavoprotein-subunit	unknown	unknown	gnl|CDD|236054
NZ_CP023703.1|WP_086772018.1|7060809_7061472_-|zf-HC2-domain-containing-protein	unknown	unknown	gnl|CDD|379219
NZ_CP023703.1|WP_150473824.1|7071509_7072322_+|hypothetical-protein	unknown	unknown	gnl|CDD|252734
NZ_CP023703.1|WP_150473822.1|7067812_7068343_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP023703.1|WP_150473817.1|7059924_7060788_+|Fpg/Nei-family-DNA-glycosylase	unknown	unknown	gnl|CDD|223344
NZ_CP023703.1|WP_086770803.1|7072318_7074454_+|EAL-domain-containing-protein	unknown	unknown	gnl|CDD|236645
NZ_CP023703.1|WP_150473819.1|7064218_7064680_-|universal-stress-protein	unknown	unknown	gnl|CDD|366180

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
NZ_CP023703.1|WP_150473828.1|7078865_7079615_+|succinate-dehydrogenase/fumarate-reductase-iron-sulfur-subunit	gnl|CDD|181038	PRK07570, PRK07570, succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated.	0
NZ_CP023703.1|WP_150473820.1|7064827_7065670_+|polysaccharide-deacetylase-family-protein	gnl|CDD|213022	cd10917, CE4_NodB_like_6s_7s, Catalytic NodB homology domain of rhizobial NodB-like proteins. This family belongs to the large and functionally diverse carbohydrate esterase 4 (CE4) superfamily, whose members show strong sequence similarity with some variability due to their distinct carbohydrate substrates. It includes many rhizobial NodB chitooligosaccharide N-deacetylase (EC 3.5.1.-)-like proteins, mainly from bacteria and eukaryotes, such as chitin deacetylases (EC 3.5.1.41), bacterial peptidoglycan N-acetylglucosamine deacetylases (EC 3.5.1.-), and acetylxylan esterases (EC 3.1.1.72), which catalyze the N- or O-deacetylation of substrates such as acetylated chitin, peptidoglycan, and acetylated xylan. All members of this family contain a catalytic NodB homology domain with the same overall topology and a deformed (beta/alpha)8 barrel fold with 6- or 7 strands. Their catalytic activity is dependent on the presence of a divalent cation, preferably cobalt or zinc, and they employ a conserved His-His-Asp zinc-binding triad closely associated with the conserved catalytic base (aspartic acid) and acid (histidine) to carry out acid/base catalysis. Several family members show diversity both in metal ion specificities and in the residues that coordinate the metal.	7.18942e-73
NZ_CP023703.1|WP_150473826.1|7075208_7076093_-|LysR-family-transcriptional-regulator	gnl|CDD|183051	PRK11242, PRK11242, DNA-binding transcriptional regulator CynR; Provisional.	1.92547e-52
NZ_CP023703.1|WP_150473816.1|7057805_7059893_+|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.	5.59385e-47
NZ_CP023703.1|WP_150473825.1|7074504_7074891_+|DUF4440-domain-containing-protein	gnl|CDD|227327	COG4994, COG4994, Uncharacterized protein conserved in bacteria [Function unknown].	6.98806e-09
NZ_CP023703.1|WP_150473815.1|7056262_7057684_-|lipase-maturation-factor-family-protein	gnl|CDD|369070	pfam06762, LMF1, Lipase maturation factor. This family of transmembrane proteins includes the lipase maturation factor, LMF1. Lipoprotein lipase and hepatic lipase require LMF1 to fold into their active states. The precise role of LMF1 in lipase folding has yet to be determined.	9.63694e-143
NZ_CP023703.1|WP_150473818.1|7063052_7064183_+|CapA-family-protein	gnl|CDD|214858	smart00854, PGA_cap, Bacterial capsule synthesis protein PGA_cap. This protein is a putative poly-gamma-glutamate capsule biosynthesis protein found in bacteria. Poly-gamma-glutamate is a natural polymer that may be involved in virulence and may help bacteria survive in high salt concentrations. It is a surface-associated protein.	2.44719e-73
NZ_CP023703.1|WP_150473823.1|7068564_7069329_-|DUF4239-domain-containing-protein	gnl|CDD|372881	pfam14023, DUF4239, Protein of unknown function (DUF4239). This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 254 and 270 amino acids in length.	8.888e-13
NZ_CP023703.1|WP_150473821.1|7065933_7066605_-|class-F-sortase	gnl|CDD|320678	cd05829, Sortase_F, Sortase domain found in the class F family of sortases. Class F sortases are mainly present in Actinobacteria, Chlorobacteria and Firmicutes. Their functions are largely unknown.	3.28953e-52
NZ_CP023703.1|WP_086772020.1|7062284_7062830_-|sigma-70-family-RNA-polymerase-sigma-factor	gnl|CDD|236605	PRK09645, PRK09645, ECF RNA polymerase sigma factor SigL.	1.44666e-74
NZ_CP023703.1|WP_086770801.1|7070272_7071244_+|hypothetical-protein	gnl|CDD|226765	COG4315, COG4315, Uncharacterized protein conserved in bacteria [Function unknown].	1.03164e-19
NZ_CP023703.1|WP_150473827.1|7076886_7078869_+|fumarate-reductase/succinate-dehydrogenase-flavoprotein-subunit	gnl|CDD|236054	PRK07573, sdhA, fumarate reductase/succinate dehydrogenase flavoprotein subunit.	0
NZ_CP023703.1|WP_086772018.1|7060809_7061472_-|zf-HC2-domain-containing-protein	gnl|CDD|379219	pfam13490, zf-HC2, Putative zinc-finger. This is a putative zinc-finger found in some anti-sigma factor proteins.	7.01102e-06
NZ_CP023703.1|WP_150474810.1|7076212_7076884_+|succinate-dehydrogenase	gnl|CDD|131101	TIGR02046, Succinate_dehydrogenase_cytochrome_b558_subunit, succinate dehydrogenase (or fumarate reductase) cytochrome b subunit, b558 family. This family consists of the succinate dehydrogenase subunit C of Bacillus subtilis, designated cytochrome b-558, and related sequences that include a fumarate reductase subunit C. This subfamily is only weakly similar to the main group of succinate dehydrogenase cytochrome b subunits described by pfam01127, so that some members score above the gathering threshold and some do not. [Energy metabolism, TCA cycle].	6.11017e-77
NZ_CP023703.1|WP_150473824.1|7071509_7072322_+|hypothetical-protein	gnl|CDD|252734	pfam04672, Methyltransf_19, S-adenosyl methyltransferase. This family contains a SAM (S-adenosyl methyltransferase) domain, with a central beta sheet with 3 alpha-helices on both sides. Crystal packing analysis of the structure Structure 3giw suggests that a monomer is the solution state oligomeric form. An unidentified ligand (UNL, cyan) was found at the putative active site surrounded by the residues His57, His170, Phe171, Tyr216 and Met22. The UNL is likely to be a phenylalanine or phenylalanine-like molecule. (details derived from TOPSAN).	1.03921e-118
NZ_CP023703.1|WP_150473817.1|7059924_7060788_+|Fpg/Nei-family-DNA-glycosylase	gnl|CDD|223344	COG0266, Nei, Formamidopyrimidine-DNA glycosylase [DNA replication, recombination, and repair].	7.28935e-66
NZ_CP023703.1|WP_086770803.1|7072318_7074454_+|EAL-domain-containing-protein	gnl|CDD|236645	PRK10060, PRK10060, cyclic di-GMP phosphodiesterase.	4.48021e-113
NZ_CP023703.1|WP_150473819.1|7064218_7064680_-|universal-stress-protein	gnl|CDD|366180	pfam00582, Usp, Universal stress protein family. The universal stress protein UspA is a small cytoplasmic bacterial protein whose expression is enhanced when the cell is exposed to stress agents. UspA enhances the rate of cell survival during prolonged exposure to such conditions, and may provide a general "stress endurance" activity. The crystal structure of Haemophilus influenzae UspA reveals an alpha/beta fold similar to that of the Methanococcus jannaschii MJ0577 protein, which binds ATP, though UspA lacks ATP-binding activity.	1.22653e-21

Protein sequences

>NZ_CP023703.1|WP_150473821.1|7065933_7066605_-|class-F-sortase
MSGYELSGMAEEEERPKKRAPWGVIALVLLTGLALIRNGSGEFDAGPPQPASAAAADARTARGTLGGAVQALPFSEPDRVRIPAIRVDAPVMQVGLDTDGWVGAPPPEDPNLAGWFTGAVSPGEKGTAVVVGHVDNTQGPAVFYGLGALKKGNHVEVARRDGKTAVFEIYGVEVFEKNNFPGDRVYASKGSPELRVITCGGGFSKANGYDGNVVAFARLIEVR
>NZ_CP023703.1|WP_150473820.1|7064827_7065670_+|polysaccharide-deacetylase-family-protein
MQKDQLFTRRGALLAGAAAVGAAGTASLFAWGTGGGTPVRPDAPAAGAPAHRLPANSSAYRLQPLTGYGPPRAADARTPLRSEPLLRIDGRGRTMVLTFDDGPDPRYTPGILDTLAEYDVRAMFFVCGEMAADQPGLLARMADEGHTVGNHTWSHPLLTKLTRRQIRSEMTRTSEVIENAYGERPRWFRAPYGAWNRAAFQLGSELGMEPLAWTVDTLDWTSPGTGTIVDRVGNGAAPGVVVLSHDAGGDRSQSVRALRRYLPRLLDSGYHITVPRRQLA
>NZ_CP023703.1|WP_150473819.1|7064218_7064680_-|universal-stress-protein
MTEQHPSPFERGTDGPKVIVVGVDGSDTSMRAAAYAAGLARRQRALLAVVYVQPVMTAGAALGAPVAEATDEIAQEIVAQIREATERSRGIFDMRWEFHTFHGDPYNGLVKAADQLKADAVVVGASEQAGHRIVGSVAVRLVKAGRWPVTVVP
>NZ_CP023703.1|WP_150473818.1|7063052_7064183_+|CapA-family-protein
MIARRHQVALALTVLLTAAAACQAHDRESASGRPAPSADRGFSLVATGDILPHGSVIERARFDAGGTGHDFGPMFAGIQPVVAGADLALCHLETVYSPADPAAASMPQLAGALAATGYDSCSTASDHSLDTGPDGVHRTLDALDSAGVRHTGTARSAAEAAAVPLLRAGGAKVAHLAYTYDTNGVPLPEGQPWAVSLIDENKIVADARNARLAGADVVVVSLHWGTQWQDAPDDRQLTLARTLTASRTGTRPDIDLILGGHAHVPQAYEKVNGTWVVYGLGDQVAGETPNHAGVVDPRANRSSVARFGFAPPARPGARWEVTKAAFVPELFDLDAGRVVDLDKALARGADVRGVRDRVRDLVLSRGGAQDGLVTGE
>NZ_CP023703.1|WP_086772020.1|7062284_7062830_-|sigma-70-family-RNA-polymerase-sigma-factor
MTAGTLTARTTTAEHELAALQREHGRPLFALLLRLCDGDRQRAEDLVQETLVRAWQHPEALRTDAFDSVRPWLLTVGRRLAIDARRARQARPAEVGDAVLENAPVCGDHADRAAAALDVREAVKTLTPQHREVLVLVYFQGASVAEAAAALGIPPGTVKSRAYYALRALRRVLPGYAPDLG
>NZ_CP023703.1|WP_086772019.1|7061622_7062135_-|hypothetical-protein
MLHRGHQSTDGTGGGELTVPMAWLYAEYIADELLRTGDLMPPTSFEFRAGRDALALTVFLSDTEGELPGIRVVTQLETWLSLTAYDQPWQDWVAGRMAQLAAEAAESEGPDPDLELASAAWRWLEETELLAPDLNAVPGGAPPGEDEGPKIWTPAWQLGLPLGHLAIHLF
>NZ_CP023703.1|WP_086772018.1|7060809_7061472_-|zf-HC2-domain-containing-protein
MRSLERHRDVGAYALGVLDEAEAFRFEDHLMECPRCAAEVTEFGATTRQLMLYRRATPRAVHPFAGPGPQLLDRLLGEVATRRRAAKRRLLYAVAAAVVVAVAGPALAMMAGGGGSGAEPVRVVAATDQKSGVWAQVTAGDEVWGSQVELEVKDAAGPRACHLIVIGHDGSEEIVTSWMVPDHDARPNTMKGGATMQSDQIARYEVRTMNGETLVVLKAG
>NZ_CP023703.1|WP_150473817.1|7059924_7060788_+|Fpg/Nei-family-DNA-glycosylase
MPELPEVEALKDFLTEHLVGHEIVRVLPVAISVLKTYDPPLAAVEGRAVTAVRRHGKFLDLETDDGLHLVTHLARAGWLHWKDRLPDGPPKPGKGPLALRVALETGEGFDLTEAGTQKRLAVYLVRDPQEVPGVARLGPDPLAADFDEERFAALLSGERRQLKGALRDQSLIAGVGNAYSDEILHAARMSPFKLAASLTPAETRTLYEALRATLTEAVERSRGVAAGRLKAEKKSGLRVHGRTGESCPVCGDTVREVSFSDSSLQYCPTCQTGGKPLADRRMSRLLK
>NZ_CP023703.1|WP_150473816.1|7057805_7059893_+|SpoIIE-family-protein-phosphatase
MVDRGASALSLPDDWPAHPDPILALNRMGGFDWDLDTGVFAMDARAHEIFDLTPEEYDGNPESLSPRVPQAESLRLDTLVTRAIKDGSENYGAYFRIRRRDGGLRWAHTQGYIRRDDTGRPRRIIGIVRDASDELRDLAAHREETALDDARREQTNVVQLTTAALAHARTVKDVIDVLKDTHGLIHLGATSLVMGLVEAGRIRLIAEGPEGSFVPGTLVTRIDEPYPMSEVVRTLTPRFIESPDEFAAGYPVLWPHLTDLKITSAAYLPLIVQARPIGAMGLLYSDRHGFTPEERNILVALGSSIAQSLQRAMFYEQEKDIAQGLQQAMLPRTIPSVPGADVAVRYRAATIGGSHGRDIGGDWYDLIPLPGGRVGAVIGDVQGHDTHAAAVMGQLRIVLRAYASEGHTPATVMARASVFLHELDTDRFATCLYTEADLATGVVQMVRAGHIDPMVRAVDGTCRRISVPGGLPLGLSAEFGRLDYPVATLELDPGHTLLLCTDGLVEQPGADLDDGMRALAELIATGPDDVRALADRLIEVAEERGGDDDVALLLLRRRAPDAPQAGSRLQQHVAPGDPEALTQARHMIRAAVRTWGAQERSDDVELVADELVTNALMHTEGAAIVTLRLLTGGGRRLRVEVEDSSSALPRRREAGDSGVSGRGLLLVELLSDVWGVEARGGGKCVWCEFGVPERS
>NZ_CP023703.1|WP_150473815.1|7056262_7057684_-|lipase-maturation-factor-family-protein
MEWFTAPDYWLSRTVFQRALACVYLVAFVTAALQFRALLGERGMLPAARFVERMPFRRAPSVFHWRCSDRFFAGCAWAGCAVSAALIAGLDSLLPLWVAMLAWLVPWALYVSIVNVGQTWYGFGWESLLLETGFLAVFLGNDEVAPPIVVLFLLRWLLFRVEFGAGLIKMRGDPCWRKLTCLDHHHETQPMPGPLSWFFHRLPRPLHRVEVAANHVTQLIVPFLLFTPQPIATAAASLMILTQLWLVLSGNFSWLNWITIVLAVPALELPTDPPAAPDAPLWYMVVVLAVAAFLLFLSHRPVLNMLSRRQVMNRSFDPLHLVNTYGAFGSVSRVRHEVVIEGTLDEVPRADSDWREYEFKGKPGDTRRWPRQFAPYHLRLDWMMWFAALSPSYAGPWFGALVERLLENDRDTLRLLRRSPFPPGEPPRHIRARLFRYRYTTWRELRETGACWERTYVREYLPPTRLAGSAQRP
>NZ_CP023703.1|WP_150473822.1|7067812_7068343_-|hypothetical-protein
MHAIRVASAAVLGACALAVSTPPAVAAESDVTPFGFSVLPSTITAGGQVALQIDRSSGGCKGAVTITSGIFDSVHIAAHRSSATTTVDYDVEVGAVYQVTFTCDGASGSTGLTVAGLRPASPTPAPYPVPRGVQAGAGGTVAGFDIKEIGLGAALIAGSVGAAYHFSRRRSGEDGT
>NZ_CP023703.1|WP_150473823.1|7068564_7069329_-|DUF4239-domain-containing-protein
MPEWLVLTLAMLAACAVVVAVTFVRHRTASEDEDPSETPDVIEYMTMWIGVVYAIVLGLAIAGVWEARSIAQDHVQAEAQSLHEISERVRVYPADVRDRVRGDVDAYVSHVVTAEWKAMADNGEVTERGDELIERLRADLTDYQPASDFEAQAYQPLLDQLAAADQARNNRAGSTGETMPGVVWFGLLAGAAITIGMVFALQIRRTTRELILAGLFSALIAFLLFLIWDFDAPYSRGITASSEPFLRLFPNAKD
>NZ_CP023703.1|WP_086770801.1|7070272_7071244_+|hypothetical-protein
MKTSWRSASLVASAVSVLALTTACGQEGGTAASSQNVGVTAPAGTVAGVGSGYGGVGAGTSPSASAPGAVGAGGAAQAGTAGQLAVSANDELGKVVIDAAGMTLYRFDADTAQPPKSNCDGDCATTWPPVPADDATAGDGIDKSLLGEVTRTDGTKQLTVDGWPVYRYAKDTNAGDTNGQGVGGKWFALAPDGKKAKSASAAPGLSVRKDPNLGDIVVDKNGMTVYRFVKDEAWPKPVTACLGACVEKWPAVAPVATNDTEGVQKKGLMSFTRPDGVKQMTVNCSPIYTFSGDKAPGDINGQGVGGTWYAVAPDGKLVGAPKQ
>NZ_CP023703.1|WP_150473824.1|7071509_7072322_+|hypothetical-protein
MERPAWAPRSIDISVPSVSRIYDYYLGGSHNFEVDREAARKAMEFMPGLPKIMQANRAFMRRAVRYAADAGITQFLDIGSGIPTFGNVHEVAREARPGARVVYVDHDPVAVAHSQVVLEGEADADVVAADLLKPRDILASGPVEQLIDLERPVALLLVAILHFVEDRDDPYSAVAELTAALAPGSLLVLTHASYEGIPLPPARAEGAVDVYKDIRNPLVMRSRDEIARFFEGYDMVEPGLVPMPHWRPETAPEDEDPYAFSGFAGVGRAS
>NZ_CP023703.1|WP_086770803.1|7072318_7074454_+|EAL-domain-containing-protein
MTAEPDGPEDRLRRFATIWSRAVFPVTSTSLTRPELEEQLLPLARRLSEALRARSFEAETPKAVGAALVGAHCTDPDALARSLDCVDAYLVLYCGEDGPQEDLRTRCSRLQHAMAAGFAQKLRERTLAEQEAIAQAALRAQGVVAQALHASEARFRAVFEGAAIGIGIADLQGNILEVNGALVRMFGGGEQAVRGRNVSEWTHADDAPQVWRLYDELVRGEREHYHVEKAFYRPDGTVLWTNLTVSLLRDPDGQPQYQLALMEDTTERRLLNLRLRYEATHDALTGLPNRTLFFERLEKVLAAGEGQRFGLCYLDLDGFKTINDSLGHAAGDRLLVEVADRLQSCATAPGEMVARLGGDEFVALTTGPDTHREVDDLAARIMNALVAPVRIEGRELTVRGSIGIVEGPAGEHSPAEVLRSADITMYRAKSAGGNRFELADPEADARAITRHGLTTALPAALERGEFFIEYQPLVHLGDGSVRGAEALVRWLHPQHGVLGPDRFIPLAEHTGLIVPLGRWVLEQSVRQVGHWRERCGEPGPLRINVNLSPCQLTHPGLVQDTVDILERAGVSPEALCLEVTESALIGADDDLLKPLRRLAEMGVDIALDDFGTGYSNLANLRRLPVSVLKLDRSFTQSMQQFPADPVDLKIVEGIVSLAHSLDLAVTVEGVETGAQAEQLRILGCDTAQGWYYARPGPPDRLHELALVDATG
>NZ_CP023703.1|WP_150473825.1|7074504_7074891_+|DUF4440-domain-containing-protein
MTQETDAVAAAIAGELSLMDPAVRASRTETVRLLDPEFTEVGASGRRYTYAETVAELPDHPGSSPTGPRYEPSAIRGVLLAPGLVHLTYTTTFAGHRAHRTSLWRRQPPETTWRMYYHQATPLPPDTP
>NZ_CP023703.1|WP_150473826.1|7075208_7076093_-|LysR-family-transcriptional-regulator
MQFQQLQYFVAVAETRHFTRAAELVHVAQPSLSQQIKALERELGADLFQRARGNITLTDAGEALLPLARRILADTETARYEVQELAQLRSGRVRLGATPSLCTGLLPDVLRAFHDRYPGIRLLIEEGGSHDLVRELARGALDLALVVLPLPTPSPALTTVDLLREDLVVVSSPESPKPGHGRRTVRIADLEGERLVMFRHGYDLRELTVAACRSAGFEPDFAVEGGEMDAVLGFVRAGLGMAVVPRMVAARSGRGLRVTPLARPGLHRVIALAHRSDVAPPRAARELQRMLLER
>NZ_CP023703.1|WP_150474810.1|7076212_7076884_+|succinate-dehydrogenase
MARTVWDSSVGKKTVMAVSGLIMLMYLVAHMIGNLKIFFGPGEFNHYAHWLRTVGEPFMHYEWTLWLIRVVLVVAVVAHAVSAYQLSRRGIKARPGKYVHKKARTSYATRTMRWGGIILGLFIVWHILDLTTGTVHSGGFQEGRPYQNVVDTFSTWYGNVIYIVAMLAVGLHVRHGFWSAAQTLGAGSRTRDRALKIVADVLALLLTAGFIAVPVGVMTKVVS
>NZ_CP023703.1|WP_150473827.1|7076886_7078869_+|fumarate-reductase/succinate-dehydrogenase-flavoprotein-subunit
MTSYADYTTGEPVADAKAPAGPIAERWDTRRFEAKLVNPANRRKHTVIVVGTGLAGGSAGATLAEQGYHVVQFCYQDSPRRAHSIAAQGGINAAKNYRNDGDSVHRLFYDTVKGGDFRARESNVHRLAQISVEIIDQCVAQGVPFAREYGGLLDTRSFGGVQVSRTFYARGQTGQQLLLGAYQALSRQIAAGNIEMHPRTEMLDLIVVDGKARGIVARDLITGRIDTYFADAVVLASGGYGNVFYLSTNAMNSNATAIWRAHRRGAYFANPCFTQIHPTCIPRTGDHQSKLTLMSESLRNDGRIWVPKAKGDDRPPNRIPEDERDYYLERIYPAFGNLVPRDIASRAAKNVCDEGRGVGPGGQGVYLDFADAIERMGRKAVEAKYGNLFDMYQRITDEDPYQVPMRIYPAVHYTMGGLWVDYDLQTTVPGLFAIGEANFSDHGANRLGASALMQGLADGYFVLPATINDYLARNPHQSPIDDRHPVVQEVLAENQDRLNLLLSVDGDRTPDSFHREVGELMWEFCGMARTDSGLRKALERIPQIREEFWRRIKVPGTGEEFNQSLEKANRVVDYLELAELMCLDALHRAESCGGHFREGSQTPDGEAARRDEEFAYVAAWEFRGSGGPPPGEHGTGTGAPVLHKEDLAFEYVHPTQRSYA
>NZ_CP023703.1|WP_150473828.1|7078865_7079615_+|succinate-dehydrogenase/fumarate-reductase-iron-sulfur-subunit
MKLTLRVWRQRNADAEGAMSTYEVDGISSDMSFLEMLDTLNEELILKGEDPVAFDHDCREGICGACSLVINGDAHGPERTTTCQLHMRSFQDGDTIDVEPWRASAFPVIKDLVVDRTAFDRIIQAGGYITAPTGAAPEAHATAVPKPDADFAFEHAECIGCGACVAACPNGAAMLFTSAKVNHLNVLPQGAPERETRVLDMVAQMDEEGFGGCTLAGECATACPKGIPLVSITAMNKEWLRATRKVAKR

Crispr_ID: NZ_CP023703_10

• CRISPR_ID: NZ_CP023703_10
• CRISPR_location: 7557009-7557100
• CRISPR_type: Orphan
• Repeat_type: NA
• Spacer_info: 1 spacers
• Cas_protein_info: csa3

Consensus repeat of NZ_CP023703_10

Consensus_repeat	Method
GGACGGGGTCGTCCGGTGCCCTGCGC	CRISPRCasFinder

spacers of NZ_CP023703_10

>10.1|7557035|40|NZ_CP023703|CRISPRCasFinder
GCATCCCACTCCGGCGGTTGCCGGAGGCTGATCGGGCCCA

CRISPR arrays and Neighbor proteins around NZ_CP023703_10

CRISPR arrays

The CRISPR arrays of NZ_CP023703_10

>merge|NZ_CP023703|10|7557009-7557100|CRISPRCasFinder
GGACGGGGTCGTCCGGTGCCCTGCGCGCATCCCACTCCGGCGGTTGCCGGAGGCTGATCGGGCCCAGGACGGGGTCGTCCGGTGCCCTGCGC

>NZ_CP023703|10|9|7557009-7557100|CRISPRCasFinder
GGACGGGGTCGTCCGGTGCCCTGCGC	GCATCCCACTCCGGCGGTTGCCGGAGGCTGATCGGGCCCA
GGACGGGGTCGTCCGGTGCCCTGCGC

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP023703.1|WP_150474172.1|7557227_7558781_+|PucR-family-transcriptional-regulator	unknown	unknown	gnl|CDD|379258
NZ_CP023703.1|WP_150474173.1|7558969_7560193_-|cytochrome-P450	unknown	unknown	gnl|CDD|225035
NZ_CP023703.1|WP_086769505.1|7553478_7554099_-|threonylcarbamoyl-AMP-synthase	unknown	unknown	gnl|CDD|183245
NZ_CP023703.1|WP_150474174.1|7560189_7561437_-|cytochrome-P450	unknown	unknown	gnl|CDD|225035
NZ_CP023703.1|WP_150474164.1|7546454_7547483_-|LLM-class-flavin-dependent-oxidoreductase	unknown	unknown	gnl|CDD|274928
NZ_CP023703.1|WP_150474165.1|7547551_7549054_-|metallophosphoesterase	unknown	unknown	gnl|CDD|277324
NZ_CP023703.1|WP_150474177.1|7562390_7562813_-|roadblock/LC7-domain-containing-protein	unknown	unknown	gnl|CDD|214939
NZ_CP023703.1|WP_150474175.1|7561433_7562060_-|ATP-binding-protein	unknown	unknown	gnl|CDD|225138
NZ_CP023703.1|WP_150474179.1|7565378_7565615_+|hypothetical-protein	unknown	unknown	unknown
NZ_CP023703.1|WP_150474838.1|7545430_7546414_+|TauD/TfdA-family-dioxygenase	unknown	unknown	gnl|CDD|181947
NZ_CP023703.1|WP_150474167.1|7550140_7550974_-|hypothetical-protein	unknown	unknown	gnl|CDD|225837
NZ_CP023703.1|WP_086769987.1|7564560_7565028_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP023703.1|WP_150474169.1|7552548_7553304_-|dienelactone-hydrolase-family-protein	unknown	unknown	gnl|CDD|223489
NZ_CP023703.1|WP_150474176.1|7562031_7562394_-|DUF742-domain-containing-protein	unknown	unknown	gnl|CDD|283084
NZ_CP023703.1|WP_150474171.1|7554927_7556547_+|DHA2-family-efflux-MFS-transporter-permease-subunit	unknown	unknown	gnl|CDD|129794
NZ_CP023703.1|WP_150474166.1|7549107_7549938_-|DUF1684-domain-containing-protein	unknown	unknown	gnl|CDD|377941
NZ_CP023703.1|WP_150474168.1|7551167_7552361_-|sugar-hydrolase	unknown	unknown	gnl|CDD|185755
NZ_CP023703.1|WP_150474178.1|7562809_7564252_-|sensor-histidine-kinase	unknown	unknown	gnl|CDD|340391
NZ_CP023703.1|WP_150474170.1|7554214_7554688_+|MarR-family-transcriptional-regulator	unknown	unknown	gnl|CDD|197670
NZ_CP023703.1|WP_086769988.1|7565699_7566056_-|winged-helix-turn-helix-transcriptional-regulator	csa3	COG0640_csa3_CAS-I-A	gnl|CDD|238042

HMMScan for Signature genes

Protein	Cas_name	Cas_description	E-value	Identity	Coverage
NZ_CP023703.1|WP_086769988.1|7565699_7566056_-|winged-helix-turn-helix-transcriptional-regulator	csa3	COG0640_csa3_CAS-I-A	1.4e-13	46.0	1.1

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
NZ_CP023703.1|WP_150474172.1|7557227_7558781_+|PucR-family-transcriptional-regulator	gnl|CDD|379258	pfam13556, HTH_30, PucR C-terminal helix-turn-helix domain. This helix-turn-helix domain is often found at the C-terminus of PucR-like transcriptional regulators such as Bacillus subtilis pucR and is likely to be DNA-binding.	6.05498e-08
NZ_CP023703.1|WP_150474173.1|7558969_7560193_-|cytochrome-P450	gnl|CDD|225035	COG2124, CypX, Cytochrome P450 [Secondary metabolites biosynthesis, transport, and catabolism].	3.1885e-76
NZ_CP023703.1|WP_086769505.1|7553478_7554099_-|threonylcarbamoyl-AMP-synthase	gnl|CDD|183245	PRK11630, PRK11630, threonylcarbamoyl-AMP synthase.	1.02943e-77
NZ_CP023703.1|WP_150474174.1|7560189_7561437_-|cytochrome-P450	gnl|CDD|225035	COG2124, CypX, Cytochrome P450 [Secondary metabolites biosynthesis, transport, and catabolism].	5.23773e-30
NZ_CP023703.1|WP_150474164.1|7546454_7547483_-|LLM-class-flavin-dependent-oxidoreductase	gnl|CDD|274928	TIGR04027, Luciferase-like_monooxygenase, putative FMN-dependent luciferase-like monooxygenase, KPN_01858 family. This protein family consists of luciferase-like monooxygenases (LLM), and include KPN_01858 from Klebsiella pneumoniae as a representative member. Most are from species that lack F420 biosynthesis, so the family is likely to bind FMN as its cofactor. This family is closely associated with a binding protein-dependent ABC transporter, suggesting a role in catabolism. [Unknown function, Enzymes of unknown specificity].	6.34293e-35
NZ_CP023703.1|WP_150474165.1|7547551_7549054_-|metallophosphoesterase	gnl|CDD|277324	cd07378, MPP_ACP5, Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain. Acid phosphatase 5 (ACP5) removes the mannose 6-phosphate recognition marker from lysosomal proteins. The exact site of dephosphorylation is not clear. Evidence suggests dephosphorylation may take place in a prelysosomal compartment as well as in the lysosome. ACP5 belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.	5.78329e-07
NZ_CP023703.1|WP_150474177.1|7562390_7562813_-|roadblock/LC7-domain-containing-protein	gnl|CDD|214939	smart00960, Robl_LC7, Roadblock/LC7 domain. This family includes proteins that are about 100 amino acids long and have been shown to be related. Members of this family of proteins are associated with both flagellar outer arm dynein and Drosophila and rat brain cytoplasmic dynein. It is proposed that roadblock/LC7 family members may modulate specific dynein functions. This family also includes Golgi-associated MP1 adapter protein and MglB from Myxococcus xanthus, a protein involved in gliding motility. However the family also includes members from non-motile bacteria such as Streptomyces coelicolor, suggesting that the protein may play a structural or regulatory role.	4.00445e-12
NZ_CP023703.1|WP_150474175.1|7561433_7562060_-|ATP-binding-protein	gnl|CDD|225138	COG2229, COG2229, Predicted GTPase [General function prediction only].	6.69049e-34
NZ_CP023703.1|WP_150474838.1|7545430_7546414_+|TauD/TfdA-family-dioxygenase	gnl|CDD|181947	PRK09553, tauD, taurine dioxygenase; Reviewed.	1.52893e-64
NZ_CP023703.1|WP_150474167.1|7550140_7550974_-|hypothetical-protein	gnl|CDD|225837	COG3300, COG3300, MHYT domain (predicted integral membrane sensor domain) [Signal transduction mechanisms].	2.3435e-37
NZ_CP023703.1|WP_150474169.1|7552548_7553304_-|dienelactone-hydrolase-family-protein	gnl|CDD|223489	COG0412, COG0412, Dienelactone hydrolase and related enzymes [Secondary metabolites biosynthesis, transport, and catabolism].	2.26836e-54
NZ_CP023703.1|WP_150474176.1|7562031_7562394_-|DUF742-domain-containing-protein	gnl|CDD|283084	pfam05331, DUF742, Protein of unknown function (DUF742). This family consists of several uncharacterized Streptomyces proteins as well as one from Mycobacterium tuberculosis. The function of these proteins is unknown.	1.12662e-10
NZ_CP023703.1|WP_150474171.1|7554927_7556547_+|DHA2-family-efflux-MFS-transporter-permease-subunit	gnl|CDD|129794	TIGR00711, Uncharacterized_MFS-type_transporter_YhcA, drug resistance transporter, EmrB/QacA subfamily. This subfamily of drug efflux proteins, a part of the major faciliator family, is predicted to have 14 potential membrane-spanning regions. Members with known activities include EmrB (multiple drug resistance efflux pump) in E. coli, FarB (antibacterial fatty acid resistance) in Neisseria gonorrhoeae, TcmA (tetracenomycin C resistance) in Streptomyces glaucescens, etc. In most cases, the efflux pump is described as having a second component encoded in the same operon, such as EmrA of E. coli. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Other].	2.20544e-77
NZ_CP023703.1|WP_150474166.1|7549107_7549938_-|DUF1684-domain-containing-protein	gnl|CDD|377941	pfam07920, DUF1684, Protein of unknown function (DUF1684). The sequences featured in this family are found in hypothetical archaeal and bacterial proteins of unknown function. The region in question is approximately 200 amino acids long.	1.66676e-63
NZ_CP023703.1|WP_150474168.1|7551167_7552361_-|sugar-hydrolase	gnl|CDD|185755	cd09216, GH64-LPHase-like, glycoside hydrolase family 64: laminaripentaose-producing, beta-1,3-glucanase (LPHase)-like. This subfamily is represented by the laminaripentaose-producing, beta-1,3-glucanase (LPHase) of Streptomyces matensis and related bacterial and ascomycete proteins. LPHase is a member of glycoside hydrolase family 64 (GH64), it is an inverting enzyme involved in the cleavage of long-chain polysaccharide beta-1,3-glucans, into specific pentasaccharide oligomers. LPHase is a two-domain crescent fold structure: one domain is composed of 10 beta-strands, eight coming from the N-terminus of the protein and two from the C-terminal region, and the protein has a second inserted domain; this cd includes both domains. This protein has an electronegative, substrate-binding cleft, and conserved Glu and Asp residues involved in the cleavage of the beta-1,3-glucan, laminarin, a plant and fungal cell wall component. Among bacteria, many beta-1,3-glucanases are implicated in fungal cell wall degradation. Also included in this family is GluB , the beta-1,3-glucanase B from Lysobacter enzymogenes Strain N4-7. Recombinant GluB demonstrated higher relative activity toward the branched-chain beta-1,3 glucan substrate zymosan A than toward linear beta-1,3 glucan substrates. Sometimes these two domains are found associated with other domains such as in the Catenulispora acidiphila DSM 44928 carbohydrate binding family 6 protein in which they are positioned N-terminal of a carbohydrate binding module, family 6 (CBM_6) domain. In the Cellulosimicrobium cellulans, glucan endo-1,3-beta-glucosidase, they are positioned N-terminal of a RICIN, carbohydrate-binding domain.	8.91269e-175
NZ_CP023703.1|WP_150474178.1|7562809_7564252_-|sensor-histidine-kinase	gnl|CDD|340391	cd00075, HATPase, Histidine kinase-like ATPase domain. This superfamily includes the histidine kinase-like ATPase (HATPase) domains of several ATP-binding proteins such as histidine kinase, DNA gyrase B, topoisomerases, heat shock protein 90 (HSP90), phytochrome-like ATPases and DNA mismatch repair proteins. Domains belonging to this superfamily are also referred to as GHKL (gyrase, heat-shock protein 90, histidine kinase, MutL) ATPase domains.	3.30839e-14
NZ_CP023703.1|WP_150474170.1|7554214_7554688_+|MarR-family-transcriptional-regulator	gnl|CDD|197670	smart00347, HTH_MARR, helix_turn_helix multiple antibiotic resistance protein.	2.50851e-10
NZ_CP023703.1|WP_086769988.1|7565699_7566056_-|winged-helix-turn-helix-transcriptional-regulator	gnl|CDD|238042	cd00090, HTH_ARSR, Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric repressors. ARSR subfamily of helix-turn-helix bacterial transcription regulatory proteins (winged helix topology). Includes several proteins that appear to dissociate from DNA in the presence of metal ions.	2.91727e-11

Protein sequences

>NZ_CP023703.1|WP_150474171.1|7554927_7556547_+|DHA2-family-efflux-MFS-transporter-permease-subunit
MPSTTVDHSGLPASTAARPPATGRFRSNAWLTLCAVAFGLFMVQLDASVVAIANPEIGRDLKASTADLQWVTNSYLLALAATLILGGKLGDRFGRRTFYLVGVVGFTVSSVAIGLSGSITGVIVFRALQGVFGGLLMPNTLGLLRAVFPPKKFGMAVGIWAMVSAVSTALGPIVGGLLVEHVNWESVFYINLPIGVVAFAFSALVLPQSRNSTGHHRFDVPGVLLLAVGLISLVLGVVKGETWGWTSAGTWAAILAGLLVLAAFGWYETRVEHPLLPMRLFRNRSLTVGAIITALNFFVLLGAIFFIMLYLQNVRGYTPVEAGVRTLPLSLASLVASPLGAALTGRFGARLCMPLGMILQGVACFGLLTWSTDSSYVTMWPPFVALGLGVGMVLAASSDAIVGNAPVRDGGVAGGLQATMLQIGGALGTSVLVSVISARVGSTLGGELTRAGVPAATAAGLGEAKDAVAMGVAPVSAAMPGQLRAAVAEGSAQAFMNGLHAASVVTGLLCLVGAVVAAVGLGGRGSAAPRGADAGGAAV
>NZ_CP023703.1|WP_150474170.1|7554214_7554688_+|MarR-family-transcriptional-regulator
MSDSSAPTGGTDRLAAELAACLPALHRALDRRVGSAYPHPKPPEGQLLLLRFVARHEGTTVREAADALLMKPNNVSALVSQMTERGMLERRQDSTDKRVAHLYLTATSRRRLAEVRDLETGYLSEALLSLTDGEMDALGSAIGALISLTRHLHAAAH
>NZ_CP023703.1|WP_086769505.1|7553478_7554099_-|threonylcarbamoyl-AMP-synthase
MAKYYDVHPDNPQPRTIAQVAAAIRADALIAYPTDSCYALGCRIGSRDGVDRIRSIRELDDKHHFTLVCQDFAQLGQFVHVDNDVFRAIKATTPGSYTFILPATKEVPRMLQHPKKKTVGVRIPDHVVTQALLAELGEPLLSSTLLLPGEEEPMTQGWEIKDLLDNSVDGVLDSGDCGTEPTTVIDFSEGEAQIVRYGAGDASRFE
>NZ_CP023703.1|WP_150474169.1|7552548_7553304_-|dienelactone-hydrolase-family-protein
MTAVQGTAVDVPTEDGVADAYLSRPAAGVPRPGVLLYQDAFGLRPHLRAMADRLAGAGYAVLVPNVFYRHGRSPVVELPEFIDTEARPDIFERLLPVMRSLTPDLVTRDAGAYLRWMARSPLVADGPVAVTGYCMGARLSLLTAGAHPERVAAAAGFHGGRLATEAPDSPHLVAGRVTAELYFGHADDDPALPPEEKERLEKALTAAGVRHRCEVYEGARHGFTQADTAAYQEAASERHWAALLDLLTRTF
>NZ_CP023703.1|WP_150474168.1|7551167_7552361_-|sugar-hydrolase
MFRTLKSRLTAAAGAAALVGTLLSLGPPAQAAVPATIPLKITNNSGRGEPLYVYNLGTLLTTGRQGWADANGTFHAWPAGGNPPTPAPDASITGPAAGGSATIRIPKFSGRIYFSYGQKLVFRLTTGGLVQPAVQNPSDPNRNILFNWSEYTLNDSGLWLNSTQVDMFSAPYAVGVQRSDGSTVSTGRLRPGGYNGFFNALRGQPGGWANLIQTRSDGTVLRALSPLYGVETGALPRTVLDDYINRVWQKYATSTLTVTPFADQPGTKYFGRVSGGVMNFTNSAGAVVTSFQKPDADSVFGCHRLLDAPNDAVRGPISRTLCAGFNRSTLLANPNQPDSTSAGFYQDTVTNHYARKIHAQMADGKAYAFAFDDVGHHESLVHDGSPLQAYLTLDPLN
>NZ_CP023703.1|WP_150474167.1|7550140_7550974_-|hypothetical-protein
MDGTVDGFRYGWVTPVAAYVMACLGGALGLRCIVRSLLDEESWRPGWLALGAASIGCGIWTMHFIAMIGFQVEEARIGYDAGLTLLSLLVAVVVVGIGVFIVGYRGAGVAALCLAGTVTGLGVAAMHYLGMAAMHLDGSIRYDPFTVALSVLIAVVAATAALWAAVSIRGFVTSLGASLVMGVAVSGMHYTGMAAVSVHVHGVSPSWVGDAPTSLLLPMLIGPVIFLLLAAVVVMFDPLLVLGEGDWNRTARAGRAAVPEEDRTAGRSVPRRSWSDR
>NZ_CP023703.1|WP_150474166.1|7549107_7549938_-|DUF1684-domain-containing-protein
MTVQEDRDIDRTGFVREWELWHRRKEGVLAGPHGFLAITGLHWLSPEPARFDDAPGAWSSTAEGVVVDLADGEELTLDGTVVRGRYAFGVIAERDSVYVAAGDALIEVAKRGGHDILRPRHPGNALRTAFSHTPAYAPDPRWVREGRFVPHPRPRPVTVGAAVEGLEHVYDSPGQVEFELDGTTYRLTAFNGGTPGSLTVLFTDATSGVTTYAANRSLQLAAPDGEGRVTLDFNRAGNLPCAYTDLATCPLPPAENRLPVAVEAGERIPLERGGRD
>NZ_CP023703.1|WP_150474165.1|7547551_7549054_-|metallophosphoesterase
MSDSSRDTAQGAGWGAHDPGTYGQLMPAETKKISWLDPRMLWAARNGVLASWFGDPTGRTRGRWVEQRTAAGAPADKVIRRPEPDRFSFMVIGDTGEGDDPQYAAVPGFLKVGQDTSFAVLASDVIYPAGSADDYDGKFFRPYRDYRAPIYAIPGNHDWYEDLGAFMRVFCDAPPLPAEPAPRPSSRAWLRSRLWHRPRQSDGQRLDDARALRGHASQQAVQPGPYWAIDSGPVRIIGIDTGLLGTLDAEQGAWLREVARGPRPKILITGSPLYVDGEHQPCPIEGGGTVDEIVRDPENRFVAAIGGDIHNYQRYPVTLPDGRTLQYVVAGGGGAFMHATHTIPRVSVGGVEEAGFRCYPLRGDSLAFYSRLYGRRLRMRRFFSLTEDEATAVIAERLGIPPTRGPGGPVRITRRIRLVATLLGTARRPDRGTRFRLPVRKIYTSLFSPSSATYSPPFFKCFLRLDVSPQSVRLRCYAATGNRAQELDPPVEDEVTIALA
>NZ_CP023703.1|WP_150474164.1|7546454_7547483_-|LLM-class-flavin-dependent-oxidoreductase
MPSTPRPLRKLGFLTIGLFDEADPRRGHETTLEIIELGERLGFDSAWLRHRHLQYGISSPVAVLAAASQRTSRIELGTAVIPLGWENPLRLAEDLATVDVLSGGRLNPGVSVGPPMHFDRVKEALYPDTADAEDFGYGRARRLLDLVRGEPASGFSGTEGFEVFSDRVQPHSPGLGSRLWYGSGSLGSARWAGENGMNFLTSSVVKAEGPDGEGDFADLQLALVRAFRAAHPDGDAARVSQGLVVIPTDSATPEQRAKYEEFAARRLPRTTSPQGPARLLFAPDLVGTSAELAERLHAHAAFREIDEVAFALPFTFAPEDYVQILTDMATHLGPALGWKPGV
>NZ_CP023703.1|WP_150474838.1|7545430_7546414_+|TauD/TfdA-family-dioxygenase
MAKGVTTDAALEECVRAAGLTLRPAAGHIGAGIEGADLAAGLDDAQVTAIRAAVLRWKVVFFRGQRLDHAGHVAFARRFGEPVVLRKRGSASPADFPEIETTADRLELGGRFGMDHEEWLGRRRHTLLRGWHCDHGARVDPPAATILRAETVPPYGGDTTWSNLAAAYAGLSAPLRRFADGLRAEHRLGVGYQPRPGDDAYVRHLLDHQVASVHPLVRVHPETGERVLYVNGYYVEQITDLSRAESAAILELLLAEATRPEYTVRFRWEPGSVAFWDNRATIHLAPSDTTHLGFPRTMHRVMLTGDIPAGVDGRPSEPVTGTEPGHW
>NZ_CP023703.1|WP_150474172.1|7557227_7558781_+|PucR-family-transcriptional-regulator
MTGRDDERRHAEAVSGQADSAWAQELLDHLRPTGRDIARVVDWLGATVGASVSLCDEHGTPLAGSPAPLDEGLVTDIVSGRLASASWEGDGRHLRLIRVELPTPAAAGVLAVVRTAPFDRRAGDIVTHTAAALELLLRARRTAATGHRLARATSDLRLAILQLLMVEDTSAARRVAAGLWPGLLDTDTACVYVVESTPESRDRLAEACIEATREQSLVVRCPAVDAHVIVVTPRDTTAADLRDVCRRHPGTFLGGSARQSLAHTAAAYGQAVSALAVAHFRPDKTAVYAERTHPERLMDPAVLRAWTTRLLRPLDTLAHHTRAELLATTRLGLEFTAVSAAKVLGVSRNTVRARMERVENLLGADFSDLAVRAAVHLALNTEAGLTEDRTAATEVPVRLGDLLTGPALRTWAHGLLARLDSDGRDLRGTLRAWISAGGNAERAAQLLGVHAQTVREHVRGAEPVLERRLLAAGGDLYEVVLAHLASGALDPPDLHPDLHTEVHPGLRADARPDVRQA
>NZ_CP023703.1|WP_150474173.1|7558969_7560193_-|cytochrome-P450
MTTTDRIVLDPFGSDLHAESARLRALGPIVPIELPGGIPAWAPTGYDTLRELILDPQVSKDPRKHWRLWPELGTHPTWGWILGWVGVVNMLSTYGTDHARLRRLVAPSFTARRTESLRQRVETITAELLDDLDRGGDTADLKAAFAHPLPMRIICELFGVPEDMREDHVQLVASIMDTTDPTPEHAERVQERIGSVLGGLIAYKSEHPGDDMTTELIRVRDEEGDRLSGEELLYTLLLVIGAGFETTVNLIGNAVVALLRAPEQLAAVRRGDLGWDAVVDETLRLYPSIATLPLRFAVSDLKVGDVTIPAGDAIVTTYAAAGVDPAHYGPDAEVFDAARRADDHLAFGIGVHRCIGAPLGRMEALTALPALFDRFPQLRLDTGAGELEQVPSFIASGWQTIPVRLRG
>NZ_CP023703.1|WP_150474174.1|7560189_7561437_-|cytochrome-P450
MTTYPPDRHDFSRSAPVRLWEDGFASDPHRYYAALSAQGPIGWAELAPGVPAYLVTDRRAALDVLHDEETFSHDPRAWEGTVPADSPVLGMMRWRPNALFADGAAHVRYRTTLIDVFDLVEPHDLRARVHRAVRLLVDRIGPHGGADLVADFSRPLMALVFNDLFGLPDSAGDRLEAGLGKMMEGGAQAAEGEAEYGRYVLELIAAKAERPGDDLPSRLLGHPAGLTGEEVTWQVFLTLGAGYEPTANLLSNTLSRILGNPLYYSTLTSGARPVMDAVVEVLHHETPLSNYGIYYARRPVSFHGVWLRDAVPVVVSYGALGVRAELEATAGRLPNDASHLSWGAGSHACPVKQHTLLIVTEAIERLTQWLPDLDPVLPRERLTWRPGPFHRSLTALPVRFSPRAADRPHRSGVPS
>NZ_CP023703.1|WP_150474175.1|7561433_7562060_-|ATP-binding-protein
MASAPSSTPSAPRAPGAIHQPDTARDLVKILVAGPFGVGKTTLIDSVSEIRPLHTEEHLSEASARVDDLDGVRDKATTTVAIDFGRISLPGGVVLYLFGTPGQERFRSLWDDIAYGALGALVLVDSRRLDASFDVLGLVEDSGLPYAVAFNAFPDSPTHHGEERLRRALDLEPSTPLVTCDARDANSSIDALLALVDHLITRDPAEAR
>NZ_CP023703.1|WP_150474176.1|7562031_7562394_-|DUF742-domain-containing-protein
MTARPAGRPLVPAYLSTGGVARPSRPHLERLSVLARTGQSVPPGLPAAELALLDALEGGSLAVVEAAALLGLPVSALCVLAAGLADRDLIHTRAPIPPADRFDPDLLKRVADGLRALKHA
>NZ_CP023703.1|WP_150474177.1|7562390_7562813_-|roadblock/LC7-domain-containing-protein
MTSRNTGDTAWALEPILQVPHVVAAVMLTRDGLVTGYTDALSQPSAERVAAISSTVQGACRTAAAAFADRDKAEVRQVVIESDHGYVLIVPTDHGTCVAAYGDGEVRLDLLAHRVHSQVARLGEKAMAAAPRGADDNTPA
>NZ_CP023703.1|WP_150474178.1|7562809_7564252_-|sensor-histidine-kinase
MIELPDLVAGGLAAGTLSALALGGGLLRLRRQQTRQRAEISALRTQLDGSLRAFTAEVEHLAARRVPAAAQRVAHPHLAVPGPLQPLTVGTPLGIALENVLLALQAEVASQRTRVDAAAQAGMRGATREIQAALYRLQDALRRLQQRYDDPELAQTLFQLDHENEQSLRRAQVAAVVCGAWVGLAREESHLVDAVTGGQARLAGYQRVKVHNHLEPGTALVSHAVEPVAIIVAELLDNALRHSAPDTDVVVSLEHVHHGVCVTVDDAGLGMTRDERDRAQRLVAGDAPILLTDLGDPPRMGLAAIGRLTRQFDLGVDVSSASPYGGVRAVLRVDSHLLSRLDPADRPPAPSAPRTTRRSGPAAPAPTHAYGTHDAVPDAPRHHTPTDENGDGEGDGNGNDGLPQRRRRRTRPAPAAVPEASAPPASSRPARRPEEAAAALGALQSGTAAARSEAAPAAGTPTAAAAHDTDHTHDEGGAAR
>NZ_CP023703.1|WP_086769987.1|7564560_7565028_-|hypothetical-protein
MSYAMWARGVEWLAAASTDPRNCKREWDQGHGVTLLEAGRYWNVLSVPDRLGLLTLDLLWQPTLPVPGPTLVDTAAQRVGFFLPPDPASRWIGDGLRHVGRGSWVAVPPPYRPARFLEWLIPPDGTGALHSPATLELALRQANGTLAVLPPPRGA
>NZ_CP023703.1|WP_150474179.1|7565378_7565615_+|hypothetical-protein
MATGTETGDVTGTRDKDYNLIWYVEACLNNALRLETYIQDAERDKDTEVADLFRKAQADSRKGAEMGKDLLRARLSGG
>NZ_CP023703.1|WP_086769988.1|7565699_7566056_-|winged-helix-turn-helix-transcriptional-regulator
MQVPLYQAKAEFFRMLGHPVRIRVLELLQGGPVAVRDLLTEIEIEPSSLSQQLAVLRRSGIVVSIREGSTVSYALAGGDVAELLRAARRILTELIAGQHELLAELRQSEPSVPAPPLP

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity
NZ_CP023703_9	9.3|7067193|27|NZ_CP023703|CRT	7067193-7067219	27	MG893203	Vibrio phage VP06, complete genome	21513-21539	4	0.852
NZ_CP023703_9	9.3|7067193|27|NZ_CP023703|CRT	7067193-7067219	27	MF754113	Vibrio phage vB_VpaS_KF3, complete genome	135-161	4	0.852
NZ_CP023703_9	9.3|7067193|27|NZ_CP023703|CRT	7067193-7067219	27	MF754114	Vibrio phage vB_VpaS_KF4, complete genome	21494-21520	4	0.852
NZ_CP023703_2	2.1|1198444|29|NZ_CP023703|CRISPRCasFinder	1198444-1198472	29	CP054935	Nocardiopsis flavescens strain NA01583 plasmid unnamed2, complete sequence	5361-5389	5	0.828
NZ_CP023703_2	2.1|1198444|29|NZ_CP023703|CRISPRCasFinder	1198444-1198472	29	CP054935	Nocardiopsis flavescens strain NA01583 plasmid unnamed2, complete sequence	23715-23743	5	0.828
NZ_CP023703_7	7.2|5133673|33|NZ_CP023703|CRISPRCasFinder	5133673-5133705	33	MT936332	Streptomyces phage phiRKBJ001, complete genome	35700-35732	5	0.848
NZ_CP023703_7	7.2|5133673|33|NZ_CP023703|CRISPRCasFinder	5133673-5133705	33	MT498053	Streptomyces phage PHTowN, complete genome	35061-35093	5	0.848
NZ_CP023703_7	7.2|5133673|33|NZ_CP023703|CRISPRCasFinder	5133673-5133705	33	MT897908	Streptomyces phage ShakeNBake, complete genome	35079-35111	5	0.848
NZ_CP023703_7	7.2|5133673|33|NZ_CP023703|CRISPRCasFinder	5133673-5133705	33	MT498037	Streptomyces phage Dryad, complete genome	36247-36279	5	0.848
NZ_CP023703_2	2.1|1198444|29|NZ_CP023703|CRISPRCasFinder	1198444-1198472	29	NZ_CP041043	Paracoccus sp. AK26 plasmid pAK3, complete sequence	67540-67568	6	0.793
NZ_CP023703_2	2.1|1198444|29|NZ_CP023703|CRISPRCasFinder	1198444-1198472	29	NZ_CP021653	Ralstonia solanacearum strain RS 488 plasmid unnamed, complete sequence	1115303-1115331	6	0.793
NZ_CP023703_2	2.1|1198444|29|NZ_CP023703|CRISPRCasFinder	1198444-1198472	29	NZ_CP012940	Ralstonia solanacearum strain UW163 plasmid unnamed, complete sequence	863862-863890	6	0.793
NZ_CP023703_2	2.1|1198444|29|NZ_CP023703|CRISPRCasFinder	1198444-1198472	29	NZ_CP012688	Ralstonia solanacearum strain UY031 plasmid unnamed, complete sequence	1115310-1115338	6	0.793
NZ_CP023703_2	2.1|1198444|29|NZ_CP023703|CRISPRCasFinder	1198444-1198472	29	NZ_AP014705	Methylobacterium aquaticum strain MA-22A plasmid pMaq22A_1p, complete sequence	539442-539470	6	0.793
NZ_CP023703_2	2.1|1198444|29|NZ_CP023703|CRISPRCasFinder	1198444-1198472	29	NZ_CP024310	Sinorhizobium fredii strain NXT3 plasmid pSfreNXT3c, complete sequence	1031139-1031167	6	0.793
NZ_CP023703_2	2.1|1198444|29|NZ_CP023703|CRISPRCasFinder	1198444-1198472	29	NC_017575	Ralstonia solanacearum Po82 megaplasmid, complete sequence	1367269-1367297	6	0.793
NZ_CP023703_2	2.1|1198444|29|NZ_CP023703|CRISPRCasFinder	1198444-1198472	29	NZ_CP026308	Ralstonia solanacearum strain IBSBF 2571 plasmid unnamed, complete sequence	1367213-1367241	6	0.793
NZ_CP023703_2	2.1|1198444|29|NZ_CP023703|CRISPRCasFinder	1198444-1198472	29	CP047139	Ralstonia solanacearum strain CFBP 8695 plasmid unnamed, complete sequence	1042868-1042896	6	0.793
NZ_CP023703_2	2.1|1198444|29|NZ_CP023703|CRISPRCasFinder	1198444-1198472	29	NZ_CP051295	Ralstonia solanacearum strain CIAT_078 plasmid megaplasmid, complete sequence	855600-855628	6	0.793
NZ_CP023703_2	2.1|1198444|29|NZ_CP023703|CRISPRCasFinder	1198444-1198472	29	NZ_CP023064	Sinorhizobium sp. CCBAU 05631 plasmid pSS05631b, complete sequence	849967-849995	6	0.793
NZ_CP023703_2	2.1|1198444|29|NZ_CP023703|CRISPRCasFinder	1198444-1198472	29	CP047137	Ralstonia solanacearum strain CFBP 8697 plasmid unnamed, complete sequence	1000070-1000098	6	0.793
NZ_CP023703_2	2.1|1198444|29|NZ_CP023703|CRISPRCasFinder	1198444-1198472	29	NZ_CP012944	Ralstonia solanacearum strain IBSBF1503 plasmid unnamed, complete sequence	1030568-1030596	6	0.793
NZ_CP023703_7	7.2|5133673|33|NZ_CP023703|CRISPRCasFinder	5133673-5133705	33	MK305891	Streptomyces phage Gibson, complete genome	35253-35285	6	0.818
NZ_CP023703_7	7.2|5133673|33|NZ_CP023703|CRISPRCasFinder	5133673-5133705	33	MH019216	Streptomyces phage Wentworth, complete genome	35513-35545	6	0.818
NZ_CP023703_9	9.3|7067193|27|NZ_CP023703|CRT	7067193-7067219	27	NC_019893	Singulisphaera acidiphila DSM 18658 plasmid pSINAC01, complete sequence	53853-53879	6	0.778
NZ_CP023703_9	9.3|7067193|27|NZ_CP023703|CRT	7067193-7067219	27	LR743530	Xanthomonas phage Suba genome assembly, chromosome: 1	4862-4888	6	0.778
NZ_CP023703_2	2.1|1198444|29|NZ_CP023703|CRISPRCasFinder	1198444-1198472	29	NZ_CP034352	Streptomyces sp. W1SF4 plasmid p2, complete sequence	236036-236064	7	0.759
NZ_CP023703_2	2.1|1198444|29|NZ_CP023703|CRISPRCasFinder	1198444-1198472	29	NZ_CP029358	Azospirillum sp. CFH 70021 plasmid unnamed3	39115-39143	7	0.759
NZ_CP023703_2	2.1|1198444|29|NZ_CP023703|CRISPRCasFinder	1198444-1198472	29	NC_017966	Tistrella mobilis KA081020-065 plasmid pTM2, complete sequence	476200-476228	7	0.759
NZ_CP023703_2	2.1|1198444|29|NZ_CP023703|CRISPRCasFinder	1198444-1198472	29	NZ_CP010016	Burkholderia thailandensis 34 plasmid unnamed, complete sequence	71521-71549	7	0.759
NZ_CP023703_9	9.3|7067193|27|NZ_CP023703|CRT	7067193-7067219	27	NZ_CP016593	Ketogulonicigenium vulgare strain SKV plasmid pKvSKV1, complete sequence	126551-126577	7	0.741
NZ_CP023703_9	9.3|7067193|27|NZ_CP023703|CRT	7067193-7067219	27	NC_017386	Ketogulonicigenium vulgare WSH-001 plasmid 1, complete sequence	61747-61773	7	0.741
NZ_CP023703_9	9.3|7067193|27|NZ_CP023703|CRT	7067193-7067219	27	NC_014621	Ketogulonicigenium vulgare Y25 plasmid pYP1, complete sequence	28381-28407	7	0.741
NZ_CP023703_9	9.3|7067193|27|NZ_CP023703|CRT	7067193-7067219	27	NZ_CP012909	Ketogulonicigenium vulgare strain Hbe602 plasmid 1, complete sequence	126554-126580	7	0.741
NZ_CP023703_9	9.3|7067193|27|NZ_CP023703|CRT	7067193-7067219	27	KJ510412	Mycobacterium phage ZoeJ, complete genome	20398-20424	7	0.741
NZ_CP023703_7	7.2|5133673|33|NZ_CP023703|CRISPRCasFinder	5133673-5133705	33	MT658802	Mycobacterium phage Aziz, complete genome	20016-20048	8	0.758
NZ_CP023703_7	7.2|5133673|33|NZ_CP023703|CRISPRCasFinder	5133673-5133705	33	MF319184	Mycobacterium phage GenevaB15, complete genome	20016-20048	8	0.758
NZ_CP023703_7	7.2|5133673|33|NZ_CP023703|CRISPRCasFinder	5133673-5133705	33	KT186229	Streptomyces phage Verse, complete genome	21799-21831	8	0.758
NZ_CP023703_7	7.2|5133673|33|NZ_CP023703|CRISPRCasFinder	5133673-5133705	33	KT186228	Streptomyces phage Amela, complete genome	21805-21837	8	0.758
NZ_CP023703_9	9.3|7067193|27|NZ_CP023703|CRT	7067193-7067219	27	NZ_CP023017	Ralstonia solanacearum strain SL3022 plasmid unnamed, complete sequence	975164-975190	8	0.704
NZ_CP023703_1	1.5|842804|32|NZ_CP023703|PILER-CR	842804-842835	32	NC_015170	Deinococcus proteolyticus MRP plasmid pDEIPR03, complete sequence	53282-53313	9	0.719
NZ_CP023703_7	7.1|5133616|33|NZ_CP023703|CRISPRCasFinder	5133616-5133648	33	NC_047905	Streptomyces phage Attoomi, complete genome	35943-35975	9	0.727
NZ_CP023703_7	7.2|5133673|33|NZ_CP023703|CRISPRCasFinder	5133673-5133705	33	NZ_CP027794	Rhodococcus hoagii strain DSSKP-R-001 plasmid plas1, complete sequence	66959-66991	9	0.727
NZ_CP023703_7	7.1|5133616|33|NZ_CP023703|CRISPRCasFinder	5133616-5133648	33	NZ_CP022367	Azospirillum sp. TSH58 plasmid TSH58_p02, complete sequence	1400282-1400314	10	0.697
NZ_CP023703_4	4.1|4085762|48|NZ_CP023703|CRISPRCasFinder	4085762-4085809	48	NZ_CP018784	Curtobacterium pusillum strain AA3 plasmid pCPAA3, complete sequence	184735-184782	11	0.771

1. spacer 9.3|7067193|27|NZ_CP023703|CRT matches to MG893203 (Vibrio phage VP06, complete genome) position: , mismatch: 4, identity: 0.852

tagcaacaacggcaacaacggtgggaa	CRISPR spacer
caacaacaacgccaacaacggtgtgaa	Protospacer
.*.******** *********** ***

2. spacer 9.3|7067193|27|NZ_CP023703|CRT matches to MF754113 (Vibrio phage vB_VpaS_KF3, complete genome) position: , mismatch: 4, identity: 0.852

tagcaacaacggcaacaacggtgggaa	CRISPR spacer
caacaacaacgccaacaacggtgtgaa	Protospacer
.*.******** *********** ***

3. spacer 9.3|7067193|27|NZ_CP023703|CRT matches to MF754114 (Vibrio phage vB_VpaS_KF4, complete genome) position: , mismatch: 4, identity: 0.852

tagcaacaacggcaacaacggtgggaa	CRISPR spacer
caacaacaacgccaacaacggtgtgaa	Protospacer
.*.******** *********** ***

4. spacer 2.1|1198444|29|NZ_CP023703|CRISPRCasFinder matches to CP054935 (Nocardiopsis flavescens strain NA01583 plasmid unnamed2, complete sequence) position: , mismatch: 5, identity: 0.828

ggccggcgccgccaggccacgcccggccc	CRISPR spacer
gggcagcgccgccaggccacgcccagttc	Protospacer
** *.*******************.*..*

5. spacer 2.1|1198444|29|NZ_CP023703|CRISPRCasFinder matches to CP054935 (Nocardiopsis flavescens strain NA01583 plasmid unnamed2, complete sequence) position: , mismatch: 5, identity: 0.828

ggccggcgccgccaggccacgcccggccc	CRISPR spacer
gggcagcgccgccaggccacgcccagttc	Protospacer
** *.*******************.*..*

6. spacer 7.2|5133673|33|NZ_CP023703|CRISPRCasFinder matches to MT936332 (Streptomyces phage phiRKBJ001, complete genome) position: , mismatch: 5, identity: 0.848

ccaccgaggagccctcggaggagcc-gacgacgg	CRISPR spacer
tcaccgaggagcgctgggaggagccggactacg-	Protospacer
.*********** ** ********* *** *** 

7. spacer 7.2|5133673|33|NZ_CP023703|CRISPRCasFinder matches to MT498053 (Streptomyces phage PHTowN, complete genome) position: , mismatch: 5, identity: 0.848

ccaccgaggagccctcggaggagcc-gacgacgg	CRISPR spacer
tcaccgaggagcgctgggaggagccggactacg-	Protospacer
.*********** ** ********* *** *** 

8. spacer 7.2|5133673|33|NZ_CP023703|CRISPRCasFinder matches to MT897908 (Streptomyces phage ShakeNBake, complete genome) position: , mismatch: 5, identity: 0.848

ccaccgaggagccctcggaggagcc-gacgacgg	CRISPR spacer
tcaccgaggagcgctgggaggagccggactacg-	Protospacer
.*********** ** ********* *** *** 

9. spacer 7.2|5133673|33|NZ_CP023703|CRISPRCasFinder matches to MT498037 (Streptomyces phage Dryad, complete genome) position: , mismatch: 5, identity: 0.848

ccaccgaggagccctcggaggagcc-gacgacgg	CRISPR spacer
tcaccgaggagccctggcaggagccggactacg-	Protospacer
.************** * ******* *** *** 

10. spacer 2.1|1198444|29|NZ_CP023703|CRISPRCasFinder matches to NZ_CP041043 (Paracoccus sp. AK26 plasmid pAK3, complete sequence) position: , mismatch: 6, identity: 0.793

ggccggcgccgccaggccacgcccggccc	CRISPR spacer
ccccggcgccgccaggccacggccgatgc	Protospacer
  ******************* ***.. *

11. spacer 2.1|1198444|29|NZ_CP023703|CRISPRCasFinder matches to NZ_CP021653 (Ralstonia solanacearum strain RS 488 plasmid unnamed, complete sequence) position: , mismatch: 6, identity: 0.793

ggccggcgccgccaggccacgcccggccc	CRISPR spacer
gaacagcgatgccaggccacgcccggccg	Protospacer
*. *.*** .****************** 

12. spacer 2.1|1198444|29|NZ_CP023703|CRISPRCasFinder matches to NZ_CP012940 (Ralstonia solanacearum strain UW163 plasmid unnamed, complete sequence) position: , mismatch: 6, identity: 0.793

ggccggcgccgccaggccacgcccggccc	CRISPR spacer
gaacagcgatgccaggccacgcccggccg	Protospacer
*. *.*** .****************** 

13. spacer 2.1|1198444|29|NZ_CP023703|CRISPRCasFinder matches to NZ_CP012688 (Ralstonia solanacearum strain UY031 plasmid unnamed, complete sequence) position: , mismatch: 6, identity: 0.793

ggccggcgccgccaggccacgcccggccc	CRISPR spacer
gaacagcgatgccaggccacgcccggccg	Protospacer
*. *.*** .****************** 

14. spacer 2.1|1198444|29|NZ_CP023703|CRISPRCasFinder matches to NZ_AP014705 (Methylobacterium aquaticum strain MA-22A plasmid pMaq22A_1p, complete sequence) position: , mismatch: 6, identity: 0.793

ggccggcgccgccaggccacgcccggccc	CRISPR spacer
gtcgggcgccgcgaggtcacgcccggcaa	Protospacer
* * ******** ***.**********  

15. spacer 2.1|1198444|29|NZ_CP023703|CRISPRCasFinder matches to NZ_CP024310 (Sinorhizobium fredii strain NXT3 plasmid pSfreNXT3c, complete sequence) position: , mismatch: 6, identity: 0.793

ggccggcgccgccaggccacgcccggccc	CRISPR spacer
agccggcgccgccgggccacgcgccgatc	Protospacer
.************.******** * * .*

16. spacer 2.1|1198444|29|NZ_CP023703|CRISPRCasFinder matches to NC_017575 (Ralstonia solanacearum Po82 megaplasmid, complete sequence) position: , mismatch: 6, identity: 0.793

ggccggcgccgccaggccacgcccggccc	CRISPR spacer
gaacagcgatgccaggccacgcccggccg	Protospacer
*. *.*** .****************** 

17. spacer 2.1|1198444|29|NZ_CP023703|CRISPRCasFinder matches to NZ_CP026308 (Ralstonia solanacearum strain IBSBF 2571 plasmid unnamed, complete sequence) position: , mismatch: 6, identity: 0.793

ggccggcgccgccaggccacgcccggccc	CRISPR spacer
gaacagcgatgccaggccacgcccggccg	Protospacer
*. *.*** .****************** 

18. spacer 2.1|1198444|29|NZ_CP023703|CRISPRCasFinder matches to CP047139 (Ralstonia solanacearum strain CFBP 8695 plasmid unnamed, complete sequence) position: , mismatch: 6, identity: 0.793

ggccggcgccgccaggccacgcccggccc	CRISPR spacer
gaacagcgatgccaggccacgcccggccg	Protospacer
*. *.*** .****************** 

19. spacer 2.1|1198444|29|NZ_CP023703|CRISPRCasFinder matches to NZ_CP051295 (Ralstonia solanacearum strain CIAT_078 plasmid megaplasmid, complete sequence) position: , mismatch: 6, identity: 0.793

ggccggcgccgccaggccacgcccggccc	CRISPR spacer
gaacagcgatgccaggccacgcccggccg	Protospacer
*. *.*** .****************** 

20. spacer 2.1|1198444|29|NZ_CP023703|CRISPRCasFinder matches to NZ_CP023064 (Sinorhizobium sp. CCBAU 05631 plasmid pSS05631b, complete sequence) position: , mismatch: 6, identity: 0.793

ggccggcgccgccaggccacgcccggccc	CRISPR spacer
agccggcgccgccgggccacgcgccgatc	Protospacer
.************.******** * * .*

21. spacer 2.1|1198444|29|NZ_CP023703|CRISPRCasFinder matches to CP047137 (Ralstonia solanacearum strain CFBP 8697 plasmid unnamed, complete sequence) position: , mismatch: 6, identity: 0.793

ggccggcgccgccaggccacgcccggccc	CRISPR spacer
gaacagcgatgccaggccacgcccggccg	Protospacer
*. *.*** .****************** 

22. spacer 2.1|1198444|29|NZ_CP023703|CRISPRCasFinder matches to NZ_CP012944 (Ralstonia solanacearum strain IBSBF1503 plasmid unnamed, complete sequence) position: , mismatch: 6, identity: 0.793

ggccggcgccgccaggccacgcccggccc	CRISPR spacer
gaacagcgatgccaggccacgcccggccg	Protospacer
*. *.*** .****************** 

23. spacer 7.2|5133673|33|NZ_CP023703|CRISPRCasFinder matches to MK305891 (Streptomyces phage Gibson, complete genome) position: , mismatch: 6, identity: 0.818

ccaccgaggagccctcggaggagcc-gacgacgg	CRISPR spacer
tgaccgaggagcgctgggaggagccggactacg-	Protospacer
. ********** ** ********* *** *** 

24. spacer 7.2|5133673|33|NZ_CP023703|CRISPRCasFinder matches to MH019216 (Streptomyces phage Wentworth, complete genome) position: , mismatch: 6, identity: 0.818

ccaccgaggagccctcggaggagcc-gacgacgg	CRISPR spacer
tgaccgaggagcgctgggaggagccggactacg-	Protospacer
. ********** ** ********* *** *** 

25. spacer 9.3|7067193|27|NZ_CP023703|CRT matches to NC_019893 (Singulisphaera acidiphila DSM 18658 plasmid pSINAC01, complete sequence) position: , mismatch: 6, identity: 0.778

tagcaacaacggcaacaacggtgggaa	CRISPR spacer
caacaacaacggcaacagcggtggtgg	Protospacer
.*.**************.****** ..

26. spacer 9.3|7067193|27|NZ_CP023703|CRT matches to LR743530 (Xanthomonas phage Suba genome assembly, chromosome: 1) position: , mismatch: 6, identity: 0.778

tagcaacaacggcaacaacggtgggaa	CRISPR spacer
cagcaacagcggcaacaatggtggcgg	Protospacer
.*******.*********.***** ..

27. spacer 2.1|1198444|29|NZ_CP023703|CRISPRCasFinder matches to NZ_CP034352 (Streptomyces sp. W1SF4 plasmid p2, complete sequence) position: , mismatch: 7, identity: 0.759

ggccggcgccgccaggccacgcccggccc	CRISPR spacer
caccgccgccgccacgccacgcccgtacg	Protospacer
 .*** ******** **********  * 

28. spacer 2.1|1198444|29|NZ_CP023703|CRISPRCasFinder matches to NZ_CP029358 (Azospirillum sp. CFH 70021 plasmid unnamed3) position: , mismatch: 7, identity: 0.759

ggccggcgccgccaggccacgcccggccc	CRISPR spacer
tggtggcgcggccatgccacgcccggcga	Protospacer
 * .***** **** ************  

29. spacer 2.1|1198444|29|NZ_CP023703|CRISPRCasFinder matches to NC_017966 (Tistrella mobilis KA081020-065 plasmid pTM2, complete sequence) position: , mismatch: 7, identity: 0.759

ggccggcgccgccaggccacgcccggccc	CRISPR spacer
agcccgcgccgccagaccacgcccacatc	Protospacer
.*** **********.********.  .*

30. spacer 2.1|1198444|29|NZ_CP023703|CRISPRCasFinder matches to NZ_CP010016 (Burkholderia thailandensis 34 plasmid unnamed, complete sequence) position: , mismatch: 7, identity: 0.759

ggccggcgccgccaggccacgcccggccc	CRISPR spacer
gcccggcgcccccaggccaggcccgcgga	Protospacer
* ******** ******** *****    

31. spacer 9.3|7067193|27|NZ_CP023703|CRT matches to NZ_CP016593 (Ketogulonicigenium vulgare strain SKV plasmid pKvSKV1, complete sequence) position: , mismatch: 7, identity: 0.741

tagcaacaacggcaacaacggtgggaa	CRISPR spacer
cttcaacaaaggcaacaacggtggtgc	Protospacer
.  ****** ************** . 

32. spacer 9.3|7067193|27|NZ_CP023703|CRT matches to NC_017386 (Ketogulonicigenium vulgare WSH-001 plasmid 1, complete sequence) position: , mismatch: 7, identity: 0.741

tagcaacaacggcaacaacggtgggaa	CRISPR spacer
cttcaacaaaggcaacaacggtggtgc	Protospacer
.  ****** ************** . 

33. spacer 9.3|7067193|27|NZ_CP023703|CRT matches to NC_014621 (Ketogulonicigenium vulgare Y25 plasmid pYP1, complete sequence) position: , mismatch: 7, identity: 0.741

tagcaacaacggcaacaacggtgggaa	CRISPR spacer
cttcaacaaaggcaacaacggtggtgc	Protospacer
.  ****** ************** . 

34. spacer 9.3|7067193|27|NZ_CP023703|CRT matches to NZ_CP012909 (Ketogulonicigenium vulgare strain Hbe602 plasmid 1, complete sequence) position: , mismatch: 7, identity: 0.741

tagcaacaacggcaacaacggtgggaa	CRISPR spacer
cttcaacaaaggcaacaacggtggtgc	Protospacer
.  ****** ************** . 

35. spacer 9.3|7067193|27|NZ_CP023703|CRT matches to KJ510412 (Mycobacterium phage ZoeJ, complete genome) position: , mismatch: 7, identity: 0.741

tagcaacaacggcaacaacg-----gtgggaa	CRISPR spacer
gagcaacaacggcaacaacgtgcccgc-----	Protospacer
 *******************     *.     

36. spacer 7.2|5133673|33|NZ_CP023703|CRISPRCasFinder matches to MT658802 (Mycobacterium phage Aziz, complete genome) position: , mismatch: 8, identity: 0.758

ccaccgaggagccctcggaggagccgacgacgg	CRISPR spacer
cgcgccaggagccctcgaacgagccgacgactc	Protospacer
*   * ***********.* ***********  

37. spacer 7.2|5133673|33|NZ_CP023703|CRISPRCasFinder matches to MF319184 (Mycobacterium phage GenevaB15, complete genome) position: , mismatch: 8, identity: 0.758

ccaccgaggagccctcggaggagccgacgacgg	CRISPR spacer
cgcgccaggagccctcgaacgagccgacgactc	Protospacer
*   * ***********.* ***********  

38. spacer 7.2|5133673|33|NZ_CP023703|CRISPRCasFinder matches to KT186229 (Streptomyces phage Verse, complete genome) position: , mismatch: 8, identity: 0.758

ccaccgaggagccctcggaggagccgacgacgg	CRISPR spacer
tcagggtcgagctgtcggaggagccgacgacgc	Protospacer
.**  *  ****. ****************** 

39. spacer 7.2|5133673|33|NZ_CP023703|CRISPRCasFinder matches to KT186228 (Streptomyces phage Amela, complete genome) position: , mismatch: 8, identity: 0.758

ccaccgaggagccctcggaggagccgacgacgg	CRISPR spacer
tcagggtcgagctgtcggaggagccgacgacgc	Protospacer
.**  *  ****. ****************** 

40. spacer 9.3|7067193|27|NZ_CP023703|CRT matches to NZ_CP023017 (Ralstonia solanacearum strain SL3022 plasmid unnamed, complete sequence) position: , mismatch: 8, identity: 0.704

tagcaacaacggcaacaacggtgggaa	CRISPR spacer
cggcaacaacggcaacaacggcaacgc	Protospacer
..*******************... . 

41. spacer 1.5|842804|32|NZ_CP023703|PILER-CR matches to NC_015170 (Deinococcus proteolyticus MRP plasmid pDEIPR03, complete sequence) position: , mismatch: 9, identity: 0.719

cccgctcgaactcctcccgggggtatcccggc	CRISPR spacer
gggacacgaactcatcccgggcgtatccctgg	Protospacer
   .* ******* ******* ******* * 

42. spacer 7.1|5133616|33|NZ_CP023703|CRISPRCasFinder matches to NC_047905 (Streptomyces phage Attoomi, complete genome) position: , mismatch: 9, identity: 0.727

gcacggcgaccccgtcgaccaagccgccgaaga	CRISPR spacer
ccacggccaccccgtcggccaagcccaaggcca	Protospacer
 ****** *********.*******   *.  *

43. spacer 7.2|5133673|33|NZ_CP023703|CRISPRCasFinder matches to NZ_CP027794 (Rhodococcus hoagii strain DSSKP-R-001 plasmid plas1, complete sequence) position: , mismatch: 9, identity: 0.727

ccaccgaggagccctcggaggagccgacgacgg	CRISPR spacer
ccaccgaggagtccacggaggagctggacgcct	Protospacer
***********.** *********.*.  .*  

44. spacer 7.1|5133616|33|NZ_CP023703|CRISPRCasFinder matches to NZ_CP022367 (Azospirillum sp. TSH58 plasmid TSH58_p02, complete sequence) position: , mismatch: 10, identity: 0.697

gcacggcgaccccgtcgaccaagccgccgaaga	CRISPR spacer
cgggtgcgaccacgtcgaccatgccgccgtcgc	Protospacer
  .  ****** ********* *******  * 

45. spacer 4.1|4085762|48|NZ_CP023703|CRISPRCasFinder matches to NZ_CP018784 (Curtobacterium pusillum strain AA3 plasmid pCPAA3, complete sequence) position: , mismatch: 11, identity: 0.771

caagcccggtgctctgctgctgagctacacgccgatg-----cgccgacgtgg	CRISPR spacer
agagtccggtgctctgctgctgagctacacgccgatggtgttcatcgt-----	Protospacer
 .**.********************************     *..**