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_CP044427	Serinicoccus sp. W204 chromosome, complete genome	7 crisprs	csa3,cas3,DinG,WYL,cas4,DEDDh,RT	1	4	0	0

1. NZ_CP044427

CRISPR-Cas detection and classification

Crispr_ID: NZ_CP044427_1

• CRISPR_ID: NZ_CP044427_1
• CRISPR_location: 675730-675815
• CRISPR_type: Orphan
• Repeat_type: NA
• Spacer_info: 1 spacers

Consensus repeat of NZ_CP044427_1

Consensus_repeat	Method
GACGACGGCGCGACCACCGCCGGCGACGA	CRISPRCasFinder

spacers of NZ_CP044427_1

>1.1|675759|28|NZ_CP044427|CRISPRCasFinder
CACGACCACCGATGACGGCGCGACCACG

CRISPR arrays and Neighbor proteins around NZ_CP044427_1

CRISPR arrays

The CRISPR arrays of NZ_CP044427_1

>merge|NZ_CP044427|1|675730-675815|CRISPRCasFinder
GACGACGGCGCGACCACCGCCGGCGACGACACGACCACCGATGACGGCGCGACCACGGACGACGGCGCGAGCACCGCCGGCGACGA

>NZ_CP044427|1|1|675730-675815|CRISPRCasFinder
GACGACGGCGCGACCACCGCCGGCGACGA	CACGACCACCGATGACGGCGCGACCACG
GACGACGGCGCGAGCACCGCCGGCGACGA

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP044427.1|WP_158060237.1|671312_672521_+|acetyl-CoA-C-acetyltransferase	unknown	unknown	gnl|CDD|180261
NZ_CP044427.1|WP_158060249.1|692211_692985_+|hypothetical-protein	unknown	unknown	unknown
NZ_CP044427.1|WP_158060233.1|666763_668437_+|3-hydroxyacyl-CoA-dehydrogenase	unknown	unknown	gnl|CDD|236211
NZ_CP044427.1|WP_158060235.1|669039_669555_-|methylmalonyl-CoA-epimerase	unknown	unknown	gnl|CDD|319912
NZ_CP044427.1|WP_158060251.1|694035_694827_+|electron-transfer-flavoprotein-subunit-beta/FixA-family-protein	unknown	unknown	gnl|CDD|238847
NZ_CP044427.1|WP_158060238.1|672535_673504_+|methylmalonyl-Co-A-mutase-associated-GTPase-MeaB	unknown	unknown	gnl|CDD|224617
NZ_CP044427.1|WP_158060234.1|668457_668778_+|hypothetical-protein	unknown	unknown	unknown
NZ_CP044427.1|WP_158060242.1|676884_677889_+|tetratricopeptide-repeat-protein	unknown	unknown	gnl|CDD|225660
NZ_CP044427.1|WP_158060250.1|693102_693906_+|hypothetical-protein	unknown	unknown	unknown
NZ_CP044427.1|WP_158060248.1|691853_692210_+|PadR-family-transcriptional-regulator	unknown	unknown	gnl|CDD|224609
NZ_CP044427.1|WP_158060240.1|674060_675317_-|divalent-metal-cation-transporter	unknown	unknown	gnl|CDD|224826
NZ_CP044427.1|WP_158060247.1|690802_691603_+|enoyl-CoA-hydratase/isomerase-family-protein	unknown	unknown	gnl|CDD|180270
NZ_CP044427.1|WP_158060245.1|685759_687847_-|DUF3416-domain-containing-protein	unknown	unknown	gnl|CDD|200482
NZ_CP044427.1|WP_158060246.1|687891_690129_-|glycogen-debranching-protein-GlgX	unknown	unknown	gnl|CDD|131155
NZ_CP044427.1|WP_158060243.1|677932_684010_-|alpha-D-glucose-phosphate-specific-phosphoglucomutase	unknown	unknown	gnl|CDD|235445
NZ_CP044427.1|WP_158060231.1|665599_665986_-|GtrA-family-protein	unknown	unknown	gnl|CDD|377229
NZ_CP044427.1|WP_158060244.1|684009_685746_-|maltose-alpha-D-glucosyltransferase	unknown	unknown	gnl|CDD|274140
NZ_CP044427.1|WP_158060239.1|673533_674049_+|GNAT-family-N-acetyltransferase	unknown	unknown	gnl|CDD|379228
NZ_CP044427.1|WP_158060236.1|669647_671189_+|amidohydrolase-family-protein	unknown	unknown	gnl|CDD|238625
NZ_CP044427.1|WP_158060232.1|666000_666696_-|endonuclease-NucS	unknown	unknown	gnl|CDD|235114

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
NZ_CP044427.1|WP_158060237.1|671312_672521_+|acetyl-CoA-C-acetyltransferase	gnl|CDD|180261	PRK05790, PRK05790, putative acyltransferase; Provisional.	0
NZ_CP044427.1|WP_158060251.1|694035_694827_+|electron-transfer-flavoprotein-subunit-beta/FixA-family-protein	gnl|CDD|238847	cd01714, ETF_beta, The electron transfer flavoprotein (ETF) serves as a specific electron acceptor for various mitochondrial dehydrogenases. ETF transfers electrons to the main respiratory chain via ETF-ubiquinone oxidoreductase. ETF is an heterodimer that consists of an alpha and a beta subunit which binds one molecule of FAD per dimer . A similar system also exists in some bacteria. The homologous pair of proteins (FixA/FixB) are essential for nitrogen fixation. The beta subunit protein is distantly related to and forms a heterodimer with the alpha subunit.	4.58241e-80
NZ_CP044427.1|WP_158060233.1|666763_668437_+|3-hydroxyacyl-CoA-dehydrogenase	gnl|CDD|236211	PRK08268, PRK08268, 3-hydroxy-acyl-CoA dehydrogenase; Validated.	2.39746e-112
NZ_CP044427.1|WP_158060238.1|672535_673504_+|methylmalonyl-Co-A-mutase-associated-GTPase-MeaB	gnl|CDD|224617	COG1703, ArgK, Putative periplasmic protein kinase ArgK and related GTPases of G3E family [Amino acid transport and metabolism].	1.51434e-113
NZ_CP044427.1|WP_158060235.1|669039_669555_-|methylmalonyl-CoA-epimerase	gnl|CDD|319912	cd07249, MMCE, Methylmalonyl-CoA epimerase (MMCE). MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) interconverts (2R)-methylmalonyl-CoA and (2S)-methylmalonyl-CoA. MMCE has been found in bacteria, archaea, and in animals. In eukaryotes, MMCE is an essential enzyme in a pathway that converts propionyl-CoA to succinyl-CoA, and is important in the breakdown of odd-chain length fatty acids, branched-chain amino acids, and other metabolites. In bacteria, MMCE participates in the reverse pathway for propionate fermentation, glyoxylate regeneration, and the biosynthesis of polyketide antibiotics. MMCE is closely related to glyoxalase I and type I extradiol dioxygenases.	6.27649e-52
NZ_CP044427.1|WP_158060242.1|676884_677889_+|tetratricopeptide-repeat-protein	gnl|CDD|225660	COG3118, COG3118, Thioredoxin domain-containing protein [Posttranslational modification, protein turnover, chaperones].	5.03701e-31
NZ_CP044427.1|WP_158060248.1|691853_692210_+|PadR-family-transcriptional-regulator	gnl|CDD|224609	COG1695, COG1695, Predicted transcriptional regulators [Transcription].	8.23405e-22
NZ_CP044427.1|WP_158060240.1|674060_675317_-|divalent-metal-cation-transporter	gnl|CDD|224826	COG1914, MntH, Mn2+ and Fe2+ transporters of the NRAMP family [Inorganic ion transport and metabolism].	6.012e-44
NZ_CP044427.1|WP_158060247.1|690802_691603_+|enoyl-CoA-hydratase/isomerase-family-protein	gnl|CDD|180270	PRK05809, PRK05809, short-chain-enoyl-CoA hydratase.	1.09042e-72
NZ_CP044427.1|WP_158060245.1|685759_687847_-|DUF3416-domain-containing-protein	gnl|CDD|200482	cd11344, AmyAc_GlgE_like, Alpha amylase catalytic domain found in GlgE-like proteins. GlgE is a (1,4)-a-D-glucan:phosphate a-D-maltosyltransferase, involved in a-glucan biosynthesis in bacteria. It is also an anti-tuberculosis drug target. GlgE isoform I from Streptomyces coelicolor has the same catalytic and very similar kinetic properties to GlgE from Mycobacterium tuberculosis. GlgE from Streptomyces coelicolor forms a homodimer with each subunit comprising five domains (A, B, C, N, and S) and 2 inserts. Domain A is a catalytic alpha-amylase-type domain that along with domain N, which has a beta-sandwich fold and forms the core of the dimer interface, binds cyclodextrins. Domain A, B, and the 2 inserts define a well conserved donor pocket that binds maltose. Cyclodextrins competitively inhibit the binding of maltooligosaccharides to the S. coelicolor enzyme, indicating that the hydrophobic patch overlaps with the acceptor binding site. This is not the case in M. tuberculosis GlgE because cyclodextrins do not inhibit this enzyme, despite acceptor length specificity being conserved. Domain C is hypothesized to help stabilize domain A and could be involved in substrate binding. Domain S is a helix bundle that is inserted within the N domain and it plays a role in the dimer interface and interacts directly with domain B. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.	0
NZ_CP044427.1|WP_158060246.1|687891_690129_-|glycogen-debranching-protein-GlgX	gnl|CDD|131155	TIGR02100, Glycogen_operon_protein_GlgX_homolog, glycogen debranching enzyme GlgX. This family consists of the GlgX protein from the E. coli glycogen operon and probable equivalogs from other prokaryotic species. GlgX is not required for glycogen biosynthesis, but instead acts as a debranching enzyme for glycogen catabolism. This model distinguishes GlgX from pullanases and other related proteins that also operate on alpha-1,6-glycosidic linkages. In the wide band between the trusted and noise cutoffs are functionally similar enzymes, mostly from plants, that act similarly but usually are termed isoamylase. [Energy metabolism, Biosynthesis and degradation of polysaccharides].	0
NZ_CP044427.1|WP_158060243.1|677932_684010_-|alpha-D-glucose-phosphate-specific-phosphoglucomutase	gnl|CDD|235445	PRK05402, PRK05402, 1,4-alpha-glucan branching protein GlgB.	0
NZ_CP044427.1|WP_158060231.1|665599_665986_-|GtrA-family-protein	gnl|CDD|377229	pfam04138, GtrA, GtrA-like protein. Members of this family are predicted to be integral membrane proteins with three or four transmembrane spans. They are involved in the synthesis of cell surface polysaccharides. The GtrA family are a subset of this family. GtrA is predicted to be an integral membrane protein with 4 transmembrane spans. It is involved is in O antigen modification by Shigella flexneri bacteriophage X (SfX), but does not determine the specificity of glucosylation. Its function remains unknown, but it may play a role in translocation of undecaprenyl phosphate linked glucose (UndP-Glc) across the cytoplasmic membrane. Another member of this family is a DTDP-glucose-4-keto-6-deoxy-D-glucose reductase, which catalyzes the conversion of dTDP-4-keto-6-deoxy-D-glucose to dTDP-D-fucose, which is involved in the biosynthesis of the serotype-specific polysaccharide antigen of Actinobacillus actinomycetemcomitans Y4 (serotype b). This family also includes the teichoic acid glycosylation protein, GtcA, which is a serotype-specific protein in some Listeria innocua and monocytogenes strains. Its exact function is not known, but it is essential for decoration of cell wall teichoic acids with glucose and galactose.	3.49535e-14
NZ_CP044427.1|WP_158060244.1|684009_685746_-|maltose-alpha-D-glucosyltransferase	gnl|CDD|274140	TIGR02456, Trehalose_synthase, trehalose synthase. Trehalose synthase interconverts maltose and alpha, alpha-trehalose by transglucosylation. This is one of at least three mechanisms for biosynthesis of trehalose, an important and widespread compatible solute. However, it is not driven by phosphate activation of sugars and its physiological role may tend toward trehalose degradation. This view is accentuated by numerous examples of fusion to a probable maltokinase domain. The sequence region described by this model is found both as the whole of a trehalose synthase and as the N-terminal region of a larger fusion protein that includes trehalose synthase activity. Several of these fused trehalose synthases have a domain homologous to proteins with maltokinase activity from Actinoplanes missouriensis and Streptomyces coelicolor (). [Energy metabolism, Biosynthesis and degradation of polysaccharides].	0
NZ_CP044427.1|WP_158060239.1|673533_674049_+|GNAT-family-N-acetyltransferase	gnl|CDD|379228	pfam13508, Acetyltransf_7, Acetyltransferase (GNAT) domain. This domain catalyzes N-acetyltransferase reactions.	7.68562e-13
NZ_CP044427.1|WP_158060236.1|669647_671189_+|amidohydrolase-family-protein	gnl|CDD|238625	cd01300, YtcJ_like, YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. The Arabidopsis homolog LAF3 has been identified as a factor required for photochrome A signalling.	1.34844e-85
NZ_CP044427.1|WP_158060232.1|666000_666696_-|endonuclease-NucS	gnl|CDD|235114	PRK03298, PRK03298, endonuclease NucS.	3.72465e-157

Protein sequences

>NZ_CP044427.1|WP_158060240.1|674060_675317_-|divalent-metal-cation-transporter
MSTTTSPAHAPGSRWAAVGPGLLMASAAIGASHLVASTQAGALFGWQLVGLILVANLLKYPFFRFGPQFTAESGLSLVEGYARKGRGYLIVFFILCIYSSVVSAAGVALLCTVILAYLLPASWGLGVPLLATLLMGITWALLVGGRYKALDTVTKVILVVLSLSTVVAVVMAASQGTVREPGFLDPSPWNLATLAFLVALIGWMPAPIEVSALNSLWIRAKAQDRTVRPQDIIFDFNLGFIVSTVLAVIFVALGVFVQYGSGEELQMAGGAYIPQLMSMYGAAIGTWAVPLMALIAFAAMFGTVITVVDGYARASAESLRLLRRRPDFSRREKNLWITGISLAALAIVLWMSAELADMLRYAMISAFVTAPVFAWLNFSLVRRGPRLSPALRWLSWAGLVFLVGFTLLFLLTLVGAVG
>NZ_CP044427.1|WP_158060239.1|673533_674049_+|GNAT-family-N-acetyltransferase
MTNVEDYLIRRPTRSDTVPFSTLHVHVWRSAYRGLMEDRVLDALEPSSFAATWMAVGSGYDEGTIPDDGRGFWVATLHEEPVGFIFFGPGRDEDRPVQRQLYSLNVHPEHHGLGIAQRLMDEGLGPGEAYLWVARGNGRAIRFYERNGFTLDRTESTGRHDGVTELRMVRH
>NZ_CP044427.1|WP_158060238.1|672535_673504_+|methylmalonyl-Co-A-mutase-associated-GTPase-MeaB
MRSRRSVDVPALVEQARAGSSRALGRLITLVENAHPALREVMALLAPHTGQARIIGLTGSPGVGKSTSTSMLVRALRQRDLRVGVLAVDPSSPFSGGALLGDRIRLSEHSLDPGVYIRSMASRGHLGGLAWSTPQALRVMDAAGCEVILVETVGVGQSEVEIAGLADTTLVLLAPGMGDGVQAAKAGILEVGDVFVVNKADRDGADTTVRELRQMISLGDRTEPGLWRPPVLKAVADRHEGGEEVVEALDRHLAWMQEHDELDRRRRTRAAREVEAIALQRLRARMGEVLGDGALAEATEEVLAGRLDPYAAADQVVSRVAG
>NZ_CP044427.1|WP_158060237.1|671312_672521_+|acetyl-CoA-C-acetyltransferase
MSDTTSVLVAGARTPMGRLLGSLAGFSGADLGGIAIKGALEKAGISGDQVDYVIMGQVLTAGAGQIPARQAAVAGGIPMDVPALTINKVCLSGINAIALADQLVRSGEADIVVAGGQESMSQAPHLLPRSREGYKYGDVTARDHMAYDGLWDAFTDQAMGNLTEAANESDSQHEFSREEQDAYSARSHQLAAQAWEKGLFEEAVVPVPIPQRKGDPIEFKTDEGIRPDTTVESLGKLRPAFRKDGTITAGSASQISDGACAVVVMSKAKAEELGLAWLAEIGAHGMVAGPDSTLQTQPSRAIVAACKKEGIEPTDLDLVELNEAFAVVALASTQELGLDPEKVNVNGGAIAMGHPIGMSGARIVLHLALELQRRGGGTGAAALCGGGGQGDALIVRVPQSQG
>NZ_CP044427.1|WP_158060236.1|669647_671189_+|amidohydrolase-family-protein
MPDLLVRDVRLVALDAPLPEQAPVPGEPVDVLVRDGAIIAVGEGVRERVEALGIPVLDGKGRHAVPGLWDMHVHMVQWGLSRTRLDTSGTSGPQEVLGLVAARLAGGLDTPTGMLVGYGHRTGSWDERPTVAALDAVTGEVPVALIAGDAHHGWLNTAALRLVGGPMVTGVVSEGAWFPLYDRLQRLQGAAQEAEFGVAQAVAAAHARGIVGIVDLEFGQPWLQWRARTAGETPPLRARTAVYPEGLDAVIAAGVRTGDPIRATDGLVTMGPLKVITDGSLNTRTAWCCQPYADAAEPDLAHGAPNLPADELVELLQRAHDAGLEAALHAIGDAAVSTVLDAFTATGAGGSVEHAQLVDLTDLQRWSRLPVRASVQPAHLLDDRTVTEQCWPERTHRTFVLRGFLDAGIELAFGSDAPVSPLDPWLAMAAAVHRGAEGEESWHPEQQISPREALAASVDGRRIRAGAPGDLVLLDIDPLGADGPQSTSAEQAARLRKMTVSATVLDGQVVHEA
>NZ_CP044427.1|WP_158060235.1|669039_669555_-|methylmalonyl-CoA-epimerase
MNTTPTGGSVDRPEGRHRDRGPADDLSPFLLCVDHVGLAVPDLDAAIAFHCEVLGHRLVHQETNTEQGVREAMIAVGPPESEGGNATTMLQLLAPTGPESTIAKFLDRNGPGLQQLAYRVSDIEAASALLRERGLRLLYDEPRRGTAGSRINFIHPKDAGGVLVELVEPAG
>NZ_CP044427.1|WP_158060234.1|668457_668778_+|hypothetical-protein
MGRSNRPRRHGRPRKGVAGGGLPPSVQRGGVGEVRYAGQLWLVRQVRPNDSGRSYLCPGCQQEVSAGTAHTVVWPAESMRELENRRHWHTVCWSARERRRPGGSFA
>NZ_CP044427.1|WP_158060233.1|666763_668437_+|3-hydroxyacyl-CoA-dehydrogenase
MREITTVGVIGLGTMGAGIVEVFARGGLQVIGVETTQDYADRGRGILQASTDRAVAKGKLDEDGQAHILDRITISTDLGDLKDADLVVEAVPEVLSLKHEVFAKLDDIIAEDAVLASNTSSLSITQIAAGTRHPDRVVGLHFFNPAPILKLVEVITTVRTDTALIDAVVELSERIGKKPVVVGDRAGFVANYLLFGYFVSALRMLEQGHVSREDLDTAMRVGAGLPMGPCTLMDLVGLDVCHHIGDVIYSHTRSPMHAPSPMLERMVTAGLLGRKSGRGFYTYARAGSGQVVEDEQTPAAPEGFGLSAVGVVGGGEVADELASRLQEAGYAVTRVTDPGSDEELAGLADVGLVIEAAAAPEAPAEDELEEEGLWVEEAGEDLWEQLGAAVGPDTVLATVNPDAAVVVGALSGRPEKAAVLSIHTPTHHGQVVEIGRSSATDDSTVALLREVVTRIGAEPVVCKDRAGLVVDALLMPHLGDAVRMLDEGYASVQDIDTALQYGLGYPAGPFAMVDHLGADEVLAVLEELRSAGGLPADAVAPSPLLVEHVLLDRPFTG
>NZ_CP044427.1|WP_158060232.1|666000_666696_-|endonuclease-NucS
MRVVIARCSVDYQGALQAHLPLATRLLMVKADGSVLIHSDGGSYKPLNWMAPPCTMAELEPDDLERQEGVQSIWLVRHGKREDTLRIRLHDVLSDTSHDLGVDPGLVKDGVESQLQALLAEHVQTLGLGWTLLRREYHTAIGPVDLLCRDRDGRTVAVEIKRRGEIDGVEQLTRYLELLNRDPHLAPVAGVFAAQVIKPQAKVLATDRGIRCVTLDYEALRGLDDAESRLF
>NZ_CP044427.1|WP_158060231.1|665599_665986_-|GtrA-family-protein
MSALARFLVVGVANTLVYYLLYRLLLLGLAYLPAHLLAYGVGIVFSFFANSLYTFRVRPTWRRFLIFPSTTLVNFLVVTLGSVLLVERGWVDERWATLLMTVAAVPVTFLLTRLVLTSRRGGRAESAA
>NZ_CP044427.1|WP_158060242.1|676884_677889_+|tetratricopeptide-repeat-protein
MTQQPFSPAALRGAVDLSGLGARPRGGTQQPPSAASAQGSGPAETGAVPGRQGALVTMDDSSFESVVTASLTAPVVLVLWSPQAPESAQHLRELVDAARSSGGRFQVAAADLAASPGIMQALTPLLQQAFGQVSSLPVVIGLLGGQPMPFYVGVQPMAQVDQLLTKFLEAAVANGVTGRVEVGAADAPVDEAGEEGELPPLHQAAYDAIDRGDWAAAITAYEQALEQDPSDEMARLGLGQVRLLERTSTLDLAAVRARAAADPTDVSAQIEAADVDVVGGHVEDGFARLVDTVRRTSDKDRDAARTHLLSLFEVVGPQDPRVQKARSALMSALF
>NZ_CP044427.1|WP_158060243.1|677932_684010_-|alpha-D-glucose-phosphate-specific-phosphoglucomutase
MPTLTPPFEEFLPDWVARQRWFRGKTAGGPPRLRRIGSVRWEDPLGEVGLEDHIVIDESGPEPVVYQIPLSYRAEAVAFMSAGLVGTAEHSELGTRYVYDATHDPVFAQVLLQHMYAGTDVPSAHARRLAAHDTVPALRTAQVLTGEQSNTSIMVQLHREGDPVIIKVFRVLADGDNPDVVVQAAISDTGSRQVPSPLGYVEGRWSTDDGEARGHLVFAQEFLPDTRDAWQGALEACRDEADFTAAAHTLGAATAAVHRALREAFGTTEPDDERRRTLVTQMRRRAEAAYADAPELAQVAAQVEAVYARLESQPLPTLQRIHGDYHLGQVLQVPDRGWVLLDFEGEPLRPLPERTAPDLTLRDVAGMLRSFDYAAASVSLTGERAGWARAARQAFVEGYAEESGEDVSAQQDVLDALELDKALYEASYEARNRPDWLAIPVAAVHRLVAGAVQVAPGPDSGAEHTAARETPTDPPTGSAAAPLSDAAPVETSSTPGAQSTSQDDADDAVPTEDSDDLGATEQVQTQQTQQTHETQGTEEASVAVDERTGDEAQIPDASIPDDDYGSSLIEMEHVHQTVAHPGDRALASGGVPHAPVAPPRGAFDLELPPLAPVGHRPGESAGTAAAGTEGRTLTSGELRALSASGWSGVVDLDPAASRDRAWQDAIGSPDVVTGRTVGGAASGDSADEDGGASDVRAGTKVTRRPLEGPSEPSAPHTRPLDLEEATDVVHGLHRNPHALLGAHPHEGHVTIRTLQPEAEAVEVVLGQGRTVSMTHETGGIWVAVIPEPEVPAYRLQVAGSEGARLVDEAYRHTSSLGETDLHLIGEGRHEELWRALGSHVMTVRDELGPVTGTRFAVWAPHALAVHVIGDFNGWNGNTHALRAHDSVGVWELFVPGVREGAHYKYDITGPDGVRRAKADPMARASEVPPFNNSVVTVSRHRWSDGDAAWMRRRSENNIHHGPMSIYEMHLGSWRQGLSYEQLADELVDYVADLGFTHVEFMPVMQHPYGGSWGYHVTGYFAADSRFGHEDGLRYLIDRLHCAGIGVILDWVPGHFATDPWALARFDGTPIYEHPDPRKGWHSEWGSYIFDFGHPQVRNFLVANATYWLEEFHADGLRVDGVASMLYLDYSRQPGQWVPNRYGGRENLEAVALLQETNATAYRRSPGVVMIAEESTSWPGVTAPVDEGGLGFGFKWNMGWMHDTLDYLGQSPYARAHHHHTMTFSMVYAFGEKYILPISHDEVVHGKGSLVRKMAGDAWQKFATMRAFLAYQWSHPGKQLLFMGTEFGQVREWADQASLSWELTQRPEHAGVLALVRDLNRLYHELPALWQIDHHEDGFRWLDANDASRNLYSYLRWGDEGPDGLRPAVVVLVNFSGVTQHQVHVGLPYGGRWHEALNTDAEVYGGSGQGNMGYVQAYDHPHQHQPFSALVTVPPMGAIYLVPDPEPEAATVDEEGALEPGSAEGAASEDSPTRHARAGQPARSEDLVDVAQLLAAYTEIVPDPDDVDQQVAFGTSGHRGSALDGAFNEQHILATTQAICDYRRDQGTDGPLFLGRDTHALSEPAWRSALEVLIGNGVDVHIDSGEGYTPTPAVSRAILQHNRETPDAQGEADGIVVTPSHNPPRDGGFKYNPPHGGPADTDATSWIADRANELLRAGLDEVQRVPFEQAHTRAAGYDFMGEYVRALPRVIDLDAIREAGVRIGADPLGGAAVDYWGAIAQEHGLDLTVVNPDVDPTWRFMTLDWDGKIRMDCSSPDAMASLIEVMRGEQGGQPRFDVATGNDADADRHGIVTPDAGLMNPNHYLAVAIDYLYGGARPDWPQDIAIGKTLVSSSMIDKVAQSLGQQLIEVPVGFKWFVPGLLDGSVGFGGEESAGASFLCRDGSVWSTDKDGIILALLAAEIIARTGRTPSQRYAELVAEHGDPAYARVDAPAGREQKGRLKKLSARDISATELAGEQITAVLTEAPGNDAAIGGVKVATEHAWFAARPSGTEDVYKIYAESFRGPEHLAQVQAEAQQVVDQALRG
>NZ_CP044427.1|WP_158060244.1|684009_685746_-|maltose-alpha-D-glucosyltransferase
MRGLNLHQPGLKHDPDWFRKAVFYEVLVRAFDDSDGSGSGDFTGLINRLDYLQWLGVDCLWIPPFYASPLRDGGYDVADYTAVLPEFGTLPDFRELISQAHERGIRIITDLVMNHTSDQHAWFQASRSDPEGPYGHFYVWSDTDEKYADARIIFVDTETSNWTFDPVRRQFFWHRFFSHQPDLNFENPAVQEAMFDVVRFWMDLGIDGFRLDAVPYLFEEEGTNCENLPRTHEFLAELRAMVDAEYPGRVLLAEANQMPAEVVDYYGTEEAPECHMCFHFPVMPRLFYALREEKAEPIIRVMDETPPIPPGTQWGTFLRNHDELTLEMVSAEERAAMYGWYAPDPRMRANIGIRRRLAPLLDNSRSELELINALLLSLPGSPCLYYGDEIGMGDNIWLTDRDAVRTPMQWTPDRNAGFSTADPGKLYLPVVGSLVYHYNNVNVEAQMASGASLLHWTRGMLHVRSTHEVFGVGDYVPCEADNDTVLAFCRMMPETEQSEQREGVPAVLCINNLSSRPQAATVVLPEQFKGAEVQDLFGGQGFVDVTPEGTITLTLGSRGFYWLGLTPSTPVTPATEES
>NZ_CP044427.1|WP_158060245.1|685759_687847_-|DUF3416-domain-containing-protein
MTEHSTTSAQPASSPPAPDRSVLALLGQEPIDRIPVLDVEPIVDGGRRPTKSVVGELFTLSATVFREGHDAVNATAVLVDPDGQERHVPMVSTNPGLSHWRTVVHADREGVWGFRVEGWSDPYGTWEHDGTIKVRAGVDVDLMLEEGARVLERAVEEVDHTDEDRTVLKEAIDLLRRSSLPAEERLQAGIDPRVREVMASSPLRDAVSASPTYTWWVERPLALTGAWYEIFPRSEGATHDPETGLWTTGTFATASERLPGIAEMGFDVVYLTPVHPIGTTNRKGRNNSLTTEEHDPGSPYAIGSPDGGHDALHPELGDWEDFDAFVARAEDEGLHVALDLALQASPDHPWASEHPEFFTTRADGTIAYAENPPKKYQDIYPLNFDNAPDSIYAEVRRVVQVWIDHGVKIFRVDNPHTKPVEFWQWLIADVAVDHPEVIWLSEAFTKPMMMRTLAKVGFQQSYTYYAWRNTAEELREYVTELATETAPYMRPSFWPTTHDILTPYMQVGGVTAHLVRSTLAATLVPTYGIYAGFEHVENVPRPGAEEHIDNEKYEYKDRRWGEAVPGREDLTGWLTLLNRIRREHPSLHWLRNITFHDADNENLLVFSKHGGGADDGSAQDTIIVVANLDPFGIHGSRLHLDLSALGLGLGEQPGQRFRAHDLVTGADWIWDETPYVELGPGYGREPVHIVHATTA
>NZ_CP044427.1|WP_158060246.1|687891_690129_-|glycogen-debranching-protein-GlgX
MPPLSRPRRSTDRPPPLGLTRTEAGPELAVLARHATSVEVEIFGPDGAHAVTVPLTRNAYGIWWDSVPQLTPGTRYGLRVHGPWAPDQGHRHNPAKLLLDPYAGAVEGEVSWVPEVYGHRVDRHRGGGHLAGDPVVRDERDSAPYVPRSVVVDHDGFDWAGDILPRVPWTDTVIYEAHVRGLTMRHPDVPPELRGTYAGLAHPAVVEHLVQLGVTTVELLPVHAFTSEPALVRRGLSNYWGYNTLGFFAPHARYAAAQDPQGVVDEVKGAVRALHAAGLEVILDVVYNHTAEQGSGEGPTLSWRGLDNHSYYRLDARGRDVDVTGCGNTVDLREPMVARMVLDSLRHWVERYHVDGFRFDLAPALARGRDDAYDRDHPFHVALQTDPVLSRVKLIAEPWDVGVHGWRTGQFPGPMAEWNDRYRDGVRSFWLSDVGRALNGAPGQGIRDLATRLAGSADLFSHDDRGPTASINYAASHDGFTLADLTAYEQRHNYANGEDNRDGHGDNRSFNHGVEGSSTDPVVLTSRERSVRNLLATVLLSTGVPMLLGGDELGRTQEGNNNAYCQDNPITWVDWQLEPWQRELLADARTLTALRRELAVLRPPEFPLHQAVPGRTRLRWYDEHGQQVNEQGWQDPRRRTVVAVYDSLHQDFDGLGGSDATGTPPQVVALVLHAGPDRIGVTLPVLERVLDWTVRWSSERPVSEDGKEGQAPDPQQPLREGQTRSTGATSFTVLVGRVDPATPGR
>NZ_CP044427.1|WP_158060247.1|690802_691603_+|enoyl-CoA-hydratase/isomerase-family-protein
MSRTVQTASEFVRVEVDSGIATIRIDRPKMNPLSIEVQDALAEAARIVTADDEVAAVVIYGGEKVFAAGADIKEMQTMGYTDMVQRASIIQDCFTQVARIPKPVIAAIEGYALGAGNELAMCADFRVAAADAKLGQPEILLGVIPGAGGTQRLARLVGVSKAKDLVYTGRMIDAAEAQEIGLVDKVAEPGEAYATAVEMAQRYVHGPAFALRAAKETIDRGLDGDLATGLAIEAMQFAGVFATQDREIGMTSFVKEGPGKATFEGR
>NZ_CP044427.1|WP_158060248.1|691853_692210_+|PadR-family-transcriptional-regulator
MNTEQWPSEWLRGVLGVCVLRILLDGPSYGYAITQRLAEAGLGTVKGGTLYPLLGRLEEAGHVEVDWRPGEGGPGRKFYALTEQGRAEAGEQSARWVDFTTTTRSLTDEALAQTTGRN
>NZ_CP044427.1|WP_158060249.1|692211_692985_+|hypothetical-protein
MNSKATRATGPMVERIFGDPGAIAPSVEKAWRDDFIIELRLRSLPGEAIGDALMTVESHVAESGEKAQDAFGEAKTYAREVAAATGTAARGWSVSAATVASTLLGLAGMLLSVRAFGSWLDGEPIGVTTGELVGLAVLILLASTLFFTATLRMLVEHRWLALPVPALLVGGLVGLHIALDEPLFELPALAVGVAGVLSLTASVLLSWVEEPAGLDQVTAPGQAPTVTTKSRMAAVLIFPLMTLGLFIFTWVLHLIVT
>NZ_CP044427.1|WP_158060250.1|693102_693906_+|hypothetical-protein
MNSIAKRPTEGDPRAVTETHSRTTDHLRLAPSVEPAWVEDFVLEQRLLGVPGDRIGDALALVQSHVAESGESVHEAFGDPVAYAREAASTRRVDDDRDLSWILGSGLGLAGMLLTLFGVQAWIDGDGRLALTVGHLVALGLVVVAFALLHLASEPFLRFVLRRPWSTLGLFVLHFAAMVAAFVFLRTPVAHVPAGATVAVGVTTLALGTLLEWRSRTAGQLEDPILGPGEGRPARRRLDWFGGLTLLMFPVLTVAMVGFSLLVARLS
>NZ_CP044427.1|WP_158060251.1|694035_694827_+|electron-transfer-flavoprotein-subunit-beta/FixA-family-protein
MNIVVCVKYVPDAQADRTFKTDHTTDRETVDGLLSELDEYAVEEALKIVQAGEGEITVLTMGPDDAVAAVKKGLQMGADKGVHVNDVAIAGSDAVATSLVLAKAIEKIGVEGGGVDLVLTGLGSTDGAMSVLPAMLAERLGMPQVTWASELAVEGGMARITRHNEAVTETVEANLPAVVSVTDQINDPRYPSFKGIMAAKKKPVEEWSLADLGVDPSEVGLGASWTSVVSAEARPPRQAGELVTDEGDGGAKLVEFLASRRFA

Crispr_ID: NZ_CP044427_2

• CRISPR_ID: NZ_CP044427_2
• CRISPR_location: 736103-736194
• CRISPR_type: Orphan
• Repeat_type: NA
• Spacer_info: 1 spacers

Consensus repeat of NZ_CP044427_2

Consensus_repeat	Method
CCGCGACCCCTGCGGCGTCACCGCAG	CRISPRCasFinder

spacers of NZ_CP044427_2

>2.1|736129|40|NZ_CP044427|CRISPRCasFinder
CCTGCAGTTCGGGGCAGGCCCCCGCGGCGAGGCCGTCCCT

CRISPR arrays and Neighbor proteins around NZ_CP044427_2

CRISPR arrays

The CRISPR arrays of NZ_CP044427_2

>merge|NZ_CP044427|2|736103-736194|CRISPRCasFinder
CCGCGACCCCTGCGGCGTCACCGCAGCCTGCAGTTCGGGGCAGGCCCCCGCGGCGAGGCCGTCCCTCCGCGACCCCTGCGGCGTCAGCGCAG

>NZ_CP044427|2|2|736103-736194|CRISPRCasFinder
CCGCGACCCCTGCGGCGTCACCGCAG	CCTGCAGTTCGGGGCAGGCCCCCGCGGCGAGGCCGTCCCT
CCGCGACCCCTGCGGCGTCAGCGCAG

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP044427.1|WP_158060287.1|738706_739909_-|glycine-C-acetyltransferase	unknown	unknown	gnl|CDD|235893
NZ_CP044427.1|WP_158060288.1|739919_740969_-|L-threonine-3-dehydrogenase	unknown	unknown	gnl|CDD|180054
NZ_CP044427.1|WP_158062608.1|743964_746781_+|FAD-binding-oxidoreductase	unknown	unknown	gnl|CDD|223354
NZ_CP044427.1|WP_158060283.1|734005_734833_-|SGNH/GDSL-hydrolase-family-protein	unknown	unknown	gnl|CDD|238861
NZ_CP044427.1|WP_158060276.1|727126_727771_-|helix-turn-helix-transcriptional-regulator	unknown	unknown	gnl|CDD|378968
NZ_CP044427.1|WP_158060277.1|727837_729082_+|MFS-transporter	unknown	unknown	gnl|CDD|340863
NZ_CP044427.1|WP_158060290.1|746855_747509_-|oligoribonuclease	unknown	unknown	gnl|CDD|235429
NZ_CP044427.1|WP_158060286.1|736388_737717_+|hypothetical-protein	unknown	unknown	gnl|CDD|236641
NZ_CP044427.1|WP_158060291.1|747554_748757_+|PrsW-family-intramembrane-metalloprotease	unknown	unknown	gnl|CDD|379143
NZ_CP044427.1|WP_158060289.1|743025_743505_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP044427.1|WP_158062605.1|737773_738682_+|zinc-ABC-transporter-substrate-binding-protein	unknown	unknown	gnl|CDD|376518
NZ_CP044427.1|WP_158060278.1|729085_729367_-|Rho-termination-factor	unknown	unknown	gnl|CDD|377850
NZ_CP044427.1|WP_158060279.1|729441_730233_+|ribonuclease-PH	unknown	unknown	gnl|CDD|178914
NZ_CP044427.1|WP_158062607.1|741887_743006_+|YihY/virulence-factor-BrkB-family-protein	unknown	unknown	gnl|CDD|224214
NZ_CP044427.1|WP_158060285.1|735567_735867_+|DUF3618-domain-containing-protein	unknown	unknown	gnl|CDD|378834
NZ_CP044427.1|WP_158060282.1|733138_734002_+|PhzF-family-phenazine-biosynthesis-protein	unknown	unknown	gnl|CDD|223461
NZ_CP044427.1|WP_158060281.1|732163_733102_+|homoserine-kinase	unknown	unknown	gnl|CDD|234920
NZ_CP044427.1|WP_158062606.1|741131_741653_+|AAA-family-ATPase	unknown	unknown	gnl|CDD|235825
NZ_CP044427.1|WP_158060284.1|735004_735481_-|thioredoxin-dependent-thiol-peroxidase	unknown	unknown	gnl|CDD|224146
NZ_CP044427.1|WP_158060280.1|730226_730937_+|non-canonical-purine-NTP-pyrophosphatase	unknown	unknown	gnl|CDD|234648

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
NZ_CP044427.1|WP_158060287.1|738706_739909_-|glycine-C-acetyltransferase	gnl|CDD|235893	PRK06939, PRK06939, 2-amino-3-ketobutyrate coenzyme A ligase; Provisional.	0
NZ_CP044427.1|WP_158060288.1|739919_740969_-|L-threonine-3-dehydrogenase	gnl|CDD|180054	PRK05396, tdh, L-threonine 3-dehydrogenase; Validated.	0
NZ_CP044427.1|WP_158062608.1|743964_746781_+|FAD-binding-oxidoreductase	gnl|CDD|223354	COG0277, GlcD, FAD/FMN-containing dehydrogenases [Energy production and conversion].	3.46841e-70
NZ_CP044427.1|WP_158060283.1|734005_734833_-|SGNH/GDSL-hydrolase-family-protein	gnl|CDD|238861	cd01823, SEST_like, SEST_like. A family of secreted SGNH-hydrolases similar to Streptomyces scabies esterase (SEST), a causal agent of the potato scab disease, which hydrolyzes a specific ester bond in suberin, a plant lipid. The tertiary fold of this enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles two of the three components of typical Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxylic acid.	4.56018e-50
NZ_CP044427.1|WP_158060276.1|727126_727771_-|helix-turn-helix-transcriptional-regulator	gnl|CDD|378968	pfam12840, HTH_20, Helix-turn-helix domain. This domain represents a DNA-binding Helix-turn-helix domain found in transcriptional regulatory proteins.	8.03272e-10
NZ_CP044427.1|WP_158060277.1|727837_729082_+|MFS-transporter	gnl|CDD|340863	cd06173, MFS_MefA_like, Macrolide efflux protein A and similar proteins of the Major Facilitator Superfamily of transporters. This family is composed of Streptococcus pyogenes macrolide efflux protein A (MefA) and similar transporters, many of which remain uncharacterized. Some members may be multidrug resistance (MDR) transporters, which are drug/H+ antiporters (DHAs) that mediate the efflux of a variety of drugs and toxic compounds, conferring resistance to these compounds. MefA confers resistance to 14-membered macrolides including erythromycin and to 15-membered macrolides. It functions as an efflux pump to regulate intracellular macrolide levels. The MefA-like family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	1.4355e-36
NZ_CP044427.1|WP_158060290.1|746855_747509_-|oligoribonuclease	gnl|CDD|235429	PRK05359, PRK05359, oligoribonuclease; Provisional.	4.00275e-109
NZ_CP044427.1|WP_158060286.1|736388_737717_+|hypothetical-protein	gnl|CDD|236641	PRK10019, PRK10019, nickel/cobalt efflux transporter RcnA.	0.00171335
NZ_CP044427.1|WP_158060291.1|747554_748757_+|PrsW-family-intramembrane-metalloprotease	gnl|CDD|379143	pfam13367, PrsW-protease, Protease prsW family. This is a family of putative peptidases, possibly belonging to the MEROPS M79 family. PrsW, appears to be a member of a widespread family of membrane proteins that includes at least one previously known protease. PrsW appears to be responsible for Site-1 cleavage of the RsiW anti-sigma factor, the cognate anti-sigma factor, and it senses antimicrobial peptides that damage the cell membrane and other agents that cause cell envelope stress, The three acidic residues, E75, E76 and E95 in Aflv_1074, appear to be crucial since their mutation to alanine renders the protein inactive. Based on predictions of the bioinformatics programme TMHMM it is likely that these residues are located on the extracytoplasmic face of PrsW placing them in a position to act as a sensor for cell envelope stress.	4.17515e-45
NZ_CP044427.1|WP_158062605.1|737773_738682_+|zinc-ABC-transporter-substrate-binding-protein	gnl|CDD|376518	pfam01297, ZnuA, Zinc-uptake complex component A periplasmic. ZnuA includes periplasmic solute binding proteins such as TroA that interacts with an ATP-binding cassette transport system in Treponema pallidum. ZnuA is part of the bacterial zinc-uptake complex ZnuABC, whose components are the following families, ZinT, pfam09223, pfam00950, pfam00005, all of which are regulated by the transcription-regulator family FUR, pfam01475. ZinT acts as a Zn2+-buffering protein that delivers Zn2+ to ZnuA (TroA), a high-affinity zinc-uptake protein. In Gram-negative bacteria the ZnuABC transporter system ensures an adequate import of zinc in Zn2+-poor environments, such as those encountered by pathogens within the infected host.	7.70591e-90
NZ_CP044427.1|WP_158060278.1|729085_729367_-|Rho-termination-factor	gnl|CDD|377850	pfam07498, Rho_N, Rho termination factor, N-terminal domain. The Rho termination factor disengages newly transcribed RNA from its DNA template at certain, specific transcripts. It it thought that two copies of Rho bind to RNA and that Rho functions as a hexamer of protomers. This domain is found to the N-terminus of the RNA binding domain (pfam07497).	0.000314946
NZ_CP044427.1|WP_158060279.1|729441_730233_+|ribonuclease-PH	gnl|CDD|178914	PRK00173, rph, ribonuclease PH; Reviewed.	1.72553e-164
NZ_CP044427.1|WP_158062607.1|741887_743006_+|YihY/virulence-factor-BrkB-family-protein	gnl|CDD|224214	COG1295, Rbn, Ribonuclease BN family enzyme [Replication, recombination, and repair].	1.36256e-56
NZ_CP044427.1|WP_158060285.1|735567_735867_+|DUF3618-domain-containing-protein	gnl|CDD|378834	pfam12277, DUF3618, Protein of unknown function (DUF3618). This domain family is found in bacteria, and is approximately 50 amino acids in length.	1.44985e-08
NZ_CP044427.1|WP_158060282.1|733138_734002_+|PhzF-family-phenazine-biosynthesis-protein	gnl|CDD|223461	COG0384, COG0384, Predicted epimerase, PhzC/PhzF homolog [General function prediction only].	1.02621e-71
NZ_CP044427.1|WP_158060281.1|732163_733102_+|homoserine-kinase	gnl|CDD|234920	PRK01212, PRK01212, homoserine kinase; Provisional.	5.82256e-61
NZ_CP044427.1|WP_158062606.1|741131_741653_+|AAA-family-ATPase	gnl|CDD|235825	PRK06547, PRK06547, hypothetical protein; Provisional.	2.3243e-37
NZ_CP044427.1|WP_158060284.1|735004_735481_-|thioredoxin-dependent-thiol-peroxidase	gnl|CDD|224146	COG1225, Bcp, Peroxiredoxin [Posttranslational modification, protein turnover, chaperones].	1.80765e-70
NZ_CP044427.1|WP_158060280.1|730226_730937_+|non-canonical-purine-NTP-pyrophosphatase	gnl|CDD|234648	PRK00120, PRK00120, dITP/XTP pyrophosphatase; Reviewed.	7.07876e-80

Protein sequences

>NZ_CP044427.1|WP_158060285.1|735567_735867_+|DUF3618-domain-containing-protein
MADKQPDRSMQEIEADIAATRSRMARTVDELAYRVNPQTLKANAIARVQGEIQQVVHRAQDKVVDPTGEPRYENIAKALGGVAATALTLGTLRRLFNRG
>NZ_CP044427.1|WP_158060284.1|735004_735481_-|thioredoxin-dependent-thiol-peroxidase
MSRLEPGQPAPGWTLTDAAGRTVSLSDFAGRKLIIYVYPAAMTPGCTTQACDFRDNEAVFQQHGYAVVGVSPDSSEKLARFAEKELLPFPLLSDPDKEMLTAYGAYGEKKNYGRTVVGVIRSTFVIDEEGVLELAKYNVRATGHVASLAKQLGIALPA
>NZ_CP044427.1|WP_158060283.1|734005_734833_-|SGNH/GDSL-hydrolase-family-protein
MNTPHPGRRHLLIVAGCGLALAAASAFPANGSPQRFVYDALGDSFASGSGAAAAQDACGRNDLAYPHVLDGRMRIALDDFAACGGATIPSMLATQMAALGTETDLVTVSIGGNDIGWSAAVTACLVGTEAQCAQSIQATTQSIEQQLPADLGAAYTQIRVAAPDAHVVVTGYPRLFSPEHGDFVPFPQLPGMISVAEQRLLNDGADLLNAVIADVAADHGFQFVDVTSRFTGHGVNAGDAWLTGLDHPVPLHPTAEGQHAYGVALRSQINPTSLR
>NZ_CP044427.1|WP_158060282.1|733138_734002_+|PhzF-family-phenazine-biosynthesis-protein
MTTSASPATLRFSQVDVFSASGLHGNPVAVVHDADGLAEETMGAFARWTNLSETTFLLRPTDPAADYRVRIFTTGGELPFAGHPTLGSAHAWLEAGGVPRNPDRVVQECGVGLVPVRRGERLAFAAPPLLRSGPVDAGQAAVVRQALGLHEEQVLQMGWVDNGPGWVGIELVSAQEVLAVEPVLHLSGQLKAGLVGRWPDPEAAGKDVEVRAFYGDGVAFMEDPVTGSLNAGLAQWLVGQGRLPDRYVAGQGSRLRRDGRVYVVSEAGEVWVGGDATVTVRGQVLLR
>NZ_CP044427.1|WP_158060281.1|732163_733102_+|homoserine-kinase
MTGALRAGLSVAVRVPASTANLGPGFDTVGLALGLHDEYAVQVLPEPGHLEVLLEGEGAGQLPTDEGHLVAGRLREALEAGGIGWLGGYGLRLTCRNTIPMSAGLGSSAAAIVGGLGLGFALVRDGALTEADLGLVNTHAGVTEGHPDNSSASVYGGLTVSWMPSPQVVRTARPVLHPDVVPVVLMPAGHRLDTALARSVLGPQVARVDAIRQAGRAALLVHALTSEPTLLLDATEDWMHQEQRREVYPVTMGAVETLRALGHAAVVSGAGPTVLCLTTRELKDVVVAEARSWGREWKVAAPGVPGIGLQLR
>NZ_CP044427.1|WP_158060280.1|730226_730937_+|non-canonical-purine-NTP-pyrophosphatase
MVSERRLVLATRNGHKVGELREILADVLRTTGLELVGLDAFAGLEDVVESGVTFAENALLKARYAAASTGLPALADDSGLAVDVLGGAPGVFSARWAGPLAQATGVAKDEANNRLLLAQLADVPDEYRGAGFVCAAALVVPGRGGVEGEAGRAAGSGGAGGGVGGGVAATEVVREGTCRGVLAREPRGANGFGYDPLLVRPDGRTLAEHTAGEKNAISHRGAAFRELAGDIERLLG
>NZ_CP044427.1|WP_158060279.1|729441_730233_+|ribonuclease-PH
MTRHDGRTPDQLRDIRFTRNWLDHAEGSVLVEFGRTRVLCAASFTQGVPRWRKGSGKGWTTAEYAMLPRATHTRSDRESVRGRIGGRTHEISRLIGRSLRAVVDLQALGENTIQIDCDVLQADGGTRTAAITGAYVALVDAIENARAQGLIPKGKEPMTGSVCAVSVGVVAGEPVLDLDYVEDVDADTDMNVVMTGDGRFVEIQGTAEGVPFDRELLDALLDLAAEGCAELTARQAMAFGGDDMGGADSHEAGAAIDLGPPTW
>NZ_CP044427.1|WP_158060278.1|729085_729367_-|Rho-termination-factor
MAQKKQEEDPGPSVKDPEVYEALRDDGASKEKAARIANAAANSSRSEVGERGGEAGSYEDRTVEDLRKRAAELDIEGRSSMTKGELIDALRNH
>NZ_CP044427.1|WP_158060277.1|727837_729082_+|MFS-transporter
MFRPASSAAPLWRQPGYLTWLLTDTAVGLATQVQAFVLPLVVILLTSDPALAGAVAALGVGARVVTTLVGGVLADRHDLRRLMVLSGGLGAGLAVLMAVAYATGLGVTALAVLNMLAGIRAGLLGVASDAALKQVVSSEQLPVASSANQARDAAVQLGAGPAGGALLVLGPVIALLTTAAVFVTSALSALALKGDFQADRDPSTAGSAWREAADGVRWLWGQQVLRRILCVAMLLNLGLTSGVTTLIYGLSVQGLDPARIGLVTSAIGSAMLVGAVAATRIVQHVPSGVVATVGMAMAGLSMAALPFVPGFWPTLAVLFVGTLGAPACNAAMMSYFMHLVPRRLLGRALSGASLLTTGAVPLSPVIAGLGLAWVGLTPTLMTAGTICLLAVLALLADRGLRTLPRPADWPEPQA
>NZ_CP044427.1|WP_158060276.1|727126_727771_-|helix-turn-helix-transcriptional-regulator
MAAHVRMTSPMLKAMTHPLRRRIVSLMRHDQPMRAVDLARQLDVPANSVSFHLRTLADAGMIIEAPEHARDRRDRVWVAAGDGFSVPDPGTLQEEDEPALRAYLDQAGIDLQELVRTALVWAVEWSSGRDEVQRAAISLGTLRATRAEIDLLVEELESVIRRTRQRLQESEAGEVRQDWDFLTLVAEAGLGQAGSAQAAPAPRATAAAAGSTDR
>NZ_CP044427.1|WP_158060286.1|736388_737717_+|hypothetical-protein
MSSCAQDAPDPATEPTAEVSEEGTGTAEAGGQDEEGQTEDHGDDDDHGHGHDHDHGHGHDHDPGGSADDARPSAEVAGASPRLGLTYDGGVLVVDAMTLEVLGDFPAEGFVRLNPAGDDRHLLLTGGPGFRLLDTGAWSVPHGDHDHSYTTEPLLTDLAFQAERPGHVVTHADQTVLFDDGTGQITVLDPDELTIDALPATVEHSTPEPHHGVALILEDGSLLHTLGDEDARVGAAIVDADGQELARSEQCPGVHGEAVAGGDAVVLGCEDGVLVLHGDHFHKVSTGQEYSRIGNLAGHQDFPVVLGDYKTDPDADLERPTTVSLIDVEAEELTLVELPASYSFRSLGIGPDGQALVLGTDGALHVIDTEQGEILDSIAVVAPWEEPTDWQEPRPTLHVLGNFGYVTEPATSQLHVVDLRSGEVIDDAELPQVPNEITGVSG
>NZ_CP044427.1|WP_158062605.1|737773_738682_+|zinc-ABC-transporter-substrate-binding-protein
MLTACGGAGPPDEASTKDSGGSDEDSLAVVAAFYPLAYAVERVAGDRVELTTLTAPGADPHTLELSPGDVRTVAEADLVVYSGGMQAPVDSVVHATRDVHALDVAPLLDLKRTGAGVDEEVSDAEGTPHPVDPHWWLDLDRYAVAAGVIADELSLLDPAGADAYRRGAEALAGDLGELAAEYEDGLAQCRQQIVVTSHEAFGYLTDAHGLVQVGISGLAPEAEPSPARMADIAAVVREHDVDTVYAEVILGSQLAETIASETGARVLVLDPVEGITSASPGSNYLEVMRSNLEALRDGQGCS
>NZ_CP044427.1|WP_158060287.1|738706_739909_-|glycine-C-acetyltransferase
MYGVKDQLRAELDQIEADGLTKKERLITTAQSSHIGTTQGDALNFCANNYLGLANHPEVVAAAREALDEWGFGMASVRFICGTQTLHRDLERAIADFVGTEDAILFPSCFDANGAIFEVLLTAEDAVISDELNHASIIDGVRLSKAQRFRFRNRDMVDLRAQLEAARAADTRRTLIVTDGAFSMDGYLAPLEQICDLAEEFGAMVMVDDSHATGFVGQGGRGSHEACGVFDGVNNRIDILTGTFGKALGGGSGGFVAGPQEVVDLLKQRGRPYLFSNAVAPSVVAGSLKALAIARDSDEPRQVLRRNAELFRSLMTEAGFDLLPGEHAIVPVMFPGEDGALKASQIADVMLTKGVYVIAFSFPVVPRGRARIRVQLSAAHSEDDVRACVGAFVAARDEVG
>NZ_CP044427.1|WP_158060288.1|739919_740969_-|L-threonine-3-dehydrogenase
MRALVKPSAGPGLVLTDVPEPSPGPGEVKIRVLRAGLCGTDLHIQAWDDWAASMLQPPLVVGHEFYGEIVELGQGVPGDRYGLQVGQRCSVEGHVVCGHCRNCRAGRRHMCVNTSNLGVNRDGCFADYVVVPHSNVWVQPDLIDPDLGAVFDPLGNAVHTALSFPLEGEDVLITGAGPIGVMAAAVARHAGARYVVVTDVSAPRLEQARAVGADLAVDVSRERISNAQRRLGMTEGFDVVLEMSGSPRAMSELIDNCTHGAKVAMLGLPAEPYAIDWGKVITHMITLKGIYGREMYETWYKMTAMLQTSQLLRDRIRSVITHRFPAEQWEQAFAAARSGEVGKVIMDWS
>NZ_CP044427.1|WP_158062606.1|741131_741653_+|AAA-family-ATPase
MAVVRREGGRRSTDGPLVVAVDGPSGSGKTVLGTALAARLDAPLVHMDDLFPGWGGLAQAPGLLATQVLEPLARGDRAAYRRWDWHRDDWAQSVAVPPTQLLVVEGCGSSVGPAARYVAVAVWVEADPAERMRRGLARDGESYRPHWERWAAQEEVLFRADGTRERADVLVRT
>NZ_CP044427.1|WP_158062607.1|741887_743006_+|YihY/virulence-factor-BrkB-family-protein
MERGKDDGKFERAQDNAPDSPSDLPKSHWKGVLKRTLSEFGKDGGPDLAAALTYFAIMSLAPMVLALSTLLSLFGQSGAEGEGGAINEVIDQLGGDLGVQQDTLETVKSYIASMGESGGAGILLVVGLLGALWSASNYVNAFSRMMNKVYEIEEGRPVWKLRPWLLVITLLMLLGLVTIILSVTLSGAVSEAVFGAIGLSGTVDTVWNIAKWPVILVILVVMVALLYWGTPNVRQPSFKWLSPGAALAVIVAILAAAGFFFYLTGFGGEESYNATYGAIGGVIILLLLIFIINNVLVIGAELDAELERGRELAAGMPAEEDILLPPRDVKGTQKKEAKQADAVREARKQRMTAAGELRRQGKDVGLEGRGKD
>NZ_CP044427.1|WP_158060289.1|743025_743505_-|hypothetical-protein
MNPATISEADAITLVRAEARRLMVLGGAGLLVAMLLYLGVSILWLERPVQEAATRALPLLVLVAVLAYFFQLPRWVRARQGPVVRGTVGRLTEDEIVLEGGQQGAVSVVLPRGTTGFRPGDRVWVCPDLQPAQTVAVVVPAHVTSPRPVISARALPVRD
>NZ_CP044427.1|WP_158062608.1|743964_746781_+|FAD-binding-oxidoreductase
MSRLGRLGQEMATDRPLERHALAHDASHYLLIPDVVVRPRSTEEVAALLRACAQEGMPLTFRSGGTSLSGQAVTEHVLVDTRLHFSRDVQVLDDGARVRVAPGVTVRQVNARLAPYRTKLGPDPASEGACTVGGVVANNSSGMHCGTEFNTYETLDSLVVVLSSGTVLDTGAEDAGERLRALEPALHEGLLRLRDRLRGDPESVATVRRLFSLKNTMGYGLNSFLDHDDPVAILEHLMVGSEGTLGFIASVTFQTVPVRPKVATGLLVFDTVRAATGVVPQIVEAGAVTAELLDAASLRVSALAPGAPAQITGLQVEEHAALLVEWHADTAEELAGVTSAAQQVLEALPLTAPAVLTGAVAERAALWTVRKALYSAVAGARPQGTNALLEDIAVPLDVLGRTCVDLTAMFDRHGYEESVIFGHAKDGNVHFMLNERFTDPVALQRYADFTEDMVELVLARGGTLKAEHGTGRIMAPFVERQYGHELYAVMRELKALFDPAGLLGPGTILGDDPLVHLKDLKTAPVVEEEVDRCVECGFCEPVCPSRDLTLTPRQRIVLRREMTAAADRGHLELAASLEADYDYPGLQTCAVDGMCQTACPVQINTGDLVRRLRAEDAGPIAQGSWAAAARGWAPVSRAGSIGLSVADRLPGPLGEAATGLARRVLPDELVPAYHRELPRGGPARRQVEHPAAEAVLFPACVGSMFGPEEGSQGASAALVRLAGRAGAGVRTPTGLAGLCCGTPWKSKGLTQGYAVMARRVLPALWEASGQGRLPVVTDAASCTAGVRVMVQNAAEHGHPESVGIRVVDAVEWAATALLPRLPDPRRVGRVVLHPTCGTQTLGVTIYLERLAASLSHEVVVPTDWGCCGFAGDRGLLHPELTASATAPEVAELSQRGLLDAHPQDTIFLSDNRTCEIGMTRATGRTYRHVLEQLESATR
>NZ_CP044427.1|WP_158060290.1|746855_747509_-|oligoribonuclease
MAGERIVWIDCEMTGLDLQADALVEVACLVTDSELNVLGDGVDVVIRPPQEALDQMGDFVREMHTQSGLLPLLENGTTLQDAQERVLAYVREHVPEGRKAPLGGNTVGTDRTFLARDMPELETHLHYRIVDVSSIKELARRWYPRAYFAAPKKTGGHRALGDIQDSIAELRYYREAVFKDQPGLDTATLRGIAARHTTIPASPEPPATPGSPEPLTP
>NZ_CP044427.1|WP_158060291.1|747554_748757_+|PrsW-family-intramembrane-metalloprotease
MSHAPPPPPTGDPVHAGWHQLMTYQPQVPAPANPTRRPMLRGIVGWSVVAVVFGLAALAMTFVVTTAVGPRAALLALVSSAIALGIVIPLFLWVDRLEAEPPRLLWFAFLWGALISTLGALVLGELGLAFFAGLDADPMVLGAVVIAPVTEEVLKGLGVLLIFLLARREFNGVIDGIVYAGIVAAGFAFVENILYLGTMYVDGGVPGLVAIFVMRCLVSPFAHPMFTICIGLALGLIAHRRRWSSAWIVLLGLAGAIFLHGLWNYSAVVRAEAYLLIFVLVQIPLFVGFLLLLYWARRRESRLLRDILTGYGLNGWYTPAEVAMLADPGERRRARAWARGIGGRRAQQAMRAFQDESGELAMVRKHMVHGGGGTDPHWLEHERRLLKAVSAHRQVFVPRA

Crispr_ID: NZ_CP044427_3

• CRISPR_ID: NZ_CP044427_3
• CRISPR_location: 1405079-1405162
• CRISPR_type: Orphan
• Repeat_type: NA
• Spacer_info: 1 spacers

Consensus repeat of NZ_CP044427_3

Consensus_repeat	Method
CACAACGTGGGATCAAGGTTGTGCGG	CRISPRCasFinder

spacers of NZ_CP044427_3

>3.1|1405105|32|NZ_CP044427|CRISPRCasFinder
AGGGATCCCCCTCGGGCGCGTTGTCTGCGCGA

CRISPR arrays and Neighbor proteins around NZ_CP044427_3

CRISPR arrays

The CRISPR arrays of NZ_CP044427_3

>merge|NZ_CP044427|3|1405079-1405162|CRISPRCasFinder
CACAACGTGGGATCAAGGTTGTGCGGAGGGATCCCCCTCGGGCGCGTTGTCTGCGCGACACAAGGTGGGATCAAGGTTGTGCGG

>NZ_CP044427|3|3|1405079-1405162|CRISPRCasFinder
CACAACGTGGGATCAAGGTTGTGCGG	AGGGATCCCCCTCGGGCGCGTTGTCTGCGCGA
CACAAGGTGGGATCAAGGTTGTGCGG

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP044427.1|WP_158060780.1|1413961_1415026_+|ATP-dependent-DNA-ligase	unknown	unknown	gnl|CDD|240135
NZ_CP044427.1|WP_158060763.1|1396941_1397721_-|glycerophosphodiester-phosphodiesterase	unknown	unknown	gnl|CDD|176504
NZ_CP044427.1|WP_158060779.1|1413414_1413876_-|peptide-methionine-(R)-S-oxide-reductase-MsrB	unknown	unknown	gnl|CDD|376583
NZ_CP044427.1|WP_158060761.1|1395973_1396168_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP044427.1|WP_158060775.1|1409101_1410013_-|ammonia-dependent-NAD(+)-synthetase	unknown	unknown	gnl|CDD|234831
NZ_CP044427.1|WP_158060770.1|1404300_1404945_-|DUF3000-domain-containing-protein	unknown	unknown	gnl|CDD|378665
NZ_CP044427.1|WP_158060776.1|1409954_1411001_-|DUF4349-domain-containing-protein	unknown	unknown	gnl|CDD|379526
NZ_CP044427.1|WP_158060778.1|1412693_1413401_+|chlorite-dismutase-family-protein	unknown	unknown	gnl|CDD|377705
NZ_CP044427.1|WP_158060772.1|1405941_1406973_+|uroporphyrinogen-decarboxylase	unknown	unknown	gnl|CDD|234644
NZ_CP044427.1|WP_158060773.1|1407132_1407360_+|hypothetical-protein	unknown	unknown	unknown
NZ_CP044427.1|WP_158060777.1|1411206_1412697_+|protoporphyrinogen-oxidase	unknown	unknown	gnl|CDD|237009
NZ_CP044427.1|WP_158060774.1|1407305_1409024_-|ABC-F-family-ATP-binding-cassette-domain-containing-protein	unknown	unknown	gnl|CDD|223562
NZ_CP044427.1|WP_158060768.1|1401436_1402966_-|UDP-N-acetylglucosamine-1-carboxyvinyltransferase	unknown	unknown	gnl|CDD|238796
NZ_CP044427.1|WP_158060764.1|1397845_1398448_+|CDP-alcohol-phosphatidyltransferase-family-protein	unknown	unknown	gnl|CDD|223632
NZ_CP044427.1|WP_158060766.1|1399371_1400556_+|1-acyl-sn-glycerol-3-phosphate-acyltransferase	unknown	unknown	gnl|CDD|153251
NZ_CP044427.1|WP_158060769.1|1403035_1404301_-|ribonuclease-D	unknown	unknown	gnl|CDD|223426
NZ_CP044427.1|WP_158060765.1|1398449_1399367_+|phosphatidate-cytidylyltransferase	unknown	unknown	gnl|CDD|366491
NZ_CP044427.1|WP_158060767.1|1400624_1401419_-|hypothetical-protein	unknown	unknown	gnl|CDD|179854
NZ_CP044427.1|WP_158060771.1|1405211_1406012_-|GNAT-family-N-acetyltransferase	unknown	unknown	gnl|CDD|224584
NZ_CP044427.1|WP_158060762.1|1396420_1396810_+|hypothetical-protein	unknown	unknown	unknown

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
NZ_CP044427.1|WP_158060780.1|1413961_1415026_+|ATP-dependent-DNA-ligase	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.	2.09919e-110
NZ_CP044427.1|WP_158060763.1|1396941_1397721_-|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.	9.44198e-84
NZ_CP044427.1|WP_158060779.1|1413414_1413876_-|peptide-methionine-(R)-S-oxide-reductase-MsrB	gnl|CDD|376583	pfam01641, SelR, SelR domain. Methionine sulfoxide reduction is an important process, by which cells regulate biological processes and cope with oxidative stress. MsrA, a protein involved in the reduction of methionine sulfoxides in proteins, has been known for four decades and has been extensively characterized with respect to structure and function. However, recent studies revealed that MsrA is only specific for methionine-S-sulfoxides. Because oxidized methionines occur in a mixture of R and S isomers in vivo, it was unclear how stereo-specific MsrA could be responsible for the reduction of all protein methionine sulfoxides. It appears that a second methionine sulfoxide reductase, SelR, evolved that is specific for methionine-R-sulfoxides, the activity that is different but complementary to that of MsrA. Thus, these proteins, working together, could reduce both stereoisomers of methionine sulfoxide. This domain is found both in SelR proteins and fused with the peptide methionine sulfoxide reductase enzymatic domain pfam01625. The domain has two conserved cysteine and histidines. The domain binds both selenium and zinc. The final cysteine is found to be replaced by the rare amino acid selenocysteine in some members of the family. This family has methionine-R-sulfoxide reductase activity.	4.01069e-76
NZ_CP044427.1|WP_158060775.1|1409101_1410013_-|ammonia-dependent-NAD(+)-synthetase	gnl|CDD|234831	PRK00768, nadE, ammonia-dependent NAD(+) synthetase.	3.94466e-145
NZ_CP044427.1|WP_158060770.1|1404300_1404945_-|DUF3000-domain-containing-protein	gnl|CDD|378665	pfam11452, DUF3000, Protein of unknown function (DUF3000). This is a bacterial family of uncharacterized proteins.	1.63954e-76
NZ_CP044427.1|WP_158060776.1|1409954_1411001_-|DUF4349-domain-containing-protein	gnl|CDD|379526	pfam14257, DUF4349, Domain of unknown function (DUF4349). This family of proteins is found in bacteria and archaea. Proteins in this family are typically between 282 and 353 amino acids in length. There is a single completely conserved residue D that may be functionally important.	9.84609e-55
NZ_CP044427.1|WP_158060778.1|1412693_1413401_+|chlorite-dismutase-family-protein	gnl|CDD|377705	pfam06778, Chlor_dismutase, Chlorite dismutase. This family contains chlorite dismutase enzymes of bacterial and archaeal origin. This enzyme catalyzes the disproportionation of chlorite into chloride and oxygen. Note that many family members are hypothetical proteins.	1.31178e-95
NZ_CP044427.1|WP_158060777.1|1411206_1412697_+|protoporphyrinogen-oxidase	gnl|CDD|237009	PRK11883, PRK11883, protoporphyrinogen oxidase; Reviewed.	1.21548e-128
NZ_CP044427.1|WP_158060774.1|1407305_1409024_-|ABC-F-family-ATP-binding-cassette-domain-containing-protein	gnl|CDD|223562	COG0488, Uup, ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only].	6.16708e-96
NZ_CP044427.1|WP_158060768.1|1401436_1402966_-|UDP-N-acetylglucosamine-1-carboxyvinyltransferase	gnl|CDD|238796	cd01555, UdpNAET, UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes enolpyruvyl transfer as part of the first step in the biosynthesis of peptidoglycan, a component of the bacterial cell wall. The reaction is phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine = phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine. This enzyme is of interest as a potential target for anti-bacterial agents. The only other known enolpyruvyl transferase is the related 5-enolpyruvylshikimate-3-phosphate synthase.	5.86139e-125
NZ_CP044427.1|WP_158060764.1|1397845_1398448_+|CDP-alcohol-phosphatidyltransferase-family-protein	gnl|CDD|223632	COG0558, PgsA, Phosphatidylglycerophosphate synthase [Lipid metabolism].	1.21745e-07
NZ_CP044427.1|WP_158060766.1|1399371_1400556_+|1-acyl-sn-glycerol-3-phosphate-acyltransferase	gnl|CDD|153251	cd07989, LPLAT_AGPAT-like, Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: AGPAT-like. Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are such LPLATs as 1-acyl-sn-glycerol-3-phosphate acyltransferase (AGPAT, PlsC), Tafazzin (product of Barth syndrome gene), and similar proteins.	3.15853e-32
NZ_CP044427.1|WP_158060769.1|1403035_1404301_-|ribonuclease-D	gnl|CDD|223426	COG0349, Rnd, Ribonuclease D [Translation, ribosomal structure and biogenesis].	3.22883e-80
NZ_CP044427.1|WP_158060765.1|1398449_1399367_+|phosphatidate-cytidylyltransferase	gnl|CDD|366491	pfam01148, CTP_transf_1, Cytidylyltransferase family. The members of this family are integral membrane protein cytidylyltransferases. The family includes phosphatidate cytidylyltransferase EC:2.7.7.41 as well as Sec59 from yeast. Sec59 is a dolichol kinase EC:2.7.1.108.	6.3528e-31
NZ_CP044427.1|WP_158060767.1|1400624_1401419_-|hypothetical-protein	gnl|CDD|179854	PRK04457, PRK04457, polyamine aminopropyltransferase.	2.23502e-09
NZ_CP044427.1|WP_158060771.1|1405211_1406012_-|GNAT-family-N-acetyltransferase	gnl|CDD|224584	COG1670, RimL, Acetyltransferases, including N-acetylases of ribosomal proteins [Translation, ribosomal structure and biogenesis].	1.84678e-24
NZ_CP044427.1|WP_158060772.1|1405941_1406973_+|uroporphyrinogen-decarboxylase	gnl|CDD|234644	PRK00115, hemE, uroporphyrinogen decarboxylase; Validated.	0

Protein sequences

>NZ_CP044427.1|WP_158060770.1|1404300_1404945_-|DUF3000-domain-containing-protein
MVSRISDARPRQRSAGTPGAPEDTIFTRALAGVREAQVRPELVLEEVPAPSRLAPHAVALSGEVVPSHLTDDDEAAATGRFVLLHDPEGPEPWEGTWRAVTYAKAQMEPEVGHDPLAGQAGWSWLTDALDEAGLAYVAPAGTVTCVTSESFGALADREPTVELEIRASWTPVLTPDREPDELAATLGAWGDLLCTLAGLPPLPEGVVALSGTRR
>NZ_CP044427.1|WP_158060769.1|1403035_1404301_-|ribonuclease-D
MAVDPALNADPSSDFEPLDAPAEGVPGVVDTTEGLREALDALRSGEGPVAVDAERASGYRYGQRAYLVQLRREGVGTLLIDPIAFEDLTAIGHALAGTEWVLHAATQDIPCLAEVGMRPAQLFDTELGGRLAGLPRVGLSAVLEYYLGVTLAKEHSAVDWSTRPLPEPWLRYAALDVELLIDLRDRMERDLAEQGKLDWARQEFDALTRFTGPPGPNDPDAWRRTSGMHRLRKPRALAALRELWLVRDAIARERDVSPGRVLPDSTLVDLAMRQPRDATSLAPDRAERSHSRQRRAEQGLLRYQGAWLGAIRAVQELAEDELPEPTKRGDGPPPPRAWADRDPGAAARLTEVRAGLAALSERVDVPVENLMQPDTVRRLLWRPPAQRDAEGLDAAAAEQGARPWQRELVVPLLVSAVERHP
>NZ_CP044427.1|WP_158060768.1|1401436_1402966_-|UDP-N-acetylglucosamine-1-carboxyvinyltransferase
MTESYLSRIGALIRDARRHKDLTQADLAHLLGTSQSAVARIEQGKQNLSLEMIARIGEKLDSEIVQVSSGVPQNLRITGGVKLSGEIDVRTSKNAAVALLCASMINKGRTTLRNLARIEEVNRITEVLTSIGFKIRWLPDSSDLEIVPPEKIDLAAMDETAARRTRTIIMFLGPLLHEFDNFELPYAGGCDLGTRTVEPHMTALRQFGLEVTATTGFYHAIVDTSVWPTRAIVLTERGDTVTENVLLAAARHRGTTVIRNASSNYMVQDLCVFLRELGVQIEGLGTTTLTVTGVEHIEQDIEYSPSEDPIEAMSLLAAAVVTGSEITIRRVPIEFMEIELAVLDTMGMEYDLTEEYTSANGHTRLVDLTTRPGPLKAPMDKIHPLPFPGLNIDNLPFFAIIAACAQGSTLIHDWVYENRAIYLTELTTLGAKVHLMDPHRVMIEGPTRWRAGEIMCPPALRPGVVILLAMLAAPGVSVLRNVYVINRGYEDLAVRLNALGAQIQTFRDI
>NZ_CP044427.1|WP_158060767.1|1400624_1401419_-|hypothetical-protein
MSIVWDERGGATVMRDGHAQSYVDPDDPLLLVFEYVEQIGLVLQALCPGPAPLATTHVGGGGLTLARWIHRVHPGSPQIVLEPDSALTELVRRELPLPRGHRIRVRPVTGEEGITALRDGSAEVIVQDAYADGRIPARLTGTWWAAQVARVLAPGGLLVVNAADEPGLRWLARFTATLRTVLPHVGLLVLREVAKGRRYGNVVVVASHRPLDDVSLTRVATRATFPTTWRPSADTARGEAGVLPFGPVGEPSPPPPDSGVLRLR
>NZ_CP044427.1|WP_158060766.1|1399371_1400556_+|1-acyl-sn-glycerol-3-phosphate-acyltransferase
MTTGIWAARVRHMLWRGLCTLAGGVRIGGHVPPGPKVLVANHTSHADTAALLAALPPSCRPRFVAAQDYWFDRAWRRAVVTTLVGALPVARAGSGYEALRDAARPVLGDGGSVVIYPEGTRGAPGTPVGEFRSGALRLAADLDVPLVPVGISGTGRVLPKHGRLRPEGVVLRFGDPLPAAQCRDTSPEVVRSAVQALRDDSEAVPWRDSRTFTWLERRSDAQLMGAGFLWGAAEALSWPIMAEVYVVAVGAAQPGRAGRVATSVAAGSVVGVVGHALLARRGVHLPAPLTRPRMHRQARADLRRSGPAGIWRQMFNGVPVKVYASAAGELGTPLVPFALHTAGARPTRMAMAATVVLLAGRWAHPLMRRRYPEFLILGSAVFAEGLHQVIRRWR
>NZ_CP044427.1|WP_158060765.1|1398449_1399367_+|phosphatidate-cytidylyltransferase
MPAVNGPAQWWDQLLHHDRVLTLPVELPWFGEVTGRGVFNLYVTLAVLAVGGLAVVVLRQPELRTRWTTWVLIAPVVGIPIWLGRGPTALLAVLLAVLAVIEFARLIALPRPETWLLLILAVLYPVAAWQWPELLLLAPVIALGCALPAILRGDTTLGVERAAFTAFGSIWLCWSLAHLVVLWEDAFVVVFAAAAADVAAYAGGKSLRRFRWAARPLSPLSPNKTVGGLVGAVLGAVLILLILGELSVGMVVAVAVGGVLGDLLESMMKRRAGVKDAGAWLPGFGGLLDRVDSLLVVLPLAAVLG
>NZ_CP044427.1|WP_158060764.1|1397845_1398448_+|CDP-alcohol-phosphatidyltransferase-family-protein
MQGLYALKPWYTRRLNGVVDAAVSRGFSPDLFTAVGIVGAAMAGVALGLGWWWLALPLLALRLAGANLDGAVARARGVSRPWGFVLNEIGDRFGDLLMWAGLAWWAAQHSTNALVWVLVATVAATLPTFASLSAAGAGATRRNGGPLGKTERCLLVVVGCAVPTWLVGVSAVVVAGSVLTAALRLRSAHRELRAPVEVAP
>NZ_CP044427.1|WP_158060763.1|1396941_1397721_-|glycerophosphodiester-phosphodiesterase
MRTAYLDHPGPIPMAHRGYDAGGTGLENTMAAFRAAVELGYRYVETDVHATRDGVVLAFHDETLDRVTDRRGRIQELAWREVSRARVGAGEPVPRLEDLLEEWPGLRVNIDIKSPGAVVPLVRVIERMRAHERVCVTSFSDQRRRAAVMRLTRPVVTSAGQSSTAAFRAAAALPPLVRPSVVARTLRGVDGLQVPAEHLGIEVVTPTSVAAAQEVGAFVHVWTINDPAEMDRLLDLGVDGIVTDRADLLKGVLTARGQW
>NZ_CP044427.1|WP_158060762.1|1396420_1396810_+|hypothetical-protein
MALEPVGHAVHPSGGLLHQAGGHRGAFGALGHLAELVGQAVQALGRTVLLVAGLTGHVAGHLVQQALDLALGLLRDVLCLLHGGLRNLAGTVLDILSDRGGLLLGSVRSAARGVLVERSFTHVFFSLSG
>NZ_CP044427.1|WP_158060761.1|1395973_1396168_-|hypothetical-protein
MYATTPGVPTAYATREQPSTLDTAAEPLPVGDELIGQQDDLVGQDDELIGYEDGLGSRENGDRL
>NZ_CP044427.1|WP_158060771.1|1405211_1406012_-|GNAT-family-N-acetyltransferase
MNHTGVCGASCPRAARTRGLSAGTVWLLCCARVVTLRVSHEGLATLGTMCASPEPSDPADSPDVAAVAAVPAVAAPVSAAHARIAGELPRQTSRLVLRELTPADAAAVHAYRSVPEVTRYLGHPPLDPDGARDLVDRWLADPAGLSVALELDGAVVGDVRLWFWPSSVKAPATSEEVDAGLGYALHPGQQGQGLATEAVGEIVQLVLGPGGIRRITTRVFAAATPSSKLLCRLGFHLDGVDRAAVLAPEGEVWWDDECWSLLRSDR
>NZ_CP044427.1|WP_158060772.1|1405941_1406973_+|uroporphyrinogen-decarboxylase
MPADSPLVRAARGQEAPHTPVWFMRQAGRSLPEYRKLREGVPMLQSCRTPELVTEITLQPVRRHGVDAAIFFSDIVVPLQAVGLDLDIVPGTGPVVAEPVRTRADLDRIPELTPEHVPDIAQSVDLLVAELGATPLIGFAGAPFTLASYLVEGGPSKNHERTKALMHGDPELWHDLCARLAQISLTFLQVQAAAGASAVQLFDSWAGFLSRADYEQHVLPHSRAVLQGFTEAHPEVPRIHFGVGTGELLPLMADAGTEVIGVDYRVSLTDALERTGGRYAVQGNLDPALLFAPWEALERRVREIVAEGQAAPGHIFNLGHGVLPHTDPEVLTRVTALVHELTS
>NZ_CP044427.1|WP_158060773.1|1407132_1407360_+|hypothetical-protein
MDQERLVRQPRDWRFDPWLVGTSALAVALALALDLPWWGAGLLGGGGYALGLLLTVTVQRWRRTRASSQTGSSAS
>NZ_CP044427.1|WP_158060774.1|1407305_1409024_-|ABC-F-family-ATP-binding-cassette-domain-containing-protein
MGHVDLSQISFVLPDGRPLLDEVSLRVGEGAVVALVGPNGTGKTTLLRIIAGDLEPHGGSLNRSGGLGVMRQFIGSVRDDSTVRDLLVSVAPERIGQAARALDATELAIMEVDDEPAQMAYAQALADWGDVGGYEQETRWDEVTTTALGLPFEQAQWRRVRTLSGGEQKRLVLEALLRGPEEVLLLDEPDNYLDVPGKQWLESALQATTKTVLLVSHDRELLSRAATRIVTLEPSAAGATAWTHPGSFATWHQARRERNARLEEELKRWDEEHAKLRRLMLMYKQKAAYNSDMAARYQAARTRLQRFEDAGPPEKIALEQNVRMRLTGGRTAKRAVVCRRLELLAPGEGTGEALMRPFDLEVWYGERVAVLGSNGSGKSHFLRLLAAGGSDPDVEHQPIGAASGGPTPVRHTGVARLGSRVRPGWFAQTHEGLQTGEAGRTLLQILHRGDEHRHGRTREEAARVLDRYGLARAAEQTFESLSGGQQARFQILLLELSGATLLLLDEPTDNLDLHSAEALEEGLAGFEGTVLAVTHDRWFARGFDRFLVFGAGGTVYEADEPVWDEARVRRQR
>NZ_CP044427.1|WP_158060775.1|1409101_1410013_-|ammonia-dependent-NAD(+)-synthetase
MTDQQLQQEIRTALEVVDPESFDAAREGGRRIDFLARYLQETGLRGYVLGISGGVDSTAAGRLAQLAVERVREAGGEAQFVGIRLPYREQKDEADAQAAVEFIAADEILTVDIGPATDALWDELERAGIGGGQESAHYHRGNVKARERMTAQFAVAGVRGMAVLGTDQAAEALVGFYTKFGDGAADLVPLFGLPKNRVRDICRWLGAPDTLVDKVPTADLESDRPMLADEEALGVTYAAIDDYLEGREVSEEDERTITGWYRRTAHKRALPITPDGFLGRPGGRDAASREVIAEEPEAQGPSA
>NZ_CP044427.1|WP_158060776.1|1409954_1411001_-|DUF4349-domain-containing-protein
MRTKWITAVLALLLVLAGCSAGSTNDSSPAGADSDASVEQFEDDAGMERAQPDSAMDGDGEAAAADDSTVAGGSVAPGAVTTEDAPMMVRRVELKMLVEDVAAAAAQARASVSGAGGWVQSEEIVPGTEDRDGHGSMVLRVPSSDLDGIITSLSELGEVTFTRSTAEDVTAEYRDVEARVATLEAGAERLRDLIADAPSVESIASLERELTSREADLDALKARMKVLEADVSRSTITLHLAEESDDLEVLNEDDDTGFMSGLRAGWEAFVASGTIALTAIGALLPFLALAALLGIPLLLWRRRRTRARTGTTRATSRQAGAAQAGLASKDDRPAAAAGDPDGPGSGRP
>NZ_CP044427.1|WP_158060777.1|1411206_1412697_+|protoporphyrinogen-oxidase
MPSYLVVGGGISGLASAVGILDADPAAQVTVLEGSDRVGGKLRGAQVAGRMVDVGAEAVLARRPEALELIDRAGLAGDVVHPTGASAQVWSRGSLHPMPRRTLMGVPADPEALRGLLTDEEVERALAEVVPKTASPGISDPDPRVDDISVGDLVADRLGPAVVDRLVEPLLGGVYAGHARLLSARAALPQLRTLVGDGGSLTGAVDRMLPAPTDGTQSQVAAPVFATVLGGLHRLPDALADLLAERGATVRTGAVARELHVLPEGGFEVVTGPRPAPTAYRADRVVLAVPPAPTARLLASLAPQAADLLQRVETASVAVITLALPSAELGELTGSGFLVPPVEGLRIKAATFSATKWAWVRELGQGAGPEGQDLTFLRASIGRHREESTLQHPDDELVEAARADLALVLGRDLPEHVDAHVQRWGGGLPQYAVGHVDLVEQVHTAVDRVPGLAVCGAGYEGVGIPACIASARRAVDRLTDHPTDPAPPAHSRSTTA
>NZ_CP044427.1|WP_158060778.1|1412693_1413401_+|chlorite-dismutase-family-protein
MSNYTHPTPEQAEEINAEIRYAAYSVFRAAAPLPQDREGLAQEVEQLFAELSGHGLVVRGVYDVAGLRADADLMVWWHAEEVELVQTAYQRFRQTHLGQHLEPVWSNVGLHRPAEFNRGHVPAFLSGHEPKKFLCVYPFVRSYEWYVLDPAERGQMLREHGVAAKDYKDVLANTISSFALGDYEWLLAFEADELHRIVDLMRDLRNTQARLHVREEVPFFTGPRVEVAELVARLP
>NZ_CP044427.1|WP_158060779.1|1413414_1413876_-|peptide-methionine-(R)-S-oxide-reductase-MsrB
MSTQHSTPATDSARPDAAAAYSQAKSEQEWREQLSPEEYHVLREAGTERPFTGEYNSTTTEGVYACRACGVELFRSETKFEAHCGWPSFYAPLAEDRVQYIQDDSLGRPRTEVRCASCGSHLGHVFEGEGYETPTDLRYCMNSISMTLVPAQD
>NZ_CP044427.1|WP_158060780.1|1413961_1415026_+|ATP-dependent-DNA-ligase
MADATMLTAPGPDGEDREVRLSSPDKVVWPADEASAAITKADLAAYLTAVAEPMLRGLADRPVTLQRVRGGIEGEVFYSKNPPKGVPGWSRTTMVTYPSGRSHPQLVVDDLATLLWTAQMGTVTWHPWPVRTGDNDHPDEVRIDLDPQPGRAFADVVEAARGLREVMQEVGLSPHVKTTGNRGVHVFAAIEPRLEFLEVRHAVIGLARELERRLPDLVTTAWWKEERGERIFVDFNQATRDRTLAAAWSPRIQPGAPVSVPVTWEQLGDVVPGELTVHTAPAWLSEHGDPWAGLHDQPGRIDGAYALWEADRERGLGELNFPPDHPKMPGEPPRVQPSKKVAEHWDEDGNRIEG

Crispr_ID: NZ_CP044427_4

• CRISPR_ID: NZ_CP044427_4
• CRISPR_location: 2170734-2170837
• CRISPR_type: Orphan
• Repeat_type: NA
• Spacer_info: 1 spacers

Consensus repeat of NZ_CP044427_4

Consensus_repeat	Method
GTCGCCGGTCGGGGGCGAACCGCGTCGCCGGTCGGGG	CRISPRCasFinder

spacers of NZ_CP044427_4

>4.1|2170771|30|NZ_CP044427|CRISPRCasFinder
CAAACCGTGTCGCCGGTCGGGGGCAAACCG

CRISPR arrays and Neighbor proteins around NZ_CP044427_4

CRISPR arrays

The CRISPR arrays of NZ_CP044427_4

>merge|NZ_CP044427|4|2170734-2170837|CRISPRCasFinder
GTCGCCGGTCGGGGGCGAACCGCGTCGCCGGTCGGGGCAAACCGTGTCGCCGGTCGGGGGCAAACCGCGTCGCCGGTCGGGGCGAACCGCGTCGCCGGTCGGGG

>NZ_CP044427|4|4|2170734-2170837|CRISPRCasFinder
GTCGCCGGTCGGGGGCGAACCGCGTCGCCGGTCGGGG	CAAACCGTGTCGCCGGTCGGGGGCAAACCG
CGTCGCCGGTCGGGGCGAACCGCGTCGCCGGTCGGGG

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP044427.1|WP_158061365.1|2172396_2173422_+|DUF2236-domain-containing-protein	unknown	unknown	gnl|CDD|378343
NZ_CP044427.1|WP_158061369.1|2175846_2176389_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP044427.1|WP_158061371.1|2180141_2180423_-|acylphosphatase	unknown	unknown	gnl|CDD|237712
NZ_CP044427.1|WP_158061366.1|2173461_2174682_-|signal-recognition-particle-docking-protein-FtsY	unknown	unknown	gnl|CDD|236686
NZ_CP044427.1|WP_158061360.1|2166716_2167799_-|amidohydrolase-family-protein	unknown	unknown	gnl|CDD|238624
NZ_CP044427.1|WP_158061358.1|2163607_2164912_+|isocitrate-lyase	unknown	unknown	gnl|CDD|237893
NZ_CP044427.1|WP_158061364.1|2170838_2172488_-|signal-recognition-particle-protein	unknown	unknown	gnl|CDD|236780
NZ_CP044427.1|WP_158061370.1|2176388_2180045_-|chromosome-segregation-protein-SMC	unknown	unknown	gnl|CDD|274008
NZ_CP044427.1|WP_158061362.1|2168576_2169311_-|mismatch-specific-DNA-glycosylase	unknown	unknown	gnl|CDD|381679
NZ_CP044427.1|WP_158061361.1|2167859_2168564_+|N-acetyltransferase	unknown	unknown	unknown
NZ_CP044427.1|WP_158061354.1|2160394_2160919_-|ribosome-maturation-factor-RimM	unknown	unknown	gnl|CDD|234650
NZ_CP044427.1|WP_158061356.1|2161271_2161832_-|30S-ribosomal-protein-S16	unknown	unknown	gnl|CDD|184724
NZ_CP044427.1|WP_158061372.1|2180316_2181477_+|Gfo/Idh/MocA-family-oxidoreductase	unknown	unknown	gnl|CDD|223745
NZ_CP044427.1|WP_158061367.1|2174740_2175334_+|hypothetical-protein	unknown	unknown	gnl|CDD|236571
NZ_CP044427.1|WP_158061359.1|2164997_2166662_+|malate-synthase-A	unknown	unknown	gnl|CDD|236432
NZ_CP044427.1|WP_158061355.1|2161026_2161269_-|RNA-binding-protein	unknown	unknown	gnl|CDD|179479
NZ_CP044427.1|WP_158061363.1|2169213_2170410_-|M4-family-metallopeptidase	unknown	unknown	gnl|CDD|341060
NZ_CP044427.1|WP_158061373.1|2181503_2181815_+|hypothetical-protein	unknown	unknown	unknown
NZ_CP044427.1|WP_158061357.1|2161962_2163489_-|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl|CDD|238045
NZ_CP044427.1|WP_158061368.1|2175369_2175687_-|hypothetical-protein	unknown	unknown	unknown

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
NZ_CP044427.1|WP_158061365.1|2172396_2173422_+|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.	6.10955e-49
NZ_CP044427.1|WP_158061371.1|2180141_2180423_-|acylphosphatase	gnl|CDD|237712	PRK14422, PRK14422, acylphosphatase; Provisional.	7.45318e-38
NZ_CP044427.1|WP_158061360.1|2166716_2167799_-|amidohydrolase-family-protein	gnl|CDD|238624	cd01299, Met_dep_hydrolase_A, Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.	2.24472e-64
NZ_CP044427.1|WP_158061358.1|2163607_2164912_+|isocitrate-lyase	gnl|CDD|237893	PRK15063, PRK15063, isocitrate lyase; Provisional.	0
NZ_CP044427.1|WP_158061364.1|2170838_2172488_-|signal-recognition-particle-protein	gnl|CDD|236780	PRK10867, PRK10867, signal recognition particle protein; Provisional.	0
NZ_CP044427.1|WP_158061370.1|2176388_2180045_-|chromosome-segregation-protein-SMC	gnl|CDD|274008	TIGR02168, Chromosome_partition_protein_Smc, chromosome segregation protein SMC, common bacterial type. SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins].	0
NZ_CP044427.1|WP_158061362.1|2168576_2169311_-|mismatch-specific-DNA-glycosylase	gnl|CDD|381679	cd10028, UDG-F2_TDG_MUG, Uracil DNA glycosylase family 2, includes thymine DNA glycosylase, mismatch-specific uracil DNA glycosylase and similar proteins. Uracil DNA glycosylase family 2 consists of thymine DNA glycosylase (TDG), which removes uracil and thymine from G:U and G:T mismatches in double-stranded DNA. It includes mismatch-specific uracil DNA glycosylase (MUG), the prokaryotic homolog of TDG. Escherichia coli MUG is highly specific to G:U mismatches but also repairs G:T mismatches at high enzyme concentration. Uracil-DNA glycosylases (UDGs) initiate repair of uracils in DNA. Uracil in DNA can arise as a result of misincorporation of dUMP residues by DNA polymerase or via deamination of cytosine. Uracil in DNA mispaired with guanine is one of the major pro-mutagenic events, causing G:C->A:T mutations. Thus, UDG is an essential enzyme for maintaining the integrity of genetic information. UDGs have been classified into various families on the basis of their substrate specificity, conserved motifs, and structural similarities. Although these families demonstrate different substrate specificities, often the function of one enzyme can be complemented by the other..	1.27711e-57
NZ_CP044427.1|WP_158061366.1|2173461_2174682_-|signal-recognition-particle-docking-protein-FtsY	gnl|CDD|236686	PRK10416, PRK10416, signal recognition particle-docking protein FtsY; Provisional.	9.14154e-147
NZ_CP044427.1|WP_158061354.1|2160394_2160919_-|ribosome-maturation-factor-RimM	gnl|CDD|234650	PRK00122, rimM, 16S rRNA-processing protein RimM; Provisional.	1.2752e-52
NZ_CP044427.1|WP_158061356.1|2161271_2161832_-|30S-ribosomal-protein-S16	gnl|CDD|184724	PRK14520, rpsP, 30S ribosomal protein S16; Provisional.	2.30272e-65
NZ_CP044427.1|WP_158061367.1|2174740_2175334_+|hypothetical-protein	gnl|CDD|236571	PRK09565, PRK09565, heme-binding protein.	0.00574685
NZ_CP044427.1|WP_158061359.1|2164997_2166662_+|malate-synthase-A	gnl|CDD|236432	PRK09255, PRK09255, malate synthase; Validated.	2.40225e-132
NZ_CP044427.1|WP_158061355.1|2161026_2161269_-|RNA-binding-protein	gnl|CDD|179479	PRK02821, PRK02821, RNA-binding protein.	3.08473e-30
NZ_CP044427.1|WP_158061363.1|2169213_2170410_-|M4-family-metallopeptidase	gnl|CDD|341060	cd09597, M4_TLP, Peptidase M4 family including thermolysin, protealysin, aureolysin, and neutral protease. This peptidase M4 family includes several endopeptidases such as thermolysin (EC 3.4.24.27), aureolysin (the extracellular metalloproteinase from Staphylococcus aureus), neutral protease from Bacillus cereus, protealysin, and bacillolysin (EC 3.4.24.28). Typically, the M4 peptidases consist of a presequence (signal sequence), a propeptide sequence, and a peptidase unit. The presequence is cleaved off during export while the propeptide has inhibitory and chaperone functions and facilitates folding. The propeptide remains attached until the peptidase is secreted and can be safely activated. All peptidases in this family bind a single catalytic zinc ion which is tetrahedrally co-ordinated by three amino acid ligands and a water molecule that forms the nucleophile on activation during catalysis. The active site is found between two sub-domains; the N-terminal domain contains the HEXXH zinc-binding motif while the helical C-terminal domain, which is unique for the family, carries the third zinc ligand. These peptidases are secreted eubacterial endopeptidases from Gram-positive or Gram-negative sources that degrade extracellular proteins and peptides for bacterial nutrition. They are selectively inhibited by Steptomyces metalloproteinase inhibitor (SMPI) as well as by phosphoramidon from Streptomyces tanashiensis. A large number of these enzymes are implicated as key factors in the pathogenesis of various diseases, including gastritis, peptic ulcer, gastric carcinoma, cholera and several types of bacterial infections, and are therefore important drug targets. Some enzymes of the family can function at extremes of temperatures, while some function in organic solvents, thus rendering them novel targets for biotechnological applications. Thermolysin is widely used as a nonspecific protease to obtain fragments for peptide sequencing. It has also been used in production of the artificial sweetener aspartame.	2.16711e-115
NZ_CP044427.1|WP_158061357.1|2161962_2163489_-|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.	3.10078e-13
NZ_CP044427.1|WP_158061372.1|2180316_2181477_+|Gfo/Idh/MocA-family-oxidoreductase	gnl|CDD|223745	COG0673, MviM, Predicted dehydrogenases and related proteins [General function prediction only].	2.39385e-59

Protein sequences

>NZ_CP044427.1|WP_158061363.1|2169213_2170410_-|M4-family-metallopeptidase
MEGTHSTHRPHARCGIVPGYLLRRIAQAEPELAPALEFALRDGEATRGRRELLGTRWPGGHAPLQGRLMVPPVRLANTPAGEVLSLPDHVPLPEDAAPDRQVHDAEHGTLLPGRLVRTETGDGPWEPAVEEAFDGLGATWEVLARVYGWDSLDGQGMPLVATVHYARNYANAFWDGRQMVFGDGDGVYFHRFTASIDVIAHELAHGMTQYTAGLTYVGQSGALNESASDVWGALVRQWVRDETVAEADWLIGADLFTDRVQGVALRSMAAPGTAYDDPVLGADPQPGHMDDYVVLPHDADHDNGGVHINSGIPNRAFHLFATALGGRSWERAGTVWFDTMATRGLIPRDCDFATFARVTLQVAAGRYGVGSEEEQALLSAWDQVGLRPGEADPVALST
>NZ_CP044427.1|WP_158061362.1|2168576_2169311_-|mismatch-specific-DNA-glycosylase
MAWARRRSRRCCRPGTRWGCGRGKPTPWRCPPELCHAALPCYSDRRLGRVATRRFTKTELESFRDREVPDLLPADGSAVRLLFVGINPGLWTAATQTHFAHPVNRFYPALLRAGIIEHAIDPAAGMTDEDRAHLLGRGIGITNLAPRATARADELSKEELRQGGQRLRETVRRVRPRVVAVAGITAYRSAFGVRTAVAGRQADPLEEAVLWVVPNPSGLNAHETVDSLAASYAHPAREARVLAR
>NZ_CP044427.1|WP_158061361.1|2167859_2168564_+|N-acetyltransferase
MDRVDLTALLRGAAGGRFPPVDGGVSRARPWRAGVEAAVAFTGHAVLAVAAEVSDEALLRLGVHGYGGVHDPRLVAALAGQGEIGVLDVLLVAPATEPTAQAPGPETRPDSDVPVAPLVTRPDLACAERARHAHLWRDDVRVLGLPDHETTGLATLSRGIAGLTEVGIQAEDGEAGQLLAGALARVPRGELVLASVTPGNARSLRFFLRRGFVPVGSVQQWRPRRVRPVDDATG
>NZ_CP044427.1|WP_158061360.1|2166716_2167799_-|amidohydrolase-family-protein
MSAPALHIQGSVLVGPGEVLDEVWVIEGVVSLTPPMSGEVQTVHGYAVPGLVDAHCHVGLEAHGAVDDARAEEHALADRDAGALLLRDAGSPADTRWVQEREDLPRLIRAGRHIARTKRYLRNFAWEIEPEDLVEYVRQEARNGDGWVKLVGDWVDRESGDLGVCWPVDILTEAITAAHEEGARVTAHCFGEQSLADFAAAGTDCIEHATGLTDETIDTFAAQRIAIVPTLVNIDNFPKFAEAGRGKFPTYADHMMDLYERRYETVAKAREAGVPVYVGTDAGGQLPHGLVAREVEALTRTGMSNLEAIGAATWAAREWLGRPGIAEGEAADIVVYRDDPREDVRTMADPHRVILRGHLY
>NZ_CP044427.1|WP_158061359.1|2164997_2166662_+|malate-synthase-A
MPRHTLAANPVSHPHAPYPHHTRRTQDEDTMDQDQYPTGLLDETRLQALRTLERETRTELHALIEARKDLSRTIREGAELEVPAAARHTRDDDAWRVRPHPADLTYRLVELATPATPEHAKGALASGADVWVADLEDMLVPTQARLFAAQRVIQEVATTRSGDPEPGVPTLMVRPRGLHLDEAHFLVDDAPASAALTDTFTFLARCGATLQDNGTGPYVYLPKLETAAEARWWDRTLARMEELLGLPQGCTRVSVLVETVQAVYELEDIVHELRERVTGLAAGRWDYVFSHLRTYGARPDHVLPDRDAFTMNTRFLRTYSDAIVRVCRRRGVQAIGGPIALAAGGPFDESVSMTHARVHRDKAREAAEGFDGAWVLHPALVPVARAPFEERDRHREEGDLPEPARPSGAIDPGALRDVSSLAGSATLTGVRTALRSSLTYLTGWLAGEGTITLAGHVEDFGTVELNRMQLWQWLFHGTRLAEGPTMSERLLDRMLEDEVSLLRRRGGREDLLQLAVTLLRESMVAEEPPAFLYQQAYEALLSVERTGDGDAAVA
>NZ_CP044427.1|WP_158061358.1|2163607_2164912_+|isocitrate-lyase
MTTTTPSTERTPFAQQAQEIEHDWASNPRWKDVERRYSAEDVVRLRGSVVEEHTLARRGAERLWEALETTPFTRALGALTGNQAVQMVKGGLEAIYLSGWQVAADANLAGETYPDQSLYPANSVPAVVRRINNALKRADQVAWMNGETDVNYFAPIVADAEAGFGGPLNVFELMKSMIAAGAAGVHWEDQLASEKKCGHLGGKVLVPTSQHVRTLNSARLAADVLGVPSLVIARTDALAADLLTSDVDEIDREFTTGERTSEGFFRVRSGIEPVLARAKAYAPYADLIWVETGTPDLGLAREFAEELHKDFPDQKLAYNCSPSFNWRSALSDAEVAEFQDKLGELGYAFQFITLAGFHSLNHGMFHLAHSYARQGMSAYVELQEAEFADAERGYTAVRHQAEVGTGYFDAVSTAVNPESSTTALSGSTESEQFH
>NZ_CP044427.1|WP_158061357.1|2161962_2163489_-|helix-turn-helix-domain-containing-protein
MRTSHARVLPFRPSTRLDGVEDEVRAGQADPVAVGRRIRHYRRRCRLTLADVATEVGMSPSALSLIENGHREPRVSTLAALAATLQVDTAALLSGGAPTRRDALEVRWQRAQRSEGFETLGIPTVRTGAGLPDDALEALVGLYETVVGLQQQRAATPEFARLANAELRALMREADNYFPEIEARAAELVRVVDHSHGPVTREAVSRMARHVGFELEVVPDVPASTRTVTDLDHRRIYLPARGAHDIRAAALQALGHVVLEHEPPRDYAEFLAQRVEINYFAAAVLVPELTAVPFLQRAKAQRDIALEDLRDAYGVSYETAAHRFCNLATRHLDLRVHFMRTSADGVIYKAYENDGVRFPMDASGAIEGARVCRAWTARVVFGEPVGSAYAQYTDTGRGTFWCTAVAEQTPAGVFSVSLGVPFDQVRWMRGRETTQRRVSGCPDPRCCTQPPAELARQWAGKVWPSARAHSHLLAVMPPGVFPGVDDTEVLRFVADHAPGWEGAEDLAQ
>NZ_CP044427.1|WP_158061356.1|2161271_2161832_-|30S-ribosomal-protein-S16
MAVKIRLKRMGKIRAPYYRVVVMDSRTKRDGRAIEEIGKYHPTEEPSLIDIDSERAQYWLGVGAQPTEQVAALLKVTGDWQKHKGEPGAEGTLKHKEPKPDKRALYEAALAAADKEDGGNSPDTRRRKAKAEEPKAEDAPAEEPKTEEPKTEEPKTEEPKAEEASVEEAASDAAAAEDTQADKAEA
>NZ_CP044427.1|WP_158061355.1|2161026_2161269_-|RNA-binding-protein
MIEEALEHLVKGIVDHDGDVSVRTKSSRYGDILEVRVHPEDLGRVIGRRGRTASALRTVVGALAGGQKVRVDIVDTDRVR
>NZ_CP044427.1|WP_158061354.1|2160394_2160919_-|ribosome-maturation-factor-RimM
MSQPETFIVARVGKPHGLRGEVTVQVHTDDPERRFVTGAVFTTEPEGVGPLELATVRVHQGVYLLGFGGHTDRSAAETLRGTRLLVPDADEPEDEDGWREEDLQGMEAVLTDGSSVGEVVALHLREVQDLLEIRTPDGRDLLVPFVEELVPEIDEDAHRVVLDPPPGLLELGEK
>NZ_CP044427.1|WP_158061364.1|2170838_2172488_-|signal-recognition-particle-protein
MFNSLSDRLALTFKNLKRKGTVTESDLNATIRDIRMALLDADVALPVVKEFTGAVRERGLGAEVHQALNPAQQIVKIVNEELVSILGGQTRRITLAKTPPTVIMLAGLQGSGKTTFAGKLGRWLADQGHTPLLVAADLQRPNAVTQLEVVGQRAGVAVFAPERGNVFGHDAALESGEGTRSFGDPVDVAVDGVEDARRKGHDVVIIDTAGRLAVDVNLMRQAHDIRLETNAHEVLFVIDAMIGQAAVETAKAFADGVGITGSVLTKLDGDARGGAALSVATVTGQPIMFASTGEGVKDIELFHPDRMASRILDMGDVLTLIEQAEKAFDRVQAQEMTRKFLSEEDFTFDDFLEQMSAIKRMGSLKQMLGMMPGMQQMRAQLDSLDEKEFDRVEAMVRSMTPFERNHPKQINGSRRARIARGSGVSVSEVNQLLERFAEAQKMMRQLKKGGMPGMPGMPGMPGMGGAGGKRSKTPQKKKGKSGNPAKRAQQEREAVQKAQAAREASLESAFGAGALGQDEAGTPSGQGGDLAGLKLPAGFEKFLGDQDKK
>NZ_CP044427.1|WP_158061365.1|2172396_2173422_+|DUF2236-domain-containing-protein
MVALRSDSVTVPLRLRFLKVSARRSERELNTPQGYVGPVADPIRTARRRLAEALRDRVAGPDAERRAHAIWVAPGERRFAPDDPICRVQGHAGMYAGGIRALLLQSLHPLAMAGIGEHSGFRGDPWGRLQRTSEFIAMTTFGPVETAEKILDRINKVHTTVVGTAHDGRPYDATDPHLLRWVHVAEIDSFLLAHQRYSRTPLTPPEADRYVEQAAWAAGRLGIPDPPLTVAELESQLASYRPELEATPGALDVARFLLLEPPLPVAARPGFWLLAAGAVEMLPGYARELLNLRLPGPLRATDKVALRVLARPLGRVGTAAVSWAMSDPQEPRNRPDNSAGA
>NZ_CP044427.1|WP_158061366.1|2173461_2174682_-|signal-recognition-particle-docking-protein-FtsY
MGPINELWEILAVVSIVVLAGLALLVALVRGRGGRSTTLPPGAERDRPPAVGTDPVGQEPGDGEVLLEDRPADVQDRGGVAAQEIELEEAAALERPASARGRLQRLRARLARSNTAMGHVLLALLSREGLSESDWEDVEDTLLASDLGVEATTELVNALRTQVKIEGTTDPEVVRSWLRTDLLRLVDPTMDRRIAASRTENHPAVILVVGVNGTGKTTSVGKLGRVLVAEDKDILFGAADTFRAAAADQLSTWGERVGVPTVRSQLEGADPASVAYEAVKAGIDLESDVVIIDTAGRLHTKRGLMDELGKIKRVVEKLAPVGEVLLVLDATTGQNGMRQAEEFAKEVAITGIVLTKLDGTAKGGIVVNVQRKLGVPVKLIGLGEGPDDLAPFDPEAFVDAIVGRAS
>NZ_CP044427.1|WP_158061367.1|2174740_2175334_+|hypothetical-protein
MRRTSTAALALAALLTVAACGTETGTPDAGGDAPTSTEQDTISPGDPDETGETGETGETGDPGDSTRDPGDSTGDPGDSTGDPGDGTEDPDGKVLADTRGDGHFFIDSLEVRQAESDPVQLFLDVEGNAPTPCHTVAYEVQQDADTFLVHLTTLEKGEMRCTQVLVPYDITIPLGETDTFPVTIDVNDGEQVLTVNG
>NZ_CP044427.1|WP_158061368.1|2175369_2175687_-|hypothetical-protein
MLALVVAMIICVSLGAGVVAFVMLEARREGRGEFWTAEGEELIAGVRRTGERVRERGSRLGSTAAERSQALRERLPERPAPGRDAVARPSRPVPGPSDEDLPAAS
>NZ_CP044427.1|WP_158061369.1|2175846_2176389_-|hypothetical-protein
MQVYGGGEFPAYIIDEETLREELLSEEDTQEWLEETPEDPHAVSFWRMLGELDRALTVGEAALADQEPMAPGWAAAAVRLAHVHHWRTEYAEAHELLTAAEEVFARSGDDGGPDLRMLAFVRQHRAKALFDEGRLAQAEEQAVAALRLRQELGEPEGVLASSQQTVARIRRARDRPATGG
>NZ_CP044427.1|WP_158061370.1|2176388_2180045_-|chromosome-segregation-protein-SMC
MYVKSLTLKGFKSFASSTTLRLEPGITCIVGPNGSGKSNVVDALAWVMGEQGAKSLRGGKMEDVIFAGTSGRAPLGRAEVSMTIDNTDGALPIDYSEVTITRTMFRSGGSEYAINGTACRLLDVQELLSDSGIGREMHVIVGQGQLDQVLRATPEERRGFIEEAAGVLKHRKRKERALRKLETMEGNLTRLTDLTAEIRRQLGPLGRQAETARRAATIQGEVRDARLRILADDLVQLTSALAQEMADERALIERRARVQAAVQAAEAQVAELEDERARSAPALQVAQDHWYSLSSLLERLRALRDLSAERVRLLGAEEEDLRAEAVGRPGGRDPEQLLAQAEKVREEENALLAKVAELAVALEEAEGLRRQAEAAHAKEQARLQRLARAAADRREGLARLAGQVAARRSRIEAGEGEIARLQATAAAVQERAVTAEQEFAALEGTVLDVEEGEEGLDARYEAAEEKRESAEAEVQRWQSDLREAQGEQGALQARVEALALSLRRTDGASALLDADRSAVSGIRGTVTSELTVEPGREAAIAAALGWAGEALVVEGLEPAQQALGWLREQDQGRAGMLVAELADGAQETPRAEWPDLPGYAVWAADVVTAPDPALTRAVHGLLDRVALVPGGQDAAVLVRSTPGVTVVTDQGDVYGPGWVHGGSAAAPSLLELQSAFDEAQEGVQAAERRAQAATFSLAGAREALQEAAAEAEAALDDLHDSDARMTAVAEQLSQLGQATRVARAEHERTTAAITTAEQSLATTRAELAELEQRLADAEVLASQEGTEDPDTSERERLAESAARARTAETEARLALRTQEERAKALAGRADTLESAARNELAARQRAAQRRARRAHERATAEAVSRGAVYVLGLTEQALAAATTARQQAQTEQTQLDQALAVARSRARNLADELRDLTDSVHADEIARAEHRLRIEALEARSLEELGVDPETLVEEYGPQLPVPHVPGPDEDPDAEDFPEPRPFVREEQDKRLRRAERALAQLGRVNPLALEEFAALEERHTFLTEQVEDLRRSKADLLEIVKEVDERVERVFTEAFHDTAAQFERVFSRLFPGGEGRIILTDPSNMLTTGIEVEARPPGKKIKRLSLLSGGERSLTAVALLVAIFKARPSPFYIMDEVEAALDDTNLGRLITLFEELRDSSQLIVITHQKRTMEIADALYGVSMQGDGVTTLVSQRVRDVAPKGGRPQTDQEHTKEPA
>NZ_CP044427.1|WP_158061371.1|2180141_2180423_-|acylphosphatase
MERALIFVRGRVQGVGFRWWTRARALELGLVGHARNLPDGRVEVNAQGDRAALDALIGLLEGDPSTSSRPGRVDGITTQWHAPREGLTGFVER
>NZ_CP044427.1|WP_158061372.1|2180316_2181477_+|Gfo/Idh/MocA-family-oxidoreductase
MRACPTRPSSRARARVHQRKPTPWTRPRTKISARSIPAHYGGAVTEKSAYPPITDRPIRWGLLAAGKIAHALAQAVRETEGGQLVAVAARDAVRAAEFARAHDIPLSYGGYEELCTDPDVDVVYISSTNPHHADQAVRCLESGKHVLVEKPIALTVADAERIVETARTRGLFAMEAMWTRCQPLVLDLADRVREGQIGRVRSFHAAFTVPFEYDAAHRIFDLENGGGALLDLGVYPVALAHLLLGHPTDVQVLGATVPTGVDAQAALQWMNADGAVAQVICDSQSHGSSRTVVRGTEGWIEVHGPVTQPESFTVHRGPDAEEGEHVTGDRRGFVHEVEEVHRCLREGLLQSPLVPHADTVAIMTILESARRELGVRYPQEPEPLHT
>NZ_CP044427.1|WP_158061373.1|2181503_2181815_+|hypothetical-protein
MTQLLVFLLGALVALMVLGHLATPLGERQPPRRWTPVYLMDRVPHAITLFREAGALQRRRLEQAAAERESQVKDQGRRVEDLEDTGDTGDTEDPDGEDPRGRT

Crispr_ID: NZ_CP044427_5

• CRISPR_ID: NZ_CP044427_5
• CRISPR_location: 2612995-2613081
• CRISPR_type: Orphan
• Repeat_type: NA
• Spacer_info: 1 spacers

Consensus repeat of NZ_CP044427_5

Consensus_repeat	Method
CTCGGCACAACGTGGGGTCAAGGTTGTGC	CRISPRCasFinder

spacers of NZ_CP044427_5

>5.1|2613024|29|NZ_CP044427|CRISPRCasFinder
TGAGGAATCACCCCCTCGCGCGTGGTCTA

CRISPR arrays and Neighbor proteins around NZ_CP044427_5

CRISPR arrays

The CRISPR arrays of NZ_CP044427_5

>merge|NZ_CP044427|5|2612995-2613081|CRISPRCasFinder
CTCGGCACAACGTGGGGTCAAGGTTGTGCTGAGGAATCACCCCCTCGCGCGTGGTCTACTCGGCACAACGTGGGATCAAGGTTGTGC

>NZ_CP044427|5|5|2612995-2613081|CRISPRCasFinder
CTCGGCACAACGTGGGGTCAAGGTTGTGC	TGAGGAATCACCCCCTCGCGCGTGGTCTA
CTCGGCACAACGTGGGATCAAGGTTGTGC

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP044427.1|WP_158061707.1|2611666_2612968_+|MFS-transporter	unknown	unknown	gnl|CDD|340883
NZ_CP044427.1|WP_158061704.1|2606260_2609734_-|DNA-directed-RNA-polymerase-subunit-beta	unknown	unknown	gnl|CDD|234749
NZ_CP044427.1|WP_158061710.1|2615319_2615748_-|50S-ribosomal-protein-L11	unknown	unknown	gnl|CDD|234661
NZ_CP044427.1|WP_158061711.1|2615841_2616696_-|transcription-termination/antitermination-protein-NusG	unknown	unknown	gnl|CDD|180161
NZ_CP044427.1|WP_158061712.1|2616758_2617031_-|preprotein-translocase-subunit-SecE	unknown	unknown	gnl|CDD|236066
NZ_CP044427.1|WP_158061709.1|2614462_2615176_-|50S-ribosomal-protein-L1	unknown	unknown	gnl|CDD|180071
NZ_CP044427.1|WP_158061705.1|2610217_2610610_-|50S-ribosomal-protein-L7/L12	unknown	unknown	gnl|CDD|234671
NZ_CP044427.1|WP_158061713.1|2617141_2618476_+|pyridoxal-phosphate-dependent-aminotransferase	unknown	unknown	gnl|CDD|235596
NZ_CP044427.1|WP_158061698.1|2596570_2597245_-|SMI1/KNR4-family-protein	unknown	unknown	gnl|CDD|378155
NZ_CP044427.1|WP_158061701.1|2600980_2601451_-|30S-ribosomal-protein-S7	unknown	unknown	gnl|CDD|235398
NZ_CP044427.1|WP_158061708.1|2613218_2614208_-|type-IV-toxin-antitoxin-system-AbiEi-family-antitoxin-domain-containing-protein	unknown	unknown	gnl|CDD|380141
NZ_CP044427.1|WP_158061717.1|2621563_2622271_-|ABC-transporter-permease	unknown	unknown	unknown
NZ_CP044427.1|WP_158061703.1|2602225_2606149_-|DNA-directed-RNA-polymerase-subunit-beta'	unknown	unknown	gnl|CDD|234794
NZ_CP044427.1|WP_158061700.1|2598741_2600844_-|elongation-factor-G	unknown	unknown	gnl|CDD|234569
NZ_CP044427.1|WP_158061715.1|2620090_2620915_-|MerR-family-transcriptional-regulator	unknown	unknown	gnl|CDD|133382
NZ_CP044427.1|WP_158061702.1|2601450_2601825_-|30S-ribosomal-protein-S12	unknown	unknown	gnl|CDD|235355
NZ_CP044427.1|WP_158061714.1|2618535_2619987_-|argininosuccinate-synthase	unknown	unknown	gnl|CDD|235434
NZ_CP044427.1|WP_158061699.1|2597427_2598621_-|elongation-factor-Tu	unknown	unknown	gnl|CDD|234596
NZ_CP044427.1|WP_158061706.1|2610677_2611310_-|50S-ribosomal-protein-L10	unknown	unknown	gnl|CDD|234632
NZ_CP044427.1|WP_158061716.1|2620881_2621373_-|GyrI-like-domain-containing-protein	unknown	unknown	gnl|CDD|214874

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
NZ_CP044427.1|WP_158061707.1|2611666_2612968_+|MFS-transporter	gnl|CDD|340883	cd17325, MFS_MdtG_SLC18_like, bacterial MdtG-like and eukaryotic solute carrier 18 (SLC18) family of the Major Facilitator Superfamily of transporters. This family is composed of eukaryotic solute carrier 18 (SLC18) family transporters and related bacterial multidrug resistance (MDR) transporters including several proteins from Escherichia coli such as multidrug resistance protein MdtG, from Bacillus subtilis such as multidrug resistance proteins 1 (Bmr1) and 2 (Bmr2), and from Staphylococcus aureus such as quinolone resistance protein NorA. The family also includes Escherichia coli arabinose efflux transporters YfcJ and YhhS. MDR transporters are drug/H+ antiporters (DHA) that mediate the efflux of a variety of drugs and toxic compounds, and confer resistance to these compounds. The SLC18 transporter family includes vesicular monoamine transporters (VAT1 and VAT2), vesicular acetylcholine transporter (VAChT), and SLC18B1, which is proposed to be a vesicular polyamine transporter (VPAT). The MdtG/SLC18 family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	3.31516e-09
NZ_CP044427.1|WP_158061704.1|2606260_2609734_-|DNA-directed-RNA-polymerase-subunit-beta	gnl|CDD|234749	PRK00405, rpoB, DNA-directed RNA polymerase subunit beta; Reviewed.	0
NZ_CP044427.1|WP_158061710.1|2615319_2615748_-|50S-ribosomal-protein-L11	gnl|CDD|234661	PRK00140, rplK, 50S ribosomal protein L11; Validated.	8.34238e-87
NZ_CP044427.1|WP_158061711.1|2615841_2616696_-|transcription-termination/antitermination-protein-NusG	gnl|CDD|180161	PRK05609, nusG, transcription antitermination protein NusG; Validated.	3.47501e-84
NZ_CP044427.1|WP_158061712.1|2616758_2617031_-|preprotein-translocase-subunit-SecE	gnl|CDD|236066	PRK07597, secE, preprotein translocase subunit SecE; Reviewed.	2.39153e-17
NZ_CP044427.1|WP_158061709.1|2614462_2615176_-|50S-ribosomal-protein-L1	gnl|CDD|180071	PRK05424, rplA, 50S ribosomal protein L1; Validated.	1.59123e-144
NZ_CP044427.1|WP_158061705.1|2610217_2610610_-|50S-ribosomal-protein-L7/L12	gnl|CDD|234671	PRK00157, rplL, 50S ribosomal protein L7/L12; Reviewed.	1.40159e-43
NZ_CP044427.1|WP_158061713.1|2617141_2618476_+|pyridoxal-phosphate-dependent-aminotransferase	gnl|CDD|235596	PRK05764, PRK05764, aspartate aminotransferase; Provisional.	0
NZ_CP044427.1|WP_158061698.1|2596570_2597245_-|SMI1/KNR4-family-protein	gnl|CDD|378155	pfam09346, SMI1_KNR4, SMI1 / KNR4 family (SUKH-1). Proteins in this family are involved in the regulation of 1,3-beta-glucan synthase activity and cell-wall formation. Genome contextual information showed that SMI1 are primary immunity proteins in bacterial toxin systems.	1.0625e-05
NZ_CP044427.1|WP_158061701.1|2600980_2601451_-|30S-ribosomal-protein-S7	gnl|CDD|235398	PRK05302, PRK05302, 30S ribosomal protein S7; Validated.	3.34714e-105
NZ_CP044427.1|WP_158061708.1|2613218_2614208_-|type-IV-toxin-antitoxin-system-AbiEi-family-antitoxin-domain-containing-protein	gnl|CDD|380141	pfam18741, MTES_1575, REase_MTES_1575. Vsr REase Fold. Fused to HEPN (SWT1/Abi2 family), along with Transglutaminase and wHTH.	0.00141167
NZ_CP044427.1|WP_158061703.1|2602225_2606149_-|DNA-directed-RNA-polymerase-subunit-beta'	gnl|CDD|234794	PRK00566, PRK00566, DNA-directed RNA polymerase subunit beta'; Provisional.	0
NZ_CP044427.1|WP_158061700.1|2598741_2600844_-|elongation-factor-G	gnl|CDD|234569	PRK00007, PRK00007, elongation factor G; Reviewed.	0
NZ_CP044427.1|WP_158061715.1|2620090_2620915_-|MerR-family-transcriptional-regulator	gnl|CDD|133382	cd01107, HTH_BmrR, Helix-Turn-Helix DNA binding domain of the BmrR transcription regulator. Helix-turn-helix (HTH) multidrug-efflux transporter transcription regulator, BmrR and YdfL of Bacillus subtilis, and related proteins; N-terminal domain. Bmr is a membrane protein which causes the efflux of a variety of toxic substances and antibiotics. BmrR is comprised of two distinct domains that harbor a regulatory (effector-binding) site and an active (DNA-binding) site. The conserved N-terminal domain contains a winged HTH motif that mediates DNA binding, while the C-terminal domain binds coactivating, toxic compounds. BmrR shares the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements.	7.39575e-32
NZ_CP044427.1|WP_158061702.1|2601450_2601825_-|30S-ribosomal-protein-S12	gnl|CDD|235355	PRK05163, rpsL, 30S ribosomal protein S12; Validated.	1.36077e-85
NZ_CP044427.1|WP_158061714.1|2618535_2619987_-|argininosuccinate-synthase	gnl|CDD|235434	PRK05370, PRK05370, argininosuccinate synthase; Validated.	0
NZ_CP044427.1|WP_158061699.1|2597427_2598621_-|elongation-factor-Tu	gnl|CDD|234596	PRK00049, PRK00049, elongation factor Tu; Reviewed.	0
NZ_CP044427.1|WP_158061706.1|2610677_2611310_-|50S-ribosomal-protein-L10	gnl|CDD|234632	PRK00099, rplJ, 50S ribosomal protein L10; Reviewed.	9.55882e-67
NZ_CP044427.1|WP_158061716.1|2620881_2621373_-|GyrI-like-domain-containing-protein	gnl|CDD|214874	smart00871, AraC_E_bind, Bacterial transcription activator, effector binding domain. This domain is found in the probable effector binding domain of a number of different bacterial transcription activators.and is also present in some DNA gyrase inhibitors. The absence of a HTH motif in the DNA gyrase inhibitors is thought to indicate the fact that these do not bind DNA.	5.65643e-08

Protein sequences

>NZ_CP044427.1|WP_158061707.1|2611666_2612968_+|MFS-transporter
MTSSPSVRWFHRLVDAHPEAEREFGGAQRVATGGLRLIGANALQSAGDQVVNAKTVLPWLFSVLGAPAALVALLVPIRESGSMLPQAAFTPWVLRAPRRTRVWMLGASVQGVSVLAMAAVALTLTGALAGVAVLAALAVFAVGRALCSIASKDVQGRAVPKGQRGQVTGIATAVSGVIAVGVGVLLHLLGPNLSAGALAAFLTAAALTWFVGVLVYAGIPEDAPDAVARAQREPWLRDLVDLVRQDAAFRHFVAARALLLVSALAPPFLVTLAVAQGSSLLAGLGSFVIAQGIASVLGGRVFGRWSDRSSRRVMTYGSVVASLTVLAVVAVVLLAQPGLVVPGLVAGYFVISLVHVGVRVARKTYVIDLAEGDQRTRYVAVANTAMGVILLVTGAVSAGLATFGELPALVFLAVLGLVGAAVSWRLPEVSRTA
>NZ_CP044427.1|WP_158061706.1|2610677_2611310_-|50S-ribosomal-protein-L10
MATPQKAAAIVELTEMFRSSGAAVLTEYRGLKVSQITELRTSMREHATYAVVKNTLTKRAAAEAGITGLDEHLVGPTAIAFVTGDPVAAAKGLRDFAKANPALVIKAGVLDGKPLSPEEITKLADLESREVLLAMLAGAMKGNLSKAVGLFAAPLSATARVVDQLRAKVEEQGGPLPASEDAPAEADAEATPAEADAEAPTDVAEGGDES
>NZ_CP044427.1|WP_158061705.1|2610217_2610610_-|50S-ribosomal-protein-L7/L12
MAKLSTEELLDQFKEMTLIELSEFVKAFEETFEVTAAAPVAVAAAGGPAAGGGDAAAEEEQDEFDVVLEAAGDKKIQVIKEVRALTSLGLKEAKDLVDGAPKAVLEKVDKEAANKAKEQLEGAGATVTVK
>NZ_CP044427.1|WP_158061704.1|2606260_2609734_-|DNA-directed-RNA-polymerase-subunit-beta
MAASRTAKKTVSTARTASGRLSFAKIREPLEVPDLLALQTESFDWLLGNEAWQARVAAAQADGRNDIPTTSGLEEIFEEISPIEDFSGSMSLSFRDHRFEEQKYSVEECQEKDMTYSAPLFVTAEFINNSTGEIKSQTVFMGDFPLMTPRGTFIVNGTERVVVSQLVRSPGVYFERSLDKTSDKDVYSAKIIPSRGAWLEFEIDKRDQVGVRVDRKRKQSVTVLLKALGWSNERILEEFGDYESIRLTLEKDHTTTQDEALLDIYRKLRPGEPPTKEAAQTLLDNLYFNPKRYDLAKVGRYKLNKKLGLQAPLEESVLGIDDVVATIKYMVALHAGDTTMDMPAGDTLVETDDIDHFGNRRLRSVGELIQNQVRTGLSRMERVVRERMTTQDVEAITPQTLINIRPVVASIKEFFGTSQLSQFMDQNNPLAGLTHKRRLSALGPGGLSRDRAGMEVRDVHPSHYGRMCPIETPEGPNIGLIGSLASYGRINPFGFVETPYRRVADGKVTDEVDYLSADEEDRFVIAQANARLDDDGTFLDERVLVRAREGEAVDVPAAEVEYMDVSAQQMVSAATAMIPFLEHDDANRALMGANMQRQAVPLVRAEAPLVGTGMEWRAALDSGDVVRATKAGVVQEVSADLVTVANDDGTYITYKIAKFTRSNQGNCYNQVVRVDVGDRVEEGQLVADGPATDGGEMALGRNLLVAFMPWEGYNYEDAIILSQRLVQDDVLSSIHIEEHEIDARDTKLGPEEITRDIPNVSEEVLADLDERGIIRIGAEVRDGDLLVGKVTPKGETELTPEERLLRAIFGEKAREVRDTSMKVPHGETGTVIGVKVFEREDGDELPPGVNQLVRVYVANRRKITDGDKLAGRHGNKGVISRILPVEDMPFLEDGTPVDVILNPLGVPGRMNIGQILELHLGWAAAQGWKIEGEPEWAELIPGDARETGPRTRVASPVFDGAGEEEIAGLLDSTTPTRDGDRLIDSGGKAKLFDGRSGEPFPEQISVGYMYILKLHHLVDDKIHARSTGPYSMITQQPLGGKAQFGGQRFGEMEVWALEAYGAAYALQELLTIKSDDVTGRVKVYESIVKGDNVPEPGIPESFKVLIKEMQSLCLNVEVLSSDGTQIDLRESDTEVFRAAEELGIDLSRREPSSVEEV
>NZ_CP044427.1|WP_158061703.1|2602225_2606149_-|DNA-directed-RNA-polymerase-subunit-beta'
MLDVNFFDELRIGLATAEDIRGWSHGEVKKPETINYRTLKPEKDGLFCEKIFGPTRDWECYCGKYKRVRFKGIICERCGVEVTRAGVRRERMGHIELAAPVTHIWYFKGVPSRLGYLLDLAPKDLEKVIYFAAYMITHVDEDGRHSDLPSLEAQIQNEKKVLENRRDADVEGRAKKLESDLAELEAEGARADAKRKVRDGAEREMNQIRRRADQQIERLEQVWDRFRNLKVQDLEGDEILYREMRDRFGMYFEGGMGAAALQKRLQTFDLTAEAAHLREIIATGKGQRKTRAIKRLKVVTSFLQTKNEPAGMVLDAVPVIPPDLRPMVQLDGGRFATSDLNDLYRRVINRNNRLKRLLDLGAPEIIVNNEKRMLQEAVDSLFDNGRRGRAVTGPGNRPLKSLSDMLKGKQGRFRQNLLGKRVDYSGRSVIVVGPQLRLHQCGLPKQMALELFKPFVMKRLVDLDHAQNIKSAKRMVERGRSVVWDVLEEVITDHPVLLNRAPTLHRLGIQAFEPQLVEGKAIQIHPLVCTAFNADFDGDQMAVHLPLSAEAQAEARILMLSSNNILKPADGRPVTMPTQDMIIGLFHLTSDAWVEPETAYLLDEDGNRHLRSFGSVAEARMAFDAGQIELGSTISLRLAQTAPPAGFELPEGTEVTEDGVASNFTLETTLGRAIFNDSLPPNYPYVTDVVDKKRLSGIVNDLAERYTKVQVAASLDSLKDSGFYWATRSGTTVAVSDVQTPERKVEILSTYEAKASKVQLQYERGLITDDERRQELIEIWTQATNEVARELETTMPKDNTIYRMVTSGARGNWFQLRQIAGMRGLMANPKGEIIPRPIKSNFREGLSVLEFFISTHGARKGLADTALRTADSGYLTRRLVDVSQDVIIREDDCGTERGFVMPIAQAGLSGGLRQHDDVETSVYARTLAESVERDGEVLAQAGIDLGDVVIDRLVEAGIEEVKVRSVLTCESLVGTCAKCYGRSLATGKLVDIGEAVGIIAAQSIGEPGTQLTMRTFHTGGVAGDDITQGLPRVVELFEARTPKAVAPIAEATGRVQVEDTDKTRRVVLTPDDGSEEQAYPVSRRSRLLVSDGDHVEVGTQLIVGAIDPKQVLRILGPRATQQHLVDQVQGVYRQQGVSIHDKHIEVIVRQMLRRITVIEAGDAELLPGTLVERGRFEGENRRVVSEGGRPASGRPELMGITKASLATDSWLSAASFQETTRVLTEAAMEAKSDPLLGLKENVILGKLIPAGTGLTRYRNLTVEPTEEAKAAAYAVPDYEDFDYAGAFGAGSGEAVRLDDLPMDEQRF
>NZ_CP044427.1|WP_158061702.1|2601450_2601825_-|30S-ribosomal-protein-S12
MPTINQLVRKGRADKVKKSDSPALKGNPQRRGVCTRVYTTTPKKPNSALRKVARVRLTSGVEVTAYIPGVGHNLQEHSIVLVRGGRVKDLPGVRYKIIRGSLDTQGVKGRNQARSRYGAKKEKK
>NZ_CP044427.1|WP_158061701.1|2600980_2601451_-|30S-ribosomal-protein-S7
MPRKGPAPKRPLIQDPVYGSQLVTQLVNKILTDGKKSTAERIVYGALEGCRAKSGTDPVQTLKRALDNVKPSLEVKSRRVGGATYQVPIEVKPGRSTTLALRWLTGYARQRREKTMTERLMNEILDASNGLGAAVKRREDTHKMADANKAFAHYRW
>NZ_CP044427.1|WP_158061700.1|2598741_2600844_-|elongation-factor-G
MAQDVLTDLRKVRNIGIMAHIDAGKTTTTERILFYTGRNHKMGETHDGASTTDWMEQEKERGITITSAAVTSFWHGTQINLIDTPGHVDFTVEVERNLRVLDGAVAVFDGKEGVEPQSETVWRQADKYGVPRMCFINKMDKMGADFYFSVQTMVDRLGASPLVMQLPIGAESDFVGVVDLLTMKALTWSLDTALGEAYDTGEIPADLQEKAEEYRNALVEKVAEADEELLEKYLGGEELTEEEIKKGVRALTLAGEVNPVFCGTAFKNKGVQPLLDAIVDYLPSPLDLPPTEGLKPGDEETVISRAPSTEEPFAALAFKIATHPFFGTLTYIRVYSGEISAGQAVMNATKGKRERLGKLFQMHANKENPVEKVSAGHIYAVIGLKDTTTGDTLCDMSEPIILESMTFPEPVIHVAIEPKTKGDQEKLGTAIQKLAQEDPTFTVRLDEETGQTVIGGMGELHLDILVDRMKREFKVEANVGAPQVAYRETIRRTVEKLDYTHKKQTGGSGQFAKVQISIEPMDTAEGELYTFDNSVTGGRIPREYIPSVDQGIQDAMQLGILAGYPLVGVKATLIDGAYHDVDSSEMAFKIAGSMAFKEAARKADPVLLEPVMAVEVRTPEDYMGEVIGDINSRRGQIQAMEDISGAKIVRAVVPLSEMFGYVGDLRSKTQGRANYTMQFDSYAEVPRNVAEEIIKKVRGE
>NZ_CP044427.1|WP_158061699.1|2597427_2598621_-|elongation-factor-Tu
MAKAKFERSKPHVNIGTIGHIDHGKTTLTAAISKVLHDKYPDLNEASPFDSIDKAPEERQRGITISIAHIEYQTEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTKEHVLLARQVGVPYIVVALNKSDMVDDEEIMELVEMEVRELLSSYEFPGDDLPVVRVSALRALEGDQKWVDSVAELMDTVDEYIPEPERDLDKPFMMPVEDVFTITGRGTVVTGRIERGVLKVNEEIEIVGIRETSAKTTVTGIEMFRKLLDEGRAGENVGLLLRGTKREDVERGQVIVKPGTITPHTEFEAQAYILSKDEGGRHTPFYDNYRPQFYFRTTDVTGVVHLPEGTEMVMPGDNTDMRVELIQPIAMEDGLMFNIREGGRTVGAGRVTKILK
>NZ_CP044427.1|WP_158061698.1|2596570_2597245_-|SMI1/KNR4-family-protein
MTDSPSHTVPQVLTALSRVGKDVRTAPGASAQTLAAAASAVGGALPQDVLELYRATDGLELARGNLHLYPLLGTDVELGVVEAAAIHRSWDWVIPAELVLLGSDGGDGAFGVWVPAGARRSVVVQAVVSLDERPALAVLGTSLAGFLAAWAAYYLPLTLGETAGVSACLDDLGVPAALREGESELDDEHLHALLAWASPDLPDDEPDPYARPVDPAVLTRLATS
>NZ_CP044427.1|WP_158061708.1|2613218_2614208_-|type-IV-toxin-antitoxin-system-AbiEi-family-antitoxin-domain-containing-protein
METAIVALMEAQGGVASGVQLTALPGVTRHTVDALVRAKVLVRVRRGSFVLGRAFAGATAWERAELQARAVGRSLAADPGGHHALSHESALMMHGLPYFGDDGLVHLVRFDGGRGRHDDTIFVHRPVEVDWLVTVDGLHVVRPALAALQVAALHGAEAGLVCLDGVLHQAETRDRKDTGERQGLAHALVEEDIERALQEGFGTATRVVHEVAQLADGRSESVGESRSRWLLQLLGFGPLLLQFPVDLGDRTVYADLKLGRWAVLIEFDGRIKYGHPDALHTEKLREDALRALGYEVVRLTWGDLVNSRLVRQKILAAIARAEAAARATA
>NZ_CP044427.1|WP_158061709.1|2614462_2615176_-|50S-ribosomal-protein-L1
MKRSKAYRAAADKIEEGKFYAPREAVRLAKETASTKYDSTLEVALRLGVDPRKADQLVRGTVNLPNGTGKTARVVVLANGDKAEAARAAGADHVGSDDLIERIGGGWTDFDAVVATPDLMGKVGRLGKILGPRGLMPNPKTGTVTMDTAKAVTEIKGGKIEFRVDKHSNLHFIIGKASFDEAKLVENYGAAIDEILRLKPSSSKGRYVTKATVSTTMGPGIPVDPARVGSIVDPSSE
>NZ_CP044427.1|WP_158061710.1|2615319_2615748_-|50S-ribosomal-protein-L11
MPPKKKVSGFIKLQIQAGAATPAPPVGPALGQHGVNIMEFVKAYNAATESQRGNVIPVEITVYEDRSFTFVTKTPPAAELIKKAAGVAKGSGEPHKTKVASLTDQQLTEIAEMKMKDLNAIDVDMAKRIIAGTARSMGINTP
>NZ_CP044427.1|WP_158061711.1|2615841_2616696_-|transcription-termination/antitermination-protein-NusG
MSEQTPDHDEVTAEQSVQDADLEAAERFDGAVETDEAAPTDVEDEVYGEADDITTEAPAAQTADDAADEEPAEEEAAEEPVDPLEEFKENLRGRFGDWYVIHSYAGYENRVKHNLETRITSLNMEDYIFEVEVPMEEVTEIKNGQRKQVRRVRMPGYVLVRMELTDESWGAVRHTPGVTGFVGNAHQPVPLLIDEVVSMLAPVFETPATPEAKGEDAAGFKLPAGAPQIDFEVGESVTVMEGPFETLPATISEILPESNKLKVLVSIFGRETPVELSYNQVAKL
>NZ_CP044427.1|WP_158061712.1|2616758_2617031_-|preprotein-translocase-subunit-SecE
MTCRQGRRSVANPAHDTEGVARNQPGSGQPPRPATFVAQVMAELRKVVQPTRQELITYTIVVFVFVVVMIGFIFGMDQVFQRLVALVFAG
>NZ_CP044427.1|WP_158061713.1|2617141_2618476_+|pyridoxal-phosphate-dependent-aminotransferase
MPFTGCPALARRWGAGSRTVRTPEVAVYGTVRTGAKMVHVSEHTQKTRISRRIGAIAESATLAVDARAKELKAQGRPVIGFGAGEPDFPTPDYIVQAAIEAAHNPVNHRYSPAGGLPDLKAAIVAKTARESGYDVEPAHVLVTNGGKQAVYNTFATLLDPGDEVILPAPYWTTYPEAIRLAGGEPVEVFAGSDQGYLVTVEQLEAARTERTKVLLFCSPSNPTGAVYPPEQVEQIGRWALEHGIWVVTDEIYEHLVYDGGQAPSVRSVVPELADTCVVLNGVAKTYAMTGWRVGWMIGPKDVIKAATNLQSHATSNVANVSQRAAIAALAGSLEAVDTMRAAFDRRRATMVEMLSAIEGVHCPMPQGAFYAYPNIEGVLGRTIRGRTPQTSTELAEIILDEVEVAVVPGEAFGPSGYLRLSYALSDDDLIEGVSRIQTLLAKTR
>NZ_CP044427.1|WP_158061714.1|2618535_2619987_-|argininosuccinate-synthase
MSKVMTSIPVGERVGIAFSGGLDTSVAVAWMREKGAVPCTYTADIGQYDEPEIETVPGRARQYGSEIARLVDCRAELVEEGLVALACGAFHLRSGGRTYFNTTPLGRAVTGTMLIKAMKEDDVNIWGDGSTFKGNDIERFYRYGLLANSNLRIYKPWLDEAFVDELGGREEMSQWLSQRDLPYRASQEKAYSTDANIWGATHEAKTLEHLDTSMEIVEPIMGVAFWDEAEHIPAETVTVAFEHGRPVAINGEDFGGDSVRLVMRANEIGGRHGLGMADQIENRIIEAKSRGIYEAPGIALLHIVYERLVNAIHNEDTIAAYHNQGRVLGRLLYEGRWLDPQALMIRESLQRWVASAVTGEVTLRLRRGDDYTIVSTDGSTFSYHPDKLSMERVTNAAFGPTDRIGQLTMRNLDIADSRARLEQYVGMGLLGAGGAAASAMGLATTSLVGELTPGGADRIAGGVGPTEDEEEALDWAAMEFGTD
>NZ_CP044427.1|WP_158061715.1|2620090_2620915_-|MerR-family-transcriptional-regulator
MGGRSRILAEVSGAAKLSIGEFSRLTWLSPKALRLYERRGLLLPDLVDDYTGYRYYRPAQAERARTIALLRRVGMPLEQIGAVLDATGGQRHALIEAYRVEITRAHERAVALLDDLASAPADQQSPESMPTVRSRLVKPWAFISRTLRTTAADLPSHIERTAAALVQRAGASFDPGQPLIVVYHGEVSWESDGPIEVRVPIVDRAKADGIEPEGMEFFVDVPFGEVQFPTILRSFDAVRDAVAGDARRAWGSPRELYFDGDPFRCQVAQRYVET
>NZ_CP044427.1|WP_158061716.1|2620881_2621373_-|GyrI-like-domain-containing-protein
MTDFTIEDRAERAWVGVSTTGELAHWGRVNAYVPQIYAALTAAGGIPQGGPIYQYHRMQTVSDPMDITVSVPVAARIELGESFETGVIPAGRYLTARPEGGPDVLVQVHGEMWQWASVQGLELAIEERADGIHWRARTEQFLTDPQTEPDRSKWAVEVAYLLK
>NZ_CP044427.1|WP_158061717.1|2621563_2622271_-|ABC-transporter-permease
MNLTLSRLALQALVGQRRGLVLLALPLLLVALAAVVRMLTGDPVGGQTILIEIGLGIVVPIVALLAANGVLGPEIDDGSVVYLLSTPVSRYVVAVSKWATAAGVSVLLSAGGLAAAALAGGLGADWVLGSAAAGAIGAVLYTALFTAFSAATRHGMIAGLVYVLILEGALASLLTGLRYVSVQAITQRLAEALSELDLGVAMGLGYAVVAALFVLVAGVGGAGWRLQRFQLRGDE

Crispr_ID: NZ_CP044427_6

• CRISPR_ID: NZ_CP044427_6
• CRISPR_location: 3034031-3034132
• CRISPR_type: Orphan
• Repeat_type: NA
• Spacer_info: 1 spacers

Consensus repeat of NZ_CP044427_6

Consensus_repeat	Method
CCCCCCACCGGGAACACGGTCTGCCCCCCACCGG	CRISPRCasFinder

spacers of NZ_CP044427_6

>6.1|3034065|34|NZ_CP044427|CRISPRCasFinder
CAACACGGTCTGCCCCCACCGGCGACACGCTCTG

CRISPR arrays and Neighbor proteins around NZ_CP044427_6

CRISPR arrays

The CRISPR arrays of NZ_CP044427_6

>merge|NZ_CP044427|6|3034031-3034132|CRISPRCasFinder
CCCCCCACCGGGAACACGGTCTGCCCCCCACCGGCAACACGGTCTGCCCCCACCGGCGACACGCTCTGCCCCCCACCGGCAACACGGTCTGCCCCCCACCGG

>NZ_CP044427|6|6|3034031-3034132|CRISPRCasFinder
CCCCCCACCGGGAACACGGTCTGCCCCCCACCGG	CAACACGGTCTGCCCCCACCGGCGACACGCTCTG
CCCCCCACCGGCAACACGGTCTGCCCCCCACCGG

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP044427.1|WP_158062154.1|3040320_3040710_-|6-carboxytetrahydropterin-synthase	unknown	unknown	gnl|CDD|376501
NZ_CP044427.1|WP_158062139.1|3031035_3031617_-|dCTP-deaminase	unknown	unknown	gnl|CDD|234753
NZ_CP044427.1|WP_158062144.1|3034229_3034697_+|DUF664-domain-containing-protein	unknown	unknown	gnl|CDD|368218
NZ_CP044427.1|WP_158062138.1|3030203_3031019_-|M15-family-metallopeptidase	unknown	unknown	gnl|CDD|350624
NZ_CP044427.1|WP_158062147.1|3035679_3037101_+|GTP-cyclohydrolase-II	unknown	unknown	gnl|CDD|238348
NZ_CP044427.1|WP_158062159.1|3043071_3043926_-|ABC-transporter-ATP-binding-protein	unknown	unknown	gnl|CDD|224048
NZ_CP044427.1|WP_158062135.1|3026417_3027353_-|cysteine-synthase-A	unknown	unknown	gnl|CDD|273463
NZ_CP044427.1|WP_158062151.1|3037793_3038999_+|cell-wall-binding-repeat-containing-protein	unknown	unknown	gnl|CDD|367829
NZ_CP044427.1|WP_158062155.1|3040780_3041746_-|zinc-binding-alcohol-dehydrogenase	unknown	unknown	gnl|CDD|176217
NZ_CP044427.1|WP_158062127.1|3024142_3024478_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP044427.1|WP_158062136.1|3030072_3030408_-|M15-family-metallopeptidase	unknown	unknown	gnl|CDD|350624
NZ_CP044427.1|WP_158062142.1|3032363_3034022_+|AMP-binding-protein	unknown	unknown	gnl|CDD|236236
NZ_CP044427.1|WP_158062152.1|3039118_3040324_-|glycosyltransferase-family-4-protein	unknown	unknown	gnl|CDD|340831
NZ_CP044427.1|WP_158062157.1|3041881_3042979_-|P1-family-peptidase	unknown	unknown	gnl|CDD|225732
NZ_CP044427.1|WP_158062149.1|3037097_3037583_+|DUF664-domain-containing-protein	unknown	unknown	gnl|CDD|368218
NZ_CP044427.1|WP_158062141.1|3031866_3032286_-|divalent-cation-tolerance-protein-CutA	unknown	unknown	gnl|CDD|376987
NZ_CP044427.1|WP_158062129.1|3024608_3024812_-|cold-shock-protein	unknown	unknown	gnl|CDD|224197
NZ_CP044427.1|WP_158062146.1|3034839_3035556_+|HAD-family-hydrolase	unknown	unknown	gnl|CDD|223620
NZ_CP044427.1|WP_158062131.1|3025254_3025635_+|YtxH-domain-containing-protein	unknown	unknown	gnl|CDD|378938
NZ_CP044427.1|WP_158062133.1|3025797_3026418_-|serine-O-acetyltransferase	unknown	unknown	gnl|CDD|223975

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
NZ_CP044427.1|WP_158062154.1|3040320_3040710_-|6-carboxytetrahydropterin-synthase	gnl|CDD|376501	pfam01242, PTPS, 6-pyruvoyl tetrahydropterin synthase. 6-Pyruvoyl tetrahydrobiopterin synthase catalyzes the conversion of dihydroneopterin triphosphate to 6-pyruvoyl tetrahydropterin, the second of three enzymatic steps in the synthesis of tetrahydrobiopterin from GTP. The functional enzyme is a hexamer of identical subunits.	3.3316e-30
NZ_CP044427.1|WP_158062139.1|3031035_3031617_-|dCTP-deaminase	gnl|CDD|234753	PRK00416, dcd, deoxycytidine triphosphate deaminase; Reviewed.	1.61852e-95
NZ_CP044427.1|WP_158062144.1|3034229_3034697_+|DUF664-domain-containing-protein	gnl|CDD|368218	pfam04978, DUF664, Protein of unknown function (DUF664). This family is commonly found in Streptomyces coelicolor and is of unknown function. These proteins contain several conserved histidines at their N-terminus that may form a metal binding site.	1.09862e-08
NZ_CP044427.1|WP_158062138.1|3030203_3031019_-|M15-family-metallopeptidase	gnl|CDD|350624	cd14852, LD-carboxypeptidase, L,D-carboxypeptidase DacB and LdcB, and related proteins. This L,D-carboxypeptidase family includes LdcB LD-Carboxypeptidase from Streptococcus pneumoniae, Bacillus anthracis, and Bacillus subtilis, and L,D-carboxypeptidase DacB from Streptococcus pneumonia and Lactococcus lactis. These enzymes are active against cell-wall-derived tetrapeptides and synthetic tetrapeptides lacking the sugar moiety but are inactive against tetrapeptides terminating in L-alanine. L,D-carboxypeptidase DacB plays a key role in the remodeling of S. pneumoniae peptidoglycan during cell division. It adopts a zinc-dependent carboxypeptidase fold and acts as an L,D-carboxypeptidase towards the tetrapeptide L-Ala-D-iGln-L-Lys-D-Ala of the peptidoglycan stem. This family also includes vanY D-Ala-D-Ala carboxypeptidase which is vancomycin-inducible and penicillin-resistant. VanY hydrolyzes depsipeptide- and D-alanyl-D-alanine-containing peptidoglycan precursors; it is insensitive to beta-lactams. All these enzymes belong to the MEROPS family M15 subfamily B.	7.77415e-29
NZ_CP044427.1|WP_158062159.1|3043071_3043926_-|ABC-transporter-ATP-binding-protein	gnl|CDD|224048	COG1123, COG1123, ATPase components of various ABC-type transport systems, contain duplicated ATPase [General function prediction only].	9.31303e-116
NZ_CP044427.1|WP_158062135.1|3026417_3027353_-|cysteine-synthase-A	gnl|CDD|273463	TIGR01136, Cysteine_synthase, cysteine synthase. This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and CysM) from cystathionine beta-synthase, a protein found primarily in eukaryotes and carrying a C-terminal CBS domain lacking from this protein. Bacterial proteins lacking the CBS domain but otherwise showing resemblamnce to cystathionine beta-synthases and considerable phylogenetic distance from known cysteine synthases were excluded from the seed and score below the trusted cutoff. [Amino acid biosynthesis, Serine family].	4.0511e-163
NZ_CP044427.1|WP_158062151.1|3037793_3038999_+|cell-wall-binding-repeat-containing-protein	gnl|CDD|367829	pfam04122, CW_binding_2, Putative cell wall binding repeat 2. This repeat is found in multiple tandem copies in proteins including amidase enhancers and adhesins.	7.32323e-15
NZ_CP044427.1|WP_158062155.1|3040780_3041746_-|zinc-binding-alcohol-dehydrogenase	gnl|CDD|176217	cd08255, 2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_like, 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members. This subgroup of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family has members identified as 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide A dehydrogenase and alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.	1.01723e-63
NZ_CP044427.1|WP_158062147.1|3035679_3037101_+|GTP-cyclohydrolase-II	gnl|CDD|238348	cd00641, GTP_cyclohydro2, GTP cyclohydrolase II (RibA). GTP cyclohydrolase II catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5' phosphate, formate, pyrophosphate (APy), and GMP in the biosynthetic pathway of riboflavin. Riboflavin is the precursor molecule for the synthesis of the coenzymes flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD) which are essential to cell metabolism. The enzyme is present in plants and numerous pathogenic bacteria, especially gram negative organisms, who are dependent on endogenous synthesis of the vitamin because they lack an appropriate uptake system. For animals and humans, which lack this biosynthetic pathway, riboflavin is the essential vitamin B2. GTP cyclohydrolase II requires magnesium ions for activity and has a bound catalytic zinc. The functionally active form is thought to be a homodimer. A paralogous protein is encoded in the genome of Streptomyces coelicolor, which converts GTP to 2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (FAPy), an activity that has otherwise been reported for unrelated GTP cyclohydrolases III.	1.61771e-88
NZ_CP044427.1|WP_158062146.1|3034839_3035556_+|HAD-family-hydrolase	gnl|CDD|223620	COG0546, Gph, Predicted phosphatases [General function prediction only].	4.79256e-13
NZ_CP044427.1|WP_158062142.1|3032363_3034022_+|AMP-binding-protein	gnl|CDD|236236	PRK08315, PRK08315, AMP-binding domain protein; Validated.	0
NZ_CP044427.1|WP_158062152.1|3039118_3040324_-|glycosyltransferase-family-4-protein	gnl|CDD|340831	cd03801, GT4_PimA-like, phosphatidyl-myo-inositol mannosyltransferase. This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.	3.60201e-23
NZ_CP044427.1|WP_158062157.1|3041881_3042979_-|P1-family-peptidase	gnl|CDD|225732	COG3191, DmpA, L-aminopeptidase/D-esterase [Amino acid transport and metabolism / Secondary metabolites biosynthesis, transport, and catabolism].	1.44626e-80
NZ_CP044427.1|WP_158062149.1|3037097_3037583_+|DUF664-domain-containing-protein	gnl|CDD|368218	pfam04978, DUF664, Protein of unknown function (DUF664). This family is commonly found in Streptomyces coelicolor and is of unknown function. These proteins contain several conserved histidines at their N-terminus that may form a metal binding site.	2.51217e-14
NZ_CP044427.1|WP_158062141.1|3031866_3032286_-|divalent-cation-tolerance-protein-CutA	gnl|CDD|376987	pfam03091, CutA1, CutA1 divalent ion tolerance protein. Several gene loci with a possible involvement in cellular tolerance to copper have been identified. One such locus in eubacteria and archaebacteria, cutA, is thought to be involved in cellular tolerance to a wide variety of divalent cations other than copper. The cutA locus consists of two operons, of one and two genes. The CutA1 protein is a cytoplasmic protein, encoded by the single-gene operon and has been linked to divalent cation tolerance. It has no recognized structural motifs. This family also contains putative proteins from eukaryotes (human and Drosophila).	2.21949e-40
NZ_CP044427.1|WP_158062129.1|3024608_3024812_-|cold-shock-protein	gnl|CDD|224197	COG1278, CspC, Cold shock proteins [Transcription].	2.39723e-35
NZ_CP044427.1|WP_158062136.1|3030072_3030408_-|M15-family-metallopeptidase	gnl|CDD|350624	cd14852, LD-carboxypeptidase, L,D-carboxypeptidase DacB and LdcB, and related proteins. This L,D-carboxypeptidase family includes LdcB LD-Carboxypeptidase from Streptococcus pneumoniae, Bacillus anthracis, and Bacillus subtilis, and L,D-carboxypeptidase DacB from Streptococcus pneumonia and Lactococcus lactis. These enzymes are active against cell-wall-derived tetrapeptides and synthetic tetrapeptides lacking the sugar moiety but are inactive against tetrapeptides terminating in L-alanine. L,D-carboxypeptidase DacB plays a key role in the remodeling of S. pneumoniae peptidoglycan during cell division. It adopts a zinc-dependent carboxypeptidase fold and acts as an L,D-carboxypeptidase towards the tetrapeptide L-Ala-D-iGln-L-Lys-D-Ala of the peptidoglycan stem. This family also includes vanY D-Ala-D-Ala carboxypeptidase which is vancomycin-inducible and penicillin-resistant. VanY hydrolyzes depsipeptide- and D-alanyl-D-alanine-containing peptidoglycan precursors; it is insensitive to beta-lactams. All these enzymes belong to the MEROPS family M15 subfamily B.	1.13699e-27
NZ_CP044427.1|WP_158062131.1|3025254_3025635_+|YtxH-domain-containing-protein	gnl|CDD|378938	pfam12732, YtxH, YtxH-like protein. This family of proteins is found in bacteria. Proteins in this family are typically between 100 and 143 amino acids in length. The N-terminal region is the most conserved. Proteins is this family are functionally uncharacterized.	0.000337626
NZ_CP044427.1|WP_158062133.1|3025797_3026418_-|serine-O-acetyltransferase	gnl|CDD|223975	COG1045, CysE, Serine acetyltransferase [Amino acid transport and metabolism].	4.53292e-82

Protein sequences

>NZ_CP044427.1|WP_158062142.1|3032363_3034022_+|AMP-binding-protein
MADTANATAHPARSHAVGSTDVPLLEQTIGDNLDSNARAHAEREALVEMATGRRWTYGELLTDVNRVARGFLASGVRRGDRVGIWAPNCAEWTIVQLATAKIGAILVNINPAYRTHELAYVLRQSGVSTIVVAESFKGSSYPSMVEEVRDECPDLVQVLVIGSPGWSAFLDGAHQVTRDRLVELQAQLTPQDPINIQYTSGTTGFPKGATLSHRNILNNAFFVGAGCGYTERDVICIPVPFYHCFGMVMGNLAAVSHGAAMVIPAPGFDASATLRAVREEQCTSLYGVPTMFIAEFALIDKGEGFSVEDLASVRTGIMAGSLCPASVMRRLIEAGITEMTICYGMTETSPVSTQTTPSDPFEKLTGTVGRVMPHLEIKIVDPATRDVVPRGTPGEFCTKGYSVMLGYWDEPERTAEVVQDGWMATGDIGVMDEEGYVEITGRIKDLVIRGGENIYPREVEEFLMGHPDVLDAQVVGVADPKYGEELMAWLRLKDGAELLTAESVREFCAGKLAHYKIPRYVRVIEEYPMTVTGKIRKVELREAGEQSLEGEG
>NZ_CP044427.1|WP_158062141.1|3031866_3032286_-|divalent-cation-tolerance-protein-CutA
MTNENGSGAAGGTTWPSAHISAAPALLEVRAAVPDTETGLALAHSLVAQQLAACVQVIGPITSVYSWQGEAQQGDEWLLLMKTTEDAFEAVSAVILAEHPYEVPEILGVRVTHALPAYAEWVRKHSDGISDAQLLHPHE
>NZ_CP044427.1|WP_158062139.1|3031035_3031617_-|dCTP-deaminase
MLLSDRDIRAQIDSGRVLLDPFEPGMIQPSSIDVRLDRYFRLFDNHKYPMIDPSQEQPELTRLIETGPEETFVLHPGEFVLASTFEQVTLPDDVAARVEGKSSLGRLGLLTHATAGFVDPGFTGHVTLELSNVATLPILLHPGMKIGQLCFFQLSSPAEHPYGSAPRGSHYQGQRGPTASRSFQSFHRTPIRD
>NZ_CP044427.1|WP_158062138.1|3030203_3031019_-|M15-family-metallopeptidase
MSVPAPAPHTEDVQPGRRPPRPLRLDRRRRRLVLQPRRASALSLVAVVAVSGIFVTRGGMPFSGAGSAEDQVEVQGAGVAVQGEPCRAEPSGAEIASGPVGGAAFGASGLGCAIPVWQALPLITLEATDAQMLFSQVTREQAVDPIDYRPDDLVSMGGGPYQARAEVAEQLDALVATAAEAGHPSLTVTSGFRSYETQAGTFADWAGRLGEERADILSARPGHSEHQLGLAVDLGGPVTISASATPRRDSGSPRTPTAGVSSSATRRAARP
>NZ_CP044427.1|WP_158062136.1|3030072_3030408_-|M15-family-metallopeptidase
MGGPFGGGARRHSLGPARAQRASAWPGRRPRGTCNYQCFGDSPEGQWVAENAHRWGFIIRYPQGGQAVTGYAWEPWHLRYVGPRAAWGMHLADEAYWEHFQPVAARAAGLD
>NZ_CP044427.1|WP_158062135.1|3026417_3027353_-|cysteine-synthase-A
MAVYDDITQTIGRTPLVRLNRLTEGIAEGAQVLVKLESANPANSVKDRIGAAIIDAAVESGELEPGGTIVEGTSGNTGIALAMVGAARGYKVVLAMPETMSVERRALLRAYGAELVLTPGAEGMKGAVAKADEIAEKEGAVRARQFANPANIAVHRATTGPEIWADTDGKIDIFVSGVGTGGTITGGGGYLKEQNPDLHLVVVEPADSPILSGGQPGPHKIQGLGANFIPDILDTDLYDEVADVTLDDSVRVARDLATQEGILAGISSGAIVHAALEVARRPESAGKTIVAIVCDFGERYLSTVLFEGLTD
>NZ_CP044427.1|WP_158062133.1|3025797_3026418_-|serine-O-acetyltransferase
MLAALVRTPGRAAGLLRRAAAGVREDLDAAIARDPATDSRLEMALASPGLHAIWTHRVSHELWDRGATLPARVISHVARAATGVEIHPGATIGRRFFIDHGMGVVIGETAEVGDDVMLYHGVTLGGRSLEPVKRHPTLGDGVTIGAGAKVLGNITLGHGAQVGANAVVTKDVPSMCVATGIPAKVRPCEPGTDPEATLYDEPALWI
>NZ_CP044427.1|WP_158062131.1|3025254_3025635_+|YtxH-domain-containing-protein
MRNKLMLLIAGGAGYVLGARAGRERYDEIADRANKLWTDPRVQEKVEEVKAKAPEVAQKVGDQAKSKADDLRSKAGGNGSNDMGGGSGGASDSSGGGYGNATGEVTGDGEIKVDDSGFGPGGDRLP
>NZ_CP044427.1|WP_158062129.1|3024608_3024812_-|cold-shock-protein
MAQGTVKWFNSEKGFGFIAQDGGGPDVFVHYSAIQTNGYKALDEAQRVEFEVTQGPKGPQADAVRPL
>NZ_CP044427.1|WP_158062127.1|3024142_3024478_-|hypothetical-protein
MSVSSSTGVVVISASSVSGASVSGAVVTAASSVASSVACAGSGGSTAYRASHTHMRIWEKLGLAVSMLEEVSGRLCICPPWTSSISSAHSSRSETGMSVTMLSPTAPMICG
>NZ_CP044427.1|WP_158062144.1|3034229_3034697_+|DUF664-domain-containing-protein
MAQDERVEDSMTGRYCLAKLDEMIDVVRGLDDETANAAPGLTGANSAYQILSHCLGMARQWTAEHILGEPTGRDRAAEFGARGDVAELVARARATRDQLAVDLSRMEPGMQVPGRPGVDTFWSHDVEGILLHVLEELCQHLGHLEITRDLVTRGS
>NZ_CP044427.1|WP_158062146.1|3034839_3035556_+|HAD-family-hydrolase
MAEEQEAWSDAQRERARQQVTSAALVLVDFDGPLARLLPGDRWREVAAQVRARAGELGGPELETALDGAPDHVQCLRRVHELAPGIVPPLVEEVTRLELAAAAQVDPADYAVEFIEQCLDRGSAVVVVTNNDPHVVARVLDPHRPRLSARLTAILGRDPDRLDALKPSPAMLLDALKLTGAQAQDAVFLGDSVTDVEAGRAAGVPVVGVAEEAERRAELLAAGALAAVPGVGHLLRPR
>NZ_CP044427.1|WP_158062147.1|3035679_3037101_+|GTP-cyclohydrolase-II
MGRTILGGVTSSLAIPLPDPSSVERLADTVLPTRHGTFRMTAYRDDVGLEHVVLSVGITDESAPGHHIGRAPLVRVHSECLTGDALGSRRCDCGEQLQRALHLIMQDGYGALVYVGGHEGRGIGLVEKLRAYELQDTGVDTVDANLRLGHDADQRTYGQTAAMLKDLGIRVVRLLSCNPAKQEALTELGVRVVSRQSLIVPRRPENAAYLRTKRERMGHDPESVDEWQALLHGGGVLTTGVLTERYADLVHPDGPKVIAQLGQSMDGFIASRTGDAVFVTGEEDREHLHRLRALVDAVVVGSATAAADDPQLTVRAVPGPHPTRVVLDPRGTLPGDSRLLTDATAPTLWIVGQGVEPVPAGDHVEVVAWHSEGPMDPAGVLSLLRERGLERVLVEGGGRLVTAFVEAGMVDRLYLTVAPVLIGDGVPGLRLAGTDRLADALRPPVVRRWQAGEDIVTELDLAATRTASRVMPV
>NZ_CP044427.1|WP_158062149.1|3037097_3037583_+|DUF664-domain-containing-protein
MTGELTVLLEHLHTERQHILAAVDGLVEEDMTRVAAPSGWSIAQLLNHLTYDDEIFWGCAIVGGDEEAVALLREGWKVPVTSGAQAVERYQYWSSRVDVVLAEADLDAPPRWWPPESIFPFPPFAQARHCVFRLLLETATHAGHLDMAREAIDGHQHLVVD
>NZ_CP044427.1|WP_158062151.1|3037793_3038999_+|cell-wall-binding-repeat-containing-protein
MRSLTTSLAVILLVATGSAPTTRGDSAPSAGESVVVAEEGRLPALTREDAEAIRLHAARALAAQPSRTAYLDSHSQSSSGFVHPVVTRHSGSDRYATAAALAIARWRDVIWADVDGVPYPHDRVILIASGQDFPDALSGGALAAYYGGPMLLTRKDSLPGATRTALAALDPDYIAVLGGTNAVSDAVVRELAQYVAGSRRVVRYGGKDRYEVSATMARDIFGGGFGQRAYVALGTNWPDGLAGAATAGSDWAPLLLTRKDGVPGVVMQTLARARPEEIVLLGGPAAVNDTVVMQLGTVAPVVRVGGADRYAVAANAAGLDPTRFGATIASGQNWPDALSGSAYAGLVGDKLLLVRSNGVPGATQQAVRAGSLALIDAVGGRTTLPEPVLNQLRSLRVRTPG
>NZ_CP044427.1|WP_158062152.1|3039118_3040324_-|glycosyltransferase-family-4-protein
MRATLVVPDRDPAAPSGGDVYDARLAAHWPDDVQVCRAPGAWPHPTDADRVVLGRLLSGLGEDPVLIDGLVASTVPELVEASARIRATVVLVHSTLSAGSGAQGAAAEELDALELRALRAADLVATTSAWSAADLGRRYGIDGVILARPGVDPAPLSPGSGAAGGPGGADSSGRKDLPGHSGSVASAPQLLTLGALTPVKNHAALLVALAGLRDLDWGLTVAGPVPDREFADHLIGVARDLGLADRVTWPGPLDGVALEQTWAQTDLLAHPSRSETWGMVVTEAHARGIPTVVSRGTGAEEALGWDPVDTRGARGWRAPVENGLIDETTLGVAIAGAAVDTDAPDQLTHVLRRWLTGQATRAAWRSAALERRDRLPGWRETAQVLHDAVAQSVGGSAGPSA
>NZ_CP044427.1|WP_158062154.1|3040320_3040710_-|6-carboxytetrahydropterin-synthase
MFTLTVRDHVMVAHSLPDPFFGPAQGLHGATYVVETTWERPELDEHNVVLDIGAATESLGEILGRLRYRNLDEVPELADQVTTTEFLCRWIADELTESVDTSGLTGLTVTLREHPDAWASYRRELGAPA
>NZ_CP044427.1|WP_158062155.1|3040780_3041746_-|zinc-binding-alcohol-dehydrogenase
MQARAYWTLAPGTGQIRAQQISPPGPGEALVRAVVSGVSRGTELLAHRGEVPPEVAAQVAGPFEEGKLPGPVKHGYLSVGVVEDGEPEWVGRRVFCLHPHQDRYVVPVTALTPLPDDVPDERAVLVGTLETAVNALWDGRPLYGDRVAVVGAGMVGASVTALLAQLPLSRLELVETDPARRPLAEELGATGVAPQDASGDCDLVFHASATQAGLQTALELLGREGEVIELSWYGTTPVTVELGTTFHTRRLAVRASQVSRVSPHRPARDYADRMQVALRAARNPALDHLLAGPTPFEELPELMQRLAAGEPGLCHLVRYPD
>NZ_CP044427.1|WP_158062157.1|3041881_3042979_-|P1-family-peptidase
MSTWNAGPRNALTDVAGLAVGHHQRTGDGWLTGTTVILAPPEGAVGGVDVRGGGPGTRETALLDPRNLVERVHAVTLTGGSAFGLAAADGVMRRLYAEGRGFPMGGPGRVVPIVPGAVVFDLGRGGDFDNFPGPDFGEAACSAALQAQSAGEQPVLAQGSVGAGTGTQAGGLRGGVGSASVVIDGAVTVSALVVVNAVGSAVDPATGELWGARHLLEADVHGIPGWPDGALPSRPDAEEVESARRAAAETSTAGAVPRTLATTIGVVATDATLTKAQCARLASSGHDGMARGISPIHTMFDGDTLFGLSTASGPAPDPATFHQVLHAAGEVVTRAIVRALLAAESVTTPAGTWRSYRDAFPGAAR
>NZ_CP044427.1|WP_158062159.1|3043071_3043926_-|ABC-transporter-ATP-binding-protein
MVEESSPAVELRGVSREFRRPRTSVREKPPVVHAVRDVTLSIERGERFGIVGESGSGKSTLLRLICGLDHPTAGEVFVEGRPVHDQPGRRLGWLRQKVQLIFQDPMSSLDPRMRVGEIIAEPLVAQGRREGSRERVAELLERVGLSADMVDRYPHQFSGGQRQRISIARALAPGPDILVADEPVSALDVSVRAQVLNLIDEVVDGFDLTLIFVSHDLSVVRHTCDRIAVMQHGEVVEIAPTEQLFAAPQHPYTRSLLAAVPDLRRALAGQTTQDLAAGVRTPEP

Crispr_ID: NZ_CP044427_7

• CRISPR_ID: NZ_CP044427_7
• CRISPR_location: 3365527-3365635
• CRISPR_type: Orphan
• Repeat_type: NA
• Spacer_info: 1 spacers

Consensus repeat of NZ_CP044427_7

Consensus_repeat	Method
CTGCGGCTGCGGCGGTGGCGCACCCGCCGAG	CRISPRCasFinder

spacers of NZ_CP044427_7

>7.1|3365558|47|NZ_CP044427|CRISPRCasFinder
CAGGTGGCGCCGGAGCCGGCCGCGCAGGGCGGCTGCGGCTCAGGGGC

CRISPR arrays and Neighbor proteins around NZ_CP044427_7

CRISPR arrays

The CRISPR arrays of NZ_CP044427_7

>merge|NZ_CP044427|7|3365527-3365635|CRISPRCasFinder
CTGCGGCTGCGGCGGTGGCGCACCCGCCGAGCAGGTGGCGCCGGAGCCGGCCGCGCAGGGCGGCTGCGGCTCAGGGGCCTGCGGCTGCGGCGGCGGCGCACCCGCCGAG

>NZ_CP044427|7|7|3365527-3365635|CRISPRCasFinder
CTGCGGCTGCGGCGGTGGCGCACCCGCCGAG	CAGGTGGCGCCGGAGCCGGCCGCGCAGGGCGGCTGCGGCTCAGGGGC
CTGCGGCTGCGGCGGCGGCGCACCCGCCGAG

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP044427.1|WP_158062409.1|3372563_3373742_-|ABC-transporter-substrate-binding-protein	unknown	unknown	gnl|CDD|380667
NZ_CP044427.1|WP_158062406.1|3369745_3370576_-|ABC-transporter-ATP-binding-protein	unknown	unknown	gnl|CDD|213186
NZ_CP044427.1|WP_158062398.1|3353661_3354588_-|LysR-family-transcriptional-regulator	unknown	unknown	gnl|CDD|176115
NZ_CP044427.1|WP_158062402.1|3361609_3363988_-|bifunctional-salicylyl-CoA-5-hydroxylase/oxidoreductase	unknown	unknown	gnl|CDD|236203
NZ_CP044427.1|WP_158062410.1|3373863_3374277_-|RidA-family-protein	unknown	unknown	gnl|CDD|100004
NZ_CP044427.1|WP_158062880.1|3368082_3368862_+|PaaX-family-transcriptional-regulator	unknown	unknown	gnl|CDD|225864
NZ_CP044427.1|WP_158062401.1|3359387_3361613_-|acetyl-CoA-synthetase	unknown	unknown	gnl|CDD|131764
NZ_CP044427.1|WP_158062400.1|3357829_3359383_-|long-chain-fatty-acid--CoA-ligase	unknown	unknown	gnl|CDD|341286
NZ_CP044427.1|WP_158062397.1|3352569_3353625_+|saccharopine-dehydrogenase	unknown	unknown	gnl|CDD|240664
NZ_CP044427.1|WP_158062882.1|3374273_3375029_-|SDR-family-oxidoreductase	unknown	unknown	gnl|CDD|235546
NZ_CP044427.1|WP_158062881.1|3368981_3369704_-|ABC-transporter-ATP-binding-protein	unknown	unknown	gnl|CDD|213191
NZ_CP044427.1|WP_158062395.1|3350779_3351937_+|aminotransferase-class-I/II-fold-pyridoxal-phosphate-dependent-enzyme	unknown	unknown	gnl|CDD|224090
NZ_CP044427.1|WP_158062407.1|3370572_3371646_-|branched-chain-amino-acid-ABC-transporter-permease	unknown	unknown	gnl|CDD|119323
NZ_CP044427.1|WP_158062405.1|3365728_3366136_-|acyl-CoA-thioesterase	unknown	unknown	gnl|CDD|223894
NZ_CP044427.1|WP_158062879.1|3356297_3357812_-|methylmalonyl-CoA-mutase	unknown	unknown	gnl|CDD|239652
NZ_CP044427.1|WP_158062408.1|3371642_3372488_-|branched-chain-amino-acid-ABC-transporter-permease	unknown	unknown	gnl|CDD|119324
NZ_CP044427.1|WP_158062403.1|3364073_3364841_+|SDR-family-oxidoreductase	unknown	unknown	gnl|CDD|235546
NZ_CP044427.1|WP_158062411.1|3375118_3375916_+|1,4-dihydroxy-2-naphthoyl-CoA-synthase	unknown	unknown	gnl|CDD|180958
NZ_CP044427.1|WP_158062396.1|3352028_3352484_+|DUF3072-domain-containing-protein	unknown	unknown	gnl|CDD|371445
NZ_CP044427.1|WP_158062399.1|3354910_3356107_+|thiolase-family-protein	unknown	unknown	gnl|CDD|238383

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
NZ_CP044427.1|WP_158062409.1|3372563_3373742_-|ABC-transporter-substrate-binding-protein	gnl|CDD|380667	cd20014, PBP1_RPA0668_benzoate-like, type 1 periplasmic binding-protein component of an ABC system (RPA0668), involved in in the active transport of lignin-derived benzoate derivative compounds, and its close homologs. This group includes RPA0668 from Rhodopseudomonas palustris and its close homologs in other bacteria. Rpa0668 is the periplasmic binding-protein component of an ABC system that is involved in the active transport of lignin-derived benzoate derivative compounds. Members of this group has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP).	5.34202e-140
NZ_CP044427.1|WP_158062406.1|3369745_3370576_-|ABC-transporter-ATP-binding-protein	gnl|CDD|213186	cd03219, ABC_Mj1267_LivG_branched, ATP-binding cassette component of branched chain amino acids transport system. The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).	4.30888e-103
NZ_CP044427.1|WP_158062398.1|3353661_3354588_-|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.	2.67114e-51
NZ_CP044427.1|WP_158062402.1|3361609_3363988_-|bifunctional-salicylyl-CoA-5-hydroxylase/oxidoreductase	gnl|CDD|236203	PRK08255, PRK08255, bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase.	0
NZ_CP044427.1|WP_158062410.1|3373863_3374277_-|RidA-family-protein	gnl|CDD|100004	cd00448, YjgF_YER057c_UK114_family, YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site.	1.65589e-25
NZ_CP044427.1|WP_158062880.1|3368082_3368862_+|PaaX-family-transcriptional-regulator	gnl|CDD|225864	COG3327, PaaX, Phenylacetic acid-responsive transcriptional repressor [Transcription].	9.46786e-43
NZ_CP044427.1|WP_158062401.1|3359387_3361613_-|acetyl-CoA-synthetase	gnl|CDD|131764	TIGR02717, Uncharacterized_protein_MJ0590, acetyl coenzyme A synthetase (ADP forming), alpha domain. Although technically reversible, it is believed that this group of ADP-dependent acetyl-CoA synthetases (ACS) act in the direction of acetate and ATP production in the organisms in which it has been characterized. In most species this protein exists as a fused alpha-beta domain polypeptide. In Pyrococcus and related species, however the domains exist as separate polypeptides. This model represents the alpha (N-terminal) domain. In Pyrococcus and related species there appears to have been the development of a paralogous family such that four other proteins are close relatives. In reference, one of these (along with its beta-domain partner) was characterized as ACS-II showing specificity for phenylacetyl-CoA. This model has been constructed to exclude these non-ACS-I paralogs. This may result in new, authentic ACS-I sequences falling below the trusted cutoff.	1.30684e-109
NZ_CP044427.1|WP_158062400.1|3357829_3359383_-|long-chain-fatty-acid--CoA-ligase	gnl|CDD|341286	cd17631, FACL_FadD13-like, fatty acyl-CoA synthetase, including FadD13. This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.	9.8928e-158
NZ_CP044427.1|WP_158062397.1|3352569_3353625_+|saccharopine-dehydrogenase	gnl|CDD|240664	cd12188, SDH, Saccharopine Dehydrogenase NAD-binding and catalytic domains. Saccharopine Dehydrogenase (SDH) catalyzes the final step in the reversible NAD-dependent oxidative deamination of saccharopine to alpha-ketoglutarate and lysine, in the alpha-aminoadipate pathway of L-lysine biosynthesis. SHD is structurally related to formate dehydrogenase and similar enzymes, having a 2-domain structure in which a Rossmann-fold NAD(P)-binding domain is inserted within the linear sequence of a catalytic domain of related structure.	2.49763e-163
NZ_CP044427.1|WP_158062882.1|3374273_3375029_-|SDR-family-oxidoreductase	gnl|CDD|235546	PRK05653, fabG, 3-oxoacyl-ACP reductase FabG.	7.01473e-66
NZ_CP044427.1|WP_158062881.1|3368981_3369704_-|ABC-transporter-ATP-binding-protein	gnl|CDD|213191	cd03224, ABC_TM1139_LivF_branched, ATP-binding cassette domain of branched-chain amino acid transporter. LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.	3.54048e-98
NZ_CP044427.1|WP_158062395.1|3350779_3351937_+|aminotransferase-class-I/II-fold-pyridoxal-phosphate-dependent-enzyme	gnl|CDD|224090	COG1168, MalY, Bifunctional PLP-dependent enzyme with beta-cystathionase and maltose regulon repressor activities [Amino acid transport and metabolism].	3.32077e-111
NZ_CP044427.1|WP_158062407.1|3370572_3371646_-|branched-chain-amino-acid-ABC-transporter-permease	gnl|CDD|119323	cd06581, TM_PBP1_LivM_like, Transmembrane subunit (TM) of Escherichia coli LivM and related proteins. LivM is one of two TMs of the E. coli LIV-1/LS transporter, a Periplasmic Binding Protein (PBP)-dependent ATP-Binding Cassette (ABC) transporter involved in the uptake of branched-chain amino acids (AAs). These types of transporters generally bind type 1 PBPs. PBP-dependent ABC transporters consist of a PBP, two TMs, and two cytoplasmic ABCs, and are mainly involved in importing solutes from the environment. The solute is captured by the PBP, which delivers it to a gated translocation pathway formed by the two TMs. The two ABCs bind and hydrolyze ATP and drive the transport reaction. E. coli LivM forms a heterodimer with another TM, LivH, to generate the transmembrane pore. LivH is not included in this subgroup. The LIV-1/LS transporter is comprised of two TMs (LivM and LivH), two ABCs (LivG and LivF), and one of two alternative PBPs, LivJ (LIV-BP) or LivK (LS-BP). In addition to transporting branched-chain AAs including leucine, isoleucine and valine, the E. coli LIV-1/LS transporter is involved in the uptake of the aromatic AA, phenylalanine.	1.28436e-67
NZ_CP044427.1|WP_158062405.1|3365728_3366136_-|acyl-CoA-thioesterase	gnl|CDD|223894	COG0824, FcbC, Predicted thioesterase [General function prediction only].	2.39571e-14
NZ_CP044427.1|WP_158062879.1|3356297_3357812_-|methylmalonyl-CoA-mutase	gnl|CDD|239652	cd03680, MM_CoA_mutase_ICM_like, Coenzyme B12-dependent-methylmalonyl coenzyme A (CoA) mutase (MCM) family, isobutyryl-CoA mutase (ICM)-like subfamily; contains archaeal and bacterial proteins similar to the large subunit of Streptomyces cinnamonensis coenzyme B12-dependent ICM. ICM from S. cinnamonensis is comprised of a large and a small subunit. The holoenzyme appears to be an alpha2beta2 heterotetramer with up to 2 molecules of coenzyme B12 bound. The small subunit binds coenzyme B12. ICM catalyzes the reversible rearrangement of n-butyryl-CoA to isobutyryl-CoA, intermediates in fatty acid and valine catabolism, which in S. cinnamonensis can be converted to methylmalonyl-CoA and used in polyketide synthesis.	0
NZ_CP044427.1|WP_158062408.1|3371642_3372488_-|branched-chain-amino-acid-ABC-transporter-permease	gnl|CDD|119324	cd06582, TM_PBP1_LivH_like, Transmembrane subunit (TM) of Escherichia coli LivH and related proteins. LivH is one of two TMs of the E. coli LIV-1/LS transporter, a Periplasmic Binding Protein (PBP)-dependent ATP-Binding Cassette (ABC) transporter involved in the uptake of branched-chain amino acids (AAs). These types of transporters generally bind type 1 PBPs. PBP-dependent ABC transporters consist of a PBP, two TMs, and two cytoplasmic ABCs, and are mainly involved in importing solutes from the environment. The solute is captured by the PBP, which delivers it to a gated translocation pathway formed by the two TMs. The two ABCs bind and hydrolyze ATP and drive the transport reaction. E. coli LivH forms a heterodimer with another TM, LivM, to generate the transmembrane pore. LivM is not included in this subgroup. The LIV-1/LS transporter is comprised of two TMs (LivM and LivH), two ABCs (LivG and LivF), and one of two alternative PBPs, LivJ (LIV-BP) or LivK (LS-BP). In addition to transporting branched-chain AAs including leucine, isoleucine and valine, the E. coli LIV-1/LS transporter is involved in the uptake of the aromatic AA, phenylalanine.	3.44221e-50
NZ_CP044427.1|WP_158062403.1|3364073_3364841_+|SDR-family-oxidoreductase	gnl|CDD|235546	PRK05653, fabG, 3-oxoacyl-ACP reductase FabG.	6.23838e-72
NZ_CP044427.1|WP_158062411.1|3375118_3375916_+|1,4-dihydroxy-2-naphthoyl-CoA-synthase	gnl|CDD|180958	PRK07396, PRK07396, dihydroxynaphthoic acid synthetase; Validated.	1.75318e-117
NZ_CP044427.1|WP_158062396.1|3352028_3352484_+|DUF3072-domain-containing-protein	gnl|CDD|371445	pfam11272, DUF3072, Protein of unknown function (DUF3072). This bacterial family of proteins has no known function.	1.76318e-16
NZ_CP044427.1|WP_158062399.1|3354910_3356107_+|thiolase-family-protein	gnl|CDD|238383	cd00751, thiolase, Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA, a 2-step reaction involving a covalent intermediate formed with a catalytic cysteine. They are found in prokaryotes and eukaryotes (cytosol, microbodies and mitochondria). There are 2 functional different classes: thiolase-I (3-ketoacyl-CoA thiolase) and thiolase-II (acetoacetyl-CoA thiolase). Thiolase-I can cleave longer fatty acid molecules and plays an important role in the beta-oxidative degradation of fatty acids. Thiolase-II has a high substrate specificity. Although it can cleave acetoacyl-CoA, its main function is the synthesis of acetoacyl-CoA from two molecules of acetyl-CoA, which gives it importance in several biosynthetic pathways.	6.78254e-156

Protein sequences

>NZ_CP044427.1|WP_158062403.1|3364073_3364841_+|SDR-family-oxidoreductase
MEVGSFAGKVVVVTGGTGGIGRAVCEGFAEQGASVAVLDVRGTEQVASEVSKRYGVPAEGYELDVSDRSAVVRVMDAVVADLGGLDVLVTLAGGSLGTPKGLDEIEEEHVDLVVDVNVKGTFYCAQAALARMPDDGAVVTVSSIGGRQPSPVTGVPYAASKAAVLGLTRRLAREVGGRGQRVNAVAPGLFLTGRLQQMYDEMPAAERDEVLGAIPLGRFPELREIVDPVLFLAGPGASYITGVVLDVNGGRFMPL
>NZ_CP044427.1|WP_158062402.1|3361609_3363988_-|bifunctional-salicylyl-CoA-5-hydroxylase/oxidoreductase
MRIAIIGGGPGGLYFAALTKALDPSHEITVWERNAPDDTFGFGVVFSDETLGGIEHADRAVYEAMEAEFARWDDIDVHLDGQVWTSGGHGFAAMTRKRLLEILQARCRELGITLHFRSQAPDVDELAADYDLVLAADGLNSGVRHRYQDTFRPTLDARTCKYMWLGTTKVFDAFKFYVLRTQWGVMQVHGYPYDATGSTFILEMREDVWRAAGFDHAEDRAWVPGESDEESIARVQELCADIFEGHEVMANNSRWITFTTIRNETWRAGERGNIVILGDAAHTAHFSIGSGTKLAMEDALALAACLHEHDDLDAALSAYEEERKPVVESTQRAAQASLEWFENLDQYMDQEPEQFAFNIMTRSRRVTHDNLKVRDPEFVRQIDDWFARTTPGGRPDTPPMFQPFRLGGLELTNRIVVSPMDMYVSPGDGMPTDFHLVHLGGKAMGGAGLVMTEMVCTSPEGRITPGCTGIWTDEQAAAWRRIVDEVHRLSSAKIGLQVGHSGRKGSTKLMWEGMDQPLEEGNWEVVAPSPLPYRPGGSQVPRELTSEDLEAIKEEHVDAARRGAEAGFDLLELHCAHGYLLSSFISPVTNQRTDEYGGGGGAGLAGRLRYPLEVFTAMREVWPAERPMTVRISATDWVEGGIGVEDAVQIAQAFKDAGADAIDVSSGQVTPDEQPAFGRSYQTPFADAIRNRVGIPTIAVGIISSWDDVNSIVLAGRADLCAVGRAHLYNPNWTLHAAVEQDYDGPGAVWPLPWRAGRRKPQTGRSDGPKPRLQLVREGETGSRHARWRPGV
>NZ_CP044427.1|WP_158062401.1|3359387_3361613_-|acetyl-CoA-synthetase
MTSEQASASPLPARPDARPAALRPLWVARGIAVVGASDRAGAVGRLPVQFLQRYGYTGGIYPVRPDGAPVAGLTSYPSVEEAARAGEVDVAMVMVAADKVVAAVQDCAAAGVGVVIVCSSGFAETGPAGAALQDELVRVAGELGVRVLGPNCIGTVGTATGQVSSFSPLFSGASTQLVPGGIGFVSQSGALGYGAVSLAFERGLGLGWVVNTGNEADIGATEVMAALAEEQQPRCTGLLGYAESLGDLSSLARVTASGVPVAMLKAGRSDAGARAAASHTGALATGDKVVDAALRRAGVVRVDDVEELLDVGDVMVLVPLVQDRQVGSDGVPGRAPGAPLRQPGGARLRRIAVVTTSGGSGILAADAIEARGLELAALADDTLADLDQIVPAYGSTANPVDVTASVMSNPDLFDQALTTIAQDPGVDAIVACFCVLTGSDVDAVVQALARVRERTGVPVVVTRTGADHLAPDAAATMRAAGLPVYPTPARAVRAVAALAQFVQAGSRAGGNDRDQPAGHAPPDLWAHTDESSLKQALAGAGLPVPVGRLVSDRDDALAAVEQAGGQAVFKAVVPGLLHKSEAGGVVLDVTSERAAEVYDRLGALRGPDGSAGQVLVEEMVPPGVEVLVGSADTPLGRILTVGVGGVLTEVVADVALRLLPIDRQDVEEMVDETRLRLLLAGARGRPPADRAALVDTIAALADLAATLPAGAELDLNPITVLAEGDGVRILDAALALADEED
>NZ_CP044427.1|WP_158062400.1|3357829_3359383_-|long-chain-fatty-acid--CoA-ligase
MDVGTMLTRAGRRFGDRVAVEGSTAADRRSFAELADRVTRIASGLRALGLEPGDRVLDLQSNSTAYLETDLAIRAAGLVRVALNYRLHPSDWQRIATDCTARGLIYHERFADDIAPVREQVPHVVVVGEGPETDLEALATGATAGPLSVRDPGDLCGLHYSSGTTGHPKGAQRTHRNWFASVVNMTHDVLDGPPGPDDCYVHAGPVTHTSGLFVLPFFVAGARQIVLPTWDPQTFLEAVGERGATHTALVPTMVARLLSHGTTREDLAGLKMLGYAGAPMPPEQMRRAHERLTPHLVQYYGLVEAIPPVTVLDATDHARGLADQPELLTSAGRPALGVELAVVDEDGRPVPDGEVGEVITRGDHVMAGYYNAEQRTDLSKAVVDGWLHTGDLGRLSGDGHLWLIDRKGDMIISGGYNIYPREVEEVIAEVPEVGEVAVVGVADADWGQRVVALVTARAGAEVDPERVREHCATRMASYKKPKEVRVVSEFPLNSTGKIAKKVLRADLEQEQEQEGMP
>NZ_CP044427.1|WP_158062879.1|3356297_3357812_-|methylmalonyl-CoA-mutase
MRVDYAPEGAERPGQYPYSRGVSAEPKVWIMGQYAGFGTAKESNVRFRALLEAGVTGFSVAMDLPSQMGIDSDDPRAAGEVGRVGVAIDSLADIEVLMDGIPLEELSQVRTTANSIGYLWAALFVALAEKRGVHPDQFGMFIQNDVLKEFIARGTQIFPPEASLRLSVDTIEYVSREAPSWVPLAMSGYHIRESGASATQEIAFTFANARAYLDECVRRGVDVDQVAPTLFTFLAITTDVLPEVAKFRAARRVWARLMRERYGARDPRSEQLRIFAFTAGSTLTAQQPLNNVVRTSVEATVAALAGVQTLHVSAYDEALGVPTEHAATLALRTQQVVAFETGLTTTLDPLAGAYAVETLTDELEASIWSLMEDIEERGGALEAIGSGRFARDLAEAAYRHSQQVETGERTVVGVNKFPAPTEPLEVFTIDPGTEQAQAESVRRLRHTRDQTAVDSALAQLAQDVREGRSVMPATIEAVKAYATLGEVVEVLRDELGTWRPSAEF
>NZ_CP044427.1|WP_158062399.1|3354910_3356107_+|thiolase-family-protein
MLGEEVFLLDAVRTPFGKLRGGLSHVRTDDLAAVPLRSLLERHPGLDPARVEDVYYGNTNGAGEENRNVARMAALLAGLPVTVPGATTNRLCASGSEALVQAARSIAVGDADLVVAGGVEGMSRAPYVLPKPDEALPRAVELHQTTVGWRMVNPAFPAEWTTSLGASAQAVATERGIGREEMDEYAVRSHQRVHAAYEAAAHKGFVEPLEGVERDESLRPAASMETLGALRPAFTRDGTVTAGNSSPVNDGAMAALVGTAAMAQELGLEPIARIVASRTVAVSPEQFAVAPVPAIRQLLERTGKGFGDVDLWEINEAFAAMVLSTLHDLPELGRDALESHVNVNGGAIAIGHPLGASAPRVVVDLARELRRRGGGIGVAAACIGVGQGTALMIEVPRP
>NZ_CP044427.1|WP_158062398.1|3353661_3354588_-|LysR-family-transcriptional-regulator
MCKDCYMFNPEHLRTLRTVVEEGTLVAAADLMGLTPSAVSQQLARLQQEAGQAVLVRRGRNLAPTDAAAVLVRMAEEVQRLDESARAELERLTKDVSGPLVVGAFATAVRALLPAALTDLRRAHPHLAPTIREAEPELSLDLVRGGQLDLAVVHDWTDYRLTLPAGLSTHDIGQDVVDLVAPVGMSLPRRRDGRVDLHELDGQTWIDDTPGVYSDWLLGTLREAGLSYRIGATVDTYPGKLALAGAGFGVTLVPRLGRDLVPDSVVVLPLHDPPTRRVFLAHRQAAERRPAVEAAVRAIRRAWADLET
>NZ_CP044427.1|WP_158062397.1|3352569_3353625_+|saccharopine-dehydrogenase
MTRPHLWIRAEARPTEQRVPIVPADARRLIEDGFTVTVEESPTRVISLAEYVEAGCAVAPRGSWVDAPEGAVVVGIKELPEDPDDLAHTHVFFAHAYKGQEGADRVLDRFRRGGGELLDVEYLTVDGKRVVAFGFWAGYVGAALAVLRHRGLLTGGVSPMSREELDAMLQQGPALASGAPAGATAEPERALVIGSQGRSGTGAMAALAVAGCALTRWDRADTEVIDKNALLAHDIMVNCVASDRPREPFLATADVDVPRRLRTVADVTCDVTSEANLLPFNTAITTWEEPVRAFGSVGNPLEVIAIDNLPSLLPRESSESFSAELTPLLPDLADRQGPWAASLEWFRRHLR
>NZ_CP044427.1|WP_158062396.1|3352028_3352484_+|DUF3072-domain-containing-protein
MTFPTDPTQPPLDVPESDPTGNPGPDTPAPSQPVADPPQEPLPGSVPQPGPGPEPGADPAPEPLPRAAANNAQASEVLGSSTPQDDPGQLQRDPEEWVTGDDPATEAQKSYLDRLASSAGEQIPAEGLTKAQASEHIDRLQDRTGIEPRQS
>NZ_CP044427.1|WP_158062395.1|3350779_3351937_+|aminotransferase-class-I/II-fold-pyridoxal-phosphate-dependent-enzyme
MASPFDLTLEQLREHRSAKWSRVPADVLPAWTAEMDVRTAPAITDALHLAVERSDFGYAGDPAPVISAFTGFARDTWGWDPAEGGGTMRLFADVGQAAIEVLRAVTSPGDRVIINPPVYLSFYPWLQSVGVEPLEVPLLDVASGGRLDLAGMEHALASGARVVLLCTPHNPLGHVYTQEELAAVADLAAAHDALVISDEIHAPLVHPGSPTPFRPFLTVSEAARRVGIALHSPSKAWNIAGLKTAIGITATPGRWPGLREDLDWSSSILGQYAAVAAYTDSREWLGTVRAEVEQRTHQLVDLLAEHLPAVRYTPGHASYLAWLDCRDLGLGDNPAATFLERGKVALSPGPAFGIGGAGFARLNIGTSQELMTEAVRRMAAALHSG
>NZ_CP044427.1|WP_158062405.1|3365728_3366136_-|acyl-CoA-thioesterase
MTQVVVTRTVDWVDTDAAGHYHHSAVIRWVEAAENALHEELGLLDLFGTAPRVRYEVDYLDRLWFREQVGTTLWVEKVGTSSLAYAFEVVGPRGAAARGRMICVNVGAVDSAGSAGGACPWPPEVRERLESHADG
>NZ_CP044427.1|WP_158062880.1|3368082_3368862_+|PaaX-family-transcriptional-regulator
MTIYGLYAREVGGWLSVSTLIRLMTRLDVDEPAVRSSISRLKRRGILEPERIDGRAGYALSAQAREILDAGDRRIFRRRRGTVDEGWVLAVFSVPESERRRRHTLRSRLSWLGFGSVGPGVWVAPAHLYDEAREMLLREDLAEYVDLFQATYLGFSAAAEEVARWWDLEGLGELYEQFYAEHAPVLASWRARRGKDDAGMAFADYVRVLTAWRRLPYLDPGLAPELLPRDWAGTRSADLFFALQRRLEGPSHRFVDEVS
>NZ_CP044427.1|WP_158062881.1|3368981_3369704_-|ABC-transporter-ATP-binding-protein
MPPAPPSTPILATRGLVSGYDGSRVLHGVDIAIPEGGVLALLGRNGVGKSTLINTIMGLVRPMAGSVTVAGQEVAGARPDRIAKLGVGLVPQGRRVYGPLTVAEHLDISDRSGRQGAWTRERVIDLLPRLGERMRNRGDQLSGGEQQMLAIARALLTNPTILLLDEPSDGLAPAIVQQVGEVVREVCAAGMTVLVVEQNLRLALSVADHVVVMQKGAVHWDVSVDEFRRNRTRAEELLGI
>NZ_CP044427.1|WP_158062406.1|3369745_3370576_-|ABC-transporter-ATP-binding-protein
MTSRPDTRDTPHTQGSSGAPALRLHGLGKDFGSLSAVKDVSFDVAPGARHAVIGPNGAGKSTLFALVAGALPATAGTVMLHGDDVTKLSEHARARRGLVRTFQHSSLFLSATARENILIAVQRRHGVQGQPWRAVTRRRALLAEADEVLEQLMLQDRSGATAGSLSHGERRQLEVAVALATRPSVLLLDEPAAGMSPADTMAFQELVLGLPAEVTVLLVEHDLDLVFGVADRVTVLHLGEHLLTGDPDEVRASDAVQHAYLGAEDTSELFLEDGPG
>NZ_CP044427.1|WP_158062407.1|3370572_3371646_-|branched-chain-amino-acid-ABC-transporter-permease
MSTTQPAPQARQATRGARQGARPQADPRRPFRPDLRTSVVVGAVLVALLAIPWVLGTYAVMTFTKILIFAVLAMSVNLLTGITGLPTLGQAAYFGVGAYAGALTAIHFSELGIVQILVAVGAGVIAALLTGPVAIRARGVAFLMITLAIGEIAYSAAGQLHGITRGTDGLSGIPPVVVAPGMEGLRNQGYIYYYVLAVAILAYVLVAILLRSPLGLTLRGLRDNESRLRAVGYRTGSYALAAYVIAGGLAALAGSLWTSSQRFVAPGDMGFQVAALALLAVIVGGVGSMWGACLGAMVVIFTRDYLGQMASGHGPLLLGILFVLAVYLLPKGLAGGPRQWGGLLRRLRKSAAGEVEV
>NZ_CP044427.1|WP_158062408.1|3371642_3372488_-|branched-chain-amino-acid-ABC-transporter-permease
MIDGVAFGLLLFTLAVGLSLVFGMMDVLNLAHGTLYLAGAYTAYALSDGSWLGLLIAIVVGLLVGVLGGGLLAAAVAPLQGRGHLDQAALTLGISFIVAEIFLMVFSAETLSAAPPAALAGSITVLGYTYPLYRLVFIGVAGVLAALVYLAFERSSVGALVRATVADRDMVRAMGVDTRKILFGVFAFGAALATLGGVLGAPILAPGPHVDQRVLVLSLVVVVIGGLGSVRGALLGALLIGQVQTLGVALLPTYAPFLLFGAMLFVLAVRPQGLFATGKTA
>NZ_CP044427.1|WP_158062409.1|3372563_3373742_-|ABC-transporter-substrate-binding-protein
MTARPKTYLLALVAAGSLTLGACGGGTLGGGGDDDEGPVKIGLLVPQSGVYTSLGDDMRAGFEVYLDQHDNQLGGQEVEVILADEGETADSGRAAADRLVQQDQVHVVTGVVNSAVMNGIVDLFEGGEIPLVGSNASPTTLTDVEYIWRTSYVNDEPGEALGAYVAENTEGSVYFLAADYQAGIDEVTGFKSTFEPAAGEIAGEVYTPFPATTNFQPFLANARSSGAEAMFTFYAGGAAVEFVKQYEQFGLKDEITHYSAGFLTEGGVLDGQGDSALGTFTSMNYNYDLENELNAQFVADYEEKTDRKPTTYAMASYDAAKVLDLAIAEAGGPDSQAINEAIGGLGEIESPRGTWRFNDNGTPIQMWYLREVQEVDGELTNVVVEELGELGG
>NZ_CP044427.1|WP_158062410.1|3373863_3374277_-|RidA-family-protein
MIELVNPPELGQPKGFSHAVVGTGRTVFLAGQTALSPEGVIVGDTVVEQFERALSNLLVSLHAAGGEPTDLATLTIYIVDVDDYKAHGREIGKVWRKLMGAHYPATAGIGVARLWDLEALVEVQGMAVVEPREGLAD
>NZ_CP044427.1|WP_158062882.1|3374273_3375029_-|SDR-family-oxidoreductase
MEQPVALVTGAGRGIGAGVAAALSNEGYAVALTSRSRDQLEETAARCAGPTLVLPTDLTAPGAIEEVVDRVEQEWAAPQVVVANAGAGVSASVDRTTDEQWQQMLDLNLTAPFRLLRRTIPAMKQAEHGRIVVVASVAAKLGEPYISAYTASKHGVLGLVRSAAAELARTGVTVNAVCPGYVDTPMTAQTVQGIVDKTGRTPEQALAALEAKSPLHRLITVEEVVEAVLTCVRNSGMTGQGINVDGGGLQS
>NZ_CP044427.1|WP_158062411.1|3375118_3375916_+|1,4-dihydroxy-2-naphthoyl-CoA-synthase
MIRPEDFTDVTYEVEESWAVVTINRPERYNSFRGRTVDELIAALKHAWADSRVACVILTGAGEKAFCAGGDVKERAETGSYGETEWGLFQIQQLHQVIRDIPKPVIAAVNGVAVGGGHVLHVLCDLSVASSTARFGQSGPRVGSFDAGFGSAYLARVVGEKRARQIWFLLDLYDAETAERWGLVNDVVPPEQLMDKAREYAAKISSYSPTALRFLKHSFNADSDHMQGLGNIAFAGLDLFVQTEEAKEGANAFSEKRTPDFSPWR

Self-targeting detection

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_ID	Protospacer_location	Mismatch	Identity
NZ_CP044427_4	4.1|2170771|30|NZ_CP044427|CRISPRCasFinder	2170771-2170800	30	NZ_CP044427.1	1932282-1932311	1	0.967
NZ_CP044427_4	4.1|2170771|30|NZ_CP044427|CRISPRCasFinder	2170771-2170800	30	NZ_CP044427.1	362624-362653	2	0.933
NZ_CP044427_4	4.1|2170771|30|NZ_CP044427|CRISPRCasFinder	2170771-2170800	30	NZ_CP044427.1	1109279-1109308	2	0.933
NZ_CP044427_4	4.1|2170771|30|NZ_CP044427|CRISPRCasFinder	2170771-2170800	30	NZ_CP044427.1	1109302-1109331	2	0.933
NZ_CP044427_4	4.1|2170771|30|NZ_CP044427|CRISPRCasFinder	2170771-2170800	30	NZ_CP044427.1	1932259-1932288	2	0.933

1. spacer 4.1|2170771|30|NZ_CP044427|CRISPRCasFinder matches to position: 1932282-1932311, mismatch: 1, identity: 0.967

caaaccgtgtcgccggtcgggggcaaaccg	CRISPR spacer
caaaccgtgtccccggtcgggggcaaaccg	Protospacer
*********** ******************

2. spacer 4.1|2170771|30|NZ_CP044427|CRISPRCasFinder matches to position: 362624-362653, mismatch: 2, identity: 0.933

caaaccgtgtcgccggtcgggggcaaaccg	CRISPR spacer
caaagcgtgtcgccggtcgggggcaaagcg	Protospacer
**** ********************** **

3. spacer 4.1|2170771|30|NZ_CP044427|CRISPRCasFinder matches to position: 1109279-1109308, mismatch: 2, identity: 0.933

caaaccgtgtcgccggtcgggggcaaaccg	CRISPR spacer
caaaccgtgtcgccggtcagggacaaaccg	Protospacer
******************.***.*******

4. spacer 4.1|2170771|30|NZ_CP044427|CRISPRCasFinder matches to position: 1109302-1109331, mismatch: 2, identity: 0.933

caaaccgtgtcgccggtcgggggcaaaccg	CRISPR spacer
caaaccgtgtcgccggtcagggacaaaccg	Protospacer
******************.***.*******

5. spacer 4.1|2170771|30|NZ_CP044427|CRISPRCasFinder matches to position: 1932259-1932288, mismatch: 2, identity: 0.933

caaaccgtgtcgccggtcgggggcaaaccg	CRISPR spacer
caaaccgtgtccccggccgggggcaaaccg	Protospacer
*********** ****.*************

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity
NZ_CP044427_1	1.1|675759|28|NZ_CP044427|CRISPRCasFinder	675759-675786	28	NZ_AP014579	Burkholderia sp. RPE67 plasmid p1, complete sequence	1384835-1384862	4	0.857
NZ_CP044427_1	1.1|675759|28|NZ_CP044427|CRISPRCasFinder	675759-675786	28	NC_016626	Burkholderia sp. YI23 plasmid byi_1p, complete sequence	1237737-1237764	4	0.857
NZ_CP044427_1	1.1|675759|28|NZ_CP044427|CRISPRCasFinder	675759-675786	28	NZ_CP049734	Rhizobium leguminosarum strain A1 plasmid unnamed1, complete sequence	185350-185377	5	0.821
NZ_CP044427_1	1.1|675759|28|NZ_CP044427|CRISPRCasFinder	675759-675786	28	CP049734	Rhizobium leguminosarum strain A1 plasmid pRLa11, complete sequence	302589-302616	5	0.821
NZ_CP044427_1	1.1|675759|28|NZ_CP044427|CRISPRCasFinder	675759-675786	28	NC_022995	Burkholderia sp. M701 plasmid pM7012 DNA, complete sequence	386522-386549	6	0.786
NZ_CP044427_1	1.1|675759|28|NZ_CP044427|CRISPRCasFinder	675759-675786	28	NZ_CP034950	Enterococcus faecium strain NM213 plasmid unnamed1, complete sequence	4578-4605	6	0.786
NZ_CP044427_1	1.1|675759|28|NZ_CP044427|CRISPRCasFinder	675759-675786	28	NZ_CP035169	Lactobacillus plantarum strain SRCM103418 plasmid unnamed1	47167-47194	6	0.786
NZ_CP044427_1	1.1|675759|28|NZ_CP044427|CRISPRCasFinder	675759-675786	28	NZ_CP035115	Lactobacillus plantarum strain SRCM103295 plasmid unnamed2	26293-26320	6	0.786
NZ_CP044427_1	1.1|675759|28|NZ_CP044427|CRISPRCasFinder	675759-675786	28	NZ_CP035567	Lactobacillus plantarum strain SRCM103300 plasmid unnamed1	59567-59594	6	0.786
NZ_CP044427_1	1.1|675759|28|NZ_CP044427|CRISPRCasFinder	675759-675786	28	NZ_KY349138	Mycolicibacterium sp. CBMA 213 plasmid pCBMA213_2, complete sequence	106898-106925	7	0.75
NZ_CP044427_1	1.1|675759|28|NZ_CP044427|CRISPRCasFinder	675759-675786	28	NZ_AP022593	Mycolicibacterium arabiense strain JCM 18538 plasmid pJCM18538, complete sequence	4922757-4922784	7	0.75
NZ_CP044427_1	1.1|675759|28|NZ_CP044427|CRISPRCasFinder	675759-675786	28	NC_022536	Rhizobium sp. IRBG74 plasmid IRBL74_p, complete sequence	257496-257523	7	0.75
NZ_CP044427_1	1.1|675759|28|NZ_CP044427|CRISPRCasFinder	675759-675786	28	NZ_CP054613	Paenibacillus cellulosilyticus strain KACC 14175 plasmid unnamed4, complete sequence	949181-949208	7	0.75
NZ_CP044427_1	1.1|675759|28|NZ_CP044427|CRISPRCasFinder	675759-675786	28	NC_042132	Gordonia phage Sour, complete genome	38275-38302	7	0.75
NZ_CP044427_1	1.1|675759|28|NZ_CP044427|CRISPRCasFinder	675759-675786	28	NZ_CP026926	Agrobacterium tumefaciens strain 1D1609 plasmid pTi1D1609, complete sequence	27852-27879	7	0.75
NZ_CP044427_1	1.1|675759|28|NZ_CP044427|CRISPRCasFinder	675759-675786	28	NZ_CP026928	Agrobacterium tumefaciens strain 1D1609 plasmid pAt1D1609b, complete sequence	86377-86404	7	0.75
NZ_CP044427_5	5.1|2613024|29|NZ_CP044427|CRISPRCasFinder	2613024-2613052	29	NC_011961	Thermomicrobium roseum DSM 5159 plasmid unnamed, complete sequence	484089-484117	7	0.759
NZ_CP044427_3	3.1|1405105|32|NZ_CP044427|CRISPRCasFinder	1405105-1405136	32	NC_011961	Thermomicrobium roseum DSM 5159 plasmid unnamed, complete sequence	172061-172092	8	0.75
NZ_CP044427_3	3.1|1405105|32|NZ_CP044427|CRISPRCasFinder	1405105-1405136	32	NZ_CP033220	Parasedimentitalea marina strain W43 plasmid pW43A, complete sequence	159825-159856	8	0.75
NZ_CP044427_6	6.1|3034065|34|NZ_CP044427|CRISPRCasFinder	3034065-3034098	34	NZ_CP037902	Cupriavidus metallidurans strain BS1 plasmid p1, complete sequence	291495-291528	8	0.765

1. spacer 1.1|675759|28|NZ_CP044427|CRISPRCasFinder matches to NZ_AP014579 (Burkholderia sp. RPE67 plasmid p1, complete sequence) position: , mismatch: 4, identity: 0.857

cacg-accaccgatgacggcgcgaccacg	CRISPR spacer
-gcgcaccaccgacgacggcgcggccacg	Protospacer
 .** ********.*********.*****

2. spacer 1.1|675759|28|NZ_CP044427|CRISPRCasFinder matches to NC_016626 (Burkholderia sp. YI23 plasmid byi_1p, complete sequence) position: , mismatch: 4, identity: 0.857

cacg-accaccgatgacggcgcgaccacg	CRISPR spacer
-gcgcaccaccgacgacggcgcggccacg	Protospacer
 .** ********.*********.*****

3. spacer 1.1|675759|28|NZ_CP044427|CRISPRCasFinder matches to NZ_CP049734 (Rhizobium leguminosarum strain A1 plasmid unnamed1, complete sequence) position: , mismatch: 5, identity: 0.821

cacgaccaccgatgacggcgcgaccacg	CRISPR spacer
gaagaccaccgatggcggcgcgacctgg	Protospacer
 * ***********.**********  *

4. spacer 1.1|675759|28|NZ_CP044427|CRISPRCasFinder matches to CP049734 (Rhizobium leguminosarum strain A1 plasmid pRLa11, complete sequence) position: , mismatch: 5, identity: 0.821

cacgaccaccgatgacggcgcgaccacg	CRISPR spacer
gaagaccaccgatggcggcgcgacctgg	Protospacer
 * ***********.**********  *

5. spacer 1.1|675759|28|NZ_CP044427|CRISPRCasFinder matches to NC_022995 (Burkholderia sp. M701 plasmid pM7012 DNA, complete sequence) position: , mismatch: 6, identity: 0.786

cacgaccaccgatgacggcgcgaccacg	CRISPR spacer
ctcgaccaccggagacggcgcgacctgc	Protospacer
* *********. ************   

6. spacer 1.1|675759|28|NZ_CP044427|CRISPRCasFinder matches to NZ_CP034950 (Enterococcus faecium strain NM213 plasmid unnamed1, complete sequence) position: , mismatch: 6, identity: 0.786

cacgaccaccgatgacggcgcgaccacg	CRISPR spacer
tacgaccaacgatgacggtgcgacggca	Protospacer
.******* *********.***** .*.

7. spacer 1.1|675759|28|NZ_CP044427|CRISPRCasFinder matches to NZ_CP035169 (Lactobacillus plantarum strain SRCM103418 plasmid unnamed1) position: , mismatch: 6, identity: 0.786

cacgaccaccgatgacggcgcgaccacg	CRISPR spacer
tacgaccaacgatgacggcacgacggca	Protospacer
.******* **********.**** .*.

8. spacer 1.1|675759|28|NZ_CP044427|CRISPRCasFinder matches to NZ_CP035115 (Lactobacillus plantarum strain SRCM103295 plasmid unnamed2) position: , mismatch: 6, identity: 0.786

cacgaccaccgatgacggcgcgaccacg	CRISPR spacer
tacgaccaacgatgacggcacgacggca	Protospacer
.******* **********.**** .*.

9. spacer 1.1|675759|28|NZ_CP044427|CRISPRCasFinder matches to NZ_CP035567 (Lactobacillus plantarum strain SRCM103300 plasmid unnamed1) position: , mismatch: 6, identity: 0.786

cacgaccaccgatgacggcgcgaccacg	CRISPR spacer
tacgaccaacgatgacggcacgacggca	Protospacer
.******* **********.**** .*.

10. spacer 1.1|675759|28|NZ_CP044427|CRISPRCasFinder matches to NZ_KY349138 (Mycolicibacterium sp. CBMA 213 plasmid pCBMA213_2, complete sequence) position: , mismatch: 7, identity: 0.75

cacgaccaccgatgacggcgcgaccacg	CRISPR spacer
ggtcgtcaccgaggacggcgcgaccacg	Protospacer
 .. ..****** ***************

11. spacer 1.1|675759|28|NZ_CP044427|CRISPRCasFinder matches to NZ_AP022593 (Mycolicibacterium arabiense strain JCM 18538 plasmid pJCM18538, complete sequence) position: , mismatch: 7, identity: 0.75

cacgaccaccgatgacggcgcgaccacg	CRISPR spacer
cggcaccaccgatggcggcgcgaccgac	Protospacer
*.  **********.**********.  

12. spacer 1.1|675759|28|NZ_CP044427|CRISPRCasFinder matches to NC_022536 (Rhizobium sp. IRBG74 plasmid IRBL74_p, complete sequence) position: , mismatch: 7, identity: 0.75

cacgaccaccgatgacggcgcgaccacg	CRISPR spacer
ctttggcaccaatgacggcgcgaccaca	Protospacer
* . . ****.****************.

13. spacer 1.1|675759|28|NZ_CP044427|CRISPRCasFinder matches to NZ_CP054613 (Paenibacillus cellulosilyticus strain KACC 14175 plasmid unnamed4, complete sequence) position: , mismatch: 7, identity: 0.75

cacgaccaccgatgacggcgcgaccacg	CRISPR spacer
cacgaccaccgatgacggagccgaattg	Protospacer
****************** ** .   .*

14. spacer 1.1|675759|28|NZ_CP044427|CRISPRCasFinder matches to NC_042132 (Gordonia phage Sour, complete genome) position: , mismatch: 7, identity: 0.75

cacgaccaccgatgacggcgcgaccacg	CRISPR spacer
cgtcgccaccgaggacggcgcgaccaac	Protospacer
*.. .******* *************  

15. spacer 1.1|675759|28|NZ_CP044427|CRISPRCasFinder matches to NZ_CP026926 (Agrobacterium tumefaciens strain 1D1609 plasmid pTi1D1609, complete sequence) position: , mismatch: 7, identity: 0.75

cacgaccaccgatgacggcgcgaccacg	CRISPR spacer
ctttggcaccaatgacggcgcgaccaca	Protospacer
* . . ****.****************.

16. spacer 1.1|675759|28|NZ_CP044427|CRISPRCasFinder matches to NZ_CP026928 (Agrobacterium tumefaciens strain 1D1609 plasmid pAt1D1609b, complete sequence) position: , mismatch: 7, identity: 0.75

cacgaccaccgatgacggcgcgaccacg	CRISPR spacer
ctttggcaccaatgacggcgcgaccaca	Protospacer
* . . ****.****************.

17. spacer 5.1|2613024|29|NZ_CP044427|CRISPRCasFinder matches to NC_011961 (Thermomicrobium roseum DSM 5159 plasmid unnamed, complete sequence) position: , mismatch: 7, identity: 0.759

tgaggaatcaccccctcgcgcgtggtcta	CRISPR spacer
agtggaagcacccccgcgcgcgtggtggt	Protospacer
 * **** ******* **********   

18. spacer 3.1|1405105|32|NZ_CP044427|CRISPRCasFinder matches to NC_011961 (Thermomicrobium roseum DSM 5159 plasmid unnamed, complete sequence) position: , mismatch: 8, identity: 0.75

agggatccccctcgggcgcgttgtctgcgcga	CRISPR spacer
ggagatccgcctcgggcgcgatgtctgcagcg	Protospacer
.*.***** *********** *******.  .

19. spacer 3.1|1405105|32|NZ_CP044427|CRISPRCasFinder matches to NZ_CP033220 (Parasedimentitalea marina strain W43 plasmid pW43A, complete sequence) position: , mismatch: 8, identity: 0.75

agggatccccctcgggcgcgttgtctgcgcga	CRISPR spacer
gtggatccccctcgcgcgcattgtccatgaga	Protospacer
. ************ ****.*****...* **

20. spacer 6.1|3034065|34|NZ_CP044427|CRISPRCasFinder matches to NZ_CP037902 (Cupriavidus metallidurans strain BS1 plasmid p1, complete sequence) position: , mismatch: 8, identity: 0.765

caacacggtctgcccccaccggcgacacgctctg	CRISPR spacer
ccgggcgcgctgccgccagcggcgacacgctctg	Protospacer
* . .**  ***** *** ***************