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_CP047185	Rathayibacter sp. VKM Ac-2805 chromosome, complete genome	5 crisprs	WYL,csa3,cas3,DEDDh	0	2	0	0

1. NZ_CP047185

CRISPR-Cas detection and classification

Crispr_ID: NZ_CP047185_1

• CRISPR_ID: NZ_CP047185_1
• CRISPR_location: 112240-112356
• CRISPR_type: Orphan
• Repeat_type: NA
• Spacer_info: 1 spacers

Consensus repeat of NZ_CP047185_1

Consensus_repeat	Method
TGCGACAACTCCTGGACACTCGCGGGCTCTGGTC	CRISPRCasFinder

spacers of NZ_CP047185_1

>1.1|112274|49|NZ_CP047185|CRISPRCasFinder
ACCGCGCCCGGTCGCCCATTGTCCAGGAGTTGTCGCACTCGCGCTCGAC

CRISPR arrays and Neighbor proteins around NZ_CP047185_1

CRISPR arrays

The CRISPR arrays of NZ_CP047185_1

>merge|NZ_CP047185|1|112240-112356|CRISPRCasFinder
TGCGACAACTCCTGGACACTCGCGGGCTCTGGTCACCGCGCCCGGTCGCCCATTGTCCAGGAGTTGTCGCACTCGCGCTCGACTGCGACAACTCCTGGACACTCGCGGGCTCCGGTC

>NZ_CP047185|1|1|112240-112356|CRISPRCasFinder
TGCGACAACTCCTGGACACTCGCGGGCTCTGGTC	ACCGCGCCCGGTCGCCCATTGTCCAGGAGTTGTCGCACTCGCGCTCGAC
TGCGACAACTCCTGGACACTCGCGGGCTCCGGTC

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP047185.1|WP_160033067.1|99874_101047_+|PspC-domain-containing-protein	unknown	unknown	gnl|CDD|226951
NZ_CP047185.1|WP_104225736.1|121066_121888_-|ammonia-dependent-NAD(+)-synthetase	unknown	unknown	gnl|CDD|234831
NZ_CP047185.1|WP_160033069.1|101921_104306_-|DUF839-domain-containing-protein	unknown	unknown	gnl|CDD|225752
NZ_CP047185.1|WP_160033073.1|106012_107977_+|peptidase-M13	unknown	unknown	gnl|CDD|226118
NZ_CP047185.1|WP_104222833.1|108137_109040_+|serine-hydrolase	unknown	unknown	gnl|CDD|379138
NZ_CP047185.1|WP_104222839.1|101043_101685_+|response-regulator-transcription-factor	unknown	unknown	gnl|CDD|225107
NZ_CP047185.1|WP_159911790.1|109186_109390_+|hypothetical-protein	unknown	unknown	unknown
NZ_CP047185.1|WP_160033075.1|109453_111148_-|BCCT-family-transporter	unknown	unknown	gnl|CDD|376718
NZ_CP047185.1|WP_160033081.1|119236_120190_+|alpha/beta-hydrolase-fold-domain-containing-protein	unknown	unknown	gnl|CDD|369561
NZ_CP047185.1|WP_104225742.1|112761_113286_+|DUF2017-domain-containing-protein	unknown	unknown	gnl|CDD|378185
NZ_CP047185.1|WP_104222830.1|111258_112185_+|LLM-class-F420-dependent-oxidoreductase	unknown	unknown	gnl|CDD|274648
NZ_CP047185.1|WP_104225738.1|117261_117936_+|DNA-repair-protein	unknown	unknown	gnl|CDD|178801
NZ_CP047185.1|WP_104222847.1|120345_120951_+|nucleoside-deaminase	unknown	unknown	gnl|CDD|238612
NZ_CP047185.1|WP_104222823.1|118139_119189_+|zinc-dependent-alcohol-dehydrogenase-family-protein	unknown	unknown	gnl|CDD|176247
NZ_CP047185.1|WP_160033079.1|114324_114831_+|hypothetical-protein	unknown	unknown	gnl|CDD|182015
NZ_CP047185.1|WP_104225739.1|114904_117061_+|AAA-domain-containing-protein	unknown	unknown	gnl|CDD|274529
NZ_CP047185.1|WP_104250704.1|104953_105814_+|NmrA-family-NAD(P)-binding-protein	unknown	unknown	gnl|CDD|187578
NZ_CP047185.1|WP_160033077.1|113417_114236_+|DUF1206-domain-containing-protein	unknown	unknown	gnl|CDD|377695
NZ_CP047185.1|WP_160033071.1|104428_104812_-|transcriptional-regulator	unknown	unknown	gnl|CDD|224647
NZ_CP047185.1|WP_104222829.1|112400_112691_+|ATP-dependent-Clp-protease-adapter-ClpS	unknown	unknown	gnl|CDD|178809

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
NZ_CP047185.1|WP_160033067.1|99874_101047_+|PspC-domain-containing-protein	gnl|CDD|226951	COG4585, COG4585, Signal transduction histidine kinase [Signal transduction mechanisms].	1.4052e-12
NZ_CP047185.1|WP_104225736.1|121066_121888_-|ammonia-dependent-NAD(+)-synthetase	gnl|CDD|234831	PRK00768, nadE, ammonia-dependent NAD(+) synthetase.	1.34871e-168
NZ_CP047185.1|WP_160033069.1|101921_104306_-|DUF839-domain-containing-protein	gnl|CDD|225752	COG3211, PhoX, Predicted phosphatase [General function prediction only].	2.12703e-171
NZ_CP047185.1|WP_160033073.1|106012_107977_+|peptidase-M13	gnl|CDD|226118	COG3590, PepO, Predicted metalloendopeptidase [Posttranslational modification, protein turnover, chaperones].	0
NZ_CP047185.1|WP_104222833.1|108137_109040_+|serine-hydrolase	gnl|CDD|379138	pfam13354, Beta-lactamase2, Beta-lactamase enzyme family. This family is closely related to Beta-lactamase, pfam00144, the serine beta-lactamase-like superfamily, which contains the distantly related pfam00905 and PF00768 D-alanyl-D-alanine carboxypeptidase.	1.579e-33
NZ_CP047185.1|WP_104222839.1|101043_101685_+|response-regulator-transcription-factor	gnl|CDD|225107	COG2197, CitB, Response regulator containing a CheY-like receiver domain and an HTH DNA-binding domain [Signal transduction mechanisms / Transcription].	7.73489e-54
NZ_CP047185.1|WP_160033075.1|109453_111148_-|BCCT-family-transporter	gnl|CDD|376718	pfam02028, BCCT, BCCT, betaine/carnitine/choline family transporter.	0
NZ_CP047185.1|WP_104250704.1|104953_105814_+|NmrA-family-NAD(P)-binding-protein	gnl|CDD|187578	cd05269, TMR_SDR_a, triphenylmethane reductase (TMR)-like proteins, NMRa-like, atypical (a) SDRs. TMR is an atypical NADP-binding protein of the SDR family. It lacks the active site residues of the SDRs but has a glycine rich NAD(P)-binding motif that matches the extended SDRs. Proteins in this subgroup however, are more similar in length to the classical SDRs. TMR was identified as a reducer of triphenylmethane dyes, important environmental pollutants. This subgroup also includes Escherichia coli NADPH-dependent quinine oxidoreductase (QOR2), which catalyzes two-electron reduction of quinone; but is unlikely to play a major role in protecting against quinone cytotoxicity. Atypical SDRs are distinct from classical SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.	1.15077e-69
NZ_CP047185.1|WP_160033081.1|119236_120190_+|alpha/beta-hydrolase-fold-domain-containing-protein	gnl|CDD|369561	pfam07859, Abhydrolase_3, alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes.	7.47351e-67
NZ_CP047185.1|WP_104225742.1|112761_113286_+|DUF2017-domain-containing-protein	gnl|CDD|378185	pfam09438, DUF2017, Domain of unknown function (DUF2017). This is an alpha-helical domain found in gene neighborhoods that contain genes encoding ubiquitin, cysteine synthases and JAB peptidases.	3.21183e-39
NZ_CP047185.1|WP_104222830.1|111258_112185_+|LLM-class-F420-dependent-oxidoreductase	gnl|CDD|274648	TIGR03560, F420_Rv1855c, probable F420-dependent oxidoreductase, Rv1855c family. Coenzyme F420 has a limited phylogenetic distribution, including methanogenic archaea, Mycobacterium tuberculosis and related species, Colwellia psychrerythraea 34H, Rhodopseudomonas palustris HaA2, and others. Partial phylogenetic profiling identifies protein subfamilies, within the larger family called luciferase-like monooxygenanases (pfam00296), that appear only in F420-positive genomes and are likely to be F420-dependent. This model describes one such subfamily, exemplified by Rv1855c from Mycobacterium tuberculosis. [Unknown function, Enzymes of unknown specificity].	1.14511e-101
NZ_CP047185.1|WP_104225738.1|117261_117936_+|DNA-repair-protein	gnl|CDD|178801	PRK00024, PRK00024, DNA repair protein RadC.	2.6791e-39
NZ_CP047185.1|WP_104222847.1|120345_120951_+|nucleoside-deaminase	gnl|CDD|238612	cd01285, nucleoside_deaminase, Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn dependent and catalyze the deamination of nucleosides. The zinc ion in the active site plays a central role in the proposed catalytic mechanism, activating a water molecule to form a hydroxide ion that performs a nucleophilic attack on the substrate. The functional enzyme is a homodimer. Cytosine deaminase catalyzes the deamination of cytosine to uracil and ammonia and is a member of the pyrimidine salvage pathway. Cytosine deaminase is found in bacteria and fungi but is not present in mammals; for this reason, the enzyme is currently of interest for antimicrobial drug design and gene therapy applications against tumors. Some members of this family are tRNA-specific adenosine deaminases that generate inosine at the first position of their anticodon (position 34) of specific tRNAs; this modification is thought to enlarge the codon recognition capacity during protein synthesis. Other members of the family are guanine deaminases which deaminate guanine to xanthine as part of the utilization of guanine as a nitrogen source.	9.66849e-20
NZ_CP047185.1|WP_104222823.1|118139_119189_+|zinc-dependent-alcohol-dehydrogenase-family-protein	gnl|CDD|176247	cd08287, FDH_like_ADH3, formaldehyde dehydrogenase (FDH)-like. This group contains proteins identified as alcohol dehydrogenases and glutathione-dependant formaldehyde dehydrogenases (FDH) of the zinc-dependent/medium chain alcohol dehydrogenase family. The MDR family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. FDH converts formaldehyde and NAD to formate and NADH. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.	0
NZ_CP047185.1|WP_160033079.1|114324_114831_+|hypothetical-protein	gnl|CDD|182015	PRK09646, PRK09646, ECF RNA polymerase sigma factor SigK.	0.000198461
NZ_CP047185.1|WP_104225739.1|114904_117061_+|AAA-domain-containing-protein	gnl|CDD|274529	TIGR03346, chaperone_ClpB, ATP-dependent chaperone ClpB. Members of this protein family are the bacterial ATP-dependent chaperone ClpB. This protein belongs to the AAA family, ATPases associated with various cellular activities (pfam00004). This molecular chaperone does not act as a protease, but rather serves to disaggregate misfolded and aggregated proteins. [Protein fate, Protein folding and stabilization].	0
NZ_CP047185.1|WP_160033071.1|104428_104812_-|transcriptional-regulator	gnl|CDD|224647	COG1733, COG1733, Predicted transcriptional regulators [Transcription].	3.92034e-34
NZ_CP047185.1|WP_160033077.1|113417_114236_+|DUF1206-domain-containing-protein	gnl|CDD|377695	pfam06724, DUF1206, Domain of Unknown Function (DUF1206). This region consists of two a pair of transmembrane helices and occurs three times in each of the family member proteins.	3.16911e-12
NZ_CP047185.1|WP_104222829.1|112400_112691_+|ATP-dependent-Clp-protease-adapter-ClpS	gnl|CDD|178809	PRK00033, clpS, ATP-dependent Clp protease adaptor protein ClpS; Reviewed.	1.22566e-35

Protein sequences

>NZ_CP047185.1|WP_104222830.1|111258_112185_+|LLM-class-F420-dependent-oxidoreductase
MQFRVFTEPQQGASYEDLLAVAQAAESLGYDGFFRSDHYLRMGDGDPGVGPSDAWTTLAGLARETERIALGTLVSSVTYRPPGILAIQVAQVDAMSGGRAELGLGTGWFEQEHAAYGIPFPPRRFDLLEEQLEIVTGLWSTPVGERYSFAGEHYTLTDSPALPKPARLPLPVIVGGGGPKRTPALAARFASEFNLPFPEFDAIPGAFERVDEACRAIGREPSSLVHSVALIAVGGGDEAEFTRRAAAIGREPAELREHGVAGGVDEAVDRLESLREAGCERVYLQFMDLQDLDHLDFFAREVLPRLSA
>NZ_CP047185.1|WP_160033075.1|109453_111148_-|BCCT-family-transporter
MSEHPSSPDTAPATAGTPTPPHRLARWVFWPAAALTLSIAAFAILAPDAATSVFSTLQTTVVNTFSWYYVLIAAVFVAFAIWMGVSRFGDIKLGADDDEPEFSMLAWISLLFAAGMGIGLVFYGVAEPLTHFATPRPGVTGTETELAQSAISQTYLHWGVHAWSIYVVVGLALAYAIHRRKRPVSIRWALEPLLGRRVRGGWGNAIDVVALVGTMFGVATSLGLGVTQISAGLEASGIVESSLAVQIVVIAVVTGLTVFSLISGVGKGMKWLSTGNLLLAAALLVFVLVAGPTQFLLREFVQSLGNYLQNFIGLTFTVSAYSGREGEQWQASWTTFYWGWWMSWAPFVGIFIARVSKGRTVREFVGGVLLVPTIMTFLWFSVLGGTAIYRELYGDGGLVGADGSVDTNLALFSMLQGLPAGSVLTIGAIILIGIFFVTSADSGALVMAMIATGGQAEPRNPIRVFFAVATALLALSLLIAGGLDALQTAAILSALPFSVVMILMCIATVIAFRREIRAYDKARRRAFVGDIGTFYGLEVEDPAEREPAHPIKRLAHRLKPGSKE
>NZ_CP047185.1|WP_159911790.1|109186_109390_+|hypothetical-protein
MSSFGFDAPEDVTDTTRPDGDSLPVPPEDPAEIDDPESIDEALDEGADARLGDDQDPPEHPFIPSPS
>NZ_CP047185.1|WP_104222833.1|108137_109040_+|serine-hydrolase
MVIPTSETRRESRRNRRGRHKGGGDRENFQRGFDALGRLAIDGVVVSARAVDLATGRTLFAVDDSVSMPTASLGTVVLLIEVAARLANEPQENLRLVDRTAADAVSGSGLWQHLQVPSMPIADLAALVGASSDNLATNVLLRRVGLDAVRERAEALGLSRTALLDVVRDERGPDDAPQLSIGSARELTWLLATLANGEIVDAAVSSRVIGWLSLGTDLSMVAASFGLDPLAHRHPDHGVLLVNATGTDVGVRAEAGVLRGPRAGVAYAVATQFDDTTLHYRLAVLEGMRTLGADLLEYVH
>NZ_CP047185.1|WP_160033073.1|106012_107977_+|peptidase-M13
MTSTTPRSGIDRSELDPATRPQDDLYRHVNGLWIDRTEIPADKARYGSFHVLQEEAEKAVRDIIVEAQTAQHGTEERLFGDLYASFMDEERAEELGAAPIADDLAAVQRVDSIPGLLRAVGAFERTGVPGLFGLFVDNDPGSPERYLVFVNQGGLGLPDESYYREEEFASVREAYTPFVARMLALAGIDAAETRAERIVALETDLAAAHWDKVRSRDSQATYNLRSWSEVEELAAGVDLGVWLTAMGAPEGALAEVVVRQPSFLQGLAGLLTEDRLPAWRDWLSWQVIRGAAAYLSSGFVDANFDFYGRTLTGTPQKRERWKRAVSLVEGSLGEAVGRTYVARHFPETAKAAMDVLVANLIEAYRRSIVDLEWMSPATRERALEKLAKFTPKIGYPVRWRDYSALSIDPADLLGNARRVAEFEFARELGKIGRPLDRDEWFMTPQTINAYYNPGFNEIVFPAAILQFPFFDEARDPAANYGAIGAVIGHEIGHGFDDQGSRFDGDGRLTDWWTEEDRAAFEERTKALIAQYDALAPATTPGHYVNGALTIGENIGDLGGLGIAWKAYLLSLDGEEPPVVDGLTGAERFFLSWAQAWQQKSRDEETIRLLAIDPHAPAEFRCNQIVRNIDEFYATFDVSEGDALWLSPSERVTIW
>NZ_CP047185.1|WP_104250704.1|104953_105814_+|NmrA-family-NAD(P)-binding-protein
MTLVVTGATGHLGRLAVEHLLARGTAASDIVATGRDAAKLEALAADLGVRTAVADFDDPASLDAAFSGAEAVLLVSGSEVGRRVAQHTAAIDAAVRAGARLVYTSAPKATTSALILAPEHKATEEAIAASGVPAVVLRNGWYNENYEQTVAELASTGSTLSSAGEGRVASAARTDYAEAAAVALTDPSLVGTVHELSGDTAWSFDELAAIVAEVAGRDAAISHVSSDEHARVLTGAGVPEGGVGFVVGLDANIADGLLGGTDGSLARLIGRPTTPIRAYVEEQLGR
>NZ_CP047185.1|WP_160033071.1|104428_104812_-|transcriptional-regulator
MTIADSPLLAGDVYSADCPSREVFGHVTSKWGVLVLAALAPGTLRWGALRRRIGGISEKMLAQTLRILEEDGFVHREARPVVPPHVEYRLTPLGAELADRLLPVVEWIAGNVGAVLEARSEGRREGR
>NZ_CP047185.1|WP_160033069.1|101921_104306_-|DUF839-domain-containing-protein
MSDTARRPLLLPMAGHVRGKRSPVTCALKCANACSTATCNTSHNSYFRDIVSSQLSRRSALGLGLAGAVTVAVASAGGAPTAEAAVATAADGSPLAFTPIAPVPYTVDRFTVPEGFAWQPIIRWGDPLFADSPAFDIADQTEAAQAAQFGYNNDYTDIVEIPGSKRLRALLVVNHEYTNESIMFPAAQLEAEPERVRAVGRAAHGLSVVELVRTAVDRPWAYVRGGERNRRYLLDTPYEVTGAAAGTDLLKTVADPEGRTVLGTLGNCSGGTTPWGTILSGEENFNGYFRAVGTSDAEKRYGLADSETSRLWELDDPRFDARTPGYENEPNRFGWIVEFDPFDPDSTPKKHTALGRLKHEGANVIIAPDGRVVAYQGDDERFDYLYKFVSTKRYIEGDRAHNKTLLEEGDLYVARFTGDSPVAEITGTGAVPSDGGFDGIGEWLPLVLNGASTIAGMSVAEVLVHTRQAADAAGATKMDRCEDVQPSLVSGRIYVACTNNSARGTEGAKEGATEVNPRTENRDGHIVEIIEDGGDQTGRTFTWNLLMLCGDQAQGDVVYFSGFPADQVSPISCPDNLAFDSVGNLWISTDGAPSGIGYNDGLFKVALEGATRGRVEQFLSVPRDAETCGPIVHDLDQHVFVAVQHPGEEGTFEAPTSFFPDYGSTAAGAVAAPRPTIVQILPASQVVAPTPTPTAGPTTAPTTPPTTAPTATPTTAPTAGPTAAPTAAPSPVPTTAPTGTPTPLPVGGSGGGLASTGVESVGLIAGATALLAAGATALGLGARRRAAAEGDPEV
>NZ_CP047185.1|WP_104222839.1|101043_101685_+|response-regulator-transcription-factor
MTRVLLVDDHSIFRSGLRADLAPELEVVGEAADVDSAVGLVASLAPEVVLLDVHLPGGAGGGGAEVLRRSAGSSSRFLALSVSDAAEDVVGVIRAGARGYITKASSGAEVSRAVLAVAGGDAVFSPRLAGFVLDAFGALAGEQAESGDELDRLSAREREVMRLIARGYAYKEAAAELFISVKTVESHVSAVLRKLQLSSRYELTAWASARRLL
>NZ_CP047185.1|WP_160033067.1|99874_101047_+|PspC-domain-containing-protein
MSTVPGTAVRPPLRRPRTMLLGGVCTAVADHLGWSVRRTRVLALLTTALGGGGALLYLWLWALVPLAPLDSRDADPAVRRSAPVAGLLTLAAAVAALAVLITVDSGDDADITRALVAVGLLAGGAVGWSLGLDRGDAVRPARYGSAVRLASCALLVLAGAAVLTGRPSALNAVLAVGVLLIAAGVLAAPRVVTLWSELMGERAARVREEQRAEIAAHLHDSVLQTLALIQNRAGASSEVARIARAQERELRDWLFERDVPVANDLAAEVRAIAAAVELDYPVHLEVVAVGASVPGAAALLAATREAVLNAARHAGGDVSVYLESSVQGVDVFVRDRGPGVVLDEVPGDRLGIRESIIGRMARAGGSATVRPGVGGTGTEVHLRLPAEVER
>NZ_CP047185.1|WP_104222829.1|112400_112691_+|ATP-dependent-Clp-protease-adapter-ClpS
MADTIERADERLATRSAAEVPWIVLVWDDPVNLMSYVSYVFRSYFGFGRAEAERLMLQVHTEGRAVVATGNREEMERHVEAMHGYGLWATLQKADA
>NZ_CP047185.1|WP_104225742.1|112761_113286_+|DUF2017-domain-containing-protein
MRAFRRDSSGAAVARFDREEAGILRHLAGEMLELLDRGASSEEARSDPALARLLPDAYRDDAEAADEFRRFTAPDLAARKMDDARAVTAALDAGDGTSHGRIFEGLGEVAVRLEEPQAIAWLRALTDMRLALAVRLGIDDTDDVVPEEGSAAAIRSVYDWLGGVQDGLVRAVDV
>NZ_CP047185.1|WP_160033077.1|113417_114236_+|DUF1206-domain-containing-protein
MNTPSTADAQRTADDIQDSRAVRTLARGGFAANGLVHLLIGVIALGVARGGGGEADQSGALGALAAQPGGLVVLWICTVGLFGLALWGLLEAFLVRPRESALKTWGSRLKEAGKAVVYGALGVTALKFATGGGSSSSESSESASAQVLSAPGGVVLLVMAGLAVLAVGGVFVYRGASRKFLENVAEPGGTAGTVVTVLGVAGYVAKGVVLGALGVLLIVAAVTHDPEQAGGLDEALKSLVELPAGVFLLGFVAVGLIAYGLFCFARARWPRL
>NZ_CP047185.1|WP_160033079.1|114324_114831_+|hypothetical-protein
MSAGGEDATGGRVRPPLTQDAARLLARSATGDASALGELVDRFGGLVSACVGTVQADPAGRDRLCTDVFTAVWRRSREGARSPEPVLWVLEVLCETLGSAHELARRPLGSGLLALDCPDRELLLLAAAGGFSQAEISALTGVDELRLRSILRNALETLQGRDSDLLTA
>NZ_CP047185.1|WP_104225739.1|114904_117061_+|AAA-domain-containing-protein
MQAGRMPQQDEKSALEQYGVNLTAIAASGKLDPVIGRDAEIRRVSQVLTRRTKNNPVLIGEPGVGKTAVVEGLAQRIVAGDVAESLKGKQLVSLDLSALIAGAKYRGEFEERLKAVLQEIEESDGRIITFIDELHTLMGAGGGEGSVAAANMLKPMLARGELRMIGATTLDEYRQYIEKDAALERRFQQVFVGEPTVEDTVAILRGLKERYEAHHKVAIADSALVAAASLSNRYITSRQLPDKAIDLIDEAASRLRMEIDSAPVEIDELRRSVDRLRLEELALKKEKDEASKARLEKLREDLARRGAQLEELQERWERERASLNRVGELKNRLDALRIAAERAQREGKLERASKLLYGDIPVIERELAAAEAEEEPAEGRMVNEQVTADDIAAVIAAWTGIPVGRLLQGETEKLLHLETELHRRLIGQDEAVSAVADAVRRTRAGISDPDRPTGSFLFLGPTGVGKTELAKALADHLFDDEKAMVRIDMSEYGEKFAVSRLVGAPPGYIGYEQGGQLTEAVRRRPYSVVLLDEIEKAHPEVFDVLLQVLDDGRLTDGQGRTVDFRNTILILTSNLGSQFLVDPALSRPQKEEAVQQMVRQAFKPEFVNRLDDIVIFDALDRTELGEIVSLYVDRLSRRLSERRLDLAVTPAARGWLAERGYDPQYGARPLRRLMQRAIDDQLATALLGGTVRDGDVVLVDVAPDGESLSVTAGMPASD
>NZ_CP047185.1|WP_104225738.1|117261_117936_+|DNA-repair-protein
MSFETPGPRMADLPPEERPRERLRAYGPEALTDAETLAVLIGAGVRGANATVVAQRLLARFGGIDAVARAGVGDLMRHRGVGEVAACRLVASFELRRRMNRASRAARVTDAAGLAGLVAPLLAARPVETVLAVALAESGAVRDVLTLADGAPAHAEIPVAAVLAEVLARGAAGIGLAHSHAGEAVVLPSDRAATRAIADGAEACGLRFLAHVVIGRDGWAEAQP
>NZ_CP047185.1|WP_104222823.1|118139_119189_+|zinc-dependent-alcohol-dehydrogenase-family-protein
MRATLIHGERDIRLEEVPDPQLSTGRDAIVRVTAACVCGSDLWPYRGVTPTKEAHRIGHEFVGVVEEIGDDVHDVAVGDFVIAPFYVCDGTCANCANGVSTSCLTGGWWGAEVREEGFADGAQGEKVRVPLADGTLFRVGIDPDPALIPSLLTLADVMGTGHHAAVSAGVTAGSTVAVVGDGAVGLCAVLAAKRLGATTIIAMSRHESRQNLARRFGATHIVETRGDEGVARVRELTGGIGADCVLECVGTKESMQQALDSARPGGMVGYVGVPNGGPELPVRQMFGSNVGVNGGVAPVRGYMAELLPDVLSGAIEPGLVFDLELPLEEIAEAYAAMDERRAIKTLVRP
>NZ_CP047185.1|WP_160033081.1|119236_120190_+|alpha/beta-hydrolase-fold-domain-containing-protein
MTASARTAATAPLFHPDLALGRFLPPIVLGPRLLRLATRRAAEGGEAPPDIVVDDVEIPAAGAAPVRARSYRPRILRGTAPALLWVHGGGMVLGSHLQDEASCIDFARTLGITVVSVDYRLAPAHPAPAAVEDVLAAFDWLVEHAQERGVDPARIAVGGASAGGGIAAGATLLAHDRGGAQPAFQLLVYPMLDDRTVTRPGPPPRGVRVWTPGSNRFGWTAYLAGEPGGPGVTAYAAPARRDDLTGLPPAWIGVGGLDLFHDEDVRYAERLRAAGVPCGLEIVEGAFHGFDALFRRTGVAKRFWAAQAAALGEALLA
>NZ_CP047185.1|WP_104222847.1|120345_120951_+|nucleoside-deaminase
MDRLATRYEIALPAWIGDALRDVPEVLPSLEDRMALVHALADRNFREGNGGPFAAIVVERDSGRLVSVGVNVVLGSGVSSGHAEVTALGLAQTALGTWDLGGEGLPAHDLVVNWRPCVQCYGATMWSGVRRLVVAGSGPELEEISTFDEGPMREDWAAQFEARGIEVVDGVLRDEALDVFRAYRASVDSGEVLVYNARADS
>NZ_CP047185.1|WP_104225736.1|121066_121888_-|ammonia-dependent-NAD(+)-synthetase
MRDVQQQIISELHVSPAVDPAVEVERRSGFLADYLRSTGAKGLVLGISGGQDSSLAGRLCQLAVEQVRASGGDASFIAVRLPYKVQADEEDAQLALTFIRPDRQVVFDIHQGVDGVAAAFGDAVDEPISDFVKGNVKARMRMIAQYAIAGQAGMLVVGTDHAAEAVTGFFTKYGDGGADVLPLTGLTKRQGRSLLEHLDAPARLYEKAPTADLLDDNPGQTDETNLGLTYADLDTYLEGGEVDQAVAEAIEARYAATEHKRQVPLSMFDDWWR

Crispr_ID: NZ_CP047185_2

• CRISPR_ID: NZ_CP047185_2
• CRISPR_location: 1880611-1880935
• CRISPR_type: Orphan
• Repeat_type: NA
• Spacer_info: 5 spacers

Consensus repeat of NZ_CP047185_2

Consensus_repeat	Method
CNNNNNNNNCGAGGNCGCC	CRT

spacers of NZ_CP047185_2

>2.1|1880630|47|NZ_CP047185|CRT
GCGATCCGCGGCACCGTGGCGACCGAGGCCGCCGAGACCCGCGCCAC
>2.2|1880696|53|NZ_CP047185|CRT
GCGATCCGCTCCGAGGCCGAGCGCGAGGCCGCGGAGATGCGCGCCGTCGCCGC
>2.3|1880768|38|NZ_CP047185|CRT
CGCGCCGAGGCCGCCCGCCTCGCCCAGGCCAACGAGCT
>2.4|1880825|26|NZ_CP047185|CRT
TCCGAGGTCGACCGGCTCCGGGCGGC
>2.5|1880870|47|NZ_CP047185|CRT
CAGGCGCGCGCGGCGGTCGAGGCCGAGGTGCTCTCGACCCGCGCCGC

CRISPR arrays and Neighbor proteins around NZ_CP047185_2

CRISPR arrays

The CRISPR arrays of NZ_CP047185_2

>merge|NZ_CP047185|2|1880611-1880935|CRT
CGCCGTCCGCGAGGCCGCCGCGATCCGCGGCACCGTGGCGACCGAGGCCGCCGAGACCCGCGCCACCGCGAAGCGCGAGGCCGCCGCGATCCGCTCCGAGGCCGAGCGCGAGGCCGCGGAGATGCGCGCCGTCGCCGCCCGCGAGATCGAGGTCGCCCGCGCCGAGGCCGCCCGCCTCGCCCAGGCCAACGAGCTCCTGCGGGCCGAGGTCGCCTCCGAGGTCGACCGGCTCCGGGCGGCCGTCGAGGCCGAGGTCGACCAGGCGCGCGCGGCGGTCGAGGCCGAGGTGCTCTCGACCCGCGCCGCGCTCGACGCCGAGGTCGCC

>NZ_CP047185|2|1|1880611-1880935|CRT
CGCCGTCCGCGAGGCCGCC	GCGATCCGCGGCACCGTGGCGACCGAGGCCGCCGAGACCCGCGCCAC
CGCGAAGCGCGAGGCCGCC	GCGATCCGCTCCGAGGCCGAGCGCGAGGCCGCGGAGATGCGCGCCGTCGCCGC
CCGCGAGATCGAGGTCGCC	CGCGCCGAGGCCGCCCGCCTCGCCCAGGCCAACGAGCT
CCTGCGGGCCGAGGTCGCC	TCCGAGGTCGACCGGCTCCGGGCGGC
CGTCGAGGCCGAGGTCGAC	CAGGCGCGCGCGGCGGTCGAGGCCGAGGTGCTCTCGACCCGCGCCGC
GCTCGACGCCGAGGTCGCC

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP047185.1|WP_160034481.1|1868823_1869306_+|Cys-tRNA(Pro)-deacylase	unknown	unknown	gnl|CDD|237976
NZ_CP047185.1|WP_160034475.1|1861796_1864304_-|NAD-dependent-DNA-ligase-LigA	unknown	unknown	gnl|CDD|236137
NZ_CP047185.1|WP_160034487.1|1878087_1879884_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP047185.1|WP_160034495.1|1885877_1886816_-|phosphatidate-cytidylyltransferase	unknown	unknown	gnl|CDD|366491
NZ_CP047185.1|WP_104223894.1|1887483_1888215_-|UMP-kinase	unknown	unknown	gnl|CDD|234735
NZ_CP047185.1|WP_160034479.1|1866751_1868824_+|glycogen-debranching-protein-GlgX	unknown	unknown	gnl|CDD|200465
NZ_CP047185.1|WP_160036197.1|1872226_1874443_+|DUF3416-domain-containing-protein	unknown	unknown	gnl|CDD|200482
NZ_CP047185.1|WP_160034491.1|1881598_1882324_-|alpha/beta-fold-hydrolase	unknown	unknown	gnl|CDD|225496
NZ_CP047185.1|WP_160034493.1|1882663_1884412_-|sodium:proton-antiporter	unknown	unknown	gnl|CDD|223104
NZ_CP047185.1|WP_160034483.1|1869428_1872002_-|alpha-glucan-family-phosphorylase	unknown	unknown	gnl|CDD|340852
NZ_CP047185.1|WP_104223932.1|1882320_1882557_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP047185.1|WP_104223896.1|1889356_1890304_-|30S-ribosomal-protein-S2	unknown	unknown	gnl|CDD|235396
NZ_CP047185.1|WP_160034485.1|1877128_1878091_-|tetratricopeptide-repeat-protein	unknown	unknown	gnl|CDD|225660
NZ_CP047185.1|WP_104226865.1|1885263_1885815_-|DivIVA-domain-containing-protein	unknown	unknown	gnl|CDD|188337
NZ_CP047185.1|WP_104223931.1|1874880_1877052_+|1,4-alpha-glucan-branching-protein-GlgB	unknown	unknown	gnl|CDD|235445
NZ_CP047185.1|WP_104232511.1|1864300_1865404_-|tRNA-2-thiouridine(34)-synthase-MnmA	unknown	unknown	gnl|CDD|234664
NZ_CP047185.1|WP_104262836.1|1884471_1885212_-|hypothetical-protein	unknown	unknown	gnl|CDD|275060
NZ_CP047185.1|WP_160034477.1|1865463_1866753_-|aminotransferase-class-V-fold-PLP-dependent-enzyme	unknown	unknown	gnl|CDD|224029
NZ_CP047185.1|WP_104223895.1|1888350_1889178_-|elongation-factor-Ts	unknown	unknown	gnl|CDD|236491
NZ_CP047185.1|WP_104232499.1|1886896_1887451_-|ribosome-recycling-factor	unknown	unknown	gnl|CDD|178850

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
NZ_CP047185.1|WP_160034481.1|1868823_1869306_+|Cys-tRNA(Pro)-deacylase	gnl|CDD|237976	cd00002, YbaK_deacylase, This CD includes cysteinyl-tRNA(Pro) deacylases from Haemophilus influenzae and Escherichia coli and other related bacterial proteins. These trans-acting, single-domain proteins are homologs of ProX and also the cis-acting prolyl-tRNA synthetase (ProRS) inserted (INS) editing domain. The bacterial amino acid trans-editing enzyme YbaK is a deacylase that hydrolyzes cysteinyl-tRNA(Pro)'s mischarged by prolyl-tRNA synthetase. YbaK also hydrolyzes glycyl-tRNA's, alanyl-tRNA's, seryl-tRNA's, and prolyl-tRNA's. YbaK is homologous to the INS domain of prolyl-tRNA synthetase (ProRS) as well as the trans-editing enzyme ProX of Aeropyrum pernix which hydrolyzes alanyl-tRNA's and glycyl-tRNA's.	2.47667e-71
NZ_CP047185.1|WP_160034475.1|1861796_1864304_-|NAD-dependent-DNA-ligase-LigA	gnl|CDD|236137	PRK07956, ligA, NAD-dependent DNA ligase LigA; Validated.	0
NZ_CP047185.1|WP_160034495.1|1885877_1886816_-|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.	1.68116e-50
NZ_CP047185.1|WP_104223894.1|1887483_1888215_-|UMP-kinase	gnl|CDD|234735	PRK00358, pyrH, uridylate kinase; Provisional.	7.75049e-131
NZ_CP047185.1|WP_160034479.1|1866751_1868824_+|glycogen-debranching-protein-GlgX	gnl|CDD|200465	cd11326, AmyAc_Glg_debranch, Alpha amylase catalytic domain found in glycogen debranching enzymes. Debranching enzymes facilitate the breakdown of glycogen through glucosyltransferase and glucosidase activity. These activities are performed by a single enzyme in mammals, yeast, and some bacteria, but by two distinct enzymes in Escherichia coli and other bacteria. Debranching enzymes perform two activities: 4-alpha-D-glucanotransferase (EC 2.4.1.25) and amylo-1,6-glucosidase (EC 3.2.1.33). 4-alpha-D-glucanotransferase catalyzes the endohydrolysis of 1,6-alpha-D-glucoside linkages at points of branching in chains of 1,4-linked alpha-D-glucose residues. Amylo-alpha-1,6-glucosidase catalyzes the endohydrolysis of 1,6-alpha-D-glucoside linkages at points of branching in chains of 1,4-linked alpha-D-glucose residues. In Escherichia coli, GlgX is the debranching enzyme and malQ is the 4-alpha-glucanotransferase. TreX, an archaeal glycogen-debranching enzyme has dual activities like mammals and yeast, but is structurally similar to GlgX. TreX exists in two oligomeric states, a dimer and tetramer. Isoamylase (EC 3.2.1.68) is one of the starch-debranching enzymes that catalyzes the hydrolysis of alpha-1,6-glucosidic linkages specific in alpha-glucans such as amylopectin or glycogen and their beta-limit dextrins. 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_CP047185.1|WP_160036197.1|1872226_1874443_+|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_CP047185.1|WP_160034491.1|1881598_1882324_-|alpha/beta-fold-hydrolase	gnl|CDD|225496	COG2945, COG2945, Predicted hydrolase of the alpha/beta superfamily [General function prediction only].	7.95776e-17
NZ_CP047185.1|WP_160034493.1|1882663_1884412_-|sodium:proton-antiporter	gnl|CDD|223104	COG0025, NhaP, NhaP-type Na+/H+ and K+/H+ antiporters [Inorganic ion transport and metabolism].	2.76683e-63
NZ_CP047185.1|WP_160034483.1|1869428_1872002_-|alpha-glucan-family-phosphorylase	gnl|CDD|340852	cd04299, GT35_Glycogen_Phosphorylase-like, proteins similar to glycogen phosphorylase. This family is most closely related to the oligosaccharide phosphorylase domain family and other unidentified sequences. Oligosaccharide phosphorylase catalyzes the breakdown of oligosaccharides into glucose-1-phosphate units. They are important allosteric enzymes in carbohydrate metabolism.	0
NZ_CP047185.1|WP_104223896.1|1889356_1890304_-|30S-ribosomal-protein-S2	gnl|CDD|235396	PRK05299, rpsB, 30S ribosomal protein S2; Provisional.	2.01029e-157
NZ_CP047185.1|WP_160034485.1|1877128_1878091_-|tetratricopeptide-repeat-protein	gnl|CDD|225660	COG3118, COG3118, Thioredoxin domain-containing protein [Posttranslational modification, protein turnover, chaperones].	1.9377e-42
NZ_CP047185.1|WP_104226865.1|1885263_1885815_-|DivIVA-domain-containing-protein	gnl|CDD|188337	TIGR03543, divI1A_rptt_fam, DivIVA domain repeat protein. Members of this protein family contain two full and two partial repeats of a domain found at the N-terminus of Bacillus subtilis cell-division initiation protein DivIVA. The portion repeated four times in these proteins includes the motif GYxxxxVD.	1.57038e-59
NZ_CP047185.1|WP_104223931.1|1874880_1877052_+|1,4-alpha-glucan-branching-protein-GlgB	gnl|CDD|235445	PRK05402, PRK05402, 1,4-alpha-glucan branching protein GlgB.	0
NZ_CP047185.1|WP_104232511.1|1864300_1865404_-|tRNA-2-thiouridine(34)-synthase-MnmA	gnl|CDD|234664	PRK00143, mnmA, tRNA-specific 2-thiouridylase MnmA; Reviewed.	1.83814e-178
NZ_CP047185.1|WP_104262836.1|1884471_1885212_-|hypothetical-protein	gnl|CDD|275060	TIGR04216, halo_surf_glyco, major cell surface glycoprotein. Members of this family are the S-layer-forming halobacterial major cell surface glycoprotein. The highest scores below model cutoffs are fragmentary paralogs to actual members of the family. Modifications include at N-linked and O-linked glycosylation, a C-terminal diphytanylglyceryl modification, and probable cleavage of the PGF-CTERM tail.	0.00177717
NZ_CP047185.1|WP_160034477.1|1865463_1866753_-|aminotransferase-class-V-fold-PLP-dependent-enzyme	gnl|CDD|224029	COG1104, NifS, Cysteine sulfinate desulfinase/cysteine desulfurase and related enzymes [Amino acid transport and metabolism].	1.37024e-135
NZ_CP047185.1|WP_104223895.1|1888350_1889178_-|elongation-factor-Ts	gnl|CDD|236491	PRK09377, tsf, elongation factor Ts; Provisional.	4.18059e-116
NZ_CP047185.1|WP_104232499.1|1886896_1887451_-|ribosome-recycling-factor	gnl|CDD|178850	PRK00083, frr, ribosome recycling factor; Reviewed.	8.34656e-89

Protein sequences

>NZ_CP047185.1|WP_160034487.1|1878087_1879884_-|hypothetical-protein
MRFVFAIIATVIAAAMIVLGIGQRTVWAPPESLTAETALDSSAPYAVIDGSTLGANPGRQTITVEGSGDLVVAYAPTSDVLGWVGGSSYDAIGYERADDTLTSAEETGERVQLSSDVETADAAVVDPRGSDLWLEEFEGSGSVTLALDVPEDVSILIASDGTAPAADSVRVSWPVDTATPLAGPLLLGGAVFLLLGLVLYIWAFVHLRRQHGPRRKGPQGRIPRGARRPRPRAGIQASTASPAPSRRRAALVLPVVLGTTVLLSGCSSDYWPDLAAGASEAPTASATATAGAEPVSAEPTPVVTTQQAEAVVAEVADVASRADTARDAGILAERFQGEALTERTTNYDVVAKGGTIDPPQTIPASPVSLVLPQDTESWPRLVTAVVQNSTDSTQAPIALMMSQASPRVDYKVDYAISLEANARIPDVAPVTVGTSIVAPDSRLMKLAPQSVGSAYADVLANGDSSQYAELFAADGDTLRGQVGVDKKNADREALPDTASIEFSNAAGTSPTIALATNDSGALVAASIAETSTVRPTAEGSTVSTSGASQTLLGTDKSTTGIETTYGYQLLFYVPPVGSEEKIVMLGWSQGLVSVVQLP
>NZ_CP047185.1|WP_160034485.1|1877128_1878091_-|tetratricopeptide-repeat-protein
MSTVPPLPGNLRGAVDLSSLVNRRTPPAASAGAPAAPAAPGGAPGANPLLLTAGDAEFDQVVQLSSRVPVIVDLRGSWSDQSQSMTALLEKVVVSYAGAFVLVGVDVESSPQLAQAFQVQSVPTVAAIIGGRPVPLFSGLVAEEQLRDLLEQVLQLAAQNGVTGTVPVEGPAPAEGAEPEPEPLPPHHQEAYDAIDRGDYAAAITEYETAIAQNPRDDLAVAGLAQVRLLARLQGRTLDDIRSTAAAEPSNLDAQLAVADLDVSGGHVEDAFDRLLSMFPRLDAEGKAAVRARLLELFEIVGQTDPRVNKARARLTGLLY
>NZ_CP047185.1|WP_104223931.1|1874880_1877052_+|1,4-alpha-glucan-branching-protein-GlgB
MPDIPEWVLQQLATGSNALPHDVLGQHLVAAPGVSDPVTVVRVRRPLAEKVAVVLATGARVELSHLSDGIWQGFHVLGPQAYTVEARYGGGGEWTAEDPYRFSKTVGDFDLYLIGEGRHERLWEALGARHREHEGVWGTSFAVWAPHAQAARVVGDFNDWNGEGHSLRNLGTTGVWEIFVPGVEPGASYKFDLLSRDGHWVRKADPMARATEVPPATASKVPVSHHQWGDSGWMEKRASVDPHTQPLSVYEMHLGSWRPGLGYRDLADPLIEYVTELGFTHVEFMPLAEHPFGGSWGYQVTGYYAASSRFGTADDLKYLIDRLHQAGIGVIVDWVPGHFPKDDFALARFDGEPLYEHPDWRRGEQMDWGTYVFDFGHTQVRNFLVANALFWLEEFHVDALRVDAVASMLYLDYSRKEGEWLPNQYGGREHLEAISFLQEVNATAYKLHPGIMMIAEESTSWPGVTQPTSSGGLGFGLKWNMGWMHDSLDYMANDPLWRQYHLGEITFSFVYAFSEKFVLPISHDEVVHGKGSLIQKMPGDHWQQLANVRAYLAFMWAHPGKQLLFMGQEFGQYSEWSEERGLDWWILDQPSHRGLWSLVGQLNRVYRDSPSLWELDHEQSGFEWIDGGAAAANVVSFLRKDSEGRPIAVIANFSGSPVHGYRVSLPTAGRWEELVNTDAEIYGGSGVGNFGAVEAREEPWAGRPASAELVLPPLAVLYLRPAD
>NZ_CP047185.1|WP_160036197.1|1872226_1874443_+|DUF3416-domain-containing-protein
MPFGKAQNGKDARRAGRGRAPQEASAPPETAAPAPAAAPEATPAPPAADSAPAAPVTADAPHASPATATTGSGYRVRAERLPIIDPQPRLEDDRWPAKAFVGEVVPFAATAFREGHDLIGVDLLLRSPSGAESEHRMSLLATGTDRYGRLVALDEEGDWSYRIRAYADDWATWLHTAEVKIPAGLDIDVTFAIGEGLLRSGADDSARPEGERSLLSDTAARVGDTTLSAEERLAAATDPAVHGALDARPVMSLTSVSEPRTVHAERTRAGVGAWYEFFPRSEGAVRHEDGTVTSGSFRTAIDRLPAVAAMGFDVLYLPPIHPIGRSFRKGPNNTLDAGEHDPGSPWAIGSAEGGHDAIHPDLGTEDDFRAFHAAVEAAGLELALDFALQASPDHPWVTSHPEWFTTLPDGSIAYAENPPKKYQDIYPINFDNDPEGIRQESLRVLRHWIDLGVRIFRVDNPHTKPLDFWEWIIHEVNAEHPEVVFLAEAFTRPAIMRALGKVGFQQSYSYFTWRNTKAELGEFFTSISHETADYMRPNLFVNTPDILTEYLQYGGRSAYKVRAALAATASPLWGVYAGYELVENVARPGAEENIDNEKYEYKTRDWAGAEESGRSLAPYITRLNEIRRSHPALGQLRNLHVHGSDDDAILVYSKHLQAAFTGTGTDDTIIVVVNTDPHSARETTVHLDLPAIGLDWSATFEVEDLITGAVWTWGSDDYVRLDSFVEPVHILSVKADER
>NZ_CP047185.1|WP_160034483.1|1869428_1872002_-|alpha-glucan-family-phosphorylase
MKAIRRFIVRSVLPPELSALGDLAGNLRWAWHEPARRLFERVDPELWRRGGADPTALLGAVSPERLAELAGDQGFVDEAWRLRDELERYRTEPRWYQSLPESAPRSIAYFSPEFGIAAALPQYSGGLGILAGDHLKASSDLGVPLTGVGLFYRSGYFSQKLSADGWQLESYPSLDPDGLPLRVVRLADGSPARIVLALPEGRALYARVWRAEVGRVTLLLLDTDIPENEDSLRSVTDRLYGGGGEHRLLQELLLGIGGVRALELWAEVSGGVLPEVFHTNEGHAGFQGLERISGLIGAGLDFDQALQVVRASTVFTTHTPVPAGIDRFDRGMIEEYFSTELLPGVQVEDVLALGAEPGDSGTAFNMAYMGLRLAQRSNGVSTLHGEVSRSMFSSLWPGFETAEVPIGSVTNGVHAATWTDPILRRLAEERLGTDDTTRADWASGSLGDTELWAARRAMREQLVRDARRRAARSWREQNPGGLPPAWLDELLDPDVLTIGFARRVPTYKRLTLMLHDPERLRALLTHPQHPIQIVIAGKSHPADEEGKRLIQRLVRFAQEPDVRRRIVFLPDYDIAMAQLLYPGTDVWLNNPLRPLEACGTSGMKAALNGSLNLSILDGWWNEYFDGENGWAIPSSDRALDPEARDTLEAEALYELLETEVVPRYYERDHDGVPRRWVRSIRHTLATLSPELSAERMVRQYVEALYSPAAEAGRAVAADHFEPAKELATWKRRVRAGWPGVAVASVESGGIDAVPQRGDRLAVRAGVRLGELSPADVSVEVVYGTTAADGSLTEVRHHELEVVEESGAVVPADAVGRVPYAGVVTLDRSGSFGYTVRVVPRHPLLARSAELGLAAAAG
>NZ_CP047185.1|WP_160034481.1|1868823_1869306_+|Cys-tRNA(Pro)-deacylase
MARSGPGTPATVALTAAGVPFTPRQYRHDPATSRYGLEAAEALGVEPERVFKTLMVDVDGELVVGVVPVTGSLGLKELAAAVGGRRAAMADPVLAQRRTGYVLGGISPLGQRTLHRTVIDETVELHDTVLVSGGRRGFDIELAPADLVAATAALLADIAR
>NZ_CP047185.1|WP_160034479.1|1866751_1868824_+|glycogen-debranching-protein-GlgX
MTSHDPLARLGVTVDDQGGELRVWSESASAVDLLLYDEKDPTWVTRTVPLARDDAAVWSARSDLLAPGRRYALRVDGPTGPRHRFDPRRALLEPYSRGLHRVAENEWRSVVVDDAFDWGSSSRPGTPMDRTVIYEAHVKGLTRLNPALPVELRGTYAGLAHESTVSALLELGVTAVELLPVHAFVSEQRLLRQGLTNYWGYNTLNFFAPHAAYASSTAQRGGPTAVLREFKGMVKLLHEAGLEVILDVVYNHTAEEGPGGPMSSLRGIDDAGWYRQTPEGHYVDVTGCGNTIDFGRPAAQRLALDSMRYWSGEVGIDGFRLDLAATLGRDEIAHFRSDHPLLRAAVEDPALTGVKMIAEPWDVGMGGWQTGNFPAGWSEWNDRYRDRARNFWLSDIDYARRAGTAPVGIGGFATRLSGSSNTFSAERGPLASVNFVTAHDGFTLADLVSYNVKHNIGNGESNRDGADTNRSFNHGFEGPTTDERITLARRKAMRNLLGTLLLSAGVPMITAGDETGRSQRGNNNAYCQDSDLTWVRWEGLADWQLALRAHTRTLLRLRREHPALRPSRYGSGDASEPGATTMTWFDAHGRGMSEHDWTSAANRTLQYLAASTPVEGEPDRVLLVVHGVEQDTTVVLADGEGVTGYTRLWNSEEPEPLEHGESFEPGQVIRVAATSMQLFAAHGPAAEQDA
>NZ_CP047185.1|WP_160034477.1|1865463_1866753_-|aminotransferase-class-V-fold-PLP-dependent-enzyme
MRLTVVTGTGSLRAPDAGRRAAVIYLDHAATTPLRASALAAFAEASAHGGNPSSVHGSGQEARRRLEDARSALAGVLGCEPIEVILTAGGTEAVNLGIKGLYWQRRSEDPARVRVLVAEGEHHATLDSAAWLAEHEGAVLEWLPLDDEGTLRPEALAAALEEDPGSVALVTVLWVNNEIGTINPIAELAAACARAGVPLHVDAVAALGHVPLRIAEIRRASGSGRGAGLAAVSVSGHKVGGPIATGALVLARDARVVPVLHGGGQQRGVRSGTQDVPGAAAFAAAAVEADDELSAEAQRLAALRDRLVAGVLAAVPGATLTGPALDSGRRVANNAHLAFPGAQGDSLLFLLDTAGVSVSTGSACTAGIPEPSHVVLALGRSEDEARGVLRMTLGHTSTDADVDALLAALPGAYARAARAGLSNRAVLPA
>NZ_CP047185.1|WP_104232511.1|1864300_1865404_-|tRNA-2-thiouridine(34)-synthase-MnmA
MSGGVDSAVAAARAVEAGHDVVGVHLALSRMPGTLRTGSRGCCTIEDSMDAQRAANVLGIPYYVWDFSERFKLDVVDDFVAEYSAGRTPNPCMRCNERIKFAALLEKALDLGFDAVCTGHYASLRTAADGSPELHRASDEAKDQSYVLGVLTEQQLRHSMFPLGSTPSKAIVRAEAAERGLSVASKPDSYDICFIPDGDTRGWLAERVAPETGAVVDRDGAVVGSHEGAHGYTVGQRRGLHLGVPAPDGRPRFVLEVRPVSNEVVVGPREALRIGEIAGERFTWAGAAPEDADAPFRCDVQIRAHADPVPASAMVSHVDGRVELVITPDSPLDGVAPGQTAVVYLGTRVLGQCTIDRTVAADAAVLR
>NZ_CP047185.1|WP_160034475.1|1861796_1864304_-|NAD-dependent-DNA-ligase-LigA
MSAVEPAARVEELRARIRSASDDYYAADSSPLSDAEYDALVRELAALEAEHPELAAEDSPTLTVGGIVGAGLAPIDHAERMLSLDNVFSAEELREWCEKTVASADRPVAWLTELKIDGLAISLHYEDGRLVTAATRGDGRTGEDVTVNALRVAGIPERLSGEGHPALVEVRGEVFIPVAAFAELNALQETLRDEAVEEARTRWSSRPPATRGVFEEEKARTSALRRFPTFANPRNAASGGLRQQLDKKSGLDLRAGEARVGSLALYVHGIGAWPDPPVATQSEVYGLLSSWGLPVSGHNRVSASVEEVLAFVDRYGRERHSVEHEIDGVVVKVDELELHDELGATSRAPRWAIAYKYPPEEVHTKLLDIVVSVGRTGRATPFAQMTKVKVAGSEVRQATLHNADVVKAKGVLIGDTVVLRKAGDVIPEVLGPVVELRDGSEREFVMPTQCPECGTTLAPAKEGDVDLRCPNAESCPAQVRGRVEHIGSRGALDIEALGEVSAAALTQPLVPAEPPLRTEAGLFELTVADLFPIEVVVRDSETGLQKLDAKGDPKVVTPFKRKRQLAKDGAFDPEAGAFAGDAASVPSTNALRLIENIERAKTKELWRLLVSLSIRHVGPVAARALAGYFGSLDAIRGARRDELAAVDGVGGIIADALIAWFEIDWHVEIVDRWAAAGVRFATPGHPGPGAADAAGGVLAGLTVVATGSLEGYSREGAQEAILAAGGKAGSSVSKKTDYVAAGPGAGSKLGKAEALGLRIITAAEFHLLVTEGPDAIALPEEASADAPEEAAAGPDEDVAGASHSDLSPEDDAVPEIDAVPDTTAPSTEEPTGPDA
>NZ_CP047185.1|WP_160034491.1|1881598_1882324_-|alpha/beta-fold-hydrolase
MTHEIRGGVVLPARREDIELHTADGLTLVGELALPLEREPVATLVTLHPLPTHGGFMDSHILRKAAARLPALADLAVLRFNTRGTASPRGTSEGAFGHGTEERADVAAALALVADRGLPHPWLVGWSFGTELALKWGREHPVEGAILLSPPLHRTSAEEVAAWGEDGRPLVALVPEFDDYLRPEAAAERFASVPQLDLVAVEGGKHLWVGEAQTRRVLDEIVRVVAPASSPLPTEWAGELG
>NZ_CP047185.1|WP_104223932.1|1882320_1882557_-|hypothetical-protein
MLAGFRRTESHAGREWNVQPVSAARAVKNYLCPGCGLTIDIGQPHLVTWRADGALGDAADLAGRRHWHTHCWRIRGAR
>NZ_CP047185.1|WP_160034493.1|1882663_1884412_-|sodium:proton-antiporter
MDYALLGVVGIITVVTVARFSSRLGIAAPLLLVVIGIGASYLPGVPDIEVEPELILAGVLPPLLYSAAIQVPLTDFRRNLRSIFGLSVLLVVVTALVVGGFLYLVFPDLSLPAAIALGAVVSPTDAVAATSIGKKLGLPPRLVTVLEGESLVNDASALVLLRAATAAAAVVGASVTTDAIDVGEVGVLFVYSVLMAIVLGLVMGVLTVFVRSKLRDPVLDTAVSFAVPFLAYIPAEELGASGVLAVVVTGIYTGHNSARFLSPQSRISERVNWRTAQFLLENGVFLLMGAEIKAIVSGVVDSGEFGVGTAVLLGLATVVILIVLRALFVWPLLLWLRSSGRRAERINRRLAVGLMRLRNSATSDERFRRRQVRAERLYLRRETDLAATTSEAFGWRGGVVLSWSGMRGVVTLAAAQSLPDETPYRSQLILIAFTVAVVTLLLQGATLPALIRLTGIQGTDGEADRRELATLLDEVAATGIQALPEAVAELPDGEAGERVLERVRRDTLTRSQVAWEQVGRAEDAPLGPHAQYLRLRRAVLLAEREALLDARGRGVYSSRTLRRAQLMLDAEETRLEMDDSSH
>NZ_CP047185.1|WP_104262836.1|1884471_1885212_-|hypothetical-protein
MVAQHPQTSVAHTPANRTSGRPAVPHQTPVRRSWARIPVTVLAFTASIAFAMVNVVDPSSGAVASPYYQAPARFNGDSAQRLVVADAVERTVQRDSFGAEAKPTPTPTPTPTPTETQTASATVDEEESGSAEAETAAPVQRAAAPDPGSAKAIAYDMIVQRGWADSEYDCLVLLWNRESGWNVYAENKSSGAYGIPQALPGSKMASAGSDWATNASTQITWGLGYISGRYGSPCGAWAHSESVGWY
>NZ_CP047185.1|WP_104226865.1|1885263_1885815_-|DivIVA-domain-containing-protein
MTAPFPRARESRPGYDTAEVDSFLASAREAYSQLSGGPADLRAADLRHTAFTLRKGGYSAPHVDAALERLEDAFALRERQYAIAARGEEAWLADARSTAQEIVNRLARAPRERFTRAGALTTGYNIRQVDAFADRISGYFRDGSVLTVDDVRTVSFAPQRGGYAEAQVDLLLDTVVDVMLAVR
>NZ_CP047185.1|WP_160034495.1|1885877_1886816_-|phosphatidate-cytidylyltransferase
MVTRDALRARAQQGRADVERQLEATRAQLEATNDRLTARSGRNLVSATAIGLLGGGAMVVSLLLVKELFMVLAGVVVLLAALELSNALRHAGRDIPRIPTGIVAVVAVPAAYYGGLGAAWATVLGGSVLVGLWRLGEQLLRRTASSRRDLALDIGLGAFVQGYTTFLGAFAIRLVAEPGGQLWAFAFLVLVIVVDTGAYVSGLTWGKHPMAPRISPKKTWEGFAGAAVAGIVVGVLLALLMLGQPWWVGAVFGAVVLLTATLGDLAESLIKRDIGIKDMSSWLPGHGGVLDRLDSILPSAAAAYVLYFLFAH
>NZ_CP047185.1|WP_104232499.1|1886896_1887451_-|ribosome-recycling-factor
MISDVLADAKTKMGKAVEVAKEDFSTVRTGRANPGMFQKVLVSYYGTPTPLSQLASMQNQEARTLVLTPYDKGSLRDIEQAIRDMPNLGANPTNDGTIIRVTLPELTAERRKEFVKIVRTKAEDAKIAVRNIRRKGKDDLDALKGDIGDDELARGEKELEALTKQHVDAIDEALKRKESELLEV
>NZ_CP047185.1|WP_104223894.1|1887483_1888215_-|UMP-kinase
MTETDAMTTGKRRRVLLKLSGEAFGAGTLGVNPDVISALAREIADAATEVEISVVVGGGNFFRGAELSQRGMDRGRADYMGMLGTVMNALALQDFLEQAGAETRVQSAIAMTQVAEPYIPRRAIRHMEKGRVVIFGAGAGLPYFSTDTVAAQRALETHADVVLVAKNGVDGVYDADPRTNPDAKKLDALTYQEALQRGLKVVDSTAFSLCMDNGMPMQVFGMEPSGNVAKAIRGAELGTLVSN
>NZ_CP047185.1|WP_104223895.1|1888350_1889178_-|elongation-factor-Ts
MANFSLADVKTLREQLGTGMVDTKNALVEADGDLDKAVEILRLKGAKGNAKRADRSTSEGLVAAAEKDGVATMIELACETDFVAKGTKFIALADAVLAAVVAAGSTTVEEALAAPADGKTVADLINDEAAILGEKVELRRVASVSGEHFAIYLHKTNKDLPPQVGVVVGYAGEDAETARSVAQHISFANPSYLSREDVPQSEVDNERRIVEEISRGEGKPEAALPKIIEGRVNAYFKQVALLDQDYAKDNKLSVSKVLSDAGLTVSGFARFKVGA
>NZ_CP047185.1|WP_104223896.1|1889356_1890304_-|30S-ribosomal-protein-S2
MAVVTMRQLLDSGVHFGHQTRRWNPKMKRFILTERSGSYIIDLQQSLAYIDKTYDFVKETVAHGGTILFVGTKKQAQNAISEQATRVGQPYVNQRWLGGLLTNFQTVSKRLARMKELEELDFDDTSKSGFTKKELLIKKRELDKLHKSLGGIRNLSKTPSALWVVDTKKEHLAIDEAKKLGIPVIGILDTNCDPDEVQYPIPGNDDAIRSVSLLTRIVADAAAEGLIQRHQKPEAEGNVSAVEPLAEWEQELLSTGAPAADVQEPNEQAGAETEKVADAEAETADEAVVEAETPAAEEAPEADAAATSTDETATA

Crispr_ID: NZ_CP047185_3

• CRISPR_ID: NZ_CP047185_3
• CRISPR_location: 2356415-2356570
• CRISPR_type: Orphan
• Repeat_type: NA
• Spacer_info: 1 spacers

Consensus repeat of NZ_CP047185_3

Consensus_repeat	Method
GCAAGGCGGAGGAGGAAGCGATACCGGCGGTATCGCGCCCGACGACAACGCCGC	CRISPRCasFinder

spacers of NZ_CP047185_3

>3.1|2356469|48|NZ_CP047185|CRISPRCasFinder
GAATGCCCCCTCCAGCACCCGCGGGCGCGGGCCGCGGAGGGGTCGGAT

CRISPR arrays and Neighbor proteins around NZ_CP047185_3

CRISPR arrays

The CRISPR arrays of NZ_CP047185_3

>merge|NZ_CP047185|3|2356415-2356570|CRISPRCasFinder
GCAAGGCGGAGGAGGAAGCGATACCGGCGGTATCGCGCCCGACGACAACGCCGCGAATGCCCCCTCCAGCACCCGCGGGCGCGGGCCGCGGAGGGGTCGGATGCAAGGCGGAGGAGGAAGCGATACCGGCGGTATCGCGCCCGACGACAACGCCGC

>NZ_CP047185|3|2|2356415-2356570|CRISPRCasFinder
GCAAGGCGGAGGAGGAAGCGATACCGGCGGTATCGCGCCCGACGACAACGCCGC	GAATGCCCCCTCCAGCACCCGCGGGCGCGGGCCGCGGAGGGGTCGGAT
GCAAGGCGGAGGAGGAAGCGATACCGGCGGTATCGCGCCCGACGACAACGCCGC

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP047185.1|WP_104297193.1|2355299_2356139_-|NAD(P)H-hydrate-dehydratase	unknown	unknown	gnl|CDD|238576
NZ_CP047185.1|WP_160034974.1|2359215_2360238_-|magnesium/cobalt-transporter-CorA	unknown	unknown	gnl|CDD|213364
NZ_CP047185.1|WP_159914943.1|2366182_2366884_-|sigma-70-family-RNA-polymerase-sigma-factor	unknown	unknown	gnl|CDD|131992
NZ_CP047185.1|WP_104232782.1|2352268_2353771_-|oxidoreductase	unknown	unknown	gnl|CDD|99778
NZ_CP047185.1|WP_104224119.1|2368408_2369485_+|ribosome-small-subunit-dependent-GTPase-A	unknown	unknown	gnl|CDD|224084
NZ_CP047185.1|WP_104257090.1|2361851_2365688_+|multifunctional-oxoglutarate-decarboxylase/oxoglutarate-dehydrogenase-thiamine-pyrophosphate-binding-subunit/dihydrolipoyllysine-residue-succinyltransferase-subunit	unknown	unknown	gnl|CDD|237030
NZ_CP047185.1|WP_104224449.1|2350459_2350762_-|thiamine-binding-protein	unknown	unknown	gnl|CDD|376658
NZ_CP047185.1|WP_160034968.1|2350813_2352127_-|DUF2029-domain-containing-protein	unknown	unknown	gnl|CDD|378217
NZ_CP047185.1|WP_160034963.1|2345733_2346966_+|hypothetical-protein	unknown	unknown	unknown
NZ_CP047185.1|WP_104246745.1|2349116_2350331_-|MFS-transporter	unknown	unknown	gnl|CDD|225371
NZ_CP047185.1|WP_160034970.1|2353767_2354643_-|FAD:protein-FMN-transferase	unknown	unknown	gnl|CDD|376782
NZ_CP047185.1|WP_160034972.1|2356594_2357641_-|DUF21-domain-containing-protein	unknown	unknown	gnl|CDD|224173
NZ_CP047185.1|WP_159914941.1|2365922_2366186_-|alpha-ketoglutarate-decarboxylase	unknown	unknown	gnl|CDD|188261
NZ_CP047185.1|WP_104224453.1|2354629_2355130_-|FMN-binding-protein	unknown	unknown	gnl|CDD|214897
NZ_CP047185.1|WP_104232788.1|2369481_2369976_+|thioredoxin-dependent-thiol-peroxidase	unknown	unknown	gnl|CDD|224146
NZ_CP047185.1|WP_159914945.1|2367049_2368405_+|3-phosphoshikimate-1-carboxyvinyltransferase	unknown	unknown	gnl|CDD|235037
NZ_CP047185.1|WP_104225499.1|2357633_2359010_-|HlyC/CorC-family-transporter	unknown	unknown	gnl|CDD|224173
NZ_CP047185.1|WP_159914921.1|2347009_2347669_+|response-regulator	unknown	unknown	gnl|CDD|225107
NZ_CP047185.1|WP_104246650.1|2360266_2361706_-|GuaB1-family-IMP-dehydrogenase-related-protein	unknown	unknown	gnl|CDD|181127
NZ_CP047185.1|WP_160034965.1|2348042_2349080_-|alcohol-dehydrogenase-catalytic-domain-containing-protein	unknown	unknown	gnl|CDD|176221

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
NZ_CP047185.1|WP_104297193.1|2355299_2356139_-|NAD(P)H-hydrate-dehydratase	gnl|CDD|238576	cd01171, YXKO-related, B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of the ATP binding site, the substrate binding site and the Mg2+binding site and structural homology this group is a member of the ribokinase-like superfamily.	1.33216e-46
NZ_CP047185.1|WP_160034974.1|2359215_2360238_-|magnesium/cobalt-transporter-CorA	gnl|CDD|213364	cd12830, MtCorA-like, Mycobacterium tuberculosis CorA-like subfamily. This bacterial subfamily belongs to the Thermotoga maritima CorA (TmCorA)-like family of the MIT superfamily of essential membrane proteins involved in transporting divalent cations (uptake or efflux) across membranes. This subfamily includes the Mg2+ transporter Mycobacterium tuberculosis CorA (which also transports Co2+). Thermotoga maritima CorA forms funnel-shaped homopentamers, the tip of the funnel is formed from two C-terminal transmembrane (TM) helices from each monomer, and the large opening of the funnel from the N-terminal cytoplasmic domains. The GMN signature motif of the MIT superfamily occurs just after TM1, mutation within this motif is known to abolish Mg2+ transport by a related protein, Saccharomyces cerevisiae Alr1p. Natural variants in this signature sequence may be associated with the transport of different divalent cations. The functional diversity of the MIT superfamily may also be due to minor structural differences regulating gating, substrate selection, and transport.	2.85187e-149
NZ_CP047185.1|WP_159914943.1|2366182_2366884_-|sigma-70-family-RNA-polymerase-sigma-factor	gnl|CDD|131992	TIGR02947, putative_RNA_polymerase_sigma_factor, RNA polymerase sigma-70 factor, TIGR02947 family. This group of sigma factors are members of the sigma-70 family (TIGR02937). They and appear by homology, tree building, bidirectional best hits and (with the exception of a paralog in Thermobifida fusca YX) one-to-a-genome distribution, to represent a conserved family. This family is restricted to the Actinobacteria and each gene examined is followed by an anti-sigma factor in an apparent operon.	2.07847e-92
NZ_CP047185.1|WP_104232782.1|2352268_2353771_-|oxidoreductase	gnl|CDD|99778	cd00322, FNR_like, Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and has a variety of physiological functions including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation in many organisms. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one- electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and 2 electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).	3.94222e-40
NZ_CP047185.1|WP_104224119.1|2368408_2369485_+|ribosome-small-subunit-dependent-GTPase-A	gnl|CDD|224084	COG1162, COG1162, Predicted GTPases [General function prediction only].	2.38461e-80
NZ_CP047185.1|WP_104257090.1|2361851_2365688_+|multifunctional-oxoglutarate-decarboxylase/oxoglutarate-dehydrogenase-thiamine-pyrophosphate-binding-subunit/dihydrolipoyllysine-residue-succinyltransferase-subunit	gnl|CDD|237030	PRK12270, kgd, multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit.	0
NZ_CP047185.1|WP_104224449.1|2350459_2350762_-|thiamine-binding-protein	gnl|CDD|376658	pfam01910, Thiamine_BP, Thiamine-binding protein. The crystal structure of two of these members shows that this domain has a ferredoxin like fold and is likely to exists as at least homodimers. Sulphate ions are are located at the dimer interfaces, which are thought to confer additional stability. Although the function of this domain remains to be identified, its structure suggests a role in protein-protein interactions possibly regulated by the binding of small-molecule ligands. Solution of the structure of the hyperthermophilic anaerobic Thermotoga maritima sequence, UniProtKB:Q9WYV6, shows that this has a beta-alpha-beta-beta-alpha-beta ferredoxin-like fold and assembles as a homotetramer. It was possible to identify a pocket in each monmer that bound an unidentified ligand. It was also found that it bound charged thiamine though not hydroxymethyl pyrimidine. It is proposed that it is transporting charged thiamine around the cytoplasm. Under oxidative conditions this bacterium is under stress, and the transcriiptional unit within which this protein is expressed is up-regulated in these conditions, suggesting that the chelation of cytoplasmic thaimine is part of the response mechanism to such oxidatvie stress, which is mediated by this family.	1.54734e-32
NZ_CP047185.1|WP_160034968.1|2350813_2352127_-|DUF2029-domain-containing-protein	gnl|CDD|378217	pfam09594, GT87, Glycosyltransferase family 87. The enzymes in this family are glycosyltransferases. PimE is involved in phosphatidylinositol mannoside (PIM) synthesis, a major class of glycolipids in all mycobacteria. PimE is a polyprenol-phosphate-mannose-dependent mannosyltransferase that transfers the fifth mannose of PIM. The family also includes alpha(1-->3) arabinofuranosyltransferase, invloved in the synthesis of of mycobacterial arabinogalactan.	0.007481
NZ_CP047185.1|WP_104246745.1|2349116_2350331_-|MFS-transporter	gnl|CDD|225371	COG2814, AraJ, Arabinose efflux permease [Carbohydrate transport and metabolism].	3.9533e-76
NZ_CP047185.1|WP_160034970.1|2353767_2354643_-|FAD:protein-FMN-transferase	gnl|CDD|376782	pfam02424, ApbE, ApbE family. This prokaryotic family of lipoproteins are related to ApbE from Salmonella typhimurium. ApbE is involved in thiamine synthesis. It acts as an FAD:protein FMN-transferase, catalyzing the attachment of an FMN residue to a threonine residue of a protein via a phosphoester bond in such bacterial flavoproteins.	1.37324e-27
NZ_CP047185.1|WP_160034972.1|2356594_2357641_-|DUF21-domain-containing-protein	gnl|CDD|224173	COG1253, TlyC, Hemolysins and related proteins containing CBS domains [General function prediction only].	2.27712e-72
NZ_CP047185.1|WP_159914941.1|2365922_2366186_-|alpha-ketoglutarate-decarboxylase	gnl|CDD|188261	TIGR02949, putative_anti-sigma_factor, anti-sigma factor, TIGR02949 family. This group of anti-sigma factors are associated in an apparent operon with a family of sigma-70 family sigma factors (TIGR02947). They and appear by homology, tree building, bidirectional best hits and one-to-a-genome distribution, to represent a conserved family. This family is restricted to the Actinobacteria. [Transcription, Transcription factors].	8.29235e-09
NZ_CP047185.1|WP_104224453.1|2354629_2355130_-|FMN-binding-protein	gnl|CDD|214897	smart00900, FMN_bind, This conserved region includes the FMN-binding site of the NqrC protein as well as the NosR and NirI regulatory proteins.	8.92426e-05
NZ_CP047185.1|WP_104232788.1|2369481_2369976_+|thioredoxin-dependent-thiol-peroxidase	gnl|CDD|224146	COG1225, Bcp, Peroxiredoxin [Posttranslational modification, protein turnover, chaperones].	1.41875e-71
NZ_CP047185.1|WP_159914945.1|2367049_2368405_+|3-phosphoshikimate-1-carboxyvinyltransferase	gnl|CDD|235037	PRK02427, PRK02427, 3-phosphoshikimate 1-carboxyvinyltransferase; Provisional.	5.91257e-149
NZ_CP047185.1|WP_104225499.1|2357633_2359010_-|HlyC/CorC-family-transporter	gnl|CDD|224173	COG1253, TlyC, Hemolysins and related proteins containing CBS domains [General function prediction only].	5.05501e-117
NZ_CP047185.1|WP_159914921.1|2347009_2347669_+|response-regulator	gnl|CDD|225107	COG2197, CitB, Response regulator containing a CheY-like receiver domain and an HTH DNA-binding domain [Signal transduction mechanisms / Transcription].	1.37793e-26
NZ_CP047185.1|WP_104246650.1|2360266_2361706_-|GuaB1-family-IMP-dehydrogenase-related-protein	gnl|CDD|181127	PRK07807, PRK07807, GuaB1 family IMP dehydrogenase-related protein.	0
NZ_CP047185.1|WP_160034965.1|2348042_2349080_-|alcohol-dehydrogenase-catalytic-domain-containing-protein	gnl|CDD|176221	cd08260, Zn_ADH6, Alcohol dehydrogenases of the MDR family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. This group has the characteristic catalytic and structural zinc sites of the zinc-dependent alcohol dehydrogenases. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.	4.43267e-156

Protein sequences

>NZ_CP047185.1|WP_104297193.1|2355299_2356139_-|NAD(P)H-hydrate-dehydratase
MGERVGTAEAARSIRVPREDDDKYTRGVLGIATGSERYPGAAVLGVEAAVRTGVGMVRYLGPERPAGLVLARRPEVVTAVGRVQAWLVGSGTSAEDRSDEERRTLIEQLHSGVPVVLDAGALDLIDEAAGPVVITPHYRELAGVLGRAGLDADAATIAEAPGEWARRAADRLGVCVLLKGGTTHVVAGGVELEVSGSTPWLATAGSGDVLGGVLGALLAGRAADAEAAGTTLTAEDLAPVAAAAAVLHAEAGRSASAGGPIAALDIAEHLPGVVAALLR
>NZ_CP047185.1|WP_104224453.1|2354629_2355130_-|FMN-binding-protein
MTAKTTTPARYALTLLAGAGTLAALAACSSTTTTGSDAADAATTTAPSTATSSAPEATGAASSAASGSSYADGTYEAEGAYTSPGGNEKVGVSLTLADGVVTDVTVTPESENPTGQQYQSRFAGGIAGEVVGKQLDELKVSKVSGSSLTSGGFNDAVETIKADATA
>NZ_CP047185.1|WP_160034970.1|2353767_2354643_-|FAD:protein-FMN-transferase
MPRPDAPTVLGHAWRFDAIGTGWQIDTAEPLEPSHRSRVEARIAEYDRTWSRFRDDSAVSQLRVGGEHVFPDEAADLFALYDVLDELTGGAVTPFVGGSLEQLGYDSAYTLVPRGPAVPAPSWAAARRGAAGLRVEPGTVVDVGAAGKGQLVDLVLEELDGAGPAVVDASGDLRGVGAGPVRVGLEHPWDPSSALGVAVPGDRALCGSASNRRAWGSGLHHVLDGRTGAPVESIVATWAVADTALVADGLATALFVCPPEALAERFDFEFVRVRSDGTLHYSPSFPGEVFR
>NZ_CP047185.1|WP_104232782.1|2352268_2353771_-|oxidoreductase
MIGTFDRALGRVTTYRLVWMTLAALLLVAVGYAAAGLIFSTPLEILGTTLVAVASTALVSAVLARLFRSRAHLESSLVTGLLIACLLFPTADPRGLAVIALVGAIAAASKYVLAWRGRHLFNPAAVAVLIIGFTGLNAGAWWIASGAIWPFVVVGSLLIVARVRRWAVFAVFVVVAGGVSVQQAVQNGQDLGAAAALVLTAYPFVFAGAFMLTEPLTLAPRRSQQLIIAVVAALVASVPFHIGVVSATPELGLVVGNALAFAFAFRQRRRHTLELASTRVLAPGIAEYRFRSRSPLTFEPGQWLELDLPHRADSRGSRRTFSVSSAPSDGEIAIALRMPEKASSFKRALAALEPGDSLRATSVGGDFVLPADPAVPLLLVAGGIGITPFASQLRSLADGPRRDVVVVVAAPSLAEVAYRDLLQESGARVVLCSKEAPTDLPARWSHVTGRLTAELLADAVPDAGRRVGYVSGSPSFVDSVRGALRGAGAKRIRTDAFAGY
>NZ_CP047185.1|WP_160034968.1|2350813_2352127_-|DUF2029-domain-containing-protein
MPSSPPRASSRPLARLRENRDSVAVLWGAFALVHVVLSLLALFAPGLPMGDVSIVYKEWMRTAVEGGGIAGIDTGWVYPILAWGPIAASWLFGSAGYDPMWLVLVALADAAAFALLLRGRSAPRLAAARWWLLFLVLLGPIAIGRIDAFTAPPAIAGMLWAATRPGVAALLLTVATWIKVWPAAILAAAVLVLRGRLRMILVPAVASVIIVLAVVLVGGGDQVFSFVTDQTDRGLQIEAVVSTPWMWLSVLPGSGSYVYYAADINTFEMHGPGTEFAASLMTPLLALAMLGVALLGARALARRADPARLFPLLALTFVVVFIDTNKVLSPQYIVWLAPPVIAGLIACRDGAFDRPAKLTLVTAALTQVVYPYLYLFLLWSHWWMVLVLTVRNILLVVLLGWLLRELWRMGTARVVAPGATTSASSLTGETRLAPQGS
>NZ_CP047185.1|WP_104224449.1|2350459_2350762_-|thiamine-binding-protein
MLVAFSVAPSGGEAPDASVHDAVAAAVRIVRESGLPSRTTSMFTEIEGEWDEVFDVVKRATEAVGAFGTRVSLVLKADIRPGYSGEIDGKIARLNDALGE
>NZ_CP047185.1|WP_104246745.1|2349116_2350331_-|MFS-transporter
MGGFGIGSTEFVAMGLLPQLAADLLPGVWAASQEQAVSQAGMLISAYALGVVVGAPTIAAAAARWPRKRLLLTLLVAFTVGTIGSALLPSFPLVLAARFVAALPHGAYFGIASLVAADLMGPGKRGKGVAFVLSGLTIANVVGVPAITWVGQVAGWRSAYLVVAVLFALTVVAVQLLVPAQPGNPAATVRNELRAFGRLQVWMTLLVGAIGFGGLFAMYSYISPLATEVTGLPLGAVPWILVVIGLGMTVGNLVGGWAADRDVRRALVVFFAGVGVSLIGLALSASSVVGLVVFAFLSAGFSAAASPAIQTRLMDVARDSQTIAAALNHSALNIGNSVGAALGGLTIAAGLGYLSPIWVGVGLTAAGIVLAFGSIAIDRARGTVYPVHREPAQPGTGGIPVDAL
>NZ_CP047185.1|WP_160034965.1|2348042_2349080_-|alcohol-dehydrogenase-catalytic-domain-containing-protein
MRAVSYSSFSALPAIVEVPEPACPVDGVLVRVAATGVCRSDWHAWKGHDDSVVLPQIPGHEFAGTVIATGAQVSLFAVGDRVTAPFVFACGDCEQCREGATQVCLRQQQPGFTLDGSFAESVVVPGADLNLVRLPASVGFVEAAGLGCRFGTAYHALHVRGRVAPGEWVAVLGCGGVGLSAVIVALAAGARVVASDVSAPAREAAAALGAVTVSGGEGAAEAIRAATGGGAHLSVDAVGSRATAEASIAALRPRGRHVQVGLLLGPDAAPAIPLGRVIAQELELLGSHGIARSGYTALLDDIVAGRLRPADSVGRTIAFEDLPAALAAMDAPAAAPGMTVAVLAP
>NZ_CP047185.1|WP_159914921.1|2347009_2347669_+|response-regulator
MTPTADSKITLAVVDDHKMLLGALTEWIRGAASDIQLVAAVASWPELLTHPEFPVDVVLLDLDLKDNIPISVKLSTLKTTGVKTVLMSTYSEPAVVREALASGALGYLVKTEDADMIVEAIRAAKDGHSYISHELDMALSTGDSDGAPKLSAQERRVMALYGGGEPVKSVAFELGISEETAKSYLKRIREKYRVVGIDVGTKVALRKRAIHDGILIETD
>NZ_CP047185.1|WP_160034963.1|2345733_2346966_+|hypothetical-protein
MSAAPESPAPLLGRVPATPGRSSRSTRSIRRQQEGLGTNYLGSGLNGIAAAIMAYELLIFLSTSARYGDLAPAAIAWVLVVLAFGAAVLAIHLGGRRLPLPVYLCFLLAVGIAVVLDLVAVTESGSARTVPTAAVAGAVAHAALIVHRRGIEILAVSALVSIAEVIAFLSMESGGAGALSVRISALVVTIAPAVVVVVMMRGFRRMVQLEIDRALVQSTTLGPRYAVGMLASEELARLDLAAERLLAEVGDGSVPLPLDAQRAALAASLATQLRLHLIEGRRETWLHHAVLESELLAPLVDLDDPDGTAGLLGHQQRDGLLSAIWLIADSATGLAVVLHVESGSPRDPGAETAARGLLVPITLRSSGAPLHGVDPATWEAIAQVGVFRDTSRDGELRIEIDCLVDNPADR
>NZ_CP047185.1|WP_160034972.1|2356594_2357641_-|DUF21-domain-containing-protein
MSDWAGIAWLVVLLAANAFFVGAEFAVISARRSQIEPLAESGRRSAITALAAMEHATLMLATTQLGITVCSLLILNVSEPAIHHLLEVPLRAVGIPDELSGTVAFVITLLIVSFLHVVLGEMVPKNISFSMPDRAVLLLAPPLVAIARVLRPIIVALNAVSNGVLRLFKVEPKDEANSTFTLEEVQTIVDQSTREGTLRDSTGTLLAAFEFTEKKVHDVALPLDGIVSLPSGATPADVERAVAKHGFSRYVILGEDGTPEGYIHLKDVLDLDGDTEGAKFRLPVPAKRIRQLASIFEATDLEDALAIMRRTGAHLARAFDEQGRATGVLFLEDIIEELVGEVDDATRR
>NZ_CP047185.1|WP_104225499.1|2357633_2359010_-|HlyC/CorC-family-transporter
MGTEWLLLGVGLLLTLGTGVFVASEFALVNLDRADLEARRDRGETRLGMTIAALRVTSTHLSSAQLGITLTTLLTGYTMEPALSTLLQEPFSGLGIPEEALAPVMTVVAIVIATLLSMILGELVPKNFALALPRATAKLVVPLQTAFTTVFRPAVALLNGSANALLRLVGIEPKEELSGARSAEELSSLVRHSASAGLLEEDTADLLGRTLRFSALTAGDVMTPRLRLSTVERASTAQDVLDLARTTGFSRFPITDDDIDDIVGVVHVKQAVAVPRGKRSDVPVTALRSEPLRVPETMKLDVLLTELRGRGFQLAVVVDEYGGTAGVATLEDLVEELVGEVADEHDRSRADVVKLPGSTTFPGMLRPDEVLDRAGVHIPEEGPYETVAGFVMSELGRLPAVGDRVDVEGGSLRVERLDGRRIDRLRFTPDPDADPDGIPDPLADVARGHRGRKESDDE
>NZ_CP047185.1|WP_160034974.1|2359215_2360238_-|magnesium/cobalt-transporter-CorA
MTIVDNAVYVDGRRIRNPDSLEDTFELMRDEHGMAWIGLYRPTREEVEAVAEEFGLHPLAVEDALSGHQRAKLERYDDGLFVVLRPARYADAAETVVFGELHVFVGPDFVVTIRHADSPDLARVRRRLEEDPALLARGPEAVLYAILDQVVDEYAPVVFGVQGDVDEIEDQLFGDDSDDGLSERIYRLSREVIHFQRSVQPLTALLHELLQESTPVEGEPSPSPERIELRRSLRDVLDHTIRVTEAVDSLRAILDQALTVHSTLVSRRQTETGLAQNDVVRKISSWAAILFAPTLVAGIYGMNFDDMPELHWRLGYPWALGLMVLFGFALYAVFKRKKWL
>NZ_CP047185.1|WP_104246650.1|2360266_2361706_-|GuaB1-family-IMP-dehydrogenase-related-protein
MRFSGGTPSGDLTYSDVFLVPGRSSVTSRLDVSLAPGDGTGATIPVVSSNMNSVTGQRLAATLARRGGLGVLPQDMPLQALDAAIRWVKRQPVAFSGALTASPATTVEEALRILPAVAGHGFVVQEEGGAILGCVPAARLATALPDARLGDLVHSATPSIDADDVPTARAAFDLMVAADLDFAPVLHHGALVGTLSRTGALRSTVYDPALDADGRLRVAAAIGINGDVEAKARALVSAGVDVLVLDTAHGHQEGMLRALRTVSALDLGVPIAAGNVVTADAVHDLVDAGADILKVGVGPGAMCTTRMMTAVGRPQFSAVLETAERAHELGAHVWADGGVRYPRDVALALAAGAASVMIGSWFAGTIEAPGELRSDAAGRVYKESWGMASAKAVQERFDRLDAYELARKRLFAEGISSSTIYLDPLRPSVEDLLDMITSGVRSSFTYAGARSVADFHERAHVGLQSAAGYEEGKALPVSW
>NZ_CP047185.1|WP_104257090.1|2361851_2365688_+|multifunctional-oxoglutarate-decarboxylase/oxoglutarate-dehydrogenase-thiamine-pyrophosphate-binding-subunit/dihydrolipoyllysine-residue-succinyltransferase-subunit
MRRARPDDRGRINGESGRSAVSSQLTGAGTEQGAEDFGANEWLVEELYEQYSADRASVDESWWPILERYGAQLANSGKDAPAPAPAAAPAPAASKPAAAAERVSSSGGGAVTHPAAASSSESTPASRTTSKQPKAQPIPADAPVSKPSAEDSTPDEDVVTPLRGMAKSLATNMDASLSIPTATSVRTIPAKLMIDNRIVINNHLRRTRGGKVSFTHLIGWALIRALKDFPSQNVFYDEVDGKPAVVAPAHVNLGIAIDMPKPDGTRALLVPSIKRADTLSFTAYLSAYEDLVKRARGNKLVAGDFAGTTLSLTNPGGIGTVHSVPRLMKGQGCIIGAGALEYPAEFQGASEKTLVELGIGKTITLTSTYDHRVIQGAGSGEFLKIVHELLLGGRGFYEDIFAALRIPYDPIHWSTDIAVDLAERVSKTARVQELINSFRVRGHLMADVDPLEYVQRSHPDLAIESHGLTFWDLDREFVTDGFGGKRQLKLRDILGILRDSYCRTVGVEYMHIQDPEQRAWMQQKLERGYEKPGHDEQLRILGKLNEAEAFETFLQTKYVGQKRFSLEGGESLIALLDAVLQGAADEHLDEVAIGMAHRGRLNVLTNIAGKTYGQIFREFEGTQDPRTVQGSGDVKYHLGTEGTFRGAAGEEIPVYLAANPSHLEAVNGVLEGIVRAKQDRKPIGTFTTLPILVHGDAAMAGQGVVVETLQMSQLRAYRTGGTIHININNQVGFTTPPHEARTSIYSTDGAKTIQAPIFHVNGDDPEAVVHVGQLAFEYRQRFHRDVVIDLICYRRRGHNEGDDPSMTQPLMYSLIEAKRSVRKLYTEALVGRGDITEEEYDRAHQDFQDRLERAFAETHAAQTGAIPVITADGDSVADLELPDAQQGEDYPGEPEVTGVKTEVVTRIGDAFTTPPEGFTVHPKLQQLLAKRQEMSRSGSIDWAFGELLALGSLLLEDTPVRLVGQDTRRGTFVQRHAVLHDRENGQEWLPLMNLSEQQARLWIYDSLLSEYAAMAFEYGYSVERPDSLVLWEAQFGDFANGAQIVIDEFISSAEQKWGQRSSLVLLLPHGYEGQGPDHSSARIERYLQMCAERNMTVARPSTPASYFHLLRRQAYSRPRRPLIVFTPKAMLRLRGASSPVEDFTSGRFQPVIDDARIQDASAVKRVLLHAGKVHYDLKAELEKKPDDGIALVRVEQYYPAPIEELRGIAERYPDAELVWVQDEPENQGAWPFMALEVAPKLGRSMRVVSRPSAASPAAGSAKRHASEQADLLSRALTR
>NZ_CP047185.1|WP_159914941.1|2365922_2366186_-|alpha-ketoglutarate-decarboxylase
MTDSGCTKAKAELEEYLHNELCKEDAADIREHMAGCIDCADEAKVGVVLTVAVQRACKETAPEDLRAQVLGMLRDEHAAHSQTPARL
>NZ_CP047185.1|WP_159914943.1|2366182_2366884_-|sigma-70-family-RNA-polymerase-sigma-factor
MTRDDEPRTTSADEAPEPADAEQTIVETVEESLDDAPVEAPVDLRSLFEQQALPFIDQLYAAGLRMTKNPSDAQDLVQETFAKAFGAFRQFEQGTNLKAWLYRILTNTFINSYRKKQREPYQSAIDELEDWQLGGAESTTATSSRSAEAEAIDHLPDTAVKEALQAIPEDFRLAVYFADVEGFSYQEIADIMKTPVGTVMSRLHRGRRMLRERLTDYARERGFRAAFTSGSTK
>NZ_CP047185.1|WP_159914945.1|2367049_2368405_+|3-phosphoshikimate-1-carboxyvinyltransferase
MVFSRYSAPEFDPYGDARALPGDDAWPAPLAAGALDAEVGLPGSKSLTNRELVLAALADGPSTLRAPLHSRDSALMIEALRSLGTTIRESGSTGGFGADLVVEPAEELLGSTTIDCGLAGTVMRFVPPLAGLALGPTTFDGDAYAAKRPMGATIASLRALGVDVADDGRGALPFTVHGSGSVRGGDVVVDASRSSQFVSALLLAGARFDEGLHLRHEGSAVPSRPHIDMTVAALAARGVEVGTPADGEWTVARQPIAGADVLIEPDLSNAAPFLAAALVTGGRVRLRHWPAVTTQVGAHLERILPLFGARVERDGEDLVVTGGDEILGVDLDLSEGGELAPALAALAALASTPSTLTGIGHIRHHETDRLAALAAEITGLGGRVTELEDGLRIEPAELHGGRWRTYSDHRMAHAGALIGLVVPGVVIEDVATTAKTLPQFPELWTTLAGSV
>NZ_CP047185.1|WP_104224119.1|2368408_2369485_+|ribosome-small-subunit-dependent-GTPase-A
MSWWTDSGLDADGALDDFDGYDESDARVRPNPKGTKPRTKNRPAYEDAEIAMVLGVDRGRYTVMIGDGTPEEHEFTAARARELRRQAIVAGDRVDVVGDSSGDEGTLARIVRIRERSTLLRRSADDTDAIERVIVANADQMLCVVAAADPEPRTRLVDRYLVAAFDAGITPMLCITKTDLADPAPFLRNFEGLDLRVFLSSQDEPPVDEIADALLGHETVVVGHSGVGKSTLVNKLVPDAHRAIGRVNTVTGRGRHTSSSTVSLRVERGDRHGWVIDTPGVRSFGLGHVNTDNILGAFTTLAVIARDCPRGCTHLPDSPDCAIIEAVEGGLLGASGPERLDSLQRLLTTFATTDGSRR
>NZ_CP047185.1|WP_104232788.1|2369481_2369976_+|thioredoxin-dependent-thiol-peroxidase
MTDLSPLPAEARLAAGDSAPEFTLPNQDGEPVSLADYRGRRVILFFYPEADTPGCTTEACDFRDNAASLRDSGYEVLGISRDAPEALRRWADAQGIAYPLLSDPDMTVHRAYAVWGEKSLYGKTVVGVLRSTFVVGAEGALEFAQYGVRATGHVQALRKKLKLV

Crispr_ID: NZ_CP047185_4

• CRISPR_ID: NZ_CP047185_4
• CRISPR_location: 2446501-2446692
• CRISPR_type: Orphan
• Repeat_type: NA
• Spacer_info: 4 spacers

Consensus repeat of NZ_CP047185_4

Consensus_repeat	Method
GCCGCCGGAGCACCCGCCTTCACC	CRISPRCasFinder

spacers of NZ_CP047185_4

>4.1|2446525|18|NZ_CP047185|CRISPRCasFinder
GTCGCGGAATCGGGCTTC
>4.2|2446567|18|NZ_CP047185|CRISPRCasFinder
GCCGGAGCACCCGCCTTC
>4.3|2446609|18|NZ_CP047185|CRISPRCasFinder
CCAGGACCGTCCGGCTCG
>4.4|2446651|18|NZ_CP047185|CRISPRCasFinder
GCCGGAGCGCCTGCCTTC

CRISPR arrays and Neighbor proteins around NZ_CP047185_4

CRISPR arrays

The CRISPR arrays of NZ_CP047185_4

>merge|NZ_CP047185|4|2446501-2446692|CRISPRCasFinder
GCGGCCGGAGCATCCGGCTTCCCTGTCGCGGAATCGGGCTTCGCTTCCCGGGCATCCGCCTTCGCCGCCGGAGCACCCGCCTTCACCCCAGGACCACCCGCCTTCACCCCAGGACCGTCCGGCTCGGCTGCCGGAGCACCCGCCTTCACCGCCGGAGCGCCTGCCTTCGCGGCCGGAGCATCCGGCTTCGCC

>NZ_CP047185|4|3|2446501-2446692|CRISPRCasFinder
GCGGCCGGAGCATCCGGCTTCCCT	GTCGCGGAATCGGGCTTC
GCTTCCCGGGCATCCGCCTTCGCC	GCCGGAGCACCCGCCTTC
ACCCCAGGACCACCCGCCTTCACC	CCAGGACCGTCCGGCTCG
GCTGCCGGAGCACCCGCCTTCACC	GCCGGAGCGCCTGCCTTC
GCGGCCGGAGCATCCGGCTTCGCC

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP047185.1|WP_104232824.1|2443311_2443803_-|PH-domain-containing-protein	unknown	unknown	gnl|CDD|367615
NZ_CP047185.1|WP_160035022.1|2443802_2444570_-|biotin--[acetyl-CoA-carboxylase]-ligase	unknown	unknown	gnl|CDD|223417
NZ_CP047185.1|WP_104225651.1|2441538_2442006_-|5-(carboxyamino)imidazole-ribonucleotide-mutase	unknown	unknown	gnl|CDD|376377
NZ_CP047185.1|WP_160036221.1|2440177_2441488_-|LytR-family-transcriptional-regulator	unknown	unknown	gnl|CDD|224235
NZ_CP047185.1|WP_104238027.1|2458865_2459699_+|purine-nucleoside-phosphorylase	unknown	unknown	gnl|CDD|236183
NZ_CP047185.1|WP_104223170.1|2455140_2456901_+|ATP-grasp-domain-containing-protein	unknown	unknown	gnl|CDD|227111
NZ_CP047185.1|WP_104225462.1|2449334_2449556_+|acyl-CoA-carboxylase-subunit-epsilon	unknown	unknown	gnl|CDD|379386
NZ_CP047185.1|WP_104223169.1|2452341_2453043_-|response-regulator-transcription-factor	unknown	unknown	gnl|CDD|225107
NZ_CP047185.1|WP_104223223.1|2436519_2437395_+|glycosyltransferase-family-2-protein	unknown	unknown	gnl|CDD|224137
NZ_CP047185.1|WP_104223228.1|2454346_2455042_+|septum-formation-inhibitor-Maf	unknown	unknown	gnl|CDD|178901
NZ_CP047185.1|WP_104223164.1|2444716_2446321_+|acyl-CoA-carboxylase-subunit-beta	unknown	unknown	gnl|CDD|227136
NZ_CP047185.1|WP_104225461.1|2450100_2451144_-|hypothetical-protein	unknown	unknown	unknown
NZ_CP047185.1|WP_160035028.1|2453066_2454371_-|class-I-SAM-dependent-RNA-methyltransferase	unknown	unknown	gnl|CDD|225174
NZ_CP047185.1|WP_104283337.1|2457322_2458759_-|NAD(P)H-quinone-dehydrogenase	unknown	unknown	gnl|CDD|236112
NZ_CP047185.1|WP_104223224.1|2439053_2440157_+|glycosyltransferase-family-4-protein	unknown	unknown	gnl|CDD|340838
NZ_CP047185.1|WP_160035018.1|2438178_2439024_+|dTDP-4-dehydrorhamnose-reductase	unknown	unknown	gnl|CDD|367904
NZ_CP047185.1|WP_160035026.1|2451140_2452355_-|ATP-binding-protein	unknown	unknown	gnl|CDD|226951
NZ_CP047185.1|WP_104232821.1|2437456_2438065_-|dTDP-4-dehydrorhamnose-3,5-epimerase-family-protein	unknown	unknown	gnl|CDD|376414
NZ_CP047185.1|WP_160035020.1|2442118_2443249_-|5-(carboxyamino)imidazole-ribonucleotide-synthase	unknown	unknown	gnl|CDD|235674
NZ_CP047185.1|WP_160035030.1|2459695_2461363_+|phospho-sugar-mutase	unknown	unknown	gnl|CDD|100092

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
NZ_CP047185.1|WP_104232824.1|2443311_2443803_-|PH-domain-containing-protein	gnl|CDD|367615	pfam03703, bPH_2, Bacterial PH domain. Domain found in uncharacterized family of membrane proteins. 1-3 copies found in each protein, with each copy flanked by transmembrane helices. Members of this family have a PH domain like structure.	1.29687e-08
NZ_CP047185.1|WP_160035022.1|2443802_2444570_-|biotin--[acetyl-CoA-carboxylase]-ligase	gnl|CDD|223417	COG0340, BirA, Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme metabolism].	6.84934e-46
NZ_CP047185.1|WP_104225651.1|2441538_2442006_-|5-(carboxyamino)imidazole-ribonucleotide-mutase	gnl|CDD|376377	pfam00731, AIRC, AIR carboxylase. Members of this family catalyze the decarboxylation of 1-(5-phosphoribosyl)-5-amino-4-imidazole-carboxylate (AIR). This family catalyze the sixth step of de novo purine biosynthesis. Some members of this family contain two copies of this domain.	2.34765e-75
NZ_CP047185.1|WP_160036221.1|2440177_2441488_-|LytR-family-transcriptional-regulator	gnl|CDD|224235	COG1316, LytR, Transcriptional regulator [Transcription].	4.25471e-27
NZ_CP047185.1|WP_104238027.1|2458865_2459699_+|purine-nucleoside-phosphorylase	gnl|CDD|236183	PRK08202, PRK08202, purine nucleoside phosphorylase; Provisional.	1.0208e-118
NZ_CP047185.1|WP_104223170.1|2455140_2456901_+|ATP-grasp-domain-containing-protein	gnl|CDD|227111	COG4770, COG4770, Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid metabolism].	0
NZ_CP047185.1|WP_104225462.1|2449334_2449556_+|acyl-CoA-carboxylase-subunit-epsilon	gnl|CDD|379386	pfam13822, ACC_epsilon, Acyl-CoA carboxylase epsilon subunit. This family includes the epsilon subunits of propionyl-CoA carboxylase, EC:6.4.1.3, and acetyl-CoA carboxylase, EC:6.4.1.2. These enzymes are involved in the biosynthesis of long-chain fatty acids. The epsilon subunit is necessary for an efficient interaction between the alpha and beta subunits of these enzymes.	4.62339e-05
NZ_CP047185.1|WP_104223169.1|2452341_2453043_-|response-regulator-transcription-factor	gnl|CDD|225107	COG2197, CitB, Response regulator containing a CheY-like receiver domain and an HTH DNA-binding domain [Signal transduction mechanisms / Transcription].	1.13154e-25
NZ_CP047185.1|WP_104223223.1|2436519_2437395_+|glycosyltransferase-family-2-protein	gnl|CDD|224137	COG1216, COG1216, Predicted glycosyltransferases [General function prediction only].	5.41959e-52
NZ_CP047185.1|WP_104223228.1|2454346_2455042_+|septum-formation-inhibitor-Maf	gnl|CDD|178901	PRK00148, PRK00148, Maf-like protein; Reviewed.	1.56907e-76
NZ_CP047185.1|WP_104223164.1|2444716_2446321_+|acyl-CoA-carboxylase-subunit-beta	gnl|CDD|227136	COG4799, COG4799, Acetyl-CoA carboxylase, carboxyltransferase component (subunits alpha and beta) [Lipid metabolism].	0
NZ_CP047185.1|WP_160035026.1|2451140_2452355_-|ATP-binding-protein	gnl|CDD|226951	COG4585, COG4585, Signal transduction histidine kinase [Signal transduction mechanisms].	1.68932e-10
NZ_CP047185.1|WP_104283337.1|2457322_2458759_-|NAD(P)H-quinone-dehydrogenase	gnl|CDD|236112	PRK07845, PRK07845, flavoprotein disulfide reductase; Reviewed.	0
NZ_CP047185.1|WP_104223224.1|2439053_2440157_+|glycosyltransferase-family-4-protein	gnl|CDD|340838	cd03809, GT4_MtfB-like, glycosyltransferases MtfB, WbpX, and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide.	5.60457e-77
NZ_CP047185.1|WP_160035018.1|2438178_2439024_+|dTDP-4-dehydrorhamnose-reductase	gnl|CDD|367904	pfam04321, RmlD_sub_bind, RmlD substrate binding domain. L-rhamnose is a saccharide required for the virulence of some bacteria. Its precursor, dTDP-L-rhamnose, is synthesized by four different enzymes the final one of which is RmlD. The RmlD substrate binding domain is responsible for binding a sugar nucleotide.	1.82582e-112
NZ_CP047185.1|WP_160035028.1|2453066_2454371_-|class-I-SAM-dependent-RNA-methyltransferase	gnl|CDD|225174	COG2265, TrmA, SAM-dependent methyltransferases related to tRNA (uracil-5-)-methyltransferase [Translation, ribosomal structure and biogenesis].	5.54716e-71
NZ_CP047185.1|WP_104232821.1|2437456_2438065_-|dTDP-4-dehydrorhamnose-3,5-epimerase-family-protein	gnl|CDD|376414	pfam00908, dTDP_sugar_isom, dTDP-4-dehydrorhamnose 3,5-epimerase. This family catalyze the isomerisation of dTDP-4-dehydro-6-deoxy -D-glucose with dTDP-4-dehydro-6-deoxy-L-mannose. The EC number of this enzyme is 5.1.3.13.	3.41991e-72
NZ_CP047185.1|WP_160035020.1|2442118_2443249_-|5-(carboxyamino)imidazole-ribonucleotide-synthase	gnl|CDD|235674	PRK06019, PRK06019, phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed.	3.22995e-160
NZ_CP047185.1|WP_160035030.1|2459695_2461363_+|phospho-sugar-mutase	gnl|CDD|100092	cd05799, PGM2, This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The mammalian PGM2 is thought to be a phosphopentomutase that catalyzes the conversion of the nucleoside breakdown products, ribose-1-phosphate and deoxyribose-1-phosphate to the corresponding 5-phosphopentoses. PGM2L1 is thought to catalyze the 1,3-bisphosphoglycerate-dependent synthesis of glucose 1,6-bisphosphate and other aldose-bisphosphates that serve as cofactors for several sugar phosphomutases and possibly also as regulators of glycolytic enzymes. PGM2 and PGM2L1 belong to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.	0

Protein sequences

>NZ_CP047185.1|WP_104223164.1|2444716_2446321_+|acyl-CoA-carboxylase-subunit-beta
MTANTERPAPDLYTTAGKIADLRNRYHEAVTASGEAAIEKQHAKGKMTARERIDTLLDPGSFVELDEFVRHRTHAFGMEKKRPYGDAVVTGTGTIHGRQVAVYSQDFTIFGGSLGEVAGEKIIKVMDLALKTGVPIIGILDSGGARIQEGVVALGKYGEIFRRNTAASGVIPQISIICGPAAGGAVYSPALTDFVIMVDKTSQMFVTGPDVIKTVTGEDVGMEELGGALTHNKISGVSHYLASDENDALDYARTLLSFLPDNNLSPVPVFETEVDLETTDADRFLDTVIPDSPNQPYDMRAVIEHIVDEGDFLEVQPLFAPNIVIGFGRVEGRSVGIIANQPSAMAGTLNIEAGEKASRFVRFCDAFSLPILTLVDVPGYLPGTDQEWTGVIRRGAKLLYAYAEATVPLVTVILRKAYGGAYIVMGSKQLGADINLAWPTAEIAVMGGQGAVNILYRNEIRKAEEAGEDVAAVRTRLANEYTYNVASPFLAAERGELDGVIEPSATRVSVIKALRALRTKRANLPAKKHGNIPL
>NZ_CP047185.1|WP_160035022.1|2443802_2444570_-|biotin--[acetyl-CoA-carboxylase]-ligase
MLLPLSSAVSPRVLALESAGSTNDELRERAAADPAVWPHLSVVATGDQRAGRGRLGRVWQAPAGRTLAASTLVDASALGAEASGWLPLVAGAALARALAPLVDGDVAVKWPNDVLIDGRKVAGILAERLPDGRVVVGTGVNLLLTEAELPVPTATSLALAGARTTSADEVLAAFLTGFQGLLAPLLAQGDAEASGAAAAVRASCGTLGTRVRLELPDGTQEEGTASALAPDGSLLLEQGGALRSFPAGDVTHLRS
>NZ_CP047185.1|WP_104232824.1|2443311_2443803_-|PH-domain-containing-protein
MARTDPADRELARLTPRARRAVAPVVGLLLLTWTGFYFAAQFELALQRWIIGLGTALLVLLLCAPGIAGWASVRYRVTASGLSARRGVASIRRAEVVFDRRMEVAVERSLGQRLARCGDVRILQAGAEVFVLRDLPDPELTADLLREAIGAAPALEQEWPPPA
>NZ_CP047185.1|WP_160035020.1|2442118_2443249_-|5-(carboxyamino)imidazole-ribonucleotide-synthase
MRVGVIGGGQLARMMIPAAVELGIEIAVLAESEGAPAGLAATRVGDYRDEATVLAFAETVDVVTFDHEHVPQPILRELVARGVAVHPGPDALLFAQDKLMMRRRLTELGVPVPEWAEVSSAEELGEFLAEHGGSAVVKTARGGYDGKGVRVVRGAHEADDWFSALAEDGRGGSLLVEELVGFRRELAQLVARRPSGESILWPVVESVQRDGVCAEVIAPAPASAGRLAAAAAEIAQTIADSLGVTGVLAVELFETTDDRILVNELAMRPHNSGHWTMDGSTTSQFEQHLRAVLDLPLGATGCRDPWTVMVNVLGGPVGESLTDRYPRVLADHPGVKVHNYGKEPRPGRKVGHVNAGGDDLDLVVYEARAAAAVLTD
>NZ_CP047185.1|WP_104225651.1|2441538_2442006_-|5-(carboxyamino)imidazole-ribonucleotide-mutase
MGSDSDWSVMQAASTVLAEFGVAHEVRVVSAHRTPEAMIAYGREARGRGLKVVIAGAGGAAHLPGMLAAVTSLPVVGVPVPLARLDGLDSLLSIVQMPAGVPVATVSIGGARNAGLLAVKILATADDALSAALDAFAADLEVQVAAKNDALVAGL
>NZ_CP047185.1|WP_160036221.1|2440177_2441488_-|LytR-family-transcriptional-regulator
MTRRAWWLLIVNLLVPGSAQVLAGNRRLGRLGLGFTLGLWVALLVAVLLYFVFPTGLYTLATFDVSMLALQAALVVYGVVWAVLTLDTLRLIRVVRVRPRMRGVLAFATIALMAVSVGTTAYGTYLLGVTRGTLSSIFGGGAIEQPIDGRYNVMLLGGDAGEDRDGLRPDSISVVSIDASSGKASIIGVSREFVDFPFPETSPMHELYPDGYDTENCAVDVCKLNSVYTEVELKHPELYPDAVDHGSEPGIEAMRDAVEGILDLRIQYYALIDMEGFAQLIDALGGIDIDYVADEPLPLGGLPDSDGVMQGVNQWIDPGHWHFNGEQALAYARSRYTTSDYDRMARQRQVQEALLAQFEPGNVLAKFQDVASAGSQVIKTDVPQGMLGYFVQLGLKTKSQPVDPIELVPPAVDPEDPDYDVVHSLVSAGLSGDSAP
>NZ_CP047185.1|WP_104223224.1|2439053_2440157_+|glycosyltransferase-family-4-protein
MLARVPGGIGRYTEELTRELIATAPRDCEVEAVVSAHPPEKEEELRLRLPGLARIHRLPLGRRELSRAWQYGIAIPAGGGMIHAPSLFAPLRSHDGSEGEQIAVTIHDTVPWTHPETLTPHGAKWHRAMAKRARKHADAVVVPTHAVAHQLSQLMDFGDRLRVIGGAVGSGLVVPEDADERATALGLPPEYVLSVGTLEPRKGLVSLIAAFGGASAPAIPLLLVGPTGWGDLDVASVADEQGLDETRVRALGVLSDADLAVVLSRATLFVYPSIAEGFGLPVLEAMHFGVPVVHSDDPALMEVAADAGVAVERGDAKDYPDRLALAMSSVLADTGLRERMSVAGRDRSRAFSWRDSAERVWALHADL
>NZ_CP047185.1|WP_160035018.1|2438178_2439024_+|dTDP-4-dehydrorhamnose-reductase
MTFLITGASGMLGTDLRATLGSRPSTALGRSDLDVTDLDAVRAAVAGHDAVVNCAAYTRVDDAETDEEEAHRVNAVGARNLALATAETGAALVQVSTDYVFDGSATTPYPEDHPRNPISAYGRTKAEGERLVLEANPERGYVVRTAWLYGEHGGNFAKTMVRLAGAHETLTVVDDQHGQPTWTADLAARLIELVDAEAPAGVYHGTSSGETTWLGFARAVFAKAGLDPERLRPTDSGSFVRPAPRPAYSVLGHDGWSRAGLPPLRSWQDALAAAPLEAVTP
>NZ_CP047185.1|WP_104232821.1|2437456_2438065_-|dTDP-4-dehydrorhamnose-3,5-epimerase-family-protein
MQIRELDIPDVYEVTPRQFPDDRGVFYEFYRFDRLAEKVGHPLSLRQGNTSVSRRGTVRGIHFAQIPPSQAKYVSCFSGAVLDYVIDVRVGSPTFGRWESILLDDVDRRSVYIAEGVAHAFVALTEGAVVSYLVNATFDPVREKGIDPLDEQIGLRFPEEAGELLLSPKDTDAPTLAEAEAQGLLPTWDEARAFYTELDSAS
>NZ_CP047185.1|WP_104223223.1|2436519_2437395_+|glycosyltransferase-family-2-protein
MARSTLPIAVVVVTHFSGEVLRACLESVPEATEHDVRIVVVDNLTTDDSVRSVVERLPQVEFHETGQNLGYGRAVNYAVDRLGPEVEWILVTNPDTVFLPGSIDALYAAATADDRIGSIGPRILDSDGTIYPSARALPSLGTGVGHAVFAHVWPGNPWSATYRRSRAVETLRHGRMEAGWLSGACVMVRRTAFEEIGGFDDRYFMYFEDVQLGDSLGQRGWTNVYLADAVVSHLGGHSTRLASARMLAVHHRSAYLYLAQKYGAWYQAPIRAAVRAGLGARVALMRLRSKS
>NZ_CP047185.1|WP_104225462.1|2449334_2449556_+|acyl-CoA-carboxylase-subunit-epsilon
MTASDSAPAVVISTPGLDAAEIAAVTAVVTALTSRTEAEPETPQELSGGWNDRAAAVRRPLRPAPGAWRSFSG
>NZ_CP047185.1|WP_104225461.1|2450100_2451144_-|hypothetical-protein
MIAYPRPLLQALGAGFSLYHVVLAFFSFRISPATPADLVAVALYVAATVVALWPGATTRLALPVAVGMTAVAVALPLLVAPSLDPGASNGYSTWYIAAVGTLMTIVCARRRAACAWVGVGFLIVHTVFWAGPAALATLGVVGGIAWVAIAQLLIVELGRAGSEARVLEAAERAAASWRAAEEAHLTEREVRLEQTRALAADMLLRIAEPGPGLTDEERRECRLLEAAVRDEIRGRRLLDDEVRRLVLDARRRGVTVSVLDDGGLDRTSEGESRRVLGELAQALSGIREEVDRVVVRTASADSASAVTVVGLRTAGDGSAGALGSDDAGDEVDAWVEIRRDGVGGRDV
>NZ_CP047185.1|WP_160035026.1|2451140_2452355_-|ATP-binding-protein
MAGAEAPIARRNAGRERIDRIISTVVSFFGFGFGVQTVPPILAQLPLLRPEVAWPVLALVFGSLTAAVVTAVLRRGTRTTAVLVAVGVLIALLTWPAAVSTGGADRETPWIWYLLTIGTAFCTIAAPLRIAIAYVSVTTVLFGLLRVLPSGGGAEPTRAILDAAYVGIVGFVMLVLITVLRQSADQIDRAQTTAMEQYEAAMRQHAGEVERVEVDALVHDNVLATLLSAASAESPAERALVSSMAQRTLAVLLPDHEPEPPEGLVPLELLQRQLAHAASTFGTEIAVATAEGVDPRATTLPRPVAEALLGAVWQALANSVQHAGPSGSVHRAVHGLLGDGAVEVVVEDDGRGFRLADVPRERLGIRLSILERVHNARGSARVDSTPGEGTRVVLSWRADAGGGP
>NZ_CP047185.1|WP_104223169.1|2452341_2453043_-|response-regulator-transcription-factor
MGGMEPHVDAAEAPRVRVAIVDDHESVRLGVAAAVESAGMQVVAAAETVQALESTIGGAEIEVLVLDLSLNDGSSITSNVKWGQVRGSAVLVHSIADRVVAVREALAAGAAGVIPKSSPMSTVVAAIRTVARGEVLNNLEWASAIDADDDFARAVLGRRERDVLHLYASGLPLKLVAERLQISVSTAKEYLDRIRDKYVEIGRPAPTKVDLLRRAVEDGILPGIDPDDGDGGR
>NZ_CP047185.1|WP_160035028.1|2453066_2454371_-|class-I-SAM-dependent-RNA-methyltransferase
MAQTPSRASARPDGADDALGTEIELDISNVAHGGVFVARHEGRVVFVPDVLPGERVRARISEVRHDSFWRAEALEVLEASEHRVEHVWPEAALDRRPEERVGGAELGHADLAYQRELKRLVLVDSFSRFARREIEVEVSPIGGDDASGGLGWRTRNRLHVDDDGRVGPYAARSHHVVTVESLPLATADSFLAAPLGERLAPGSVVDLVDAAGSEGAAVLVHDPSDKRARRDRTVVSEFVADRTFRVDRTGFWQVHRGAAAALFEAVQAAVDADAADTSAANHDLYGGVGLLAAALADRLGAGVRVTSVESDSRATEHALENLADQVGARAVTARVDRYLRDVVAQADARERARWRAATVVLDPPRSGAGRAVTDALAELRPAQLVYVACDPVALARDVGALTGAGYELERLEGFDLFPHTSHVEAVARLVRRED
>NZ_CP047185.1|WP_104223228.1|2454346_2455042_+|septum-formation-inhibitor-Maf
MLGTGSVPSVEHPTAWARPQGALVRLYLASTSPARLALLRASGIEPVVVPSEVDEPAAVARAEQERGAALDADATVSLLARAKAHAVLRPDIDGLVLGGDSAFVLDGVVHGKPHEPERARERWRAQRGRTGRLHSGHWLVDHRGGRIVAEAGAVTSAAVTFADDIDDAEIDAYVATGEPLEVAGAFTIDGRGAGFITAIEGDPSTVIGMSVPTLRTLVRSLGVDWTALWNR
>NZ_CP047185.1|WP_104223170.1|2455140_2456901_+|ATP-grasp-domain-containing-protein
MPKITKVLVANRGEIAVRVIRAARDSGIASVAVYADQDRDAVHSRLADEAYALGGTTSAETYLVIDKLLSVARRSGADAVHPGYGFLAENADFARAVIDAGLIWIGPGPEAIERLGDKVSARHVAEKVGAPLAPGTLNPVSGAAEVLEFVDQYGLPVAIKAAFGGGGRGLKVARERDEVEELFASATREAVAAFGRGECFVEKYLDQPRHVETQCLADAHGNVVVVSTRDCSLQRRHQKLVEEAPAPFLTDAQNTELYRASKAILQEVGYLGAGTCEFLIGKDGTVSFLEVNTRLQVEHPVSEEITGIDLVREQFRLAEGGVLDYDDPAPRGHSFEFRINGEDAGRGFLPAPGPVHVFKAPGGPGVRVDSGVVAGDVISGSFDSLLAKLIVTGDSREQALERSRRALAEFEVTGLPTVLPFHRAIVEDPAFAPEGGAPFTIYTRWIETEFENTIPAWSGEPGATDEPAARRNVVVEVDGRRVEVTLPGDLVGSGPARGAAAASPKRRGSSSVSTVTGDSVASPMQATIVKVAVAEGDTVVTGDLVVVLEAMKMEQPLTAHKDGVVKGLDATAGATVPAGHVLLQIV
>NZ_CP047185.1|WP_104283337.1|2457322_2458759_-|NAD(P)H-quinone-dehydrogenase
MAYEFERAQRIAVLGGGPGGYEAAIAGAQLGAEVTLVERVGVGGSAVITDVVPSKSLIATAEATNAIGEAADLGVQFFTRSELNKPVRPDVAVNLATVNKRLLGLARQQSEDMRANLVHHGVRIVQGDGRLDGSNALIVSTAAGGEGMDFDRIEADTIVVSVGASPRVLPTAAPDGERILSWTQLYNLKSVPEHLIVVGSGVTGAEFASAYRALGARVTLISSRDQVLPGEDADAAAVIENVFKRNGMVVLSKSRADRVERTEKGVQAVLSDGRVVEGSHCLMAVGSVPNTAGIGLEEAGVQLTESGHIRVNRVARTSVPSIYAAGDCTTFLPLASVAAMQGRTGVFHAMGDAVNPTEVRNVAANIFTQPEIATVGWSQREIEEGIAQGEIYKLPLAANPRAKMMGIRDGFVKLFARTGSGTVIGGVIVAPKASELIFPLALAVEHRLTVDQVARAFTVYPSLTGSISDAARAMHIVT
>NZ_CP047185.1|WP_104238027.1|2458865_2459699_+|purine-nucleoside-phosphorylase
MSDQTLHPLDAPDADPFEIAARAAAQIAEATGVEKHDIALTLGSGWGKAADAIGETTATVEATEILGFSKPAVHGHGGTLRSVLLPTGRRALIIGARTHYYEGYGVRRVAHSVRTAAATGATVMILTNGAGGIKEHWTPGTPVLISDHINLTADSPLEGATFVDLTDLYSSRLRDLARGTRPELDEGVYVQFRGPHYESPAEVQMAKIIGGHIVGMSTALEAIAAREAGMEVLGMSLITNLAAGIQKTPLSHEEVLEAGRDAEDDLARLLAGITGAL
>NZ_CP047185.1|WP_160035030.1|2459695_2461363_+|phospho-sugar-mutase
MSADVRELAEAWLAQDPDPETREELVGLLTASDSGDASARAELEDRFGARLAFGTAGLRGAIAAGSNRMNRVLVSQAAVGLADFLLAQGVQRPVVVIGYDGRKNSRVFAEDSAALMAGAGVDAVLLPRLLPTPVLAFAVRHLGADAGVMVTASHNPPQDNGYKVYLGGADEGSQIVPPVDSEIAERILAVARDRRVPELPRGEYRLADESVVAAYIEATASVGRQSAPLRIVYTAMHGVGWETAHRVLSAAGFDEPAVVVEQIEPDAAFPTVAFPNPEEAGALDLAFSTARSGRAQLIVANDPDADRFAAAVPDASAPEGFRRLTGNEVGALLGWRAAEQARREGRTGGALACSIVSSPALGAVAADYGLDFAETLTGFKWISRVPDLVFGYEEALGYLVNPGTVRDKDGVSAALAFLSLASGLAAEERTIDDELESFAERFGLFGSEQISLRVTDHSEIGRIMAGLRATPPTAIGGLAVERSEDLLAEGGALPPTDALRFSLDGARLIARPSGTEPKVKLYLDAWSHDSDADARRAAVSSRLAALRTGAAELLA

Crispr_ID: NZ_CP047185_5

• CRISPR_ID: NZ_CP047185_5
• CRISPR_location: 3131853-3131984
• CRISPR_type: Orphan
• Repeat_type: NA
• Spacer_info: 1 spacers

Consensus repeat of NZ_CP047185_5

Consensus_repeat	Method
GCGAGGCGTACCGAACTGGCATCTCGCGGAGAGGGGA	CRISPRCasFinder

spacers of NZ_CP047185_5

>5.1|3131890|58|NZ_CP047185|CRISPRCasFinder
CGGGCGGGGCGCGGGCGTGCGCGAGGGCGAGATGCCACTTGGGTACGCGACACGCCGC

CRISPR arrays and Neighbor proteins around NZ_CP047185_5

CRISPR arrays

The CRISPR arrays of NZ_CP047185_5

>merge|NZ_CP047185|5|3131853-3131984|CRISPRCasFinder
GCGAGGCGTACCGAACTGGCATCTCGCGGAGAGGGGACGGGCGGGGCGCGGGCGTGCGCGAGGGCGAGATGCCACTTGGGTACGCGACACGCCGCGCGAGGCGTACCGAACTGGCATCTCGCGGGGAGGGGA

>NZ_CP047185|5|4|3131853-3131984|CRISPRCasFinder
GCGAGGCGTACCGAACTGGCATCTCGCGGAGAGGGGA	CGGGCGGGGCGCGGGCGTGCGCGAGGGCGAGATGCCACTTGGGTACGCGACACGCCGC
GCGAGGCGTACCGAACTGGCATCTCGCGGGGAGGGGA

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP047185.1|WP_160035512.1|3130856_3131804_+|3,4-dioxygenase-subunit-beta	unknown	unknown	gnl|CDD|239540
NZ_CP047185.1|WP_160035506.1|3128158_3129046_+|NAD-binding-protein	unknown	unknown	gnl|CDD|224995
NZ_CP047185.1|WP_104237941.1|3121462_3123298_-|DEAD/DEAH-box-helicase	unknown	unknown	gnl|CDD|236941
NZ_CP047185.1|WP_160035518.1|3134327_3135482_-|hypothetical-protein	unknown	unknown	gnl|CDD|226951
NZ_CP047185.1|WP_160035514.1|3132025_3132430_+|TOBE-domain-containing-protein	unknown	unknown	gnl|CDD|133390
NZ_CP047185.1|WP_104222440.1|3136776_3137190_-|CrcB-family-protein	unknown	unknown	gnl|CDD|376809
NZ_CP047185.1|WP_160035508.1|3129305_3129662_+|hypothetical-protein	unknown	unknown	gnl|CDD|319925
NZ_CP047185.1|WP_160035522.1|3137894_3138980_+|CHAP-domain-containing-protein	unknown	unknown	gnl|CDD|226451
NZ_CP047185.1|WP_160035516.1|3133217_3134231_+|ATP-binding-cassette-domain-containing-protein	unknown	unknown	gnl|CDD|226361
NZ_CP047185.1|WP_160035502.1|3126180_3126987_-|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl|CDD|224332
NZ_CP047185.1|WP_160035510.1|3129907_3130702_+|molybdate-ABC-transporter-substrate-binding-protein	unknown	unknown	gnl|CDD|270256
NZ_CP047185.1|WP_104237929.1|3135478_3136144_-|response-regulator-transcription-factor	unknown	unknown	gnl|CDD|225107
NZ_CP047185.1|WP_160035520.1|3137186_3137711_-|universal-stress-protein	unknown	unknown	gnl|CDD|366180
NZ_CP047185.1|WP_104222446.1|3132429_3133221_+|molybdate-ABC-transporter-permease-subunit	unknown	unknown	gnl|CDD|130643
NZ_CP047185.1|WP_160035504.1|3127010_3128117_-|NAD(P)-binding-domain-containing-protein	unknown	unknown	gnl|CDD|240625
NZ_CP047185.1|WP_160035500.1|3125266_3126034_-|DUF2437-domain-containing-protein	unknown	unknown	gnl|CDD|376566
NZ_CP047185.1|WP_104345752.1|3124462_3125239_-|SDR-family-oxidoreductase	unknown	unknown	gnl|CDD|236040
NZ_CP047185.1|WP_160035498.1|3123390_3124431_-|zinc-binding-dehydrogenase	unknown	unknown	gnl|CDD|176194
NZ_CP047185.1|WP_104226584.1|3136396_3136780_-|CrcB-family-protein	unknown	unknown	gnl|CDD|223317
NZ_CP047185.1|WP_160035524.1|3139040_3139754_-|alpha/beta-fold-hydrolase	unknown	unknown	gnl|CDD|223730

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
NZ_CP047185.1|WP_160035512.1|3130856_3131804_+|3,4-dioxygenase-subunit-beta	gnl|CDD|239540	cd03457, intradiol_dioxygenase_like, Intradiol dioxygenase supgroup. Intradiol dioxygenases catalyze the critical ring-cleavage step in the conversion of catecholate derivatives to citric acid cycle intermediates. They break the catechol C1-C2 bond and utilize Fe3+, as opposed to the extradiol-cleaving enzymes which break the C2-C3 or C1-C6 bond and utilize Fe2+ and Mn+. The family contains catechol 1,2-dioxygenases and protocatechuate 3,4-dioxygenases. The specific function of this subgroup is unknown.	1.77527e-59
NZ_CP047185.1|WP_160035506.1|3128158_3129046_+|NAD-binding-protein	gnl|CDD|224995	COG2084, MmsB, 3-hydroxyisobutyrate dehydrogenase and related beta-hydroxyacid dehydrogenases [Lipid metabolism].	1.14006e-71
NZ_CP047185.1|WP_104237941.1|3121462_3123298_-|DEAD/DEAH-box-helicase	gnl|CDD|236941	PRK11634, PRK11634, ATP-dependent RNA helicase DeaD; Provisional.	0
NZ_CP047185.1|WP_160035518.1|3134327_3135482_-|hypothetical-protein	gnl|CDD|226951	COG4585, COG4585, Signal transduction histidine kinase [Signal transduction mechanisms].	6.31078e-18
NZ_CP047185.1|WP_160035514.1|3132025_3132430_+|TOBE-domain-containing-protein	gnl|CDD|133390	cd04762, HTH_MerR-trunc, Helix-Turn-Helix DNA binding domain of truncated MerR-like proteins. Proteins in this family mostly have a truncated helix-turn-helix (HTH) MerR-like domain. They lack a portion of the C-terminal region, called Wing 2 and the long dimerization helix that is typically present in MerR-like proteins. These truncated domains are found in response regulator receiver (REC) domain proteins (i.e., CheY), cytosine-C5 specific DNA methylases, IS607 transposase-like proteins, and RacA, a bacterial protein that anchors chromosomes to cell poles.	9.75943e-10
NZ_CP047185.1|WP_104222440.1|3136776_3137190_-|CrcB-family-protein	gnl|CDD|376809	pfam02537, CRCB, CrcB-like protein, Camphor Resistance (CrcB). CRCB is a family of bacterial integral membrane proteins with four TMs.. Over expression in E. coli also leads to camphor resistance.	6.60924e-26
NZ_CP047185.1|WP_160035508.1|3129305_3129662_+|hypothetical-protein	gnl|CDD|319925	cd07264, VOC_like, uncharacterized subfamily of vicinal oxygen chelate (VOC) family. The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.	5.7211e-15
NZ_CP047185.1|WP_160035522.1|3137894_3138980_+|CHAP-domain-containing-protein	gnl|CDD|226451	COG3942, COG3942, Surface antigen [General function prediction only].	1.63775e-12
NZ_CP047185.1|WP_160035516.1|3133217_3134231_+|ATP-binding-cassette-domain-containing-protein	gnl|CDD|226361	COG3842, PotA, ABC-type spermidine/putrescine transport systems, ATPase components [Amino acid transport and metabolism].	2.07176e-75
NZ_CP047185.1|WP_160035502.1|3126180_3126987_-|helix-turn-helix-domain-containing-protein	gnl|CDD|224332	COG1414, IclR, Transcriptional regulator [Transcription].	5.42606e-40
NZ_CP047185.1|WP_160035510.1|3129907_3130702_+|molybdate-ABC-transporter-substrate-binding-protein	gnl|CDD|270256	cd13538, PBP2_ModA_like_1, Substrate binding domain of putative molybdate-binding protein;the type 2 periplasmic binding protein fold. This subfamily contains domains found in ModA proteins of putative ABC-type transporter. Molybdate transport system is comprised of a periplasmic binding protein, an integral membrane protein, and an energizer protein. These three proteins are coded by modA, modB, and modC genes, respectively. ModA proteins serve as initial receptors in the ABC transport of molybdate mostly in eubacteria and archaea. After binding molybdate with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ModA proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.	5.34237e-77
NZ_CP047185.1|WP_104237929.1|3135478_3136144_-|response-regulator-transcription-factor	gnl|CDD|225107	COG2197, CitB, Response regulator containing a CheY-like receiver domain and an HTH DNA-binding domain [Signal transduction mechanisms / Transcription].	2.39474e-37
NZ_CP047185.1|WP_160035520.1|3137186_3137711_-|universal-stress-protein	gnl|CDD|366180	pfam00582, Usp, Universal stress protein family. The universal stress protein UspA is a small cytoplasmic bacterial protein whose expression is enhanced when the cell is exposed to stress agents. UspA enhances the rate of cell survival during prolonged exposure to such conditions, and may provide a general "stress endurance" activity. The crystal structure of Haemophilus influenzae UspA reveals an alpha/beta fold similar to that of the Methanococcus jannaschii MJ0577 protein, which binds ATP, though UspA lacks ATP-binding activity.	2.36902e-11
NZ_CP047185.1|WP_104222446.1|3132429_3133221_+|molybdate-ABC-transporter-permease-subunit	gnl|CDD|130643	TIGR01581, Molybdenum_transport_system_permease_protein_modB., NifC-like ABC-type porter. This model describes a clade of ABC porter genes with relatively weak homology compared to its neighbor clades, the molybdate (TIGR02141) and sulfate (TIGR00969) porters. Neighbor-Joining, PAM-distance phylogenetic trees support the separation of the clades in this way. Included in this group is a gene designated NifC in Clostridium pasturianum. It would be reasonable to presume that NifC acts as a molybdate porter since the most common form of nitrogenase is a molybdoenzyme. Several other sequences falling within the scope of this model are annotated as molybdate porters and one, from Halobacterium, is annotated as a sulfate porter. There is presently no experimental evidence to support annotations with this degree of specificity.	2.77401e-69
NZ_CP047185.1|WP_160035504.1|3127010_3128117_-|NAD(P)-binding-domain-containing-protein	gnl|CDD|240625	cd05300, 2-Hacid_dh_1, Putative D-isomer specific 2-hydroxyacid dehydrogenase. 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomains but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric. Formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of formate ion to carbon dioxide with the concomitant reduction of NAD+ to NADH. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of the hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases. FDHs are found in all methylotrophic microorganisms in energy production and in the stress responses of plants.	2.80831e-108
NZ_CP047185.1|WP_160035500.1|3125266_3126034_-|DUF2437-domain-containing-protein	gnl|CDD|376566	pfam01557, FAA_hydrolase, Fumarylacetoacetate (FAA) hydrolase family. This family consists of fumarylacetoacetate (FAA) hydrolase, or fumarylacetoacetate hydrolase (FAH) and it also includes HHDD isomerase/OPET decarboxylase from E. coli strain W. FAA is the last enzyme in the tyrosine catabolic pathway, it hydrolyzes fumarylacetoacetate into fumarate and acetoacetate which then join the citric acid cycle. Mutations in FAA cause type I tyrosinemia in humans this is an inherited disorder mainly affecting the liver leading to liver cirrhosis, hepatocellular carcinoma, renal tubular damages and neurologic crises amongst other symptoms. The enzymatic defect causes the toxic accumulation of phenylalanine/tyrosine catabolites. The E. coli W enzyme HHDD isomerase/OPET decarboxylase contains two copies of this domain and functions in fourth and fifth steps of the homoprotocatechuate pathway; here it decarboxylates OPET to HHDD and isomerises this to OHED. The final products of this pathway are pyruvic acid and succinic semialdehyde. This family also includes various hydratases and 4-oxalocrotonate decarboxylases which are involved in the bacterial meta-cleavage pathways for degradation of aromatic compounds. 2-hydroxypentadienoic acid hydratase encoded by mhpD in E. coli is involved in the phenylpropionic acid pathway of E. coli and catalyzes the conversion of 2-hydroxy pentadienoate to 4-hydroxy-2-keto-pentanoate and uses a Mn2+ co-factor. OHED hydratase encoded by hpcG in E. coli is involved in the homoprotocatechuic acid (HPC) catabolism. XylI in P. putida is a 4-Oxalocrotonate decarboxylase.	3.58743e-45
NZ_CP047185.1|WP_104345752.1|3124462_3125239_-|SDR-family-oxidoreductase	gnl|CDD|236040	PRK07523, PRK07523, gluconate 5-dehydrogenase; Provisional.	2.50388e-115
NZ_CP047185.1|WP_160035498.1|3123390_3124431_-|zinc-binding-dehydrogenase	gnl|CDD|176194	cd08232, idonate-5-DH, L-idonate 5-dehydrogenase. L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of L-lodonate to 5-ketogluconate in the metabolism of L-Idonate to 6-P-gluconate. In E. coli, this GntII pathway is a subsidiary pathway to the canonical GntI system, which also phosphorylates and transports gluconate. L-ido 5-DH is found in an operon with a regulator indR, transporter idnT, 5-keto-D-gluconate 5-reductase, and Gnt kinase. L-ido 5-DH is a zinc-dependent alcohol dehydrogenase-like protein. The alcohol dehydrogenase ADH-like family of proteins is a diverse group of proteins related to the first identified member, class I mammalian ADH. This group is also called the medium chain dehydrogenases/reductase family (MDR) which displays 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 GroES-like catalytic domain. 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. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.	2.48004e-132
NZ_CP047185.1|WP_104226584.1|3136396_3136780_-|CrcB-family-protein	gnl|CDD|223317	COG0239, CrcB, Integral membrane protein possibly involved in chromosome condensation [Cell division and chromosome partitioning].	2.36704e-20
NZ_CP047185.1|WP_160035524.1|3139040_3139754_-|alpha/beta-fold-hydrolase	gnl|CDD|223730	COG0657, Aes, Esterase/lipase [Lipid metabolism].	1.3645e-11

Protein sequences

>NZ_CP047185.1|WP_160035512.1|3130856_3131804_+|3,4-dioxygenase-subunit-beta
MTRIPEPRSTPDGPAYEGRRLDRPEEEVVDQGLPFDVGTLFSRRGVLTLVGAGAATLGLAACATGGSGSASSAAATATATPTAIATAGAGTAVAGEIPDETAGPYPGDGSNGVDVLERSGIVRSDLRTSIGGGATADGVPLALTLTILDAANGGVPFAGAAVYVWHCDAHGDYSMYSSGVEDETYLRGVQVADASGVVSFASIAPACYSGRWPHIHFEVYPGVDSITDASNAIATSQVALQEEACTAVYALDAYAGSAANLARVGLDTDSVFGDDGGALQLATMSGSPASGYSAELTASVDTRTAPTAGAAPRSR
>NZ_CP047185.1|WP_160035510.1|3129907_3130702_+|molybdate-ABC-transporter-substrate-binding-protein
MHRRLLPLVPAAAALLLLAGCSAPSTPAGDAASDGATSSAGGSVTVFAAASLKAAFTELATGFEAAEPGARVELSFAGSSDLATQIVNGAPADVFASADERTMSTVAEAGLVDGNPVDIATNTLEIAVPPGNPAQVASLADLARPGTATVVCAPQVPCGAAAVAVEQAAGVDIFPVSEESSVTDVLGKVSSGEADAGLVYATDVRGAAGSVTGIPFAEASQAVNTYPIAALTGAGDPATAAAFVAYVASDAGRAVLAAAGFGAP
>NZ_CP047185.1|WP_160035508.1|3129305_3129662_+|hypothetical-protein
MASGVATVWVPVTDMERAVAFYRDTLGLEVKDTSDDWSELDAGGLMIGLNARESATVAEQGGAVISFQPDGSIEDELERLTARGASIEGEISDHEWGRILPFKDSEGNDLQFYSPPQS
>NZ_CP047185.1|WP_160035506.1|3128158_3129046_+|NAD-binding-protein
MPDTTTVALPPARTGFVGLGSMGAPMAQRLVAAGVPLGITARPASADRARRAVPEAQWHDSARSLAAASDVLIVMVPDLPQLEEVLEGEEGVLAAGADLVLVVCSSVSASGLRELAGRHPGLRLIDAPVSGGTEGAEAGTLSIMVGGAEEDVARVLPVLSACGTAVRLGPLGAGEVAKACNQLVVAATMTAIAEAAVIAERSGLDLDTLLALLQGGYAGSRVLETKRAALVARDYTPTGVASFMDKDLRAAADEAEATGTSAPLLGTLRTVFRDLVDAGLGDEDLAVVHRFVAER
>NZ_CP047185.1|WP_160035504.1|3127010_3128117_-|NAD(P)-binding-domain-containing-protein
MGAGRFGGEPPAPSREGTPVTDRLRVVIASPLSPELIARIVELEPRLDVVADQSLLPPMRHPGDHGGDPSFQRTPEQQRAFDELVDSADVLYGVPDETPAALARTASANPRLRWVQTMPAGGGAQVRAAGLDDAQLERIAFSTSAGVHSEPLAEFGVFGLLAGAKSLPRLQSLQRERVWGGRWTMGLISEQTVLIVGLGTIGRATARKLQQLGARVIGTSRHETEVEHVDEIVAPDAIAEVAGRIDGVVVTLPGTAATEKLVGSEFFAALRPGASFVSVGRGTVVDEEALLAALDDGRVGFAALDVVAEEPLEQSSPLWSHPSVLISPHTAALNVAEDRLIAELFARNATRFLDGEPLINRVDTVEFY
>NZ_CP047185.1|WP_160035502.1|3126180_3126987_-|helix-turn-helix-domain-containing-protein
MARPDAPPTTVDSDRGSGAPAVSRAMRILDLLADAGGPRTLTDIARELGIAKSSTSNLCVALEEGRLIRRVGSGFLLGRRTVELGSHYLAGFDPVREFYRLCEESPVLSRQLVQIALLDGTRVLYLAVHEGRERFALSASVGDRYPASATAVGTALLAELDDSEIAERFADDRDIVVFTDRSTSSTRELLRKVAAARVRGYAIDDGELHPSVLGVAVAVPAATRSDLSVAVGVSLVRPVADDQEEVVAALREAAAALGRPPLVAGGHA
>NZ_CP047185.1|WP_160035500.1|3125266_3126034_-|DUF2437-domain-containing-protein
MRLARIRADGGPAVVLQVAGEWREIEDAFAAEPIETGRRWPVEGAQLLAPVEPRVILGMAHNGSAVDRLLPPQAFHKTAHTLAGPGDPIVLDEGIGPVVVEGELALVIGRTARHLTPEDALAHVLGATVANDVTAPGMIAADGLFLQGKNGDGWTPLGPWIETGVDVDAVGITVSVDGDVRAVSSTARLGWRAAEILVHLTSHLTLHPGDVVLTGSPGTAVEVEPGQEVLIALDGIGALASRTVPGPPRAAPPQP
>NZ_CP047185.1|WP_104345752.1|3124462_3125239_-|SDR-family-oxidoreductase
MLFDLTDRVALVTGSSRGIGRAVATGLAEAGATVVLNGLDPERLEAARAELAERFPGTDDRPRIHARAFDVTDDAAAEAGVAWIEEAVGPLRILVNNAGVQHRVPLLELEVADWERVLRTNLTSAFVVGRAAAKRMIPRGAGKIVNVASVQADLARPTIAPYTASKGGIRNLTRAMTAEWAQHGIQVNAIAPGYIHTEMTQGLVDDEAFNSWILGRTPAARWGRVEDLIGPAVWLASDGSDYVNGQVVFIDGGMTVVV
>NZ_CP047185.1|WP_160035498.1|3123390_3124431_-|zinc-binding-dehydrogenase
MTALVPASTTRVVVHAAGDLRVEEAPLAPRGPGEALVAVAYGGICGSDLHYWTHGAAGESILREPLTLGHEVVGTVVEAAVDGSGPPVGAAVAVHPATARGEWPDGRPNLATEGTYLGSAARMPHTQGAFARHAVLPARMLRELPAGLGLREAALAEPASVAWHAVSRAGEVSGRRALVIGSGPIGALIVAVLKRAGAAEIVAVDLAEEPLAIARAVGATRTIRATDAVAIAEVAADVVFESSGSPRGLASAVRGAARGGTVVMVGLLPSGEQPALISLAITRELRLIGSFRFVDEIDKVLAALADGSLAVAPVVTQVVPLERALEAFELARDASRSSKVLLDFTP
>NZ_CP047185.1|WP_104237941.1|3121462_3123298_-|DEAD/DEAH-box-helicase
MASTDTPDSAPEADTASESAPTLTFSDLGLSDPVLKALKEVGYETPSAIQAATIPSLLSGRDVLGVAQTGTGKTAAFALPILSRLDVSQKTPQALVLAPTRELALQVCEAFERYASGLRGVHVLPVYGGQGYGTQLSALRRGVHVVVGTPGRIMDHLEKGTLDLSQLKFLVLDEADEMLKMGFAEDVETILADTPVEKQIALFSATMPAQIRRISGKYLKEPEEITVKNKTTTSVNTTQRYLMVSYPQKVDALTRILEVENFEGMIVFVRTKSETETLAEKLRARGYTAAAISGDVAQAQRERTVEQLKSGKLDILVATDVAARGLDVERISHVVNYDIPIDTESYVHRIGRTGRAGRSGAAISFVTPRERRLLAAIEKATRQPLTEMRMPSVEDVNVTRLSRFDDAITAALADTERLQRFRDIIGHYVEHHDVVESDVAAALAIVAQGEEPLLLSPDDPRFARREREDRDSRPDRGDRPERGDRFDRGGDRGERPERRQRPANSNLASYRIEVGRRQRVEPRQIVGALANEGGLNRGDFGHIDIRPDFSIVELPADLPQDVLDRLADTRISGQLIELKPDRRPSRAGADRGARPSGPSRSSERPERKPRY
>NZ_CP047185.1|WP_160035514.1|3132025_3132430_+|TOBE-domain-containing-protein
MPQIRIKDAAAALGVSDDTLRRWIENGTLESARDSSGRRVVDGLEVARLARANAVLPEDPSPVARSARNRFVGIVTGIVMDTVMAQVELQCGPHRVVSLMSSEAVRELGLEPGSPAVAVVKATTVIVETPLARG
>NZ_CP047185.1|WP_104222446.1|3132429_3133221_+|molybdate-ABC-transporter-permease-subunit
MRTGSGLPRWVVAVAALGALLVLLPLAAILARVDWPQFLPLITSDSSVAALLLSLRTSAVATLLCLLLGTPMALVLARTAFPGQRLLRSLVLLPLVLPPVVGGLALLFTFGRMGLLGGALEALGVRIAFSTTAVVIAQTFVALPFLVLTLEGALRSAGARYESVAATLGASPGTVLRRITLPLILPGLASGAILSFARALGEFGATLTFAGSLEGTTRTLPLEIYLQRESDPDAAVALALVLVVVAVLVIGLAHGRSARGVPR
>NZ_CP047185.1|WP_160035516.1|3133217_3134231_+|ATP-binding-cassette-domain-containing-protein
MSLLLEARLAARGIDVRIDVAEGETIALLGPNGAGKSTVLELIAGLVRADSGRATVGGDLLFEDRRWTPPHRRPVALLAQDPLLFPHLSVRENAAFGPRSAGAGRARSLERAERELAAAGVADLADRRPGSLSGGQAQRVALARALATDPRLLLLDEPLAAVDARTAPVLRRMLREVLADRSAIVVTHDVLDAWTLADRVLVLHGGRVVEEGPTARVLTRPRTAFTAELAGLELLEGVRTATGLRTADGHELSGVAAEPVAVGAAVLAAVRPSAVSVGEGGLRAVITDVEQRGDAVRVRSALLTADVPAADAARLDLAPGREAGFTVAPQDLLVYPA
>NZ_CP047185.1|WP_160035518.1|3134327_3135482_-|hypothetical-protein
MSAGPRDAREDNRIVLGAMALLGGVLSLLAALQAVFALGMLSRTLRGVDPGPLLDVTTRVLVNVSTIGLAIALVAVLRPERSTGGGRVARTAVIAVGMGLVRCCLQVLTGVYPLSALPALAVELVVGSTVIALITAYGYLLVRAARRVREKEREHARASVQALEAVQALQREELRVRRDVAQSLHGGLQNGLVVLTAELHAVASTSDEAASERLLAIAARLDRLREDEVRAVGHALYPVEIDHGLVPAVRDLVARLPPEIAVDLDLGRIPALAAEGAEPPLDQRMLLVRFLEEAVTNALKHGGASSLRVRGDEEAGVVVLTLDDDGRGLVEGSTRSGLARLERQLAVYGGSLELSDSPVLAGARLRARLPLPGAAPGGDGGRTE
>NZ_CP047185.1|WP_104237929.1|3135478_3136144_-|response-regulator-transcription-factor
MTSVGGVPELRLAVVDDQPLYRHMLSSLLRAVPGVRSVVEAGSATEARSVLRPAELDVAILDIELGDGDGIELGRRLRSTAPGLGIVLLSAVDAMHRFLRLDRAEARGWSYLSKTSSLSAPALLASVRATADGRTVLDPALVAARAARRDSPVAALSPRQYEVLSGLASGLTNAAIGERLGIAVRSVDNHVNAVYASLGVRSDGERNPRVDATLLFLEHTG
>NZ_CP047185.1|WP_104226584.1|3136396_3136780_-|CrcB-family-protein
MTPGLLLAVALAGGVGAAARLVVDGVARSLVPARWPVGTALINVSGSLLLGVVTGLVLAGVLDPVWRAVLGTGVLGGFTTFSTASVETARLLLDRRWAAGLGYGVGTAALAVAAAAAGLALTGVRLS
>NZ_CP047185.1|WP_104222440.1|3136776_3137190_-|CrcB-family-protein
MTRPLHLRPSAILLVAAGGAVGTAARAAIGAALPPLGVVPVATLAVNLPGAFLLGLLLEALARRGPDEGGRRTLRLLLGTGVLGGFTTYSTFSLDTVALLEGGHVVEYLLYAGGTLVLGVLAAALGIAVAGRRRAAA
>NZ_CP047185.1|WP_160035520.1|3137186_3137711_-|universal-stress-protein
MTAPTPTGPVLVGIVDGQRPEVLRTAARVAADAGAALLLVSVSADPYLVGEYVDPMTGGIPLGFVGAAADRGEGPFLPPGLRETVEHELDGSTVQWSLRAARGEPALALAEVAEEVDARMIVVGTRDAGVLASIAEFLSGSVAAHLAHRQHRPVLVVPRADRDPSRPAPWDLAE
>NZ_CP047185.1|WP_160035522.1|3137894_3138980_+|CHAP-domain-containing-protein
MSKPGIPTPEESAGTPTTASLTRREAREAERRAARAETETGAATAGGAVESSGSDETIASAENGDSAGTAPTAVDAATAVATAPTVSVEVPAVASPASRSIPASPRRASASRPVAPRTAAPVRARGLSRRALAFGTFSVVGGLFATAAIPAYGARSSSATATGRAAANRVGLQNLTVSSDAAGQTAVRDAFAAPTQAQLDEASRQAAVLSGSNGGEFSTVQTRAVGDDYPWPYETIDDDGGGLSPLGYYYRECVDFVAWRLNRDAGRTSAPWKYTWGNITPLGGSAYEWPDNWAAKGWATSSVPIVGCVAWWTYNHVSYVQKVNDDGTVLLEEYNYGGKHSYVTRTFPTAQVPLFLYPPVL
>NZ_CP047185.1|WP_160035524.1|3139040_3139754_-|alpha/beta-fold-hydrolase
MQQTEGREPDEVRRYGKAPEQIADVFRGAPGGARRPVVLVHGGFWRARWDRRHARPLAAALADRGHDVLLPEYRRTGDTGGGWPGTGDDVLAVLAALAALLPGAGPVTLVGHSAGGHLAVWSQAARPSPLVAAVVALAGVLDLAAASADRLSDDAVGELLGGDLALLPGADPAQLPAPPQPTTLIHGVLDEDVPVAYSRRYADRHLAVQLHELADADHMALVDPTTPAFAILLAALG

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity
NZ_CP047185_2	2.4|1880825|26|NZ_CP047185|CRT	1880825-1880850	26	NZ_CP022999	Rhizobium sp. 11515TR strain 10195 plasmid p11515TR-A, complete sequence	217708-217733	2	0.923
NZ_CP047185_2	2.4|1880825|26|NZ_CP047185|CRT	1880825-1880850	26	NZ_CP042998	Aquisphaera giovannonii strain OJF2 plasmid pOJF2_1, complete sequence	45648-45673	3	0.885
NZ_CP047185_2	2.4|1880825|26|NZ_CP047185|CRT	1880825-1880850	26	NZ_CP029831	Azospirillum ramasamyi strain M2T2B2 plasmid unnamed7, complete sequence	654483-654508	4	0.846
NZ_CP047185_2	2.4|1880825|26|NZ_CP047185|CRT	1880825-1880850	26	NZ_CP032054	Streptomyces clavuligerus strain F1D-5 plasmid pSCL1, complete sequence	237301-237326	4	0.846
NZ_CP047185_2	2.4|1880825|26|NZ_CP047185|CRT	1880825-1880850	26	NZ_CP032054	Streptomyces clavuligerus strain F1D-5 plasmid pSCL1, complete sequence	814019-814044	4	0.846
NZ_CP047185_2	2.4|1880825|26|NZ_CP047185|CRT	1880825-1880850	26	NZ_CP027859	Streptomyces clavuligerus strain ATCC 27064 plasmid pCLA1, complete sequence	1212269-1212294	4	0.846
NZ_CP047185_2	2.4|1880825|26|NZ_CP047185|CRT	1880825-1880850	26	NZ_CP016560	Streptomyces clavuligerus strain F613-1 plasmid pSCL4, complete sequence	471255-471280	4	0.846
NZ_CP047185_2	2.4|1880825|26|NZ_CP047185|CRT	1880825-1880850	26	NZ_CP024892	Rhodococcus ruber strain YYL plasmid pYYL1.1, complete sequence	77598-77623	4	0.846
NZ_CP047185_2	2.4|1880825|26|NZ_CP047185|CRT	1880825-1880850	26	NZ_CP043044	Gluconobacter thailandicus strain HD924 plasmid unnamed1, complete sequence	48712-48737	5	0.808
NZ_CP047185_2	2.4|1880825|26|NZ_CP047185|CRT	1880825-1880850	26	NC_016113	Streptomyces cattleya NRRL 8057 = DSM 46488 plasmid pSCAT, complete sequence	1430191-1430216	5	0.808
NZ_CP047185_2	2.4|1880825|26|NZ_CP047185|CRT	1880825-1880850	26	NZ_LR026982	Rhodoplanes piscinae isolate Rhod_plasmid plasmid 1, complete sequence	21346-21371	5	0.808
NZ_CP047185_2	2.4|1880825|26|NZ_CP047185|CRT	1880825-1880850	26	NZ_CP009572	Sphingomonas taxi strain ATCC 55669 plasmid STP1, complete sequence	6224-6249	5	0.808
NZ_CP047185_2	2.4|1880825|26|NZ_CP047185|CRT	1880825-1880850	26	CP054922	Streptomyces sp. NA03103 plasmid unnamed2, complete sequence	84975-85000	5	0.808
NZ_CP047185_2	2.4|1880825|26|NZ_CP047185|CRT	1880825-1880850	26	NC_017585	Streptomyces cattleya NRRL 8057 = DSM 46488 plasmid pSCATT, complete sequence	383072-383097	5	0.808
NZ_CP047185_2	2.4|1880825|26|NZ_CP047185|CRT	1880825-1880850	26	NC_016623	Azospirillum lipoferum 4B plasmid AZO_p3, complete sequence	170670-170695	5	0.808
NZ_CP047185_2	2.4|1880825|26|NZ_CP047185|CRT	1880825-1880850	26	NZ_CP016452	Sinorhizobium sp. RAC02 plasmid pBSY16_1, complete sequence	767510-767535	5	0.808
NZ_CP047185_2	2.4|1880825|26|NZ_CP047185|CRT	1880825-1880850	26	NZ_CP039644	Azospirillum sp. TSA2s plasmid p2, complete sequence	232946-232971	6	0.769
NZ_CP047185_2	2.4|1880825|26|NZ_CP047185|CRT	1880825-1880850	26	NZ_CP054615	Azospirillum oryzae strain KACC 14407 plasmid unnamed1, complete sequence	31289-31314	6	0.769
NZ_CP047185_2	2.4|1880825|26|NZ_CP047185|CRT	1880825-1880850	26	NC_016588	Azospirillum lipoferum 4B plasmid AZO_p6, complete sequence	236216-236241	6	0.769
NZ_CP047185_2	2.3|1880768|38|NZ_CP047185|CRT	1880768-1880805	38	NZ_CP039426	Citricoccus sp. SGAir0253 plasmid unnamed2, complete sequence	46133-46170	10	0.737
NZ_CP047185_2	2.3|1880768|38|NZ_CP047185|CRT	1880768-1880805	38	NZ_CP039431	Citricoccus sp. SGAir0453 plasmid unnamed2, complete sequence	46133-46170	10	0.737
NZ_CP047185_2	2.3|1880768|38|NZ_CP047185|CRT	1880768-1880805	38	AY576796	Actinoplanes phage phiAsp2, complete genome	12419-12456	10	0.737
NZ_CP047185_2	2.3|1880768|38|NZ_CP047185|CRT	1880768-1880805	38	NZ_CP016821	Rhodococcus sp. p52 plasmid pDF01, complete sequence	124900-124937	10	0.737

1. spacer 2.4|1880825|26|NZ_CP047185|CRT matches to NZ_CP022999 (Rhizobium sp. 11515TR strain 10195 plasmid p11515TR-A, complete sequence) position: , mismatch: 2, identity: 0.923

tccgaggtcgaccggctccgg-gcggc	CRISPR spacer
tctgaggtcgaccggctccggtgcgg-	Protospacer
**.****************** **** 

2. spacer 2.4|1880825|26|NZ_CP047185|CRT matches to NZ_CP042998 (Aquisphaera giovannonii strain OJF2 plasmid pOJF2_1, complete sequence) position: , mismatch: 3, identity: 0.885

tccgaggtcgaccggctccgggcggc	CRISPR spacer
gccgaggtcgcccggctccgagcggc	Protospacer
 ********* *********.*****

3. spacer 2.4|1880825|26|NZ_CP047185|CRT matches to NZ_CP029831 (Azospirillum ramasamyi strain M2T2B2 plasmid unnamed7, complete sequence) position: , mismatch: 4, identity: 0.846

tccgaggtcgaccggctccgggcggc	CRISPR spacer
gccgagatcgaccggctccgggtgga	Protospacer
 *****.***************.** 

4. spacer 2.4|1880825|26|NZ_CP047185|CRT matches to NZ_CP032054 (Streptomyces clavuligerus strain F1D-5 plasmid pSCL1, complete sequence) position: , mismatch: 4, identity: 0.846

tccgaggtcgaccggctccgggcggc	CRISPR spacer
gccgaggtcgaccggcaccgggaggg	Protospacer
 *************** ***** ** 

5. spacer 2.4|1880825|26|NZ_CP047185|CRT matches to NZ_CP032054 (Streptomyces clavuligerus strain F1D-5 plasmid pSCL1, complete sequence) position: , mismatch: 4, identity: 0.846

tccgaggtcgaccggctccgggcggc	CRISPR spacer
gccgaggtcgaccggcaccgggaggg	Protospacer
 *************** ***** ** 

6. spacer 2.4|1880825|26|NZ_CP047185|CRT matches to NZ_CP027859 (Streptomyces clavuligerus strain ATCC 27064 plasmid pCLA1, complete sequence) position: , mismatch: 4, identity: 0.846

tccgaggtcgaccggctccgggcggc	CRISPR spacer
gccgaggtcgaccggcaccgggaggg	Protospacer
 *************** ***** ** 

7. spacer 2.4|1880825|26|NZ_CP047185|CRT matches to NZ_CP016560 (Streptomyces clavuligerus strain F613-1 plasmid pSCL4, complete sequence) position: , mismatch: 4, identity: 0.846

tccgaggtcgaccggctccgggcggc	CRISPR spacer
gccgaggtcgaccggcaccgggaggg	Protospacer
 *************** ***** ** 

8. spacer 2.4|1880825|26|NZ_CP047185|CRT matches to NZ_CP024892 (Rhodococcus ruber strain YYL plasmid pYYL1.1, complete sequence) position: , mismatch: 4, identity: 0.846

tccgaggtcgaccggctccgggcggc	CRISPR spacer
aacgtggtcgaccgcctccgggcggc	Protospacer
  ** ********* ***********

9. spacer 2.4|1880825|26|NZ_CP047185|CRT matches to NZ_CP043044 (Gluconobacter thailandicus strain HD924 plasmid unnamed1, complete sequence) position: , mismatch: 5, identity: 0.808

tccgaggtcgaccggctccgggcggc	CRISPR spacer
aaagaggtcgcccggctccgggcgga	Protospacer
   ******* ************** 

10. spacer 2.4|1880825|26|NZ_CP047185|CRT matches to NC_016113 (Streptomyces cattleya NRRL 8057 = DSM 46488 plasmid pSCAT, complete sequence) position: , mismatch: 5, identity: 0.808

tccgaggtcgaccggctccgggcggc	CRISPR spacer
gccgaggccgaccggctgcgggcgta	Protospacer
 ******.********* ******  

11. spacer 2.4|1880825|26|NZ_CP047185|CRT matches to NZ_LR026982 (Rhodoplanes piscinae isolate Rhod_plasmid plasmid 1, complete sequence) position: , mismatch: 5, identity: 0.808

tccgaggtcgaccggctccgggcggc	CRISPR spacer
tccgaactcgaccggctccgggccaa	Protospacer
*****. **************** . 

12. spacer 2.4|1880825|26|NZ_CP047185|CRT matches to NZ_CP009572 (Sphingomonas taxi strain ATCC 55669 plasmid STP1, complete sequence) position: , mismatch: 5, identity: 0.808

tccgaggtcgaccggctccgggcggc	CRISPR spacer
atcgagggcgacgggctccgggcggt	Protospacer
 .***** **** ************.

13. spacer 2.4|1880825|26|NZ_CP047185|CRT matches to CP054922 (Streptomyces sp. NA03103 plasmid unnamed2, complete sequence) position: , mismatch: 5, identity: 0.808

tccgaggtcgaccggctccgggcggc	CRISPR spacer
ggcgaggccgaccggctcctggcgga	Protospacer
  *****.*********** ***** 

14. spacer 2.4|1880825|26|NZ_CP047185|CRT matches to NC_017585 (Streptomyces cattleya NRRL 8057 = DSM 46488 plasmid pSCATT, complete sequence) position: , mismatch: 5, identity: 0.808

tccgaggtcgaccggctccgggcggc	CRISPR spacer
gccgaggccgaccggctgcgggcgta	Protospacer
 ******.********* ******  

15. spacer 2.4|1880825|26|NZ_CP047185|CRT matches to NC_016623 (Azospirillum lipoferum 4B plasmid AZO_p3, complete sequence) position: , mismatch: 5, identity: 0.808

tccgaggtcgaccggctccgggcggc	CRISPR spacer
cccgagatcgaccggctccgggtgaa	Protospacer
.*****.***************.*. 

16. spacer 2.4|1880825|26|NZ_CP047185|CRT matches to NZ_CP016452 (Sinorhizobium sp. RAC02 plasmid pBSY16_1, complete sequence) position: , mismatch: 5, identity: 0.808

tccgaggtcgaccggctccgggcggc	CRISPR spacer
gccgagatcgaccggctgcgggcgaa	Protospacer
 *****.********** ******. 

17. spacer 2.4|1880825|26|NZ_CP047185|CRT matches to NZ_CP039644 (Azospirillum sp. TSA2s plasmid p2, complete sequence) position: , mismatch: 6, identity: 0.769

tccgaggtcgaccggctccgggcggc	CRISPR spacer
gccgaggtcgaccggcgccggggcca	Protospacer
 *************** *****    

18. spacer 2.4|1880825|26|NZ_CP047185|CRT matches to NZ_CP054615 (Azospirillum oryzae strain KACC 14407 plasmid unnamed1, complete sequence) position: , mismatch: 6, identity: 0.769

tccgaggtcgaccggctccgggcggc	CRISPR spacer
gccgaggtcgaccggcgccggggcca	Protospacer
 *************** *****    

19. spacer 2.4|1880825|26|NZ_CP047185|CRT matches to NC_016588 (Azospirillum lipoferum 4B plasmid AZO_p6, complete sequence) position: , mismatch: 6, identity: 0.769

tccgaggtcgaccggctccgggcggc	CRISPR spacer
gccgaggtcgaccggcgccggggcca	Protospacer
 *************** *****    

20. spacer 2.3|1880768|38|NZ_CP047185|CRT matches to NZ_CP039426 (Citricoccus sp. SGAir0253 plasmid unnamed2, complete sequence) position: , mismatch: 10, identity: 0.737

cgcgccgaggccgcccgcctcgcccaggccaacgagct	CRISPR spacer
cgcgccgaggccgcccgcatcgccgaggggttcacccc	Protospacer
****************** ***** ***    *.  *.

21. spacer 2.3|1880768|38|NZ_CP047185|CRT matches to NZ_CP039431 (Citricoccus sp. SGAir0453 plasmid unnamed2, complete sequence) position: , mismatch: 10, identity: 0.737

cgcgccgaggccgcccgcctcgcccaggccaacgagct	CRISPR spacer
cgcgccgaggccgcccgcatcgccgaggggttcacccc	Protospacer
****************** ***** ***    *.  *.

22. spacer 2.3|1880768|38|NZ_CP047185|CRT matches to AY576796 (Actinoplanes phage phiAsp2, complete genome) position: , mismatch: 10, identity: 0.737

cgcgccgaggccgcccgcctcgcccaggccaacgagct	CRISPR spacer
caggaacgggccgcccggctcgcccaggccaccgaggc	Protospacer
*. *   .********* ************* **** .

23. spacer 2.3|1880768|38|NZ_CP047185|CRT matches to NZ_CP016821 (Rhodococcus sp. p52 plasmid pDF01, complete sequence) position: , mismatch: 10, identity: 0.737

cgcgccgaggccgcccgcctcgcccaggccaacgagct-----	CRISPR spacer
cgcgccgaggccgtccgcctcgccaag-----cgtgtccgcac	Protospacer
*************.********** **     ** *..