CRISPRimmunity

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Overview of predicted results

Overview of the results

Contig_ID	Contig_def	CRISPR array number	Contig Signature genes	Self targeting spacer number	Target MGE spacer number	Prophage number	Anti-CRISPR protein number
NZ_CP039546	Methylorubrum populi strain YC-XJ1 chromosome, complete genome	4 crisprs	csa3,DEDDh,WYL,cas3,RT,Cas9_archaeal	0	2	2	0

Results visualization

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CRISPR-Cas detection and classification

Crispr_ID: NZ_CP039546_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP039546_1

842803-842924

Orphan

Consensus_repeat	Method
CCGGGCGGATTCGGCGGCGGCGG	CRISPRCasFinder

2 spacers

The CRISPR arrays of NZ_CP039546_1

>merge|NZ_CP039546|1|842803-842924|CRISPRCasFinder
GGGGGCGGTTTCGACGGTCCCGGCGGTGGGTTCGGCGGTCCCTCGGGCGGATTCGGCCGGCCCGGCGGCGGACCGGGCGGATTCGGCGGCGGCGGTGGACCCGGCGGGTTCGGTGGCGGTCC

>NZ_CP039546|1|1|842803-842924|CRISPRCasFinder
GGGGGCGGTTTCGACGGTCCCGG	CGGTGGGTTCGGCGGTCCC
TCGGGCGGATTCGGCCGGCCCGG	CGGCGGACCGGGCGGATTCGGCGGCGGCGGTGGA
CCCGGCGGGTTCGGTGGCGGTCC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP039546.1\|WP_012452783.1\|849438_849894_+\|(2Fe-2S)-binding-protein	unknown	unknown	gnl\|CDD\|224991
NZ_CP039546.1\|WP_141950440.1\|837205_837772_+\|NUDIX-domain-containing-protein	unknown	unknown	gnl\|CDD\|239516
NZ_CP039546.1\|WP_141950443.1\|840278_840551_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP039546.1\|WP_141950453.1\|849929_852125_+\|molybdopterin-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|224446
NZ_CP039546.1\|WP_141950449.1\|844603_845092_-\|type-II-toxin-antitoxin-system-YhaV-family-toxin	unknown	unknown	gnl\|CDD\|371659
NZ_CP039546.1\|WP_141950447.1\|843650_843863_-\|DUF1289-domain-containing-protein	unknown	unknown	gnl\|CDD\|377738
NZ_CP039546.1\|WP_141950448.1\|843924_844596_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP039546.1\|WP_141950442.1\|838692_839133_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|153095
NZ_CP039546.1\|WP_012452782.1\|847565_849107_-\|HAMP-domain-containing-histidine-kinase	unknown	unknown	gnl\|CDD\|223715
NZ_CP039546.1\|WP_141950438.1\|834683_836183_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP039546.1\|WP_012452771.1\|840090_840282_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP039546.1\|WP_041371052.1\|836918_837176_+\|sulfurtransferase-TusA-family-protein	unknown	unknown	gnl\|CDD\|238180
NZ_CP039546.1\|WP_141950450.1\|845088_845490_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|374238
NZ_CP039546.1\|WP_141950441.1\|838185_838587_+\|DUF3775-domain-containing-protein	unknown	unknown	gnl\|CDD\|378888
NZ_CP039546.1\|WP_141950444.1\|840709_841585_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP039546.1\|WP_141950446.1\|842961_843654_-\|TIGR02281-family-clan-AA-aspartic-protease	unknown	unknown	gnl\|CDD\|226106
NZ_CP039546.1\|WP_141950451.1\|845528_846356_-\|adenosylcobinamide-GDP-ribazoletransferase	unknown	unknown	gnl\|CDD\|234697
NZ_CP039546.1\|WP_141950452.1\|846521_847559_+\|nicotinate-nucleotide--dimethylbenzimidazole-phosphoribosyltransferase	unknown	unknown	gnl\|CDD\|234636
NZ_CP039546.1\|WP_141950439.1\|836392_836815_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|240273
NZ_CP039546.1\|WP_141954701.1\|839281_840031_-\|outer-membrane-beta-barrel-protein	unknown	unknown	gnl\|CDD\|226163

Protein	Function_ID	Function_description	E-value
NZ_CP039546.1\|WP_141950440.1\|837205_837772_+\|NUDIX-domain-containing-protein	gnl\|CDD\|239516	cd03424, ADPRase_NUDT5, ADP-ribose pyrophosphatase (ADPRase) catalyzes the hydrolysis of ADP-ribose and a variety of additional ADP-sugar conjugates to AMP and ribose-5-phosphate. Like other members of the Nudix hydrolase superfamily, it requires a divalent cation, such as Mg2+, for its activity. It also contains a highly conserved 23-residue Nudix motif (GX5EX7REUXEEXGU, where U = I, L or V) which functions as a metal binding site/catalytic site. In addition to the Nudix motif, there are additional conserved amino acid residues, distal from the signature sequence, that correlate with substrate specificity. In humans, there are four distinct ADPRase activities, three putative cytosolic enzymes (ADPRase-I, -II, and -Mn) and a single mitochondrial enzyme (ADPRase-m). Human ADPRase-II is also referred to as NUDT5. It lacks the N-terminal target sequence unique to mitochondrial ADPRase. The different cytosolic types are distinguished by their specificities for substrate and specific requirement for metal ions. NUDT5 forms a homodimer.	6.49232e-40
NZ_CP039546.1\|WP_012452782.1\|847565_849107_-\|HAMP-domain-containing-histidine-kinase	gnl\|CDD\|223715	COG0642, BaeS, Signal transduction histidine kinase [Signal transduction mechanisms].	1.97422e-53
NZ_CP039546.1\|WP_141950453.1\|849929_852125_+\|molybdopterin-dependent-oxidoreductase	gnl\|CDD\|224446	COG1529, CoxL, Aerobic-type carbon monoxide dehydrogenase, large subunit CoxL/CutL homologs [Energy production and conversion].	1.33147e-112
NZ_CP039546.1\|WP_141950449.1\|844603_845092_-\|type-II-toxin-antitoxin-system-YhaV-family-toxin	gnl\|CDD\|371659	pfam11663, Toxin_YhaV, Toxin with endonuclease activity, of toxin-antitoxin system. YhaV causes reversible bacteriostasis and is part of a toxin-antitoxin system in Escherichia coli along with PrlF. The toxicity of YhaV is counteracted by PrlF by the formation of a tight complex which binds to the promoter of the prlF-yhaV operon. In vitro, YhaV also has endonuclease activity.	4.45026e-69
NZ_CP039546.1\|WP_141950447.1\|843650_843863_-\|DUF1289-domain-containing-protein	gnl\|CDD\|377738	pfam06945, DUF1289, Protein of unknown function (DUF1289). This family consists of a number of hypothetical bacterial proteins. The aligned region spans around 56 residues and contains 4 highly conserved cysteine residues towards the N-terminus. The function of this family is unknown. Structural modelling suggests this domain may bind nucleic acids.	7.59338e-17
NZ_CP039546.1\|WP_141950451.1\|845528_846356_-\|adenosylcobinamide-GDP-ribazoletransferase	gnl\|CDD\|234697	PRK00235, cobS, cobalamin synthase; Reviewed.	2.0661e-49
NZ_CP039546.1\|WP_141950442.1\|838692_839133_-\|hypothetical-protein	gnl\|CDD\|153095	cd04706, PLA2_plant, PLA2_plant: Plant-specific sub-family of Phospholipase A2, a super-family of secretory and cytosolic enzymes; the latter are either Ca dependent or Ca independent. Enzymatically active PLA2 cleaves the sn-2 position of the glycerol backbone of phospholipids; secreted PLA2s have also been found to specifically bind to a variety of soluble and membrane proteins in mammals, including receptors. As a toxin, PLA2 is a potent presynaptic neurotoxin which blocks nerve terminals by binding to the nerve membrane and hydrolyzing stable membrane lipids. The products of the hydrolysis cannot form bilayers leading to a change in membrane conformation and ultimately to a block in the release of neurotransmitters. PLA2 may form dimers or oligomers. This sub-family does not appear to have a conserved active site and metal-binding loop.	2.42048e-08
NZ_CP039546.1\|WP_141950441.1\|838185_838587_+\|DUF3775-domain-containing-protein	gnl\|CDD\|378888	pfam12616, DUF3775, Protein of unknown function (DUF3775). This domain family is found in bacteria, and is approximately 80 amino acids in length. There is a single completely conserved residue G that may be functionally important.	1.57876e-20
NZ_CP039546.1\|WP_041371052.1\|836918_837176_+\|sulfurtransferase-TusA-family-protein	gnl\|CDD\|238180	cd00291, SirA_YedF_YeeD, SirA, YedF, and YeeD. Two-layered alpha/beta sandwich domain. SirA (also known as UvrY, and YhhP) belongs to a family of bacterial two-component response regulators that controls secondary metabolism and virulence. The other member of this two-component system is a sensor kinase called BarA which phosphorylates SirA. A variety of microorganisms have similar proteins, all of which contain a common CPxP sequence motif in the N-terminal region. YhhP is suggested to be important for normal cell division and growth in rich nutrient medium. Moreover, despite a low primary sequence similarity, the YccP structure closely resembles the non-homologous C-terminal RNA-binding domain of E. coli translation initiation factor IF3. The signature CPxP motif serves to stabilize the N-terminal helix as part of the N-capping box and might be important in mRNA-binding.	2.48671e-21
NZ_CP039546.1\|WP_141950450.1\|845088_845490_-\|hypothetical-protein	gnl\|CDD\|374238	pfam15937, PrlF_antitoxin, prlF antitoxin for toxin YhaV_toxin. PrlF_antitoxin is a family of bacterial antitoxins that neutralizes the toxin YhaV. PrlF is labile and forms a homodimer that then binds to the YhaV toxin thereby neutralising its ribonuclease activity. Alone, it can also act as a transcription factor. The YhaV/PrlF complex binds the prlF-yhaV operon, probably regulating its expression negatively. Over-expression of PrlF leads to increased doubling time.	1.22664e-12
NZ_CP039546.1\|WP_141950452.1\|846521_847559_+\|nicotinate-nucleotide--dimethylbenzimidazole-phosphoribosyltransferase	gnl\|CDD\|234636	PRK00105, cobT, nicotinate-nucleotide--dimethylbenzimidazole phosphoribosyltransferase; Reviewed.	1.94142e-148
NZ_CP039546.1\|WP_141950446.1\|842961_843654_-\|TIGR02281-family-clan-AA-aspartic-protease	gnl\|CDD\|226106	COG3577, COG3577, Predicted aspartyl protease [General function prediction only].	3.93687e-46
NZ_CP039546.1\|WP_012452783.1\|849438_849894_+\|(2Fe-2S)-binding-protein	gnl\|CDD\|224991	COG2080, CoxS, Aerobic-type carbon monoxide dehydrogenase, small subunit CoxS/CutS homologs [Energy production and conversion].	1.69134e-74
NZ_CP039546.1\|WP_141950439.1\|836392_836815_+\|hypothetical-protein	gnl\|CDD\|240273	PTZ00110, PTZ00110, helicase; Provisional.	0.000144109
NZ_CP039546.1\|WP_141954701.1\|839281_840031_-\|outer-membrane-beta-barrel-protein	gnl\|CDD\|226163	COG3637, COG3637, Opacity protein and related surface antigens [Cell envelope biogenesis, outer membrane].	1.52059e-19

>NZ_CP039546.1|WP_141950444.1|840709_841585_+|hypothetical-protein
MSQPTEPAPSSDGAALHGPVARLLRPLVRLLVQRGITFPALTNLLRELYVNVAEYDFALPGKEQTDSRVSLLTGIHRKEVRRLRGAGAPVSQVPATVSRTSRIIARWVAAPEFTDGQGRPLPLPRSADDAAPSFESLVAGVTKDVRPRAVLDEWLDRGLVVLDPEGRVRLLEAAYLPKGGAEPQLYYFGRNLHDHIAAAAENVTAPSPRFFERAVHYDGLSDGLAGRLEARAREIAMGALKEANAEAHAACAEDAGGRHRWNFGIYIYREEVPARDSGAGPESDAAEGSAP
>NZ_CP039546.1|WP_141950443.1|840278_840551_-|hypothetical-protein
MIELRPALVPGEAPLRLGFRKRARRDMPVAPLLRSAVLAAILAAAVGSPVLRGPAIDLSPGLDPAPLQAGGRAAPHTSGTRVALVREASR
>NZ_CP039546.1|WP_012452771.1|840090_840282_-|hypothetical-protein
MRTATPTAFPTAGLVTSRIRPPHPRRARRSEPAPEPCGGETIIDFALCLILAVAVVGLLMLAL
>NZ_CP039546.1|WP_141954701.1|839281_840031_-|outer-membrane-beta-barrel-protein
MPPTQSGLFPGLCSGFLGCLIAGSACAADLPRRAAPPPPPLPPAFTWTGFYVGANAGYGFRGGSSRYSDATYGTVTESGGKGGFVGGGQIGYNYQMTPGSGWVLGAEADLQATGFGRRGDGTVGSTPYYGVAPSLDWFGTLRGRVGYAFDRWLVYGTGGFAYGGGSRSPYASAYPYTLPDTTRLGYAAGAGIEYALTDRVSVKVEGLYVDLGKQATGTTVYDATVPAYYGTGRSESGFGIVRGGLNYRF
>NZ_CP039546.1|WP_141950442.1|838692_839133_-|hypothetical-protein
MATLAHRAARRLPLAAGLTAVLLGLAPLAASAESVVAPSIEAPAIEAPAAPDLGNGLPQGALVFHGNYCGPGSRGAGLPPVDALDRACMHHDACSPPVGQGLPTCACNDRLAREAGLVARSPRISDEQRSAAEFVAMGAKALACQP
>NZ_CP039546.1|WP_141950441.1|838185_838587_+|DUF3775-domain-containing-protein
MDIALDKVTEIILRLRAVEVKEGATDPDSGSNPTDDGSIDILVGGTDDATEQEIRSMVAGLNEDERADLGALLYIGRGDYEAAEWRTAVDFAKEREAAGDTVMRELLGTPDGASLLEEGLDALGIPMDTPEAP
>NZ_CP039546.1|WP_141950440.1|837205_837772_+|NUDIX-domain-containing-protein
MPPEIRGTRTVHDGWASFVVAEVTTPEGAAVTREIEDHGEAVCVLPYDPERKVALLIRQFRAPPFFTAGVTDLLEVPAGLLDEADPEAGVRREAFEETGLRLSRLEPVSTVWSLPGISTERMHLFLAPYAEADREGPGGGLAEEHEAITVVEMPLATLAAMSEAGEIVDMKTLVLLLSLRLRRPDLFA
>NZ_CP039546.1|WP_041371052.1|836918_837176_+|sulfurtransferase-TusA-family-protein
MSQDGAVELDLSGLKCPLPALRTRKALRALPPGARLAVTATDPLAGIDIPNVVREEGAALEALERRGPAARFLIRRGAGRPAEQA
>NZ_CP039546.1|WP_141950439.1|836392_836815_+|hypothetical-protein
MSRIANLTLAGLAAASLTVTAVPTAQAAPLPAMSAAQVGGTTTVDTVGWRRGYYGGHYGPRYGYGYGYRRHNIGGALAAGAALGLIGGAIAASTAPRYYGYGYGYPAYGGYYGYGRPVGYYGGYGYPAYGGYYGYGPYGW
>NZ_CP039546.1|WP_141950438.1|834683_836183_-|hypothetical-protein
MPALSATAAVPSARRTVDRRAGLGAGLCAVLILGLVLLWWARGGWVFPLDDAYITIHNARVLIEGQDRNYGVPALVGASSLIHLALVTAVSLVLPGEAASYLVAGTGPVLFLAGLLTLGRRLGLPWPEGTALALVGLAFGAAQFLNGLETGLVMAAVTWTLVLALKAPSRRLALACGLLPFLRPELGLLSLMLMTRQARLRLAAGPDRAAALRAVAADAACVLLAAAPWLAWSFAETGALLPRTIAAKQAFFGVPSGSLAESLVYAAMLVAVGLGPAAAALPFLGRDGPAWVFGGFVALFTLGFAVTNWEVLAHNGHRYTLALLPIALFAAMRLGAIYGLRPVRLFILAQAAVALSTLPQITAGQERVAQYATVARWAQANLPQARLLIHDAGVIATASDLPLTDLVGLKSPDSIADHRRWTAPSGGAERFRAVDAIARRSGATHAIILDDAPDRFWGLLVDDLRRAGWRADPLETGSARGPYILYRLTPPPPGAAPAP
>NZ_CP039546.1|WP_141950446.1|842961_843654_-|TIGR02281-family-clan-AA-aspartic-protease
MMWLGLAILGIGLVVLVANHDGGPVMGLDSDQVAGLVSMTALLILLTAGRWRQALAMPGKTVGAILIWLAIGVVIVIGYTYRDDAQRIGANVVGALRPGTAVVGPGGEVTITRRSDGDFAVLAEVNGRAEERFVFDTGASSVVLTAGTAERLGIRPPESAFTQRVSTANGTALTAPIRLDSITVGPITERNVNAMVSRPGVLTTNLLGQSFLDRLPSYEVRGDRLILRSR
>NZ_CP039546.1|WP_141950447.1|843650_843863_-|DUF1289-domain-containing-protein
MTAIPPTKPSSPCTKVCVLDAATGLCEGCGRTREEIGLWGSLSEPQRLALMAVLPERLRRAYPEREEAAR
>NZ_CP039546.1|WP_141950448.1|843924_844596_-|hypothetical-protein
MLSLLRRLLTKRPARTAGEAAPERQPEKIDRADTAERIEILARGGFETEASTLETILDEYLSPDEVDADDRRWIEAEVARAFARKRADEATWPLETDFDRLAVAFDALDAGGIIALHCAGYTRSDGISDAAEVCHQRRERGRSSRGFVFYHGQDVEAVVANRGLYLAFGAFDDRDATMAAIAAEIVAAVEAQGLRTQWEGDVGKRILVHPIVWLKRSPSDDPW
>NZ_CP039546.1|WP_141950449.1|844603_845092_-|type-II-toxin-antitoxin-system-YhaV-family-toxin
MTDASPFAERNGWKLYRARAFRQSVDPLTEDVARLAAADPDGYRAHPRTKLLARIRSLIVEEIPRDPNAPVYALGNTLGPTHRHWRRAKFLQRFRLFFRFDSASRIIVYAWVNDETTLRKAGARSDPYAVFVRRLDDGDPPDDWDELLTDARSTEARGLSDR
>NZ_CP039546.1|WP_141950450.1|845088_845490_-|hypothetical-protein
MIRILIRISREKQIMSQPGFKGSITTTGRSEALRLDKALFKAHPEFRQKAKIRAHILGPGTMLVTLDPDEAASQEASESDPVVAAYLAFLERDMAAHPERLHPFTEIDLARLASLTEGVPVSDDESIPDDVTL
>NZ_CP039546.1|WP_141950451.1|845528_846356_-|adenosylcobinamide-GDP-ribazoletransferase
MSERSGRDLGPPFPGAEWVYDLAACLRFFTRLPIPPLPDEPAPYGAPDFRTVPRMLPVAGLLIALPAALVLVLAWEIRLGPFVAAALALVALALITGAMHEDGLADVADGFGGGQSRERSLEIMRDSRIGAYGGTALFLGLALRAAMLATLLDRSGSLAAVSLLFAAALSRSAALIPLAILAPARPGGAGAAVGRPSRATLGIAGLICLILAGLAAALGLPPFGLVLALILAPLAAFGLSALAERKIGGQTGDVVGACQQVGEIAVLLALVAATA
>NZ_CP039546.1|WP_141950452.1|846521_847559_+|nicotinate-nucleotide--dimethylbenzimidazole-phosphoribosyltransferase
MTASPTADASPFADIRRLLTEMPGPDGDALAAIRARDAQLTKPPGSLGRLEGLVEWLGAWQGKAKPTLDRPMVCVFAGSHGVVERGVSAFPAAVNRQMLDNFAAGGAAINQLCAAYGLGFRVFDLAVDLPTGDICSGPALDEKGCVATMAFGMEAVAAGTDCLAVGEMGIGNTTIAAAIYAALYGGEAEHWVGRGTGLDAAGLARKAEAVRLALQTHKDHLGDPLAVLARLGGREIAAMAGAILAARLQRVPVVLDGYVATAAAAVLHAADPHALDHCIAGHRSAEGAHGEVLERLGLKPVLSLDMRLGEASGAALALGLLKGALACHRDMATFEQAGVSGKSAD
>NZ_CP039546.1|WP_012452782.1|847565_849107_-|HAMP-domain-containing-histidine-kinase
MADLTAEMVQRGRGPSSQEVAKRRGIAREMRSARERLTSTSGLERAFDYELLRLYAQYRVGAGIPLLLLALGVAGASSIWVAPVTVAVWAAGALLATALMLVLSRRFLRQAPESLPLKRWGRLFVAAEFGQSLAWAMLLLVGVPGAQTFALFGLVIVAAVTTMLAATVPVAALSGLAPLTLAALSLLVFSRDMDTMLLVAMTVASQLFFAGLARRLYASAVGTLQSRAEKDAIFAELEQAKANSDEARRRAEEANLAKSRFLATMSHELRTPLNAILGFSEVMKNEVFGAHAAPAYREYATDIHDSGMHLLNLINEILDLSRIEAGRYDLSEEAVQLAHTVEECRHMMTLRARSKGQTFASLIDDSLPRLWADERALRQIVLNLLSNAVKFTPPGGEITIKVGWTSSGGQYVSVKDSGPGIPEDELGTVMSSFGRGSLAIKTAEQGSGLGLPIVKGLIDLHGGGFQLKSKPREGTEVIVTFPASRGMDTLPAMNLGAEKAPAETAPARRARAA
>NZ_CP039546.1|WP_012452783.1|849438_849894_+|(2Fe-2S)-binding-protein
MLTLNLNGVAREVDADPDMPLLWVIRDRLDMTGTKYGCGIAQCGACTVHMDGQPVRSCQTRIGDVGEAKITTIEGVEGKVADAVKAAWRGLDVVQCGYCQSGQIMSAIGLLTENPKPSDADIDGAMDGNVCRCGTYQRIRAAIHEAARSLA
>NZ_CP039546.1|WP_141950453.1|849929_852125_+|molybdopterin-dependent-oxidoreductase
MLKLDLTDAPVPSRRAFLTGAAAGAVLLAFRLDLKGARAAEASDALSKGPAQPNAFVRIAADDTVTVMIKHLDMGQGNTTGLTTILADELDADWSQMRVAFAPADAKLYANLLMGPVQGTGGSTAIANSWFQLRKAGAAARAMLVAAAAETWGVPAGEITVAKGVISHKSGKQARFGEFAEAAAAKPVPQEPRLKTPAEWTLIGGRVPRIDSVAKTDGTAIYSLDIRRPGQVTALVAHPPRFGATVKSVDAEAAQGLPGVVGIVTIPTGVAVIARDTWSAMKAREALKITWDESAAETRSSDAILAEYRETAKTSGLVASQAGDADAGIKGAAKVLEAEFSFPYLAHAAMEPLNATIERTADGSYDVYAGCQIQTIEQAVVAATLGVTTDKVRLHTQWAGGSFGRRATPGADYFAEAAAIVKAWDGKAPVHLVWTREDDMTAGFYRPQVYHTVKAGLNEKGQITGWRHAMVGKSIMIGSPFEAMLVKNGIDSTTVEGASDTPYALPAYRFEVHNAREGVPVLWWRSVGHTHTAHVMEVFIDELAHAAGADPVAYRLSLLTRAPRLSGVLRLAAERAGWGGKSSEKGRGLGVAVHESFGSYVAMVADVTAADSNVRVNRIVAAVDVGVAVNPDVVRAQVEGAVGFALSAVLRNRITLKDGVVQERNFDSYQPTRISEMPRVEVHIVPSEVAPTGIGEPGVPVLAPAIANAVFAATGQRVRSLPLDLSGLRGA

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Crispr_ID: NZ_CP039546_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP039546_2

3324874-3325007

Orphan

Consensus_repeat	Method
CCCTCGGTCCCGCCGCGCTGGATCATCGTCCGCATGCCGGG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP039546_2

>merge|NZ_CP039546|2|3324874-3325007|CRISPRCasFinder
CCCTCGGTCCCGCCGCGCTGGATCATCGTCCGCATGCCGGGCTGCAGCTTGCTGTCGTCCAGATCGTCGGGATGGGCGGGAATGAGGGGCAGCCCCTCGGTCCCGCCCCGCTGGATCATCGTCCGCATGCCGGG

>NZ_CP039546|2|2|3324874-3325007|CRISPRCasFinder
CCCTCGGTCCCGCCGCGCTGGATCATCGTCCGCATGCCGGG	CTGCAGCTTGCTGTCGTCCAGATCGTCGGGATGGGCGGGAATGAGGGGCAGC
CCCTCGGTCCCGCCCCGCTGGATCATCGTCCGCATGCCGGG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP039546.1\|WP_141952175.1\|3334736_3335222_+\|rRNA-maturation-RNase-YbeY	unknown	unknown	gnl\|CDD\|223396
NZ_CP039546.1\|WP_141952168.1\|3330741_3331620_+\|1-acyl-sn-glycerol-3-phosphate-acyltransferase	unknown	unknown	gnl\|CDD\|153251
NZ_CP039546.1\|WP_141952166.1\|3329517_3330198_+\|tRNA-(adenosine(37)-N6)-threonylcarbamoyltransferase-complex-dimerization-subunit-type-1-TsaB	unknown	unknown	gnl\|CDD\|274750
NZ_CP039546.1\|WP_141952157.1\|3316795_3318079_-\|adenylate/guanylate-cyclase-domain-containing-protein	unknown	unknown	gnl\|CDD\|143636
NZ_CP039546.1\|WP_141952171.1\|3332180_3333521_+\|tRNA-(N6-isopentenyl-adenosine(37)-C2)-methylthiotransferase-MiaB	unknown	unknown	gnl\|CDD\|237673
NZ_CP039546.1\|WP_141952151.1\|3312638_3314300_+\|porin	unknown	unknown	gnl\|CDD\|308243
NZ_CP039546.1\|WP_012455262.1\|3328774_3329341_+\|NifU-family-protein	unknown	unknown	gnl\|CDD\|378032
NZ_CP039546.1\|WP_141952153.1\|3314549_3316586_+\|flagellar-motor-protein-MotB	unknown	unknown	gnl\|CDD\|143586
NZ_CP039546.1\|WP_141952173.1\|3333557_3334664_+\|AAA-family-ATPase	unknown	unknown	gnl\|CDD\|224616
NZ_CP039546.1\|WP_141952155.1\|3316582_3316864_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP039546.1\|WP_041371539.1\|3318809_3321134_-\|transglycosylase-SLT-domain-containing-protein	unknown	unknown	gnl\|CDD\|381604
NZ_CP039546.1\|WP_141954911.1\|3318217_3318820_+\|HD-domain-containing-protein	unknown	unknown	gnl\|CDD\|372434
NZ_CP039546.1\|WP_012455264.1\|3330194_3330716_+\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|273701
NZ_CP039546.1\|WP_012455256.1\|3322294_3322768_+\|SsrA-binding-protein-SmpB	unknown	unknown	gnl\|CDD\|235455
NZ_CP039546.1\|WP_012455261.1\|3327724_3328135_-\|DNA-directed-RNA-polymerase-subunit-omega	unknown	unknown	gnl\|CDD\|234744
NZ_CP039546.1\|WP_141952159.1\|3321332_3322223_+\|4-hydroxy-tetrahydrodipicolinate-synthase	unknown	unknown	gnl\|CDD\|235107
NZ_CP039546.1\|WP_141952169.1\|3331624_3332065_-\|MEKHLA-domain-containing-protein	unknown	unknown	gnl\|CDD\|378025
NZ_CP039546.1\|WP_012455260.1\|3325240_3327472_-\|bifunctional-(p)ppGpp-synthetase/guanosine-3',5'-bis(diphosphate)-3'-pyrophosphohydrolase	unknown	unknown	gnl\|CDD\|223394
NZ_CP039546.1\|WP_141952162.1\|3324086_3324677_-\|orotate-phosphoribosyltransferase	unknown	unknown	gnl\|CDD\|273579
NZ_CP039546.1\|WP_141952161.1\|3322916_3323570_-\|NYN-domain-containing-protein	unknown	unknown	gnl\|CDD\|350235

Protein	Function_ID	Function_description	E-value
NZ_CP039546.1\|WP_141952175.1\|3334736_3335222_+\|rRNA-maturation-RNase-YbeY	gnl\|CDD\|223396	COG0319, COG0319, Predicted metal-dependent hydrolase [General function prediction only].	1.34753e-46
NZ_CP039546.1\|WP_141952168.1\|3330741_3331620_+\|1-acyl-sn-glycerol-3-phosphate-acyltransferase	gnl\|CDD\|153251	cd07989, LPLAT_AGPAT-like, Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: AGPAT-like. Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are such LPLATs as 1-acyl-sn-glycerol-3-phosphate acyltransferase (AGPAT, PlsC), Tafazzin (product of Barth syndrome gene), and similar proteins.	5.17417e-32
NZ_CP039546.1\|WP_141952166.1\|3329517_3330198_+\|tRNA-(adenosine(37)-N6)-threonylcarbamoyltransferase-complex-dimerization-subunit-type-1-TsaB	gnl\|CDD\|274750	TIGR03725, T6A_YeaZ, tRNA threonylcarbamoyl adenosine modification protein YeaZ. This family describes a protein family, YeaZ, now associated with the threonylcarbamoyl adenosine (t6A) tRNA modification. Members of this family may occur as fusions with ygjD (previously gcp) or the ribosomal protein N-acetyltransferase rimI, and is frequently encoded next to rimI. [Protein synthesis, tRNA and rRNA base modification].	1.71345e-48
NZ_CP039546.1\|WP_141952157.1\|3316795_3318079_-\|adenylate/guanylate-cyclase-domain-containing-protein	gnl\|CDD\|143636	cd07302, CHD, cyclase homology domain. Catalytic domains of the mononucleotidyl cyclases (MNC's), also called cyclase homology domains (CHDs), are part of the class III nucleotidyl cyclases. This class includes eukaryotic and prokaryotic adenylate cyclases (AC's) and guanylate cyclases (GC's). They seem to share a common catalytic mechanism in their requirement for two magnesium ions to bind the polyphosphate moiety of the nucleotide.	4.99659e-42
NZ_CP039546.1\|WP_141952171.1\|3332180_3333521_+\|tRNA-(N6-isopentenyl-adenosine(37)-C2)-methylthiotransferase-MiaB	gnl\|CDD\|237673	PRK14325, PRK14325, (dimethylallyl)adenosine tRNA methylthiotransferase; Provisional.	0
NZ_CP039546.1\|WP_141952151.1\|3312638_3314300_+\|porin	gnl\|CDD\|308243	pfam02530, Porin_2, Porin subfamily. This family consists of porins from the alpha subdivision of Proteobacteria the members of this family are related to pfam00267. The porins form large aqueous channels in the cell membrane allowing the selective entry of hydrophilic compounds this so called 'molecular sieve' is found in the cell walls of gram negative bacteria.	6.34876e-28
NZ_CP039546.1\|WP_012455262.1\|3328774_3329341_+\|NifU-family-protein	gnl\|CDD\|378032	pfam08712, Nfu_N, Scaffold protein Nfu/NifU N terminal. This domain is found at the N-terminus of NifU and NifU related proteins, and in the human Nfu protein. Both of these proteins are thought to be involved in the the assembly of iron-sulphur clusters.	1.48492e-42
NZ_CP039546.1\|WP_141952153.1\|3314549_3316586_+\|flagellar-motor-protein-MotB	gnl\|CDD\|143586	cd07185, OmpA_C-like, Peptidoglycan binding domains similar to the C-terminal domain of outer-membrane protein OmpA. OmpA-like domains (named after the C-terminal domain of Escherichia coli OmpA protein) have been shown to non-covalently associate with peptidoglycan, a network of glycan chains composed of disaccharides, which are crosslinked via short peptide bridges. Well-studied members of this family include the Escherichia coli outer membrane protein OmpA, the Escherichia coli lipoprotein PAL, Neisseria meningitdis RmpM, which interact with the outer membrane, as well as the Escherichia coli motor protein MotB, and the Vibrio flagellar motor proteins PomB and MotY, which interact with the inner membrane.	2.45542e-06
NZ_CP039546.1\|WP_141952173.1\|3333557_3334664_+\|AAA-family-ATPase	gnl\|CDD\|224616	COG1702, PhoH, Phosphate starvation-inducible protein PhoH, predicted ATPase [Signal transduction mechanisms].	3.00068e-126
NZ_CP039546.1\|WP_041371539.1\|3318809_3321134_-\|transglycosylase-SLT-domain-containing-protein	gnl\|CDD\|381604	cd13401, Slt70-like, 70kDa soluble lytic transglycosylase (Slt70) and similar proteins. Catalytic domain of the 70kda soluble lytic transglycosylase (LT)-like proteins, which also have an N-terminal U-shaped U-domain and a linker L-domain. LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria and the LTs in bacteriophage lambda.	1.11904e-68
NZ_CP039546.1\|WP_141954911.1\|3318217_3318820_+\|HD-domain-containing-protein	gnl\|CDD\|372434	pfam13023, HD_3, HD domain. HD domains are metal dependent phosphohydrolases.	1.77557e-65
NZ_CP039546.1\|WP_012455264.1\|3330194_3330716_+\|GNAT-family-N-acetyltransferase	gnl\|CDD\|273701	TIGR01575, rimI, ribosomal-protein-alanine acetyltransferase. Members of this model belong to the GCN5-related N-acetyltransferase (GNAT) superfamily. This model covers prokarotes and the archaea. The seed contains a characterized accession for Gram negative E. coli. An untraceable characterized accession (PIR\|S66013) for Gram positive B. subtilis scores well (205.0) in the full alignment. Characterized members are lacking in the archaea. Noise cutoff (72.4) was set to exclude M. loti paralog of rimI. Trusted cutoff (80.0) was set at next highest scoring member in the mini-database. [Protein synthesis, Ribosomal proteins: synthesis and modification].	2.69904e-23
NZ_CP039546.1\|WP_012455256.1\|3322294_3322768_+\|SsrA-binding-protein-SmpB	gnl\|CDD\|235455	PRK05422, smpB, SsrA-binding protein SmpB.	3.61421e-86
NZ_CP039546.1\|WP_012455261.1\|3327724_3328135_-\|DNA-directed-RNA-polymerase-subunit-omega	gnl\|CDD\|234744	PRK00392, rpoZ, DNA-directed RNA polymerase subunit omega; Reviewed.	4.93194e-24
NZ_CP039546.1\|WP_141952159.1\|3321332_3322223_+\|4-hydroxy-tetrahydrodipicolinate-synthase	gnl\|CDD\|235107	PRK03170, PRK03170, dihydrodipicolinate synthase; Provisional.	1.46418e-176
NZ_CP039546.1\|WP_141952169.1\|3331624_3332065_-\|MEKHLA-domain-containing-protein	gnl\|CDD\|378025	pfam08670, MEKHLA, MEKHLA domain. The MEKHLA domain shares similarity with the PAS domain and is found in the 3' end of plant HD-ZIP III homeobox genes, and bacterial proteins.	1.98013e-62
NZ_CP039546.1\|WP_012455260.1\|3325240_3327472_-\|bifunctional-(p)ppGpp-synthetase/guanosine-3',5'-bis(diphosphate)-3'-pyrophosphohydrolase	gnl\|CDD\|223394	COG0317, SpoT, Guanosine polyphosphate pyrophosphohydrolases/synthetases [Signal transduction mechanisms / Transcription].	0
NZ_CP039546.1\|WP_141952162.1\|3324086_3324677_-\|orotate-phosphoribosyltransferase	gnl\|CDD\|273579	TIGR01367, Orotate_phosphoribosyltransferase, orotate phosphoribosyltransferase, Thermus family. This model represents a distinct clade of orotate phosphoribosyltransferases. Members include the experimentally determined example from Thermus aquaticus and additional examples from Caulobacter crescentus, Helicobacter pylori, Mesorhizobium loti, and related species. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis].	1.52002e-73
NZ_CP039546.1\|WP_141952161.1\|3322916_3323570_-\|NYN-domain-containing-protein	gnl\|CDD\|350235	cd10911, PIN_LabA, PIN domain of Synechococcus elongatus LabA (low-amplitude and bright) and related proteins. This subfamily contains Synechococcus elongatus PCC 7942 LabA which participates in cyanobacterial circadian timing, it is required for negative feedback regulation of the autokinase/autophosphatase KaiC, a central component of the circadian clock system, and appears to be necessary for KaiC-dependent repression of gene expression. This subfamily belongs to the LabA-like domain family which includes the N-terminal domain of limkain b1, a human autoantigen localized to a subset of ABCD3 and PXF marked peroxisomes. Also included in the LabA-like domain family are human ZNF451, uncharacterized Bacillus subtilis YqxD, uncharacterized Escherichia coli YaiI, and the N-terminal domain of a well-conserved group of mainly bacterial proteins with no defined function, which contain a C-terminal LabA_like_C domain. Curiously Pseudomonas putida S16 NicB , which is described as a putative NADH-dependent hydroxylase involved in the microbial degradation of nicotine also falls into the LabA-like family. The PIN (PilT N terminus) domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its active center, consisting of three highly conserved catalytic residues which coordinate metal ions; in some members, additional metal coordinating residues can be found while some others lack several of these key catalytic residues. The PIN active site is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons.	5.78986e-69

>NZ_CP039546.1|WP_141952162.1|3324086_3324677_-|orotate-phosphoribosyltransferase
MTPEEVLEEFRSAGALLQGHFILSSGLRSPTFLQKMTIFSDPARTERLCRALAEVITARFGRIDIVVSPAIGGIIPGYETARHLGAKAIFVERDPGGPFTLRRGFSIPAGSRAVIVEDIVTTGLSARECLASLKDEAGEVVGAACLIDRSGGRGEIGLPLVSLVTLDIPAYSPDALPPELAAIPPVKPGSRALPKA
>NZ_CP039546.1|WP_141952161.1|3322916_3323570_-|NYN-domain-containing-protein
MSDKQRTAVFIDGANLYATTKALGFDIDYKRLLKDFQSRDNLIRAFYYTAMIEDQEYSSIRPLIDWLDYNGYRVVTKPVKEFTDSAGRRKVKGNMDIELAIDALELAPYIDHMVLFSGDGDFRSLVEAIQRRGVRVSVVSTIQTQPAMIADDLRRQADEFIDLAHLAGRIGRDPSERPARAAGEGPRRDFAERAPRANPGLESRYGIRPPSEDEAEG
>NZ_CP039546.1|WP_012455256.1|3322294_3322768_+|SsrA-binding-protein-SmpB
MAPKTEPGRRVVADNRSARFHYAIEDTFEAGIALTGTEVKSLRGGKATIGESYAGPSGNDLMLFNAYIPEYLEANRFNHDTKRPRRLLLHRRQINKLIGATQRQGYTVIPLKIYFNDKGRAKVELGLGKGKQLHDKRESVKQRDWQRDKARLMRDKG
>NZ_CP039546.1|WP_141952159.1|3321332_3322223_+|4-hydroxy-tetrahydrodipicolinate-synthase
MTDTHARLRGSMTALATPFRDGEFDEAAFRKFVNWQIEQGTHALVPTGTTGESPTLSHSEHDRVVEICVAEAAGRVPVIAGAGSNSTREAVARARHAESVGADAVLTVTPYYNKPTQEGMYAHFKAVNDAVGIPIIIYNIPGRSVVDMSVDTMKRLFELKNIAGVKDATAKIDRVSLQRQALGEDFIQLSGEDATALGFNAQGGVGCISVVSNVAPRLCADLQEATLAGDYAKALKIQDRLMPLHVQMFYESNPVPAKYALSRLGLMSEEVRLPLVPATDGCRRAVDAALAHAGLI
>NZ_CP039546.1|WP_041371539.1|3318809_3321134_-|transglycosylase-SLT-domain-containing-protein
MAFPARSLPLLLGLLLSGTAVLPQPAGAVEVRNPQPASAPAAPVSDAAAPAGQPSDGQGPASDPVAADALRLDPSAGEAASDKPLPAAASSYASTESDGPVAFPLPDAAVSPAAPSPEVPDPARPVASGETHLGPLREAIDLYRKGKVSDGDRLAAGFTDPAARALLEWVAIRAGAGISFERVVAFTRANPDWPAGPLLRRRAEERLLTEKKSPAVVRAYFATARPTSAPGKFALALALRADGLDADAADLVHDLWREESFGRSLEAKVTDAFPGVLTVIDHRYRMERALLKEDWTTAARAADYAGGSYPSLVRARRAVQGKAGAAAALAAVPPSLRNDSSYLLSRAQYFRRADKAAEAAKVLLSAPTNPEVLADGDTWWVERRIVARKLMDAGDTKTAYAVAAAHSARTSEKRIEAEFHAGWIALRFMADPAAAERHFASAASVAETPISLARAAYWQGRAAEAAGRSAEAKSFYERAALQPIAYYGQLARARLGQHSLPLRRAAELSPTARAAFDDRLFVRGLKLLAAAQMKDLALPLYIDAARSLTEEAQVNALGETAVEMRDARALVSIGKLATQRGLALDTHAYPTIGIPDYETFTAVPQVERAMVFAIARQESQFDPRAQSGVGARGLMQMMPATAQRTAKRVSTSYETDRLTSDPAYNARLGQAHLGELMEDWKGSYILAFASYNAGGGNVKKWVDAYGDPRRPEVDPIDWVERIPFTETRNYVQRVMENLQVYRNRLDGKSALMIERDLARGARTAVSAEAQPVTP
>NZ_CP039546.1|WP_141954911.1|3318217_3318820_+|HD-domain-containing-protein
MDHVTDETAALERRFAFLAEIDGLKAVLRQNRTVGERRRENSAEHSWHLAMFALVLGDHAPGLDMSRVVAMLLVHDIVEVDAGDVPIHGAYDAAALALVEQAAATRIFGLLPDAQRDGFLALWKEFEAVETAEARFAKALDRLQPLLLNTLTDGGTWAENGLSEAQVMARYRPVIERGIPGLWPFVEALVRRHYRGGATA
>NZ_CP039546.1|WP_141952157.1|3316795_3318079_-|adenylate/guanylate-cyclase-domain-containing-protein
MAATDPISDTALRRIEARFIARATESDEAETIITEFCEALAAAGLPLWRFSLAVPVIDPVFRGVSVAWRRGQGTAVFPTVHGPEGEDTFFRSPVGWLRANDLSFVRWRLDRSKGCPDLPLLGELRQQGATDYLLHAAAFAPGSAMEGVGISFATDRPGGFTEAEQAILAGLVQVIALVTAKLSLSHTMREMLSTYLGPATGARVLAGEMRRGQSTVVHAAILLADLRGFTTVADRDDPLKVVGWLDEHFDALGEPVQRHGGEISKFLGDGFLAVFPVDEPDALVCTACAGALNAAREALARNAALNAARLGDGLPPLEADIVLHYGRVVSGNVGTDRRLDFTVIGRAVNEASRIERLCDEVERPLLLSDAFARRCGAGLVPVGEFALRGVGRKQRIWGLAQEAELSERPAGGRAPEPAENTAREISP
>NZ_CP039546.1|WP_141952155.1|3316582_3316864_+|hypothetical-protein
MTDLAFSLWPELAAALALGLVVGALTGLPRERFALASAAILLVGLAVLAGLAVLRTVAGGTGLWIETAALVLGAYLAGCVLGGLGRAASGRPL
>NZ_CP039546.1|WP_141952153.1|3314549_3316586_+|flagellar-motor-protein-MotB
MSSPSSSPSSTPTLPPSQPARGRSRLIRVGWLAGLPVLALIGAAAHLGTTRVTERLERQAAEIAAATGEGQPEPWLRVSIKGRDLTAAGEAPEATQREAVIGRLAGIQGLRRLDDRTGVIEEASPFVWSVERPAADRVEANGSRPAEVGAFELAQRLKPALPRDTTLSDRARAARGAPRDFPDAAAFAVERLQDLTTGAVATLNDTVISIRGEAASLAAYDALRTALANPPQGYTLGTVEILPPVVGDFRFSVARRPDGSLELNGHVASEGAREEIRAAAAEAAEGAAVDDRMHEARGLPQGVDGTELARFVFRLAGLLHEGRVDFEGATVSVEGNALDSGAVGEAEALMREGRPAGIAAGRVALTARPIVPYVLRIRRGADSVTVSGHLPDQATREALLARLNPRFFRESIQDRTRLAAGAPAGLAAALAAAVDPLSTLASGELTVTGTDLRLTGISLYPESAARLRRALPQALPSGWSTTVSVSAGEPVTTASEAGPCGQRLAERTAGHPLRFAPGSTALAPEFYPVLDAVAALARACPGERIEVVGHLDPAGAKPETRSDPVTEEAAKETAPKPAKADPKTAKEREGKGRKGKTETRDAAKSEPKLEPKSEPKSESKPEKTEAETAEAGADLARARALAVVDYLQKAGVPLERAAAPTGVAPLSDRQGIGLSLRS
>NZ_CP039546.1|WP_141952151.1|3312638_3314300_+|porin
MKLVKSLLLGSAAGLAVVGGAQAADLPVKKAVPIEYVRVCTAYGAGFFYIPGTDTCLRVSGRARAEYGYIGSDNRDIPGGGDLSGFTGLARFNFDARTQTGYGTLRAFLRLDAASRTGNTKYSSGTNLRGAYAFSGTGQDQLGRVQNFINVDKAFVQFAGLTAGRASSFFDFYAHDFEIIGSSLGSDLPSTNLLAYTQKFGEGWSATLSMEDPNYRKNPIYSDAANATGLVPGQAGLNNVFTTAPTPIILGTNAVGNATAVAFVDAVQRSRMPDFVGSLRYDAPWGSAQFSAAVKDINTGGFIANSSLGVPGTGAVLAGNTAAALAARGINAGAQTEYGWAIQGGMKFNLPFIAPGDGLYLQGAYGEGASFYTGINRFTAGYLSNASVYAGNPFNQYLSDAIVNPLTGRIELSNSFTAVASYLHYWSPEWRSAFYASYGEIWFSQGARQAVSQANALVGAASTVAPPSYLTNAAGYGLSPALRDTYQVVTGASLIWSPVKDLDIGVEGQYIKTGVKNGRVSDSDKGGFVNNIPTRTVSSEDVFQARFRVQRDF
>NZ_CP039546.1|WP_012455260.1|3325240_3327472_-|bifunctional-(p)ppGpp-synthetase/guanosine-3',5'-bis(diphosphate)-3'-pyrophosphohydrolase
MMRQYELVERVKRYNPAANEALLNRAYVYAMRAHGTQKRASGDPFFAHPLEVAAILTDLRLDDATIVAAVLHDTVEDTAATLDEIREIFGPEIGALVDGLTKLKRLDLVSKRAVQGENFRKLLLAVAEDVRVLLVKLADRLHNMRTLHFMRDDKRARIAEETLDIYAPLAGRMGMQELRDELEDLSFRTLKPEIYATITKRLEDLSAKSGSVIESIEHDLTARLAARGITAAVKGRLKKPFSIWSKMERKSVAFEQLSDIVGFRVIVGTVAECYAALGVVHTSWPMVPGRYKDYVSTPKQNDYRSIHTTVIGPKRQRVELQIRTAEMDEIAEYGIAAHAHYKEAGKEGAEGEVHPRLATESGAYQWLRRTIELLAEGDSPEEFLEHTKLELFQDQVFCFTPKGRLIALPRGATPIDFAYAVHTDVGNTAVGAKINGRLAPLLHELANGDEVEIARSDGASPPAAWESLVVTGKARAAIRRATRTAVRRQYAGLGRQILDRAFERAGKSFSEEKLRGALPRLARASTEDVFAAVGRGEMFSGDVVKAVYPDFKEERRPGASGGPAANGAAGRLTRSKDQTMRLTFSGEADGTASSGSIPIRGLAGDLPVSFAPNGGAVPGDRIVGILTPGVGVTIYPIQSAALAAFDNEPERWLDVRWDVEGSQERFPAKLALESINEPGTLAQIAQVIAEHDGNIDNVSMKRRTQDFTDISIDLSVPDLKHLTAIVADLRGKRSVSRVERVNG
>NZ_CP039546.1|WP_012455261.1|3327724_3328135_-|DNA-directed-RNA-polymerase-subunit-omega
MARVTVEDCIEKVENRFELVLLASHRARLLAAGAPLTVERDRDKNPVVALREIGDETITAEDLKEQLIHSMQKYVEVDEPEAETVPLLSSSPAAAAVAPQSSSDDKDVQFDRMSEEDLLRGLENLAPPTETDDEGE
>NZ_CP039546.1|WP_012455262.1|3328774_3329341_+|NifU-family-protein
MFIQTEATPNPATLKFLPGRVVLPEGTFEARDAAGAERSPLATALFSVPGVSGVYFGHDFISVTKADGVNEWPQVKPAVLGAIMDHFQSGRPVLAEGTALAEDETEEFYDEADHDTVATIKDLLETRVRPAVAGDGGDITFRGYRDGIVYLEMKGACSGCPSSTATLRQGVQNLFRHFLPSVREVQAI
>NZ_CP039546.1|WP_141952166.1|3329517_3330198_+|tRNA-(adenosine(37)-N6)-threonylcarbamoyltransferase-complex-dimerization-subunit-type-1-TsaB
MRILAIDTALEACAACVATDDSDDLLAEESMPLVRGHAESLLPLIERVMARVEGGFEGLDRIAVTVGPGSYTGLRVGLSAARAIGLATGIPVVGVTTLSALLAPQLALNGEDMVAAAIDARHGAIYLQAMSVTEGTVIPPRHVGLAEAVGLLGGRRAILTGSGAPALAAAAGAAGLTVEVAETGAPQIAWVASLGLVADPEQALPRPLYLRGPDAQPQDHARLARA
>NZ_CP039546.1|WP_012455264.1|3330194_3330716_+|GNAT-family-N-acetyltransferase
MTRTVSPFWPLDWWSAWWDAWGSVPYVAPLRDAGQAADLEKLHATAFARPWAAHEFERLLCERSTEAHALRRGNALLGFVLSRKAVDEAEILTIVLAPSARGGGHSRRLLSEHLTALTFAGIRTVHLEVDEGNTPALKLYARHGFLKVGERKGYYPLPDGSRATALTMSATLS
>NZ_CP039546.1|WP_141952168.1|3330741_3331620_+|1-acyl-sn-glycerol-3-phosphate-acyltransferase
MTRVGIGLRLFVQALAFLIVIGPHWLSLRFGRGRLAAHIPVLFHRLFLRLFSVRVTQSGSPPPPGEPALVLSNHVSWLDIVALGSLRPLSFVAKSEIEGWPLIGTLAKLQRTVFIERAKRAATASVNATVGERLVSGDLIVLFAEGTTGDGLRLLPFRSSLVGAARAALSAETGGLARIRLQPLALAYPRRNGLPVTRAERPEIAWYGDMDLAPHLALFAKRGPIDVHVNWGAPIAFEPATDRKRATAQAEAAVRQGLREIRLGGPPSRPVPAAPEPLGEGADVSAPGIAAV
>NZ_CP039546.1|WP_141952169.1|3331624_3332065_-|MEKHLA-domain-containing-protein
MSLADDPRFFALLTGSFLRLVGRPLVSAPDLGPDWLYESAPFAVLAHDTSADPLFVYANRAAQRAFGYSWDEFVGMPSRLSAEAPEQAGRQRLLDAVARDGFVSGYASIRVAKDGRRFPIAEGIVWQLIDEDGRVRGQAATFPLPA
>NZ_CP039546.1|WP_141952171.1|3332180_3333521_+|tRNA-(N6-isopentenyl-adenosine(37)-C2)-methylthiotransferase-MiaB
MKKAYVKSYGCQMNAYDAGRMADVLAAEGYSATESVEEADVVVLNTCHIREKAAEKVYSELGRLRVLKGERAESGQDTRIVVAGCVAQAEGREILSRAPAVDVVVGPQSYHRLPDLLRQSRETRVVDTEFPVEDKFDHLPARRNRGVTGFLTVQEGCDKFCAFCVVPYTRGAEVSRSVAAVVEEARRLVEGGVREITLIGQNVNAYHGDGPNGTPATLGHLMDALGAVPGLLRLRYTTSHPNDFADDLIAAHAGNPLVMPYLHLPVQSGSDRILHAMNRRHTGDAYRRLIERIRTARPDIALSSDFIVGFPGESDADFAETMRLVAEIGFAAAFSFKYSPRAGTPAAEREDAVPEAVKTERLAALQQLLDQQRHAFNAAAVGTVAEILVEKTGRHPGQVAGKTPHLQAVQFDAPASTIGTLVPVRITRAGSNSLFGEVLEGAAAAA
>NZ_CP039546.1|WP_141952173.1|3333557_3334664_+|AAA-family-ATPase
MPIDVASARGPAGRNNRPSPGRPGLSETVEVSLTFDDNRLASLVFGQYDQNVAHIERRLGITGTALGNHLVVKGTPEAAEKARRVFERLYARVQKGGTTLTLGDVDGVIQEVTVQGNLFPSAEIVADNGREQFEQIATRKRGGVRARNAAQSDYIKLLRANELVFAEGPAGTGKTWLAVGHAVSLLEQGHAERLILSRPAVEAGERLGFLPGDMREKVDPYLRPIYDALYDFMEARHVDRGLQTGIIEIAPLAFMRGRTLTNAVVLLDEAQNTTSMQMKMFLTRLGENSRMIITGDPSQIDLPPGQKSGLVEAVNVLDGVEGIGRVRFRDVDVVRHDLVRRIVTAYEAASHGEAEADRNPNPRRRPLA
>NZ_CP039546.1|WP_141952175.1|3334736_3335222_+|rRNA-maturation-RNase-YbeY
MSDNEIDIAVEDARWEQAVPDLEAFTLRAVEAGLAILPDSAAGPVEVSVLLADDAAVQTLNRTWRNKDKPTNVLSFPAADGPFQPGMARPLGDVVLAYDTLLRESAEQSKPFEHHFAHLLVHGTLHLLGQDHETGEAEADAMEALEVAALRTLGIPNPYDD

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Crispr_ID: NZ_CP039546_3

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP039546_3

4176290-4176382

Orphan

Consensus_repeat	Method
ACCGTGTCGTAGACCGGCGGCGTC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP039546_3

>merge|NZ_CP039546|3|4176290-4176382|CRISPRCasFinder
ACCGTGTCGTAGACCGGCGGCGTCGTGCGGTAGACGGTGCGCGGCGGCTGGACCAGCACCCGCTCCGCGACGGTGTCGTAGACCGGCGGCGTC

>NZ_CP039546|3|3|4176290-4176382|CRISPRCasFinder
ACCGTGTCGTAGACCGGCGGCGTC	GTGCGGTAGACGGTGCGCGGCGGCTGGACCAGCACCCGCTCCGCG
ACGGTGTCGTAGACCGGCGGCGTC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP039546.1\|WP_012456051.1\|4178727_4179600_+\|RNA-polymerase-factor-sigma-32	unknown	unknown	gnl\|CDD\|236033
NZ_CP039546.1\|WP_141953198.1\|4165723_4166452_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP039546.1\|WP_012456042.1\|4166550_4166766_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP039546.1\|WP_012456045.1\|4168984_4169929_+\|ribose-phosphate-pyrophosphokinase	unknown	unknown	gnl\|CDD\|234929
NZ_CP039546.1\|WP_141953219.1\|4188034_4188976_+\|sce7725-family-protein	unknown	unknown	unknown
NZ_CP039546.1\|WP_141953214.1\|4182655_4183453_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP039546.1\|WP_141953218.1\|4187169_4188027_+\|sce7726-family-protein	unknown	unknown	unknown
NZ_CP039546.1\|WP_141953212.1\|4182360_4182663_+\|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|378935
NZ_CP039546.1\|WP_141953203.1\|4170594_4172022_-\|sensor-histidine-kinase	unknown	unknown	gnl\|CDD\|226951
NZ_CP039546.1\|WP_141953200.1\|4166915_4168460_+\|exodeoxyribonuclease-VII-large-subunit	unknown	unknown	gnl\|CDD\|234714
NZ_CP039546.1\|WP_012456050.1\|4177845_4178442_+\|CarD-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224248
NZ_CP039546.1\|WP_141953210.1\|4176998_4177337_+\|DUF3470-domain-containing-protein	unknown	unknown	gnl\|CDD\|378771
NZ_CP039546.1\|WP_141954987.1\|4179761_4180730_-\|LysR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|176114
NZ_CP039546.1\|WP_141953216.1\|4183647_4186482_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP039546.1\|WP_141953202.1\|4169941_4170598_-\|response-regulator	unknown	unknown	gnl\|CDD\|225107
NZ_CP039546.1\|WP_141953205.1\|4172248_4174048_+\|PQQ-dependent-dehydrogenase,-methanol/ethanol-family	unknown	unknown	gnl\|CDD\|199836
NZ_CP039546.1\|WP_012456046.1\|4174357_4174822_-\|transcription-elongation-factor-GreA	unknown	unknown	gnl\|CDD\|180535
NZ_CP039546.1\|WP_063987092.1\|4168588_4168816_+\|DUF4170-domain-containing-protein	unknown	unknown	gnl\|CDD\|372720
NZ_CP039546.1\|WP_141954989.1\|4186550_4186970_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP039546.1\|WP_141953207.1\|4174836_4175841_-\|acryloyl-CoA-reductase	unknown	unknown	gnl\|CDD\|176248

Protein	Function_ID	Function_description	E-value
NZ_CP039546.1\|WP_012456051.1\|4178727_4179600_+\|RNA-polymerase-factor-sigma-32	gnl\|CDD\|236033	PRK07500, rpoH2, RNA polymerase factor sigma-32; Reviewed.	6.18073e-174
NZ_CP039546.1\|WP_141953212.1\|4182360_4182663_+\|helix-turn-helix-domain-containing-protein	gnl\|CDD\|378935	pfam12728, HTH_17, Helix-turn-helix domain. This domain is a DNA-binding helix-turn-helix domain.	0.00357363
NZ_CP039546.1\|WP_012456045.1\|4168984_4169929_+\|ribose-phosphate-pyrophosphokinase	gnl\|CDD\|234929	PRK01259, PRK01259, ribose-phosphate diphosphokinase.	0
NZ_CP039546.1\|WP_141953203.1\|4170594_4172022_-\|sensor-histidine-kinase	gnl\|CDD\|226951	COG4585, COG4585, Signal transduction histidine kinase [Signal transduction mechanisms].	3.48518e-34
NZ_CP039546.1\|WP_141953200.1\|4166915_4168460_+\|exodeoxyribonuclease-VII-large-subunit	gnl\|CDD\|234714	PRK00286, xseA, exodeoxyribonuclease VII large subunit; Reviewed.	0
NZ_CP039546.1\|WP_012456050.1\|4177845_4178442_+\|CarD-family-transcriptional-regulator	gnl\|CDD\|224248	COG1329, COG1329, Transcriptional regulators, similar to M. xanthus CarD [Transcription].	3.85834e-67
NZ_CP039546.1\|WP_141953210.1\|4176998_4177337_+\|DUF3470-domain-containing-protein	gnl\|CDD\|378771	pfam11953, DUF3470, Domain of unknown function (DUF3470). This presumed domain is functionally uncharacterized. This domain is found in bacteria. This domain is about 50 amino acids in length. This domain is found associated with pfam00037. This domain has a single completely conserved residue N that may be functionally important.	4.61522e-20
NZ_CP039546.1\|WP_141954987.1\|4179761_4180730_-\|LysR-family-transcriptional-regulator	gnl\|CDD\|176114	cd08422, PBP2_CrgA_like, The C-terminal substrate binding domain of LysR-type transcriptional regulator CrgA and its related homologs, contains the type 2 periplasmic binding domain. This CD includes the substrate binding domain of LysR-type transcriptional regulator (LTTR) CrgA and its related homologs. The LTTRs are acting as both auto-repressors and activators of target promoters, controlling operons involved in a wide variety of cellular processes such as amino acid biosynthesis, CO2 fixation, antibiotic resistance, degradation of aromatic compounds, nodule formation of nitrogen-fixing bacteria, and synthesis of virulence factors, to name a few. In contrast to the tetrameric form of other LTTRs, CrgA from Neisseria meningitides assembles into an octameric ring, which can bind up to four 63-bp DNA oligonucleotides. Phylogenetic cluster analysis further showed that the CrgA-like regulators form a subclass of the LTTRs that function as octamers. The CrgA is an auto-repressor of its own gene and activates the expression of the mdaB gene which coding for an NADPH-quinone reductase and that its action is increased by MBL (alpha-methylene-gamma-butyrolactone), an inducer of NADPH-quinone oxidoreductase. The structural topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.	9.18315e-54
NZ_CP039546.1\|WP_141953202.1\|4169941_4170598_-\|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].	1.96588e-55
NZ_CP039546.1\|WP_141953205.1\|4172248_4174048_+\|PQQ-dependent-dehydrogenase,-methanol/ethanol-family	gnl\|CDD\|199836	cd10278, PQQ_MDH, Large subunit of methanol dehydrogenase (moxF). Methanol dehydrogenase is a key enzyme in the utilization of C1 compounds as a source of energy and carbon by bacteria. It catalyzes the oxidation of methanol to formaldehyde, transfering two electrons per methanol to cytochrome c(L) as the acceptor. Methanol dehydrogenase belongs to a family of dehydrogenases with pyrroloquinoline quinone (PQQ) as cofactor, which also includes dehydrogenases specific to other alcohols and membrane-bound glucose dehydrogenases. This alignment model for the large subunit contains an 8-bladed beta-propeller; the functional enzyme forms a heterotetramer composed of two large and two small subunits.	0
NZ_CP039546.1\|WP_012456046.1\|4174357_4174822_-\|transcription-elongation-factor-GreA	gnl\|CDD\|180535	PRK06342, PRK06342, transcription elongation factor GreA.	1.08243e-52
NZ_CP039546.1\|WP_063987092.1\|4168588_4168816_+\|DUF4170-domain-containing-protein	gnl\|CDD\|372720	pfam13773, DUF4170, Domain of unknown function (DUF4170).	3.50061e-43
NZ_CP039546.1\|WP_141953207.1\|4174836_4175841_-\|acryloyl-CoA-reductase	gnl\|CDD\|176248	cd08288, MDR_yhdh, Yhdh putative quinone oxidoreductases. Yhdh putative quinone oxidoreductases (QOR). QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR actin the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.	0

>NZ_CP039546.1|WP_141953207.1|4174836_4175841_-|acryloyl-CoA-reductase
MATFRAWVIEKGETGQSLALRDFDEADLMDGDVTVRVSHSGLNYKDGLAMTGKMPVVRRFPMIPGIDFAGTVEASAHPDYKAGDAVVLTGWGVGETHLGGLAERARVRGDWLVPLPDGLSPAEAMAIGTAGYTAMLSVLALERHGLAPGDGPALVTGASGGVGSVAVALLKRARWHVIAATGRSGEAEYLKGLGAAEILEREALAGEPRPLAKERWAAGIDAVGGKVLANALAMTKSGGAIAACGNAGGMDLPSSVAPFILRGVSLLGINSVTTPQEPRREAWARLARDLDRGGLAAMTRTVSLDEAGGLAKTLLEGQVRGRTVVAIDGTTPQA
>NZ_CP039546.1|WP_012456046.1|4174357_4174822_-|transcription-elongation-factor-GreA
MSRAFVREPEGGEAFEDLPDRPISSHPNYVTPEGLARIEAEVARLEAELSGLSPQQDKADHARLSRDLRYWSARKNSAELVEAFEGDTVRFGATVTVLREDDTRQTFRIVGEDEADPATGSISYVAPLARALTGKGVGDTVTVNDHEFEIAEIR
>NZ_CP039546.1|WP_141953205.1|4172248_4174048_+|PQQ-dependent-dehydrogenase,-methanol/ethanol-family
MKRVSRLALTLAAGLSPAALSPALANEDVAKRIANPAEQVLQTVDYANTRYSKLDQINAGNVKNLQVAWSFSTGVLRGHEGSPLVVGNMMYLHTPFPNLVYALDLDQGGKIVWKYEPKQDPAVIPVMCCDTVYRGLAYADGAIILHQADTTLVSLDAKTGKVNWSVKNGDSKIGETNTATVLPVKDKIIVGISGAEYGIRGHITAYDAKTGKRVWRGYSVGPDDEMLVDPEKTTTLGKPIGKDSSLKTWEGDQWKTGGGATWGWYSYDPKLNLVYYGTANPSTWNPKQRPGDNKWTMAIFARDPDTGQAKWIYQMTPHDEWDYDGINEMILTDQKVDGKERPLLTHFDRNGFAYTLDRATGELLVAEKFDPVVNWASKVDLKTGRPQVVAKYSTDQNGEDVNTKGICPAALGSKDQQPAAFSPKTQLFYVPTNHVCMDYEPFRVTYTPGQPYVGATLSMYPAPGSHGGMGNFIAWDNLQGKIKWSNPEQFSVWSGALATAGDVVFYGTLEGYLKAVDAKSGKELYRFKTASGIIGNVMTYEHKGKQHIAVLSGVGGWAGIGLAAGLTDPNAGLGAVGGYAALSSYTNLGGQLTVFALPN
>NZ_CP039546.1|WP_141953203.1|4170594_4172022_-|sensor-histidine-kinase
MRLLTGLILRVVGVVALCLMAASAWVMWDVNRTIRAEAASSADRVVREARELAWRELTWRGSSSRDAKYAFPDWRSSETLRVIAPGYCVSLAWTDEAPRRLCGGWSGMGAAPPAWFDAAYTALFGPSLPVTRTVTLNRRDAGQVIAVADHGAAARQAWRVVSVVVGVAAAMAAGIGLLATLVIGHALMPAERIVRSLRRMERGAYDLHLPAFRAREFALIARAVNDLTQRLAETTAQRAALTRRLFQVQEEERRALARDLHDEFGQCLTAASALAAAIAVGTDGERPDIAEDARAISGITERMMGTLRSTLARLRPPDLDTVGLERCLTHLVATWNARGAALAAARTAGGAPETIPAFRLDIVGSLSHVPAQAGLSLYRIAQECLTNAARHGRPSEVRLRVEGDDPARGLALSVEDDGGGAPERLEARAGYGLIGIRERVAALGGSLSIERPAGGIGVRVAAIIPFDEPAGARFA
>NZ_CP039546.1|WP_141953202.1|4169941_4170598_-|response-regulator
MSGTTILLVDDHPVVRAGYRKLLERQPGYRVIAEAESAGAAYRDYRRLKPDIVILDLSLPGASGLEAIRRIRAYDRAARILVFSMHQGTPFALKAFEAGACGYVTKSSPPHELVAAMGAVMRGAQAVSEDIAREIAAERLSGRRSPIEDLGPREVEILGLIASGMTTDAIADALSLSPKTVQNYHSSIKAKLRVQTDADLVWLSIAAGLMLRRTGPEA
>NZ_CP039546.1|WP_012456045.1|4168984_4169929_+|ribose-phosphate-pyrophosphokinase
MTSSIKIIAGNASRPLAEAIAGYLELPLANCMVRRFADMEIFVELQENVRGEDVFIVQSTSFPANDHLMELLIMIDAARRSSARRITAVIPYFGYARQDRRTSGRTPISAKLVANLITEAGADRVLTLDLHAGQIQGFFDIPTDNLFAAPVMVRDIKERLAPGERMVVSPDVGGVVRARALAKRIDASLAIVDKRRERAGESEVMNIIGDVEGQSCILVDDIVDSGGTLVNAAEALLNAGAKDVSAYITHGVLSGGAVSRIAASRMKELVITDSILPTQAVKLARNIRVISIAPLLGEAIGRTATESSVSSLFT
>NZ_CP039546.1|WP_063987092.1|4168588_4168816_+|DUF4170-domain-containing-protein
MTTTIDSDQKLHLVFGGELEDVSGVRFRDIKDLDIVGIFPDYASAQTAWRAKAQATVDSAQTRYFIVHLHRLLEP
>NZ_CP039546.1|WP_141953200.1|4166915_4168460_+|exodeoxyribonuclease-VII-large-subunit
MPLVPPPRPATAPAAPPPGEPAPSALLQANAPEWSVGDLAAALKRTLEDAFGHVRLRGEISGYRGPHGSGHAYFSLKDGSAKIDAVVWKGVLGRLRQKPKEGLEVVATGKITTFAGKSSYQIVIDSMEPAGIGAWMALLEERKRLLAAEGLFEAERKRPIPFLPRVVGVVTSPTGAVIRDILHRLEDRFPRPVLVWPVRVQGEGAADEIAAAIRGFNALSPDGPIPRPDVLIVARGGGSIEDLWAFNEEAVVRAAAESGIPLISAVGHETDTTLIDFASDRRAPTPTGAAEMAVPVRVELLAQIHDLGARQAGTMLRRIERERADFRALVRAIPGADAFLAAKRQRLDLADARLRPALAANARDSRERLNRLADRLTRRSPAIALAEARARLAGIDHRPRTAIARIIERRRDRLGAQAGLLGALSYKAVLARGYALVRDADGLPVRSSEAAAAAARLQLQFADGAVFARPEQGPAEIPPPASRPKRAPRRAAPEPARTPTEAVSEPAARQGSLF
>NZ_CP039546.1|WP_012456042.1|4166550_4166766_+|hypothetical-protein
MPICRHSIASSPRPRREAAIVRLSDYVVQRRSAPRAANDNRRSRLAPVWPWAMVAAAAPAVTAALILTRLI
>NZ_CP039546.1|WP_141953198.1|4165723_4166452_+|hypothetical-protein
MTTQGLDTRGSRKARRRLGLEGANTLVQTLAILGAGVWGVYTFVYEARIKPGLAPPSVSVKTDLARVGERGDRVAIRSTVTRTNVGQAGVRVLGLTYTVIGIRTRFSEPGGDDAAREAAFRASLTGTASLDAARDYRRESDGEPILRQGVLFSGATDLPSEPSELNPGESVSRDVIVYADRKSFDAVRFEVRLAYAKEDDRPVRLRFEAGADGGLATVPVEPCPAPKCPLRTTDFATEFSLW
>NZ_CP039546.1|WP_141953210.1|4176998_4177337_+|DUF3470-domain-containing-protein
MTYVVTDNCIKCKYMDCVEVCPVDCFYEGENMLVIHPDECIDCGVCEPECPAEAIKPDTEGNLESWLKLNADYAKTWPNITQKKDAPADAKQWDGVGGKLEAHFSPNPGSGD
>NZ_CP039546.1|WP_012456050.1|4177845_4178442_+|CarD-family-transcriptional-regulator
MTTAKKTTAAGRQGFKTGEAVVYPAHGVGRITAIEEQEIAGYKLELFVVSFEKDKMVLRVPTAKANSVGMRKLAEPELVKKALDVLTGRARIKRTMWSRRAQEYEAKINSGDLISVTEVVRDLYRSEAQPEQSYSERQLYEAALDRVVREISSVNRITETEALKLIEQSLAKSPRRAKADAEAEADAEGDDDVQEEAA
>NZ_CP039546.1|WP_012456051.1|4178727_4179600_+|RNA-polymerase-factor-sigma-32
MAEIAGMRRQFIRTAMEAPFLAREEERGLAVAWKEARDERALHRLISAHMRLVIALAGRFRHYGLPMADLVQEGHVGLMEAAARFEPERDVRFSTYATWWIRASIQDYILRNWSIVRGGTSSAQKALFFNLRRLRARLMQSTEEQVGSEIHGRIASAIGVSREDVALMDARLSGPDMSLNAPVGEESEASSERMDFLVDNAALPDETVSALVDGERRLVWLRQALTVLSERELRILRERRLAEDQATLEALGHRLGISKERVRQIENRALEKLRRALAEKFPQAPASVYA
>NZ_CP039546.1|WP_141954987.1|4179761_4180730_-|LysR-family-transcriptional-regulator
MPHPQLLRDMALFVEVARRKSFSQAAAALGMPISSLSRRITMFESTVGLRLLDRTTRKLALTSYGEAYLAQVSRLVDEAQRTFDDMMAVAKGPSGFLKIAAPPDFWVLRHLSGVITEFSALHEHIHVHVDLKPAPVDLVSDNYDLAVAIEEPRETSLIVRKVAEVENGIFGAPAYLAERGAPMTPFDLEAHQVIVPMQGTSATWTLTRGSETVSTTVGGPLSCNSLSLARRFAVAGQGLTRANVINVDNDLTTGRLQRVLPDWSLPATPVYFVTTSRLLPAKARSFIDFATKRLAAVLANASGDPRRGARAARPVERASLAP
>NZ_CP039546.1|WP_141953212.1|4182360_4182663_+|helix-turn-helix-domain-containing-protein
MKPALEAQAETWADAMPAPENARAMMNWKSYSDDADVLLPVPIFCGRANIGRTTAWRMRRDGELRFVRLTRRKVAIPLSELRRLIAERTEGGQAVEARHG
>NZ_CP039546.1|WP_141953214.1|4182655_4183453_+|hypothetical-protein
MVEHLRAVDLSPVSDAAEVTALFSGDAFRRGHRHITKGDRPGETVYLPSPQFRDRPDIRGRYGPEHGFHLPGDTDVAAISAEEFARYVDAGDLRFHLNVIDRRTSGAATRASVVGARGLAVQTPYHPEIDKGDDDKTPLSLNFIRIVAAKVRAMYFLGFSQRESWVFIPFAATEDFSGDVRRQQLYCDTAHRLAEAVGGKAALDPLLTTLPLPGACPISRKSYRVNRCMPPADIGLIDRPLARGLDDAMEAIARIEAAPLIAFDP
>NZ_CP039546.1|WP_141953216.1|4183647_4186482_+|hypothetical-protein
MTIHQAIHDCANSKVSSNWPANTPAHDAVMLFRAYGQREAGYATVAITVDGPTRTAVRFGLGLDGTLPGFVQRNNDGANLFFRPGECRDGVDPAKAGDADINALNCLWVDIDPRPTETPAECRARVDVLCRELEAVGYGPDIVVSTGGGVQLHWFTRRLTFNSPDSVNRVWASGLLKRLAHALGGDIAATNVSRLLRLPGTMNLPTKSKRTKGRVPAPATLVSARPYDPARRSLETPKAVEAFVAALAAWAAEHGYTPELHKGAVASGAGGHAAGPTRSGEKGAEHPALPEWAARALLRALGQMRNDLDRGTWANFSKAIALCCRETVGDEAVFNALHEFQNREEGRPGTADPEALQRVLAEDEPPAHLGLHEAVHLMRKHGWAEGVSFLAKLDFTGVPINDNDMPGSTERCPRPVLLQDADIAAVLDAFEASVIERCLPLYQRGGPVMAARSRYRDRCGREASASGLHMMTVANLTEFASRHFDVRRPGRKGTEVPAVLAHQIASAYLDRGQWSLPTIGALVQAPALARSGRIVSAQGFDPESGVYLADTLPGFVPPDPAHWQTEADAQWAARQGLDTIATLFSHYRFATAADRSVALAALLTPFAVHAGVRGPLFAFNGTGPGVGKSKLVDAIAVLLTGARAQSMTQGVSAAEFEKHLFGKVLEGAALLNIDNVEQPLEGDTLNAVLTQERLSIRPLGTSRTVTVEHRLTLYATGNNLVVRGDMARRVLTCRIDPGVERPELRTFPFDPAERAAAERAAIVGAALTVLAAHAHCGFPGLERLPSAYGSFEEWSRYVRAALVWLGEADPLDVTVSLREADPVLTRLGAVLSALAAVFGYGAPFGARDILPSPASDDFEAPSGENVLAPRQMLRTALQEALAEERIGRGVADAAAVGRYLGKHEGRVVDGLRLDRARNDAKRGHLYRVSRAIGINLTSAGGSGG
>NZ_CP039546.1|WP_141954989.1|4186550_4186970_+|hypothetical-protein
MKKSPKIPHLPHPSTVSEASHPLLSGGITVEPESTLLTAVREPNGRFRRGAPSPNPSGRAPVAPEVKEAARAHTADMLAVLVEVALDGAAPPAARVAAANAVLDRGHGKPVASLEAKVATVDFNAMHLDALRKMSRPSP
>NZ_CP039546.1|WP_141953218.1|4187169_4188027_+|sce7726-family-protein
MTRLFSSAVFREMASKGRSPLFSRLMELTDIANRCSSNATVGEAFDAAFGVLKTAGHRDEYIYRSALTHNVLMGTHSLNTACMLTEFRAGSCKADLAILNGTATVYEIKSERDSLARLTNQVENYKRVFAKVFVIASESHISGVLDTVPDDVGVMMLGSRYRISTVRDAEDRPERICPATVFDSLRAAEAAAILRSLAIAVPDVPNTKRHTAMRALFNDLDPTAVHVAMVKTLKRTRDLAPLSHLVDRLPRSLHAAALSIKVRRADHARVVEAISTPLDAAMGWI
>NZ_CP039546.1|WP_141953219.1|4188034_4188976_+|sce7725-family-protein
MYHPYFRGKQFELITIREMAPLLAHAGFVPIIEPVRESLGGLERTLRAICEAGGRAIVIVNPHHGDHGDDGANISALLRDKLIGNNKISAGILLRGNTSFEDAKTCFIAHEDHNPTFVHSGFNEPKALAQYLGDNLATSTHVFVSNPADTLYRRHFNSSTRILVQDGFERRKNADYAKNSPEKFSELHVTYGDLGMAGFGDFLIVGDVYSEGGGPAYAVAIHLTYIDPDNDNVMFIYHFVSTTNDTPTDPAGKFKQALDKLVEKLDSGNSKLHETTAIREFRELHAKQHFPGLGYVKKLSMKHHIETLAAYLA

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Crispr_ID: NZ_CP039546_4

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP039546_4

4696248-4696330

Orphan

Consensus_repeat	Method
CCGCCGGGCCCCGCCCCGCCGGC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP039546_4

>merge|NZ_CP039546|4|4696248-4696330|CRISPRCasFinder
CCGCCGGGACCCGCCCCGCCGGCCCCGCCGCGGGCGCGCGTGAAGCCCTCGAAATCGAAGCCGCCGCCGCCGCGCCCGCCGCC

>NZ_CP039546|4|4|4696248-4696330|CRISPRCasFinder
CCGCCGGGACCCGCCCCGCCGGC	CCCGCCGCGGGCGCGCGTGAAGCCCTCGAAATCGAAG
CCGCCGCCGCCGCGCCCGCCGCC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP039546.1\|WP_012456498.1\|4689097_4689493_-\|lactoylglutathione-lyase	unknown	unknown	gnl\|CDD\|319965
NZ_CP039546.1\|WP_141953775.1\|4702188_4703529_-\|dihydroorotase	unknown	unknown	gnl\|CDD\|181632
NZ_CP039546.1\|WP_141955039.1\|4693838_4694522_+\|MOSC-domain-containing-protein	unknown	unknown	gnl\|CDD\|225167
NZ_CP039546.1\|WP_141953771.1\|4700630_4701110_+\|NUDIX-domain-containing-protein	unknown	unknown	gnl\|CDD\|240030
NZ_CP039546.1\|WP_141953763.1\|4696732_4697284_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|339877
NZ_CP039546.1\|WP_141953749.1\|4688707_4689085_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP039546.1\|WP_141953769.1\|4699482_4700634_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP039546.1\|WP_012456509.1\|4698767_4699490_+\|SDR-family-oxidoreductase	unknown	unknown	gnl\|CDD\|212491
NZ_CP039546.1\|WP_141953765.1\|4697370_4698015_+\|pyridoxamine-5'-phosphate-oxidase	unknown	unknown	gnl\|CDD\|235555
NZ_CP039546.1\|WP_141953754.1\|4691777_4692764_+\|polyphosphate-kinase-2-family-protein	unknown	unknown	gnl\|CDD\|274737
NZ_CP039546.1\|WP_141953759.1\|4694577_4695405_-\|enoyl-ACP-reductase-FabI	unknown	unknown	gnl\|CDD\|181260
NZ_CP039546.1\|WP_012456513.1\|4701745_4702000_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP039546.1\|WP_141953758.1\|4693340_4693727_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP039546.1\|WP_141953777.1\|4703663_4704521_+\|folate-binding-protein-YgfZ	unknown	unknown	gnl\|CDD\|223431
NZ_CP039546.1\|WP_141953751.1\|4689605_4690709_+\|tyrosine-type-recombinase/integrase	unknown	unknown	gnl\|CDD\|234698
NZ_CP039546.1\|WP_141955038.1\|4687820_4688540_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP039546.1\|WP_141953756.1\|4692747_4693344_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP039546.1\|WP_141953752.1\|4691021_4691618_-\|histidine-phosphatase-family-protein	unknown	unknown	gnl\|CDD\|366010
NZ_CP039546.1\|WP_141953767.1\|4698030_4698414_-\|response-regulator	unknown	unknown	gnl\|CDD\|381101
NZ_CP039546.1\|WP_141953773.1\|4701106_4701562_+\|TIGR02301-family-protein	unknown	unknown	gnl\|CDD\|370552

Protein	Function_ID	Function_description	E-value
NZ_CP039546.1\|WP_012456498.1\|4689097_4689493_-\|lactoylglutathione-lyase	gnl\|CDD\|319965	cd16358, GlxI_Ni, Glyoxalase I that uses Ni(++) as cofactor. This family includes Escherichia coil and other prokaryotic glyoxalase I that uses nickel as cofactor. Glyoxalase I (also known as lactoylglutathione lyase; EC 4.4.1.5) is part of the glyoxalase system, a two-step system for detoxifying methylglyoxal, a side product of glycolysis. This system is responsible for the conversion of reactive, acyclic alpha-oxoaldehydes into the corresponding alpha-hydroxyacids and involves 2 enzymes, glyoxalase I and II. Glyoxalase I catalyses an intramolecular redox reaction of the hemithioacetal (formed from methylglyoxal and glutathione) to form the thioester, S-D-lactoylglutathione. This reaction involves the transfer of two hydrogen atoms from C1 to C2 of the methylglyoxal, and proceeds via an ene-diol intermediate. Glyoxalase I has a requirement for bound metal ions for catalysis. Eukaryotic glyoxalase I prefers the divalent cation zinc as cofactor, whereas Escherichia coil and other prokaryotic glyoxalase I uses nickel. However, eukaryotic Trypanosomatid parasites also use nickel as a cofactor, which could possibly be explained by acquiring their GLOI gene by horizontal gene transfer. Human glyoxalase I is a two-domain enzyme and it has the structure of a domain-swapped dimer with two active sites located at the dimer interface. In yeast, in various plants, insects and Plasmodia, glyoxalase I is four-domain, possibly the result of a further gene duplication and an additional gene fusing event.	1.86627e-24
NZ_CP039546.1\|WP_141953775.1\|4702188_4703529_-\|dihydroorotase	gnl\|CDD\|181632	PRK09060, PRK09060, dihydroorotase; Validated.	0
NZ_CP039546.1\|WP_141955039.1\|4693838_4694522_+\|MOSC-domain-containing-protein	gnl\|CDD\|225167	COG2258, COG2258, Uncharacterized protein conserved in bacteria [Function unknown].	4.03255e-76
NZ_CP039546.1\|WP_141953771.1\|4700630_4701110_+\|NUDIX-domain-containing-protein	gnl\|CDD\|240030	cd04673, Nudix_Hydrolase_15, Members of the Nudix hydrolase superfamily catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+, for their activity and contain a highly conserved 23-residue nudix motif (GX5EX7REUXEEXGU, where U = I, L or V), which functions as a metal binding and catalytic site. Substrates of nudix hydrolases include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the nudix hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance & "house-cleaning" enzymes. Substrate specificity is used to define families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required.	3.13667e-45
NZ_CP039546.1\|WP_141953763.1\|4696732_4697284_-\|hypothetical-protein	gnl\|CDD\|339877	pfam16998, 17kDa_Anti_2, 17 kDa outer membrane surface antigen. 17kDa_Anti_2 is a surface protein that is found in several Proteobacteria species.	3.37759e-11
NZ_CP039546.1\|WP_012456509.1\|4698767_4699490_+\|SDR-family-oxidoreductase	gnl\|CDD\|212491	cd05233, SDR_c, classical (c) SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.	2.45744e-64
NZ_CP039546.1\|WP_141953765.1\|4697370_4698015_+\|pyridoxamine-5'-phosphate-oxidase	gnl\|CDD\|235555	PRK05679, PRK05679, pyridoxal 5'-phosphate synthase.	7.96921e-105
NZ_CP039546.1\|WP_141953754.1\|4691777_4692764_+\|polyphosphate-kinase-2-family-protein	gnl\|CDD\|274737	TIGR03709, PPK2_rel_1, polyphosphate:nucleotide phosphotransferase, PPK2 family. Members of this protein family belong to the polyphosphate kinase 2 (PPK2) family, which is not related in sequence to PPK1. While PPK1 tends to act in the biosynthesis of polyphosphate, or poly(P), members of the PPK2 family tend to use the terminal phosphate of poly(P) to regenerate ATP or GTP from the corresponding nucleoside diphosphate, or ADP from AMP as is the case with polyphosphate:AMP phosphotransferase (PAP). Members of this protein family most likely transfer the terminal phosphate between poly(P) and some nucleotide, but it is not clear which. [Central intermediary metabolism, Phosphorus compounds].	4.91007e-159
NZ_CP039546.1\|WP_141953759.1\|4694577_4695405_-\|enoyl-ACP-reductase-FabI	gnl\|CDD\|181260	PRK08159, PRK08159, enoyl-[acyl-carrier-protein] reductase FabI.	0
NZ_CP039546.1\|WP_141953773.1\|4701106_4701562_+\|TIGR02301-family-protein	gnl\|CDD\|370552	pfam09539, DUF2385, Protein of unknown function (DUF2385). Members of this uncharacterized protein family are found in a number of alphaproteobacteria, including root nodule bacteria, Brucella suis, Caulobacter crescentus, and Rhodopseudomonas palustris. Conserved residues include two well-separated cysteines, suggesting a disulfide bond. The function is unknown.	1.03578e-36
NZ_CP039546.1\|WP_141953777.1\|4703663_4704521_+\|folate-binding-protein-YgfZ	gnl\|CDD\|223431	COG0354, COG0354, Predicted aminomethyltransferase related to GcvT [General function prediction only].	2.14529e-77
NZ_CP039546.1\|WP_141953751.1\|4689605_4690709_+\|tyrosine-type-recombinase/integrase	gnl\|CDD\|234698	PRK00236, xerC, site-specific tyrosine recombinase XerC; Reviewed.	6.50433e-126
NZ_CP039546.1\|WP_141953752.1\|4691021_4691618_-\|histidine-phosphatase-family-protein	gnl\|CDD\|366010	pfam00300, His_Phos_1, Histidine phosphatase superfamily (branch 1). The histidine phosphatase superfamily is so named because catalysis centers on a conserved His residue that is transiently phosphorylated during the catalytic cycle. Other conserved residues contribute to a 'phosphate pocket' and interact with the phospho group of substrate before, during and after its transfer to the His residue. Structure and sequence analyses show that different families contribute different additional residues to the 'phosphate pocket' and, more surprisingly, differ in the position, in sequence and in three dimensions, of a catalytically essential acidic residue. The superfamily may be divided into two main branches. The larger branch 1 contains a wide variety of catalytic functions, the best known being fructose 2,6-bisphosphatase (found in a bifunctional protein with 2-phosphofructokinase) and cofactor-dependent phosphoglycerate mutase. The latter is an unusual example of a mutase activity in the superfamily: the vast majority of members appear to be phosphatases. The bacterial regulatory protein phosphatase SixA is also in branch 1 and has a minimal, and possible ancestral-like structure, lacking the large domain insertions that contribute to binding of small molecules in branch 1 members.	1.39046e-47
NZ_CP039546.1\|WP_141953767.1\|4698030_4698414_-\|response-regulator	gnl\|CDD\|381101	cd17549, REC_DctD-like, phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and similar proteins. C4-dicarboxylic acid transport protein D (DctD) is part of the two-component regulatory system DctB/DctD, which regulates C4-dicarboxylate transport via regulation of expression of the dctPQM operon and dctA. It is an activator of sigma(54)-RNA polymerase holoenzyme that uses the energy released from ATP hydrolysis to stimulate the isomerization of a closed promoter complex to an open complex capable of initiating transcription. DctD is a member of the NtrC family, characterized by a domain architecture containing an N-terminal REC domain, followed by a central sigma-54 interaction/ATPase domain, and a C-terminal DNA binding domain. The ability of the central domain to hydrolyze ATP and thus to interact effectively with a complex of RNA polymerase, sigma54, and promoter, is controlled by the phosphorylation status of the REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.	4.69478e-15

>NZ_CP039546.1|WP_141953759.1|4694577_4695405_-|enoyl-ACP-reductase-FabI
MSEQKPGGLLAGKRGLVLGVANNRSIAWGIARSAAAHGAELAFTYQGEALKKRVEPLARELNAHVVGHCDVTDPASIDSAFAATAAVFREGIDFVVHCIAFSDKDELTGRYLETSEANFTKSLLISCYSFTAVAQRAEKIMREGGSMLTLTYYGAEKWMPHYNVMGVAKAALEASVRYLAADLGPKQIRVNAISAGPIKTLAASGIGDFRYILKWNEYNAPMRRTVTIEEVGETAAYLFSDMSRGMTGEILHVDAGYHVVGMKNPDAPDITRERD
>NZ_CP039546.1|WP_141955039.1|4693838_4694522_+|MOSC-domain-containing-protein
MRVVIEAVLTGRVAPLGTATSAIAKAPVEGPVAVGPLGLAGDEQADRRVHGGPDKAVHHYALDHAAAWRADLPGLPDLLERPGAFGENFSGFGLTERDVCVGDLWRAGSTLLQVSQARQPCFKLNLRFGVPDMARRVQASGRTGWYYRVIEPGLVTAGATLTLVERRHPDWPLSRLLHHLYVDRLDTAALRAITALAPLAESWRTLAARRLASGAVEGWRRRLGEEG
>NZ_CP039546.1|WP_141953758.1|4693340_4693727_-|hypothetical-protein
MTEGERFVGSVPRKADFHDRNKHRSYELTRQVAARLIDDPGLVANGRSYLERLVRPDPAQAHAYTLWADLLNQDVGQIVRQMLEDSPKGDLLRDTQPVFTVVSPGERIEMVEVAGLQNRSWANPDRRG
>NZ_CP039546.1|WP_141953756.1|4692747_4693344_-|hypothetical-protein
MMRRDRLDHILRAAARVTGHSTFVLVGSSAILVRCRNIPGDMLMTREADIFVPDTPETEALSDAIDANIGQGSVFHSQYGYYADGVSPGTSVMPTDWKDRVAPYHGSGCPGVTAIVPDIDDIALAKVVAWRDKDRSWLTSGIRARLFSLERMAARLGHMPEAAPEATEMVRRLTWLAAACGMPFSASGPPGSGLNPAP
>NZ_CP039546.1|WP_141953754.1|4691777_4692764_+|polyphosphate-kinase-2-family-protein
MARKNGKDGNGARDDKAEETRSQAPWSDHPPSFAGWARAAIAGSGTAPSLSPHLHLIPPPAAPGIVTVGPGQAFSLAAINPDATGGLDKAEAKAALDAQRARIRALQEKLYAEHRRSLLVVFQAIDTGGKDGTIRNVLEGVNPQGCRVWSFKVPSPEELDQDFLWRYHRRTPGRGLIGVFNRSHYEDVLVVRVKGLVPEETWRERYGLINEFERLLTLSGCVILKFFLHISKDEQKERLEARLADPEKHWKFDPADLVERKSWDAYQTAFDDALTRCSTPYAPWHVVPANRKWARNVMVARTIADTLEAMDPRFPEPRKGLEGITVPD
>NZ_CP039546.1|WP_141953752.1|4691021_4691618_-|histidine-phosphatase-family-protein
MSAVPTIWFVRHGETDWNAEGRLQGHRDTDLNARGLAQAAEAAERLRRIAGADLPTADYVASPLTRTRRTMEILRAGIGLPAAGYRADLRLREIGFGAWEGRTWAEIRRRDPSGAAARDRDRWGYQPRGEGAESYAMVEARVEEVVAELRRPTVMVAHGGVARALLVILGHLDIYAAPRLGIRQGSILVIEPAGWRWA
>NZ_CP039546.1|WP_141953751.1|4689605_4690709_+|tyrosine-type-recombinase/integrase
MMRAASPHAVDAEALLPPGDAALRAAMLGWREALARERRMAANTVEAYERDLRQFLAYRAARFGTPTIAGLIALKPRDLRAFMAARRAEGIGGRSLMRMLAGLRSFARFLEREGHGSVAALGAVRSPKVERRLPRPLPVPAALAMTAPGTRPDDSREPWVLARDAAVIALLYGSGLRISEALGLAARDAPVPGIDEVRVTGKGGKVRAVPVLPAVAEAVAAYLSLCPHPLDPEGPLFVGVKGGPLSPRVVQYAVAALRGALGLPESATPHALRHSFATHLLARQGELRAIQELLGHASLSTTQIYTKVDAARLMSAFEDAHPRARRLPEPRREKTSGPPDGTDSEQSPSSRAGYVVRSSVPSERRNA
>NZ_CP039546.1|WP_012456498.1|4689097_4689493_-|lactoylglutathione-lyase
MAKPVHTMIRVRDEARSRDYYARAFGLEPADRFDFPDFTLLYLRDPSSPFELELTVNKDRSEPYNLGDGYGHLAFVVEDAEAEHARFEREGFPVTPVKTLKHGETALATFFFATDPDGYKIEVIQKGGRFA
>NZ_CP039546.1|WP_141953749.1|4688707_4689085_+|hypothetical-protein
MRSAVCRICAFTLAVLTAFAAFPGWAQTPPDAGHARPLVIPQAEGEREGKTLGRALACGAERERVERVLRAGRARMLAAVGRALTEERYVLALDDAMRLETSLPAPSPASCEKALAALERLEKTP
>NZ_CP039546.1|WP_141955038.1|4687820_4688540_-|hypothetical-protein
MATDSGVERAREKARRGRIPLSLKLAYSAFMAVLVPVYLFHYGPTNFLYFCDIALILTLVGLWMESALLVSVCAVGILAPQLLWNVDFLVQATGHPLTGMTAYMFNAQTSPFLRGLSLFHGWLPFLLVYLVWRLGYDRRAWGVWSALAVVVLCVCFFLMPPPRPDPGLTPVNINYVWGMSDHAAQTFMPAWAWFAGLAVGIPLLISWPTHRLLNRLMPEASARSPITSLSASPAGSGPR
>NZ_CP039546.1|WP_141953763.1|4696732_4697284_-|hypothetical-protein
MRLRPCKALGKAVARTLCVREGAATRGPATRHGIAGRVAGLLTLGLAALSCGGCSGPILSFKAEEASAAPEPLVTGSIPKRPASFGRDLDGEDWRRAHAALSVALDPQGNGRPVKWENPETAMRGAINPTGLPYVAGDEICRDFLATVVGGANSRFVRGTGCKPSGGEWELKRLRASNAGAKS
>NZ_CP039546.1|WP_141953765.1|4697370_4698015_+|pyridoxamine-5'-phosphate-oxidase
MAIDRLREGDAGAPPVDPQDFTLSSDPWALFAAWMAEAEASEPCDANAMALATAGPDGLPDVRVVLLKGLDPRGLVFYTNAESAKGQQLMANPQAATVLYWKSLGRQIRARGPVSPVTREEADAYFASRHRDSRIGAIASQQSRPLTDRPTLMAEVAALSERYENGPVPRPEHWLGFRIAPVQLEFWQNGAYRLHDRVRFTRAGDGWTRARLYP
>NZ_CP039546.1|WP_141953767.1|4698030_4698414_-|response-regulator
MSEAEAKSTVLVVEDDAVIRHAAVAMVTDAGFAVREATNGNEAIRILDDGLDAGEAVCVVVTDIDMPLGIDGIKLAACIDRRWPGIGIVITSGKVRPAPGDVPTDGLFIRKPYTEEGLIAAIRSVMP
>NZ_CP039546.1|WP_012456509.1|4698767_4699490_+|SDR-family-oxidoreductase
MLLTGASRGIGHATVKRFSAAGWRVITCSRHPFPENCPWEMGPEDHLQVDLADAQDTVRGVREVAERLAAEGGLLHALVNNAGISPKGPEGERLGALTTEYEDWARVFQVNFFAPILLARGLTDELTRARGSIVNVTSIAGSRVHPFAGAAYGTSKAALAGLTREMAADFGPLGVRVNAISPGEIDTSILSPGTDKLVQQIPQRRLGTPDEVAKAIYFLCTEASSYVNGAELHINGGQHV
>NZ_CP039546.1|WP_141953769.1|4699482_4700634_+|hypothetical-protein
MSDRRAVLAALLSLIALPALAAEDGSGVEPVALPFAVKAMRGPGSDVALSVATSGLLPVARAPASADPKATASTAPPPVVVVWGEGGGAVLSLDGATLRTTLIGAEAIEGFAAAETPRGAVPGSRRALDGPLSAYLTGPTRALGGAPGQGTVLTLRERQPLGVTAEPKAVPVTTHTLAPGDDRVFAGRTPRITRLDGRPAVVAVTAQGAAGSGLALAVKGKDGAWTLAAQTPPQAGQGPGTAPLALAGLADFSGTGTPQIAAIRAPDGEGVLQLWRIADGAPTEGALTLAGEAPGYAGAAAGEEAELAALVPRGGNPPDLALPAAGRGAVAVVALKDGRPVERARIPLPAPAAHGLAVLDAGGTAKKILVGLADGRLVAVSVP
>NZ_CP039546.1|WP_141953771.1|4700630_4701110_+|NUDIX-domain-containing-protein
MNEARQEDGRLFPARPLIGVSIAVIRGGRVLLAARANEPMRGVWTLPGGLVEAGETLAAGALRELQEEVGVRAEVVGPSLTPTEIILRDEAGRIRHHYVIHPHAALWRAVEPAPGPEALAVRWARLDEVEGLQTTPGLIDTLREAFSRVGSVEGSEGSV
>NZ_CP039546.1|WP_141953773.1|4701106_4701562_+|TIGR02301-family-protein
MRTGLVRLTLSALLALTPAAEAFAQQRSSTAKSAPKPSEKDKEPPPPAEPPPAPYDRDLMRLSEIVGALAFLRSLCTEPDAAEWPARMKAILDTEGVTPNRRDRLAGAYNRGFRGYSLTYRICTPAAGEAARRYIAEGERLSHAIAGRFGG
>NZ_CP039546.1|WP_012456513.1|4701745_4702000_+|hypothetical-protein
MIHDSDTAPFDVDAESKRLALGLVTEAFAEGCLDGIDGDCMAQAALFAAFQELVATYGEDATARYAESLPERIRGGGFTTTLQH
>NZ_CP039546.1|WP_141953775.1|4702188_4703529_-|dihydroorotase
MEAPFDLVLSGGTVVNHDGAALADLGIRGGRVAAIGDLAGAAAQERRDCRGLHLLPGVIDSQVHFREPGLDHKEDLETGSRAAVMGGVTAVFEMPNTNPQTTSAAALADKVARAHHRMHCDFAFWVGGTHENAAEVAELERLPGAAGIKVFIGSSTGSLLVEDDAGVRAILSRIRRRAAFHSEDEPMLRERKGLRVPGDPSSHPVWRSPEVAVKATRRLIAIARETGARIHILHISTADEMPILADAKDVASVEVTPHHLTIDGGEAYARLGTLVQMNPPVRDAGHRDGIWRGLNDGVVDVLGSDHAPHTLEEKAKPYPDSPSGMTGVQTLVPIMLDHVNAGRLSLARLVDLTSAGPKRLFGIARKGRLAVGYDADVTVVDLKRRETIRNAWIASKCGWTPYDGVTVTGWPVGTVVRGTPVMWEGELTNPSRGEAVVFEEALPAAG
>NZ_CP039546.1|WP_141953777.1|4703663_4704521_+|folate-binding-protein-YgfZ
MPIALLPDRAVVAVSGPDATAFLQGILTCNVETLPEGEARLGALLTPQGKIQFDFLLSRDGGDGFRLDVGAERVPDLLKRLGLYRLRAKVTVAADPTLGVAAAWDGSETAADTVRVRDGRLPALGERLYFSQGAFSADATEDDYHAHRIGLGVPEGGRDFALSDAFPHEALMDQLGGVDFKKGCYVGQEVVSRMQHRGTARTRILPIVYRDGPAPAPGTEVTAGARSLGTTGSAAGHRGLATIRLDRLGDALAADEPVRAGGTVAAVGKPDFATFAFPTDTAAAG

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Self-targeting detection

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_ID	Protospacer_location	Mismatch	Identity

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity
NZ_CP039546_1	1.2\|842868\|34\|NZ_CP039546\|CRISPRCasFinder	842868-842901	34	NC_016113	Streptomyces cattleya NRRL 8057 = DSM 46488 plasmid pSCAT, complete sequence	217393-217426	6	0.824
NZ_CP039546_1	1.2\|842868\|34\|NZ_CP039546\|CRISPRCasFinder	842868-842901	34	NC_017585	Streptomyces cattleya NRRL 8057 = DSM 46488 plasmid pSCATT, complete sequence	1595722-1595755	6	0.824
NZ_CP039546_1	1.2\|842868\|34\|NZ_CP039546\|CRISPRCasFinder	842868-842901	34	NZ_CP021649	Acidovorax sp. T1 plasmid p1-T1, complete sequence	7786-7819	6	0.824
NZ_CP039546_1	1.2\|842868\|34\|NZ_CP039546\|CRISPRCasFinder	842868-842901	34	NZ_CP012477	Arthrobacter sp. ERGS1:01 isolate water plasmid unnamed2, complete sequence	109704-109737	7	0.794
NZ_CP039546_1	1.2\|842868\|34\|NZ_CP039546\|CRISPRCasFinder	842868-842901	34	NC_015952	Streptomyces violaceusniger Tu 4113 plasmid pSTRVI02, complete sequence	56939-56972	7	0.794
NZ_CP039546_1	1.2\|842868\|34\|NZ_CP039546\|CRISPRCasFinder	842868-842901	34	NC_012852	Rhizobium leguminosarum bv. trifolii WSM1325 plasmid pR132504, complete sequence	114643-114676	7	0.794
NZ_CP039546_1	1.2\|842868\|34\|NZ_CP039546\|CRISPRCasFinder	842868-842901	34	NZ_CP021372	Rhizobium sp. ACO-34A plasmid pRACO34Ad, complete sequence	314591-314624	7	0.794
NZ_CP039546_1	1.2\|842868\|34\|NZ_CP039546\|CRISPRCasFinder	842868-842901	34	NZ_LR134454	Tsukamurella tyrosinosolvens strain NCTC13231 plasmid 12, complete sequence	115219-115252	8	0.765
NZ_CP039546_1	1.2\|842868\|34\|NZ_CP039546\|CRISPRCasFinder	842868-842901	34	NZ_CP027299	Streptomyces sp. SGAir0924 plasmid unnamed_5	96701-96734	8	0.765
NZ_CP039546_1	1.2\|842868\|34\|NZ_CP039546\|CRISPRCasFinder	842868-842901	34	NC_010625	Paraburkholderia phymatum STM815 plasmid pBPHY01, complete sequence	1538925-1538958	8	0.765
NZ_CP039546_1	1.2\|842868\|34\|NZ_CP039546\|CRISPRCasFinder	842868-842901	34	NZ_CP013631	Rhizobium sp. N324 plasmid pRspN324a, complete sequence	222563-222596	9	0.735
NZ_CP039546_1	1.2\|842868\|34\|NZ_CP039546\|CRISPRCasFinder	842868-842901	34	NZ_CP029356	Azospirillum sp. CFH 70021 plasmid unnamed1	754897-754930	9	0.735
NZ_CP039546_1	1.2\|842868\|34\|NZ_CP039546\|CRISPRCasFinder	842868-842901	34	NZ_CP041162	Leisingera aquaemixtae strain R2C4 plasmid unnamed6	25750-25783	9	0.735
NZ_CP039546_1	1.2\|842868\|34\|NZ_CP039546\|CRISPRCasFinder	842868-842901	34	NZ_CP010024	Paraburkholderia fungorum strain ATCC BAA-463 plasmid pBIL, complete sequence	296984-297017	9	0.735
NZ_CP039546_1	1.2\|842868\|34\|NZ_CP039546\|CRISPRCasFinder	842868-842901	34	NC_015724	Cupriavidus necator N-1 plasmid pBB2, complete sequence	262508-262541	9	0.735
NZ_CP039546_1	1.2\|842868\|34\|NZ_CP039546\|CRISPRCasFinder	842868-842901	34	NZ_AP022607	Mycobacterium branderi strain JCM 12687 plasmid pJCM12687	217911-217944	9	0.735
NZ_CP039546_1	1.2\|842868\|34\|NZ_CP039546\|CRISPRCasFinder	842868-842901	34	NZ_CP050100	Rhizobium leguminosarum bv. trifolii strain 9B plasmid pRL9b3, complete sequence	289690-289723	10	0.706
NZ_CP039546_1	1.2\|842868\|34\|NZ_CP039546\|CRISPRCasFinder	842868-842901	34	NZ_CP049733	Rhizobium leguminosarum strain A1 plasmid pRL10, complete sequence	624054-624087	10	0.706
NZ_CP039546_1	1.2\|842868\|34\|NZ_CP039546\|CRISPRCasFinder	842868-842901	34	NZ_CP053443	Rhizobium leguminosarum bv. trifolii strain CC275e plasmid pRltCC275eC, complete sequence	255177-255210	10	0.706
NZ_CP039546_1	1.2\|842868\|34\|NZ_CP039546\|CRISPRCasFinder	842868-842901	34	NZ_CP025506	Rhizobium leguminosarum bv. viciae strain UPM791 plasmid pRlvE, complete sequence	172650-172683	10	0.706
NZ_CP039546_1	1.2\|842868\|34\|NZ_CP039546\|CRISPRCasFinder	842868-842901	34	NZ_CP030763	Rhizobium leguminosarum strain ATCC 14479 plasmid unnamed3, complete sequence	643982-644015	10	0.706
NZ_CP039546_1	1.2\|842868\|34\|NZ_CP039546\|CRISPRCasFinder	842868-842901	34	NZ_CP022668	Rhizobium leguminosarum bv. viciae strain BIHB 1217 plasmid pPR3, complete sequence	60756-60789	10	0.706
NZ_CP039546_1	1.2\|842868\|34\|NZ_CP039546\|CRISPRCasFinder	842868-842901	34	NZ_CP013412	Burkholderia thailandensis strain 2002721643 plasmid p2002721643, complete sequence	66155-66188	10	0.706
NZ_CP039546_1	1.2\|842868\|34\|NZ_CP039546\|CRISPRCasFinder	842868-842901	34	NZ_CP010016	Burkholderia thailandensis 34 plasmid unnamed, complete sequence	283665-283698	10	0.706
NZ_CP039546_1	1.2\|842868\|34\|NZ_CP039546\|CRISPRCasFinder	842868-842901	34	NZ_CP053207	Rhizobium leguminosarum bv. trifolii TA1 plasmid pRltTA1C, complete sequence	654560-654593	10	0.706
NZ_CP039546_1	1.2\|842868\|34\|NZ_CP039546\|CRISPRCasFinder	842868-842901	34	NZ_CP050088	Rhizobium leguminosarum bv. trifolii strain 23B plasmid pRL23b6, complete sequence	305197-305230	10	0.706
NZ_CP039546_1	1.2\|842868\|34\|NZ_CP039546\|CRISPRCasFinder	842868-842901	34	MG962370	Mycobacterium phage Kykar, complete genome	16189-16222	10	0.706
NZ_CP039546_1	1.2\|842868\|34\|NZ_CP039546\|CRISPRCasFinder	842868-842901	34	MT771340	Mycobacterium phage Jorgensen, complete genome	16400-16433	10	0.706
NZ_CP039546_1	1.2\|842868\|34\|NZ_CP039546\|CRISPRCasFinder	842868-842901	34	KX702320	Mycobacterium phage Bigfoot, complete genome	16342-16375	10	0.706
NZ_CP039546_1	1.2\|842868\|34\|NZ_CP039546\|CRISPRCasFinder	842868-842901	34	KM597531	Mycobacterium phage Abrogate, complete genome	17260-17293	10	0.706
NZ_CP039546_1	1.2\|842868\|34\|NZ_CP039546\|CRISPRCasFinder	842868-842901	34	MH000606	Mycobacterium phage Fascinus, complete genome	16339-16372	10	0.706
NZ_CP039546_4	4.1\|4696271\|37\|NZ_CP039546\|CRISPRCasFinder	4696271-4696307	37	NZ_CP047184	Rathayibacter sp. VKM Ac-2801 plasmid unnamed, complete sequence	26532-26568	10	0.73
NZ_CP039546_1	1.2\|842868\|34\|NZ_CP039546\|CRISPRCasFinder	842868-842901	34	NZ_CP050083	Rhizobium leguminosarum bv. trifolii strain 31B plasmid pRL31b3, complete sequence	636341-636374	11	0.676
NZ_CP039546_1	1.2\|842868\|34\|NZ_CP039546\|CRISPRCasFinder	842868-842901	34	NZ_CP040937	Hymenobacter sp. DG01 plasmid unnamed, complete sequence	249998-250031	11	0.676

1. spacer 1.2|842868|34|NZ_CP039546|CRISPRCasFinder matches to NC_016113 (Streptomyces cattleya NRRL 8057 = DSM 46488 plasmid pSCAT, complete sequence) position: , mismatch: 6, identity: 0.824

cggcggaccgggcggattcggcggcggcggtgga	CRISPR spacer
tggcggaccgggcgggttcggcggcggtgcgggc	Protospacer
.**************.***********.*  **

2. spacer 1.2|842868|34|NZ_CP039546|CRISPRCasFinder matches to NC_017585 (Streptomyces cattleya NRRL 8057 = DSM 46488 plasmid pSCATT, complete sequence) position: , mismatch: 6, identity: 0.824

cggcggaccgggcggattcggcggcggcggtgga	CRISPR spacer
tggcggaccgggcgggttcggcggcggtgcgggc	Protospacer
.**************.***********.*  **

3. spacer 1.2|842868|34|NZ_CP039546|CRISPRCasFinder matches to NZ_CP021649 (Acidovorax sp. T1 plasmid p1-T1, complete sequence) position: , mismatch: 6, identity: 0.824

cggcggaccg--ggcggattcggcggcggcggtgga	CRISPR spacer
--gtggcctggtggcggattcggcggcggcggagga	Protospacer
  *.** *.*  ******************** ***

4. spacer 1.2|842868|34|NZ_CP039546|CRISPRCasFinder matches to NZ_CP012477 (Arthrobacter sp. ERGS1:01 isolate water plasmid unnamed2, complete sequence) position: , mismatch: 7, identity: 0.794

cggcggaccgggcggattcggcggcggcggtgga	CRISPR spacer
tcgcggaccaggcggattcggcggcggccgagac	Protospacer
. *******.****************** * *.

5. spacer 1.2|842868|34|NZ_CP039546|CRISPRCasFinder matches to NC_015952 (Streptomyces violaceusniger Tu 4113 plasmid pSTRVI02, complete sequence) position: , mismatch: 7, identity: 0.794

cggcggaccg--ggcggattcggcggcggcggtgga	CRISPR spacer
--ctggtccggcggcggatgcggcggcggcggcgga	Protospacer
   .** ***  ******* ************.***

6. spacer 1.2|842868|34|NZ_CP039546|CRISPRCasFinder matches to NC_012852 (Rhizobium leguminosarum bv. trifolii WSM1325 plasmid pR132504, complete sequence) position: , mismatch: 7, identity: 0.794

--cggcggaccgggcggattcggcggcggcggtgga	CRISPR spacer
aatggcg--cgaggaggatgcggcggcggcggtgga	Protospacer
  .****  * .** **** ****************

7. spacer 1.2|842868|34|NZ_CP039546|CRISPRCasFinder matches to NZ_CP021372 (Rhizobium sp. ACO-34A plasmid pRACO34Ad, complete sequence) position: , mismatch: 7, identity: 0.794

cggcggac-cgggcggattcggcggcggcggtgga	CRISPR spacer
-gacggtcgcgggcggatttggcggcggcgttgac	Protospacer
 *.*** * **********.********** **.

8. spacer 1.2|842868|34|NZ_CP039546|CRISPRCasFinder matches to NZ_LR134454 (Tsukamurella tyrosinosolvens strain NCTC13231 plasmid 12, complete sequence) position: , mismatch: 8, identity: 0.765

cggcggaccgggcggattcggcggcggcggtgga	CRISPR spacer
ccgcgggctgggcggattcggcggcggaagcgtc	Protospacer
* ****.*.****************** .*.*

9. spacer 1.2|842868|34|NZ_CP039546|CRISPRCasFinder matches to NZ_CP027299 (Streptomyces sp. SGAir0924 plasmid unnamed_5) position: , mismatch: 8, identity: 0.765

cggcggaccgggcggattcggcggcggcggtgga	CRISPR spacer
tggcggcccgggcggagtcggcggcgcggcacga	Protospacer
.***** ********* *********  *   **

10. spacer 1.2|842868|34|NZ_CP039546|CRISPRCasFinder matches to NC_010625 (Paraburkholderia phymatum STM815 plasmid pBPHY01, complete sequence) position: , mismatch: 8, identity: 0.765

cggcgg-accgggcggattcggcggcggcggtgga	CRISPR spacer
-gatggtagcgggcgggttcgacggcggcggtgcg	Protospacer
 *..** * *******.****.*********** .

11. spacer 1.2|842868|34|NZ_CP039546|CRISPRCasFinder matches to NZ_CP013631 (Rhizobium sp. N324 plasmid pRspN324a, complete sequence) position: , mismatch: 9, identity: 0.735

cggcggaccgggcggattcggcggcggcggtgga	CRISPR spacer
taccgcgccgggcaggttcggcggcggcggtgcc	Protospacer
.. ** .******.*.****************

12. spacer 1.2|842868|34|NZ_CP039546|CRISPRCasFinder matches to NZ_CP029356 (Azospirillum sp. CFH 70021 plasmid unnamed1) position: , mismatch: 9, identity: 0.735

cggcggaccgggcggattcggcggcggcggtgga	CRISPR spacer
tcgccttgcgggcgggttccgcggcggcggtggg	Protospacer
. **    *******.*** *************.

13. spacer 1.2|842868|34|NZ_CP039546|CRISPRCasFinder matches to NZ_CP041162 (Leisingera aquaemixtae strain R2C4 plasmid unnamed6) position: , mismatch: 9, identity: 0.735

cggcggac--cgggcggattcggcggcggcggtgga	CRISPR spacer
--gctgttcgcgggcggcctcggcggcggcggtgat	Protospacer
  ** * .  ******* .***************.

14. spacer 1.2|842868|34|NZ_CP039546|CRISPRCasFinder matches to NZ_CP010024 (Paraburkholderia fungorum strain ATCC BAA-463 plasmid pBIL, complete sequence) position: , mismatch: 9, identity: 0.735

cggcggaccgggcggattcggcggcggcggtgga	CRISPR spacer
tggcttcgggggcggtttcggcggcagcggtggc	Protospacer
.***     ****** *********.*******

15. spacer 1.2|842868|34|NZ_CP039546|CRISPRCasFinder matches to NC_015724 (Cupriavidus necator N-1 plasmid pBB2, complete sequence) position: , mismatch: 9, identity: 0.735

cggcggaccgggcggattcggcggcggcggtgga	CRISPR spacer
cggcggaccgggcgcgttcggcgggttgggcagc	Protospacer
************** .********    **..*

16. spacer 1.2|842868|34|NZ_CP039546|CRISPRCasFinder matches to NZ_AP022607 (Mycobacterium branderi strain JCM 12687 plasmid pJCM12687) position: , mismatch: 9, identity: 0.735

cggcggaccgggcggattcggcggcggcggtgga	CRISPR spacer
cgaggtcggggccggattcgccggcggcggtggc	Protospacer
**. *    ** ******** ************

17. spacer 1.2|842868|34|NZ_CP039546|CRISPRCasFinder matches to NZ_CP050100 (Rhizobium leguminosarum bv. trifolii strain 9B plasmid pRL9b3, complete sequence) position: , mismatch: 10, identity: 0.706

cggcggaccgggcggattcggcggcggcggtgga	CRISPR spacer
tgctggacccggtggattcggcggcggccgcatc	Protospacer
.* .***** **.*************** *..

18. spacer 1.2|842868|34|NZ_CP039546|CRISPRCasFinder matches to NZ_CP049733 (Rhizobium leguminosarum strain A1 plasmid pRL10, complete sequence) position: , mismatch: 10, identity: 0.706

cggcggaccgggcggattcggcggcggcggtgga	CRISPR spacer
tgctggacccggtggattcggcggcggccgcatc	Protospacer
.* .***** **.*************** *..

19. spacer 1.2|842868|34|NZ_CP039546|CRISPRCasFinder matches to NZ_CP053443 (Rhizobium leguminosarum bv. trifolii strain CC275e plasmid pRltCC275eC, complete sequence) position: , mismatch: 10, identity: 0.706

cggcggaccgggcggattcggcggcggcggtgga	CRISPR spacer
tgctggacccggtggattcggcggcggccgcatc	Protospacer
.* .***** **.*************** *..

20. spacer 1.2|842868|34|NZ_CP039546|CRISPRCasFinder matches to NZ_CP025506 (Rhizobium leguminosarum bv. viciae strain UPM791 plasmid pRlvE, complete sequence) position: , mismatch: 10, identity: 0.706

cggcggaccgggcggattcggcggcggcggtgga	CRISPR spacer
tgctggacccggtggattcggcggcggccgcatc	Protospacer
.* .***** **.*************** *..

21. spacer 1.2|842868|34|NZ_CP039546|CRISPRCasFinder matches to NZ_CP030763 (Rhizobium leguminosarum strain ATCC 14479 plasmid unnamed3, complete sequence) position: , mismatch: 10, identity: 0.706

cggcggaccgggcggattcggcggcggcggtgga	CRISPR spacer
tgctggacccggtggattcggcggcggccgcatc	Protospacer
.* .***** **.*************** *..

22. spacer 1.2|842868|34|NZ_CP039546|CRISPRCasFinder matches to NZ_CP022668 (Rhizobium leguminosarum bv. viciae strain BIHB 1217 plasmid pPR3, complete sequence) position: , mismatch: 10, identity: 0.706

cggcggaccgggcggattcggcggcggcggtgga	CRISPR spacer
tgctggacccggtggattcggcggcggccgcatc	Protospacer
.* .***** **.*************** *..

23. spacer 1.2|842868|34|NZ_CP039546|CRISPRCasFinder matches to NZ_CP013412 (Burkholderia thailandensis strain 2002721643 plasmid p2002721643, complete sequence) position: , mismatch: 10, identity: 0.706

cggcggaccgggcggattcggcggcggcggtgga	CRISPR spacer
gacctgaccgtgcggattccgcggcggcgtcgct	Protospacer
 . * ***** ******** ********* .*

24. spacer 1.2|842868|34|NZ_CP039546|CRISPRCasFinder matches to NZ_CP010016 (Burkholderia thailandensis 34 plasmid unnamed, complete sequence) position: , mismatch: 10, identity: 0.706

cggcggaccgggcggattcggcggcggcggtgga	CRISPR spacer
gacctgaccgtgcggattccgcggcggcgtcgct	Protospacer
 . * ***** ******** ********* .*

25. spacer 1.2|842868|34|NZ_CP039546|CRISPRCasFinder matches to NZ_CP053207 (Rhizobium leguminosarum bv. trifolii TA1 plasmid pRltTA1C, complete sequence) position: , mismatch: 10, identity: 0.706

cggcggaccgggcggattcggcggcggcggtgga	CRISPR spacer
tgctggacccggtggattcggcggcggccgcatc	Protospacer
.* .***** **.*************** *..

26. spacer 1.2|842868|34|NZ_CP039546|CRISPRCasFinder matches to NZ_CP050088 (Rhizobium leguminosarum bv. trifolii strain 23B plasmid pRL23b6, complete sequence) position: , mismatch: 10, identity: 0.706

cggcggaccgggcggattcggcggcggcggtgga	CRISPR spacer
tgctggacccggtggattcggcggcggccgcatc	Protospacer
.* .***** **.*************** *..

27. spacer 1.2|842868|34|NZ_CP039546|CRISPRCasFinder matches to MG962370 (Mycobacterium phage Kykar, complete genome) position: , mismatch: 10, identity: 0.706

cggcggaccgggcggattcggcggcggcggtgga	CRISPR spacer
cacctccgggggcgggttcggcggcggcggaggt	Protospacer
*. *     ******.************** **

28. spacer 1.2|842868|34|NZ_CP039546|CRISPRCasFinder matches to MT771340 (Mycobacterium phage Jorgensen, complete genome) position: , mismatch: 10, identity: 0.706

cggcggaccgggcggattcggcggcggcggtgga	CRISPR spacer
cacctccgggggcgggttcggcggcggcggaggt	Protospacer
*. *     ******.************** **

29. spacer 1.2|842868|34|NZ_CP039546|CRISPRCasFinder matches to KX702320 (Mycobacterium phage Bigfoot, complete genome) position: , mismatch: 10, identity: 0.706

cggcggaccgggcggattcggcggcggcggtgga	CRISPR spacer
cacctccgggggcgggttcggcggcggcggaggt	Protospacer
*. *     ******.************** **

30. spacer 1.2|842868|34|NZ_CP039546|CRISPRCasFinder matches to KM597531 (Mycobacterium phage Abrogate, complete genome) position: , mismatch: 10, identity: 0.706

cggcggaccgggcggattcggcggcggcggtgga	CRISPR spacer
cacctccgggggcgggttcggcggcggcggaggt	Protospacer
*. *     ******.************** **

31. spacer 1.2|842868|34|NZ_CP039546|CRISPRCasFinder matches to MH000606 (Mycobacterium phage Fascinus, complete genome) position: , mismatch: 10, identity: 0.706

cggcggaccgggcggattcggcggcggcggtgga	CRISPR spacer
cacctccgggggcgggttcggcggcggcggaggt	Protospacer
*. *     ******.************** **

32. spacer 4.1|4696271|37|NZ_CP039546|CRISPRCasFinder matches to NZ_CP047184 (Rathayibacter sp. VKM Ac-2801 plasmid unnamed, complete sequence) position: , mismatch: 10, identity: 0.73

cccgccgcgggcgcgcgtgaagccctcgaaatcgaag	CRISPR spacer
atcaccgctggcgcgcgagaagccctcgaagcggtcg	Protospacer
 .*.**** ******** ************.. *  *

33. spacer 1.2|842868|34|NZ_CP039546|CRISPRCasFinder matches to NZ_CP050083 (Rhizobium leguminosarum bv. trifolii strain 31B plasmid pRL31b3, complete sequence) position: , mismatch: 11, identity: 0.676

cggcggaccgggcggattcggcggcggcggtgga	CRISPR spacer
ttctggacccggtggattcggcggcggccgcatc	Protospacer
.  .***** **.*************** *..

34. spacer 1.2|842868|34|NZ_CP039546|CRISPRCasFinder matches to NZ_CP040937 (Hymenobacter sp. DG01 plasmid unnamed, complete sequence) position: , mismatch: 11, identity: 0.676

cggcggaccgggcggattcggcggcggcggtgga	CRISPR spacer
tgctaccatgggcggattcggcggcggtggcggc	Protospacer
.* ..   .******************.**.**

Prophage detection

Region

Region Position

Protein_number

Hit_taxonomy

Key_proteins

Att_site

Prophage annotation

DBSCAN-SWA_1

1497952 : 1510440

Paracoccus_phage(25.0%)

head,protease,tail

The bacterium proteins that are colored denote the protein is present at specific phage-related keywords (such as 'capsid', 'head', 'integrase', 'plate', 'tail', 'fiber', 'coat', 'transposase', 'portal', 'terminase', 'protease' or 'lysin' and 'tRNA')

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_141950865.1\|1497952_1498582_-	glycoside hydrolase family protein	W6E9Q2	Rhizobium_phage	2.0e-25	42.1
WP_141950866.1\|1498628_1499711_-	DUF2793 domain-containing protein	A0A0K1LM04	Rhodobacter_phage	1.7e-32	36.5
WP_141950867.1\|1499737_1503640_-	hypothetical protein	A0A0B5A7K5	Paracoccus_phage	1.6e-197	36.7
WP_141950868.1\|1503666_1504125_-	peptidase P60	A0A1V0DYB6	Dinoroseobacter_phage	1.2e-30	50.0
WP_141950869.1\|1504132_1505026_-	DUF2163 domain-containing protein	A0A1V0DY93	Dinoroseobacter_phage	2.8e-52	37.5
WP_141950870.1\|1505036_1505678_-	TIGR02217 family protein	A0A0B5A2K3	Paracoccus_phage	1.0e-48	49.8
WP_141950871.1\|1505689_1506316_-\|tail	phage tail tape measure protein	G9JXH3	Shigella_phage	1.5e-07	67.4
WP_141950872.1\|1506302_1506545_-\|tail	phage tail assembly chaperone	NA	NA	NA	NA
WP_141950873.1\|1506541_1506868_-	gene transfer agent family protein	NA	NA	NA	NA
WP_141950874.1\|1506870_1507281_-\|tail	phage major tail protein, TP901-1 family	NA	NA	NA	NA
WP_141950875.1\|1507311_1507731_-	DUF3168 domain-containing protein	NA	NA	NA	NA
WP_141950876.1\|1507727_1508066_-\|head,tail	head-tail adaptor protein	NA	NA	NA	NA
WP_141950877.1\|1508088_1508664_-	hypothetical protein	NA	NA	NA	NA
WP_141950878.1\|1508697_1509444_+\|protease	trypsin-like serine protease	NA	NA	NA	NA
WP_012453341.1\|1509591_1510440_+\|protease	trypsin-like serine protease	I6WTR7	Cotesia_sesamiae_Mombasa_bracovirus	4.9e-06	23.4

DBSCAN-SWA_2

3095968 : 3103336

Cronobacter_phage(16.67%)

tRNA

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_141951863.1\|3095968_3097240_-\|tRNA	tyrosine--tRNA ligase	K4F5T3	Cronobacter_phage	9.4e-54	33.4
WP_141951864.1\|3097378_3098512_+	anhydro-N-acetylmuramic acid kinase	NA	NA	NA	NA
WP_141951865.1\|3098508_3099114_+	DUF3578 domain-containing protein	NA	NA	NA	NA
WP_012455043.1\|3099118_3099406_-	putative addiction module antidote protein	A4JWV1	Burkholderia_virus	7.4e-15	45.1
WP_141951866.1\|3099402_3099705_-	type II toxin-antitoxin system RelE/ParE family toxin	A0A141GEX6	Brucella_phage	2.0e-23	59.1
WP_141951867.1\|3099837_3100938_+	chorismate synthase	A0A291AU41	Pandoravirus	6.2e-78	47.2
WP_141951868.1\|3100973_3102050_+	3,4-dihydroxy-2-butanone-4-phosphate synthase	A0A2H4PQS2	Staphylococcus_phage	5.4e-58	36.5
WP_141951869.1\|3102148_3102382_+	hypothetical protein	NA	NA	NA	NA
WP_141954883.1\|3102406_3103336_-	histone deacetylase family protein	A0A2K9KZC4	Tupanvirus	6.1e-34	32.4

Anti-CRISPR protein detection

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

Overview of predicted results

Overview of the results

Cas Category Instructions

Results visualization

1. NZ_CP039546

Click the left colored region to show detailed information

CRISPR-Cas detection and classification

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Self-targeting detection

MGE targeting detection<

Prophage detection

Anti-CRISPR protein detection