CRISPRimmunity

Overview of predicted results

Overview of the results

Contig_ID	Contig_def	CRISPR array number	Contig Signature genes	Self targeting spacer number	Target MGE spacer number	Prophage number	Anti-CRISPR protein number
NC_014958	Deinococcus maricopensis DSM 21211, complete sequence	2 crisprs	DEDDh,csa3,WYL,cas3	0	3	0	0

1. NC_014958

CRISPR-Cas detection and classification

Crispr_ID: NC_014958_1

• CRISPR_ID: NC_014958_1
• CRISPR_location: 667370-667601
• CRISPR_type: Orphan
• Repeat_type: NA
• Spacer_info: 4 spacers

Consensus repeat of NC_014958_1

Consensus_repeat	Method
CGTCGGCGGCGGCAGC	PILER-CR

spacers of NC_014958_1

>1.1|667386|35|NC_014958|PILER-CR
GCCACCCTGCGCGACACCGGCAGCCTCATCGCCAG
>1.2|667437|38|NC_014958|PILER-CR
CTCACCGCGCACAACACCCACGGGCCCGCCCGCATCAC
>1.3|667491|35|NC_014958|PILER-CR
GTCCGCCTCCACGACGCGCACCCGCTGACCGCGCA
>1.4|667542|44|NC_014958|PILER-CR
CTGCAATGGGCGCCGCGCCTGAACGAAGGCGACCACCACATCAG

CRISPR arrays and Neighbor proteins around NC_014958_1

CRISPR arrays

The CRISPR arrays of NC_014958_1

>merge|NC_014958|1|667370-667601|PILER-CR
CGTCGGCGGCGGCAGCGCCACCCTGCGCGACACCGGCAGCCTCATCGCCAGCGTCGGCGGCGGCAGCCTCACCGCGCACAACACCCACGGGCCCGCCCGCATCACCGTCGGCGGCGGCAGCGTCCGCCTCCACGACGCGCACCCGCTGACCGCGCAGATCGGCGGCGGCAGCCTGCAATGGGCGCCGCGCCTGAACGAAGGCGACCACCACATCAGCGTCGCCGGCGGCAGC

>NC_014958|1|1|667370-667601|PILER-CR
CGTCGGCGGCGGCAGC	GCCACCCTGCGCGACACCGGCAGCCTCATCGCCAG
CGTCGGCGGCGGCAGC	CTCACCGCGCACAACACCCACGGGCCCGCCCGCATCAC
CGTCGGCGGCGGCAGC	GTCCGCCTCCACGACGCGCACCCGCTGACCGCGCA
GATCGGCGGCGGCAGC	CTGCAATGGGCGCCGCGCCTGAACGAAGGCGACCACCACATCAG
CGTCGCCGGCGGCAGC

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
NC_014958.1|WP_043816408.1|668493_668850_+|DUF2089-domain-containing-protein	unknown	unknown	gnl|CDD|378280
NC_014958.1|WP_013555748.1|671936_674414_+|tetratricopeptide-repeat-protein	unknown	unknown	gnl|CDD|226156
NC_014958.1|WP_013555732.1|656231_656939_+|bacillithiol-biosynthesis-deacetylase-BshB1	unknown	unknown	gnl|CDD|274915
NC_014958.1|WP_013555737.1|661088_661553_-|hypothetical-protein	unknown	unknown	gnl|CDD|378303
NC_014958.1|WP_013555741.1|665351_666740_-|RNB-domain-containing-ribonuclease	unknown	unknown	gnl|CDD|223631
NC_014958.1|WP_013555746.1|669266_669836_-|DUF1990-domain-containing-protein	unknown	unknown	gnl|CDD|378157
NC_014958.1|WP_013555736.1|660695_661037_+|NAD(P)H-dependent-oxidoreductase-subunit-E	unknown	unknown	gnl|CDD|239278
NC_014958.1|WP_013555749.1|674447_676019_-|HAMP-domain-containing-histidine-kinase	unknown	unknown	gnl|CDD|223715
NC_014958.1|WP_013555738.1|661709_662468_+|class-I-SAM-dependent-methyltransferase	unknown	unknown	gnl|CDD|379312
NC_014958.1|WP_013555750.1|676153_676831_-|response-regulator-transcription-factor	unknown	unknown	gnl|CDD|223816
NC_014958.1|WP_013555752.1|677668_678121_-|hypothetical-protein	unknown	unknown	unknown
NC_014958.1|WP_013555739.1|662464_663418_+|NAD(P)H-dependent-glycerol-3-phosphate-dehydrogenase	unknown	unknown	gnl|CDD|237770
NC_014958.1|WP_013555751.1|676958_677570_-|adenylate/guanylate-cyclase-domain-containing-protein	unknown	unknown	gnl|CDD|143636
NC_014958.1|WP_013555733.1|657715_658813_-|Type-1-glutamine-amidotransferase-like-domain-containing-protein	unknown	unknown	gnl|CDD|240026
NC_014958.1|WP_013555743.1|667792_668395_+|hypothetical-protein	unknown	unknown	unknown
NC_014958.1|WP_013555747.1|669908_671717_-|S8-family-serine-peptidase	unknown	unknown	gnl|CDD|173812
NC_014958.1|WP_013555734.1|658850_660071_-|NTP-transferase-domain-containing-protein	unknown	unknown	gnl|CDD|223525
NC_014958.1|WP_013555745.1|669002_669188_+|hypothetical-protein	unknown	unknown	unknown
NC_014958.1|WP_013555740.1|663438_665292_-|VWA-domain-containing-protein	unknown	unknown	gnl|CDD|378410
NC_014958.1|WP_013555735.1|660117_660660_-|5-formyltetrahydrofolate-cyclo-ligase	unknown	unknown	gnl|CDD|274270

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
NC_014958.1|WP_043816408.1|668493_668850_+|DUF2089-domain-containing-protein	gnl|CDD|378280	pfam09862, DUF2089, Protein of unknown function (DUF2089). This domain, found in various hypothetical prokaryotic proteins, has no known function. This domain is a zinc-ribbon.	5.43401e-48
NC_014958.1|WP_013555748.1|671936_674414_+|tetratricopeptide-repeat-protein	gnl|CDD|226156	COG3629, DnrI, DNA-binding transcriptional activator of the SARP family [Signal transduction mechanisms].	1.87337e-06
NC_014958.1|WP_013555732.1|656231_656939_+|bacillithiol-biosynthesis-deacetylase-BshB1	gnl|CDD|274915	TIGR04001, thiol_BshB1, bacillithiol biosynthesis deacetylase BshB1. Members of this protein family are BshB1 (YpjG), an enzyme of bacillithiol biosynthesis; either BshB1 or BshB2 (YojG) must be present, and often both are present. Bacillithiol is a low-molecular-weight thiol, an analog of glutathione and mycothiol, and is found largely in the Firmicutes. [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs].	2.97428e-61
NC_014958.1|WP_013555737.1|661088_661553_-|hypothetical-protein	gnl|CDD|378303	pfam09912, DUF2141, Uncharacterized protein conserved in bacteria (DUF2141). This domain, found in various hypothetical prokaryotic proteins, has no known function.	0.000867193
NC_014958.1|WP_013555741.1|665351_666740_-|RNB-domain-containing-ribonuclease	gnl|CDD|223631	COG0557, VacB, Exoribonuclease R [Transcription].	4.7727e-77
NC_014958.1|WP_013555746.1|669266_669836_-|DUF1990-domain-containing-protein	gnl|CDD|378157	pfam09348, DUF1990, Domain of unknown function (DUF1990). This family of proteins are functionally uncharacterized.	5.86195e-48
NC_014958.1|WP_013555736.1|660695_661037_+|NAD(P)H-dependent-oxidoreductase-subunit-E	gnl|CDD|239278	cd02980, TRX_Fd_family, Thioredoxin (TRX)-like [2Fe-2S] Ferredoxin (Fd) family; composed of [2Fe-2S] Fds with a TRX fold (TRX-like Fds) and proteins containing domains similar to TRX-like Fd including formate dehydrogenases, NAD-reducing hydrogenases and the subunit E of NADH:ubiquinone oxidoreductase (NuoE). TRX-like Fds are soluble low-potential electron carriers containing a single [2Fe-2S] cluster. The exact role of TRX-like Fd is still unclear. It has been suggested that it may be involved in nitrogen fixation. Its homologous domains in large redox enzymes (such as Nuo and hydrogenases) function as electron carriers.	1.21235e-13
NC_014958.1|WP_013555749.1|674447_676019_-|HAMP-domain-containing-histidine-kinase	gnl|CDD|223715	COG0642, BaeS, Signal transduction histidine kinase [Signal transduction mechanisms].	3.97065e-67
NC_014958.1|WP_013555738.1|661709_662468_+|class-I-SAM-dependent-methyltransferase	gnl|CDD|379312	pfam13649, Methyltransf_25, Methyltransferase domain. This family appears to be a methyltransferase domain.	6.92382e-22
NC_014958.1|WP_013555750.1|676153_676831_-|response-regulator-transcription-factor	gnl|CDD|223816	COG0745, OmpR, Response regulators consisting of a CheY-like receiver domain and a winged-helix DNA-binding domain [Signal transduction mechanisms / Transcription].	1.51682e-87
NC_014958.1|WP_013555739.1|662464_663418_+|NAD(P)H-dependent-glycerol-3-phosphate-dehydrogenase	gnl|CDD|237770	PRK14618, PRK14618, NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional.	4.69242e-139
NC_014958.1|WP_013555733.1|657715_658813_-|Type-1-glutamine-amidotransferase-like-domain-containing-protein	gnl|CDD|240026	cd04669, Nudix_Hydrolase_11, 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.	7.15808e-22
NC_014958.1|WP_013555751.1|676958_677570_-|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.	8.83289e-25
NC_014958.1|WP_013555747.1|669908_671717_-|S8-family-serine-peptidase	gnl|CDD|173812	cd07487, Peptidases_S8_1, Peptidase S8 family domain, uncharacterized subfamily 1. This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.	2.70534e-60
NC_014958.1|WP_013555734.1|658850_660071_-|NTP-transferase-domain-containing-protein	gnl|CDD|223525	COG0448, GlgC, ADP-glucose pyrophosphorylase [Carbohydrate transport and metabolism].	2.66026e-138
NC_014958.1|WP_013555740.1|663438_665292_-|VWA-domain-containing-protein	gnl|CDD|378410	pfam10138, vWA-TerF-like, vWA found in TerF C-terminus. vWA domain fused to TerD domain typified by the TerF protein. Some times found as solos.	3.23021e-72
NC_014958.1|WP_013555735.1|660117_660660_-|5-formyltetrahydrofolate-cyclo-ligase	gnl|CDD|274270	TIGR02727, Uncharacterized_protein_YqgN, 5,10-methenyltetrahydrofolate synthetase. This enzyme, 5,10-methenyltetrahydrofolate synthetase, is also called 5-formyltetrahydrofolate cycloligase. Function of bacterial proteins in this family was inferred originally from the known activity of eukaryotic homologs. Recently, activity was shown explicitly for the member from Mycoplasma pneumonia. Members of this family from alpha- and gamma-proteobacteria, designated ygfA, are often found in an operon with 6S structural RNA, and show a similar pattern of high expression during stationary phase. The function may be to deplete folate to slow 1-carbon biosynthetic metabolism. [Central intermediary metabolism, One-carbon metabolism].	4.96453e-35

Protein sequences

>NC_014958.1|WP_013555741.1|665351_666740_-|RNB-domain-containing-ribonuclease
MTAEALTAAQRTDLELIARGKQQKSRTLRERGLPETPEAAHALLLQLGLWTTHHNPHPERGGVQLTPPQHDLPDLPDEARTDLTHLTALAIDDDGNQDPDDALSLETLPDGTRRLWVHVADVAALIPPDSPADLEARARGATLYLPEGTVPMLPPAVVERLGLGLQDTSPALSISIDFEGHWEPTVVDVVATTVRVTRLTYRDAQARLDAGDPLLVDLAALAGAHRTYREDGGAVTITLPEVKVTAQDGDVHITPLPPLTARTIVQECMMLAGWAAAVWADDQEVPLPYAAQDAPHRDVRGDTLAAHWARRKTLARTRFQTAPAAHRGMGLDLYAQATSPMRRYLDLVVHQQLRAVLRGDEPLAGRDIAARTAEANMSADAVRAAERASRRHWTLKHLANHPERVWDAVIVERRGPQAVALIPDLALDTTLHSAHPVGTPLRLQLVQADLPNLQARFREVNA
>NC_014958.1|WP_013555740.1|663438_665292_-|VWA-domain-containing-protein
MLLQRGEKRRLGDLGVTTTFTVQFDAGLRGADVSVFGLDDDRQLRDDQYFVFYNQPRSPHGALTTTAQPSSAGGTFEVNLGALPASITRLMFVATHDDTPFSAAAQGTWTLTHAGGTAAQYTYAGSDFGAERAVMVAEVYRHNGEWRVAAVGQGFGGGLQALLEHFGGQAEEAAPAPAPAPDTLPEPSAEKVSLRKQQVTAVLQRAGIEHVKARVMVVMDASGSMRALYRNGVVQDTLERLIPVALKLDDNEAMEFWYYAERFAQMGDLDQHSVVGLVGDVMPQKNPLLPAHVHSIGGGNNEPPVMEDVLRQHREAQAEDRAAGVGIMPTLVLFLTDGGISGSSKKIAQLIKGSSSEPLFWQFIGLGDANYGILRQLDTLQGRVIDNSGFFAVDDIAQVTDEVLYDRMLSEFAGWWKAWQQLQPPAAPTPRPAPTAAVSLRKNGAVQLQKAATLRAALEWKGQGDLDLYAFYVLADGTSGKVYYRDLGHKDRAPYITLSGDSRVPGREEIVIHRPDALRHVLISAYSAVENGLGSFASYQPRAVVTDGGAQRVDVPVLNRNHFSFWVALASIDFTSPSGPTIRHVERYSRIGTERSPTLNADGTFTMNTGPVEFKGR
>NC_014958.1|WP_013555739.1|662464_663418_+|NAD(P)H-dependent-glycerol-3-phosphate-dehydrogenase
MSVLVLGAGGWGTALAVMLARHGTPATLWARRADFAAELRGARENRAYLPGVPLPDAVTVTEDLGVVSAFAWALVVVPSRGVEELLGNLPRTLGVVLCAKGLAEDGARLTTLAARLGFTRVAVLSGPNHAEEVARGLPAATVVASSDAAFAQDVQRALMTPSFRVYTSADVVGVELGGVLKNVMAVAGGLVDGLRLGDNAKAAILTRGLREMGRYLIASGADDDTLYGLSGLGDLIATATSVHSRNRAAGEAIARGEPPVQGGKVAEGVRTAGLLADWAQAHGHDLPITRAVARVVAGTWTPPQALASLMERGAKPE
>NC_014958.1|WP_013555738.1|661709_662468_+|class-I-SAM-dependent-methyltransferase
MQRPPFTALASVYDAIMADIEYDDWAEFVLTYLRAEGVTPRRLLDLACGTGASSAPFAARGLDVTGLDYSADMLRVARERHPHLTFVQGDLRDFQVDGPFELITCIFDSLNNLTDPADLGRALARAHAHLAPGGYLAFDVNTRAGVRDLWEGDTIEGLTETPDGREVHYHWSHHYEPDTELGVVQAFVRVEGDEFVEVHRERGYDQADLDPLLAAAGFAEWTFVEYPDYAPPALDATRVWVFARVAPEGAGA
>NC_014958.1|WP_013555737.1|661088_661553_-|hypothetical-protein
MKKMMTLAAAATVALSSCSLLGNPNNPDVSGKLTGGFPADGSVRLALAGRSLNNFTTVDSSPTQIVDAKILNGYTLDLPSNLAAGDYTVIAFLDANKDGKYNVGETIVSDDGGKRLVFKTANDASYRQGWNIRRADGTVQNQPLTGYDLTYKSN
>NC_014958.1|WP_013555736.1|660695_661037_+|NAD(P)H-dependent-oxidoreductase-subunit-E
MTAKYFRTNAHLLVCQHTNCASRGSALLHRALWNALERDGLAYYKRGGSVRLTSSGCLGACSHGPVLCVYRDAGGRLEEGWYAAVDFPLALQVARAAHEGAPLPADRKYGPAE
>NC_014958.1|WP_013555735.1|660117_660660_-|5-formyltetrahydrofolate-cyclo-ligase
MTEAAKAAWRTRVRAERSALPDVSGAVTAHLRAFLRARGARVVLAYRALPGEVDVGDLADAFELLTTRARWRPAPHLTLHPWATATERSRFGALQPPADAPRVDRARVDAVLLPALAFDEVGFRLGYGGGFYDRLLAGWAVPTVGVTPEALVLPDVPRAAHDVPVAFLATERGVRRVKGR
>NC_014958.1|WP_013555734.1|658850_660071_-|NTP-transferase-domain-containing-protein
MASRSPRARGTRVDGQSVLTLILAGGQGKRMGVLTEDRAKPVMPFGGTYHLIDFALSNCVNSGLSDVWVVEEYELHSLNDHLRNGRPWDLDRTHGGLQVLPPYTGGDEEGGFARGNAHALWLQRQLIEEFDPDVLLVLSADHVYALDYGEVIRAHVARAAQLTMVTVPVPPGERASRFGNVVVGEDGRVRQFAYKPDKPISDTVTTEVFAYDARALLAALQALAEDGGAEALGDFGERLVPHFVEGGGAYAWAFDGYWRDVGLPDAYWRAHMDLLDRQSVVLDRPDWPILTAGIPRTPARIEDGAVVRGSILSYGCEVAGTVERSVLAPGVIVEAGATVRGSVLLRDVTVRAGATVERAIVDNDACIGAGARVGAAQGDLVVVGEGASVADGAVIAAGEQVAPTGT
>NC_014958.1|WP_013555733.1|657715_658813_-|Type-1-glutamine-amidotransferase-like-domain-containing-protein
MTGTVVLIGGGLPARGETAHVERVWTAWLPAPRVAVVPTASWGRPDLTGFVEDLIAYLAGFGVEAFLLPVGTHDDADDPAVLRALDGVGGVYVLGGDTRTLADALRGSALLRRVRALVEGGGVFVGVSAGAILAGVDGVDDQGRNVDGWHLWPGRAWPHADQPDFAFMGARLRGRDHVKLRDGDAGVWRDGELRLLPRPGRHRAGVLVVRAASGPLPDVTQPVSPAERAALEVLLLERHSPYRRGAYYIVPGGGLEAGEVPEAAAVREAHEELSLDVTLVRLAARVHVPDLARTEHYFLATASGEAALHPDSPEAARASARNTYAFRWVPVTALPDLPVFPAALRALDEALARGEVLEAQAEPLS
>NC_014958.1|WP_013555732.1|656231_656939_+|bacillithiol-biosynthesis-deacetylase-BshB1
MRTVYGTPQPLDWLCLAPHPDDAEIGAGGTLIRLARAGRAVGILELTRGENGTLGTPEQREAECVDAARIMGLAWRGQLDLPDGGLMDTPEQASTLARALRLTRPRVLVIPHHHDRHPDHFGAYHLAKRAAHLAALRKAPLDGDVHRVSTTLLYQGNGDINADLVVDVEAHLHDWATAIRAHVSQFSGETVSETVTPEVIERRTARLMYWGTLTRRRYAEAFELDAPLTLDPLSL
>NC_014958.1|WP_013555743.1|667792_668395_+|hypothetical-protein
MTEHLHGRVRKILDLAASGKLADEDAAQLLGALHPRLAPEGDAVTHVLALARTPDFGPDLIAGLLTDRALPGARRPPRPPGPPSWNGIDDFVDRVTTSVEGALDFALDGRRGGKRGTPGRPGTTLRVEVEDSHGNDYRLNLPLALAEHAPRLLPPAALGAIERAGLNEHALTLLLSSQPAPGEILSANLDDGTEVRLVVQ
>NC_014958.1|WP_043816408.1|668493_668850_+|DUF2089-domain-containing-protein
MPRPLPLPFPGAQDAPIVTELEFRDAGATVRGEFTLNEFATLTPDNLEFLRLYIKVRGNLKEVERVLGVSYPTVRARFDTLLRAIGYEPEPQDPRDETLALLERGEITPEEATRRLRK
>NC_014958.1|WP_013555745.1|669002_669188_+|hypothetical-protein
MPARSTLLASAVLTVFGIVGLTVVSDARPLRAPTVVLLDQMYHSAPVVVPTQPAWLRTSHD
>NC_014958.1|WP_013555746.1|669266_669836_-|DUF1990-domain-containing-protein
MFSLRRPTAARVAAFRARAEAAGWSYAPVGGTRAGGPVRGYFLDRREVVLGHGEAVFARARRALRGWAPFAGGWPALCGTPAPVAPGVTVVLRVRTLGVYSLVANRVVYVVDEPRRFGFAYGALHGHVAAGEELFSVTHGADDAVRFSLLAFSRPQATLAYLGAPVMRAVQRRVGRAYARAMLNAVRAP
>NC_014958.1|WP_013555747.1|669908_671717_-|S8-family-serine-peptidase
MKKTSTFGLGLTLLLAACSTSTPTTPSGTAAVAAQTTSSTTSACSALYATAPSGVQVDSNLRYGQVGTLILSFTDDVTKGRAIDWMDAQLPVDLGRGLGALENLPIIALKTVVTPQLVETLQANLPGLVSVYADAPLHYNLAESVKYIKADAARATYGVNGKGVGVAIIDSGLDGLHPDLKNVGKNVKIIGPVTDVGVGGYLYADVPDSDTSSGHGTHVASTIGGSGAASAGSTRMRQGVAPGATLVGIGAGEGLSILYALQGFDFALKPDIKDTYNIRVISNSWGSSGEFAPYNPISLAAKRAYDQGVIVTFAAGNEGPDANTLNPYSASPCVISVAAGDKKGYLADFSSRGRAGDANVHPDVTAPGVDISAARATLGAAATTVPDTDNPLYATISGTSMATPHISGVVALMLEANPKLNLDSVMSIFQKTSRPMYYTVAADDGLNPSQVITKKRELWEVGYGYVDANAAVREAARLNPNRTTVTTTALPGWSSTVATSACAPLVNCVTTAHDEHLLNVPSGASALRVSTDWGNPAYDLDLEVYNPQGVLVGSSAQGTSTGESVSIPNPVAGTWKVVLKGYLNAQTTYTGTAAIDKVTLVR
>NC_014958.1|WP_013555748.1|671936_674414_+|tetratricopeptide-repeat-protein
MVLLPARVRARLAVRPTVVVAPVGVGFAQDALLQWATAHGYTVTRDLTGDETGLTVWWPRSRGALETLGNHADPRAALLLEEADLTYHLEDWANALPGLSADKAADSHAQAEGWPAALPLAAALADHPATDLAAHPLAPALLGPLLPPMPLRSAFERLAPAPLVTPDVARLLGTSADDVRALVDGGWLTPIPGGWRAPTLLRHLAAPAATARTAERIARALHDAGHTDAALGALAHAGAWRAYLRLLAAHARAQDGEAALRARLRPLPPAWAQHPDRLYLAGLLARASGDLDGADALYRAARRGARAGLRPTLLNAHGVVLALLDRADEALLAFEQAERGALGVVAGEAAHNRAGLLTRLGRHADAEASLRAAVGAFRAAGDATREARSLEVLGTLLTARGLLREALTPYEGALRLLDAQGAHASAALARVNLAEVHALLGDPGAAEQHLERADTPAGRDTHGWAERGRALVALLRDDHDDAARRLAALRAAAPADRALRAEVALLLARTHRERGDEAAARAALADARPLGWRARLEAALLGDGDLTAAIQEARAADARHELALALLHRADGDDLHEALALIRTHGYATLLGGPLATRLAGIAHTDTALRALFPISVALLGPLTVRFAGQTLRLADFPTRKSAALLVALAVADHPQPREALADRFWPDAKNPLASLQTAVYHLRSALGAPVVQGERGVLALSFPARVDTRHLEDAVARADLTALLTALPRGPEVPAVLPDLPADLAREREHAERTLTDAYRLLAAHSPASSDARRDALRALIAGDPYDLDAREQLAALHDARGEREAAAQERARLHAARHELRTR
>NC_014958.1|WP_013555749.1|674447_676019_-|HAMP-domain-containing-histidine-kinase
MTLRWRLTFFYATLVTTLLVVLGVSLTGVMQRRLLDNVDSDLLETYGQFMRLNDLASQPTYGPPNGNPFQPLDDQTRLQQIGESSFPATPLQVDLLIGQSVESVRTLPVDLLQQIARQGRQLWQINPDRPIELTGPQWTKLQRSPERNLKFTAALPALYQQAARPVRIFVALGDYSYAPSASLGSGSEKTTAVVYVARDLTNVYETIDNLRLITFVVFLIGALGAGVGAYVFSGQALKPLRQVQQAAEGIGGRTLAQRVPEPDTGDEVQSLARALNGMLDRLEASFEAQRRFTSDASHELRTPVTAISGHAGYLLRRTQPTDQQRESLGIIKSEADRLTGLIGSLLELARSDSGVLQLRLQPVLSCLFLQDIARELRPLAQAQGATLTPEGEEIPFQGDPDRLRQVLINLVSNALKAGSHAITLRSARDPNPSGPPSVRLSVQDDGPGIAPEHLGRLFDRFYRVEESRSRDQGGAGLGLAIVKSIVDAHHGQIWVESEVGVGTTVHVRLPIGNVPDLDPDDVA
>NC_014958.1|WP_013555750.1|676153_676831_-|response-regulator-transcription-factor
MERKPLVLVIEDEKDIARFIELELAAEGYATEVAFDGVTGLSKFREVNPDLVILDLMLPVLDGLEVARRIRKTSNTPIIILTAKDNIQDKVEGLDSGADDYLVKPFSIEELLARVRAHLRRVNPAVTGEVRVADLVMNLDGREIFRGGRRVELSAKEFELLELLARNPGKVFSRFEIEEKVWPEYTGGSNVVDVYIGYLRRKLEEGGERRLIHTVRGVGYVLREE
>NC_014958.1|WP_013555751.1|676958_677570_-|adenylate/guanylate-cyclase-domain-containing-protein
MTTLLLPSSPGAPSARRPVCAVVVDLAGSTSLAHRLPLEHYTAVMGELMQVLYLHLEMLRGHVLQHQGDAVICLWDIEDTPYALEAALTAHARAADLSLARLLGEHLQLRCGVACGEVMMGVIGGIEAAYGLPVNLARRLCDAGQRGWTLTCANTPLYAPHAELTPSDPLPLRGFPEPCLSYRASASGVSVTGLQNSSHMKIV
>NC_014958.1|WP_013555752.1|677668_678121_-|hypothetical-protein
MTLESTPEEFAARFAAFAAQGVVYPQPEGSPLLEFTAGGRVLYLFDRSGPYAARPGPARVVVHGVARRWALSDAREEALGAVGVSAVEGVGVVLSVARQVLVVQARLPLVLGVLGGAAGVSVGDWVAFETEPPLHGFLAEGVPARGTPGG

Crispr_ID: NC_014958_2

• CRISPR_ID: NC_014958_2
• CRISPR_location: 1955814-1955987
• CRISPR_type: Orphan
• Repeat_type: NA
• Spacer_info: 2 spacers

Consensus repeat of NC_014958_2

Consensus_repeat	Method
TCAGGCGCAGTACGAGAAGTACCT	CRISPRCasFinder

spacers of NC_014958_2

>2.1|1955838|51|NC_014958|CRISPRCasFinder
CGCCTACCAGGAAGCCGTGCACGAGCGACGGTTGCGCGAAAAGTATGCACG
>2.2|1955913|51|NC_014958|CRISPRCasFinder
TGCGTATATGAACAGCCCGGAGCGTCGGCGCGCGCAGGAGCGGTACGCGCG

CRISPR arrays and Neighbor proteins around NC_014958_2

CRISPR arrays

The CRISPR arrays of NC_014958_2

>merge|NC_014958|2|1955814-1955987|CRISPRCasFinder
TCAGGCGCAGTACGAGAAGTACCTCGCCTACCAGGAAGCCGTGCACGAGCGACGGTTGCGCGAAAAGTATGCACGTCAGGCGCAGTACGAGAAGTATCTTGCGTATATGAACAGCCCGGAGCGTCGGCGCGCGCAGGAGCGGTACGCGCGACAGGCCGCCTACGAGAAGTACCT

>NC_014958|2|1|1955814-1955987|CRISPRCasFinder
TCAGGCGCAGTACGAGAAGTACCT	CGCCTACCAGGAAGCCGTGCACGAGCGACGGTTGCGCGAAAAGTATGCACG
TCAGGCGCAGTACGAGAAGTATCT	TGCGTATATGAACAGCCCGGAGCGTCGGCGCGCGCAGGAGCGGTACGCGCG
ACAGGCCGCCTACGAGAAGTACCT

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
NC_014958.1|WP_013556972.1|1959322_1960489_-|phosphoglycerate-kinase	unknown	unknown	gnl|CDD|234613
NC_014958.1|WP_013556969.1|1956876_1957407_-|septal-ring-lytic-transglycosylase-RlpA-family-protein	unknown	unknown	gnl|CDD|223868
NC_014958.1|WP_013556963.1|1948515_1951779_-|isoleucine--tRNA-ligase	unknown	unknown	gnl|CDD|235681
NC_014958.1|WP_013556962.1|1947408_1948182_-|methyltransferase-domain-containing-protein	unknown	unknown	gnl|CDD|226591
NC_014958.1|WP_013556974.1|1961735_1962383_-|chloramphenicol-acetyltransferase	unknown	unknown	gnl|CDD|215002
NC_014958.1|WP_013556977.1|1964402_1965197_-|Cof-type-HAD-IIB-family-hydrolase	unknown	unknown	gnl|CDD|272905
NC_014958.1|WP_013556958.1|1941402_1943175_-|malto-oligosyltrehalose-trehalohydrolase	unknown	unknown	gnl|CDD|274114
NC_014958.1|WP_169311935.1|1946306_1947275_-|aliphatic-sulfonate-ABC-transporter-substrate-binding-protein	unknown	unknown	gnl|CDD|270271
NC_014958.1|WP_148235061.1|1962494_1963892_+|aspartate-kinase	unknown	unknown	gnl|CDD|235773
NC_014958.1|WP_013556965.1|1953008_1953686_+|fructose-6-phosphate-aldolase	unknown	unknown	gnl|CDD|234947
NC_014958.1|WP_013556959.1|1943362_1945471_-|glycogen-debranching-protein-GlgX	unknown	unknown	gnl|CDD|131155
NC_014958.1|WP_013556966.1|1953682_1954966_+|transcription-termination-factor-Rho	unknown	unknown	gnl|CDD|236490
NC_014958.1|WP_013556956.1|1937763_1938456_-|Bax-inhibitor-1/YccA-family-protein	unknown	unknown	gnl|CDD|198414
NC_014958.1|WP_013556964.1|1952143_1952887_-|type-I-methionyl-aminopeptidase	unknown	unknown	gnl|CDD|238519
NC_014958.1|WP_013556971.1|1958570_1959326_-|triose-phosphate-isomerase	unknown	unknown	gnl|CDD|234589
NC_014958.1|WP_013556968.1|1956455_1956815_+|response-regulator	unknown	unknown	gnl|CDD|381116
NC_014958.1|WP_013556978.1|1965248_1965977_-|TIGR00730-family-Rossman-fold-protein	unknown	unknown	gnl|CDD|129813
NC_014958.1|WP_013556973.1|1960605_1961601_-|type-I-glyceraldehyde-3-phosphate-dehydrogenase	unknown	unknown	gnl|CDD|223135
NC_014958.1|WP_013556970.1|1957403_1958447_-|aminopeptidase-P-family-protein	unknown	unknown	gnl|CDD|223085
NC_014958.1|WP_013556957.1|1938580_1941406_-|malto-oligosyltrehalose-synthase	unknown	unknown	gnl|CDD|237740

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
NC_014958.1|WP_013556972.1|1959322_1960489_-|phosphoglycerate-kinase	gnl|CDD|234613	PRK00073, pgk, phosphoglycerate kinase; Provisional.	0
NC_014958.1|WP_013556969.1|1956876_1957407_-|septal-ring-lytic-transglycosylase-RlpA-family-protein	gnl|CDD|223868	COG0797, RlpA, Lipoproteins [Cell envelope biogenesis, outer membrane].	6.37761e-27
NC_014958.1|WP_013556963.1|1948515_1951779_-|isoleucine--tRNA-ligase	gnl|CDD|235681	PRK06039, ileS, isoleucyl-tRNA synthetase; Reviewed.	0
NC_014958.1|WP_013556962.1|1947408_1948182_-|methyltransferase-domain-containing-protein	gnl|CDD|226591	COG4106, Tam, Trans-aconitate methyltransferase [General function prediction only].	1.65775e-90
NC_014958.1|WP_013556974.1|1961735_1962383_-|chloramphenicol-acetyltransferase	gnl|CDD|215002	smart01059, CAT, Chloramphenicol acetyltransferase. Chloramphenicol acetyltransferase (CAT).catalyzes the acetyl-CoA dependent acetylation of chloramphenicol (Cm), an antibiotic which inhibits prokaryotic peptidyltransferase activity. Acetylation of Cm by CAT inactivates the antibiotic. A histidine residue, located in the C-terminal section of the enzyme, plays a central role in its catalytic mechanism. There is a second family of CAT. evolutionary unrelated to the main family described above. These CAT belong to the bacterial hexapeptide-repeat containing-transferases family (see ). The crystal structure of the type III enzyme from Escherichia coli with chloramphenicol bound has been determined. CAT is a trimer of identical subunits (monomer Mr 25,000) and the trimeric structure is stabilised by a number of hydrogen bonds, some of which result in the extension of a beta-sheet across the subunit interface. Chloramphenicol binds in a deep pocket located at the boundary between adjacent subunits of the trimer, such that the majority of residues forming the binding pocket belong to one subunit while the catalytically essential histidine belongs to the adjacent subunit. His195 is appropriately positioned to act as a general base catalyst in the reaction, and the required tautomeric stabilisation is provided by an unusual interaction with a main-chain carbonyl oxygen.	9.19484e-77
NC_014958.1|WP_013556977.1|1964402_1965197_-|Cof-type-HAD-IIB-family-hydrolase	gnl|CDD|272905	TIGR00099, Uncharacterized_protein_MCAP_0867, Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily. This subfamily of sequences falls within the Class-IIB subfamily (TIGR01484) of the Haloacid Dehalogenase superfamily of aspartate-nucleophile hydrolases. The use of the name "Cof" as an identifier here is arbitrary and refers to the E. coli Cof protein. This subfamily is notable for the large number of recent paralogs in many species. Listeria, for instance, has 12, Clostridium, Lactococcus and Streptococcus pneumoniae have 8 each, Enterococcus and Salmonella have 7 each, and Bacillus subtilus, Mycoplasma, Staphylococcus and E. coli have 6 each. This high degree of gene duplication is limited to the gamma proteobacteria and low-GC gram positive lineages. The profusion of genes in this subfamily is not coupled with a high degree of divergence, so it is impossible to determine an accurate phylogeny at the equivalog level. Considering the relationship of this subfamily to the other known members of the HAD-IIB subfamily (TIGR01484), sucrose and trehalose phosphatases and phosphomannomutase, it seems a reasonable hypothesis that these enzymes act on phosphorylated sugars. Possibly the diversification of genes in this subfamily represents the diverse sugars and polysaccharides that various bacteria find in their biological niches. The members of this subfamily are restricted almost exclusively to bacteria (one sequences from S. pombe scores above trusted, while another is between trusted and noise). It is notable that no archaea are found in this group, the closest relations to the archaea found here being two Deinococcus sequences. [Unknown function, Enzymes of unknown specificity].	1.56989e-60
NC_014958.1|WP_013556958.1|1941402_1943175_-|malto-oligosyltrehalose-trehalohydrolase	gnl|CDD|274114	TIGR02402, Malto-oligosyltrehalose_trehalohydrolase, malto-oligosyltrehalose trehalohydrolase. Members of this family are the trehalose biosynthetic enzyme malto-oligosyltrehalose trehalohydrolase, formally known as 4-alpha-D-{(1->4)-alpha-D-glucano}trehalose trehalohydrolase (EC 3.2.1.141). It is the TreZ protein of the TreYZ pathway for trehalose biosynthesis, and alternative to the OtsAB system. [Energy metabolism, Biosynthesis and degradation of polysaccharides].	0
NC_014958.1|WP_169311935.1|1946306_1947275_-|aliphatic-sulfonate-ABC-transporter-substrate-binding-protein	gnl|CDD|270271	cd13553, PBP2_NrtA_CpmA_like, Substrate binding domain of ABC-type nitrate/bicarbonate transporters, a member of the type 2 periplasmic binding fold superfamily. This subfamily includes nitrate (NrtA) and bicarbonate (CmpA) receptors. These domains are found in eubacterial perisplamic-binding proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding their ligand with high affinity, they 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. These binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.	5.83303e-68
NC_014958.1|WP_148235061.1|1962494_1963892_+|aspartate-kinase	gnl|CDD|235773	PRK06291, PRK06291, aspartate kinase; Provisional.	0
NC_014958.1|WP_013556965.1|1953008_1953686_+|fructose-6-phosphate-aldolase	gnl|CDD|234947	PRK01362, PRK01362, fructose-6-phosphate aldolase.	1.05752e-142
NC_014958.1|WP_013556959.1|1943362_1945471_-|glycogen-debranching-protein-GlgX	gnl|CDD|131155	TIGR02100, Glycogen_operon_protein_GlgX_homolog, glycogen debranching enzyme GlgX. This family consists of the GlgX protein from the E. coli glycogen operon and probable equivalogs from other prokaryotic species. GlgX is not required for glycogen biosynthesis, but instead acts as a debranching enzyme for glycogen catabolism. This model distinguishes GlgX from pullanases and other related proteins that also operate on alpha-1,6-glycosidic linkages. In the wide band between the trusted and noise cutoffs are functionally similar enzymes, mostly from plants, that act similarly but usually are termed isoamylase. [Energy metabolism, Biosynthesis and degradation of polysaccharides].	0
NC_014958.1|WP_013556966.1|1953682_1954966_+|transcription-termination-factor-Rho	gnl|CDD|236490	PRK09376, rho, transcription termination factor Rho; Provisional.	0
NC_014958.1|WP_013556956.1|1937763_1938456_-|Bax-inhibitor-1/YccA-family-protein	gnl|CDD|198414	cd10432, BI-1-like_bacterial, Bacterial BAX inhibitor (BI)-1/YccA-like proteins. This family is comprised of bacterial relatives of the mammalian members of the BAX inhibitor (BI)-1 like family of small transmembrane proteins, which have been shown to have an antiapoptotic effect either by stimulating the antiapoptotic function of Bcl-2, a well-characterized oncogene, or by inhibiting the proapoptotic effect of Bax, another member of the Bcl-2 family. In plants, BI-1 like proteins play a role in pathogen resistance. A characterized prokaryotic member, Escherichia coli YccA, has been shown to interact with ATP-dependent protease FtsH, which degrades abnormal membrane proteins as part of a quality control mechanism to keep the integrity of biological membranes.	2.06145e-59
NC_014958.1|WP_013556964.1|1952143_1952887_-|type-I-methionyl-aminopeptidase	gnl|CDD|238519	cd01086, MetAP1, Methionine Aminopeptidase 1. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and Peptidase M. Catalyzes release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.	3.09519e-95
NC_014958.1|WP_013556971.1|1958570_1959326_-|triose-phosphate-isomerase	gnl|CDD|234589	PRK00042, tpiA, triosephosphate isomerase; Provisional.	5.45837e-129
NC_014958.1|WP_013556968.1|1956455_1956815_+|response-regulator	gnl|CDD|381116	cd17574, REC_OmpR, phosphoacceptor receiver (REC) domain of OmpR family response regulators. OmpR-like proteins are one of the most widespread transcriptional regulators. OmpR family members contain REC and winged helix-turn-helix (wHTH) DNA-binding output effector domain. They are involved in the control of environmental stress tolerance (such as the oxidative, osmotic and acid stress response), motility, virulence, outer membrane biogenesis and other processes. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.	3.15642e-31
NC_014958.1|WP_013556978.1|1965248_1965977_-|TIGR00730-family-Rossman-fold-protein	gnl|CDD|129813	TIGR00730, LOG_family_protein_YJL055W, TIGR00730 family protein. This model represents one branch of a subfamily of proteins of unknown function. Both PSI-BLAST and weak hits by this model show a low level of similarity to and suggest an evolutionary relationship of the subfamily to the DprA/Smf family of DNA-processing proteins involved in chromosomal transformation with foreign DNA. Both Aquifex aeolicus and Mycobacterium leprae have one member in each of two branches of this subfamily, suggesting that the branches may have distinct functions. [Hypothetical proteins, Conserved].	1.1918e-59
NC_014958.1|WP_013556973.1|1960605_1961601_-|type-I-glyceraldehyde-3-phosphate-dehydrogenase	gnl|CDD|223135	COG0057, GapA, Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate transport and metabolism].	5.5091e-174
NC_014958.1|WP_013556970.1|1957403_1958447_-|aminopeptidase-P-family-protein	gnl|CDD|223085	COG0006, PepP, Xaa-Pro aminopeptidase [Amino acid transport and metabolism].	4.67485e-111
NC_014958.1|WP_013556957.1|1938580_1941406_-|malto-oligosyltrehalose-synthase	gnl|CDD|237740	PRK14511, PRK14511, malto-oligosyltrehalose synthase.	0

Protein sequences

>NC_014958.1|WP_013556966.1|1953682_1954966_+|transcription-termination-factor-Rho
MTEPHLDAEVLPFHELQAKILPELHLIAANLGIENYRKLKKDALSLTILERQADREGQVLARGYLDISPDGYGFLQRDLLDAESRSVLVTAGIIKQYHLRTGDEVIGRARKPRENERYGTLTRVEAVNGMDPITASRRPRFDDLTPTFPDDQLVLEDPTMDDGLSLRVVDLLVPIGKGQRGLIVAPPKAGKTTLLKKVANSIVKNYPNITVMVLLVDERPEEVTDFRESVQGAQVIASTFDEPPANHVRVAEFVHERARRIVEEGGDVVILLDSITRLARANNLVTPPTGRTLSGGLDSNALHWPKRFLGAARNIRGGGSLTILATALVETGSRMDDVIFEEFKGTGNMELILSRRLEERRIFPAMDILKSGTRREDLLLDGNVMQKMWLLRKVISDMDPADAMDMLLTRMGKTANNMEFLSTLTGR
>NC_014958.1|WP_013556965.1|1953008_1953686_+|fructose-6-phosphate-aldolase
MKFFIDTAVVDEIREIHAWGVLAGVTTNPSLVVASGRDFKEVVQEIAQLVQGPTSAEVTALDAEGMINEGREVATWSEHVIVKLPLTPAGLQACKVLTSEGIKTNVTLCFNVPQALLAARAGATYISPFAGRVDDIGWDGIELIRQIKEAYVMGDIQTQVLAASVRHPQHVVQSALAGADVATIPYKVFKQMIKHPLTDAGLEGFMKDWATRAKVAESTKGSDAK
>NC_014958.1|WP_013556964.1|1952143_1952887_-|type-I-methionyl-aminopeptidase
MTITNERELQGMRRAGQVVADTLRALREALEPGVTPAELDALAGQVFARHGAQSAPRLTYDAPVNVFISVNDDAVHGLPTTRPLQAGDVVSFDVTPSVDGFIADAAVTVAVPPASPVALQLIACAEAAFDAAMRVARAGQPVNAIGRAVDTEVRRRGFTVLRELTGHGVGRALHEQPDVPNFPHPGARSRLHEGLVLAVEPIISSGRAWRTATRRDGWTICTRDGGLAAHHEHTVMITRGRPVILTA
>NC_014958.1|WP_013556963.1|1948515_1951779_-|isoleucine--tRNA-ligase
MTLFTPVNSQPRFKDLEADIQNLWQTQRVFERTQERREGQPEFVFYEGPPTANGKPALHHVLARSFKDLFPRYKVMQGYHVTRKGGWDTHGLPVEISVEKKLGLQGRNHGASREELEEFNRLCRTSVWETIQDWNTFTQRLGYWVDLQDAYITYENDYIETVWNLLKRLHAKGLVVQDYKVVPLSPRISTTLSRAELGEVDSYREVDDPSVYVRFPVIWSSLPERALAVLGGLNEEDRASLALVVWTTTPWTLPSNTLAAVNADLTYVAARSPMGTVIIAEDAVERLSSLLKDTPPLEVLATFKGADLEWVEYEPPFPEVAVELGAVQALHERGDDGRPVMHFVTLAEFVSAADGSGVAHEAPAYGAEDLELARKYGVPLMFGVDDHGVLQVTTERGKFFKDADKGLIADLKERGLMYRSGTLRHRYPFHDRTGDPILYFAKKSWYIRTNAMAERMVEENQKINWVPANIKNGRFGNWLEGNVDWAISRERYWGTPLPFWVSEDGDLIVVGSVQELSALTGRDLTDLDLHRPYIDDITFEQDGKVYRRVPEVLDVWFDSGSMPYAQWHLLTDETGARALPGAEANKAQFERHYPADFISEAIDQTRGWFYSLHAISTMLYGQPAYRNVICLGHIVDEKGAKMSKSKGNVIEPIPMFDKYGADSVRWYMFTASDPGDQKRFSERLVAEAQRNYVNTLWNVYAFFVLYANLDRPNLADAPAVADRPEIDRWLLARLEETVRDVTSALDAYDARGGGRALERFVSDLSNWYVRRNRSRFWGAGGSVDTSAYATLHEALLVVSQLTAPFTPFLADALYGNLVAALPGEHPASVHLTRWPQVRPERLNAQLTAEMAAVLKVVDLGRAVRGQHNLKTRQPLAGVTVRASTAELTAALARFETQIKEELNVKSVNLLDQYTDLVQYSLRPNLPVIGKVYGKDLPKVRAALAGADAALVARAVRDGQPFTVEADGALFELTGDQVLVDASAPEGLAAAEDGGFLVAFDTQLTRELVLEGLARDVVRGVQEARKAAGFEVQDRIRVAFDLSGDAREAAEAWQAYIAEETLAEAVSFEAGDGFEATVEGGRVFLTRV
>NC_014958.1|WP_013556962.1|1947408_1948182_-|methyltransferase-domain-containing-protein
MAWNPDQYHRFRDARDAPARDLLQLLPEAPYRAIIDLGCGTGDHTATLAQQHPDAQVTGLDSSAEMLERARTHHQPNLHFTLGAIQALHGTYDLIFSNAALQWLPDHAALLAGLWTHLRPGGTLAVQVPSNHSHDSHRLLGETADDFREALGGFTRFGPVQGASPVLTPARYAELLDTLGAANVTALEKVYPVVLPGAEGVLDWVRGTALVPYLSRLDEATGAAFLEAYRARLRARWPGDRVYYAFTRVLFVAQKPA
>NC_014958.1|WP_169311935.1|1946306_1947275_-|aliphatic-sulfonate-ABC-transporter-substrate-binding-protein
MRLLLPLTLLLTLGAANAQSATTLRLGVFPNVTHAAGLVGIKQGLFQKQLGNVKLQVKEFANGSQVNEAFAAGAIDAAYVGPGPVMNAFMRGVPIQVISGAASAGAVLVGRGDLKLRGVTALAGRKVAVPTRGSTQDISLRHLLHVNGLKASDEGGNVTIVPIDPANMPAAFASKQVDAALVQEPWGAVLEAQGAKLLVNEKGIWNGGDYTTTVLVVNTQYAKKNPEAVKDLLRGHLAAINFIRGSNAGAQKAISDQIYAFTGQRPDRDTLFKGLARTKITWDINLKTLGEYAQLNKEAGFARDVPDLARFVDLDLVRSLAK
>NC_014958.1|WP_013556959.1|1943362_1945471_-|glycogen-debranching-protein-GlgX
MNVRHGQPYPLGATFDGEGVNFALFSENARNVELCLFDDQNNETRIPVRENTAFVWHVYVPGLQPGQRYGYRVHGEYAPERGLRFNPNVVLMDPYAKALDGTERFDQGVFAYVMGEDDLVMQTEEQRGAPLGIVIDPHSFDWEGDHQPNCSFHQSVIYEAHVKGLTMLHPDVPEDLRGTYAGVATEPVLTYLKDLGITAIEFMPVHQHVDDPFLLDKGLSNYWGYSTLNFFAPDVRYSAYEKRGERGGAVREFQEMVKALHRAGIEVILDVVYNHTAEGNHMGPTLSYKGIDNPTYYRLVDGDERHYFDYTGTGNSLNVRHPQTLQLIMDSLRYWVQVMHVDGFRFDLASTLARGLHEVDQLSSFFTIIHQDPIISQVKLIAEPWDVGEGGYQVGNFPVKWAEWNGIYRDAMRAFWKGEGGLASEIGYRLTGSSDLYQSDGRKPYASINFITAHDGFTLRDTVSYNDKHNEANGENNQDGHNDNQSWNCGVEGETDDAEVNALRARQQRNFLATLFLSQGTPMMLGGDEFGRSQRGNNNAYCQDNEISWFHWDQVDEALLRYTRKLIGLRREHPALHRRKFFSGRPIRGSEERDIMWLRHDGQDMTDEDWQNPNTQSLGMFLGGRGLNDTTADGKPILDDDLLILLNASHVDLPFVLPEFGSGGPWTLLLDTADDDAGGDQPVGEATTLAGRSMKLFRRASA
>NC_014958.1|WP_013556958.1|1941402_1943175_-|malto-oligosyltrehalose-trehalohydrolase
MTDTQSASSAAKPGLAPQLGAHLVPGGTRFRAWVTTTDDVAVRVNGDTHRMAPVGDDVYEVALPVGAGARYSFVLNGQVTPDPYARFMPDGVHADAEVIDPAFTWQHADFPGVSAEACVLYELHVGTFTPEGTYRAAMAKLPYLRDLGVTAIELMPLAAFPGERGWGYDGVMLYAPFAPYGRPEDLKAFIDAAHGHGLAVLNDVVYNHFGPDGNYLHAYSDRYFTDRFHTPWGQGLDYREPHMRRLILDNARMWLQEYRFDGLRLDATHEIHDDSPTHLLRELAREVRAMRGQHLLFAEDPRNLPALVTEDELTGVWADDFHHTVRVTLTGEHEGYYAPYAGGAAAIAHVINRGWSFEGQPWPLNDEPRGAPADALGAPSFVYTLQNHDQIGNRPTGDRLHHREDVTPAQYRAASLLLLTLPMTPLLFQGQEWAASTPFQYFTDHHGELGALVSEGRRREFQHFEGFAGGDVPDPQAAATFLNSTLNWAELDEGEHARTRALYRAALGLRRSDPVLRSPSRDTLHARADGDVLIVRRADEHGTRVLVWNLGGGPVDARTHADGGEIRLHSEARDDSTLQPGEAALLAVSA
>NC_014958.1|WP_013556957.1|1938580_1941406_-|malto-oligosyltrehalose-synthase
MTAPAEQAARIPRATYRLQLHAGFNFDAARRALPYLERLGVSDVYLSPIWQAAPGSTHGYNVTDHARVSDELGGERAFTRLARDARARGLGVLVDFVPNHMGVEGGANPYWEDVLEHGQASRYAHFFDIDWNPLRRGLQNRVLLPTLGDQYGRVLERNELQVTRTGGRLFLAYWERKLPLSPRTLAPLLTRAGALLTLGADDPSRLELASVALQAAHLPGATDALAREDRVMRAQEALVMRRRLEGLTEAAPEVGRALDAAITELNADPVKLDALISEQNYRLAYWRVAAEEINYRRFFDINDLAALRMEDPDVFDWAHSALLRLLGDGLITGVRLDHTDGLYDPRGYFEALQDRARAALGAAEADDKPLYVVAEKILEPGEALPASWAIHGTTGYDFLAQLNGVFVNERAERDFTRAFRWFTGAEASYGETLHSTKHLIQRVSLSSEVNVLAEHLLRIAEADLRSRDFTLSSLRDAIREVIAAFPVYRSYVREDGSREPGDDAHIRAAVRDARRLNRDLDPTVLQYLEDVLLLRAPDEAHRAAYAGFALRFQQLTGPVTAKGAEDTAFYRYVRLVALNEVGGDPALFGTSLNAFHKETRGRADAWPHAMLATSTHDTKRGEDTRARLTALTEMPQVWADAIETLSDVGEEYARDLGGVRAPSRADEYAFYQNALGAWTGVTDEAFVGRMVDYMLKAAREAKVHTSWAQQDEAYEGALTDFVRGLLADERAVGVLRDLHERTRVAGASNGLAATLVRLTAPGVPDTYQGSEGWNLSLVDPDNRRPVPYPALGRTLTRIEREAARNALKLAQTLLRDFMTGDVKLLVTWAALQARRAHPELFMHGTYTPITAGRHVLAFARTHGAQVAVTVTPRLTALLTRDPHAWAVGAAWGSRTLPLPSAGVYVNVLTGERHRARGREPRLPLAALLRTFPLALLIRQDT
>NC_014958.1|WP_013556956.1|1937763_1938456_-|Bax-inhibitor-1/YccA-family-protein
MNQYPPSTLSARSESVVRSFIGRTYSWMTAGLALTAAIAYFVGRNPDLMVSIGRSGFLLPLVQLGIVMFLSFLAPRVSATVAGLLFMAYSAVTGLTFGVIFQFYTASDVTAAFLTTAGTFGAMSAFGFLTRRNLAPMGTFLMFALIGLIIASIVNIFIGGSTLNLIISAVGVLLFAGLTAYDTQMLRNMALQGFGDAHTQEKGAIYGALTLYLNFINMFLFILRLFSSRD
>NC_014958.1|WP_013556968.1|1956455_1956815_+|response-regulator
MSAPHLLLVDDERQILELLELTLTMNGFMVSTAQSGAEAVDLAAQRHFDLILLDVVMTPCDGFETARQLRARPGCPPIVFLTGLGGDDERQRGLDLGAAYLVKPFRPAQLLDTIRATLA
>NC_014958.1|WP_013556969.1|1956876_1957407_-|septal-ring-lytic-transglycosylase-RlpA-family-protein
MRLPRAAVLAVLLTAGAATADSVTVQPGDTLWSIARRAGVSVTDLQAWNDLPGDTIRVGMTLTVNGAAPVPSVPAATATARSAPTADWAPAGRGQAVYYGGRADAETTMTAAHPTLPFGTWVRVTHERTGQSVLVKINDRGPFGNSARVIDLSISAARALGMLSEGVAPVRLDVRR
>NC_014958.1|WP_013556970.1|1957403_1958447_-|aminopeptidase-P-family-protein
MPEFAAALTRAGVDALWVSRPENVRYVTGFTSPEDGKALLTPQGAVLYTDARYTEQARLESSAEQFIARPPATLEHAAERVRGLRVGFEADALTVAALDDLRRFWPDATLVPTTGILETLRLIKTPDEIERIRQAQRIADEAFAAVRPLIRAGAVERDIEFAIEGEMRKRGARGWAHGFIVAGGERGALPHGHASDRVLQDGELVTVDIGAVYDGYVSDMTRTVRVGEVSAELRRIYHAVLEAEEAAIRAVRPGVRAADLDTLARDILTGHGLGEAFAHSLGHGVGLAVHEGPSLRGTSDDVLEPGMVITIEPGAYLPGLGGVRIEDLVLVTEDGYEVLSTSPKEPV
>NC_014958.1|WP_013556971.1|1958570_1959326_-|triose-phosphate-isomerase
MSTPRTLLALNWKMNKTPTEAGEWAKALQEELPQTDAELVVCAPAVTLSLVAAHLYGSGAGLGAQDVSAHESGAYTGETSAAMLKDVGAAYVIVGHSERRTYHGETDAVVAAKARKALEHGLTPIVCVGEGLDVREAGEHVPYTLAQLRSSLEGVQPGSAEQLVIAYEPVWAIGTGRTATSADAEELAAAIRGALREVYPDFADGVRVLYGGSVKPDNIADICAQPNVNGALVGGAALDLRSVLSMVEALA
>NC_014958.1|WP_013556972.1|1959322_1960489_-|phosphoglycerate-kinase
MQTLDALNVQGKRVLVRVDYNVPLKDGVIQDDTRIQASLPTLKRLLDGGASLVLMSHLGRPKNGPEAKYSLEPVAARLEQLLQVPVHFVHALPSSEEALKEVRELQPGQVALLENVRFEAGEEKNDAQLVQALARLGDAFVLDAFGSAHRAHASVSGVAAALPHAGGLLLQAEVNALDRLLNDPQQPYVVIIGGAKVSDKIKVIENLLPKVDRMLIGGGMAFTFIKARGGQIGNSLHEADQLDLARRLLDEHGERLLLPVDVVAADRFAEDAATQVVPADAIPDGWMGLDIGPDTQQAYAQALSGAKTVFWNGPMGVFEMAAFANGTNAVARAVADLQGAYTVVGGGDSVSAINKSGLADQVSHVSTGGGASLELLEGQQLPGVEAMR
>NC_014958.1|WP_013556973.1|1960605_1961601_-|type-I-glyceraldehyde-3-phosphate-dehydrogenase
MKVGINGFGRIGRLVFRILTARGVDVVAINDLTDNKTLATLLKYDSTAGKFDGTVEYDESSLTVNGKQIQALAERDPANIKWGELGVDVVIESTGIFTSREGASKHLQGGAKKVIITAPAKGEDFSVVLGVNEQDYDPKNHHIISNASCTTNSLGAPMKLLDEAFGIEKAIMTTVHSYTNDQRVLDLPHSDLRRARAAAVNIIPTSTGAAKAVSQVYPALKGKFDGTSLRVPTPVGSISDVVVILGREVTVDEVNAVFKNAAEGSHKGIIAYTEDPIVLADIVGDSHSAIIDGGLTMAMGNLVKFFSWYDNEWGYSNRIADLTQLVLEKGN
>NC_014958.1|WP_013556974.1|1961735_1962383_-|chloramphenicol-acetyltransferase
MHEIDLTTWPRRQHYAFFRTLALPYFNLSANVDVTALHAAVKARGASFTAASAYVLTRAANADAFPEFRQRLRGERVVQHDRVSCSVTVLGEGDLFGFCTLPYAPDFAAFAGEARARMARAKTQPSLEEDAAADDLIFITNLPWVAFTSVQHPVPLGPADSFPRLATGRVTVQDGRRVMPLAVQGHHALMDGVHVGRYFLEVQRLLDDADAVLGG
>NC_014958.1|WP_148235061.1|1962494_1963892_+|aspartate-kinase
MKFGGTLMGDPKAIAHSASLAAASVRAGERVVVVVSAMSGVTETLLKIAASAEGGDIAFANDEIAILRSRHFGAAQALGAAPDSDAVREIRELLETLRQTVYGVYLLRELSPRTRDLIVSFGERLSAPLMDVALGGAGVRAHHLTGGAAGLTTDAHFGNARPLPGAYPRIRDRMSGLFEAGLTPVVTGFIGETEDGVITTLGRGGSDYTATILGAALGATEVWTWKDVDGVMSADPRFVPDARNLAHLSYHEVMELAYFGAKVLHPLAVTPLQERGTPLRVKSAADPDFPGTLVTSEAHADAAHPVKAVTAIRGATVLTIEGAGSFGAPDVLVDVFRVLARENLTVLMVSQSSSMSNVSLVIPRASGPHALASLKQEFGRDDRVRDFTLNEHVAVVAIVGEGMRGTKGVAAKLFGALAIEGVNLLMISQGSSELNISCAIDESDVDAALRAAHAAFDLGKERATA
>NC_014958.1|WP_013556977.1|1964402_1965197_-|Cof-type-HAD-IIB-family-hydrolase
MLGLICIDVDGTLVGSGGVIPEVVWRAAEDARERGVHLALCSGRPALAKARAYAQRLDPHGWHVFQNGASIVHVGTGESLSAAFPEDALHRQIQQARATGRLLEVYSDTDMAVEQDVPRARAHADLLGLPFQLRPLDSLPGTVVRTQWVIPIEETDALLAEPHEGLTLHPAGSPVMPDTMFVSVTRAGVDKGSAVRRVAEKLGVAMERVMMVGDGHNDVLAMQVVGHPVAMGNADAEARAAARYTVGHVDDGGLAEAIELAFTL
>NC_014958.1|WP_013556978.1|1965248_1965977_-|TIGR00730-family-Rossman-fold-protein
MTEHESLDNMTRDAWRMLRVLGELAVGFDRLAQLPHPGVTVFGSARTGIRDQYYGLARDLGAHLAASGFAVITGGGPGIMEAANRGAFEAGGVSVGINIILPYEQRPNPYQTISLECEYFHTRKELLAKAARAFVVFPGGFGTLDELAGILTLVQTRKMPAMPVYLVGRAHWAGLEGWFRETLITSGAIADDDLDLFKIVDDVSAIPADIQQYHAGEHAGFKRPTDTDRARARGDVPTSRGG

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity
NC_014958_1	1.3|667491|35|NC_014958|PILER-CR	667491-667525	35	NZ_LT703506	Mycobacterium chimaera strain Mycobacterium chimaera MC045 isolate Mycobacterium chimaera plasmid 2	175652-175686	6	0.829
NC_014958_1	1.1|667386|35|NC_014958|PILER-CR	667386-667420	35	NZ_CP041044	Paracoccus sp. AK26 plasmid pAK2, complete sequence	45804-45838	10	0.714
NC_014958_1	1.2|667437|38|NC_014958|PILER-CR	667437-667474	38	NC_016110	Streptomyces pratensis ATCC 33331 plasmid pSFLA01, complete sequence	160508-160545	10	0.737
NC_014958_1	1.3|667491|35|NC_014958|PILER-CR	667491-667525	35	NZ_CP016083	Streptomyces sp. SAT1 plasmid unnamed3, complete sequence	506311-506345	10	0.714
NC_014958_1	1.1|667386|35|NC_014958|PILER-CR	667386-667420	35	NZ_CP029830	Azospirillum ramasamyi strain M2T2B2 plasmid unnamed1, complete sequence	382606-382640	12	0.657

1. spacer 1.3|667491|35|NC_014958|PILER-CR matches to NZ_LT703506 (Mycobacterium chimaera strain Mycobacterium chimaera MC045 isolate Mycobacterium chimaera plasmid 2) position: , mismatch: 6, identity: 0.829

gtccgcctccacgacgcgcacccgctgaccgcgca-	CRISPR spacer
ctcggcctccaccacgcgcacccgct-cccgcgccg	Protospacer
 ** ******** *************  ******  

2. spacer 1.1|667386|35|NC_014958|PILER-CR matches to NZ_CP041044 (Paracoccus sp. AK26 plasmid pAK2, complete sequence) position: , mismatch: 10, identity: 0.714

gccaccctgcgcgacaccggcagcctcatcgccag	CRISPR spacer
ggcaccctgctcgacaccggccgcctcgatccgca	Protospacer
* ******** ********** *****. . *  .

3. spacer 1.2|667437|38|NC_014958|PILER-CR matches to NC_016110 (Streptomyces pratensis ATCC 33331 plasmid pSFLA01, complete sequence) position: , mismatch: 10, identity: 0.737

ctcaccgcgcacaacacccacgggcccgcccgcatcac	CRISPR spacer
atcaccccgcacagcacccacgggcccggggggcgcgc	Protospacer
 ***** ******.**************   *   *.*

4. spacer 1.3|667491|35|NC_014958|PILER-CR matches to NZ_CP016083 (Streptomyces sp. SAT1 plasmid unnamed3, complete sequence) position: , mismatch: 10, identity: 0.714

gtccgcctccacgacgcgcacccgctgaccgcgca	CRISPR spacer
ctcggccgccacgacgcgcacccgctcggtgcctc	Protospacer
 ** *** ****************** . .** . 

5. spacer 1.1|667386|35|NC_014958|PILER-CR matches to NZ_CP029830 (Azospirillum ramasamyi strain M2T2B2 plasmid unnamed1, complete sequence) position: , mismatch: 12, identity: 0.657

gccaccctgcgcgacaccggcagcctcatcgccag	CRISPR spacer
ctggtgctgtgcgacaccgccagcctcatcggtcc	Protospacer
 . .. ***.********* *********** .