CRISPRimmunity

Please click to download your results

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_013729	Kribbella flavida DSM 17836, complete sequence	8 crisprs	c2c9_V-U4,WYL,csa3,DEDDh,cas4,DinG,cas3	0	5	1	0

Results visualization

Click the left colored region to show detailed information

CRISPR-Cas detection and classification

Crispr_ID: NC_013729_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NC_013729_1

273276-273373

Orphan

Consensus_repeat	Method
GCGGGTCGGTGAGACAGCGGGCGG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NC_013729_1

>merge|NC_013729|1|273276-273373|CRISPRCasFinder
GCGGTTCGGTGAGACAGCGGCGGAGGGGGTCAGCCGGGGCGGGTCGGTGAGACAGCGGGCGGATGGCAGCCGGAGCGGGCCGGTGAGACAGCCGGGCG

>NC_013729|1|1|273276-273373|CRISPRCasFinder
GCGGTTCGGTGAGACAGCGGCGGA	GGGGGTCAGCCGGGGCGGGTCGGTGAGACAGCGGGCGGATGGCAGCCGGA
GCGGGCCGGTGAGACAGCCGGGCG

Protein	Signature genes	Signature genes Name	Protein_function
NC_013729.1\|WP_012917940.1\|260867_261959_+\|rhamnose-ABC-transporter-substrate-binding-protein	unknown	unknown	gnl\|CDD\|380655
NC_013729.1\|WP_012917954.1\|278586_279330_-\|MBL-fold-metallo-hydrolase	unknown	unknown	gnl\|CDD\|293802
NC_013729.1\|WP_041289682.1\|279326_280271_-\|prolyl-oligopeptidase-family-serine-peptidase	unknown	unknown	gnl\|CDD\|368448
NC_013729.1\|WP_012917953.1\|277598_278465_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|214906
NC_013729.1\|WP_012917943.1\|263477_265517_+\|bifunctional-rhamnulose-1-phosphate-aldolase/short-chain-dehydrogenase	unknown	unknown	gnl\|CDD\|236241
NC_013729.1\|WP_012917947.1\|269043_272241_+\|family-78-glycoside-hydrolase-catalytic-domain	unknown	unknown	gnl\|CDD\|379971
NC_013729.1\|WP_012917942.1\|262317_263481_+\|L-rhamnose-isomerase	unknown	unknown	gnl\|CDD\|274239
NC_013729.1\|WP_012917952.1\|276092_277364_-\|threonine-ammonia-lyase-IlvA	unknown	unknown	gnl\|CDD\|236318
NC_013729.1\|WP_012917949.1\|273475_274144_-\|response-regulator-transcription-factor	unknown	unknown	gnl\|CDD\|223816
NC_013729.1\|WP_012917948.1\|272387_273161_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|237171
NC_013729.1\|WP_041289678.1\|267083_268520_+\|rhamnulokinase	unknown	unknown	gnl\|CDD\|198349
NC_013729.1\|WP_148256833.1\|280332_280719_-\|hypothetical-protein	unknown	unknown	unknown
NC_013729.1\|WP_012917939.1\|259821_260841_+\|ABC-transporter-permease	unknown	unknown	gnl\|CDD\|119321
NC_013729.1\|WP_012917958.1\|282931_283825_-\|LLM-class-flavin-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|366009
NC_013729.1\|WP_012917946.1\|268524_268851_+\|LuxR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|225107
NC_013729.1\|WP_012917941.1\|261977_262313_+\|L-rhamnose-mutarotase	unknown	unknown	gnl\|CDD\|377501
NC_013729.1\|WP_012917944.1\|265547_267011_+\|L-fucose/L-arabinose-isomerase-family-protein	unknown	unknown	gnl\|CDD\|238323
NC_013729.1\|WP_012917950.1\|274140_275559_-\|HAMP-domain-containing-histidine-kinase	unknown	unknown	gnl\|CDD\|223715
NC_013729.1\|WP_148256834.1\|280846_282310_-\|LytR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224235
NC_013729.1\|WP_012917951.1\|275697_276027_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|237864

Protein	Function_ID	Function_description	E-value
NC_013729.1\|WP_012917940.1\|260867_261959_+\|rhamnose-ABC-transporter-substrate-binding-protein	gnl\|CDD\|380655	cd20000, PBP1_ABC_rhamnose, rhamnose ABC transporter substrate-binding protein. Rhamnose ABC transporter substrate-binding protein similar to periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling.	6.94079e-165
NC_013729.1\|WP_012917954.1\|278586_279330_-\|MBL-fold-metallo-hydrolase	gnl\|CDD\|293802	cd07716, RNaseZ_short-form-like_MBL-fold, uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase domain. The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme. Only the short form exists in bacteria. Members of this bacterial subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.	1.12254e-65
NC_013729.1\|WP_041289682.1\|279326_280271_-\|prolyl-oligopeptidase-family-serine-peptidase	gnl\|CDD\|368448	pfam05448, AXE1, Acetyl xylan esterase (AXE1). This family consists of several bacterial acetyl xylan esterase proteins. Acetyl xylan esterases are enzymes that hydrolyze the ester linkages of the acetyl groups in position 2 and/or 3 of the xylose moieties of natural acetylated xylan from hardwood. These enzymes are one of the accessory enzymes which are part of the xylanolytic system, together with xylanases, beta-xylosidases, alpha-arabinofuranosidases and methylglucuronidases; these are all required for the complete hydrolysis of xylan.	2.48263e-118
NC_013729.1\|WP_012917953.1\|277598_278465_+\|hypothetical-protein	gnl\|CDD\|214906	smart00910, HIRAN, The HIRAN protein (HIP116, Rad5p N-terminal) is found in the N-terminal regions of the SWI2/SNF2 proteins typified by HIP116 and Rad5p. HIRAN is found as a standalone protein in several bacteria and prophages, or fused to other catalytic domains, such as a nuclease of the restriction endonuclease fold and TDP1-like DNA phosphoesterases, in the eukaryotes. It has been predicted that this protein functions as a DNA-binding domain that probably recognises features associated with damaged DNA or stalled replication forks.	2.77686e-06
NC_013729.1\|WP_012917943.1\|263477_265517_+\|bifunctional-rhamnulose-1-phosphate-aldolase/short-chain-dehydrogenase	gnl\|CDD\|236241	PRK08324, PRK08324, bifunctional aldolase/short-chain dehydrogenase.	0
NC_013729.1\|WP_012917947.1\|269043_272241_+\|family-78-glycoside-hydrolase-catalytic-domain	gnl\|CDD\|379971	pfam17389, Bac_rhamnosid6H, Bacterial alpha-L-rhamnosidase 6 hairpin glycosidase domain. This family consists of bacterial rhamnosidase A and B enzymes. L-Rhamnose is abundant in biomass as a common constituent of glycolipids and glycosides, such as plant pigments, pectic polysaccharides, gums or biosurfactants. Some rhamnosides are important bioactive compounds. For example, terpenyl glycosides, the glycosidic precursor of aromatic terpenoids, act as important flavouring substances in grapes. Other rhamnosides act as cytotoxic rhamnosylated terpenoids, as signal substances in plants or play a role in the antigenicity of pathogenic bacteria.	3.87142e-134
NC_013729.1\|WP_012917942.1\|262317_263481_+\|L-rhamnose-isomerase	gnl\|CDD\|274239	TIGR02635, putative_xylose_isomerase, L-rhamnose isomerase, Streptomyces subtype. This clade of sequences is closely related to the L-rhamnose isomerases found in Pseudomonas stutzeri and in a number of the Rhizobiales (TIGR02629). The genes of the family represented here are found in similar genomic contexts which contain genes apparently involved in rhamnose catabolism such as rhamnulose-1-phosphate aldolase (TIGR02632), sugar kinases, and sugar transporters. [Energy metabolism, Sugars].	0
NC_013729.1\|WP_012917952.1\|276092_277364_-\|threonine-ammonia-lyase-IlvA	gnl\|CDD\|236318	PRK08639, PRK08639, threonine dehydratase; Validated.	0
NC_013729.1\|WP_012917949.1\|273475_274144_-\|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].	1.56822e-83
NC_013729.1\|WP_012917948.1\|272387_273161_+\|hypothetical-protein	gnl\|CDD\|237171	PRK12678, PRK12678, transcription termination factor Rho; Provisional.	1.03214e-07
NC_013729.1\|WP_041289678.1\|267083_268520_+\|rhamnulokinase	gnl\|CDD\|198349	cd07771, FGGY_RhuK, L-rhamnulose kinases; a subfamily of the FGGY family of carbohydrate kinases. This subfamily is predominantly composed of bacterial L-rhamnulose kinases (RhuK, also known as rhamnulokinase; EC 2.7.1.5), which are encoded by the rhaB gene and catalyze the ATP-dependent phosphorylation of L-rhamnulose to produce L-rhamnulose-1-phosphate and ADP. Some uncharacterized homologous sequences are also included in this subfamily. The prototypical member of this subfamily is Escherichia coli RhuK, which exists as a monomer composed of two large domains. The ATP binding site is located in the cleft between the two domains. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The presence of divalent Mg2+ or Mn2+ is required for catalysis. Although an intramolecular disulfide bridge is present in Rhuk, disulfide formation is not important to the regulation of RhuK enzymatic activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases.	0
NC_013729.1\|WP_012917939.1\|259821_260841_+\|ABC-transporter-permease	gnl\|CDD\|119321	cd06579, TM_PBP1_transp_AraH_like, Transmembrane subunit (TM) of Escherichia coli AraH and related proteins. E. coli AraH is the TM of a Periplasmic Binding Protein (PBP)-dependent ATP-Binding Cassette (ABC) transporter involved in the uptake of the monosaccharide arabinose. This group also contains E. coli RbsC, AlsC, and MglC, which are TMs of other monosaccharide transporters, the ribose transporter, the D-allose transporter and the galactose transporter, respectively. The D-allose transporter may also be involved in low affinity ribose transport. These transporters generally bind type 1 PBPs. PBP-dependent ABC transporters consist of a PBP, two TMs, and two cytoplasmic ABCs, and are mainly involved in importing solutes from the environment. The solute is captured by the PBP, which delivers it to a gated translocation pathway formed by the two TMs. The two ABCs bind and hydrolyze ATP and drive the transport reaction. Proteins in this subgroup have a single TM which homodimerizes to generate the transmembrane pore.	1.19465e-65
NC_013729.1\|WP_012917958.1\|282931_283825_-\|LLM-class-flavin-dependent-oxidoreductase	gnl\|CDD\|366009	pfam00296, Bac_luciferase, Luciferase-like monooxygenase.	6.75133e-64
NC_013729.1\|WP_012917946.1\|268524_268851_+\|LuxR-family-transcriptional-regulator	gnl\|CDD\|225107	COG2197, CitB, Response regulator containing a CheY-like receiver domain and an HTH DNA-binding domain [Signal transduction mechanisms / Transcription].	5.36173e-07
NC_013729.1\|WP_012917941.1\|261977_262313_+\|L-rhamnose-mutarotase	gnl\|CDD\|377501	pfam05336, rhaM, L-rhamnose mutarotase. This family contains L-rhamnose mutarotase which is a glycosyl hydrolase that converts the monosaccharide L-rhamnopyranose from the alpha to the beta stereoisomer. In Escherichia coli this enzyme is the product of the rhaM gene (also known as yiiL). The tertiary structure has been solved, in complex with L-rhamnose, and the catalytic mechanism determined. His22 is the proton donor. The enzyme naturally exists as a dimer.	5.68452e-42
NC_013729.1\|WP_012917944.1\|265547_267011_+\|L-fucose/L-arabinose-isomerase-family-protein	gnl\|CDD\|238323	cd00578, L-fuc_L-ara-isomerases, L-fucose isomerase (FucIase) and L-arabinose isomerase (AI) family; composed of FucIase, AI and similar proteins. FucIase converts L-fucose, an aldohexose, to its ketose form, which prepares it for aldol cleavage (similar to the isomerization of glucose in glycolysis). L-fucose (or 6-deoxy-L-galactose) is found in various oligo- and polysaccharides in mammals, bacteria and plants. AI catalyzes the isomerization of L-arabinose to L-ribulose, the first reaction in its conversion to D-xylulose-5-phosphate, an intermediate in the pentose phosphate pathway, which allows L-arabinose to be used as a carbon source. AI can also convert D-galactose to D-tagatose at elevated temperatures in the presence of divalent metal ions. D-tagatose, rarely found in nature, is of commercial interest as a low-calorie sugar substitute.	7.93052e-112
NC_013729.1\|WP_012917950.1\|274140_275559_-\|HAMP-domain-containing-histidine-kinase	gnl\|CDD\|223715	COG0642, BaeS, Signal transduction histidine kinase [Signal transduction mechanisms].	5.06695e-54
NC_013729.1\|WP_148256834.1\|280846_282310_-\|LytR-family-transcriptional-regulator	gnl\|CDD\|224235	COG1316, LytR, Transcriptional regulator [Transcription].	1.43342e-27
NC_013729.1\|WP_012917951.1\|275697_276027_-\|hypothetical-protein	gnl\|CDD\|237864	PRK14950, PRK14950, DNA polymerase III subunits gamma and tau; Provisional.	0.00190035

>NC_013729.1|WP_012917948.1|272387_273161_+|hypothetical-protein
MDGNTVLWIVVAAVVVLILLALIAAAAKKAKQRRIEHDRQAAVEHEQKARLSAVHAERQHAAADEVEARSRKAQAIADEKAAEARRLAAGATERREAAEQASSESSEHLTKAQELHPEAQRRDDDDSADRSPHAASWGTDAEHAEGADRHRRDVQGDDGLRRGSPEAAGTAGSPGAPMRGATEDQLSAPGAREELGNRDAGQVGDRDAGGQVGDRDADGRLMDDGRAQHAANDRPVDADPVVDPDGDGRTPRHSSQQ
>NC_013729.1|WP_012917947.1|269043_272241_+|family-78-glycoside-hydrolase-catalytic-domain
MSFRTRFGCLLAAVLLLTPLVPATGSPPATRETLQVRNLKTNNLTNPLGVPGTPPRLSWQLDGDRRGITQSRYQIRVASTPAKTARPDIWDSGVVRSTDSIEVPYGGPALTTGTAYHWTVRVWDDAGKASAWSPVATFETGPLRPGDWQGDWIGADNQPGPEWTDTTIDADVTLVKDALGVFFRGRGGVGYMWQLNQLTPDKPLLRPHVRQPGGGYVLLGEIPLAAGTDLKQRHHLRITVAGRTITTWLDGVQVDSRERSDHNAPGVVGFRTDGAEHGVVHSLKVTNVAGEVLVDTAFPAGDQTFPDGTVRAEGGLQVKGTTDLWLPGKPIPVFRKAISLPKAKKVASARIDAAAQGIYELTVNGRKAGDHQLAPGWTDYARRIQSQTYDVTKLLKSGANTLGAEVAPGWFTGNLAMFGPNKYGTDTAFIAQLRVTYTDGTADVFATDSSWQTAPGAVRVADLLNGESYDARRTASEWVPAQVRPSATAKIVPQTDQPVRVTQELKARAIPSPTPGAYLYDLGQNMVGIARLTLHGRPGQTVKIRYGEVLNPDGTLYTDNLRSAKATDHYTFATSRPETYQPRFTFHGFRYVEVSGLPTAPPASAIVGVVLGTDAEQVNEFRTNSPLVNQLHSNIVWGQRGNFLSIPTDTPARDERMGWTGDINVFARTAVYNLDSQAFLTKWLQDLRDTQRADGAYASVAPTVPNSFDGGMGNAGWADAGVNVPWTLWQAYGDTSVIRQHYASMTRYVDYLVASSNGLIRGGGDYGDWLNLDDPTPGELIGTSFVAKGARQLSQMAAAIGHTADAAKYQRVYEDVRAAFAARFVAADGKVGSDSQTGYILAFTSDLVPADRIAAAGEHFAATILRRDTHLSTGFLGVDGLLPVLTKIGRTDLAYRLLQNTSYPSWGYEIGKGATTIWERWNSINPDGTFNDVGMNSFNHYAYGAVGEWMYRTLAGLSAAEPGYRKALIAPTPGDGIDTAQLRHRTPYGEVGSQWRRLADGRFTLEVEVPANTTATVRLPAAEARQITESGRALSRAVGVSGVVDEGTTVALTVGSGNYRFAVRP
>NC_013729.1|WP_012917946.1|268524_268851_+|LuxR-family-transcriptional-regulator
MTVLHNETRPRPELSDLARASEHCGFLRATHQCGLPRATPEPALPREISHEDLKLLRLLATGLPMDAVARRLDLSERTVRRRTRAACDRLGFGTAIEAIVWAAHRGLL
>NC_013729.1|WP_041289678.1|267083_268520_+|rhamnulokinase
MAAVDLGASSGRVMVGRVGPDTLELSEVHRFSNGPVRVQGTLHWDILRLYQETLAGLGEAARTGPLDGLGIDSWAVDYGLLDAEGRLLGNPVHYRDSRTDGVMDGVLRKIPAEDLYAVTGLQQLPFNTIYQLVAERALDRATSLLLIPDLLSYWLTGVAGAEATNASTTQLYDVRFRTWSADLAGRIGVPLELLPPLREPGQVIGPVLPEVAEETGLDATTPVIAVGSHDTASSVVAVPAAAGDRFAYISSGTWSLVGLELPEPVLTPAAQEANFTNEGGVDGRTRFLKNVMGLWILQECLRVWGTDDLVQLLKGAADVPAFGVLVDPDHPSFLAPGNMPARIAEFCAQSGQEPPTSRAVIVRCVLESLALAYRRTLRRAQQVAGREVDVVHVIGGGSQNELLCQLTADACGVPVLAGPVEASALGNVLVQARALGEPLPDLDAMRALVRATHRLRRYEPQGRPADWDAAESRVFGTR
>NC_013729.1|WP_012917944.1|265547_267011_+|L-fucose/L-arabinose-isomerase-family-protein
MWSTNPTRSVDGNGLLPWVEPRRTRIGLVAGGLGAYWPQFPELLPQLQASARRVSERFAEFDCEVVDAGFISDAQEGAAAAEKLRLADCDLIVGFLTTYMTASMLVPVAQRSGAPVLLLNLQPTEAMDHATFDTGAWLAYCGACPLPEMANAFERCGIDFRSVSGYLEDERAWDRIGRWLRAAGVRAALRHGRHGLLGHLYPGMMDVITDPTLVSAQLGGHVEILEIDDLRVRVEKVTPAETEARMKVAQDVFTLDESVVEHDFRWGATVSVALDRLVEDFELDSLAYYHRGLDGETHERVAAGMILGASLLTARGVPAAGEYELRTSLAMLMMHKLGGGGSFTELQALNFHDNVVEMGHDGPAHLAISSAKPLLRGLGVYHGKRGWGVSVEFDVAHGPVTALGLGQLRDGSFKMIASEGTVVPGPLLQIGNTTSRVDFGCDPGEWTDAWSASGVAHHWALGTGHRVPELKATASLLHLPLEVVDPS
>NC_013729.1|WP_012917943.1|263477_265517_+|bifunctional-rhamnulose-1-phosphate-aldolase/short-chain-dehydrogenase
MTVTDTAAELVARSNRLGADPRNTNYAGGNTSAKGTATDPVTQQPVDLVWVKGSGGDLGTLTAAGLAVLRQDRLNALVDVYPGVEREDEMVAAFDYCLHGKGGAAPSIDTAMHGLVDAPHVDHLHPDSGIALATAADGEKLTAECFGGRVVWVPWRRPGFQLGLDIAQVKRDNPQAIGVILGGHGITAWGDTSAECEANSLEIIRTAERFLAERGKAEPFGAVVPGFEALPTEQRRQRAAALAPVIRGLASTGNPQVGHFNDDDVVLEFTAREKLAELAALGTSCPDHFLRTKVRPLVLDLPPAAPLEEAVTRLKELHLQYREDYAAYYDRHAEPDSPPMRGADPAVVLVPGVGMFSFGKDKQTARVAGEFYVNAINVMRGAEAVSSYAPIDEREKFRIEYWALEEAKLQRMPKPKPLATRIAFVTGGGSGIGKAIAHRLAAEGACVVVADLDTAAAEAVAKEIGGPDQAIAVGADVSSEAAVAAAFEQAVLAFGGVDLVVNNAGLSISKPLLETTEKDWDLQHDVMAKGSFLVSRAAAKVLIDQAIGGDIVYISSKNAVFAGPNNVAYGAAKADQAHQVRLLAAELGGHGIRVNGVNPDGVVRGSGIFAKGWGAQRAAVYGVPESELGAFYAQRTLLKREVLPEHVAAAVFALAGGDLSHTTGLHVPVDAGVAAAFLR
>NC_013729.1|WP_012917942.1|262317_263481_+|L-rhamnose-isomerase
MTTEAVKNALRRQEIELPSWAFGNSGTRFKVFSQPGVPRSPEEKIADAAVVHRYTGVAPSVALHIPWDKVDDYAALAAYAKEQGVRLGAINSNVFQDDDYKLGSVTNPDPRVRRKATDHLLECVDIMDATGSRDLKLWFSDGTNYPGQDDIQDRQDRLATALKEVYDRLGDDQRMLLEYKLFEPAFYTTDVPDWGTSYAHCLELGPKATVCIDTGHHAPGTNIEFIVAFLLRVNKLGAFDFNSRFYADDDLMVGAADPFQLFRIMNEIVRGDALDPDRGIAFMLDQCHNIEAKIPAIIRSVMNVQEATAKALLVDRDALRKAQADGDVLGANAALMDAYNTDVRPLLADLRAEQGMDPDPVAAYRRSGYFEQISKDRADGRQAGWGA
>NC_013729.1|WP_012917941.1|261977_262313_+|L-rhamnose-mutarotase
MNRYCFCLQVKPDRLDEYVERHRDVWPDMRAALHEAGWHNYSLFLRDDGLLIGYVEAEDLEAAQKAMAATEVNARWQAEMQQFFAGSDGRPPDESFLLLREIFHLTPPAED
>NC_013729.1|WP_012917940.1|260867_261959_+|rhamnose-ABC-transporter-substrate-binding-protein
MSFRLSRRTAVPLSTVAVLSLALTACGGGTTKESTANDATAAPSATTSAAADPNAPLKEGLKIAYLPKQLNNPYTDVEVGGGKVAVGEIKGEYKLVGPNDASASSQVSYINTLIQQQQDVIVVAANDPNAVCPSLNQARKADIKVVTFDSDAAKTCRDAFINQATTQGIGESLVKMAKELAGGSGEIAVLSATPNATNQNSWIEVMKTELAKPENAKLKLVKIAYGNDDDQKSFTEAQGLLQSYPNLKVIVSPTTVGIAAASRYVSASSYKGKVAITGLGLPNQMRQYVKDGTVKKFALWNPADIGYLAAYAGAALKSGQITGAQGEKFKAGKLGEYTVGAAGEIVLGPPTEFTAANIDQFNF
>NC_013729.1|WP_012917939.1|259821_260841_+|ABC-transporter-permease
MSAETAAVTDHPTGLAGRFANWNVAIIAVTVLVIAVAAATVDNFGTSQNFGFLVLDLLPIALVALPMTLVIVTGEIDLSVASTLGLCSAVMGSLWNANQPIETIIPVCLLLGAVLGAVNGFFVTVLGLPSLAVTIGTLALYRGLAFVVLGDGAVADFPALYTNWVTGTIGGTPLPNVLIVIVALAVVFGVILHATPIGRAVFAVGASEQAARFAGVRPGRLKFWLYVVSGLVAGLAGVLWTLRYSSARADNGAGLELAVVAAVLLGGVSIFGGKGALPGVIAGVVLLASLQNALRLSDVSNEALNVVTGVLLIASVLAPNLANAVRGAVQRRRHRTDLL
>NC_013729.1|WP_012917949.1|273475_274144_-|response-regulator-transcription-factor
MNRILIAEDEQRIASFVERGLRSNGFVTTVVADGETAYQEGVSGGYDLLLLDLGLPRVDGFTVLRRLREARVTMPVVILTARDGVRDTVAGLEGGADDYIAKPFAFEELLARVRLRLRSDGSGTADANILQVGDLSLDLRTRRASVDGRTVDLTAREFLLAEVFCRHPDQVLSREQLLSQVWGFDFDPGSNVVDVYIRYLRRKLGPDRIQTIRGMGYRLRPG
>NC_013729.1|WP_012917950.1|274140_275559_-|HAMP-domain-containing-histidine-kinase
MLGVLALAVTAVVFLTWQVLSARSDAAADAELTHEATKFRAYAGSPTAASLTTPEDLLDRWLQSNLPDTSEAFFTIVDGRAYHRSQGTPPARLDTDTAFVQRIGSATTPQYGWVDSTAGKVRYAVIPVRVGTEPVRAQLVLLEFRDLLAQPLEDAAKALALIGLVTLAMAAGACWIVTGRVLAPIRQVRATAEQIGASDLRRRIDVVGNDDVAQLARTFNTMLDRLEFAFTAQREFVDNAGHELRTPITVIRGHLELMSDDPRDREQTRALILDELARMNRMVDDLLVLAKSGRPDFLELEQVNLTELVVEAVAKARPLADRTWRVDESADASMLADGQRLTQALMQLVSNAVRHTRPGDRISVGSRVIPADPDGPARVLLWVEDSGAGVCVADRERIFDRFARGNDQGRTDGAGLGLAIVRSIARAHGGDARLADGGGPGARFELELPFGPAVEQSVDEELGEIVESEEVR
>NC_013729.1|WP_012917951.1|275697_276027_-|hypothetical-protein
MRSPRLVYLAVVLVLAVGGFALTRYLADRSSPGLGETVVVPAGSGVSVPPRSPGTPPATAPTTAPPTTAPTTPGADPVAPGSPRTAGENDDRDDDGIDDDLDDAVQGDD
>NC_013729.1|WP_012917952.1|276092_277364_-|threonine-ammonia-lyase-IlvA
MQGSETVARPTVGAAEVEAAVRRLDGVALRTPLQRNPRLSARTGAEVWLKREDLQIGRSYKLRGAYNLIAQLDEAAKRAGVVCASAGNHGQGLAYSCHTLGVSGRVYVPRTTPRQKRDRIAALGGAQIEVIVTGDTYDDAAAAALAEAAATGATLVPAFDDPRTVAGQGTVAVELVEQLGRTPDVLVVPVGGGGLVAGVAAYLAERHPGVRIVGVEPAGAASMAAALAAGEPVTLPQLDSFVDGAAVRRVGDVTLPLVSAAGVEMISVPEGLVCSEMLELYQTDGLIAEPAGALSAAALGHGVELKPGETVVCLLSGGNNDVSRYGEILERSLVHEGLKHYFLVTFPQEPGALRQFLDGVLGPDDDITLFEYVKRNNRETGVALVGIEIGRPGDLAGLLDRMDAAPLDIERIRPDSAEFRYLI
>NC_013729.1|WP_012917953.1|277598_278465_+|hypothetical-protein
MELIPFSLWGDALWCGQEVVRETAHEQAIRSLFPDPIPARGADLDTDADLVPEPHNRFDPRSIAVRVQGKVVGYLPRDDAHRYHPVLSELVAQGLQPQVPCHLWVSEWEPADWEGKGNHTKEFHASVAVALGQPHMLVPVNLPPPGSFHVLPPGSGIVVPGSEIRPEVLAPFFRPEGECWAYATLHAADEDDGVHDRPRTVVEVRLDDEPVGRLSPRLSAEFLPAIHYLADMRAETAARVAVRGDRFASEVILYAARSHDLPATWPDGLTRSPVASPTWHYWAGKEAN
>NC_013729.1|WP_012917954.1|278586_279330_-|MBL-fold-metallo-hydrolase
MTSLTVLGTAAPYPLPDRPCSGYLLQGGGAKVWMDAGPGSLAELLRHTSLDQLDAIWVSHLHLDHVGDVLNAYYALAYGLLPPLVRPLPVYAPAGLGKRLAGFFEQPDAGFVSNVLELRELRDGLTVELGGLQLVSGAVEHGCDAYGLRASAEGRTLAYSGDCEPCPALDELAAGVDLLLCEADSGEASGGHHTPEQAGAVARRTGVRRLVVTHVGPSLTPDAATARAAAVFGGPTACAEVGLTMPW
>NC_013729.1|WP_041289682.1|279326_280271_-|prolyl-oligopeptidase-family-serine-peptidase
MSAEELSVYQGTNPRPDDFDQFWDKALAELAGTDADASFVDATDFPLTTATAQHLYFNGTGDYRVHAKVIRPQEPAGPAVLMFHGYGGEQPRWVDLLPYAARGFTVAALDVREQVGFRTSSQEPNSFSLHNHLVHGLDGGPDSLLYKHVFLDTRRLADIIRGLPEVDGARVATTGWSQGGGLSLVCAALTPEIKYAASVYPFLTDYQRAWELNLDTNPYNEITTWFKKRDPRHLREQEVFTTLGYIDLQHLAPRVQAEVTLFVGLEDQVCPPSTQYAVYNKLTGVKELRTYPDLGHDDLPGAHDDIYQLIGAKL
>NC_013729.1|WP_148256833.1|280332_280719_-|hypothetical-protein
MAAIAWAVGLPDAVVGVFAVLGGLVALAGLWVLARPPVLLKLGEDRIEVRGLKTEWTDVTEVGRVATTHGEAIALRTKHKDGSILIPLRWLAPGRTEQLEQELRERLNTAHGYTIWDGTAGPADDRAE
>NC_013729.1|WP_148256834.1|280846_282310_-|LytR-family-transcriptional-regulator
MGLTLVSALIPGSGFVMGGRTKLGAFVMTLSFGLLALAAYIGLTNRNAVLELAVDPRRLLIATAAVVVLGLLWIWVVVASHKLLRPVSLTALGRLAGSAFVGLICFGIAVPTTVAAQTVMAQRDLVGSVFASEGNSKSATRPDVEDKKDPWADQPRLNILLLGADDGAGREGTRTDTVMVASIDTKSGDTKLISLSRNWMRMPFPEDSPLHKLYPDGFYDPDLGNVEQPEYYLDAMYRNLPAAHPGVLGPSDNEGADVLKVSAGAALGLDIDYYMQVNLKGFESIVDALGGITVNINYRVPIGGDYRGAGSADDVLPKDYLEPGRNQKLNGHDALWFARGRYGLSDISRQERQRCTIHALVSSANPGTLVTKYQQIASASKKLLQTDIPQEILPAFIELGLKVKNAKVSNIDLDKNKNFPSGRNPNYEAMREIVQKAIAPKKTVASTPASPVTPRKPSTGKSTAPPKAPAGGTEDLSDACAYHPANP
>NC_013729.1|WP_012917958.1|282931_283825_-|LLM-class-flavin-dependent-oxidoreductase
MKLGVMVPVGGSDGPDGQLPGWADTRRLAEAAEQSGLDSVWLADHFFYRDPAGTTYGMHEAWTLLSALAVVTSRVELGTMVLCASFRDPGLVAKMAATLDEVSGGRLILGVGAGWHDPEYEANGLPTDHRVGRFEEWLEIVARLVRGETVSMEGKYYTVVDNALVPAPQRRIPVLVAALRPRMLDLTAQWADAWNTAWFGAVDEKVRERLDDFDAALERNQRPAGEVATTVGVTVRDPDQPAIPDGASNALAGTVEELAEALTEYAALGVDHLVVGLEPMTPRSVERLAEAGRLAFG

You can click texts colored in the table to view more detailed information

Click the colored protein region to show detailed information

Crispr_ID: NC_013729_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NC_013729_2

1363180-1363267

Orphan

Consensus_repeat	Method
TCAGAATTTGCTGGGCCAACCCTGC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NC_013729_2

>merge|NC_013729|2|1363180-1363267|CRISPRCasFinder
TCAGAATTTGCTGGGCCAACCCTGCGCTTGAGGGGTTAACCCAGCAGATGCAGGGTTGGCCAGTCAGAATTTGCTGGGCCAACCCTGC

>NC_013729|2|2|1363180-1363267|CRISPRCasFinder
TCAGAATTTGCTGGGCCAACCCTGC	GCTTGAGGGGTTAACCCAGCAGATGCAGGGTTGGCCAG
TCAGAATTTGCTGGGCCAACCCTGC

Protein	Signature genes	Signature genes Name	Protein_function
NC_013729.1\|WP_041289839.1\|1370288_1371140_-\|alpha/beta-fold-hydrolase	unknown	unknown	gnl\|CDD\|366166
NC_013729.1\|WP_148256559.1\|1358322_1359339_-\|CAP-domain-containing-protein	unknown	unknown	gnl\|CDD\|349398
NC_013729.1\|WP_012918968.1\|1371813_1373553_-\|alpha/beta-fold-hydrolase	unknown	unknown	gnl\|CDD\|312032
NC_013729.1\|WP_012918958.1\|1361019_1362171_-\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|379112
NC_013729.1\|WP_012918952.1\|1355625_1355883_-\|hypothetical-protein	unknown	unknown	unknown
NC_013729.1\|WP_012918956.1\|1359337_1360246_+\|NAD-dependent-epimerase/dehydratase-family-protein	unknown	unknown	gnl\|CDD\|187540
NC_013729.1\|WP_012918961.1\|1364443_1365490_-\|galactose-1-phosphate-uridylyltransferase	unknown	unknown	gnl\|CDD\|238341
NC_013729.1\|WP_012918950.1\|1353812_1354601_-\|Zn-dependent-hydrolase	unknown	unknown	gnl\|CDD\|293841
NC_013729.1\|WP_012918951.1\|1354671_1355619_+\|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|181818
NC_013729.1\|WP_148256885.1\|1368168_1368732_-\|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|378968
NC_013729.1\|WP_012918954.1\|1357166_1358162_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|349398
NC_013729.1\|WP_041289180.1\|1360290_1360950_-\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|366181
NC_013729.1\|WP_012918967.1\|1371380_1371758_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|226318
NC_013729.1\|WP_012918962.1\|1365622_1366921_+\|HlyC/CorC-family-transporter	unknown	unknown	gnl\|CDD\|224173
NC_013729.1\|WP_148256884.1\|1356035_1356887_-\|CAP-domain-containing-protein	unknown	unknown	gnl\|CDD\|236090
NC_013729.1\|WP_012918960.1\|1363316_1364447_-\|galactokinase	unknown	unknown	gnl\|CDD\|223231
NC_013729.1\|WP_012918969.1\|1373564_1373963_-\|DUF805-domain-containing-protein	unknown	unknown	gnl\|CDD\|377540
NC_013729.1\|WP_012918959.1\|1362284_1363100_+\|DeoR/GlpR-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224268
NC_013729.1\|WP_012918965.1\|1368945_1370181_-\|serine/threonine-protein-kinase	unknown	unknown	gnl\|CDD\|270916
NC_013729.1\|WP_012918963.1\|1366909_1368172_-\|MFS-transporter	unknown	unknown	gnl\|CDD\|340863

Protein	Function_ID	Function_description	E-value
NC_013729.1\|WP_041289839.1\|1370288_1371140_-\|alpha/beta-fold-hydrolase	gnl\|CDD\|366166	pfam00561, Abhydrolase_1, alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes.	7.05752e-14
NC_013729.1\|WP_148256559.1\|1358322_1359339_-\|CAP-domain-containing-protein	gnl\|CDD\|349398	cd05379, CAP_bacterial, Bacterial CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain proteins. Little is known about bacterial and archaeal members of the CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain family. The wider family of CAP domain containing proteins includes plant pathogenesis-related protein 1 (PR-1), cysteine-rich secretory proteins (CRISPs), and allergen 5 from vespid venom, among others. Studies of eukaryotic proteins show that CAP domains have several functions, including the binding of cholesterol, lipids and heparan sulfate. This group includes Borrelia burgdorferi outer surface protein BB0689, which does not bind to cholesterol, lipids, or heparan sulfate, and whose function is unknown.	9.43645e-45
NC_013729.1\|WP_012918968.1\|1371813_1373553_-\|alpha/beta-fold-hydrolase	gnl\|CDD\|312032	pfam08386, Abhydrolase_4, TAP-like protein. This is a family of putative bacterial peptidases and hydrolases that bear similarity to a tripeptidyl aminopeptidase isolated from Streptomyces lividans. A member of this family is thought to be involved in the C-terminal processing of propionicin F, a bacteriocidin characterized from Propionibacterium freudenreichii.	3.38959e-11
NC_013729.1\|WP_012918958.1\|1361019_1362171_-\|GNAT-family-N-acetyltransferase	gnl\|CDD\|379112	pfam13302, Acetyltransf_3, Acetyltransferase (GNAT) domain. This domain catalyzes N-acetyltransferase reactions.	5.77709e-28
NC_013729.1\|WP_012918969.1\|1373564_1373963_-\|DUF805-domain-containing-protein	gnl\|CDD\|377540	pfam05656, DUF805, Protein of unknown function (DUF805). This family consists of several bacterial proteins of unknown function.	2.58407e-35
NC_013729.1\|WP_012918956.1\|1359337_1360246_+\|NAD-dependent-epimerase/dehydratase-family-protein	gnl\|CDD\|187540	cd05229, SDR_a3, atypical (a) SDRs, subgroup 3. These atypical SDR family members of unknown function have a glycine-rich NAD(P)-binding motif consensus that is very similar to the extended SDRs, GXXGXXG. Generally, this group has poor conservation of the active site tetrad, However, individual sequences do contain matches to the YXXXK active site motif, and generally Tyr or Asn in place of the upstream Ser found in most SDRs. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.	2.6913e-88
NC_013729.1\|WP_012918961.1\|1364443_1365490_-\|galactose-1-phosphate-uridylyltransferase	gnl\|CDD\|238341	cd00608, GalT, Galactose-1-phosphate uridyl transferase (GalT): This enzyme plays a key role in galactose metabolism by catalysing the transfer of a uridine 5'-phosphoryl group from UDP-galactose 1-phosphate. The structure of E.coli GalT reveals that the enzyme contains two identical subunits. It also demonstrates that the active site is formed by amino acid residues from both subunits of the dimer.	1.15749e-111
NC_013729.1\|WP_012918950.1\|1353812_1354601_-\|Zn-dependent-hydrolase	gnl\|CDD\|293841	cd16283, RomA-like_MBL-fold, Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain. Derepression of the romA-ramA locus results in a multidrug-resistance phenotype. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.	1.02428e-16
NC_013729.1\|WP_012918951.1\|1354671_1355619_+\|helix-turn-helix-domain-containing-protein	gnl\|CDD\|181818	PRK09393, ftrA, transcriptional activator FtrA; Provisional.	8.60893e-98
NC_013729.1\|WP_148256885.1\|1368168_1368732_-\|helix-turn-helix-domain-containing-protein	gnl\|CDD\|378968	pfam12840, HTH_20, Helix-turn-helix domain. This domain represents a DNA-binding Helix-turn-helix domain found in transcriptional regulatory proteins.	3.48628e-10
NC_013729.1\|WP_012918954.1\|1357166_1358162_-\|hypothetical-protein	gnl\|CDD\|349398	cd05379, CAP_bacterial, Bacterial CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain proteins. Little is known about bacterial and archaeal members of the CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain family. The wider family of CAP domain containing proteins includes plant pathogenesis-related protein 1 (PR-1), cysteine-rich secretory proteins (CRISPs), and allergen 5 from vespid venom, among others. Studies of eukaryotic proteins show that CAP domains have several functions, including the binding of cholesterol, lipids and heparan sulfate. This group includes Borrelia burgdorferi outer surface protein BB0689, which does not bind to cholesterol, lipids, or heparan sulfate, and whose function is unknown.	3.30057e-44
NC_013729.1\|WP_041289180.1\|1360290_1360950_-\|GNAT-family-N-acetyltransferase	gnl\|CDD\|366181	pfam00583, Acetyltransf_1, Acetyltransferase (GNAT) family. This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.	6.85958e-06
NC_013729.1\|WP_012918967.1\|1371380_1371758_+\|hypothetical-protein	gnl\|CDD\|226318	COG3795, COG3795, Uncharacterized protein conserved in bacteria [Function unknown].	1.61904e-19
NC_013729.1\|WP_012918962.1\|1365622_1366921_+\|HlyC/CorC-family-transporter	gnl\|CDD\|224173	COG1253, TlyC, Hemolysins and related proteins containing CBS domains [General function prediction only].	1.97133e-115
NC_013729.1\|WP_148256884.1\|1356035_1356887_-\|CAP-domain-containing-protein	gnl\|CDD\|236090	PRK07764, PRK07764, DNA polymerase III subunits gamma and tau; Validated.	2.18034e-07
NC_013729.1\|WP_012918960.1\|1363316_1364447_-\|galactokinase	gnl\|CDD\|223231	COG0153, GalK, Galactokinase [Carbohydrate transport and metabolism].	6.41155e-124
NC_013729.1\|WP_012918959.1\|1362284_1363100_+\|DeoR/GlpR-transcriptional-regulator	gnl\|CDD\|224268	COG1349, GlpR, Transcriptional regulators of sugar metabolism [Transcription / Carbohydrate transport and metabolism].	4.80598e-81
NC_013729.1\|WP_012918965.1\|1368945_1370181_-\|serine/threonine-protein-kinase	gnl\|CDD\|270916	cd14014, STKc_PknB_like, Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.	3.20423e-119
NC_013729.1\|WP_012918963.1\|1366909_1368172_-\|MFS-transporter	gnl\|CDD\|340863	cd06173, MFS_MefA_like, Macrolide efflux protein A and similar proteins of the Major Facilitator Superfamily of transporters. This family is composed of Streptococcus pyogenes macrolide efflux protein A (MefA) and similar transporters, many of which remain uncharacterized. Some members may be multidrug resistance (MDR) transporters, which are drug/H+ antiporters (DHAs) that mediate the efflux of a variety of drugs and toxic compounds, conferring resistance to these compounds. MefA confers resistance to 14-membered macrolides including erythromycin and to 15-membered macrolides. It functions as an efflux pump to regulate intracellular macrolide levels. The MefA-like family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	1.14217e-57

>NC_013729.1|WP_012918959.1|1362284_1363100_+|DeoR/GlpR-transcriptional-regulator
MNAAGTAEPRGRGGQLAAQRQATIVAEVNSRGAVTVAELVDRFGVSDMTIRRDLDALDSSGLLHKVHGGATSVGLRSAHEPGFDAKLTQESAAKQAIAAEAARRVQPDSAIGIGAGTTTYALARQLLRVENLTVVTNSARIADVFHSNGRSDRTVVLIGGIRTPSDALVGPIATAALQSLHLDMLFLGAHGVDAEHGLSTPNLMEAETNRSFIAASREVVLVADHTKWGTVGLSTFATWNDLDVVVTDAGLAPAARKAMRDTGCELVLATT
>NC_013729.1|WP_012918958.1|1361019_1362171_-|GNAT-family-N-acetyltransferase
MRFPEDVPVLTDGSITLRAHTTADVEPAYEACQDPQMQQWTTIPVPYLREHAVSYLTEVIPAGWRNDGSFAWAIEYDGRYAGTIDLRDTQGGQGEIGFAVAPWARGHGVMTRAVKLVVRHAFDVLGWNRVVWRAYVGNWGSRRVAWKAGFRHLVTVAGGGLQRGVRRDEWVASIGRDEELEPQGHWWDVPVVEGDNLRLRALRPDDADRVVEACTDERTQHWLAGMPSPYGRQEAEAFIEGRLENSASGEGVSWAITEPGSDLLLGNVSVFDLRNRIDATMGEVGYWLHPQARGRGVMTEAVRLAARHAFTPIEQGGLGRRRLVLYAAIGNKASAYVAEANGFTLTGTARAASPRRDGSFDDLLCFDLLSTDSRGESGPRSTE
>NC_013729.1|WP_041289180.1|1360290_1360950_-|GNAT-family-N-acetyltransferase
MRDREELVRRWQAGWSVSRGWTTVEDDNDGILTVRAGEDNRAMEYVVLDADDKPERVERAAELAQAAGGGRGAGWITLATDDREARTEQLEDLGLEVQREQDWLMTIQLSEQPALQLNDRYALHTELESDLIVTRATLHGGVVSSGRMAVVGEDAVADRIETDPAHRRRGLGSAVMASLVETAAAHGAKRGILIASIDGLRLYRSLGWKVVADIVIARC
>NC_013729.1|WP_012918956.1|1359337_1360246_+|NAD-dependent-epimerase/dehydratase-family-protein
MQVVVGAGPVGTTVARLLAERGEDVKLVTRSGGGPEHPAITKVAADATDPAALSAIASGASSLLSCGGPPYPRWAAEWPPLGASLIAAAEKTGAVLVSTGNLYPYGEPSGPIREQDPERPNSVKGAVRAKLWADALAAHQAGRIRTAEVRGSDYLGAGAASFFTIGVLPGVLKGKKVAVPADLDAPHSWTAVQDVARTLVAVAGDEAAWGRTWLVPTPPPVSLRDLAARAAELAGAPPARLTTMPPAVLWIGGLFDQQAKEIRELQYQVRRPFVIDSGQAERAFGLRPTPTDDALRDTVNAV
>NC_013729.1|WP_148256559.1|1358322_1359339_-|CAP-domain-containing-protein
MRVLPCSTAGREDSRPAANGSTSKVCQCGVAGRAEGSFGRSRSATVRSVPSSQYDEFPGHGGRRRAKRRSVAAPILAALVVLGLLAGGGWYLTRDGKDAVATGQDEPLTAGTGPSSTSPSDEPAELPTPTATPSVTPTPTPTPTLTPSRTPSATPSRTPPNKPSATPTPTRSSSAPSRGSTRTPTPSPKPTRTSTPRPTTTKPAPPSGGSAETQVLHLTNAERQKAGCGPLRSNAALTRAAEGHAADMVDRHYFDHTSLDGRSPFDRMKAAGFTGGAMAENIAVGYSSPAAVVEGWMKSTGHRKNMLNCSYTMIGIGYHSGQVKPDWGNGSWVQNFGG
>NC_013729.1|WP_012918954.1|1357166_1358162_-|hypothetical-protein
MTDSPTPGRHRGRRAAPRRSRGLVGPVVSSLSVLLAIGPVVWLMTNRDGSAVADNDATKVLNVAEDNSGPAAVDDSTSPGAPGKTGKPQATVTATLPNGMTTTITPSGTPTLGTAESTPGTPVTGGPTTVITSLPGGVTTVTVRPSGPPTIAGGTAKPKPRPASSKPTTTTTTTTTTSTPPPTTEPTPDDPPPGGGGTNAQEREVLELTNQARRRQGCRPLQLDDSLVEAAGRHASDMVRRHYLDHTNPDGQGPGDRIQAAGFRGSGWGENIAAGYESPQRVVAAWMNSDGHRANILNCKYNRIGIGFDPGQVKSDWGSGSWVQDFGRVSS
>NC_013729.1|WP_148256884.1|1356035_1356887_-|CAP-domain-containing-protein
MIAIASVVLVITPISWILLHEPQNDQADASIPYVSRDDDTYITASADPAAVTTEAPTTATPSTPPTPGQTPTPTPVPTTTPTPGQTPGTTAPTDAPTDGPTDWPTDGPTGRPTSTPTDPPTGGATTPPQPPPDEDSPGPQPTRTPTPTRTTTSSPPPEDEGNMSPAELELFHLVDNARQERGCAPLRRNNDLSDGAGSEAEGRASSGDVAETGSSKAAAGGDSMTAKTAFDRLKADSSRTLFNCGLDELGVGRGTATRETGALCGLLGVCTTRTRVAWVVDFD
>NC_013729.1|WP_012918952.1|1355625_1355883_-|hypothetical-protein
MSERDDLEPARPALFGIPPDALADERPDGRPEAAKRMGLSRHTEEGAVVAFASSLDRTKPGHRTMAWIMLVMFSAPAFYTLLLLF
>NC_013729.1|WP_012918951.1|1354671_1355619_+|helix-turn-helix-domain-containing-protein
MRTVAVLAFDGISPFHLSVPCLVFGDRLGTEHLYDVQVFAEQAGRLGTNAGFGLHVERELDVLRTADLVILPSWTPGVTPSPRLLDAIRAAHLRGATVVGLCLGSYLVAASGIAAGREVVTHWYWAEDLQKRYADLRVRADVLWSDLGDVVTSAGTASSLDCCLHLVRAHHGVEVAEQLARRIVVAPHRSGTQAQYIPVPVPPEEADDVIEKAMVWARARLDRTISLDEWAAAVALSRRTFTRQFRARTGVSGQAWLLRQRLDRARSLLETTDHPVERIATASGFGSSAALRHHFRQVLGTTPQRHRQDFTRLAG
>NC_013729.1|WP_012918950.1|1353812_1354601_-|Zn-dependent-hydrolase
MKLTHIGGPTALLELGGLRLLTDPAFDPPGEYQLPGRVVKKLTGPARQPEDLAPIDVVLLSHDQHKDNLDDAGRALLGSVPLVLSTPDAAARIDGVHGLQPWRSMQLPRPAGGTLTITGVPAQHGPDGCEPVTGVVTGFLLTADDLPTVYVSGDNASVPLVAELAERVTAGAVPGVSARSIDIAVLFAGAARTPLLDGRPLTLTSEAAAEAAHLLAAAAIVPVHTEGWAHFTEGPDHLEKTFAAAGLAARLALPTPGVPLTL
>NC_013729.1|WP_012918960.1|1363316_1364447_-|galactokinase
MTTFETVFGTAPDGVWRAPGRVNLIGEHTDYNDGLVLPIALPNQIVVSAAARADGVVAVASSGQDGVIEFSLDALEPGSVGDWAAYPAGAAWVLREAGYPIGGANLLVDSDLPSGAGLSSSAALLCATAVALLGLQEVEVDPAEVARLAQRAENSYVGAPVGLMDQMASMCCTAGHALYFDIRAMSTDQIPFDPEAEGLTLLVIDVKAPHRHVDGEYAARRKSCEQAAAVLGVPALRSIAPEDLDAALARLSDDVDRRRVRHVVTEIRRVEQAVELMRAGRLRDVGPLFTASHASLRDDFEITVPELDVAVDTALAAGALGARMTGGGFGGCIIALVETAAADRTFAAIEKAFAEHGFRTPTSLAATPSAGASRLA
>NC_013729.1|WP_012918961.1|1364443_1365490_-|galactose-1-phosphate-uridylyltransferase
MQTPRGARRTDTKLSDGRDLIYYDPADAPVRVPPADTRGLDAPKPQVQLRTDPLTGDVITYATHRNTRTYLPPADQCPLCPTKPGNPTEIPDHDYNVAVFANRFPSFAGPGRAEVVCFTSDHSKSFTDLSQGQARLVVETWADRVAELSARPDVEYIFPFENRGREIGVTLSHPHGQIYAYPFLPPRIRTLLARAREHRDATGGNLFADVLAAERTQGTRVVAENPTWTAFVPEAARWPVEVHLYPHRQVADIAELTDAERDDFAELYLNVLRRFDGLYGEPLPYIAAWHAAPVRVDRELGYLHLELLSIRRAADKIKYLAGSESGMGAFISDTRPEDVAETLRKAGS
>NC_013729.1|WP_012918962.1|1365622_1366921_+|HlyC/CorC-family-transporter
MNETLLNIVLIFVFVLIGGVFAAAEMALVSLRESQLKSIATRGRRGETVARVAANPNRFLSAVQIGVTLMGFLSAAFGGATLADGLSPHLQDLGLPPSLADTLALVLITVAISYVSIVIGELAAKRLALQRAEVFALGLAPLVDRIASAVRPVIWLLSRSTDLVVRALGGDPNANREVMTDEELRDLVSAHESLGEEERRIVDDVFEAGSRQLRELMLPRTEVDFVDAEMPAYKAVKFAAERPHSRYPVMNGSADDIVGFVHVRDLFDPAVASRSVRVGDLARDVLMLPDTAKLLPTLTEMRRRSTHLAIVLDEYGGTAGIVTLEDLVEELIGDIKDEYDEDAGETTRLRSGDVEVDGLLNLDDFADETGVELPDGPYETVAGFLAAQLGRVPAVGDEGSVDGYNITVTEMDGRRVARVRVHRVTAEEPSTS
>NC_013729.1|WP_012918963.1|1366909_1368172_-|MFS-transporter
MKDLWAVLARRRDYRLLLSADLISLTGDWVLRTGLAFHVYTLTGSTLASGGLLLASFVPLVVLGSLAGVFVDRWDRRRTMIVVNLLHVLVLLPLLAVRDEGGLWLIYLVVVTQSCLQQFFAPAEQSLVPHLVEPGQLVTANALSSQTNDIARLAGAALGGVLAATGGLPLLALVDAATYALAVLLLLRVRHRAVAVVRQRTSGALRRVKDDWVDGIRICVRSRALRIVFAFGLVTGVGEGAMSTLFAPFVSVELGGDGTAYGLIVSAQAVGGIMGGLVAAAVGGRFAAAKLWGVGAVLFGLVDLALFCYPLFWDGLAPAFALMVIVGLPGAFVVAGSMTVVQRLTDDASRGRVLGALFATEGAAVLVGITASGLLGDVVGIIPVLVAQGVGFTVGGLVVLSRSKVLGRSTAGSTATVSAG
>NC_013729.1|WP_148256885.1|1368168_1368732_-|helix-turn-helix-domain-containing-protein
MLDDPLAIRAMAHPVRLDLQALLGREGPLTAADAARRLGISQALASHHLRQLAKYDFVEPAPGKDNRERPWRLVSTSQSWRSARLTSEGAAAADVLEQLIAERALNNLAEWQQRRLQEPDILVENSGIGHTAVYLTGEELAELEEQISGLLQRYVDERPIDDKASRPPGSRLVDITRIVAVLPEYDA
>NC_013729.1|WP_012918965.1|1368945_1370181_-|serine/threonine-protein-kinase
MLVAERYRLGERLGQGGMGEVFRASDEVLGRDVALKLLLPTRRDPDATARFQREARAAATLSDPHVVTAYDFGPHDGGYFLVMELVEGRTVAEELRERGPFRADRALDVIRQAAAGLAAAHRQDIVHRDVKPGNLLLTPDGTVKITDFGIARFLTDTTTTLTATGQVLGTSFYLAPERATGQPAGKPSDIYALGCVLYQLVTGHPPFQGDQPASVMYQHVSTEPTAPSHLRPELSGPFEELLFSMLAKNPADRPTAQQIATGTTAQPVVTGELIPPAPLHPHRRRKLIGVAAALAVVAATTTGVVLETRGRELPETSNLTPATTDPSTPARPPAAKPSAKPTPVPTRPSTSTTTVSDDDDDQPVASTRVPKETDSAAAPAEDRPGKGKSKNAGKNADKGKGADKVAKSGKN
>NC_013729.1|WP_041289839.1|1370288_1371140_-|alpha/beta-fold-hydrolase
MVNETDLRLPDGRTLHVYDTHPGDDARVAVFWHHGTPNLGMPPEPLFEASDQLGLRWVSFDRPGYGGSTVAPGRTTGSVGRDVAHVADALGIGPFTVMGHSGGGSYALGCAAVLHDRVQAVVSLAGLAPYGVPGLDWFGGMIPSGVTALTAAREGREARAALDASGEQYDPEFAPVDEALFSGPWSWLGKVAGPALDAGPYGQIDDDVSYLLPWGAELDAVTAPVLLLHGGLDRIVPAAHSRWLAANLAAAELAEHPDDSHISILRHAEPALDWLRDRADQAR
>NC_013729.1|WP_012918967.1|1371380_1371758_+|hypothetical-protein
MKYVLLIHSNPQTWGHPSFLRTKEAQALPRSARDALTEQLEKLLAELTETGELVAAEPLAAPARTKVVRIRQGVRATTDGPYSEAKEQLAGVFIVDVATPERAEEIAARIPEAHFAAIELRPIEA
>NC_013729.1|WP_012918968.1|1371813_1373553_-|alpha/beta-fold-hydrolase
MTALRAGIAVASAVSLLAALNPLGSATAAEPDPLARYTGQQLSWTDCTFKPEVPTQCALMTVPRDWAAPDAGKDLKVYVSKVAATGDKGLYQGVLLTNPGGPGGQGTSMAPSIAKLQPSVNAQYDVLGMDPRGTGQTGAPGQAGLGITCQVPVGRLPEGPLDARDRSRKSISDHQQIPRVVAEACQSQADAPYITTWQTAHDMELLRQLSKAPKLNYVGYSYGSWLGAKYASLFPASTGRFVLDSSVDWQGRLQADFEDFPRMGQRQTEKLFLPWLNRMQPDVFGDTVAEAQKVIEQGRGKATALGLDPDSYDSLFAGNGSQLSWLLVMLSLTVIINGDEAGAQKLAKLPAAVRAQLDTVSRQRFGVPATKLTTAVLVKGNLGQETPDYEQLPITRFAVACGDQPTKSTQWYKRLSDWQGPKYPLFGWQYGLGEVCGPWSDTPRQTLPDLPKSVRDNVLVVQGEFDPQTSYEQAMAAVRKAPGVDVLRVDDSPFHGQYSSQGNPCVDGVVNTYLLHGSKTDNSICPSVPLLGEKQVYPVHGPVDRYADSRHAVRMPSPENSLLRALLADQISRVNSLLH
>NC_013729.1|WP_012918969.1|1373564_1373963_-|DUF805-domain-containing-protein
MRWYLTVLTKYAVFRGRAGREEFWFFTLANLIVSVLLAVADRLTGADWPAGVGPLPIGPIEGVYTVLVLLPTLAVTVRRLHDTDRSGAWLLLYLVPVIGWLVLLVLNAQAGTRGDNKYGPDPRPAGLAASTL

You can click texts colored in the table to view more detailed information

Click the colored protein region to show detailed information

Crispr_ID: NC_013729_3

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NC_013729_3

2827927-2828020

Orphan

Consensus_repeat	Method
CTCTGCCTCATCGAGCTCGCGTAGC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NC_013729_3

>merge|NC_013729|3|2827927-2828020|CRISPRCasFinder
CTCTGCCTCATCGAGCTCGCGTAGCGCGTGTCGTGCACCTCCGGTTTCGGCGTCCGGGAGGTCACCAGTCTCGGCCTCATCGAGCTCGCGTAGC

>NC_013729|3|3|2827927-2828020|CRISPRCasFinder
CTCTGCCTCATCGAGCTCGCGTAGC	GCGTGTCGTGCACCTCCGGTTTCGGCGTCCGGGAGGTCACCAGT
CTCGGCCTCATCGAGCTCGCGTAGC

Protein	Signature genes	Signature genes Name	Protein_function
NC_013729.1\|WP_041289312.1\|2833524_2833842_+\|hypothetical-protein	unknown	unknown	unknown
NC_013729.1\|WP_012920319.1\|2843105_2844098_+\|ABC-transporter-permease	unknown	unknown	gnl\|CDD\|223674
NC_013729.1\|WP_012920304.1\|2817158_2818124_+\|LysR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|176115
NC_013729.1\|WP_012920301.1\|2813894_2814809_+\|RNA-polymerase-sigma-70-factor	unknown	unknown	gnl\|CDD\|132002
NC_013729.1\|WP_012920312.1\|2831804_2833190_-\|dihydrolipoyl-dehydrogenase	unknown	unknown	gnl\|CDD\|235798
NC_013729.1\|WP_012920308.1\|2822503_2824921_+\|protein-kinase	unknown	unknown	gnl\|CDD\|270916
NC_013729.1\|WP_012920307.1\|2821661_2822384_-\|lipoyl(octanoyl)-transferase-LipB	unknown	unknown	gnl\|CDD\|184638
NC_013729.1\|WP_012920314.1\|2833946_2835440_-\|leucyl-aminopeptidase	unknown	unknown	gnl\|CDD\|234863
NC_013729.1\|WP_012920317.1\|2840199_2841207_+\|ABC-transporter-permease	unknown	unknown	gnl\|CDD\|224094
NC_013729.1\|WP_012920310.1\|2828437_2829340_-\|TIGR01777-family-protein	unknown	unknown	gnl\|CDD\|273800
NC_013729.1\|WP_049797568.1\|2813230_2813890_+\|response-regulator-transcription-factor	unknown	unknown	gnl\|CDD\|225107
NC_013729.1\|WP_148256628.1\|2818580_2820545_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|236090
NC_013729.1\|WP_158307281.1\|2836975_2839849_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|276938
NC_013729.1\|WP_012920303.1\|2815853_2817038_+\|ABC-transporter-permease	unknown	unknown	gnl\|CDD\|378925
NC_013729.1\|WP_012920299.1\|2811659_2813210_+\|sensor-histidine-kinase	unknown	unknown	gnl\|CDD\|226951
NC_013729.1\|WP_012920318.1\|2841247_2843008_+\|ABC-transporter-substrate-binding-protein	unknown	unknown	gnl\|CDD\|173871
NC_013729.1\|WP_083792976.1\|2825533_2827300_+\|DUF222-domain-containing-protein	unknown	unknown	gnl\|CDD\|367155
NC_013729.1\|WP_041289307.1\|2814975_2815857_+\|ABC-transporter-ATP-binding-protein	unknown	unknown	gnl\|CDD\|213236
NC_013729.1\|WP_012920311.1\|2829529_2831632_-\|2-oxoglutarate-dehydrogenase,-E2-component,-dihydrolipoamide-succinyltransferase	unknown	unknown	gnl\|CDD\|200219
NC_013729.1\|WP_012920315.1\|2835610_2836702_+\|glycine-cleavage-system-aminomethyltransferase-GcvT	unknown	unknown	gnl\|CDD\|234742

Protein	Function_ID	Function_description	E-value
NC_013729.1\|WP_012920319.1\|2843105_2844098_+\|ABC-transporter-permease	gnl\|CDD\|223674	COG0601, DppB, ABC-type dipeptide/oligopeptide/nickel transport systems, permease components [Amino acid transport and metabolism / Inorganic ion transport and metabolism].	2.4406e-96
NC_013729.1\|WP_012920304.1\|2817158_2818124_+\|LysR-family-transcriptional-regulator	gnl\|CDD\|176115	cd08423, PBP2_LTTR_like_6, The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional regulator, contains the type 2 periplasmic binding fold. LysR-transcriptional regulators comprise the largest family of prokaryotic transcription factor. Homologs of some of LTTRs with similar domain organizations are also found in the archaea and eukaryotic organisms. The LTTRs are composed of two functional domains joined by a linker helix involved in oligomerization: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal substrate-binding domain, which is structurally homologous to the type 2 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcriptional repressor undergoes a conformational change upon substrate binding which in turn changes the DNA binding affinity of the repressor. The genes controlled by the LTTRs have diverse functional roles including amino acid biosynthesis, CO2 fixation, antibiotic resistance, degradation of aromatic compounds, nodule formation of nitrogen-fixing bacteria, and synthesis of virulence factors, to a name a few. This substrate-binding domain shows significant homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.	4.84772e-30
NC_013729.1\|WP_012920301.1\|2813894_2814809_+\|RNA-polymerase-sigma-70-factor	gnl\|CDD\|132002	TIGR02957, putative_sigma_factor, RNA polymerase sigma-70 factor, TIGR02957 family. This group of sigma factors are members of the sigma-70 family (TIGR02937). They and appear by homology, tree building and bidirectional best hits, to represent a conserved family. This family is found in a limited number of bacterial lineages. This family includes apparent paralogous expansion in Streptomyces coelicolor A3(2), and multiple copies in Mycobacterium smegmatis MC2, Streptomyces avermitilis MA-4680 and Nocardia farcinica IFM10152.	3.84854e-115
NC_013729.1\|WP_012920312.1\|2831804_2833190_-\|dihydrolipoyl-dehydrogenase	gnl\|CDD\|235798	PRK06416, PRK06416, dihydrolipoamide dehydrogenase; Reviewed.	0
NC_013729.1\|WP_012920308.1\|2822503_2824921_+\|protein-kinase	gnl\|CDD\|270916	cd14014, STKc_PknB_like, Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.	8.54505e-28
NC_013729.1\|WP_012920307.1\|2821661_2822384_-\|lipoyl(octanoyl)-transferase-LipB	gnl\|CDD\|184638	PRK14345, PRK14345, lipoyl(octanoyl) transferase LipB.	3.59372e-126
NC_013729.1\|WP_012920314.1\|2833946_2835440_-\|leucyl-aminopeptidase	gnl\|CDD\|234863	PRK00913, PRK00913, multifunctional aminopeptidase A; Provisional.	0
NC_013729.1\|WP_012920317.1\|2840199_2841207_+\|ABC-transporter-permease	gnl\|CDD\|224094	COG1173, DppC, ABC-type dipeptide/oligopeptide/nickel transport systems, permease components [Amino acid transport and metabolism / Inorganic ion transport and metabolism].	2.80047e-80
NC_013729.1\|WP_012920310.1\|2828437_2829340_-\|TIGR01777-family-protein	gnl\|CDD\|273800	TIGR01777, Hypothetical_UPF0105_protein_Rv2216/MT2273/Mb2239., TIGR01777 family protein. This model represents a clade of proteins of unknown function including the E. coli yfcH protein. [Hypothetical proteins, Conserved].	5.80403e-107
NC_013729.1\|WP_049797568.1\|2813230_2813890_+\|response-regulator-transcription-factor	gnl\|CDD\|225107	COG2197, CitB, Response regulator containing a CheY-like receiver domain and an HTH DNA-binding domain [Signal transduction mechanisms / Transcription].	8.02043e-71
NC_013729.1\|WP_148256628.1\|2818580_2820545_-\|hypothetical-protein	gnl\|CDD\|236090	PRK07764, PRK07764, DNA polymerase III subunits gamma and tau; Validated.	3.53943e-09
NC_013729.1\|WP_158307281.1\|2836975_2839849_+\|hypothetical-protein	gnl\|CDD\|276938	cd15831, BTAD, Bacterial Transcriptional Activation (BTA) domain. The Bacterial Transcriptional Activation (BTA) domain is present in the putative transcriptional regulator Mycobacterium EmbR and the related Streptomyces antibiotic regulatory protein (SARP) family of transcription factors, which includes DnrI and AfsR, among others. Members of this family contain an N-terminal DNA-binding domain, followed by the BTA domain, and many have diverse domains at the C-terminus. EmbR contains an C-terminal forkhead-associated (FHA) domain, which mediates binding to threonine-phosphorylated sites in a sequence-specific manner. The BTA domain of EmbR contains three Tetratricopeptide repeats (TPRs) and two C-terminal helices. The TPR motif typically contains 34 amino acids, and 5 or 6 tandem repeats of the motif generate a right-handed helical structure with an amphipathic channel that is thought to accommodate an alpha-helix of a target protein.	3.17423e-32
NC_013729.1\|WP_012920303.1\|2815853_2817038_+\|ABC-transporter-permease	gnl\|CDD\|378925	pfam12698, ABC2_membrane_3, ABC-2 family transporter protein. This family is related to the ABC-2 membrane transporter family pfam01061.	1.61232e-26
NC_013729.1\|WP_012920299.1\|2811659_2813210_+\|sensor-histidine-kinase	gnl\|CDD\|226951	COG4585, COG4585, Signal transduction histidine kinase [Signal transduction mechanisms].	2.50997e-44
NC_013729.1\|WP_012920318.1\|2841247_2843008_+\|ABC-transporter-substrate-binding-protein	gnl\|CDD\|173871	cd08506, PBP2_clavulanate_OppA2, The substrate-binding domain of an oligopeptide binding protein (OppA2) from the biosynthesis pathway of the beta-lactamase inhibitor clavulanic acid contains the type 2 periplasmic binding fold. Clavulanic acid (CA), a clinically important beta-lactamase inhibitor, is one of a family of clavams produced as secondary metabolites by fermentation of Streptomyces clavuligeru. The biosynthesis of CA proceeds via multiple steps from the precursors, glyceraldehyde-3-phosphate and arginine. CA possesses a characteristic (3R,5R) stereochemistry essential for reaction with penicillin-binding proteins and beta-lactamases. Two genes (oppA1 and oppA2) in the clavulanic acid gene cluster encode oligopeptide-binding proteins that are required for CA biosynthesis. OppA1/2 is involved in the binding and transport of peptides across the cell membrane of Streptomyces clavuligerus. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains 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. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction.	1.26077e-107
NC_013729.1\|WP_083792976.1\|2825533_2827300_+\|DUF222-domain-containing-protein	gnl\|CDD\|367155	pfam02720, DUF222, Domain of unknown function (DUF222). This family is often found associated to the N-terminus of the HNH endonuclease domain pfam01844. The function of this domain is uncertain. This family has been called the 13E12 repeat family.	5.03533e-20
NC_013729.1\|WP_041289307.1\|2814975_2815857_+\|ABC-transporter-ATP-binding-protein	gnl\|CDD\|213236	cd03269, ABC_putative_ATPase, ATP-binding cassette domain of an uncharacterized transporter. This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.	1.43003e-95
NC_013729.1\|WP_012920311.1\|2829529_2831632_-\|2-oxoglutarate-dehydrogenase,-E2-component,-dihydrolipoamide-succinyltransferase	gnl\|CDD\|200219	TIGR02927, putative_dihydrolipoamide_acyltransferase, 2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase. This model represents an Actinobacterial clade of E2 enzyme, a component of the 2-oxoglutarate dehydrogenase complex involved in the TCA cycle. These proteins have multiple domains including the catalytic domain (pfam00198), one or two biotin domains (pfam00364) and an E3-component binding domain (pfam02817).	0
NC_013729.1\|WP_012920315.1\|2835610_2836702_+\|glycine-cleavage-system-aminomethyltransferase-GcvT	gnl\|CDD\|234742	PRK00389, gcvT, glycine cleavage system aminomethyltransferase GcvT.	0

>NC_013729.1|WP_083792976.1|2825533_2827300_+|DUF222-domain-containing-protein
MLTALDTVHADISRLQTYRLELLAALDANGHAAEFGARDTAHLISTRHRLDPTDVRRDLRLATALPKYDTVRASLSPFTPSDPGSTAPLHPGQAEAIVTALERIPTTARVPVENLKVAEQELVKAAHVLSPADLRRLGKRVRDTLDTDGPEPAEARALAAETLWLKRGDLGTEFGGYLAGANAELLHTLILAGAKPHKTVDGHRDPRSRGKRQADALTTILTTAAATGTAAPSHGDIKPHVTVTIALNDLATATGTGTLASGTTLSAGAIRRLACDAGLIPIVLGTDSEPLDVGTHHRFVTRPIRHALNARDKGCIICTAPPAMCEAHHIVHWANGGPTALTNLALLCRPHHTDVHQGHYTLTTHNGRPHYTRPGWADPPPAHPRPSSDDSLPTSASLTHPSPSRASRQVAPARPSTGQVVLGRPSGGQIPLAGAPNGVVAPARASSALATSAGASSGLATSAGASVEEVAPGGRSGGRTAPVGSSSGHVVFTRASVGQVASADQVVLGGRSGGLVAPARSSGGEVASAGGLGGLVAKACLPGGPASVAPVAPAQAATAQGSRAQASPTSRPPPTLAGDRLTHGSAQA
>NC_013729.1|WP_012920308.1|2822503_2824921_+|protein-kinase
MALEDISGYSLRRRLGSGSAGTVWLVRDLASGRHAVLKRIPATAADSPATLDRDLSVLKAIQHPHIARLIEVRHSGPDRLLFTQYVPAGTLTALLERRGDLSLGELVTLVNPLADALATLHQAGLHHGRLTADNIMFDADGRPVITDAALHHLAPAATPADDLTALATLTYQAGGDPTTFPAELFTQPAPTLARQVLALAPPRALNLAFERTSIATAVDSSSTAATDTAPAPTPLNATPTTTRATPTTFSTAAPTAAGNATNPSVESAAINPHPADEPLTTGSTLDPLRALTVRRFPINSSRPQSASAHPSTPRPFAHPRPALAAQPPTNDPVRPTPAEYRPTPPGLTPAEPPATASAFATESQRPTPAPHSTPAASTGQRPTPAPDSSSTTTADQRSAPTPSFPPDRLSQRHTPPFDFADAHLASETPTPASDLSRVHPAIHGPTPAFGFGGADPASETPTPASGLGDVPADPRPTPTPGFGHADPTNHRSTPASDSPNAERAREPASFLPQFSPALHPNALPPTDAVTFLAPPADAPTRPSPTGRPSRSTRHRKRSTRTSHRTPSRTPRRDTNRRAHRDTTNRLSQILAASRRVPPSRRNAYGILAMAALAAVIVLAVALTTLGVFKTPTTNPAAASPPSPTPPPAPSASTTSSSAAPPPATPVSTPTTTPAMPSAPGDRTWLQTLQSLDNRRAHAFWTLNPTELDAVYSPGSRPWTADRALLASYKSQNVRISNLRLQIQHLQQEPGPGPTITLKVTDRLISATAHTRTGQRTQLAPGPPTTRRITLTPHGKTWRITTIAPA
>NC_013729.1|WP_012920307.1|2821661_2822384_-|lipoyl(octanoyl)-transferase-LipB
MRVIKYVEAGFGAEAVDYEQAWAEQRKLHTAVVEGSGEDTVILLEHPPVYTAGKRTEAHERPMDGTPVVDVDRGGKITWHGPGQLVGYPIVKLASHVYVVDYVRRLEEALIAVCAELGVRTGRVKGRSGVWVPADERGRERKIAAIGIRVAQGVTMHGFALNCDNDLAWFDRIVPCGISDADVTTLSKELGRDVSVGEVLPTVRRELDRMLAWEEYERTPDLDHVDAAPAGITYGLAVTP
>NC_013729.1|WP_148256628.1|2818580_2820545_-|hypothetical-protein
MWGKRRYGGDVSKFLGFLLGIVVAVAGPAAFGVLTADGGIELNAKEMALAYGIGALFFWLVVSYFSGAAALGAALTFGAMIYAVHWIPNRTTNFLNDVPGVTTGMIDGIKQYTLNGLVPVLAVISLVYAIQLITRAVRRRRAARAEAARRQREQELAQAQQEAEVAAVYPAAAGNDYPAAGENRFANFGNSGYDDPFEAEPAAIQPRSQADEQTMQFPNSGVRAERDDTAVVGAAGNERAERATQVPAGADETQMMPVDRDETVVSPVTSADGADKGGKDGGGSAAAAPVVAGATAAGVAGAAAAGVAGAGVAGAAVAKESAAAGVSSRAETQVGAERAEAATTEPKDAPESVAPLAESTVAPENVKASEEMTVSPEAAKPAGETTVAPEPVKASEETKVAEASETVATPRAVERPELAGTAQSAGTPQSAGTPQSAGTPQSVGTATVAGEPTVVEARHAAPVPPTAEVPPASQAGVVADSAEPAAGSGVPARAADHETVVDDKPQATAEATKPSEQTVGAETRPMESVQPTEATEQSAGTETQPLESVQPMESAQPIESSEPTESVRPSETGQASEGAKPDGAAGPTASLGVAGFGQSNEEVGQQYRERMDGPDPEDTGEFFVDAFETPQHGGQPVAAPGMMEFPGQFRPAGA
>NC_013729.1|WP_012920304.1|2817158_2818124_+|LysR-family-transcriptional-regulator
MNVELRHLRVVVLVAEAGSVGRAARWLKVSQPSLTAQLKRIESAFGGELFERSRTGVTPTPLGRYAVERARAILVDVDHLSATVSAMTAVQSSAVRLGGFPTAPMSGIASRLRDHGEIEQVSIEVEWATSVLLQQLESGRLDFALLREFPGFELRLPTGVNARTIVDSESAYVVMAADHPLAVASRHRGEIDLADLAGEEWIGEPPDDSGFHVLFRSACEQAGFTPRVEHHSVDTSVVMGFVTSGQGVALISPTSYRMLSSEVTTRRLVGDPFHRRLLLAWSTESPRAPMAPEVCQMAVQAYDEAFAEHARWGQRQRMHVA
>NC_013729.1|WP_012920303.1|2815853_2817038_+|ABC-transporter-permease
MSTQQRSTTLRHPWQLVAHREISTKLRDKTFIGSTLFMLILVLAAVVIPALLAGNNDPDKIAVLDDSGAKVVQVADAINGGGAFEVTRVADRAAAEKAVTDGDAEAALLPADTGFVVLGDDKVDSDTQNSLREAVVNLGMEQNAAKAGLTPEQLRANTTVEEQLLNPGPLPEVVAGFVNIGLALAFYMTALGFGMMIAQSVVQEKESRVVEILAAAVPIRALLWGKVIGNTVLALGQIVVIAAASLIGLVLTDQADILEVVAPVAGWFVVFFVLGFLALAGLWAVAGSLATRQEDLGSTTLPGQMILMLPFFFSVFAGPSAKAVASFVPIASSMAMPGRMLTEDVPVWQPLVAIVLLLVATVLIVRLGARLYERTLLQTGRKLGYREAMALKPS
>NC_013729.1|WP_041289307.1|2814975_2815857_+|ABC-transporter-ATP-binding-protein
MLSVAGLTRRFGDHLALDDVTFDVVPGRMTGFVGANGAGKTTTMRIMLGVLAATAGEVHWNGAPLTHEIRRDFGYMPEERGLYPKMKIRDQLVFFGRLHGQDPNRAAERTDKILDRLGLTERAGDMLETLSLGNQQRVQIAAALVHEPIALVLDEPFSGLDPLAVDAMVDLLREEVTPEVPVLFSSHQLELVERLCDDLVVLSRGKVVAAGPVAELAAGPSATYRLVTDGDAGWLRDVGGITVRDVAGATALFDVTEAGQEQQVLQQAMSRGQVLEFGPERVALSDVFREATR
>NC_013729.1|WP_012920301.1|2813894_2814809_+|RNA-polymerase-sigma-70-factor
MPSIADPSAEPHPPDSDLEQAARVFAEVRPRLFGIAYRMLSSAAEAEDLVQEVWLRWQTCDRSAVTNPAAYLATTTTRLAINAIQSARVRRETYVGPWLPEPVDTSADPYLGAERGDALELAVLVLLERLKPNERAAYVLREAFDYPYPQIAEILQLHEPAVRQLVSRARKRVTSDRRTPVSEPEQRQLLSAFISAARSGDLAALENLFAAGVSSYSDGGGVVRAARIPVHGADRVAKFVRAFAGHFWGGIEVEWRTLNGRQAALLRRDGVLAAVVSVDASADGIEQIMWLMNPDKLEALAGTG
>NC_013729.1|WP_049797568.1|2813230_2813890_+|response-regulator-transcription-factor
MRVLLVDDQDLVRAGFRMILSVEQDIEVVGEAADGEKAVELALDLRPDVVLMDVQMPGLDGIAATQRIVAADAGKVVILTTFDRDDYLFESLGAGASGFLLKNTAPEDLVEAIQVVHSGHALLAPEVTRRVIKRFAGGGERVYRPDLVAELTDREREVLGLIARGLTNTEIAGQLFVGEATVKTHVSRVLLKLGLRDRVQAVVFAYECGLVVPGDDATS
>NC_013729.1|WP_012920299.1|2811659_2813210_+|sensor-histidine-kinase
MVSLRRSGAAPDAEAPAASGTTVSEPGTPPTTGVRAAGWERPGPTPQQRRDDVVLGLGLAMVSVIGTELARGSYPTPVDLGIGGVEPYVLSVLVTLPLCFRRRFPLTVLLVVSVLFVVAGERTLFAFAGNLVTQATQFMAIYAAAAWAKDRRRMKLAVVVVFVAMFCWLFYGFVQALRNDAIKGANDGLLSPYVSYVVLNFGVNVAYFFGAYFWGRTAWGVARQRHELEAQAAELARQQQTNARRAVIDERLRISRELHDVVAHHISSIGIQAGGARRVMESDPAAAKNALSVIENSSRTAVNEMRQLLGMLRAADPDLDDEELGVAAHKAPQAGADRLPALVVEAGGEGLEIGFHQIGRPVKLPETVSVSVYRIAQEALTNVRRHSTARTAHVTLRYLDETAVEVEVIDDGRPKHAPVGSRLGHVGIRERVALLGGESEIGPRPVGGFRVRARIPLTTPVPVEAGGGDSPPTPSADGVPAPAEGAAPRLAPPADGGEPVDGETDRPVQQSEGATQ
>NC_013729.1|WP_012920310.1|2828437_2829340_-|TIGR01777-family-protein
MKYVLAGSSGFLGQALTQDLRANGHEVTRLVRRTPSAPDELQWDPFTGRIDHTALEDADVLINLAGANIGRPWTPTYRATIRESRVRTTATLAEAAARLDNRPVFITQSGIGGYGTDCGGRILTEDSPLGDGFLADVVRVWEGAADPARTAGCRVVSFRTGIVLARQAPAFQLLSLPFRLGLGGRLGSGTQYFPVISLIDWLRAIRHTATTSTITGPVNVTLPTPTTNAAFTKALAAALHRPAILPIPAPALTTALGEFAWELLGSKRALPQALQSTGFTFTHPTTPEALAATLTHQHQH
>NC_013729.1|WP_012920311.1|2829529_2831632_-|2-oxoglutarate-dehydrogenase,-E2-component,-dihydrolipoamide-succinyltransferase
MPTSVSLPALGESVTEGTVTRWLKQVGDTVAVDEPLLEVSTDKVDTEIPSPVAGTLLEIKAAEDETVEVGAELAVIGDAGESSGSSSDAGSSDAAADASSGDAAQAQQAPAAEPQAASTESQAPAAEAQDSGAEASYSGSGSGAQDTDAAPAAQDPAQQAATDQASSSADASSGSATSSAPADTQSSGGGGTSVTLPALGESVTEGTVTRWLKQVGDDVAVDEPLLEVSTDKVDTEIPSPVAGKLLEIKVAEDETVEVGAELAVVGSADAAPAQAAPQQQAPQAEAPQAAPAQQSAPAQQAPAQQAPAAQAAPAQQAPAAQPASQAPAAQPAAQAPAAQPAAQAPAAQPAAQAPAPQAASAQTSSPAASAAPQASAPAASAPASATASSNGSSTDAPNYVTPLVRKLAAEHGVDLNAVQGTGVGGRIRKQDVLAAAEAKKAAPAAAAPAAASSGAPQAATPVSPLRGTTEKMSRIRKAIASHMVNSLKVSAQLTTVVEVDVTEIAKLRNAKKAEFEAREGVKLSFLPFFALAAVDALKQYPKLNASIDDEKGEVTYHAAEHLGIAVDAEKGLMVPVVHNAGDLNIAGLAKKIADLAARTRTNKVLPDEMAGGTFTITNTGSRGALFDTPILNQPQVGMLGTGAVVKRPVVITHPELGETIAIRQMVYLALTYDHRLVDGADAARYLTAVKQRLEEAQFDV
>NC_013729.1|WP_012920312.1|2831804_2833190_-|dihydrolipoyl-dehydrogenase
MTNPADSTTFDLVILGGGSGGYAAALRAAVLGLSVALVEKDKLGGTCLHRGCIPTKALLHAAEVADSAREGEQFGVRTTLEGVDMGGVNKYKDGVVDRLFKGLQGQIKARGITVVEGEGRLTSPTTVEVAGTTYTGRNVVIASGSYSRSLPGLELDGQRVIASEHALTLDRVPESAVILGGGVIGVEFASAWTSFGTKVTIVEALPRLVPAEDADCSKTLERAFRKRKIAFKTGTPFESVEVVDNGVRVTVAGGEVIEAEVLLVAVGRGPNTAGLGYEEVGVTLDRGFVTVDEHLQTSVPGVYAVGDIVPGLQLAHRGFQQGIFVAEHIAGLNPAPIDEAGIPRVTYSEPEVASVGLTEEQARAKYGEVEILNYNLGGNGKSQILKTQGFVKLVRAKDGAVVGLHMVGSRVGELIGEAQLIYNWEAFPADVAPLVHAHPTQNEALGEAHLALAGKPLHFHE
>NC_013729.1|WP_041289312.1|2833524_2833842_+|hypothetical-protein
MKWFGRRQKPGTMRKSDTPDQAHLREFVQTRQGVEGFVEPRTAVTEYTMLLVAVDGEWTRRRVPSVEWAHNFANKLGIPSYDAAVVGYPPRMREYNARQKKNGLA
>NC_013729.1|WP_012920314.1|2833946_2835440_-|leucyl-aminopeptidase
MSTITLSKSDAAGVKTDVVVIGVVKLDGGVALPAGTESLNAAYDGRLVEVLSGLGATGKAGEVTKVPGPKPGRSATLIAVGLGAAPDGALKTEDLRIAAGVGVRAAKTAQSVAFALPTPDTDCLRAVAEGALIGRYTYNTYKSEAPTDAPGNLTVLTDLARSKETKAALERAQVVADAVHQTRDWVNMPPSDLHPAEFAAQVQKLAKEYGVKVEVLDEKALARGGYGGILGVGQGSDNPPRLVRLSYTPKKPVTHLAYVGKGITFDSGGLSLKTASGMISMKADMAGAAAVVAATLAIARLGLPVQVTTYAAMAENMPSGSAARPSDVLTMYGGKTVEVLNTDAEGRLVLGDALVRASEDQPDLIVDVATLTGACVVALGAKVAGAFGNTDTARDRVVDAAVAAGEAMWPLPIPSEMLDKLRSHSKVADLANITGEPWGGALAAAAFLGDFVADGIDWVHLDVAGPAFNDGGASGYTPTGGTGYAVRTLVELAAAAS
>NC_013729.1|WP_012920315.1|2835610_2836702_+|glycine-cleavage-system-aminomethyltransferase-GcvT
MTSLKKSPLHERHVALGAKFAEFGGWEMPLEYSGVVAEHTAVRTSVGVFDVSHLGKARVVGPGAAAYVNSCLTNDLGKIGPGQAQYTLCCAEDGGVVDDLIAYLHADNDVFLIPNAANTAEVVRRLQADAPAGVEVTNTHDDYAILAVQGRNSDEVVGAIGLPTGHDYMAFAVAEYAGTPVVVCRTGYTGERGYELVIPNDAAVAVFDALLAAGEAYGIVPAGLGARDTLRTEMGYPLHGQDISPQITPVQARSGWAVGWKKQRFWGDQALRAEKEAGPAKILRGLRAVGRGIPRPHMTVADADGTALGEVTSGTFSPTLKKGVALALLDARVKEGDQVTVDIRGRQEPFEVVKPPFVTVNVR
>NC_013729.1|WP_158307281.1|2836975_2839849_+|hypothetical-protein
MEFRLLGPVQIWSAGQQVELKRRQERLLLAVLLLEPGKAVPAERLIELLWPEELPGSPKRALQVYMSRLRNVLAAGDSRLLSGPHGYAVETPRGRTDVELFAALVEQAKPLDDLEQRRKLLIDALALWRGPALADVASEDVRRRLCAGLDESRWAAQELRLTTELALGRHQDLLPELAELTEAQPTRESLTAARMLALYRSGRQTDALAVYADLVRHLSDELGVQPGSEVRDLQVAILRQDESLDYTAPTRGPRELPADIAVLVGRDALLHELAAVLRPQRRPSGLPAVVCLYGAAGTGKSAAAIRLGHELAGEYPDGQLFARLQDVDGEPVPPAVLLGRLLRSLGVDSVPDAVEERAALLRSTLAGKSVLTVFDDAADVGQLRPLLPADGRCAVVVTSRRPLLGLEDATHRELLPLGSATSAQLLAELSGRPAGELQPLVEYCVGLPLALRIVGARLSLIREDIADVVRTLADETRRLDYLVAGDRAVRASLDLTLRTASPTARRLFGCLALVTADEFSAWVAAPLLDLDESLAGTVLDELLSLGLVQLRRTAPATYGLHALVRARAVEELAGFSADDREMIELRYLQAVLRLLTIAEDQVGQNAYRGLEYDQGEGRPLPEADAAAAAGPAWLDVEAPVVLAAVRLAAGRPRLAAMLAMRLDDYLLVRDQREMRETALALAESATAGGDPMLEAEVLRRLFAAKAQGAAGMDELTALAGRARDVAARSGHPDMQALALGQVAYVTSSDTNYEAVVEVAEQILALADRCTDPAAVKLRALDWLSAGLAGLGRLPEAIAAKRRIRQLSTPGTRVHAIRLVLLALTLTRGEHQGAEHLDELAEIAVEARQIVDRIGDELGQAHVGLVEARLSMVRGDLAGANERLDAVAAMFAERPDAWGDVNLRITRAWVAIRGGRRNEGLRMLADGMEAVSPVDYPAAASVLREQLEVARRETSHSA
>NC_013729.1|WP_012920317.1|2840199_2841207_+|ABC-transporter-permease
MSIGSPDSTVGVEDHPASAEPVRDATVAHGKSPTRIAMDRLRKDRVAMTCLGVVLFFILIAIFAPVLAKLEGGDVSTFQPDLVDEYGFPVIGMNSEHWFGVEPKTGRDNFARWVYGARPSLIVAFVATLVGTVVGVVMGLLAGFLGGWVDRIISWFIDFVLSLPYLLFAIAMVPIVESLRGGSFNLSPEEQASTRFFVLIFVLSFFGWAGLARIIRGEVLSLREREFVLAAKAIGVPTRQVLFKELLPNLVAPIVISASLALPAYVTAEAGLSFLGVGLIEPIPSWGQTIATATNWFKADPVYLWLPVIGITALVLALALLGDAVRDAFDPKTRR
>NC_013729.1|WP_012920318.1|2841247_2843008_+|ABC-transporter-substrate-binding-protein
MQWKRITAVAATVMLTVAACGSPSSNNNTGGSNTGDAGTAQEKATDPSVKGPAPEIEGAKKGGTITVLSDVTPDTFDPTNIYYTDGNQIGKLIYRALTQYKLDEKTGKPILVPDLAEDLGTKSADGLTWTFKLKQGIKYMDGTEVKAEDYAYAIKRSFAHDLYDAGPTYQLQFFKDGDKYKGPYAAGGDNYAGVETPDNSTLVIKLAKKFDDLPFYAAFPMFTPIPKAKDTKKNYEQKPMTTGPYQVESLTPGSQLVLSKNPNWDPNTDPVRYQYPDKFDFKFAQDTIKVQRQVLASSGPDANALNYSNLDVSLYPEVKDQSQIIKGGSPCTITWPLDTRKIPFEIRQLIAKAYPFDSWRKVAGLDPQSAIPASTILPPAVPGHEKYELPGLVGKGKGAEDEAVAAEVKAKLKELGKENFELSWYYSNDDKIATQVNQLRTQVFQKAGFKVKAIGVPKAKIRTLTGDQNAPVNVGKTPAGWCSDWPSGTSWFPVLFKSDAIALGNSIGQLQDKALDAEIDRIAAMDPNQQLKEWSKVDRTVLEKHLPLVPLYYAASAFPVGKNIGHAINDVTQGMPEFTSLYLKQP
>NC_013729.1|WP_012920319.1|2843105_2844098_+|ABC-transporter-permease
MLYFVARRLVSALSVVLVTLIATFTLFFVAPTDPAAAICGERNCTAERYNEIKESLHLDRPKVQQFAEYTAGIFVGRTFEASGSTRECAAPCLGYSFKNDQPVTEMLKTRLPVTVSLVAGYAVLVLTIGVFVGSMAAKRRGSLGDRALMSSTLILSSVPYYIVALMISLYFTILYPILPRGGYTPLTDNPAKWFMGFLTPWLVLGLYFCTSYARYSRGSMVETLSEDYIRTARAKGLSDRKVTYKHALRSGLIPVITIFGLDVAGSLAGAIFTERIFDLPGIGNLVLSSLQNYDLPVIMGTVLIASGVLVTMNFLVDIAYSVVDPRVRLA

You can click texts colored in the table to view more detailed information

Click the colored protein region to show detailed information

Crispr_ID: NC_013729_4

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NC_013729_4

3329292-3329386

Orphan

Consensus_repeat	Method
GGTGGGTCAAAGGCGGGCGGCGG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NC_013729_4

>merge|NC_013729|4|3329292-3329386|CRISPRCasFinder
GGTGGGTCAAAGGCGGGCGGCGGTTTGCCCGGGCAGGTGGGGCCAGAGGCGGGTGGCGGTTTGCGCCGGGCAGGTGGGTCAGAGGCGGGCGGCGG

>NC_013729|4|4|3329292-3329386|CRISPRCasFinder
GGTGGGTCAAAGGCGGGCGGCGG	TTTGCCCGGGCAGGTGGGGCCAGAGGCGGGTGGCGGTTTGCGCCGGGCA
GGTGGGTCAGAGGCGGGCGGCGG

Protein	Signature genes	Signature genes Name	Protein_function
NC_013729.1\|WP_041289338.1\|3344832_3346191_+\|cobyrinate-a,c-diamide-synthase	unknown	unknown	gnl\|CDD\|234896
NC_013729.1\|WP_012920729.1\|3322029_3323097_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|370676
NC_013729.1\|WP_012920742.1\|3338908_3339667_+\|5'/3'-nucleotidase-SurE	unknown	unknown	gnl\|CDD\|234732
NC_013729.1\|WP_012920740.1\|3333843_3334818_+\|DUF3500-domain-containing-protein	unknown	unknown	gnl\|CDD\|378789
NC_013729.1\|WP_012920731.1\|3324168_3324960_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|223021
NC_013729.1\|WP_012920728.1\|3320821_3322033_+\|PrsW-family-intramembrane-metalloprotease	unknown	unknown	gnl\|CDD\|379143
NC_013729.1\|WP_012920737.1\|3331311_3332124_-\|serine-hydrolase	unknown	unknown	gnl\|CDD\|379138
NC_013729.1\|WP_012920739.1\|3333172_3333853_+\|phosphoglycerate-mutase-family-protein	unknown	unknown	gnl\|CDD\|214859
NC_013729.1\|WP_012920738.1\|3332207_3333176_+\|cobalamin-biosynthesis-protein	unknown	unknown	gnl\|CDD\|234919
NC_013729.1\|WP_012920743.1\|3339835_3340666_-\|hypothetical-protein	unknown	unknown	unknown
NC_013729.1\|WP_012920730.1\|3323093_3324128_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|237537
NC_013729.1\|WP_148256648.1\|3327617_3328922_+\|TerC/Alx-family-metal-homeostasis-membrane-protein	unknown	unknown	gnl\|CDD\|274743
NC_013729.1\|WP_041290144.1\|3335062_3338791_+\|cobaltochelatase-subunit-CobN	unknown	unknown	gnl\|CDD\|235663
NC_013729.1\|WP_041290142.1\|3327171_3327522_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|225197
NC_013729.1\|WP_012920727.1\|3320062_3320683_+\|dephospho-CoA-kinase	unknown	unknown	gnl\|CDD\|179560
NC_013729.1\|WP_148256977.1\|3330238_3331306_-\|dipeptide-epimerase	unknown	unknown	gnl\|CDD\|239435
NC_013729.1\|WP_012920732.1\|3325030_3327136_+\|excinuclease-ABC-subunit-UvrB	unknown	unknown	gnl\|CDD\|235395
NC_013729.1\|WP_012920745.1\|3344224_3344839_+\|cob(I)yrinic-acid-a,c-diamide-adenosyltransferase	unknown	unknown	gnl\|CDD\|235662
NC_013729.1\|WP_049797350.1\|3317172_3319932_-\|tetratricopeptide-repeat-protein	unknown	unknown	gnl\|CDD\|276938
NC_013729.1\|WP_083792860.1\|3316904_3317135_+\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|273701

Protein	Function_ID	Function_description	E-value
NC_013729.1\|WP_041289338.1\|3344832_3346191_+\|cobyrinate-a,c-diamide-synthase	gnl\|CDD\|234896	PRK01077, PRK01077, cobyrinate a,c-diamide synthase.	0
NC_013729.1\|WP_012920729.1\|3322029_3323097_+\|hypothetical-protein	gnl\|CDD\|370676	pfam09770, PAT1, Topoisomerase II-associated protein PAT1. Members of this family are necessary for accurate chromosome transmission during cell division.	1.07934e-15
NC_013729.1\|WP_012920742.1\|3338908_3339667_+\|5'/3'-nucleotidase-SurE	gnl\|CDD\|234732	PRK00346, surE, 5'(3')-nucleotidase/polyphosphatase; Provisional.	1.79307e-60
NC_013729.1\|WP_012920740.1\|3333843_3334818_+\|DUF3500-domain-containing-protein	gnl\|CDD\|378789	pfam12006, DUF3500, Protein of unknown function (DUF3500). This family of proteins is functionally uncharacterized. This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 335 to 438 amino acids in length. This protein has a conserved GHH sequence motif. This protein has two completely conserved G residues that may be functionally important.	1.81866e-111
NC_013729.1\|WP_012920731.1\|3324168_3324960_+\|hypothetical-protein	gnl\|CDD\|223021	PHA03247, PHA03247, large tegument protein UL36; Provisional.	0.00417937
NC_013729.1\|WP_012920728.1\|3320821_3322033_+\|PrsW-family-intramembrane-metalloprotease	gnl\|CDD\|379143	pfam13367, PrsW-protease, Protease prsW family. This is a family of putative peptidases, possibly belonging to the MEROPS M79 family. PrsW, appears to be a member of a widespread family of membrane proteins that includes at least one previously known protease. PrsW appears to be responsible for Site-1 cleavage of the RsiW anti-sigma factor, the cognate anti-sigma factor, and it senses antimicrobial peptides that damage the cell membrane and other agents that cause cell envelope stress, The three acidic residues, E75, E76 and E95 in Aflv_1074, appear to be crucial since their mutation to alanine renders the protein inactive. Based on predictions of the bioinformatics programme TMHMM it is likely that these residues are located on the extracytoplasmic face of PrsW placing them in a position to act as a sensor for cell envelope stress.	1.11418e-07
NC_013729.1\|WP_012920737.1\|3331311_3332124_-\|serine-hydrolase	gnl\|CDD\|379138	pfam13354, Beta-lactamase2, Beta-lactamase enzyme family. This family is closely related to Beta-lactamase, pfam00144, the serine beta-lactamase-like superfamily, which contains the distantly related pfam00905 and PF00768 D-alanyl-D-alanine carboxypeptidase.	6.23305e-38
NC_013729.1\|WP_012920739.1\|3333172_3333853_+\|phosphoglycerate-mutase-family-protein	gnl\|CDD\|214859	smart00855, PGAM, Phosphoglycerate mutase family. Phosphoglycerate mutase (PGAM) and bisphosphoglycerate mutase (BPGM) are structurally related enzymes that catalyse reactions involving the transfer of phospho groups between the three carbon atoms of phosphoglycerate... Both enzymes can catalyse three different reactions with different specificities, the isomerization of 2-phosphoglycerate (2-PGA) to 3-phosphoglycerate (3-PGA) with 2,3-diphosphoglycerate (2,3-DPG) as the primer of the reaction, the synthesis of 2,3-DPG from 1,3-DPG with 3-PGA as a primer and the degradation of 2,3-DPG to 3-PGA (phosphatase activity). In mammals, PGAM is a dimeric protein with two isoforms, the M (muscle) and B (brain) forms. In yeast, PGAM is a tetrameric protein.	1.65481e-34
NC_013729.1\|WP_012920738.1\|3332207_3333176_+\|cobalamin-biosynthesis-protein	gnl\|CDD\|234919	PRK01209, cobD, cobalamin biosynthesis protein.	3.68724e-110
NC_013729.1\|WP_012920730.1\|3323093_3324128_+\|hypothetical-protein	gnl\|CDD\|237537	PRK13875, PRK13875, conjugal transfer protein TrbL; Provisional.	1.83563e-06
NC_013729.1\|WP_148256648.1\|3327617_3328922_+\|TerC/Alx-family-metal-homeostasis-membrane-protein	gnl\|CDD\|274743	TIGR03718, R_switched_Alx, integral membrane protein, TerC family. Rfam model RF00080 describes a structured RNA element called the yybP-ykoY leader, or SraF, which may precede one or several genes in a genome. Members of this highly hydrophobic protein family often are preceded by a yybP-ykoY leader, which may serve as a riboswitch. From the larger group of TerC homologs (pfam03741), this subfamily contains TerC itself from Alcaligenes sp. plasmid IncHI2 pMER610 and from Proteus mirabilis. It also contains the alkaline-inducible E. coli protein Alx, which unlike the two TerC examples is preceded by a yybP-ykoY leader.	4.44717e-143
NC_013729.1\|WP_041290144.1\|3335062_3338791_+\|cobaltochelatase-subunit-CobN	gnl\|CDD\|235663	PRK05989, cobN, cobaltochelatase subunit CobN; Reviewed.	0
NC_013729.1\|WP_041290142.1\|3327171_3327522_+\|hypothetical-protein	gnl\|CDD\|225197	COG2315, MmcQ, Uncharacterized protein conserved in bacteria [Function unknown].	9.31591e-28
NC_013729.1\|WP_012920727.1\|3320062_3320683_+\|dephospho-CoA-kinase	gnl\|CDD\|179560	PRK03333, coaE, dephospho-CoA kinase/protein folding accessory domain-containing protein; Provisional.	1.80883e-87
NC_013729.1\|WP_148256977.1\|3330238_3331306_-\|dipeptide-epimerase	gnl\|CDD\|239435	cd03319, L-Ala-DL-Glu_epimerase, L-Ala-D/L-Glu epimerase catalyzes the epimerization of L-Ala-D/L-Glu and other dipeptides. The genomic context and the substrate specificity of characterized members of this family from E.coli and B.subtilis indicates a possible role in the metabolism of the murein peptide of peptidoglycan, of which L-Ala-D-Glu is a component. L-Ala-D/L-Glu epimerase is a member of the enolase-superfamily, which is characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.	5.32452e-94
NC_013729.1\|WP_012920732.1\|3325030_3327136_+\|excinuclease-ABC-subunit-UvrB	gnl\|CDD\|235395	PRK05298, PRK05298, excinuclease ABC subunit UvrB.	0
NC_013729.1\|WP_012920745.1\|3344224_3344839_+\|cob(I)yrinic-acid-a,c-diamide-adenosyltransferase	gnl\|CDD\|235662	PRK05986, PRK05986, cob(I)yrinic acid a,c-diamide adenosyltransferase.	4.5803e-113
NC_013729.1\|WP_049797350.1\|3317172_3319932_-\|tetratricopeptide-repeat-protein	gnl\|CDD\|276938	cd15831, BTAD, Bacterial Transcriptional Activation (BTA) domain. The Bacterial Transcriptional Activation (BTA) domain is present in the putative transcriptional regulator Mycobacterium EmbR and the related Streptomyces antibiotic regulatory protein (SARP) family of transcription factors, which includes DnrI and AfsR, among others. Members of this family contain an N-terminal DNA-binding domain, followed by the BTA domain, and many have diverse domains at the C-terminus. EmbR contains an C-terminal forkhead-associated (FHA) domain, which mediates binding to threonine-phosphorylated sites in a sequence-specific manner. The BTA domain of EmbR contains three Tetratricopeptide repeats (TPRs) and two C-terminal helices. The TPR motif typically contains 34 amino acids, and 5 or 6 tandem repeats of the motif generate a right-handed helical structure with an amphipathic channel that is thought to accommodate an alpha-helix of a target protein.	1.88915e-35
NC_013729.1\|WP_083792860.1\|3316904_3317135_+\|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].	3.39902e-07

>NC_013729.1|WP_148256648.1|3327617_3328922_+|TerC/Alx-family-metal-homeostasis-membrane-protein
MGEVEGEYSFAAVSSSRSWSSSPAPGAAGQARSEPGGRDLRSPLVVCAPEVTSVHVHDYVWYITVGLLLALLAFDVFIIGRRPHEPTTRESATAIAFYVGLAIAFGLGVWAFSGGRYAGEFFAGWLTEYSLSVDNLFIFLIIMARFQVPRKYQQTALLIGIILALIFRGVFIAVGAAAINQFSWIFYLFGAFLVYTAVHLAMQGENDDEDYKENAVIRFAKKRLNATDEYNGVKLTVIKNGKRLVTPMAIVIIALGTTDLLFALDSIPAIYGLTQEPFLVFTANVFALMGLRQLYFLLGDLLRRLIYLSIGLSVVLAFIGVKLVLHAMHVNELSFINGGEHIKWAPEIPIWFSLGFIIITLGITTVLSLYKSRSLKAAEVANGTSNGQSVAGAAGGGELDEATTAARPQDDVDPATKAEIDGLPEPHQTDVKKP
>NC_013729.1|WP_041290142.1|3327171_3327522_+|hypothetical-protein
MTGRELLEHCLSKPGAWQDEPWQGDVVAKVGDKIFAFLGRGEAVGVKCGANRDEADELVRAYPDDVRASAYIGRSGWNTIRLGGAVPDDEILELVDASYLTVVAKLPKSKRPPVAT
>NC_013729.1|WP_012920732.1|3325030_3327136_+|excinuclease-ABC-subunit-UvrB
MRQVSDLQRMVAPLKVVADFEPAGDQPAAIDELERRINAGEQDVVLLGATGTGKTATIAWLAERIQRPMLILQPNKTLAAQFANELRQFFPENAVEYFVSYYDYYQPEAYVPQTDTYIEKDSSINEEVERLRHSATWSLLTRRDVVVVATVSCIYGLGSADEYLNRMIHVKVGDETDRDGLLRKLVGVQYARNDLAGTRGTFRVRGDTLEVFPVYQELAVRVEFFGDEIERLMTLHPLTGEVLSEEDELYIGAATHYVTAPERMEHAIASIEAELADRLAELERGGQLLEAQRLRMRTTYDIEMMRQIGTCSGIENYSRHTDGRAPGTAPHCLLDYFPEDFLLVIDESHVTVPQIGGMYEGDMSRKRTLVEHGFRLPSAMDNRPLRWEEFLERIGQTVYLSATPGQYEQDKSDGFVEQIIRPTGLIDPEVIVKPTKGQIDDLIHEIRLRVERDERVLVTTLTKKMSEDLTDYLLEMGIRTRYLHSEVDTLRRVELLRELRMGEYDVLVGINLLREGLDLPEVSLVAILDADKEGFLRSGRSLIQTIGRAARNVSGAVFMYADKITPSMEQAIDETNRRRAKQVAYNLEHGVDPQPLRKKIADITDMLAREDADTAELLGNGRTQSRGKAPVPGGGKAKAGEKAKELAGGMPSSDLAELIQQLTDQMHNAAAELQFEVAARYRDEISELKKELRQMVNAGAK
>NC_013729.1|WP_012920731.1|3324168_3324960_+|hypothetical-protein
MSQQYGPPQGPPAPGGWGPGPGGYPPPPPFRPARRSSSRTKWIVIAGAALAVVLITTGAVLLITGGKEDAPVATTPVAGETLTPAPVGTLYTPPTPSPTKTEITKGPHDTGVEIGGGVWFTPAKGWVKDTDKTRSGHNYLLPEPGRPGAIDGWFWIRQTKLMGAKAFADHLVDVESNNLQHVVIGKGGFRTCPNKALKLCYATNYSAVVPVKGKKPVVFSGFVQTFEDHTGQTTATDSALQREVWAQRKQEILTMNGTLVRSF
>NC_013729.1|WP_012920730.1|3323093_3324128_+|hypothetical-protein
MNTKRDKGPDNPWVRKTDPADEEGAAPEQELPPSPWSLEVPPRPAGDAAGAGTAGTAAAGTAGGAGAAGAGGPGQAGAAGPGQVGPGQAGAADGRPAPAGGESAGSGPWAGSGGASGATSTSSAWGDKVGPPSLRRPEPVKKKPSVPPLLLPVAAGIAVVLLIAVALVVLTGGDDAATPQPSPSVTVTTPPAPTYTPPPNAIAVEHGVSVVPASGWSVLATEKQGKQLVTYAPNGQARAFFWVRQKVDVAAQTYLLGIVEGETAGEIAQLGNVRNLACPRDVLVECVAISYTSTAKAGKVKGYVEVYKRKDGVLTALDFRSRADYAAKAESDAAPMKQSVIDSL
>NC_013729.1|WP_012920729.1|3322029_3323097_+|hypothetical-protein
MSNQQPPYGQGGPNQPPYGGQPPHGQPPYQGGPPQQPPYQGQPQGQPPYQPGPPPQGQPPYQGRPPQQPPYQGQPPQQPPYQGPPQGQPPYQPGPPPQYPGQQQAPYQGQQPGYPPQGPPQGYPGGPPQFPGQQAWGPGPQGHVPRGQGKGSNKILLLAGGAVAVVAVIGIVLSLIFGGDDTKVEPDPQPTTDPTTQPTGNVDEGIEVAEGVFVKPAPGYIRKSLDKFNGVYLLKQGEAYFMVNSFKANGESTATVLPQLLGIEKKATPGDFTSDEPKERKPGADDKTPVKVVTTQSFQATATSQNGSFPVIGFVGVIERNDGVMTIIRVYGRRDKADSVKTDSAAMLKSVVASQ
>NC_013729.1|WP_012920728.1|3320821_3322033_+|PrsW-family-intramembrane-metalloprotease
MECPRCSSDVPEVSHFCHHCGTDLRSPDAGRKNAYAARPDEPVASFRLVSTIMPQGAGRQPYTYKVALGIALALTVVTAALGALPVAIMVAAFAIPIVYILYLYDVNLWEDEPVPVVAAAFVLTGVLAAVFTWLWSDRLTLSTGTIGGNDAGPAGRDLLILLLLVPVVSELIRQVGPLYLASRPRYDDLMDGFTFGVVAGVGFACFETLVLHWGWISGGFAGPGTSTGTWISVVVLHGFIKPLIYGSATGLAVAEFSGLGEKYDGFTARWVIGLLQAIVVNALFHGGVYLLGFVGGHGSTLGAILGVLWGLLLLGALIIRVRTVLHKGLLEAALESAARGGSNHASGELAFCSRCEMPLLPHSDFCSACGNSTRSVPKSERGALAQSGRPAGGYDGTTGETQA
>NC_013729.1|WP_012920727.1|3320062_3320683_+|dephospho-CoA-kinase
MLRVGLTGGIGSGKSAVSARLAARGAVVIDSDVLAREVVARGTDGLAEVVAVFGDGVLTADGELDRPAVGRIVFGDEQARRRLEAVIHPRVRARAAEIEAAAPADAVVVHDIPLLVETGQAAKFDLVLVVDVPVELQVERLTSQRGMAADEARRRIASQASREDRLAAADVVIDNSGSLDELDRRLDQVWATLTARIAGHGPDTKA
>NC_013729.1|WP_049797350.1|3317172_3319932_-|tetratricopeptide-repeat-protein
MEIRLLGPFEAVRGDEPVPGLTGRVRTLLAILALAAPDAVSVDAIGQRLWGDAPPANLRPSVQTSVARLRTLLAPHLRVDTTPGGYALRIDPAKVDVHRFMQLIESADSAADAAAQRERLTAALGLWRGEPFGGIRSDWLEQEQSPRLTEAYLSAVERRIDLDLAAGRQESALPELRELTARHPLRESLWLRLLTALHRSGRPAEALTLYEELRRRLADELGVDPEAQLRLLYAELLEATEPSGNHAAPAEPPRQLPPSPARFTGRAKALARLDSLSSVHERALTILAVHGQGGVGKTSLALHWAHRVAQRFPDGQLYLNLQGYGPGEPMHPEVALDMLLRGLGVSGAQIPDGGPARTALLRTVLADRKVLILLDNARDAEQVRPLLPGAGCLVLITSRSQLRSLAAREGAHRIALDRFSADDSTAYLTATFRPHGVRATGDELAELAQLCGHLPLALAIAAERVTREPLTGVRSLIAELLDHPDRLKVLDVDEDDDGALRVVFDWSYQVLEPERAQMFRLLALHPAQDLSLEAAAALAGATTRQAAQRLDGLVGAHLLEQQPGKRYQLHDLLRVYSVSLAEQFERPAQREEARGRLLDWYAHSALSAKKALDRTRPLLDFGAPPAGQTPLAFDDTGTAVSWFNRERQVLVAAVHDAARHGHHRAAYRLAGALWPYLVYVRALDDIFDTQRVALEAAQLSGDTAGEAATAHNAGRAYFQRGDLAQAFKHLEHAMRLFELIGDDRGRGWVLTDLGRLYRRSGDPQAAISRHQQAIVALEGADDPVVEARNHRGLADNYLAVGRARDAVNEADRAVTLNRRAGERRAESFALDTLATAWLAVGDQAAAVRYYQQSLEISRDLLDRWAEASTLTNLGHALHAAGNHPEARAQWQTALDLFTETGMPDTADLSRTTLRNLLDH
>NC_013729.1|WP_083792860.1|3316904_3317135_+|GNAT-family-N-acetyltransferase
MWWLEVRPEHRGRGLGAALLGTALRLLAARGADQVVLSVDDDAPAGDPRDRTAAKRLDARAGFREVDRLWSYRLLR
>NC_013729.1|WP_148256977.1|3330238_3331306_-|dipeptide-epimerase
MKFSTHLVSAPLHTPFVTALRTATHADSLLVSITDGEYTGWGEAPQVWKVTGESLAGAQACVEGPIATALTGLGADDLTEALRRVQGAAQANFGAKAAVDVALHDLAAHRAQKTLQGFLGSTVTTVKTDVTLSAGDSAALVQAATDRLADGFDVLKVKVGTGDAAADFDRVRRIREAVGPGPRIRLDANQGWHRRDAVTVIRALEDAGCAIELVEQPVAAADLDGMAWITDRVSTPILADESVYGVRDLVNVIRRGAADLVNVKLAKCGGLATARTLLELAREHGLGSVVGSMMESHVGVGAAAALVAAYPTTAVNDLDAAWWLEQPPVSGGIRYEGSTIHLPSTPGLGVTGLIA
>NC_013729.1|WP_012920737.1|3331311_3332124_-|serine-hydrolase
MGMTDLLRGVQGQGDFGVWLGRLDGVPVFMHAAERPHYSASTMKVLVAMAMLRKVDAGELSLEQPVTVHNDFASAAGGRFGVNRAEDEAPATWTKLGEQVTLGWLATEMITRSSNLATNLVLEQAGVDTAQAVLAEYGSGASAIQRGIDDVAAQAAGISNLMSPADLAAVLVAAGNDDSASGRYLRDLLAANEWNGEIPAGVPAGTRVEHKNGWDVRIRHDGGIVRPADAEPFVLTVCTTSELPDPDAQKLIAAIAAEAWNHRHELEAVR
>NC_013729.1|WP_012920738.1|3332207_3333176_+|cobalamin-biosynthesis-protein
MSRALGLILGFAADRLLGDPRRFHPVAGFGRAATRVEAGLYADSRAAGTAYAAVLVGSVTAAGLVAERLTTRRPVARTLLTAATTWAVVGGRSLEREAAVMSGLLEAKNLPAARDRLSHLCSRDATDLQADELARATVESIAENTSDATVAPLIWGGLFGIPGLVGYRAANTLDAMVGYRSAKYRNFGWAAARFDDLVNLVPARVCAVLTGLMSGRPRVVRRIWRRDAGKHPSPNAGPVEASFAGALDLRLGGTNTYRDEVEDRGTLGDGLRPGVSDVRRTAVLARRVSYAAAATAAILALAANEAATRRAAGPRRAERGRR
>NC_013729.1|WP_012920739.1|3333172_3333853_+|phosphoglycerate-mutase-family-protein
MNLSRRPLRIALIRHGESEANVDKTIYETLPDHAVPLTAHGREQAAEAGKRLREVFENEPVRVYVSPYLRALQTLDALGLDDLIGLAREEPRLREQDWANFQDTEDIERQEQLRDSYGHFYYRFTDGESGADVYDRVSTFLETMHRDFETPDAPRNVLLVSHGLTMRLFCMRWFHWSVKFFETLRNPDNAETRVLLRQPDFRYKLDRPFEQWTEYEPTERERSAWL
>NC_013729.1|WP_012920740.1|3333843_3334818_+|DUF3500-domain-containing-protein
MVVDQTRAAAQDLLASLSPEQRAKISAPFDTPDHEQWTYLPGDRPGLTLAELTPEQEQHVHRLLQLAYSERGLGDALGVLAAEIILRDLPDPLPAGETGGWQGTVVGERYFVRVLGDPAGFEPWAWRLNGHHLALHVTLVDGAISFTPQFFGSNPAEVREGPFAGRRFLAAEQDLGFKLLNALQPGQREIAVVSEEAPDDILTRHDPVADVSRLHRGLAYGDMSPEQRQLLSLLIGQYVGRAAGPIGLQTWQDVTAQGIERLTFAWAGATEPGAGHYYSIAGPTFLAEYDNTQSDANHIHSVWRDVRNDWGKDLLAAHYAMGRH
>NC_013729.1|WP_041290144.1|3335062_3338791_+|cobaltochelatase-subunit-CobN
MLSTADTDLLAASQAEAGWRVANPARVDLAQLPGLLDGVEVVVVRLLGGRRAWEEGLDAVIASGLPTVVLSGEAAPDAELMSLSTVPAGAVTEALAYLREGGSENLRNLAGFLRDTLLLTGDAFDPPHSLPAYGVRAGRLPNPQTDAGQPDGRPVVGIVYYRAHEISGNTAFVDALADAVEAAGARALPVYCGTLRGLDPSSDENAELFELLRSCDVLVTTLLAAGGTVAANASAGGADDAWDAGALASLDIPLIQGLALTSTREQWLDSDAAISPLDAATQVAIPEFDGRLITIPFSFKAYDAEGIASYRPDLERCARLAGIAVAQARLRHVPAAEKKIALVLSSYPTKHARIGNAVGLDTPASAVVLLGQLKDAGYDLGPDLDLDELQGADGADGLIHRLIAAGGHDVDWLTDEQLAGAVAKIPLSTYALWFGRVPETLQKAMTEAWGEAPGSLYVDTSGPEPAIALAALRFGNVVLMIQPPRGFGENPVAIYHDPDMAPSHHYLAAYRWLEAPVADGGFGAHAVVHLGKHGTLEWLPGKGIGMAADCAPDAVLGNLPLVYPFIVNDPGEGTQAKRRGHAVIVDHLVPPMARAETYGDMAKLEYLLDEYATVQALDPEKVPTLRAQIWTLIQAAQLHHDLHTDEKPDDEEFDEFVLHLDGYLCEIKDVQIRDGLHVLGGGPEGEARVNLVLAVLRAAQMWGGTTGAVPGLRSALGKTFDVDEAALLADPGRAVPAELAALSELADLPAVSAADGVDLLEAVARKLVLGMETLSWDAAKVPVVVGEVLGRQSAGVEASLRFACDEVVPRLARTGDELTNVLRALDGRFVEAGPSGSPTRGLVNVLPTGRNFYAVDPKAIPSRNAWDVGVALADSLLARHKAETGEWPRSVGLTVWGTSAMRTQGDDLAEVLWLLGCRPVWDEASRRVSGFEVVPVEELGRPRVDVTVRISGFFRDAFPHVVAWLDEAVRTVAELDEDPADNYLRAHVLDDVAAGNDLRSSTARVFGSKPGSYGAGLLPLVDARNWRTDAELAEVYAVWGGYAYGKDLDGAQARPSMERAYARIQVAAKNADTREHDIMDSDDYFQYHGGMVAMVRHLTGSNPKAYIGDSAVPAQVKTRTLEEETKRVFRARVVNPRWMAAMQRHGYKGAFEMAATVDYLFGYDATAGVVDDWMYETLTTEYVANPEVAEFFRKSNPWARHGIAERLLEAAQRGLWSEPSEEALDTLRTAVLETEGDIEDRG
>NC_013729.1|WP_012920742.1|3338908_3339667_+|5'/3'-nucleotidase-SurE
MAPLRVLITNDDGYQARGIRALATAIAAAGHEVLVVAPLDDQSGVGSARRGLVDRPIRTTEETEDGITYLGVDGTPALAVTLARAGAFGPSPDVVASGINHGHNIGVPILHSGTVAAALTAATQGLSAIAVSLDSEDPKHLDTAALVAARALDWLATEPAGTVITVNVPDRPLDELEGVRRATLAPIERSRITGGTAPTGEPMIRLEPPAAAPSPDTDEALLAAGYVTVTPLIGIREAPGDAAATYLNQHLT
>NC_013729.1|WP_012920743.1|3339835_3340666_-|hypothetical-protein
MTHQTFDLVRRLDPAADDALGDVTPASRAELLAGILDSPVDVVAARRSRHPVRRLAPVLVAASLLGGVVVSTSGWPGGTREQALGPALSFSTEGEFLKVRILDPVADSRRYNEEFKAQGLDIELVLIPASPSQVGQADGQLYSGSNTRQRIRFESVPAGCVEAATYPCVPEFTIPKDYRGTARFGINRAAAPGEQYAATGALNGRDEPLEGIQWLNRPVGEISAILRQRGFSITYRWPTGRQNPNATPPPTWYVIEPSFARQNNLVELEVSPRPMK
>NC_013729.1|WP_012920745.1|3344224_3344839_+|cob(I)yrinic-acid-a,c-diamide-adenosyltransferase
MPKGQPSVVPVDGLTTRQRRNRPLLMVHTGEMKGKSTAAFGLALRGWNQGWNIGVFQFVKSAKWKVGEESAFRALGQLHEATGQGGPVEWHKMGEGWSWSRKAGTEQDHAADALEGWREIQRRIAAETHDLYVLDEFTYPTKWGWIDVDEVVDTLTHRPGHQYVVITGRDADQRLLDAADLVTEMTKVKHPMDAGQKGQKGIEW
>NC_013729.1|WP_041289338.1|3344832_3346191_+|cobyrinate-a,c-diamide-synthase
MVIPRIVVAAPASGAGKTTVAVGLMAALRRAGHTVAGFKVGPDYIDPGFHAVATSRPGRNLDPMLSGEQRVAPLFAHGAAGADVAVVEGVMGLYDGALGTEGFSSTAHVSKLLRAPVVLVVDASAAGRSVGAVVQGFVAYDTGVRIVGVILNKVGTDRHEAEARAGVAPTGVPVIGVLRRDTRLTVPSRHLGLVPADEQRAQAEAAVDAAAELVRAGVDLEAFMVAARAATPLDTEAWDPTAEVTPAEESRPVVAMAGGPVFSFRYTETAELLTAAGADVATFDPLHDSLPEGTAALYLGGGFPEMHAEALSDNERLRAQVASAAAAGLPVIAECAGLLYLCRELDGHAMTGVLPATARMTPKLTLGYRTAVAASTTAFFDEGRRVRGHEFHRTEVRLDADDSPAWYLPGGKLEGISRPAVHASYLHLHWTATPDVPARLVAAARVHVGLEK

You can click texts colored in the table to view more detailed information

Click the colored protein region to show detailed information

Crispr_ID: NC_013729_5

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NC_013729_5

3468121-3468812

Orphan

Consensus_repeat	Method
CCGCAGCANCCGANCCAGCCGCA	CRT

12 spacers

The CRISPR arrays of NC_013729_5

>merge|NC_013729|5|3468121-3468812|CRT
CCGCAACAGCCGACGATCCCGCCGATGCCCCAGCACCCACCCACCACCCCGCCGCACCCGCACCAGCCGCAGCATCCGTATGCGCCGCAGCAGCCGAGCCAGCCGCAGCAGCCGTATGCGCCGCAGCAGCCAAGCCAGCCGCAGCATCCGTATGCGCCGCAGCACCCGAACCAGCCGCAGCAGCCAAGCCAGCCGCAGCAGCCGCATGGGCCGCAGCACCCGAGCCAGCCGCAGCACCCGAACCAACCGCAGCAGCCGTACGCACCGCAGCACCCGAGCCAGCCGCATCCGCAGCAGCCGCATGGGCCGCAGCACCCGAGCCAGCCGCAGCACCCGAACCAACCGCAGCAGCCGTACGCACCGCAGCACCCGAGCCAGCCGCATCCGCAGCAGCCGCATGGGCCGCAGCACCCGAGCCAGCCGCAGCACCCGAACCAACCGCAGCAGCCGTACGCACCGCAGCACCCGAGCCAGCCGCATCCGCAGCAGCCGCATGGGCCGCAGCACCCGAACCAGCCGCAGCACCCGAGCCAGCCGCGGCACCCGAGCCAGCCGCGGCACCCGAACCAACCGCGGCACCCGTATGCGCCGCAGCAGCCCAACCAGCCGCAGCACCCATATGCGCCGCAGCAGCCCAACCAGCCGCAGCAGCCGAGCCAGCCGCAGCACCCGCATGCGCCGAACCAGCCGCA

>NC_013729|5|1|3468121-3468812|CRT
CCGCAACAGCCGACGATCCCGCC	GATGCCCCAGCACCCACCCACCACCCCGCCGCACCCGCACCAGCCGCAGCATCCGTATGCG
CCGCAGCAGCCGAGCCAGCCGCA	GCAGCCGTATGCGCCGCAGCAGCCAAGCCAGCCGCAGCATCCGTATGCG
CCGCAGCACCCGAACCAGCCGCA	GCAGCCAAGCCAGCCGCAGCAGCCGCATGGG
CCGCAGCACCCGAGCCAGCCGCA	GCACCCGAACCAACCGCAGCAGCCGTACGCA
CCGCAGCACCCGAGCCAGCCGCA	TCCGCAGCAGCCGCATGGG
CCGCAGCACCCGAGCCAGCCGCA	GCACCCGAACCAACCGCAGCAGCCGTACGCA
CCGCAGCACCCGAGCCAGCCGCA	TCCGCAGCAGCCGCATGGG
CCGCAGCACCCGAGCCAGCCGCA	GCACCCGAACCAACCGCAGCAGCCGTACGCA
CCGCAGCACCCGAGCCAGCCGCA	TCCGCAGCAGCCGCATGGG
CCGCAGCACCCGAACCAGCCGCA	GCACCCGAGCCAGCCGCGGCACCCGAGCCAG
CCGCGGCACCCGAACCAACCGCG	GCACCCGTATGCGCCGCAGCAGCCCAACCAGCCGCAGCACCCATATGCG
CCGCAGCAGCCCAACCAGCCGCA	GCAGCCGAGCCAGCCGCAGCAC
CCGCATGCGCCGAACCAGCCGCA

Protein	Signature genes	Signature genes Name	Protein_function
NC_013729.1\|WP_012920866.1\|3471864_3475890_+\|type-VII-secretion-protein-EccC	unknown	unknown	gnl\|CDD\|274858
NC_013729.1\|WP_012920857.1\|3459733_3462754_+\|excinuclease-ABC-subunit-UvrA	unknown	unknown	gnl\|CDD\|234734
NC_013729.1\|WP_049797355.1\|3475886_3476306_+\|hypothetical-protein	unknown	unknown	unknown
NC_013729.1\|WP_012920858.1\|3462949_3463267_+\|hypothetical-protein	unknown	unknown	unknown
NC_013729.1\|WP_012920870.1\|3481183_3482518_-\|S8-family-peptidase	unknown	unknown	gnl\|CDD\|173790
NC_013729.1\|WP_012920861.1\|3464184_3464592_+\|hypothetical-protein	unknown	unknown	unknown
NC_013729.1\|WP_012920856.1\|3458807_3459467_-\|MBL-fold-metallo-hydrolase	unknown	unknown	gnl\|CDD\|293792
NC_013729.1\|WP_012920860.1\|3463742_3464051_+\|hypothetical-protein	unknown	unknown	unknown
NC_013729.1\|WP_012920855.1\|3457047_3458430_+\|ribosome-biogenesis-GTPase-Der	unknown	unknown	gnl\|CDD\|179525
NC_013729.1\|WP_012920868.1\|3478729_3480412_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|370676
NC_013729.1\|WP_012920863.1\|3470030_3470501_+\|hypothetical-protein	unknown	unknown	unknown
NC_013729.1\|WP_041289350.1\|3463402_3463723_+\|hypothetical-protein	unknown	unknown	unknown
NC_013729.1\|WP_049797356.1\|3476298_3477345_+\|hypothetical-protein	unknown	unknown	unknown
NC_013729.1\|WP_012920864.1\|3470527_3470869_+\|hypothetical-protein	unknown	unknown	unknown
NC_013729.1\|WP_012920853.1\|3455643_3456330_+\|(d)CMP-kinase	unknown	unknown	gnl\|CDD\|234579
NC_013729.1\|WP_012920865.1\|3470875_3471763_-\|hypothetical-protein	unknown	unknown	unknown
NC_013729.1\|WP_012920869.1\|3480574_3481111_+\|Rieske-(2Fe-2S)-protein	unknown	unknown	gnl\|CDD\|239550
NC_013729.1\|WP_041289349.1\|3458616_3458829_-\|hypothetical-protein	unknown	unknown	unknown
NC_013729.1\|WP_063822834.1\|3477442_3478720_+\|secretion-protein-snm4	unknown	unknown	gnl\|CDD\|274855
NC_013729.1\|WP_012920854.1\|3456326_3457055_+\|1-acyl-sn-glycerol-3-phosphate-acyltransferase	unknown	unknown	gnl\|CDD\|153251

Protein	Function_ID	Function_description	E-value
NC_013729.1\|WP_012920855.1\|3457047_3458430_+\|ribosome-biogenesis-GTPase-Der	gnl\|CDD\|179525	PRK03003, PRK03003, GTP-binding protein Der; Reviewed.	0
NC_013729.1\|WP_012920866.1\|3471864_3475890_+\|type-VII-secretion-protein-EccC	gnl\|CDD\|274858	TIGR03924, T7SS_EccC_a, type VII secretion protein EccCa. This model represents the N-terminal domain or EccCa subunit of the type VII secretion protein EccC as found in the Actinobacteria. Type VII secretion is defined more broadly as including secretion systems for ESAT-6-like proteins in the Firmicutes as well as in the Actinobacteria, but this family does not show close homologs in the Firmicutes. [Protein fate, Protein and peptide secretion and trafficking].	0
NC_013729.1\|WP_012920853.1\|3455643_3456330_+\|(d)CMP-kinase	gnl\|CDD\|234579	PRK00023, cmk, (d)CMP kinase.	1.11891e-74
NC_013729.1\|WP_012920857.1\|3459733_3462754_+\|excinuclease-ABC-subunit-UvrA	gnl\|CDD\|234734	PRK00349, uvrA, excinuclease ABC subunit UvrA.	0
NC_013729.1\|WP_012920856.1\|3458807_3459467_-\|MBL-fold-metallo-hydrolase	gnl\|CDD\|293792	cd06262, metallo-hydrolase-like_MBL-fold, mainly hydrolytic enzymes and related proteins which carry out various biological functions; MBL-fold metallohydrolase domain. Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases which can catalyze the hydrolysis of a wide range of beta-lactam antibiotics, hydroxyacylglutathione hydrolases (also called glyoxalase II) which hydrolyze S-d-lactoylglutathione to d-lactate in the second step of the glycoxlase system, AHL lactonases which catalyze the hydrolysis and opening of the homoserine lactone rings of acyl homoserine lactones (AHLs), persulfide dioxygenase which catalyze the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria, flavodiiron proteins which catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J which has both 5'-3' exoribonucleolytic and endonucleolytic activity and ribonuclease Z which catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors, cyclic nucleotide phosphodiesterases which decompose cyclic adenosine and guanosine 3', 5'-monophosphate (cAMP and cGMP) respectively, insecticide hydrolases, and proteins required for natural transformation competence. The diversity of biological roles is reflected in variations in the active site metallo-chemistry, for example classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, human persulfide dioxygenase ETHE1 is a mono-iron binding member of the superfamily; Arabidopsis thaliana hydroxyacylglutathione hydrolases incorporates iron, manganese, and zinc in its dinuclear metal binding site, and flavodiiron proteins contains a diiron site.	1.89087e-39
NC_013729.1\|WP_012920870.1\|3481183_3482518_-\|S8-family-peptidase	gnl\|CDD\|173790	cd04077, Peptidases_S8_PCSK9_ProteinaseK_like, Peptidase S8 family domain in ProteinaseK-like proteins. The peptidase S8 or Subtilase clan of proteases have a Asp/His/Ser catalytic triad that is not homologous to trypsin. This CD contains several members of this clan including: PCSK9 (Proprotein convertase subtilisin/kexin type 9), Proteinase_K, Proteinase_T, and other subtilisin-like serine proteases. PCSK9 posttranslationally regulates hepatic low-density lipoprotein receptors (LDLRs) by binding to LDLRs on the cell surface, leading to their degradation. The binding site of PCSK9 has been localized to the epidermal growth factor-like repeat A (EGF-A) domain of the LDLR. Characterized Proteinases K are secreted endopeptidases with a high degree of sequence conservation. Proteinases K are not substrate-specific and function in a wide variety of species in different pathways. It can hydrolyze keratin and other proteins with subtilisin-like specificity. The number of calcium-binding motifs found in these differ. Proteinase T is a novel proteinase from the fungus Tritirachium album Limber. The amino acid sequence of proteinase T as deduced from the nucleotide sequence is about 56% identical to that of proteinase K.	6.90416e-124
NC_013729.1\|WP_012920869.1\|3480574_3481111_+\|Rieske-(2Fe-2S)-protein	gnl\|CDD\|239550	cd03467, Rieske, Rieske domain; a [2Fe-2S] cluster binding domain commonly found in Rieske non-heme iron oxygenase (RO) systems such as naphthalene and biphenyl dioxygenases, as well as in plant/cyanobacterial chloroplast b6f and mitochondrial cytochrome bc(1) complexes. The Rieske domain can be divided into two subdomains, with an incomplete six-stranded, antiparallel beta-barrel at one end, and an iron-sulfur cluster binding subdomain at the other. The Rieske iron-sulfur center contains a [2Fe-2S] cluster, which is involved in electron transfer, and is liganded to two histidine and two cysteine residues present in conserved sequences called Rieske motifs. In RO systems, the N-terminal Rieske domain of the alpha subunit acts as an electron shuttle that accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron in the alpha subunit C-terminal domain to be used for catalysis.	2.46041e-21
NC_013729.1\|WP_063822834.1\|3477442_3478720_+\|secretion-protein-snm4	gnl\|CDD\|274855	TIGR03920, T7SS_EccD, type VII secretion integral membrane protein EccD. Members of this family are EccD, a component of actinobacterial type VII secretion systems (T7SS) with ten to eleven predicted transmembrane helix regions. [Protein fate, Protein and peptide secretion and trafficking].	4.83943e-13
NC_013729.1\|WP_012920868.1\|3478729_3480412_+\|hypothetical-protein	gnl\|CDD\|370676	pfam09770, PAT1, Topoisomerase II-associated protein PAT1. Members of this family are necessary for accurate chromosome transmission during cell division.	4.94186e-16
NC_013729.1\|WP_012920854.1\|3456326_3457055_+\|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.	4.97358e-36

>NC_013729.1|WP_012920861.1|3464184_3464592_+|hypothetical-protein
MVNWSVEAAAAMEGLKGLQTEAAGFEAIGTKLSNALTTAGTQASLNGKGGPIGIAISEFVEKWKDSLPGMVKHTGDVMQGTANALNALANGQQEMALAAQRGIQLAEGVDPRQAIRSAAAAARAEHQPPSTNRAV
>NC_013729.1|WP_012920860.1|3463742_3464051_+|hypothetical-protein
MSGRNSYDSGASAETQAAIKSLSAQIETLIAQHQANVKAMRGDATMTKVMDEYGAVEQKFNAAATEVQGIIKSLAATLAQFDNHANTAFTAASKAVQDIGNV
>NC_013729.1|WP_041289350.1|3463402_3463723_+|hypothetical-protein
MGKDTLSTLAKKTGGNTQDLGGLVKRLAAAAQPLEGKLQGAGHDAFIAFKGRVDSIANDLNAGLAAIAKGQSGMDAATRTGESDMAQAAKKAEGAANFDGAKFTKR
>NC_013729.1|WP_012920858.1|3462949_3463267_+|hypothetical-protein
MSRQYDTQLIESVAVRRRRLREAWLFGAARSRHTLDEGVGKLFAGVAVAAVVCAGCVGYSFIQDSKDKNPNGPVAPSPSTSVSTGPSAPVGADPSTTARPTPTRS
>NC_013729.1|WP_012920857.1|3459733_3462754_+|excinuclease-ABC-subunit-UvrA
MSDRLIVRGAREHNLKDVSLDLPRDAMIVFTGLSGSGKSSLAFDTIFAEGQRRYVESLSAYARQFLGQMDKPDVDFIEGLSPAVSIDQKSTSRNPRSTVGTITEVYDYLRLLFARAGRPHCPECGEPIAKQTPQQIVDRVMELDEGTRFQVLAPVIRGRKGEYLDLFRQLTGQGFSRARVDGDTIQLTEPPKLDKQKKHTIDVVVDRLAVKSSAKQRLTDSVETALGLSGGIVTLDFVDLDEKDPQRERRFSEKLACPNDHPLQLDELEPRSFSFNSPYGACPACSGLGTRMEVDPELLVPDPSKSLDEGAIQPWSGANVSQYFERLLTALAKDLKIKTTTPFGELPEKARRALLTGHDRQVHVSYKNRYGRERSYYTTFEGVIPYVERRHAEASSDTSRERFEEYMREVPCLTCNGARLKPISLAVTLGGKNIAEISAMSIDEVHGFLVELDLSPREKQIAERVTKEIGERLRFLLDVGLDYLALNRPAGSLSGGEAQRIRLATQIGSGLVGVLYVLDEPSIGLHQRDNRRLIDTLVRLKDLGNTLIVVEHDEDTIDHADWVVDIGPGAGEHGGQVVVSGTVEDLRNHPDSITGAYISGRREIPIPPVRRPLTEGRELTVYGAREHNLQDIDVTVPLGVFVAVTGVSGSGKSTLVNDILYTSLARQIYGARAVPGRHTKISGLEQVDKVIHVDQSPIGRTPRSNPATYTGVWDHVRKLFAETPEAKVRGYQQGRFSFNVKGGRCEACSGDGTLKIEMNFLPDVYVPCEVCHGARYNRETLEVHYKGKTVADVLDMPIEEAAEFFEAIPAISRHLKTLNEVGLGYVRLGQPAPTLSGGEAQRVKLASELQKRSTGRTVYVLDEPTTGLHFEDIRKLLGVLGGLVDKGNSVLVIEHNLDVIKTADWIIDLGPEGGRRGGTLVAEGTPEEVAANPASYTGQFLAEILHGRAAKPSAKKAAEKTATVTKKAPASKAPAKKAVAAKKTVAKKVAAQKAPAKKVAAKRAAG
>NC_013729.1|WP_012920856.1|3458807_3459467_-|MBL-fold-metallo-hydrolase
MSDYHGNVRVGGPAQTHELAQLMITKVAVGPMDNNAYLLRCRQTDEQLLIDAANDAHTLLTVIGAAGIGRVVTTHRHQDHWQALAEVVAATGATTVAGRYDAEGIEVPTDELVDDGDRLEFGRIGLRVIHLTGHTPGSIALLYDDPAGPPHLFTGDSLFPGGVGNTRGNAENFTSLLNDVQTKLFDQLPDETWVYPGHGADTTLGAERPHLPEWRARGW
>NC_013729.1|WP_041289349.1|3458616_3458829_-|hypothetical-protein
MARPRLVSGFAEYRPEQTRRTPEQPISVRARSTVDVSRLGLVLRERRHPRPAPLAPGTGVLLRAEPTTDR
>NC_013729.1|WP_012920855.1|3457047_3458430_+|ribosome-biogenesis-GTPase-Der
MSDLPTGYEYDAEPSHDRDDQGPLPVLAIVGRPNVGKSTLVNRIIGRREAVVEDTPGVTRDRVSYDADWAGRAFTVVDTGGWDPDAVGMAALVAAQAEVAIHAADAVLFVVDATVGITDADEAVVRVLRKSGKPVVLAANKVDDQRVEAEAMNLWSLGIGEPFPISAMHGRGTGDMLDAVLAALPEAPPERDAEIGGPRRVAIVGKPNVGKSSLLNKVAKEDRVVVSDVSGTTVDPVDELITLAGRQWRFIDTAGIRRKVKNVQGHEYYASLRTNSAIERAEVVVVVIDASEPMTEQDLRIMNTVEEAGKALVIAYNKWDLVDEDRRYYLEREIDRDLVQFRWAPRVNISALTGRHMEKLVPAIEAALDGWQTRVPTGQLNAFLGRLVAAHPHPVRSGKQPKILFGTQASTMPPTFALFTSGQIESSYQRFIERRLREDFGFVGSPVHVQVRARQKKAKR
>NC_013729.1|WP_012920854.1|3456326_3457055_+|1-acyl-sn-glycerol-3-phosphate-acyltransferase
MRAELTGHHELPRTDDLAPLPYRLGTVLRRAVRPYLRWRYDLTVHHDERFPRTGPVLLAPNHLGLLDGPLLGAIAPRMLHQLGKIEAFQGVQGKVLHLAGQIPVDRTTYDTLAVRKAIKVLRDGNVLSIYPEGTRGPGDFRRVRTGVAYLAMVSGAPILPVALLGTRLPGGDIELFPPRGSRVDVVYGEPFSVERVPFPRRHSDVRAVADQIGEVLRAHVRAAVEATGHPLPGAPDQKDPDE
>NC_013729.1|WP_012920853.1|3455643_3456330_+|(d)CMP-kinase
MIIAVDGPSGSGKSSTARGVATRLGLSYLDTGAMYRAVTWSVLEHGLDLTDVTAVAERARAVDLGISTDPGLAHFTADGSDVTEAIRDPRISENVSKVATNLDVRKELIRRQREIIDAAQPGGGIVVEGRDIATVVATDAELKVLLTADQEARMARRKAELAAGSVTAEQLRDQIVRRDADDATVSQFEVASDGAVTIDSTHLTLEEVVDVISRLAKEAEAAPRDQES
>NC_013729.1|WP_012920863.1|3470030_3470501_+|hypothetical-protein
MKAREYLFLRTSESVQAVAEWIQQEFALEPIPNGSDDEDEIGLRGPARTADATVGYEVMYNIYPVHEPEPDEIQAIDTYPVEIDIWLGKDEGTQGQEARLVFEHLIKARPDVPILLCHELSDLIAAYVPGRGVHEFPDPVTIYAGHADAWRDWVPA
>NC_013729.1|WP_012920864.1|3470527_3470869_+|hypothetical-protein
MADEIEIDPGTLARARQALADWMNEHEDDDEPRLEAESFEGWQVWPVEEFLVFSSPGGFTNMLYLVGEGVVRAFSYSSETEEYAAAAARAERDGTEPPAPPAPAISWENWNDQ
>NC_013729.1|WP_012920865.1|3470875_3471763_-|hypothetical-protein
MTDTPFDRRHVLDLVADLLPVLVPDAELDPAGPIVKLRWSRGGLTSSAEVGLTELIDRCREQPHHLWPRTVDDWLRAVVDEIGVATDEHLYGAVAERQRVTLRPQGWSAAYDSVLAGLSVPFGRYFEIVFGIQSGPDWHRLTQVRRVMHGLHLPGSPSGLELTLNGLAGLTLQEVPGTPYRMFHRPGDQTVGLALVDHEQALPNGGKGRGTLLALPATDLLAVCPIDRRDDMQVRVDEFAHWVAKAHADAVDPCSPGVYWLVGELLAELPVDLDITPSVTLPKALKSPFWRRRRT
>NC_013729.1|WP_012920866.1|3471864_3475890_+|type-VII-secretion-protein-EccC
MSTRLVHRPARSTRSIDTGQPRVIETPPPGARGKAGGGAMQALMPAVGVLGSVGMMSTMRTGTSAVIGVGVLALTVVGTFGMMFSQRGRSGKESREQRNRYLDYLERLREEFGRMERQNRKAALALNPPADALVDCVRDPARLWERRRSDPDFLLVRCATGRMPVVPATLAASGSMMDPPDPFMLAEAEALARRFALMPDMPLTIPLDLAGNVSIVGDRDGVVRIARALMLQAAVFHAPEDLEFAASFPQAALDQWQWVGWLPHAVDPERREGPHPFRRIAAKPAELAELIHDDLASRVKLASEARRGSLGTDQRRMIQRMLVLHDTYGDVATEVTPADPTLGIGELGVTVLHLVQDRMQEPGNVAIRITVQEGRVLVEDLRGGGYLTAEGQLDDTPLATAEGLARTLAPLRLSEESLEEDASLKTVDFMSLLQIDDPGSVDLERMWVPRHERAFLRVPIGLDSQGQPVVLDLKESAQLGMGPHGLCIGATGSGKSEVLRTLVMGLLATHSPEDLAMVLIDYKGGATFAPFDGVPHVAGIITNLVDDPSLTERAYASLAGEVQRRQQMLKDAGNVANITDYRLLREQRPEMPPFPHLFVLIDEFGELLTARPDFIDLFLSIGRIGRSIGVHLLLASQRVEGGKLRGLETYLSYRLGLRTFSEEESRTVLDTDDAFHLPPLPGFGYLKVDTSVYQRFRAAYVSGPYKGRVAAEEEKENDGPAVRPYLVTPYQQPDLEQLAAEDEKKDDEDDSTERTTGPTVLGVFVEQVKPAATPVPQVWLPPLPKMCTLDQVGGPVDITAERGLQYAVPNPAISPPIGVVDDPRKQSQSVLRLDLTQAGGHCALIGGPASGKTTFLRTLVTSLAHSYTPKEVAIYAIDLAGGGLQPLADLPHVGGVAIRTDRERIRRTLEEVRGMLDQREIVFRDRGIDTMERLRAMHAAGEVPELPVADVVLVLDNYGAIKTTFDELEEPIADLVQRGSSYGIHLVTAMLRWSDVRMATQALFGTVLELRLNDPSDSNIDRRLQETMRNAGPGRVLTPRNKLFAQLALPRVDSLLQDDDLSEAMQGQALALSSAWQGPVAPPVRVLPLRLERRTMPTPQQEPVRVPIGLDETAMAPVLLDLFERDGNLVIFGDTASGKTNLLKLIMQQLVDRYSSDEVVFAVMDPRRGLRGFLPDAYLGGYATSGRVGAGLAGGVSGELEKRLPDDLNDAAPPPVAGPKVIVVADDYDLLTSGGQAPMDPFLPYIASGRDIGLHFVIARRASGAGRALYEPFLTTVTESGTAGLVLSGDKSEGALFTGATPGNFPAGRGLFVRRGERPSLIQTALADGTVSAAEAEGGVK
>NC_013729.1|WP_049797355.1|3475886_3476306_+|hypothetical-protein
MSYDVVALIDGRPSYQDVLAGMMAAGPDWLVREVSDGAVLQLCDAEGAPLASLEAPILIQVPGEVERLLGPELAGTATPVWWMEVRANPQSGGPALADRYAEKLVERLGGRVWKPAPPPFDPPTPRTPAAQNNAGGNNA
>NC_013729.1|WP_049797356.1|3476298_3477345_+|hypothetical-protein
MPNPVELSPAIDVRTGKVVVIMQDRPVVGMSAWLVDALAAAEAAGLGVQLVTPATTRLTFNVRTTLFSGYESRWVVTEPNGEGAYDGLGGSKLQWNGEMFAAVAAGEQDKVDMSPTFATVDLELPWQLLVTARVRYQALESTVVGKAAEQLFTDLTGTAPAGWGTAEPVTQPWNVGRLTAYCRRRAPKPTWLSVVGGPDGLSASGSVEIHRRPAGLEEVVTFAVATPDGLPTPDAVQQVGERLADAFTLVSFFAQGARGNGVDTNAMPHWTGVPAPMAMAVGNEALRGAGAEKALDLTGVAEITPVKIGPAASPAVWYPIGDGKSQLDWNVYSALLGRLVPPGAPARG
>NC_013729.1|WP_063822834.1|3477442_3478720_+|secretion-protein-snm4
MDAVLPVDEPLGRLMPDLLRMLGEPIDPSPRRRYLTTPTGQTVSLELTLGSAQIGDGAVLRLAAEGEVPPPPTVYDVAEEAVDDLERRGTTFQRKHRHWAAGAALTFALLAGAIALVRSAEPDVAAFIVLVVAIVTGLGGVVLGRAGQRATAITLLVVTPILLAIVAWSLGVSEDWSTPMRWGVTALGLALGPLLFAMAGLAGGGLVGGGTAMLFALIWIIGVAAGVSADKLSALIAVVAVLLLGVLPRLALSMSGLTALDDRRARGNEIGRPDVEAALNAAHVGLALSATAIALWSAAAGVVLALHGSAWTVSIAALLALLLCSRSRLYPLAAEVLGLFLAAGVVLAALVQDLSQQPVGGTLVAVGLLVVVAMVGAFGLTWTPQDHVQVRLGQVLDQLQVLAVVALVPLVLGAFGVFSDLLDVF
>NC_013729.1|WP_012920868.1|3478729_3480412_+|hypothetical-protein
MTGPNWQADMMARLDDESATAAAPPESPAGAGQPPVQQPAPEPTMPPPPAPVGAGWGAPVPPQEQQPQYTNQSPHQPQYQAQQQWQQPAPPQGPYQEQQWQQPPQSYGPPQQQAPYYPPQQYAPPPEQQYQYQQPAPPYPQYQQPPVQQYEPQGPPPYQQAPAYEQPPYGAVPPAPYQEQYAPPPPQYPPQPQQYGPPPQQQYQAAQQQAYQPPPQQYPQPQPPAYDPNYGPPAQYQQGYEQPPVGDGSWNAPAPQEPTGWDTPMPDGGPGPQAYTPSYQDPLAGPLPVASDSVGLQHEDRPGGFFRRIGRFAAEAAYIAGASGRMQRDVENIAVIRRPIGIGRMIGVVGPVPQAGTSTVTALLADTIAAQRSDIVLAVDACPREGKLTHRLAQGITSTPGARIQLARAEPTADAISDVLAARNVGGANQIPISLVDCPAGLFEQATGYVAGSAHAVALVIPSSRDDALSSINQLDQLSVAGQQMLVQKGLVIIAENRPDDPEPVRWLQSAVSDRGLGYVVLPYDEHLARVWPLRPEQLEPATRRAALELAARLVERATR
>NC_013729.1|WP_012920869.1|3480574_3481111_+|Rieske-(2Fe-2S)-protein
MSDDKTANLDRVIASVRDRRSVLRGAAVAGLAGVSAPLLAACGDDGQAGGTPSGAASSPTSAPSSAPSSAPSSAPSSAPSAGGPVLGPAADVPVGGGAVFKEAKVVVTQPTAGQYKGFSAVCTHSGCLVAKVADNTIDCNCHGSKFNATDGSVVTGPAREPLAAVNVSVQGGNIVGSA
>NC_013729.1|WP_012920870.1|3481183_3482518_-|S8-family-peptidase
MTPFNIPFRATAVAGAALLLVPVLGAAPATAREAPTTERSEPLIRGAGSPAAVPGTYIVVLAGNPSAAMTRATTRSLATAYDLTVRKEFRSSLRGFSAAMTPEQAENVARDPQVAYVQQNQVFTAKQDDPPWGLDRTDQRELPLDRKFTPSVAADNVSVYVIDTGIYPEHKDFGGRASVGTDTIGDGQNGVDCAGHGSHVAGTIAGTTYGVAKQAKVYGVRVLNCIGSGTTETVVSGIEWVTANAKKPAVANLSLGGSIDDATDAAVRASIESGISYAVAAGNESTDACNVSPAREPLAITVGATDREDTRPKFSNYGSCVDLSGPGVEITSVAINDPEATRTMSGTSMAAPHVAGVIALYLSTHPEATPAEVSKALLETATPDEVQNPGANSPNRLLFLGPFEPPTTPTPTPTPTPTPTPTPTPSPTTSPTPTGTPTSAPAPR

You can click texts colored in the table to view more detailed information

Click the colored protein region to show detailed information

Crispr_ID: NC_013729_6

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NC_013729_6

4670404-4670504

Orphan

Consensus_repeat	Method
CGGGCACCGGCCAGTACGCGGGGGCCGG	CRISPRCasFinder

1 spacers

csa3

The CRISPR arrays of NC_013729_6

>merge|NC_013729|6|4670404-4670504|CRISPRCasFinder
CGGGCTGGTGCCAATGCGCGGGCACCGGCCAGTACGCGGGGGCCGGTGCGCGGGGATCGGCCAGTGCAGTGCCCGGGCACCGGCCAGTACGCGGGGACCGG

>NC_013729|6|5|4670404-4670504|CRISPRCasFinder
CGGGCTGGTGCCAATGCGCGGGCACCGG	CCAGTACGCGGGGGCCGGTGCGCGGGGATCGGCCAGTGCAGTGCC
CGGGCACCGGCCAGTACGCGGGGACCGG

Protein	Signature genes	Signature genes Name	Protein_function
NC_013729.1\|WP_012921913.1\|4662228_4664268_-\|primosomal-protein-N'	unknown	unknown	gnl\|CDD\|237844
NC_013729.1\|WP_012921930.1\|4680152_4681286_-\|glutamine-hydrolyzing-carbamoyl-phosphate-synthase-small-subunit	unknown	unknown	gnl\|CDD\|237139
NC_013729.1\|WP_148257044.1\|4675657_4676821_-\|quinone-dependent-dihydroorotate-dehydrogenase	unknown	unknown	gnl\|CDD\|235388
NC_013729.1\|WP_012921921.1\|4671940_4672255_-\|DNA-directed-RNA-polymerase-subunit-omega	unknown	unknown	gnl\|CDD\|234744
NC_013729.1\|WP_012921915.1\|4664739_4665933_-\|methionine-adenosyltransferase	unknown	unknown	gnl\|CDD\|235374
NC_013729.1\|WP_012921919.1\|4669357_4670338_-\|hypothetical-protein	unknown	unknown	unknown
NC_013729.1\|WP_012921914.1\|4664460_4664646_+\|hypothetical-protein	unknown	unknown	unknown
NC_013729.1\|WP_041290362.1\|4673894_4674230_-\|hypothetical-protein	unknown	unknown	unknown
NC_013729.1\|WP_041290361.1\|4670535_4671789_-\|bifunctional-phosphopantothenoylcysteine-decarboxylase/phosphopantothenate--cysteine-ligase-CoaBC	unknown	unknown	gnl\|CDD\|235513
NC_013729.1\|WP_041289432.1\|4674803_4675640_-\|orotidine-5'-phosphate-decarboxylase	unknown	unknown	gnl\|CDD\|234651
NC_013729.1\|WP_012921926.1\|4674405_4674804_-\|hypothetical-protein	unknown	unknown	unknown
NC_013729.1\|WP_041290359.1\|4661095_4662031_-\|cyclase-family-protein	unknown	unknown	gnl\|CDD\|377240
NC_013729.1\|WP_049797609.1\|4672257_4672818_-\|guanylate-kinase	unknown	unknown	gnl\|CDD\|234719
NC_013729.1\|WP_012921908.1\|4657977_4658601_-\|HAD-family-phosphatase	unknown	unknown	gnl\|CDD\|319790
NC_013729.1\|WP_012921909.1\|4658597_4659833_-\|MFS-transporter	unknown	unknown	gnl\|CDD\|340887
NC_013729.1\|WP_012921929.1\|4676838_4680153_-\|carbamoyl-phosphate-synthase-large-subunit	unknown	unknown	gnl\|CDD\|235393
NC_013729.1\|WP_012921923.1\|4672988_4673303_-\|30S-ribosomal-protein-S13	unknown	unknown	gnl\|CDD\|235358
NC_013729.1\|WP_041289431.1\|4668174_4669314_-\|winged-helix-DNA-binding-domain-containing-protein	unknown	unknown	gnl\|CDD\|377630
NC_013729.1\|WP_012921917.1\|4666325_4667891_+\|alpha/beta-hydrolase	unknown	unknown	gnl\|CDD\|312032
NC_013729.1\|WP_012921910.1\|4659926_4660925_+\|winged-helix-turn-helix-transcriptional-regulator	csa3	COG0640_csa3_CAS-I-A	gnl\|CDD\|238042

Protein	Function_ID	Function_description	E-value
NC_013729.1\|WP_012921913.1\|4662228_4664268_-\|primosomal-protein-N'	gnl\|CDD\|237844	PRK14873, PRK14873, primosomal protein N'.	0
NC_013729.1\|WP_012921930.1\|4680152_4681286_-\|glutamine-hydrolyzing-carbamoyl-phosphate-synthase-small-subunit	gnl\|CDD\|237139	PRK12564, PRK12564, carbamoyl-phosphate synthase small subunit.	0
NC_013729.1\|WP_148257044.1\|4675657_4676821_-\|quinone-dependent-dihydroorotate-dehydrogenase	gnl\|CDD\|235388	PRK05286, PRK05286, quinone-dependent dihydroorotate dehydrogenase.	3.16751e-172
NC_013729.1\|WP_012921921.1\|4671940_4672255_-\|DNA-directed-RNA-polymerase-subunit-omega	gnl\|CDD\|234744	PRK00392, rpoZ, DNA-directed RNA polymerase subunit omega; Reviewed.	9.97342e-16
NC_013729.1\|WP_012921915.1\|4664739_4665933_-\|methionine-adenosyltransferase	gnl\|CDD\|235374	PRK05250, PRK05250, S-adenosylmethionine synthetase; Validated.	0
NC_013729.1\|WP_041290361.1\|4670535_4671789_-\|bifunctional-phosphopantothenoylcysteine-decarboxylase/phosphopantothenate--cysteine-ligase-CoaBC	gnl\|CDD\|235513	PRK05579, PRK05579, bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; Validated.	0
NC_013729.1\|WP_041289432.1\|4674803_4675640_-\|orotidine-5'-phosphate-decarboxylase	gnl\|CDD\|234651	PRK00125, pyrF, orotidine 5'-phosphate decarboxylase; Reviewed.	2.70797e-104
NC_013729.1\|WP_041290359.1\|4661095_4662031_-\|cyclase-family-protein	gnl\|CDD\|377240	pfam04199, Cyclase, Putative cyclase. Proteins in this family are thought to be cyclase enzymes. They are found in proteins involved in antibiotic synthesis. However they are also found in organisms that do not make antibiotics pointing to a wider role for these proteins. The proteins contain a conserved motif HXGTHXDXPXH that is likely to form part of the active site.	3.4568e-18
NC_013729.1\|WP_049797609.1\|4672257_4672818_-\|guanylate-kinase	gnl\|CDD\|234719	PRK00300, gmk, guanylate kinase; Provisional.	7.30193e-95
NC_013729.1\|WP_012921908.1\|4657977_4658601_-\|HAD-family-phosphatase	gnl\|CDD\|319790	cd02603, HAD_sEH-N_like, N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX/HAD4 alpha-D-glucose 1-phosphate phosphatase, and related domains, may be inactive. This family includes the N-terminal phosphatase domain of human soluble epoxide hydrolase (sEH). sEH is a bifunctional enzyme with two distinct enzyme activities, the C-terminal domain has epoxide hydrolysis activity and the N-terminal domain (Ntermphos), which belongs to this family, has lipid phosphatase activity. The latter prefers mono-phosphate esters, and lysophosphatidic acids (LPAs) are the best natural substrates found to date. In addition this family includes Gallus gallus sEH and Xenopus sEH which appears to lack phosphatase activity, and Escherichia coli YihX/HAD4 which selectively hydrolyzes alpha-Glucose-1-P, phosphatase, has significant phosphatase activity against pyridoxal phosphate, and has low beta phosphoglucomutase activity. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.	2.65834e-32
NC_013729.1\|WP_012921909.1\|4658597_4659833_-\|MFS-transporter	gnl\|CDD\|340887	cd17329, MFS_MdtH_MDR_like, Multidrug resistance protein MdtH and similar multidrug resistance (MDR) transporters of the Major Facilitator Superfamily. This family is composed of Escherichia coli MdtH and similar multidrug resistance (MDR) transporters from bacteria and archaea, many of which remain uncharacterized. MDR transporters are drug/H+ antiporters (DHA) that mediate the efflux of a variety of drugs and toxic compounds, and confer resistance to these compounds. MdtH confers resistance to norfloxacin and enoxacin. MdtH-like MDR transporters belong to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	2.66345e-67
NC_013729.1\|WP_012921929.1\|4676838_4680153_-\|carbamoyl-phosphate-synthase-large-subunit	gnl\|CDD\|235393	PRK05294, carB, carbamoyl-phosphate synthase large subunit.	0
NC_013729.1\|WP_012921923.1\|4672988_4673303_-\|30S-ribosomal-protein-S13	gnl\|CDD\|235358	PRK05179, rpsM, 30S ribosomal protein S13; Validated.	1.60324e-05
NC_013729.1\|WP_041289431.1\|4668174_4669314_-\|winged-helix-DNA-binding-domain-containing-protein	gnl\|CDD\|377630	pfam06224, HTH_42, Winged helix DNA-binding domain. This family contains two copies of a winged helix domain.	1.63321e-44
NC_013729.1\|WP_012921917.1\|4666325_4667891_+\|alpha/beta-hydrolase	gnl\|CDD\|312032	pfam08386, Abhydrolase_4, TAP-like protein. This is a family of putative bacterial peptidases and hydrolases that bear similarity to a tripeptidyl aminopeptidase isolated from Streptomyces lividans. A member of this family is thought to be involved in the C-terminal processing of propionicin F, a bacteriocidin characterized from Propionibacterium freudenreichii.	1.07575e-15
NC_013729.1\|WP_012921910.1\|4659926_4660925_+\|winged-helix-turn-helix-transcriptional-regulator	gnl\|CDD\|238042	cd00090, HTH_ARSR, Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric repressors. ARSR subfamily of helix-turn-helix bacterial transcription regulatory proteins (winged helix topology). Includes several proteins that appear to dissociate from DNA in the presence of metal ions.	1.21389e-12

>NC_013729.1|WP_012921919.1|4669357_4670338_-|hypothetical-protein
MKCSFLRRLLAVALPLAAVLVPAGSAAADDPMCSLPSVGDVYAYQQAPEASVLTGRVTPKAGCPSTGILTAVRSGEQIFFGDAMFEVPLGTQSGDWYLSSFTVHDVASGTSQTRTFQPVAPYLLRVLDQTRITSTAPASYVGYGDLVTVSGYLEGWTAADGWRRMPGRDLSITTGNGVDGHPNVPTVTDASGAYRLDVRIYNSFAGSVVFAGDERWLGSSGFNDAQVHGLVSVSVSDRTPAVGQRVVVTGKVAPGAVPVWVERRVGTQWVKVTATVAAGADGRYRLTYRPDTRGVQQLRVWNDGTEPQSRMGVQPYVKEFELAVHR
>NC_013729.1|WP_041289431.1|4668174_4669314_-|winged-helix-DNA-binding-domain-containing-protein
MKLSWQSVVARRMQRHHLRVPSGGSPAEVVRAMCGAHAQVLSAGEVSVALRLESATRLDVQQALWQDRTLVKTFGPRGTVHLLPTEDLPLWTGALGALPSSGSQPTAEMRMTSEQTAEVVAAIGGALSEHDLTVDELTDEVVARTGAWAGDLVMPAFQGYWPRWRQAIPAAATAGVLCYGPNRGRKTTYTNPHRFAPPFTPQNGEEALSELLRRYLYAYGPATPQQFAKWLGTSPAFVTKVFQRSDLQQVELDGEPAWLVEGDTEWPAEPARGVRLLPYFDAYAVGSHPRDRVFPGKASTRALAGGQAGNYPVLLVDGLVAGVWHQRKAGRKLQVTVEPIDELGAGQLRALDDVVQRLGEIVDAQPVLTIGEITVGPHA
>NC_013729.1|WP_012921917.1|4666325_4667891_+|alpha/beta-hydrolase
MPKRALLALGLAVLSSVTVSTFSASATPLGTDARPQTQPTPAGGVASVPVPVLNWAPCDTSGDGYQCTTAQVPLDYSQPQGAKVTLSLIRKPATVPSQRIGSLFTNPGGPGLAASLMVRDLGENAPVELRERYDIVGFDPRAVGGSTPKVSCVTLPEYAEQWAATPGRLSSGGFERAVTFGKRFSDGCVANNAALLPHLGTENTARDMDLLRAAVGDEQLNFFGFSYGTYLGTVYANLFPQRTRVLALDGAVGPDSFVNRPYDNNHRQYVAAEASLNRFFAWCTKSPADCSFGDGRPADAFRRLQASLDVTPVRDANGKVVARGGLFTFWVSLELGYGQSNWSWLATELQKAATTRSGALVSPMSDAYTRYMNLNTAIECADRRFPQDVNLLRGKLAAAIQAAPLLGPALAHGPANYDQGHAQACAQWPAERKSSYAGPWNAPGAATALVIGTTHDPDVPFQDAVELTNALDNARLLTFEGTTHTTWHYSACTRSIITRYLIDGTLPPHHTVCADEPMPTR
>NC_013729.1|WP_012921915.1|4664739_4665933_-|methionine-adenosyltransferase
MARRLFTSESVTEGHPDKIADQISDSILDALLAEDPKSRVAVETLITTGLVVVAGEVTTSAYVDIPGIVRSRILEIGYDSSLKGFDGASCGVQVAIGSQSPDIAQGVNTAYESRTDSSQDALDLQGAGDQGLMFGYASNETPELMPLPITIAHRLSERLSEVRKDGTMAYLRPDGKTQVTVEYDGDKAVRVDTVVVSSQHAADISLDSMLTPDVKKHVVDPILEQFEIDSTDYRLLVNPTGRFEIGGPMGDAGLTGRKIIIDTYGGMARHGGGAFSGKDPSKVDRSAAYAMRWVAKNIVAAGLAARAECQVAYAIGKAAPVGFYVDTFGTETVPVDKITDAVLEVFDLRPAAIIRDLDLLRPIYTQTAANGHFGRTGDDFTWERTDRVDALKAAVAK
>NC_013729.1|WP_012921914.1|4664460_4664646_+|hypothetical-protein
MCPVDETEGDDVQTGRADRVRQAAQSSARPAAGNELQHVDPCRAAMQWAVSTSPTIHQLTR
>NC_013729.1|WP_012921913.1|4662228_4664268_-|primosomal-protein-N'
MALNGDSPEQLTLLRETVRRSRTKEPAGITETLPVARVAVDVSLPHLDRPFDYLVPDDLADAAQPGARVKVRFAGKDLDGFVLDRLATSEHDGKLSRIRKVVSPEQVLTPEVADLCRAVADRYAGVFADVTRLAVPPRLAKVEAEALRCNQPVRPVSSTSLSEWAPYPRAEGFLDAVRREEAPRAIWTAVPGADWALAFAQAAAVCASTGRGALLLAPDARDLERLAAACAKVLGRDGFVTLSADLGPTARYRAFITALRGCTRVVIGTRAAAFAPVSNLGLVALWDDGDDSYAEPRAPYPHAREVLLLRAYRQQCAALLGGFARSAETAALLESGWAAELIAERTVIRAAAPSVHIAGESDRDLARDPAARAARLPHQAFEVAREGLRTGPVLVQVPRAGYLPSLVCQTCRTPSRCSTCGGSLRRTGSSGPASCSVCGRPATDHRCPECGDTRMRAAVVGARRTAEELGRAFPGVLVRTSGGDHMLDQIPDQPALIVTTPGAEPVPEKGYSAALLLDTWLLLARPDLRAPEEAVRRWFNAAAMVRSARDGGQVIMMGEPSATPLQAVVRWSPEGFATRELDERRAARLAPAAKLAELVGASEAVADMVARVRQLVDPAAGLEVLGPVDVDDETVRAVVRTPRAYGSALARVLKEALSARGTKKLAGPLRVQVDPATFG
>NC_013729.1|WP_041290359.1|4661095_4662031_-|cyclase-family-protein
MPSQDDVLAYFDTLSNWGRWGDDDELGTLNHITDDVRLAAARAVRHGRSVSCGWEVAVPAEMERSTTTCPCAADMPGAEHMPAPFRNDRRWGYSNERLGIMFHGNTITHLDSPCHLFWDGRMYNGRSHALVDTATGSSWAAVTAAANGILTRGVLLDVARVRDVPWLEPGQGVFPDDLEQAERRQGVRVRPGDAVLLRTGYGRVRHDAGGTGGFTQAGWHASCLPWLQERGVALIGADTPQDVQPSGYDDVLMPVHAVSLVAMGLWMLDNCDLEACAATAVELGQWDFQLAVAPVRFAGTSGSPVNPIATF
>NC_013729.1|WP_012921910.1|4659926_4660925_+|winged-helix-turn-helix-transcriptional-regulator
MISIRLNTDDVSRIRFAFSPLWEAVTSVRALSNNSFGSVHGPWLRKVRPIADGDDLTLLRALIPPVGYIPDFITPAPPRRSTSFESGLATVAATPHELVVSEISQLHAETPDPLLPGLIADPAGALTQITAALRSYWQRTIEPDWARMRALLQEDLVFRLDELAAGGLDRLFRNLHPSIRLTGDRIEIDRPFFSCDGVPLAGQGVLLVPCVFTWPAGLAVTAAPHVPTITYPPRGLGRLWENQQDTTGSPLADLVGRTRAAIVSHLDLPMSTTHLAHALDVSAPTLSVHLGILRSAGVVDSRRDGRTVLYYRTALGNHLLAASGTTTLHESA
>NC_013729.1|WP_012921909.1|4658597_4659833_-|MFS-transporter
MTAIGAPRERAPKLPRAFWALWVCQLVNRLGSFVQPFLVLYLTQDRHLSPGTAGAVAAAVGAGSVVSQLVGGWLSDRIGRRRTMLIGFLGTAAALILLGSAGSLEMIAVTAFTVGLLGDLFRPAVQATVADLLDPRERVRAYGLLFWAINLGFSVSTVSAGVLASVGYSLLFWINAATSVVAALVIWRMVPETRPVLDEGPRRSLLPVALRDTTFVLMILIQIGYATIYFQGYSTLPLAMAADGLPSATYGLVIALNGVVIVVVQPFVGRRLAAFDRPRLLAGSMLLVGLGFGIGAVVHSWWGYGLSVVVWTIGEIGFAAVIGAVFADLAPVDLRGGYLGLAGSMSFGLGSVIGPLIGTNALEHLGATATWLACAVLGVVLFLAQLGMSPALHARANAAGERDPDFRRVEA
>NC_013729.1|WP_012921908.1|4657977_4658601_-|HAD-family-phosphatase
MIEQKVDVVVFDIGGVLLDWNPDYLYAELIPDEQQRRHFLTAITTPEWNMQQDAGRPWAEAVAELSALHPEHAEWIAAYDTGWLKMVKGLLDDTVDLLTELQAQGVPTYALTNFSGEKWAVAKETFPILDSFAGEVVSGHEQVVKPDEKIYRILIERFALDPARTFYTDDVQRNVDGARAAGLDAELFTTAGTLRTQLRDRGLALRP
>NC_013729.1|WP_041290361.1|4670535_4671789_-|bifunctional-phosphopantothenoylcysteine-decarboxylase/phosphopantothenate--cysteine-ligase-CoaBC
MTRPVHPPKKPSVVLGVGGGIAAYKVCDLLRRLTESGHQVRVVPTAAALEFVGAATWAALSGQPVTADPFGYVHEVPHVRIGKGADLVVVAPATANLIAKAAHGLADDLLTNTLLTARCPILFAAAMHTEMWEHPATQANVAILRSRGITVLDPAVGRLTGADTGRGRLPEPAEIFAISQLMLADSTARAAGESVADLTGKHVLVSAGGTREHLDPVRYLGNSSSGKQGYALARIAAARGAKVTLVAANSELPDPAGVQVVPVTSTRDLYDEITGRAADADAIVMAAAPADFRPADVAEHKIKKTEDGAVPAVQLVQNPDILATVAHDRQRAGQVIVGFAAETGDASHSVLDLGRAKLARKGCDLLVVNDVSGGKVFGSDLNEAVVLDRDGNALPVPSGSKDALAGVIWNLVASRWH
>NC_013729.1|WP_012921921.1|4671940_4672255_-|DNA-directed-RNA-polymerase-subunit-omega
MSGNQPVAIGITSPPIDDLLTHTDSKYKLVLYSAKRARQINAYYSQLGEGLLEYVGPLVETHVQEKPLSIAMREINDGVLTCTDIDPEAEAEAAAAAAEKSAAE
>NC_013729.1|WP_049797609.1|4672257_4672818_-|guanylate-kinase
MTVLAGPTAVGKGTVAAEIRERFPDVWISVSATTRKARPGEVHGVHYLFVSDDEFDRMIADGELLEWAVVHKAARYGTPKQPVLDKLAAGRPALLEIDLQGARQVRATMPEAHFVFLAPPSWDELVRRLVGRGTETADERERRLETAVLELAAEKEFDVTIVNASVREAADQLVKLIRSPSISGKS
>NC_013729.1|WP_012921923.1|4672988_4673303_-|30S-ribosomal-protein-S13
MPLPSLTPEQRAAALDKAAAARRERAEIKNRIRHSGASPTEVLQEGQTNEVIGKMRVSALLQCIPGVGKVRAQQIMQRAGISETRRVRGLGSNQIAALMREFAE
>NC_013729.1|WP_041290362.1|4673894_4674230_-|hypothetical-protein
MSVGVLTACSGGDYCAELKSYAEAVKGLDIKDSGAVDKMRGEAKKLSKSAPDDLKDDWKVVLDYSEKAKDAGGDQTKLAELAKNDGEKIGKASEAIAKHAKDTCKVSIENS
>NC_013729.1|WP_012921926.1|4674405_4674804_-|hypothetical-protein
MPARRQYAAAAALVVAAVIGVTALTAPSGNDQAADYCTGLRTYTTALGGFNDPSDTAALDKLIQDASGLAKSSPDSLKADWTLLHGYLEDVRAADGDQAKLQQIGAATGRQASEAGQRIAEHGTRSCGITTA
>NC_013729.1|WP_041289432.1|4674803_4675640_-|orotidine-5'-phosphate-decarboxylase
MSNQPFGTRLRAAMVDRGPLCVGIDPHAHLLESWGLPDTTEGLAAFTNGVVDALADRVAVFKPQSAFFERFGSAGIAVLEQATIRLREAGALVIIDAKRGDIGTTMAGYAAAYLAEKAPLACDALTVSPYLGFGSLQPTIDEARAAGAGLFVLALTSNPEGPQFQSARTTDGPTVAGAVLDGLRALNADTEDLGSFGAVVGATIAKTDENLDIRGPLLAPGLGAQGATAESLLEVFGPAVRNVVPASSREILGAGPDARGLQDAAARANDAYRAVLGY
>NC_013729.1|WP_148257044.1|4675657_4676821_-|quinone-dependent-dihydroorotate-dehydrogenase
MVRPVLYRLGRGDAEVAHEQTLHGLRRLTRVPGAVSALSRSYGALPAGLARTVFGVRFPSPVGLAAGMDKNGIALPAWRALGFGFVEVGTVTAHPQPGNEKPRLFRLVESEAVINRMGFNNLGSAALADRLAAYGPLGYPLGISIGKSKVTPIEDAVEDYVTSLRRLYRFGDYFAVNVSSPNTPGLRSLQDAGHLRELLAALHTEAAALAGSGSGSGFGATSGSGAESRSGAESGSGAESGSGSGAVKPILVKIAPDLTEAAIDELLGVCTDAGVAGIIATNTTIGREALAPADQALAAEAGGLSGRPLTEISAKTVAHIHAETGGALPIIGVGGILDPSDAARLIDAGASLVQLYTGLIYRGPGLVRATNRLLAANHRPATPSTPS
>NC_013729.1|WP_012921929.1|4676838_4680153_-|carbamoyl-phosphate-synthase-large-subunit
MPRRTDIESVLVIGSGPIVIGQACEFDYSGTQACRVLKEEGFRVVLVNSNPATIMTDPEFADATYVEPITPEFVEKVIEKERPDVLLATLGGQTALNAAIALHDNGVLDKYGVELIGASVDAIQRGENRESFKAIVETLGAEVARSVVCHTMDDVLGAAAEMGYPLVVRPSFTMGGVGSGMAYNELDLRRIAGAGLVASPTTEVLIEESIVGWKEYELEVMRDKADNVVIVCSIENVDPMGVHTGDSVTVAPAMTLTDREYQTMRDLAIGIIREVGVDTGGCNIQFAVNPADGRLIVIEMNPRVSRSSALASKATGFPIAKIAAKVAIGYTLDEIPNDITRQTPASFEPTLDYVVVKVPRFAFEKFPAADATLTTHMKSVGEAMAIGRNYTEALQKALRSLEKPEARFSWAGPPATELEPLLERIRTPHDGRLRTIMDAIRAGATPEQIHDATRIDPWFVDQLYLIHETALQVAAAPRLTPDILRLAKRHGFSDLQLAEIRDLAEDVVRGVRQALGIRPVYKTVDTCAAEFAAATPYHYSSYDEETEVAPRTKPAVLILGSGPNRIGQGIEFDYSCVHASMALRDAGYCTVMVNCNPETVSTDYDTSDRLYFEPLTCEDVLEIVYAEMQAGPIAGVIVQLGGQTPLGLAQRLADAGVPIVGTSPQAIHLAEERGAFGKVLAEASLPAPKHGTAMSFGEAQEIAAEIGFPVLVRPSYVLGGRGMEIVYSDAELTAALRRLSGDQLAADWEHPVLIDRFLDDAVEIDVDGLFDGEELFLGGVMEHIEEAGVHSGDSSCALPPITLGNADIEKIRQSTEAIARGVGVRGLLNVQYALAGDVLYVLEANPRASRTVPFVSKATATPLAKAAARVMLGATIAQLRTEGMLPQTGDGGTLPPSTPIAVKEAVMPFNRFRTIDGSSVDTVLGPEMRSTGEVMGIDDTFGTAFAKSQAGASQPLPGSGKVFVSVANRDKRHMIFPVKRLADLGFQIYATEGTADVLRRNGVEAVTVRKSSQGPGPNGEPTIVQMVQDGELNLIVNTPIGVTQGGSPRIDGYEIRSAAVARNIPCITTVQGLAAAVQGIEAQQAGGIGVRSLQDWVSRIRGQQ
>NC_013729.1|WP_012921930.1|4680152_4681286_-|glutamine-hydrolyzing-carbamoyl-phosphate-synthase-small-subunit
MSQPASGPALLVLEDGRAFAGTSYGATGETFGEAVFTTGMTGYQETLTDPSYHRQIVTQTAPHIGNTGVNDEDDESQRIWVAGYVVRDPARVPSNWRATRTLDDQLKAQGIVGISGIDTRALTRHLRERGAMRAGISTEILDPAQLLRKVLEQPQMTGADLASEVTVTEPYVVPAEGDKRFTVVALDLGIKSMTPKRMAERGIEVHVLPSTASLEEILARDPDGIFMSNGPGDPQTTEHPTTLLKALLEQNKPYFGICFGNQVFGRALGLGTFKLKYGHRGINQPVLDRATGKVEITSQNHGFAVDAPIEESVETPYGTAEVSHVSLNDNVVEGLRLTGRDGRVLAFSVQYHPEAAAGPHDSAYLFDRFVELMEGRS

You can click texts colored in the table to view more detailed information

Click the colored protein region to show detailed information

Crispr_ID: NC_013729_7

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NC_013729_7

4771428-4771577

Orphan

Consensus_repeat	Method
GAGCACCCGCCAGCCACGAAATCGTCGTACGAGTAGCTGGCGGGTGCTC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NC_013729_7

>merge|NC_013729|7|4771428-4771577|CRISPRCasFinder
GAGCACCCGCCAGCCACGAAATCGTCGTACGAGTAGCTGGCGGGTGCTCACAGTCAACGCGATGTGGCCAGTCGCGGCTCCCCGTGCCACGCACCGACCTCGAGCACCCACCAGCCACGAAATCGTCGTACGAGTAGCTGGCGGGTGCTC

>NC_013729|7|6|4771428-4771577|CRISPRCasFinder
GAGCACCCGCCAGCCACGAAATCGTCGTACGAGTAGCTGGCGGGTGCTC	ACAGTCAACGCGATGTGGCCAGTCGCGGCTCCCCGTGCCACGCACCGACCTC
GAGCACCCACCAGCCACGAAATCGTCGTACGAGTAGCTGGCGGGTGCTC

Protein	Signature genes	Signature genes Name	Protein_function
NC_013729.1\|WP_148256698.1\|4767765_4767984_-\|hypothetical-protein	unknown	unknown	unknown
NC_013729.1\|WP_012922013.1\|4769359_4770715_-\|PLP-dependent-aminotransferase-family-protein	unknown	unknown	gnl\|CDD\|224089
NC_013729.1\|WP_012922011.1\|4766102_4767779_+\|TIGR04141-family-sporadically-distributed-protein	unknown	unknown	gnl\|CDD\|275009
NC_013729.1\|WP_012922022.1\|4779006_4780464_-\|DUF2029-domain-containing-protein	unknown	unknown	gnl\|CDD\|227937
NC_013729.1\|WP_012922017.1\|4774278_4774752_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|184712
NC_013729.1\|WP_012922018.1\|4774932_4776096_-\|HAMP-domain-containing-histidine-kinase	unknown	unknown	gnl\|CDD\|223715
NC_013729.1\|WP_012922014.1\|4770852_4771356_+\|hypothetical-protein	unknown	unknown	unknown
NC_013729.1\|WP_012922015.1\|4771648_4773304_+\|bifunctional-3'-5'-exonuclease/DNA-polymerase	unknown	unknown	gnl\|CDD\|237876
NC_013729.1\|WP_012922021.1\|4778056_4779010_+\|threonine/serine-dehydratase	unknown	unknown	gnl\|CDD\|107205
NC_013729.1\|WP_012922004.1\|4759410_4760016_-\|helix-turn-helix-transcriptional-regulator	unknown	unknown	gnl\|CDD\|366102
NC_013729.1\|WP_012922024.1\|4781398_4782403_+\|serine/threonine-protein-kinase	unknown	unknown	gnl\|CDD\|270916
NC_013729.1\|WP_012922023.1\|4780622_4781279_-\|HAD-family-hydrolase	unknown	unknown	gnl\|CDD\|223620
NC_013729.1\|WP_012922020.1\|4777129_4778023_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|223267
NC_013729.1\|WP_012922012.1\|4768381_4769287_-\|pyridoxal-5'-phosphate-synthase-lyase-subunit-PdxS	unknown	unknown	gnl\|CDD\|179769
NC_013729.1\|WP_012922009.1\|4763216_4764083_+\|hypothetical-protein	unknown	unknown	unknown
NC_013729.1\|WP_148256697.1\|4762224_4762653_-\|hypothetical-protein	unknown	unknown	unknown
NC_013729.1\|WP_083792896.1\|4773307_4774309_-\|sigma-70-family-RNA-polymerase-sigma-factor	unknown	unknown	gnl\|CDD\|236196
NC_013729.1\|WP_012922006.1\|4761417_4762161_+\|MerR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|133378
NC_013729.1\|WP_041289438.1\|4776177_4776879_-\|response-regulator	unknown	unknown	gnl\|CDD\|223816
NC_013729.1\|WP_085956231.1\|4760095_4761355_+\|FAD-binding-oxidoreductase	unknown	unknown	gnl\|CDD\|223354

Protein	Function_ID	Function_description	E-value
NC_013729.1\|WP_012922013.1\|4769359_4770715_-\|PLP-dependent-aminotransferase-family-protein	gnl\|CDD\|224089	COG1167, ARO8, Transcriptional regulators containing a DNA-binding HTH domain and an aminotransferase domain (MocR family) and their eukaryotic orthologs [Transcription / Amino acid transport and metabolism].	1.23927e-78
NC_013729.1\|WP_012922011.1\|4766102_4767779_+\|TIGR04141-family-sporadically-distributed-protein	gnl\|CDD\|275009	TIGR04141, conserved_hypothetical_protein, sporadically distributed protein, TIGR04141 family. This model describes a sporadically distributed conserved hypothetical protein in which complete members average over 500 amino acids in length, although matching sequences frequently are truncated or broken into tandem ORFs. Regular co-clustering with known markers of mobility (integrases, transposases, phage proteins, restriction enzymes, etc.) suggests this family also is part of the mobilome. The function is unknown.	5.61789e-155
NC_013729.1\|WP_012922022.1\|4779006_4780464_-\|DUF2029-domain-containing-protein	gnl\|CDD\|227937	COG5650, COG5650, Predicted integral membrane protein [Function unknown].	4.35514e-29
NC_013729.1\|WP_012922006.1\|4761417_4762161_+\|MerR-family-transcriptional-regulator	gnl\|CDD\|133378	cd00592, HTH_MerR-like, Helix-Turn-Helix DNA binding domain of MerR-like transcription regulators. Helix-turn-helix (HTH) MerR-like transcription regulator, N-terminal domain. The MerR family transcription regulators have been shown to mediate responses to stress including exposure to heavy metals, drugs, or oxygen radicals in eubacterial and some archaeal species. They regulate transcription of multidrug/metal ion transporter genes and oxidative stress regulons by reconfiguring the spacer between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates.	1.99255e-19
NC_013729.1\|WP_012922017.1\|4774278_4774752_-\|hypothetical-protein	gnl\|CDD\|184712	PRK14501, PRK14501, putative bifunctional trehalose-6-phosphate synthase/HAD hydrolase subfamily IIB; Provisional.	0.00537578
NC_013729.1\|WP_012922015.1\|4771648_4773304_+\|bifunctional-3'-5'-exonuclease/DNA-polymerase	gnl\|CDD\|237876	PRK14975, PRK14975, bifunctional 3'-5' exonuclease/DNA polymerase; Provisional.	0
NC_013729.1\|WP_012922021.1\|4778056_4779010_+\|threonine/serine-dehydratase	gnl\|CDD\|107205	cd01562, Thr-dehyd, Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. Although the nitrogen atoms of most amino acids are transferred to alpha-ketoglutarate before removal, the alpha-amino group of threonine can be directly converted into NH4+. The direct deamination is catalyzed by threonine dehydratase, in which pyridoxal phosphate (PLP) is the prosthetic group. Threonine dehydratase is widely distributed in all three major phylogenetic divisions.	5.71562e-120
NC_013729.1\|WP_012922004.1\|4759410_4760016_-\|helix-turn-helix-transcriptional-regulator	gnl\|CDD\|366102	pfam00440, TetR_N, Bacterial regulatory proteins, tetR family.	1.62998e-07
NC_013729.1\|WP_012922023.1\|4780622_4781279_-\|HAD-family-hydrolase	gnl\|CDD\|223620	COG0546, Gph, Predicted phosphatases [General function prediction only].	1.38147e-26
NC_013729.1\|WP_012922020.1\|4777129_4778023_+\|hypothetical-protein	gnl\|CDD\|223267	COG0189, RimK, Glutathione synthase/Ribosomal protein S6 modification enzyme (glutaminyl transferase) [Coenzyme metabolism / Translation, ribosomal structure and biogenesis].	1.67663e-07
NC_013729.1\|WP_012922012.1\|4768381_4769287_-\|pyridoxal-5'-phosphate-synthase-lyase-subunit-PdxS	gnl\|CDD\|179769	PRK04180, PRK04180, pyridoxal 5'-phosphate synthase lyase subunit PdxS.	0
NC_013729.1\|WP_012922024.1\|4781398_4782403_+\|serine/threonine-protein-kinase	gnl\|CDD\|270916	cd14014, STKc_PknB_like, Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.	6.04791e-102
NC_013729.1\|WP_012922018.1\|4774932_4776096_-\|HAMP-domain-containing-histidine-kinase	gnl\|CDD\|223715	COG0642, BaeS, Signal transduction histidine kinase [Signal transduction mechanisms].	4.70082e-50
NC_013729.1\|WP_083792896.1\|4773307_4774309_-\|sigma-70-family-RNA-polymerase-sigma-factor	gnl\|CDD\|236196	PRK08241, PRK08241, RNA polymerase subunit sigma-70.	1.3324e-134
NC_013729.1\|WP_041289438.1\|4776177_4776879_-\|response-regulator	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].	9.27119e-80
NC_013729.1\|WP_085956231.1\|4760095_4761355_+\|FAD-binding-oxidoreductase	gnl\|CDD\|223354	COG0277, GlcD, FAD/FMN-containing dehydrogenases [Energy production and conversion].	5.07236e-31

>NC_013729.1|WP_012922014.1|4770852_4771356_+|hypothetical-protein
MKRSIVAAGAGALALAGSVLAAPVAHAEERVCRGTLGAVTVDNVRVPVGASCTLNRTTVKGTVKVESNARLSTSSARVNGNVQAEGHAHVYLYASTVGGSVQLKQGRTASLRSNQVKGDVQSFTNRGAQDFTANRIDGNLQCKSNVPAPTGSGNVVGGTKEDQCRRL
>NC_013729.1|WP_012922013.1|4769359_4770715_-|PLP-dependent-aminotransferase-family-protein
MWRGSDLDPVDGTKTEQVEALVLRRIERGDLSIGSRLPSERVLAERLGVSRVTVVRALDQLRADGVLETRRGSGTHVRPLDRLLDPIAPVSTVTAGDQPVLDLRFATTAAPHDVAEVAAQIVAEGLPQAMGGDGPPPGGSLELRTALAERLTLEGVPTEPGQLTLTVGAAAGLNAALAGLDLGPGVAITETPTYPAAFDLLRNHRLDVVGWPAGVWDTDQLAHLCRRHKPKVIYLQADNHNPTGLSLPADRRTAVVEIARRYGAALISDETMRPLWLAGGKQADPLSRYPRTVSVGSLSKTVWGGLRVGWVRTGRQLRRKINTSARLSVTSPSALDDLLALAILDRLDRVISRRKTRLRANLAALENGLDTVPGVAWATPTGGMTLWLELTEVRSRRALEAAREQGLLLGAGDLFTPDGTDRRHLRIPFTAPPATLRLVVARLAAAIAQSS
>NC_013729.1|WP_012922012.1|4768381_4769287_-|pyridoxal-5'-phosphate-synthase-lyase-subunit-PdxS
MTDTETTTPQTGTAKVKRGMAEMLKGGVIMDVVTAEQARIAEDAGAVAVMALERVPADIRAQGGVSRMSDPDMIDSIIAAVSIPVMAKARIGHFVEAQVLQSLGVDYIDESEVLTPADYANHIDKWQFTVPFVCGATNLGEALRRITEGAAMIRSKGEAGTGDVSNATTHMRQIRQELRRLQNLPEDELFVAAKELQAPYELVKEVAAAGKLPVVLFTAGGIATPADAAMMMQLGAEGVFVGSGIFKSGNPAQRAEAIVKATTFYDDPDVVAKVSRGLGEAMVGINVDEIPQPHRLAERGW
>NC_013729.1|WP_148256698.1|4767765_4767984_-|hypothetical-protein
MTPALALYELLFDAAPRRPAKETPSTTAVEVAGWLGPLGELAAEVMIAGTRLPHEAVGYELLSAESEVLNRI
>NC_013729.1|WP_012922011.1|4766102_4767779_+|TIGR04141-family-sporadically-distributed-protein
MVHRAPRSRNLTLHRLWRTPADPAGLIDALDQEQLNLLEQFEFTAVTVGGAAGLWVQGSYRTRDGESAEWCAAASRTTGQAVHFVDARSAGLLLLIIDGRSYAIGYGQGFRLLSSDEKDRRFGLEFAIRALDPKHVSKLMRRRPGHRGRTEVTRMPEGSPIWAFDVTDAYADLVGSASGKSESFQLTHTKADKPVPVDGGVGLHIRLATDPIEMVADIRTIAEVLARERQPELEFADRVRPLYDKTLLAQLEADFEALLSSTPDEVRHRLSSVVPTELAELVDDVRTFKVTLGGGTRTTTEIAVENLLNRASILQAGTRVRAFREGRITAFQDDGASYSVGDARAIDWLEAVLPVDDQHFALVDGQWYEIDAGYQVRLQEHVEELLAVHSDLVLPDWRPHHTEGQYNDAAGLDPDLGLVCLDRKGVRDEFHRRWGFEACDLLGPDNELIHVKKASGSSPLSHLFMQACVAVQGLEGSSTARTRFRELVRKHGRGRELAEGFEPTKVVFGILLKAGEEVTSKTLFPFAQAALVQASRFLHSARIDVEVRAIHLADVRSD
>NC_013729.1|WP_012922009.1|4763216_4764083_+|hypothetical-protein
MNHALDLGSRKFWRLVGKPVDLAVDHSWLRAPMSRSSAVGDGWLSAEATHHGGTVDEDAATADPSAGPAPGLLPAMTILDGPGFDASRLDPRIRDFYEHTAAWHMEVWTGWSPLFWPAGELIARLFGRRVEQLSLPMRPLDVAYGMDSRVRVIRNRDGEQVGAAWLRTLRPSGRYVFSGCYSARRLPGAAQPSVHVAFPLESGNVQVFLRPVNSDGGGLVLESPPGRFGQDGAYVVVHDDGRDFAARVPLHETFRLYCDPYGVLRTDHELRIGRTWMMRLHYKMEHAR
>NC_013729.1|WP_148256697.1|4762224_4762653_-|hypothetical-protein
MAEILRHSDCADLPPSFGDRRRRARHRDERAGRHDMLLYESAMQVVPVLLIALFIETRSVDPQASRAMRRWVNVHDRGYAALGIVAFMVSMLVVADIVAAGRAPAAIVIATLSGCMGMLYTRILQRFAHDRGPRRDQASADR
>NC_013729.1|WP_012922006.1|4761417_4762161_+|MerR-family-transcriptional-regulator
MAWSTREIAQLAGTTLRAVRHYHDIGLLAEPQRRTNGYKQYEVAHLVRILRIKRLTELGFSLSQIATMDDTDDQPVEALRTLDAELAATIERLQRARVELGVILRQPTPAELPPGFAASDVVARMSPADRSFIVVLTRVLGAETMRAWADLLREPVIDPVAQRFDTLPADADEQTRAAVARDLVPYVRTLSAKHPDVKITNAGTRYSARYVEQAVGQALRELYNSAQLDVLRRISRLLSDPHDQPAQ
>NC_013729.1|WP_085956231.1|4760095_4761355_+|FAD-binding-oxidoreductase
MLTSGTEYEAALSIWNGAVTSRPLAVVRCAGPADVQAGVRTAREKGLPLSVRGGGHDWAGRALADGGLTLDLSPMRQVSVDPVTAIATVAGGATAADVAAAAQRAGLVAVTGTAGSVGMAGLTLGGGYGPLSGRFGLAADNLLSAGVVLADGTLVTADDEHDPELLWALRGGGGNFGVVTTMRIQLHAVPAILAGMIMYRFDALPELEESLLRGPDELTVQAGFITTPTGEPALFAAPTWCGDPEVGTRELQRLTELGEPLAAQVGPTTMVDQLAQIDAMFPAGRHVEIATRTVTGLDRTVQDILLDAANAKTSPLSAISLHSLHGAAARVPADATAFRNRTPHLMVETIAVWEPGDPDEKRHRDWVRATDRLPGGYPNLLGPDDTERTAAVFGPNTERLVAAKRRYDPELVFHAPGKL
>NC_013729.1|WP_012922004.1|4759410_4760016_-|helix-turn-helix-transcriptional-regulator
MTEPPRGRRAEYAAATRAAITDAARLLFARHGFFATKIDDIAAEARVAPATVYAVAGGKQGLIRTLVDLWSQAPIVAQTLSQIETLTDPDEILRHTAAVVRSMRETYGDIIRLVLSTAPHNPEVAENLRVATTRYREAIETVATRLHDVGGLREGTTVAEASDILWFYFGYSGYFTLHDDNGWTYERSESWLVTQAAAALR
>NC_013729.1|WP_012922015.1|4771648_4773304_+|bifunctional-3'-5'-exonuclease/DNA-polymerase
MDERWAVAPVEGGGALLVALHPDGQPAGPIRREPDLAAAIGSRPQVSRWVWRSTAEIYPRLLAAGVRVERCYDVECAEVLLLGHEGRLGEPRSAAAAWARLTDQPVPPDPPMRAAEPGEQSSLFEIESEPLPFEALLRVYADQLRRHQQAEYPERMRLLTASESSGMLIAAEMDRAGLPWSAETHRALLTELLGERYAGGGEPRRLTELAEQVSAAFGRRVRPDLPADVLKAFKQAGYQLTSTRRWELQTIDHPAVEPLIEYKKLYRIYTANGWSWLNDWVHDGRFRPGFVPGGTVSGRWITNGGGGLQIPKVIRRAVVADPGWRLVVADASQLEPRVLAAISRDPGLMEVAGNAADLYKAVSDKAFSGDRAMAKLAVLGAIYGQTSGDGLKNLAALRKRFPKAVAYVDDAARAGEEGRLVRTWLGRTCPPSGSQLDSAQLEGPPADEPQVDSRRARARGRFTRNFVVQGSAADWALLMMAALRQSIATYKAELVFFQHDEVIVHCPAEEADQVAAAIQAAGDLAGTLTFGATPTRFPFGTAIVQCYADAK
>NC_013729.1|WP_083792896.1|4773307_4774309_-|sigma-70-family-RNA-polymerase-sigma-factor
MHHRAGGRQLTEDAFAEQTERYRHELRVHCYRMLGSYDDAEDLVQETFLRAWRHRADFEGRSSFRAWLYRIATNACLDDLRRPQRVLPYQLEPASWPTDPRPGRDDLPWLQPYPDVLLDRAEEPDAQVIRRETIELAFLTAIQQLPARQRAVVIFRDVLGWPAKDTAELLGTTVASVNSALQRARPVLREHLPPRRTEWAPAGDPSAVEQALLTKYLEAFEAGDAPALAALMHEDVRVTMPPYPFWYAGRDRAEQVFAANFEPGGPANRGAWRFLISGVNRQPALAAYLRVPGDTVFRPFGFDVFRIENGLIAELTAFELTDFPAYGLPGRLT
>NC_013729.1|WP_012922017.1|4774278_4774752_-|hypothetical-protein
MLLAAGAVLLLLFVVYGSWTAGRLDRLHHRVATARARLETELARRSALVAELAGSGVLDPASSLLLLDAAHRARTAPEEEREQRESALTRAIVATGTDVQPWAGELAAALRRVQLARRFHNDIVVSTRELRRRRLVTWFRLAGHAPMPCTIELEDGS
>NC_013729.1|WP_012922018.1|4774932_4776096_-|HAMP-domain-containing-histidine-kinase
MNRDTATIFALTALWTLAVAAFGALVLWRFRRRSLRITMIVVALVPMAAALAAIGQSTRAMFISAHDSLVVMWTLAFSGLLGLLMAVLLAHWISAGSRDVGRRLRDLGTAYESVGVAANGNVPAELAELTNELETTRQRLAASRERERALEASRRELVAFMSHDLRTPLAGLRALSEGLEDGVIDDVPGALRQLRTTVDRMTGLVDDLFELSRLSAAPLPRRRSAVSLHELADDVAGETSEHARSVGVTVTVKAPADDDRLAVHGDADELTRAVTNLVGNAIRHTAPGGTVEIAVDRAPDGRVRLAVTDGCGGIPADDLERVFDIGWRGDEQRTPATVGADTREAGGGLGLAIARGVVESHGGTIAVSNVPGGCAFSIDLPRVTAHS
>NC_013729.1|WP_041289438.1|4776177_4776879_-|response-regulator
MLVVDDDPTVSNVVSAYLTKAGYDARVVPDGVKAVEVWQQWKPSVVVLDVMLPGLSGLEVLRRLRSADDGAAVIMLSARGEEEDRLVGLEVGADDYVVKPFSPRELVLRVQALLRREERLAGLDLTPTKLHAGPVVIDTAARTATLDGAELSLTHREFDLLAFLVAHAGKAYTKVELLRRVWGWDFGDSSTVIVHVRRLREKIEADPSDPKLVLTVPRTGYLFAGDAMAGAGR
>NC_013729.1|WP_012922020.1|4777129_4778023_+|hypothetical-protein
MTVRIALATSADHPDLHEDDQPLVPALRTAGLDPVIEVWSDPSVDWSSYDAVLLRSVWDYHTRYVEFAEWLGQLDKAGVRVLNDSALVRWNADKSYLLELRERGVAIVPSQVAAGACLREVVAGLAGQEIVIKPTVSASALNTVRGVAGSEQLERAMDDLPDTVYLVQPFQREIVTDGEWSLMFFGGVYSHAVVKRPAAGDYRVQHEYGGTVERVEPSPAVLGAATAALAAGSRTAPAYARVDGIVSAGRFLLMELELIEPYLFFPDHAPAVDALATAVADQLAAAQPRGQAVAAAG
>NC_013729.1|WP_012922021.1|4778056_4779010_+|threonine/serine-dehydratase
MPTLDDVRRAADQLSGRIHRTPMVTCSALDAMFGGPLSLKAELFQKTGSFKVRGLLSKTLQLTPEQRERGVVTVSAGNAAGALAWAARDAGVPATVVMATTAVQGKIDAARAYGAQVELVDGDLITAYEAIRDERKLTGVHPFDDLDVITGHGSLGLELLADAPQVRTVLVPIGGGGLISGVALAVKLLDPSVRVVGVEPAGADVVSRSLAAGSPQKLPTAKSLADGLAAPVCGAHTFALISQYVDEVVRVGEDAILAATRLVMSRTKLALEPAAAAPFAALLEGSLQLTGPTASVISGGNLDVGQLFGSGSLGDTP
>NC_013729.1|WP_012922022.1|4779006_4780464_-|DUF2029-domain-containing-protein
MSPVTSRDAQDAQARPAPSEADPAVAGLTVGLGGPTGRFARLSSSWWTPLRIALAVCTVTFALGVLQKAPCMDAGWDRQSWRPFKALCYSDIGYLYQERGFAEGNVPFLDTGNYPVLEYPVLTGGFMEAAAQITWVITGDPEQDVTVEQKRDTAGVFFVVNVVLLFLCALLLVGLTVATARGVATRPGAPRGQPLDALYVAAAPVLALTSTINWDLFAVVLTAGAMYAWSRGKPIWFGVLLGLGTAAKFYPFLLLGPLLIVCLRGRKLWPWFQAVVAAVVAWVLVNAPIYLLAKEEWLSFWVFNDERASDYGSIWYVLKLAGNEVADVNKLNIVIFAGLCLSIAILGLMAPRPPRFAQLAFLVVAAFLLVNKVYSPQYVLWLLPLVALARPKLRDWLVWQACECFYWMMVWLHLAQFLAPGQPEAPDKIYWFSVILRMAGTLWLMIVVARDILLPDKDPVRHGDLVDDPGDGVAPDLPAREPVRV
>NC_013729.1|WP_012922023.1|4780622_4781279_-|HAD-family-hydrolase
MRLKVSHIVWDWNGTLLDDNAAVLAAVNEVCAGFGRPPLSWDEWREVYARPMRLSYERILDRELSEDDWAKVDKLYHERYDLLLHTCGLAPGVPDGLHAWSASGRTQSLLSMWFHAQLVPTIDGFGLTELFSRVDGLTTAVGGDSKAEHLARHLTAQDLDPTDVVLIGDVVDDATAAASVGAQCVLVTTGAMSRTALQATGFPVTDSVPDALTLLATD
>NC_013729.1|WP_012922024.1|4781398_4782403_+|serine/threonine-protein-kinase
MRIAKRYRLESLLGRGGMGEVWRATDEVLDRPVAVKLLPPGQTDPDAMERFRHEALTAAVVNNPHVIGIHDFGPYGDSCYLVMELVDGRNLAAELRRQGPFGPADAAWIAAQVAEGLAAAHHEGVVHRDIKPGNLLMTADRTVKIADFGIACFVTEAAGPDTPDGYVLGTSYYLAPERATAQPAGPAADIYSLGCVLHQLLTGGPPFVADTPTGVLRQHLHGCPVQPTGVRRDFRQFLLRMLAKDPEDRPDANDVAAWCWRTYLNTPRRHLSLLGHRTPAHPPAPSPTALSAMSARSARSAVSAPTVLTADTALTAETAQSTLTADATVPMAAV

You can click texts colored in the table to view more detailed information

Click the colored protein region to show detailed information

Crispr_ID: NC_013729_8

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NC_013729_8

5376412-5376622

Orphan

Consensus_repeat	Method
CCCCAGCCGTCCACCTTGAGCACGCCCCAGCCGTCTGCCTCGGCGCGCGAC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NC_013729_8

>merge|NC_013729|8|5376412-5376622|CRISPRCasFinder
CCCCAGCCGTCCACCTTGAGCACGCCCCAGCCGTCTGCCTCGGCGCGCGACGACTGCCCGGTGCTCAAAGTCGCCCTCCGCCCCAGCCGTCCACCTTGAGCACGGCCCAGCCGTCTGCCTCGGCGCGCGACAACTGCCCGGTGCTCAAAGTCGCCCTCCGCCCCAGCCGTCCACCTCGAGCACGGCCCAGCCGTCTGCCTCGGCGCGCGAC

>NC_013729|8|7|5376412-5376622|CRISPRCasFinder
CCCCAGCCGTCCACCTTGAGCACGCCCCAGCCGTCTGCCTCGGCGCGCGAC	GACTGCCCGGTGCTCAAAGTCGCCCTCCGCCCCAGCCGTCCACCTTGAGCACGGCCCAGCCGTCTGCCTCGGCGCGCGACAACTGCCCGGTGCTCAAAGTCGCCCTCCG
CCCCAGCCGTCCACCTCGAGCACGGCCCAGCCGTCTGCCTCGGCGCGCGAC

Protein	Signature genes	Signature genes Name	Protein_function
NC_013729.1\|WP_012922547.1\|5374524_5376198_-\|methylmalonyl-CoA-mutase	unknown	unknown	gnl\|CDD\|239652
NC_013729.1\|WP_012922545.1\|5371738_5372737_-\|tetratricopeptide-repeat-protein	unknown	unknown	gnl\|CDD\|225660
NC_013729.1\|WP_012922557.1\|5383330_5383768_+\|methylmalonyl-CoA-epimerase	unknown	unknown	gnl\|CDD\|213772
NC_013729.1\|WP_012922555.1\|5381008_5381965_-\|methylmalonyl-Co-A-mutase-associated-GTPase-MeaB	unknown	unknown	gnl\|CDD\|224617
NC_013729.1\|WP_012922556.1\|5381987_5383205_-\|acetyl-CoA-C-acetyltransferase	unknown	unknown	gnl\|CDD\|180261
NC_013729.1\|WP_012922550.1\|5377369_5378116_+\|maleylpyruvate-isomerase-family-mycothiol-dependent-enzyme	unknown	unknown	gnl\|CDD\|274422
NC_013729.1\|WP_012922553.1\|5379688_5380405_-\|PH-domain-containing-protein	unknown	unknown	gnl\|CDD\|367615
NC_013729.1\|WP_148257075.1\|5368151_5368934_+\|NAD-dependent-epimerase/dehydratase-family-protein	unknown	unknown	gnl\|CDD\|223528
NC_013729.1\|WP_012922543.1\|5368930_5369707_+\|IclR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224332
NC_013729.1\|WP_012922537.1\|5362548_5363658_-\|hypothetical-protein	unknown	unknown	unknown
NC_013729.1\|WP_012922559.1\|5385012_5386344_+\|crotonyl-CoA-carboxylase/reductase	unknown	unknown	gnl\|CDD\|188164
NC_013729.1\|WP_012922538.1\|5363657_5364878_-\|glucarate-dehydratase	unknown	unknown	gnl\|CDD\|239439
NC_013729.1\|WP_083793003.1\|5365749_5366622_-\|sugar-ABC-transporter-permease	unknown	unknown	gnl\|CDD\|224096
NC_013729.1\|WP_148257076.1\|5372765_5374400_-\|potassium-transporter-TrkA	unknown	unknown	gnl\|CDD\|367001
NC_013729.1\|WP_012922549.1\|5376768_5377269_-\|MarR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|197670
NC_013729.1\|WP_012922541.1\|5366675_5367992_-\|sugar-ABC-transporter-substrate-binding-protein	unknown	unknown	gnl\|CDD\|270303
NC_013729.1\|WP_012922558.1\|5383943_5384858_+\|sensor-histidine-kinase	unknown	unknown	gnl\|CDD\|379605
NC_013729.1\|WP_041289468.1\|5378760_5379681_+\|LysR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|223656
NC_013729.1\|WP_012922539.1\|5364883_5365753_-\|carbohydrate-ABC-transporter-permease	unknown	unknown	gnl\|CDD\|223472
NC_013729.1\|WP_012922551.1\|5378144_5378669_-\|sugar-O-acetyltransferase	unknown	unknown	gnl\|CDD\|100047

Protein	Function_ID	Function_description	E-value
NC_013729.1\|WP_012922547.1\|5374524_5376198_-\|methylmalonyl-CoA-mutase	gnl\|CDD\|239652	cd03680, MM_CoA_mutase_ICM_like, Coenzyme B12-dependent-methylmalonyl coenzyme A (CoA) mutase (MCM) family, isobutyryl-CoA mutase (ICM)-like subfamily; contains archaeal and bacterial proteins similar to the large subunit of Streptomyces cinnamonensis coenzyme B12-dependent ICM. ICM from S. cinnamonensis is comprised of a large and a small subunit. The holoenzyme appears to be an alpha2beta2 heterotetramer with up to 2 molecules of coenzyme B12 bound. The small subunit binds coenzyme B12. ICM catalyzes the reversible rearrangement of n-butyryl-CoA to isobutyryl-CoA, intermediates in fatty acid and valine catabolism, which in S. cinnamonensis can be converted to methylmalonyl-CoA and used in polyketide synthesis.	0
NC_013729.1\|WP_012922539.1\|5364883_5365753_-\|carbohydrate-ABC-transporter-permease	gnl\|CDD\|223472	COG0395, UgpE, ABC-type sugar transport system, permease component [Carbohydrate transport and metabolism].	7.66859e-66
NC_013729.1\|WP_012922545.1\|5371738_5372737_-\|tetratricopeptide-repeat-protein	gnl\|CDD\|225660	COG3118, COG3118, Thioredoxin domain-containing protein [Posttranslational modification, protein turnover, chaperones].	2.73736e-58
NC_013729.1\|WP_012922557.1\|5383330_5383768_+\|methylmalonyl-CoA-epimerase	gnl\|CDD\|213772	TIGR03081, Methylmalonyl-CoA_epimerase_mitochondrial, methylmalonyl-CoA epimerase. Members of this protein family are the enzyme methylmalonyl-CoA epimerase (EC 5.1.99.1), also called methylmalonyl-CoA racemase. This enzyme converts (2R)-methylmalonyl-CoA to (2S)-methylmalonyl-CoA, which is then a substrate for methylmalonyl-CoA mutase (TIGR00642). It is known in bacteria, archaea, and as a mitochondrial protein in animals. It is closely related to lactoylglutathione lyase (TIGR00068), which is also called glyoxylase I, and is also a homodimer.	3.53422e-55
NC_013729.1\|WP_012922555.1\|5381008_5381965_-\|methylmalonyl-Co-A-mutase-associated-GTPase-MeaB	gnl\|CDD\|224617	COG1703, ArgK, Putative periplasmic protein kinase ArgK and related GTPases of G3E family [Amino acid transport and metabolism].	2.89794e-122
NC_013729.1\|WP_012922553.1\|5379688_5380405_-\|PH-domain-containing-protein	gnl\|CDD\|367615	pfam03703, bPH_2, Bacterial PH domain. Domain found in uncharacterized family of membrane proteins. 1-3 copies found in each protein, with each copy flanked by transmembrane helices. Members of this family have a PH domain like structure.	5.81365e-07
NC_013729.1\|WP_148257075.1\|5368151_5368934_+\|NAD-dependent-epimerase/dehydratase-family-protein	gnl\|CDD\|223528	COG0451, WcaG, Nucleoside-diphosphate-sugar epimerases [Cell envelope biogenesis, outer membrane / Carbohydrate transport and metabolism].	2.25346e-22
NC_013729.1\|WP_012922543.1\|5368930_5369707_+\|IclR-family-transcriptional-regulator	gnl\|CDD\|224332	COG1414, IclR, Transcriptional regulator [Transcription].	4.58731e-56
NC_013729.1\|WP_012922556.1\|5381987_5383205_-\|acetyl-CoA-C-acetyltransferase	gnl\|CDD\|180261	PRK05790, PRK05790, putative acyltransferase; Provisional.	0
NC_013729.1\|WP_012922559.1\|5385012_5386344_+\|crotonyl-CoA-carboxylase/reductase	gnl\|CDD\|188164	TIGR01751, crotonyl_CoA_reductase, crotonyl-CoA carboxylase/reductase. The enzyme represented by this model can convert crotonyl-CoA to butyryl-CoA (crotonyl-CoA reductase activity), but more importantly, in the presence of CO2, generates (2S)-ethylmalonyl-CoA. In serine cycle methylotrophic bacteria this enzyme is involved in the process of acetyl-CoA to glyoxylate. In other bacteria the enzyme is used to produce extender units for incorporation into polyketides such as tylosin from Streptomyces fradiae and coronatine from Pseudomonas syringae.	0
NC_013729.1\|WP_012922538.1\|5363657_5364878_-\|glucarate-dehydratase	gnl\|CDD\|239439	cd03323, D-glucarate_dehydratase, D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to form 5-keto-4-deoxy-D-glucarate (5-KDG) , the initial reaction of the catabolic pathway for (D)-glucarate. GlucD belongs to the enolase superfamily of enzymes, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and that is stabilized by coordination to the essential Mg2+ ion.	5.55706e-180
NC_013729.1\|WP_083793003.1\|5365749_5366622_-\|sugar-ABC-transporter-permease	gnl\|CDD\|224096	COG1175, UgpA, ABC-type sugar transport systems, permease components [Carbohydrate transport and metabolism].	1.16345e-77
NC_013729.1\|WP_148257076.1\|5372765_5374400_-\|potassium-transporter-TrkA	gnl\|CDD\|367001	pfam02254, TrkA_N, TrkA-N domain. This domain is found in a wide variety of proteins. These protein include potassium channels, phosphoesterases, and various other transporters. This domain binds to NAD.	9.8075e-19
NC_013729.1\|WP_012922549.1\|5376768_5377269_-\|MarR-family-transcriptional-regulator	gnl\|CDD\|197670	smart00347, HTH_MARR, helix_turn_helix multiple antibiotic resistance protein.	9.6702e-22
NC_013729.1\|WP_012922541.1\|5366675_5367992_-\|sugar-ABC-transporter-substrate-binding-protein	gnl\|CDD\|270303	cd13585, PBP2_TMBP_like, The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and similar oligosaccharides; possess type 2 periplasmic binding fold. This family includes the periplasmic trehalose/maltose-binding component of an ABC transport system and related proteins from archaea and bacteria. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. 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.	4.1621e-54
NC_013729.1\|WP_012922558.1\|5383943_5384858_+\|sensor-histidine-kinase	gnl\|CDD\|379605	pfam14417, MEDS, MEDS: MEthanogen/methylotroph, DcmR Sensory domain. MEDS is prototyped by DcmR and is likely to function with the PocR domain in certain organisms in sensing hydrocarbon derivatives. The MEDS domain occurs fused to Histidine Kinase and as stand-alone version. Sequence analysis shows that it is a catalytically inactive version of the P-loop NTPase domain of the RecA superfamily.	3.91795e-18
NC_013729.1\|WP_041289468.1\|5378760_5379681_+\|LysR-family-transcriptional-regulator	gnl\|CDD\|223656	COG0583, LysR, Transcriptional regulator [Transcription].	1.64162e-27
NC_013729.1\|WP_012922550.1\|5377369_5378116_+\|maleylpyruvate-isomerase-family-mycothiol-dependent-enzyme	gnl\|CDD\|274422	TIGR03083, TIGR03083, uncharacterized Actinobacterial protein TIGR03083. This protein family pulls together several groups of proteins, each very different from the others. They share in common three conserved regions. The first is a region of about 38 amino acids, nearly always at the N-terminus of a protein. This region has a bulky hydrophobic residue, usually Trp, at position 29, and a His residue at position 37 that is invariant, so far, in over 150 instances. The second conserved region has a motif [DE]xxxHxxD. The third conserved region contains a hydrophobic patch and a well-conserved Arg residue. Most examples are found in the Actinobacteria, including the genera Mycobacterium, Corynebacterium, Streptomyces, Nocardia, Frankia, etc. The pattern of near-invariant residues against a backdrop of extreme sequence divergence suggests enzymatic activity and conservation of active site residues.	7.90835e-12
NC_013729.1\|WP_012922551.1\|5378144_5378669_-\|sugar-O-acetyltransferase	gnl\|CDD\|100047	cd03357, LbH_MAT_GAT, Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively at the C6 position of the nonreducing end glucosyl moiety. GAT specifically acetylates galactopyranosides. Furthermore, MAT shows higher affinity toward artificial substrates containing an alkyl or hydrophobic chain as well as a glucosyl unit. Active MAT and GAT are homotrimers, with each subunit consisting of an N-terminal alpha-helical region and a C-terminal left-handed parallel alpha-helix (LbH) subdomain with 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).	2.82521e-64

>NC_013729.1|WP_012922547.1|5374524_5376198_-|methylmalonyl-CoA-mutase
MDAEQIAAGQRRWQQRYDASRRREADFTTLSGTEVAPVYGPPEGVDDPRMERIGWPGEFPFTRGLYPTGYRGRTWTIRQFAGFGNAEDTNARYKMILNGGGGGLSVAFDMPTLMGRDSDDPKALGEVGHCGVAIDSAADMDRLFKDIPLQDVTTSMTISGPAVPAFVMYLVAAERQGADITKLNGTLQTDIFKEYIAQKEWLFPPEPHLRLIGDLMEYCAANIPAYKPLSVSGYHIREAGSTAAQELAFTLADGFGYVELGLSRGLDVDVFAPGLSFFFDSHLDFFEEIAKFRAARRIWARWLRDVYGAKTDKAQWLRFHTQTAGVSLTAQQPVNNVVRTAVEALAAVLGGTNSLHTNALDETLALPTDESAEIALRTQSVLMEEIGVTNVADPLGGSWYVEALTDQLEQQAEEIFTRIREMSPDGTMTGGILRGIEDGWFMAEIADAAFEYQQKLEKGEKKIVGVNTLTDTVAGELEILRVSHEVEIEQCRALAARKAQRDEAQVRRTLTALVEAARGTGSLIEPMLEAARAEATMGEICDVLRDEWGEYREPARF
>NC_013729.1|WP_148257076.1|5372765_5374400_-|potassium-transporter-TrkA
MLRVVTELVSSGEEVTAIVNPASRHIERIAELGAQVMGVRVVRESVLRRAGIDTDGKKPSTARALVLLDADDVHNVHTALTARDMDENLRIVVQMVNPRIGAQLHQLLGDCVVISGPSLAAPAFVADALEDDELTWLELGGRRMVAGPAELIREKVTVLADTTSSATPELLPLSSADPAGDIVLGTGVRHLRRKRDVRRTGWVMATRDVLDRRVRVIAAVMALLVVIGTALTHWIAGVEWLRALYLVMGAVTSAGIEDDVFANAQPWAKVAAVVVQLTGIVLVALLTAVIVDSLIGARLSRVIGGVRGRPRNHVIVCGLGTVGARVLEILAERGVAVVGVEHDEEAPGVQTAHRLRIPLVMGDSSQEETLRLAGAPRAQAVLAITNGDITNLETAMVVRDLNPDARITMRMFDHDLAHKVERMLGLGHSRSVSMLVAPAIAAAVANRRTQATVPAGRRVLLLTEVTVERDSVAVGRRLGELDEAGGLRVLACQTGTGWDWSPPFQQTLVAGTKIAVAGTRSGLARLLLATRAPHRPGRSERIGP
>NC_013729.1|WP_012922545.1|5371738_5372737_-|tetratricopeptide-repeat-protein
MSQPNFSRPGAIDLSSLRQPPARPGGPGGPGAPARPGGPGGPGAGGPGGGPGGPGGGGVTGPYVLTVSEQSFQTDVIERSVQHPVVVEFWSPRSEASVALGPVLARLTTEYGGKFLLARIDVDANPQLAQAVGVQSIPLVIAVLRGQVVPLFQGALGEPEARQYLDQLLTVAVANGITGRAEPVGPAAPAEQAEPALDPRYEAAENAVAAGDLDGAITAYETLLKETPNDAEAKAGLARVQLVKRTRDVPAEVRTRAADNPTDIEAQLLVADVDLMGGHVEDAFARLIRTIQSTAGDERNTVRLHLLELFEVVGGDDERVIKARRQLMTALF
>NC_013729.1|WP_012922543.1|5368930_5369707_+|IclR-family-transcriptional-regulator
MTTEEVRLVKSAERTLRILEVLGEARGPISVTELHKRTGYPRSSLHQLLHTMIATGWIESTSEGALVGIGSRALLVGTAYLDRDPALPFGIRTLEKIREETGYTSHYARLDGGSVIYLATRESLSPHRATSRVGRQLPAYATSLGKALLAELTLTEVSLAVPADPLPGLTPHTVPNQVELAIELEQTRQRGYSLEREQNTLGLGCIGVPVPYRIPATDAISCSIPIDQCTDAEVERVAAIIREQVQLLATKLRAEGIR
>NC_013729.1|WP_148257075.1|5368151_5368934_+|NAD-dependent-epimerase/dehydratase-family-protein
MVVTGAAGLVGGLLRPRLARPGRTLRLVDVAPIDDLSDGEQFVQASVTDLDAMERVCTGADLLVHLGGHSSERPWQQILETNIQGGYVVLEAAHRTGVPRVLLGSSLHATGYVRADEAAAEPVLQPCPDTYYGVGKVTLEALGSLYADRCGLIVVSARICTVGETIGTGGRTLSTWVSPGDLARLVEATAILDKPGHHLVWAVSDNTRGWFSLAAGRAIGFHPEDDAEHHIGPGTDQTHDPHAVLAGAFVDDDHPLGGTW
>NC_013729.1|WP_012922541.1|5366675_5367992_-|sugar-ABC-transporter-substrate-binding-protein
MRISPRRAAAALSAMALVGSLSACGGDDSAGDAGAPLEFWTRSGPEGATTYKAILAAFTAKTGIQVNYQGVLEFDTQLQTKASSKKLPDLWVNDASLLGTYQGQGYTTPVEPGQIEGGDAIDAATWQQNKGLDGQLYGVPYSRQAFGTLVRVDWRKKLGLPQPKTWDDLTALATAFATKDPDGNGKKDTYGMVVPGSSKNGYIGWWGISYIWQAGGDILAPAGEGKYKSVINSPQTRTGLEFIRRQFCTPGNVVPGSLNLTTSEAPFFQEGKAGIYLTGPYAFGTYDKILGKDKYEVVPMPKGPVSTTTLGDGENIYFGAGSQKSDEAKKLAAFLISPEGQEIGMKAEESKYPTVRLPVNRGVDVHKVLGDPRWDLIQKQYLDDTKTFVWSIKFQPIRQALGEGVNAMMSSCDSDLDAGLKKLDQAITAELKAQDVLG
>NC_013729.1|WP_083793003.1|5365749_5366622_-|sugar-ABC-transporter-permease
MLSGPGWLPWVLLLPALLFALMFKFIPMVEGLRMSLFKVQPFLGDQWVGLENYRTVLTDSRFRSALGHTLLLGIGQTVGALVLGFLLALLLEGQTRSLWVLRTAIFLPVVTAVAVIGEVWRILYFPTETGFVNSIAGWFGLGPFGFLNDPDQALVSVMVVGVWTAAPYNMVIILAGLAGIDRTLYEAAAVDGVSRWQRIRYIVLPGLRPAISVLLTLAAIRSLRIFTEVFVLTGGGPAGSTEVWMTRVFSLGFQRNDLGVASAASTLLLLVTVVLTLGMRLLTRQKESGS
>NC_013729.1|WP_012922539.1|5364883_5365753_-|carbohydrate-ABC-transporter-permease
MSMSSQFDTALGWSPRLGVGKVLRILLCAVVLFVFAAPFLTIFAGAFNKTTDSTQVTLYPQDPTLLGFQIAGEKGIWGYFLNSLVIVGGGLLLQLTVSVLAAYALARRKFRGHTVVMLLFLLTMMLPEEVIAVPLSQVLAELPFLGISLKGSVFGVILPVALWGFTILIMTEFMKEIPREIEEAARLDGVGELRMLWVIVLPLSKPVLGVATIFGFMMIWDQYLLPLIAADDPSDYTLTVALSVLRSDGTVGPGVLLAGALIALVPSLVVYLLMQRSLIRGITAGATKG
>NC_013729.1|WP_012922538.1|5363657_5364878_-|glucarate-dehydratase
MKITDLAITPIAFADPPLLNATGVHEPLALRTVVQLHVADGVVGLGEGSGELVVLERLARVRPALVGQSVFDTSAIEAIVFAELGNDVPPIQKRSVFSIIEVACLDAQGKLLGLPVVDLLGGAVRQTVTYSGYLFYKWAGHPGQAADEWGEALDPAGLVAQAARMIDLHGFGSLKLKGGVFPPDQEIAAVRALAEAFPGIPLRIDPNGAWSVATSQYVAAELAGVLEYLEDPTLTTPAMAQVAAAASMPLATNMCVVSPETVPEAIRLGAVQIVLSDHHYWGGLRHTRELGALCATFGLGLSMHSNSHLGISLAAMTHVAAATPNLAYACDTHYPWNSGDDVITVPFEFADGALRVPAGPGLGVELDEAKLFRLHRQYVASGRTTRADTAYLRQVDPAYDPSLPRF
>NC_013729.1|WP_012922537.1|5362548_5363658_-|hypothetical-protein
MTAVYLYPWDLDGDPAAPELIESLGASSVVLAAAYHSVRAATPRHPRHRIVEAPSGLYVPVRPEAWGSLRPPSASGWAGEDAFNRAAAQVSLPVQAWVVLTHSSAVGRLDPSVCVRSAFGDVYDYALCPSSEQVRAYAQVLVGEVARQTGVSAMVLEACGPMGAGHQSAHEKTAGADWSPVDQALLSICFCRACTAAYAAAGLDVPAVAGAIRAGLGASSVEHALGASASVVLEVRRQAIVELRTAVVAEARAAGVREVSLHASTDPWATGPAAFLDSVAGGIDCPIAPAWELTTAGARRVLDLHRLGATRIGAYVTALPPVPAHAETLATHWQSLLSAGATDLHIYHAGLASTSRLTAIREAIEAVTA
>NC_013729.1|WP_012922549.1|5376768_5377269_-|MarR-family-transcriptional-regulator
MARKRPLPFDPIDEASRQWARRWGAVEQMRAVTSLMRAQQIVIGELDDILRKHNLSFARFEALVLLTFSRRGSLPLGKMGERLQVHPTSVTSIVRRLEAAGLVTRTPHPDDGRAVLCAITPEGRELVERATADLVAADFALRGLTDEQLKVLWSVLEPLRHNAGDF
>NC_013729.1|WP_012922550.1|5377369_5378116_+|maleylpyruvate-isomerase-family-mycothiol-dependent-enzyme
MSLPPERASFYLDCLRADSSRLAEVGRIGLAATVPSCPGWTVDTVLRHTATVYLHKIEILRLGRRPDPWPPDLTAHDTFALYDEARAGIVEALEQAGTSLETWTFSPDDHTSGFWFRRMALETAVHRIDAELAHDIATPVDQELAVDGIDELLVLMLGGPWWAEGDTEHPVDATVRITTAGRSWTVDANATSATVTSGTDGPADAEVFGEPTEIFLWLWGRLDQQLVQTAGDDAVVTAFRARVAECTT
>NC_013729.1|WP_012922551.1|5378144_5378669_-|sugar-O-acetyltransferase
MTTLTVPPDFRERVARAIRLTEQLNTLPYDDQPAIRATWSELIGRPVDETFRLIPPVYSDYGINVRVGRDVFVNQGCRFNDFGGIEIGDQVMLGPNVSLISSGHPVAPAQRRSGITAAPIRVERNVWIGASAIILQGVTVGADAVVGAGAVVTRDVPPGALVAGSPARVVRDLY
>NC_013729.1|WP_041289468.1|5378760_5379681_+|LysR-family-transcriptional-regulator
MELEAVRTFVAAAEAGQFQAAADELGVTQQAVSKRIAALERQLGVLLFARSPRGAQLSIDGQAFLPPARELLRAAERAEASVLAGRRPLRIDVLNRRTAPATALHAFHQSHPGVELDVVTLPDASAGTAVAAVANGTIDATFRAVWDRRQIVPPVRAARVIDDPHQLLVGPRHPLASADQLTLADLAPYRIWMPGLRSDTEWGTYYDQLAAAFSLAIDTAGPSFGVEVLLDELATSADRATFVGEGTRYLWPEAYDLRRLQVVDPTPVYPHSIIWREDNPHPGLAAFLDHLHTARAGAVGREIWVP
>NC_013729.1|WP_012922553.1|5379688_5380405_-|PH-domain-containing-protein
MAGIGLFRIFDPKVRRHLISDEGEVVIDEVRHHWVVFALPMLEVALATGLLITMLWMPMTGAGVVLVIVLVLLGHAFWRFLSEHRDRFVVTNMRVMRIRGVFSQTVATTPIARILDITLQKPIVGRFFGYGHFVFESAAQDQGFREIRFVSRPDDRDLTIQRVIQRTGLRASASVDVVQGDDDDTDDDGTGPIGMDSSQDVTTTVPRQVPAATRVASSSSKSIFNSERANWTDQDRED
>NC_013729.1|WP_012922555.1|5381008_5381965_-|methylmalonyl-Co-A-mutase-associated-GTPase-MeaB
MSRRTAPVAELVERAREGDSRSVARLISLVEDESPLLREVMAALAPHAGQAHIVGITGSPGVGKSTSTSALVSAYRATGKRVGVLAVDPSSPFSGGALLGDRVRMQDHATDAGVFIRSMASRGHLGGLAWTTPQALRVLDAAGFDVVLVETVGVGQSEVEIAGMADTTLVLLAPGMGDGIQAAKAGILEVGDIYVVNKADRDGAQNVTRDLRAMLALAEREPDDWRPPILKTVASRNEGVDEVVAAIEDRLVWMRGSGVLADRRRSRARDEIEAIAMTALRSRFAHLHGDARLDVLAAKVATGATDPYAAADELIAAL
>NC_013729.1|WP_012922556.1|5381987_5383205_-|acetyl-CoA-C-acetyltransferase
MSDSTRSSQLETVIVAGARTPIGRLLGGLKGFTGADLGGFAIKGALDKAGVAPEQVEYVIMGQVLQAGAGQIAARQAAVKAGIPMDVPAITINKVCLSGLNAIALASQLIRAGEYDVVVAGGMESMTNAPHLLPKSREGFKYGDTTLVDSMAYDGLWDAFTDQAMGSLTEQHNTENLELTREEQDQFSARSHQLAAESWKNGVFTDEVVPVEVPQRKGDPLVVDTDEGVRGDTTVESLAKLRPAFGKDGTITAGSASQISDGGCAVVVMSKAKAEELGLSWIAEIGAHGSVAGPDSSLQSQPAKAIVKACSKEGVDPAALDLIEINEAFAAVGIASARELNLDLDKVNVNGGAIALGHPIGMSGARLVLHLALELQRRGGGTGVAALCGGGGQGDALILRVPVRS
>NC_013729.1|WP_012922557.1|5383330_5383768_+|methylmalonyl-CoA-epimerase
MEHLTATQTLFEAIDHVGVAVADFDEAVRFYAETFGMTVAHEEVNEEQGVREAMLSIGDSGSSIQLLAPLSDSSPIAKFLDRNGPGIQQLAYRVRDLDAVSATLRERGAQLLYDEPRRGTAGSRINFIHPKSAGGVLVELVEPAR
>NC_013729.1|WP_012922558.1|5383943_5384858_+|sensor-histidine-kinase
MPTGSASESPHLAPAGFRHDAFVYTDDDDFVRQAVTYVHDGLAAGETVVAVLPEVRNSLLRKELDGVADQVVFLDMTQLGRNPARIIPLWRTLLDQAPDIPLRGLGEPAYPGRTPSELAEAALHELLLDVAFEHTSPFHLRCPYSASLPIRPAEVHVSAAGPARTAAERVFRTPLAAVPAQARQREFGRDDLTEVRYEVNTAAKELGMPAGRIEDIELALHEICTNSVRFGGGQGRLSWWTADGNLVCDVADGGRIDDLLVGRVLPPADGLGGRGVWLAHQLCDLVQIRSGDTGTQVRLHTRLR
>NC_013729.1|WP_012922559.1|5385012_5386344_+|crotonyl-CoA-carboxylase/reductase
MKQILDAILAGDNATLGGLDVPDHYRGITVHADETAMFEGLETKEKDPRKSLHLDDVPTPELGPGEALVAVMASAINYNTVWTSIFEPVSTFSFLKRYGKLSPLTARHDLPYHVVGSDLAGVVLRTGPGVNAWKPGDEVVAHCLSVELESPDGHNDTMLDSEQRIWGFETNFGGLAELALVKSNQLMPKPAHLTWEEAASPGLVNSTAYRQLVSANGANLKQGDVVLIWGASGGLGSYATQFALNGGAVPVCVVSSPEKAEICRAMGAELIIDRSAEDYRFWRDEQTQDPTEWKRLGAKIRELTGGDDPDIVFEHPGRETFGASVYVARRGGTIVTCASTSGFLHEYDNRYLWMNLKRIVGSHFANYREAWEANRLIAKGMVHPTVSRVYPLEETGQAAYDVHRNLHQGKVGVLTLAPAEGLGVRDEELRAKHLDRINRFRDR

You can click texts colored in the table to view more detailed information

Click the colored protein region to show detailed information

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
NC_013729_5	5.10\|3468642\|31\|NC_013729\|CRT	3468642-3468672	31	NC_047866	Aeromonas phage Ahp1, complete genome	34625-34655	5	0.839
NC_013729_5	5.3\|3468300\|31\|NC_013729\|CRT	3468300-3468330	31	NZ_CP030074	Streptomyces sp. ZFG47 plasmid unnamed1, complete sequence	722237-722267	7	0.774
NC_013729_5	5.10\|3468642\|31\|NC_013729\|CRT	3468642-3468672	31	MN844877	Sphaerotilus phage vB_SnaP-R1, complete genome	35900-35930	7	0.774
NC_013729_5	5.10\|3468642\|31\|NC_013729\|CRT	3468642-3468672	31	NZ_CP006369	Aureimonas sp. AU20 plasmid pAU20b, complete sequence	241227-241257	7	0.774
NC_013729_5	5.10\|3468642\|31\|NC_013729\|CRT	3468642-3468672	31	AP017627	Pleomorphomonas sp. SM30 plasmid pSM30-1 DNA, complete genome	132154-132184	7	0.774
NC_013729_5	5.3\|3468300\|31\|NC_013729\|CRT	3468300-3468330	31	NZ_CP015739	Shinella sp. HZN7 plasmid pShin-03, complete sequence	115088-115118	8	0.742
NC_013729_5	5.3\|3468300\|31\|NC_013729\|CRT	3468300-3468330	31	NC_047816	Ralstonia phage RS-PI-1, complete genome	15993-16023	8	0.742
NC_013729_5	5.4\|3468354\|31\|NC_013729\|CRT	3468354-3468384	31	MT740740	Ralstonia phage Gervaise, complete genome	45582-45612	8	0.742
NC_013729_5	5.4\|3468354\|31\|NC_013729\|CRT	3468354-3468384	31	MT740727	Ralstonia phage Alix, complete genome	24475-24505	8	0.742
NC_013729_5	5.4\|3468354\|31\|NC_013729\|CRT	3468354-3468384	31	MT740732	Ralstonia phage Darius, complete genome	3800-3830	8	0.742
NC_013729_5	5.4\|3468354\|31\|NC_013729\|CRT	3468354-3468384	31	MT740731	Ralstonia phage Claudette, complete genome	51713-51743	8	0.742
NC_013729_5	5.4\|3468354\|31\|NC_013729\|CRT	3468354-3468384	31	LT999987	Pseudomonas phage vB_PaeS_PAO1_HW12 genome assembly, complete genome: monopartite	28170-28200	8	0.742
NC_013729_5	5.4\|3468354\|31\|NC_013729\|CRT	3468354-3468384	31	MK511036	Pseudomonas phage BR327, partial genome	27826-27856	8	0.742
NC_013729_5	5.4\|3468354\|31\|NC_013729\|CRT	3468354-3468384	31	JQ762257	Pseudomonas phage MP42, complete genome	27524-27554	8	0.742
NC_013729_5	5.4\|3468354\|31\|NC_013729\|CRT	3468354-3468384	31	MK511018	Pseudomonas phage CF28, partial genome	27858-27888	8	0.742
NC_013729_5	5.4\|3468354\|31\|NC_013729\|CRT	3468354-3468384	31	NC_026601	Pseudomonas phage vB_PaeS_PAO1_Ab30, complete genome	27831-27861	8	0.742
NC_013729_5	5.4\|3468354\|31\|NC_013729\|CRT	3468354-3468384	31	NC_030918	Pseudomonas phage JBD93, complete genome	27226-27256	8	0.742
NC_013729_5	5.4\|3468354\|31\|NC_013729\|CRT	3468354-3468384	31	MH719192	Pseudomonas phage Ps56, complete genome	30423-30453	8	0.742
NC_013729_5	5.4\|3468354\|31\|NC_013729\|CRT	3468354-3468384	31	EU272037	Pseudomonas phage MP38, complete genome	27493-27523	8	0.742
NC_013729_5	5.4\|3468354\|31\|NC_013729\|CRT	3468354-3468384	31	KM389459	UNVERIFIED: Pseudomonas phage F_ET309sp/Pa1651 clone contig00001 genomic sequence	28005-28035	8	0.742
NC_013729_5	5.4\|3468354\|31\|NC_013729\|CRT	3468354-3468384	31	JX434032	Pseudomonas phage JBD30, complete genome	27563-27593	8	0.742
NC_013729_5	5.4\|3468354\|31\|NC_013729\|CRT	3468354-3468384	31	KU199708	Pseudomonas phage JBD69, complete genome	27546-27576	8	0.742
NC_013729_5	5.4\|3468354\|31\|NC_013729\|CRT	3468354-3468384	31	DQ631426	Pseudomonas phage DMS3, complete genome	27092-27122	8	0.742
NC_013729_5	5.4\|3468354\|31\|NC_013729\|CRT	3468354-3468384	31	JX434031	Pseudomonas phage JBD24, complete genome	27676-27706	8	0.742
NC_013729_5	5.4\|3468354\|31\|NC_013729\|CRT	3468354-3468384	31	KM389326	UNVERIFIED: Pseudomonas phage F_KK2074sp/Pa1651 clone contig00001 genomic sequence	10467-10497	8	0.742
NC_013729_5	5.4\|3468354\|31\|NC_013729\|CRT	3468354-3468384	31	KM389461	UNVERIFIED: Pseudomonas phage F_TK432sp/Pa1651 clone ctg7180000000005 genomic sequence	9369-9399	8	0.742
NC_013729_5	5.6\|3468450\|31\|NC_013729\|CRT	3468450-3468480	31	MT740740	Ralstonia phage Gervaise, complete genome	45582-45612	8	0.742
NC_013729_5	5.6\|3468450\|31\|NC_013729\|CRT	3468450-3468480	31	MT740727	Ralstonia phage Alix, complete genome	24475-24505	8	0.742
NC_013729_5	5.6\|3468450\|31\|NC_013729\|CRT	3468450-3468480	31	MT740732	Ralstonia phage Darius, complete genome	3800-3830	8	0.742
NC_013729_5	5.6\|3468450\|31\|NC_013729\|CRT	3468450-3468480	31	MT740731	Ralstonia phage Claudette, complete genome	51713-51743	8	0.742
NC_013729_5	5.6\|3468450\|31\|NC_013729\|CRT	3468450-3468480	31	LT999987	Pseudomonas phage vB_PaeS_PAO1_HW12 genome assembly, complete genome: monopartite	28170-28200	8	0.742
NC_013729_5	5.6\|3468450\|31\|NC_013729\|CRT	3468450-3468480	31	MK511036	Pseudomonas phage BR327, partial genome	27826-27856	8	0.742
NC_013729_5	5.6\|3468450\|31\|NC_013729\|CRT	3468450-3468480	31	JQ762257	Pseudomonas phage MP42, complete genome	27524-27554	8	0.742
NC_013729_5	5.6\|3468450\|31\|NC_013729\|CRT	3468450-3468480	31	MK511018	Pseudomonas phage CF28, partial genome	27858-27888	8	0.742
NC_013729_5	5.6\|3468450\|31\|NC_013729\|CRT	3468450-3468480	31	NC_026601	Pseudomonas phage vB_PaeS_PAO1_Ab30, complete genome	27831-27861	8	0.742
NC_013729_5	5.6\|3468450\|31\|NC_013729\|CRT	3468450-3468480	31	NC_030918	Pseudomonas phage JBD93, complete genome	27226-27256	8	0.742
NC_013729_5	5.6\|3468450\|31\|NC_013729\|CRT	3468450-3468480	31	MH719192	Pseudomonas phage Ps56, complete genome	30423-30453	8	0.742
NC_013729_5	5.6\|3468450\|31\|NC_013729\|CRT	3468450-3468480	31	EU272037	Pseudomonas phage MP38, complete genome	27493-27523	8	0.742
NC_013729_5	5.6\|3468450\|31\|NC_013729\|CRT	3468450-3468480	31	KM389459	UNVERIFIED: Pseudomonas phage F_ET309sp/Pa1651 clone contig00001 genomic sequence	28005-28035	8	0.742
NC_013729_5	5.6\|3468450\|31\|NC_013729\|CRT	3468450-3468480	31	JX434032	Pseudomonas phage JBD30, complete genome	27563-27593	8	0.742
NC_013729_5	5.6\|3468450\|31\|NC_013729\|CRT	3468450-3468480	31	KU199708	Pseudomonas phage JBD69, complete genome	27546-27576	8	0.742
NC_013729_5	5.6\|3468450\|31\|NC_013729\|CRT	3468450-3468480	31	DQ631426	Pseudomonas phage DMS3, complete genome	27092-27122	8	0.742
NC_013729_5	5.6\|3468450\|31\|NC_013729\|CRT	3468450-3468480	31	JX434031	Pseudomonas phage JBD24, complete genome	27676-27706	8	0.742
NC_013729_5	5.6\|3468450\|31\|NC_013729\|CRT	3468450-3468480	31	KM389326	UNVERIFIED: Pseudomonas phage F_KK2074sp/Pa1651 clone contig00001 genomic sequence	10467-10497	8	0.742
NC_013729_5	5.6\|3468450\|31\|NC_013729\|CRT	3468450-3468480	31	KM389461	UNVERIFIED: Pseudomonas phage F_TK432sp/Pa1651 clone ctg7180000000005 genomic sequence	9369-9399	8	0.742
NC_013729_5	5.8\|3468546\|31\|NC_013729\|CRT	3468546-3468576	31	MT740740	Ralstonia phage Gervaise, complete genome	45582-45612	8	0.742
NC_013729_5	5.8\|3468546\|31\|NC_013729\|CRT	3468546-3468576	31	MT740727	Ralstonia phage Alix, complete genome	24475-24505	8	0.742
NC_013729_5	5.8\|3468546\|31\|NC_013729\|CRT	3468546-3468576	31	MT740732	Ralstonia phage Darius, complete genome	3800-3830	8	0.742
NC_013729_5	5.8\|3468546\|31\|NC_013729\|CRT	3468546-3468576	31	MT740731	Ralstonia phage Claudette, complete genome	51713-51743	8	0.742
NC_013729_5	5.8\|3468546\|31\|NC_013729\|CRT	3468546-3468576	31	LT999987	Pseudomonas phage vB_PaeS_PAO1_HW12 genome assembly, complete genome: monopartite	28170-28200	8	0.742
NC_013729_5	5.8\|3468546\|31\|NC_013729\|CRT	3468546-3468576	31	MK511036	Pseudomonas phage BR327, partial genome	27826-27856	8	0.742
NC_013729_5	5.8\|3468546\|31\|NC_013729\|CRT	3468546-3468576	31	JQ762257	Pseudomonas phage MP42, complete genome	27524-27554	8	0.742
NC_013729_5	5.8\|3468546\|31\|NC_013729\|CRT	3468546-3468576	31	MK511018	Pseudomonas phage CF28, partial genome	27858-27888	8	0.742
NC_013729_5	5.8\|3468546\|31\|NC_013729\|CRT	3468546-3468576	31	NC_026601	Pseudomonas phage vB_PaeS_PAO1_Ab30, complete genome	27831-27861	8	0.742
NC_013729_5	5.8\|3468546\|31\|NC_013729\|CRT	3468546-3468576	31	NC_030918	Pseudomonas phage JBD93, complete genome	27226-27256	8	0.742
NC_013729_5	5.8\|3468546\|31\|NC_013729\|CRT	3468546-3468576	31	MH719192	Pseudomonas phage Ps56, complete genome	30423-30453	8	0.742
NC_013729_5	5.8\|3468546\|31\|NC_013729\|CRT	3468546-3468576	31	EU272037	Pseudomonas phage MP38, complete genome	27493-27523	8	0.742
NC_013729_5	5.8\|3468546\|31\|NC_013729\|CRT	3468546-3468576	31	KM389459	UNVERIFIED: Pseudomonas phage F_ET309sp/Pa1651 clone contig00001 genomic sequence	28005-28035	8	0.742
NC_013729_5	5.8\|3468546\|31\|NC_013729\|CRT	3468546-3468576	31	JX434032	Pseudomonas phage JBD30, complete genome	27563-27593	8	0.742
NC_013729_5	5.8\|3468546\|31\|NC_013729\|CRT	3468546-3468576	31	KU199708	Pseudomonas phage JBD69, complete genome	27546-27576	8	0.742
NC_013729_5	5.8\|3468546\|31\|NC_013729\|CRT	3468546-3468576	31	DQ631426	Pseudomonas phage DMS3, complete genome	27092-27122	8	0.742
NC_013729_5	5.8\|3468546\|31\|NC_013729\|CRT	3468546-3468576	31	JX434031	Pseudomonas phage JBD24, complete genome	27676-27706	8	0.742
NC_013729_5	5.8\|3468546\|31\|NC_013729\|CRT	3468546-3468576	31	KM389326	UNVERIFIED: Pseudomonas phage F_KK2074sp/Pa1651 clone contig00001 genomic sequence	10467-10497	8	0.742
NC_013729_5	5.8\|3468546\|31\|NC_013729\|CRT	3468546-3468576	31	KM389461	UNVERIFIED: Pseudomonas phage F_TK432sp/Pa1651 clone ctg7180000000005 genomic sequence	9369-9399	8	0.742
NC_013729_5	5.10\|3468642\|31\|NC_013729\|CRT	3468642-3468672	31	NZ_CP039644	Azospirillum sp. TSA2s plasmid p2, complete sequence	70754-70784	8	0.742
NC_013729_5	5.10\|3468642\|31\|NC_013729\|CRT	3468642-3468672	31	NZ_CP014802	Salipiger profundus strain JLT2016 plasmid pTPRO6, complete sequence	114942-114972	8	0.742
NC_013729_5	5.10\|3468642\|31\|NC_013729\|CRT	3468642-3468672	31	NC_011961	Thermomicrobium roseum DSM 5159 plasmid unnamed, complete sequence	678238-678268	8	0.742
NC_013729_5	5.3\|3468300\|31\|NC_013729\|CRT	3468300-3468330	31	KF977490	Rhizobium phage vB_RglS_P106B, complete genome	10119-10149	9	0.71
NC_013729_5	5.4\|3468354\|31\|NC_013729\|CRT	3468354-3468384	31	NZ_CP029776	Deinococcus actinosclerus strain Deinococcus actinosclerus SJTR plasmid unnamed2, complete sequence	137479-137509	9	0.71
NC_013729_5	5.6\|3468450\|31\|NC_013729\|CRT	3468450-3468480	31	NZ_CP029776	Deinococcus actinosclerus strain Deinococcus actinosclerus SJTR plasmid unnamed2, complete sequence	137479-137509	9	0.71
NC_013729_5	5.8\|3468546\|31\|NC_013729\|CRT	3468546-3468576	31	NZ_CP029776	Deinococcus actinosclerus strain Deinococcus actinosclerus SJTR plasmid unnamed2, complete sequence	137479-137509	9	0.71
NC_013729_5	5.10\|3468642\|31\|NC_013729\|CRT	3468642-3468672	31	KU998238	Gordonia phage Splinter, complete genome	180-210	9	0.71
NC_013729_5	5.10\|3468642\|31\|NC_013729\|CRT	3468642-3468672	31	NC_030911	Gordonia phage Vendetta, complete genome	180-210	9	0.71

1. spacer 5.10|3468642|31|NC_013729|CRT matches to NC_047866 (Aeromonas phage Ahp1, complete genome) position: , mismatch: 5, identity: 0.839

gcacccgagccagccgcggcacc-cgagccag	CRISPR spacer
gcacccgagccagcagcggcccctcgagtcc-	Protospacer
************** ***** ** ****.*

2. spacer 5.3|3468300|31|NC_013729|CRT matches to NZ_CP030074 (Streptomyces sp. ZFG47 plasmid unnamed1, complete sequence) position: , mismatch: 7, identity: 0.774

gcagccaagccagccgcagcagccgcatggg	CRISPR spacer
gcagcccaaccagccgcagcagcagtacccg	Protospacer
****** *.************** *.*.  *

3. spacer 5.10|3468642|31|NC_013729|CRT matches to MN844877 (Sphaerotilus phage vB_SnaP-R1, complete genome) position: , mismatch: 7, identity: 0.774

gcacccgagccagccgcggcacccgagccag	CRISPR spacer
gtgcccgagccagtcgcgtcacccgagaagg	Protospacer
*..**********.**** ********  .*

4. spacer 5.10|3468642|31|NC_013729|CRT matches to NZ_CP006369 (Aureimonas sp. AU20 plasmid pAU20b, complete sequence) position: , mismatch: 7, identity: 0.774

gcacccgagccagccgcggcacccgagccag	CRISPR spacer
gcaccggagccagcggcggcaccggcgaggg	Protospacer
***** ******** ******** * *  .*

5. spacer 5.10|3468642|31|NC_013729|CRT matches to AP017627 (Pleomorphomonas sp. SM30 plasmid pSM30-1 DNA, complete genome) position: , mismatch: 7, identity: 0.774

gcacccgagccagccgcggcacccgagccag	CRISPR spacer
tcgacggggcgagccgcggcacccgcgccag	Protospacer
 *. * *.** ************** *****

6. spacer 5.3|3468300|31|NC_013729|CRT matches to NZ_CP015739 (Shinella sp. HZN7 plasmid pShin-03, complete sequence) position: , mismatch: 8, identity: 0.742

gcagccaagccagccgcagcagccgcatggg	CRISPR spacer
tgagccatgccagccgcatcagccggaaacg	Protospacer
  ***** ********** ****** * . *

7. spacer 5.3|3468300|31|NC_013729|CRT matches to NC_047816 (Ralstonia phage RS-PI-1, complete genome) position: , mismatch: 8, identity: 0.742

gcagccaagccagccgcagcagccgcatggg	CRISPR spacer
ccgcccacgcctgccgcagcagccgcagcgc	Protospacer
 *. *** *** ***************  *

8. spacer 5.4|3468354|31|NC_013729|CRT matches to MT740740 (Ralstonia phage Gervaise, complete genome) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
cgacccgaaccaacagcagcagccgatgacc	Protospacer
  ************ **********   .*

9. spacer 5.4|3468354|31|NC_013729|CRT matches to MT740727 (Ralstonia phage Alix, complete genome) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
cgacccgaaccaacagcagcagccgatgacc	Protospacer
  ************ **********   .*

10. spacer 5.4|3468354|31|NC_013729|CRT matches to MT740732 (Ralstonia phage Darius, complete genome) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
cgacccgaaccaacagcagcagccgatgacc	Protospacer
  ************ **********   .*

11. spacer 5.4|3468354|31|NC_013729|CRT matches to MT740731 (Ralstonia phage Claudette, complete genome) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
cgacccgaaccaacagcagcagccgatgacc	Protospacer
  ************ **********   .*

12. spacer 5.4|3468354|31|NC_013729|CRT matches to LT999987 (Pseudomonas phage vB_PaeS_PAO1_HW12 genome assembly, complete genome: monopartite) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
gcacccgcaccacccgcagcagcgcccagcc	Protospacer
******* **** **********  .  **

13. spacer 5.4|3468354|31|NC_013729|CRT matches to MK511036 (Pseudomonas phage BR327, partial genome) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
gcacccgcaccacccgcagcagcgcccagcc	Protospacer
******* **** **********  .  **

14. spacer 5.4|3468354|31|NC_013729|CRT matches to JQ762257 (Pseudomonas phage MP42, complete genome) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
gcacccgcaccacccgcagcagcgcccagcc	Protospacer
******* **** **********  .  **

15. spacer 5.4|3468354|31|NC_013729|CRT matches to MK511018 (Pseudomonas phage CF28, partial genome) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
gcacccgcaccacccgcagcagcgcccagcc	Protospacer
******* **** **********  .  **

16. spacer 5.4|3468354|31|NC_013729|CRT matches to NC_026601 (Pseudomonas phage vB_PaeS_PAO1_Ab30, complete genome) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
gcacccgcaccacccgcagcagcgcccagcc	Protospacer
******* **** **********  .  **

17. spacer 5.4|3468354|31|NC_013729|CRT matches to NC_030918 (Pseudomonas phage JBD93, complete genome) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
gcacccgcaccacccgcagcagcgcccagcc	Protospacer
******* **** **********  .  **

18. spacer 5.4|3468354|31|NC_013729|CRT matches to MH719192 (Pseudomonas phage Ps56, complete genome) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
gcacccgcaccacccgcagcagcgcccagcc	Protospacer
******* **** **********  .  **

19. spacer 5.4|3468354|31|NC_013729|CRT matches to EU272037 (Pseudomonas phage MP38, complete genome) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
gcacccgcaccacccgcagcagcgcccagcc	Protospacer
******* **** **********  .  **

20. spacer 5.4|3468354|31|NC_013729|CRT matches to KM389459 (UNVERIFIED: Pseudomonas phage F_ET309sp/Pa1651 clone contig00001 genomic sequence) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
gcacccgcaccacccgcagcagcgcccagcc	Protospacer
******* **** **********  .  **

21. spacer 5.4|3468354|31|NC_013729|CRT matches to JX434032 (Pseudomonas phage JBD30, complete genome) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
gcacccgcaccacccgcagcagcgcccagcc	Protospacer
******* **** **********  .  **

22. spacer 5.4|3468354|31|NC_013729|CRT matches to KU199708 (Pseudomonas phage JBD69, complete genome) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
gcacccgcaccacccgcagcagcgcccagcc	Protospacer
******* **** **********  .  **

23. spacer 5.4|3468354|31|NC_013729|CRT matches to DQ631426 (Pseudomonas phage DMS3, complete genome) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
gcacccgcaccacccgcagcagcgcccagcc	Protospacer
******* **** **********  .  **

24. spacer 5.4|3468354|31|NC_013729|CRT matches to JX434031 (Pseudomonas phage JBD24, complete genome) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
gcacccgcaccacccgcagcagcgcccagcc	Protospacer
******* **** **********  .  **

25. spacer 5.4|3468354|31|NC_013729|CRT matches to KM389326 (UNVERIFIED: Pseudomonas phage F_KK2074sp/Pa1651 clone contig00001 genomic sequence) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
gcacccgcaccacccgcagcagcgcccagcc	Protospacer
******* **** **********  .  **

26. spacer 5.4|3468354|31|NC_013729|CRT matches to KM389461 (UNVERIFIED: Pseudomonas phage F_TK432sp/Pa1651 clone ctg7180000000005 genomic sequence) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
gcacccgcaccacccgcagcagcgcccagcc	Protospacer
******* **** **********  .  **

27. spacer 5.6|3468450|31|NC_013729|CRT matches to MT740740 (Ralstonia phage Gervaise, complete genome) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
cgacccgaaccaacagcagcagccgatgacc	Protospacer
  ************ **********   .*

28. spacer 5.6|3468450|31|NC_013729|CRT matches to MT740727 (Ralstonia phage Alix, complete genome) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
cgacccgaaccaacagcagcagccgatgacc	Protospacer
  ************ **********   .*

29. spacer 5.6|3468450|31|NC_013729|CRT matches to MT740732 (Ralstonia phage Darius, complete genome) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
cgacccgaaccaacagcagcagccgatgacc	Protospacer
  ************ **********   .*

30. spacer 5.6|3468450|31|NC_013729|CRT matches to MT740731 (Ralstonia phage Claudette, complete genome) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
cgacccgaaccaacagcagcagccgatgacc	Protospacer
  ************ **********   .*

31. spacer 5.6|3468450|31|NC_013729|CRT matches to LT999987 (Pseudomonas phage vB_PaeS_PAO1_HW12 genome assembly, complete genome: monopartite) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
gcacccgcaccacccgcagcagcgcccagcc	Protospacer
******* **** **********  .  **

32. spacer 5.6|3468450|31|NC_013729|CRT matches to MK511036 (Pseudomonas phage BR327, partial genome) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
gcacccgcaccacccgcagcagcgcccagcc	Protospacer
******* **** **********  .  **

33. spacer 5.6|3468450|31|NC_013729|CRT matches to JQ762257 (Pseudomonas phage MP42, complete genome) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
gcacccgcaccacccgcagcagcgcccagcc	Protospacer
******* **** **********  .  **

34. spacer 5.6|3468450|31|NC_013729|CRT matches to MK511018 (Pseudomonas phage CF28, partial genome) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
gcacccgcaccacccgcagcagcgcccagcc	Protospacer
******* **** **********  .  **

35. spacer 5.6|3468450|31|NC_013729|CRT matches to NC_026601 (Pseudomonas phage vB_PaeS_PAO1_Ab30, complete genome) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
gcacccgcaccacccgcagcagcgcccagcc	Protospacer
******* **** **********  .  **

36. spacer 5.6|3468450|31|NC_013729|CRT matches to NC_030918 (Pseudomonas phage JBD93, complete genome) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
gcacccgcaccacccgcagcagcgcccagcc	Protospacer
******* **** **********  .  **

37. spacer 5.6|3468450|31|NC_013729|CRT matches to MH719192 (Pseudomonas phage Ps56, complete genome) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
gcacccgcaccacccgcagcagcgcccagcc	Protospacer
******* **** **********  .  **

38. spacer 5.6|3468450|31|NC_013729|CRT matches to EU272037 (Pseudomonas phage MP38, complete genome) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
gcacccgcaccacccgcagcagcgcccagcc	Protospacer
******* **** **********  .  **

39. spacer 5.6|3468450|31|NC_013729|CRT matches to KM389459 (UNVERIFIED: Pseudomonas phage F_ET309sp/Pa1651 clone contig00001 genomic sequence) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
gcacccgcaccacccgcagcagcgcccagcc	Protospacer
******* **** **********  .  **

40. spacer 5.6|3468450|31|NC_013729|CRT matches to JX434032 (Pseudomonas phage JBD30, complete genome) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
gcacccgcaccacccgcagcagcgcccagcc	Protospacer
******* **** **********  .  **

41. spacer 5.6|3468450|31|NC_013729|CRT matches to KU199708 (Pseudomonas phage JBD69, complete genome) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
gcacccgcaccacccgcagcagcgcccagcc	Protospacer
******* **** **********  .  **

42. spacer 5.6|3468450|31|NC_013729|CRT matches to DQ631426 (Pseudomonas phage DMS3, complete genome) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
gcacccgcaccacccgcagcagcgcccagcc	Protospacer
******* **** **********  .  **

43. spacer 5.6|3468450|31|NC_013729|CRT matches to JX434031 (Pseudomonas phage JBD24, complete genome) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
gcacccgcaccacccgcagcagcgcccagcc	Protospacer
******* **** **********  .  **

44. spacer 5.6|3468450|31|NC_013729|CRT matches to KM389326 (UNVERIFIED: Pseudomonas phage F_KK2074sp/Pa1651 clone contig00001 genomic sequence) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
gcacccgcaccacccgcagcagcgcccagcc	Protospacer
******* **** **********  .  **

45. spacer 5.6|3468450|31|NC_013729|CRT matches to KM389461 (UNVERIFIED: Pseudomonas phage F_TK432sp/Pa1651 clone ctg7180000000005 genomic sequence) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
gcacccgcaccacccgcagcagcgcccagcc	Protospacer
******* **** **********  .  **

46. spacer 5.8|3468546|31|NC_013729|CRT matches to MT740740 (Ralstonia phage Gervaise, complete genome) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
cgacccgaaccaacagcagcagccgatgacc	Protospacer
  ************ **********   .*

47. spacer 5.8|3468546|31|NC_013729|CRT matches to MT740727 (Ralstonia phage Alix, complete genome) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
cgacccgaaccaacagcagcagccgatgacc	Protospacer
  ************ **********   .*

48. spacer 5.8|3468546|31|NC_013729|CRT matches to MT740732 (Ralstonia phage Darius, complete genome) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
cgacccgaaccaacagcagcagccgatgacc	Protospacer
  ************ **********   .*

49. spacer 5.8|3468546|31|NC_013729|CRT matches to MT740731 (Ralstonia phage Claudette, complete genome) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
cgacccgaaccaacagcagcagccgatgacc	Protospacer
  ************ **********   .*

50. spacer 5.8|3468546|31|NC_013729|CRT matches to LT999987 (Pseudomonas phage vB_PaeS_PAO1_HW12 genome assembly, complete genome: monopartite) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
gcacccgcaccacccgcagcagcgcccagcc	Protospacer
******* **** **********  .  **

51. spacer 5.8|3468546|31|NC_013729|CRT matches to MK511036 (Pseudomonas phage BR327, partial genome) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
gcacccgcaccacccgcagcagcgcccagcc	Protospacer
******* **** **********  .  **

52. spacer 5.8|3468546|31|NC_013729|CRT matches to JQ762257 (Pseudomonas phage MP42, complete genome) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
gcacccgcaccacccgcagcagcgcccagcc	Protospacer
******* **** **********  .  **

53. spacer 5.8|3468546|31|NC_013729|CRT matches to MK511018 (Pseudomonas phage CF28, partial genome) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
gcacccgcaccacccgcagcagcgcccagcc	Protospacer
******* **** **********  .  **

54. spacer 5.8|3468546|31|NC_013729|CRT matches to NC_026601 (Pseudomonas phage vB_PaeS_PAO1_Ab30, complete genome) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
gcacccgcaccacccgcagcagcgcccagcc	Protospacer
******* **** **********  .  **

55. spacer 5.8|3468546|31|NC_013729|CRT matches to NC_030918 (Pseudomonas phage JBD93, complete genome) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
gcacccgcaccacccgcagcagcgcccagcc	Protospacer
******* **** **********  .  **

56. spacer 5.8|3468546|31|NC_013729|CRT matches to MH719192 (Pseudomonas phage Ps56, complete genome) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
gcacccgcaccacccgcagcagcgcccagcc	Protospacer
******* **** **********  .  **

57. spacer 5.8|3468546|31|NC_013729|CRT matches to EU272037 (Pseudomonas phage MP38, complete genome) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
gcacccgcaccacccgcagcagcgcccagcc	Protospacer
******* **** **********  .  **

58. spacer 5.8|3468546|31|NC_013729|CRT matches to KM389459 (UNVERIFIED: Pseudomonas phage F_ET309sp/Pa1651 clone contig00001 genomic sequence) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
gcacccgcaccacccgcagcagcgcccagcc	Protospacer
******* **** **********  .  **

59. spacer 5.8|3468546|31|NC_013729|CRT matches to JX434032 (Pseudomonas phage JBD30, complete genome) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
gcacccgcaccacccgcagcagcgcccagcc	Protospacer
******* **** **********  .  **

60. spacer 5.8|3468546|31|NC_013729|CRT matches to KU199708 (Pseudomonas phage JBD69, complete genome) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
gcacccgcaccacccgcagcagcgcccagcc	Protospacer
******* **** **********  .  **

61. spacer 5.8|3468546|31|NC_013729|CRT matches to DQ631426 (Pseudomonas phage DMS3, complete genome) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
gcacccgcaccacccgcagcagcgcccagcc	Protospacer
******* **** **********  .  **

62. spacer 5.8|3468546|31|NC_013729|CRT matches to JX434031 (Pseudomonas phage JBD24, complete genome) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
gcacccgcaccacccgcagcagcgcccagcc	Protospacer
******* **** **********  .  **

63. spacer 5.8|3468546|31|NC_013729|CRT matches to KM389326 (UNVERIFIED: Pseudomonas phage F_KK2074sp/Pa1651 clone contig00001 genomic sequence) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
gcacccgcaccacccgcagcagcgcccagcc	Protospacer
******* **** **********  .  **

64. spacer 5.8|3468546|31|NC_013729|CRT matches to KM389461 (UNVERIFIED: Pseudomonas phage F_TK432sp/Pa1651 clone ctg7180000000005 genomic sequence) position: , mismatch: 8, identity: 0.742

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
gcacccgcaccacccgcagcagcgcccagcc	Protospacer
******* **** **********  .  **

65. spacer 5.10|3468642|31|NC_013729|CRT matches to NZ_CP039644 (Azospirillum sp. TSA2s plasmid p2, complete sequence) position: , mismatch: 8, identity: 0.742

gcacccgagccagccgcggcacccgagccag	CRISPR spacer
attcccgatccagccgcggcaccggagctgc	Protospacer
.. ***** ************** ****..

66. spacer 5.10|3468642|31|NC_013729|CRT matches to NZ_CP014802 (Salipiger profundus strain JLT2016 plasmid pTPRO6, complete sequence) position: , mismatch: 8, identity: 0.742

gcacccgagccagccgcggcacccgagccag	CRISPR spacer
aacatcgcgcccgccgcggcacccgagcccg	Protospacer
.   .** *** ***************** *

67. spacer 5.10|3468642|31|NC_013729|CRT matches to NC_011961 (Thermomicrobium roseum DSM 5159 plasmid unnamed, complete sequence) position: , mismatch: 8, identity: 0.742

gcacccgagccagccgcggcacccgagccag	CRISPR spacer
gcttgtgagccagccgccgcacccgcgcctt	Protospacer
** . .*********** ******* ***

68. spacer 5.3|3468300|31|NC_013729|CRT matches to KF977490 (Rhizobium phage vB_RglS_P106B, complete genome) position: , mismatch: 9, identity: 0.71

gcagccaagccagccgcagcagccgcatggg	CRISPR spacer
ccttggaagccaaccgcagcagccgcattta	Protospacer
 *    ******.***************  .

69. spacer 5.4|3468354|31|NC_013729|CRT matches to NZ_CP029776 (Deinococcus actinosclerus strain Deinococcus actinosclerus SJTR plasmid unnamed2, complete sequence) position: , mismatch: 9, identity: 0.71

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
ccacccgaaccacccgcagccgcctcgcctg	Protospacer
 *********** ******* *** ..* ..

70. spacer 5.6|3468450|31|NC_013729|CRT matches to NZ_CP029776 (Deinococcus actinosclerus strain Deinococcus actinosclerus SJTR plasmid unnamed2, complete sequence) position: , mismatch: 9, identity: 0.71

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
ccacccgaaccacccgcagccgcctcgcctg	Protospacer
 *********** ******* *** ..* ..

71. spacer 5.8|3468546|31|NC_013729|CRT matches to NZ_CP029776 (Deinococcus actinosclerus strain Deinococcus actinosclerus SJTR plasmid unnamed2, complete sequence) position: , mismatch: 9, identity: 0.71

gcacccgaaccaaccgcagcagccgtacgca	CRISPR spacer
ccacccgaaccacccgcagccgcctcgcctg	Protospacer
 *********** ******* *** ..* ..

72. spacer 5.10|3468642|31|NC_013729|CRT matches to KU998238 (Gordonia phage Splinter, complete genome) position: , mismatch: 9, identity: 0.71

gcacccgagccagccgcggcacccgagccag	CRISPR spacer
ctcccagagccagccgcgccacccgacacca	Protospacer
 . ** ************ *******  * .

73. spacer 5.10|3468642|31|NC_013729|CRT matches to NC_030911 (Gordonia phage Vendetta, complete genome) position: , mismatch: 9, identity: 0.71

gcacccgagccagccgcggcacccgagccag	CRISPR spacer
ctcccagagccagccgcgccacccgacacca	Protospacer
 . ** ************ *******  * .

Prophage detection

Region

Region Position

Protein_number

Hit_taxonomy

Key_proteins

Att_site

Prophage annotation

DBSCAN-SWA_1

5529810 : 5543258

Orpheovirus(37.5%)

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_063822851.1\|5529810_5533047_-	S8 family serine peptidase	A0A217EQY2	Bacillus_phage	4.4e-31	38.5
WP_012922700.1\|5533190_5534162_-	WYL domain-containing protein	A0A1B0RXM1	Streptococcus_phage	1.4e-09	25.4
WP_012922702.1\|5535272_5535755_+	hypothetical protein	NA	NA	NA	NA
WP_012922703.1\|5535797_5536268_-	6,7-dimethyl-8-ribityllumazine synthase	A0A2I2L4Y7	Orpheovirus	2.3e-13	34.8
WP_012922704.1\|5536267_5537500_-	bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase/GTP cyclohydrolase II	A0A2H4PQS2	Staphylococcus_phage	2.4e-94	45.4
WP_012922705.1\|5537499_5538177_-	nicotinamide mononucleotide transporter	NA	NA	NA	NA
WP_012922706.1\|5538173_5538806_-	riboflavin synthase	A0A2H4PQS5	Staphylococcus_phage	3.7e-35	42.4
WP_012922707.1\|5538807_5539842_-	bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6-(5-phosphoribosylamino)uracil reductase RibD	A0A2I2L4R9	Orpheovirus	5.9e-38	30.5
WP_012922708.1\|5540421_5542023_+	ABC-F family ATP-binding cassette domain-containing protein	A0A2I4R674	Erysipelothrix_phage	2.4e-22	32.5
WP_148257081.1\|5542175_5543258_+	protein kinase	A0A2I2L4T9	Orpheovirus	1.3e-11	27.8

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. NC_013729

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

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