ID B9WB15_CANDC Unreviewed; 2467 AA.
AC B9WB15;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=CHK1 {ECO:0000313|EMBL:CAX43585.1};
GN OrderedLocusNames=Cd36_18070 {ECO:0000313|CGD:CAL0000163942};
GN ORFNames=CD36_18070 {ECO:0000313|EMBL:CAX43585.1};
OS Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS NRRL Y-17841) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=573826 {ECO:0000313|EMBL:CAX43585.1, ECO:0000313|Proteomes:UP000002605};
RN [1] {ECO:0000313|EMBL:CAX43585.1, ECO:0000313|Proteomes:UP000002605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841
RC {ECO:0000313|Proteomes:UP000002605};
RX PubMed=19745113; DOI=10.1101/gr.097501.109;
RA Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT Candida albicans.";
RL Genome Res. 19:2231-2244(2009).
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DR EMBL; FM992689; CAX43585.1; -; Genomic_DNA.
DR RefSeq; XP_002418285.1; XM_002418240.1.
DR GeneID; 8045843; -.
DR KEGG; cdu:CD36_18070; -.
DR CGD; CAL0000163942; Cd36_18070.
DR VEuPathDB; FungiDB:CD36_18070; -.
DR eggNOG; KOG0519; Eukaryota.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_000835_0_0_1; -.
DR OrthoDB; 2734979at2759; -.
DR Proteomes; UP000002605; Chromosome 2.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0036180; P:filamentous growth of a population of unicellular organisms in response to biotic stimulus; IEA:UniProt.
DR GO; GO:1900445; P:positive regulation of filamentous growth of a population of unicellular organisms in response to biotic stimulus; IEA:UniProt.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR041664; AAA_16.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43719:SF28; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK2; 1.
DR PANTHER; PTHR43719; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF13191; AAA_16; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CAX43585.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 356..634
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 2000..2221
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 2336..2462
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 53..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2390
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2467 AA; 279442 MW; 579B84A614BE7FF5 CRC64;
MSMNCFNSHE NARDCEKETI TTTEYHESEQ PDVKAIRNFK FFKMDEAETK NNSNLQISNL
SPLDSQSEPP SVLSLNHSTI PEQYERSQGT PDPLHTPEIS LSDYLYDQTL SPQGFDNSRE
NFNIHQTIAS LFEDNSSVIS QESVEDTKTT LSSETTDNLS LSNASYLTNI NFVQNHLEYL
SQNFSGNPSS NGLSPSSSSS SQIDFDAANL TPESIPGYIL NKKFGPVHQS TDSVYNAIKV
AQNKTNDFHS NAVASQKPLD LNSKVIVRLS PNIFHNLSLS RFLNEWYILS GKHSSKKHRV
WSNESLTNEY VQKKTIPIFD KEDARFRPTL PLNIPGVLYP QEILNFRVNS DDYPLKQASP
STNQKRFAMV YPDNDYKTFK QLSMLAVYEQ QTRQGSFSSD EARRKSSSGF NVGVNAPTIE
AGSLDSLGTL MQNHHLGTNS TNGDPLHSKL AKFDYEIIKS PMKLIEVLTD IMRVVETISV
IHELGFVHNG LTSNNLLKSE KNARDIKVTG WGFAFSFSEN CSHGYRNKHL AQVQDLIPYM
APEVLAITNS VVEYRSDFYS LGVIMYELIL GTLPFKNSNP QTLIRMHNFE KPIAPSMLAP
SWISEKLSSV VMKLLEKNPR NRYSDCHSLL HDLTEVKNMY ISKLLESGES GQTGNLNLSD
QQYYLAKEIV PHPEKMGVIP VLGLREHFIG RGDFLQNVTE TYNSNQNGVD LVFISGESGR
GKSLILQDLQ AGAVLKHNFY YSWKFSFFGA DTHVYRFLVE GVQKIITQIL NSSEEIRNTW
RDLILTHIPI DLSILFYLIP ELKVLLGKKY TSIYQHKVGM GTSRNTLKEN QTLRLEIKLR
QILKEFFRLI AKQGLSIFLD DVQWCSEESW RLLCDVLDFD SSGEAKEGVS IKVVVCYALN
ADHLENVDTE HKKVSFCRYA KQSNLNLHEF NIPHIPLEDA IDFLCEPYVK SDYRLSGEHL
NLVDNLNDTN KNPNDNLKAI PTIIQELYQS SGGNVLLLVF LTRMTKLSGK VPFSHFSNRD
SHLYDYLSNN NYGSTRNEIL ANYLNMGTSS DARALLKIAA LISSGSGFFF SDLIVATDLP
MAETFQLLQI CIHSRIIVPT STYYKVPMDL IASDQTPFDL TDDNIWKLAT LCSYKFFHDS
ICTHIIKELN ASGEFKELSR LCGLRFYNTI TKERLLNIGG YLQMATHFRN SYEAARPEEN
EKYVEVLVQA GRYAISTYNM KLSQWFFNVV GELVYNLDSK TQLKSVLTIA ENHFNSCEFE
QCLNVVENAQ RKFGFDRLIF CIQIIRCKIE LGDYDEANQI AIECLQELGV PLNDDECVGK
NSFETFSGKI PLSVAEIRGI LKIKKCKNSR TLLMYQLVSE LIVLFKVQGK DRMRKFLTAY
AMSQIYSQGS SPYCAVILID FAQSLVNEHT TSGMLKAKEL SVVMLSLVNR APEISLSYVQ
SIYEYYFSCH AVLFESIEKM SDLINPGNAS SDCTRSSFYS SFHLMVHVSK IFFSCMNGEG
LKMFSASRAK SYLLGDSHTT EMDNFLYDSE MLLCGHSKLN EFMIKYQSFN QTSVGKFCYY
LIVLCVMARD KRFDDAASLI LQVVEDLSES LPVSFLHHQY YLICGKVFAY RQTKMPESDE
QVEHILERQF VRYELWASTN ESILLPRYLL LNAYKQIREN NVDKLEILDS FEEALQTTQR
YHNVYDMCWI NFECARWLIN IKQKRHRISR MVKQGLKIMR SLELKNHLRL SEIEFGEYIE
DEHQKNKWAG LTDNLVLDSV ATSQQQNMES RLSSNDDKQS VRGKHYTKKE LDNHLLRLHL
DGHGTSIDLN SAICECLAIS EALDENSILT KLMASAIKYS GATYGVIVTK KNQETPFLRT
IGSQQNIHTL NNIPISDDIC PTQLIRHVLH TGETVNKAHD HIGFANNFGN EYFQATDKKY
SVVCLPLKSQ LGFFGAIYLE AGEGSFGHED LFNERKCDLL QLFCTQAAVA LGKERLLLQM
EVAKMAAEDA TDEKASFLAN MSHEIRTPFN SLLSFAIFLL DTKLDSTQRE YVEAIQSSAM
ITLNIIDGIL AFSKIEHGSF TLENAPFSLN DCIETAIQVS GETVLNDQIE LVFCNNCPEI
EFVVGDLTRF RQIIINLVGN AIKFTTKGHV LISCDSRKLT EERVEINVSV QDSGIGIPKK
SQNKVFGAFS QVDGSARRQY GGSGLGLAIS KKLTELMGGT IRFESEEGIG TTFFVSVIMD
AKVYSTPPFS SNKKCLIYSK HRLTAKSIAK ILKYFGLTVE VTNDKSDFLA SVASNDIVFI
DRGMETNASG AAKVIPIDAK PFKRNKLISI LKEQPSSPAK VHGTNEFDLS KKYPLRILLA
EDNLLNYKVC LKHLDKLGYK ADHAKDGVIV LDKCKELLEK NEKYDVILMD IQMPRKDGIT
ATRDLKTLFH TYQKESWLPV IVALTANVAG DDKKKCLEEG MFDFITKPIL PKELRRILTK
VGESVNI
//
