ID STE7_CANAW Reviewed; 589 AA.
AC C4YLK8; P46599; P78596;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Serine/threonine-protein kinase STE7 homolog;
DE EC=2.7.12.2;
GN Name=HST7; Synonyms=STE7; ORFNames=CAWG_01727;
OS Candida albicans (strain WO-1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294748;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=WO-1;
RX PubMed=8544826; DOI=10.1007/bf00418030;
RA Clark K.L., Feldmann P.J., Dignard D., Larocque R., Brown A.J., Lee M.G.,
RA Thomas D.Y., Whiteway M.;
RT "Constitutive activation of the Saccharomyces cerevisiae mating response
RT pathway by a MAP kinase kinase from Candida albicans.";
RL Mol. Gen. Genet. 249:609-621(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WO-1;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.12.2;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.12.2;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.2;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase subfamily. {ECO:0000305}.
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DR EMBL; L19195; AAB59338.1; -; Genomic_DNA.
DR EMBL; CM000309; EEQ43489.1; -; Genomic_DNA.
DR PIR; S60154; S60154.
DR PIR; S60159; S60159.
DR AlphaFoldDB; C4YLK8; -.
DR SMR; C4YLK8; -.
DR PaxDb; 5476-C4YLK8; -.
DR VEuPathDB; FungiDB:CAWG_01727; -.
DR HOGENOM; CLU_000288_63_23_1; -.
DR OMA; SWAKKIR; -.
DR PHI-base; PHI:462; -.
DR Proteomes; UP000001429; Chromosome R.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004708; F:MAP kinase kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:RHEA.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd06620; PKc_Byr1_like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR049613; Byr1-like_cat.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR47448; DUAL SPECIFICITY MITOGEN-ACTIVATED PROTEIN KINASE KINASE DSOR1-LIKE PROTEIN; 1.
DR PANTHER; PTHR47448:SF1; SERINE_THREONINE-PROTEIN KINASE STE7 HOMOLOG; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..589
FT /note="Serine/threonine-protein kinase STE7 homolog"
FT /id="PRO_0000413043"
FT DOMAIN 249..565
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 374
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 255..263
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 278
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 402
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 408
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT CONFLICT 83
FT /note="Q -> T (in Ref. 1; AAB59338)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="A -> S (in Ref. 1; AAB59338)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 589 AA; 65218 MW; D334AA13E13DA686 CRC64;
MTRTTRIDTQ EATKHKDLPP VPSPLSLSSN PNPECLMESK SLGRKNFKKL SLDASPVKST
SGSLRSSDMM SIKEPTSLRQ KRQRPPPILH LPTASSSATS TPTSNITGSS SASSIQFAQK
SPGSGVIVSQ TLSRPSSAGG IPSSGYSSLN VNQSNRNVDP DNVVSTDMIL NQISNLDLTS
MNHHRQHYQN SHHHLPTTNR KRQTVISSIS PTKSSAASSP LEPQIQSLPA SSQSPIATTS
ALKLNNKDLL TLKQLGSGNS GSVSKILHIP TQKTMAKKII HIDSKSVIQT QIIRELRILH
ECHSPYIIEF YGACLNNNNT IVICMEYCNC GSLDKILPLC ENKQFPTFVL KKLSFAILSG
LTYLYTTHKI IHRDIKPNNV LMTHKGEFKL CDFGVSRELT NSLAMADTFV GTSMYMSPER
IQGLDYGVKS DVWSTGLMLI ELASGVPVWS EDDNNNDDDE DDEDDAYVRQ GSIAAERNGQ
NSPSRSRKNK QKGNGYNSYN GPEGILDLLQ RIVNEDAPTL TNKINPVTKL PYDKYLCQFI
DLCLIKDDSV RKTPWQLLED KEHFFKGVEE GVYDKEHKSW AKKIRKCKV
//
