ID   STE7_CANAX              Reviewed;         589 AA.
AC   P0CY25; P46599; P78596;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 1.
DT   03-AUG-2022, entry version 24.
DE   RecName: Full=Serine/threonine-protein kinase STE7 homolog;
DE            EC=2.7.12.2;
GN   Name=STE7; Synonyms=HST7;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 11651 / B792 / 171D;
RX   PubMed=9185854; DOI=10.1016/s0378-1119(96)00758-5;
RA   Singh P., Ghosh S., Datta A.;
RT   "A novel MAP-kinase kinase from Candida albicans.";
RL   Gene 190:99-104(1997).
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; U72980; AAC49733.1; -; Genomic_DNA.
DR   AlphaFoldDB; P0CY25; -.
DR   SMR; P0CY25; -.
DR   VEuPathDB; FungiDB:CAWG_01727; -.
DR   VEuPathDB; FungiDB:CR_03900W_A; -.
DR   BRENDA; 2.7.12.2; 1096.
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   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   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 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_0000086687"
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"
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