STE7_CANAL
ID STE7_CANAL Reviewed; 589 AA.
AC Q5A6T5; A0A1D8PSL2;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Serine/threonine-protein kinase STE7 homolog;
DE EC=2.7.12.2;
GN Name=HST7; Synonyms=STE7; OrderedLocusNames=CAALFM_CR03900WA;
GN ORFNames=CaO19.469, CaO19.8100;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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; CP017630; AOW31128.1; -; Genomic_DNA.
DR RefSeq; XP_717333.2; XM_712240.2.
DR AlphaFoldDB; Q5A6T5; -.
DR SMR; Q5A6T5; -.
DR BioGRID; 1223967; 4.
DR STRING; 237561.Q5A6T5; -.
DR PRIDE; Q5A6T5; -.
DR GeneID; 3640953; -.
DR KEGG; cal:CAALFM_CR03900WA; -.
DR CGD; CAL0000197730; HST7.
DR VEuPathDB; FungiDB:CR_03900W_A; -.
DR eggNOG; KOG0581; Eukaryota.
DR HOGENOM; CLU_000288_63_23_1; -.
DR InParanoid; Q5A6T5; -.
DR OrthoDB; 688282at2759; -.
DR PRO; PR:Q5A6T5; -.
DR Proteomes; UP000000559; Chromosome R.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004708; F:MAP kinase kinase activity; IGI:CGD.
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:0009267; P:cellular response to starvation; IMP:CGD.
DR GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR GO; GO:0044182; P:filamentous growth of a population of unicellular organisms; IMP:CGD.
DR GO; GO:0036170; P:filamentous growth of a population of unicellular organisms in response to starvation; IMP:CGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:CGD.
DR GO; GO:0000165; P:MAPK cascade; IGI:CGD.
DR GO; GO:1990277; P:parasexual reproduction with cellular fusion; IMP:CGD.
DR GO; GO:0071507; P:pheromone response MAPK cascade; IMP:CGD.
DR GO; GO:1900436; P:positive regulation of filamentous growth of a population of unicellular organisms in response to starvation; IMP:CGD.
DR GO; GO:0006468; P:protein phosphorylation; IMP:CGD.
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 Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..589
FT /note="Serine/threonine-protein kinase STE7 homolog"
FT /id="PRO_0000413042"
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..233
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..233
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; 65224 MW; 6C1209F89BD7A8F5 CRC64;
MTRTTRIDTQ EATKHKDLPP VPSPLSLSSN PNPECLMESK SLGRKNFKKL SLDASPVKST
SGSLRSSDMM SIKEPTSLRQ KRQRPPPILH LPTASSSATS TPTSNITGSS SASSIQFAQK
SPGSGVIVSQ TLSRPSSAGG IPSSGYSSLN VNQSNRNVDP DNVVSTDMIL NQISNLDLTS
MNHHRQHYQN SHHHLPTTNR KRQTVISSIS PTKSSAASSS LEPQIQSLPA SSQSPIATTS
SLKLNNKDLL 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
