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 27-MAR-2024, entry version 126. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 EnsemblFungi; CR_03900W_A-T; CR_03900W_A-T-p1; CR_03900W_A. 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; 587955at2759; -. 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:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:1900436; P:positive regulation of filamentous growth of a population of unicellular organisms in response to starvation; IMP:CGD. 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 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 //