ID STE11_YEAS6 Reviewed; 717 AA.
AC B5VNQ3;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 08-NOV-2023, entry version 63.
DE RecName: Full=Serine/threonine-protein kinase STE11;
DE EC=2.7.11.25;
GN Name=STE11; ORFNames=AWRI1631_123920;
OS Saccharomyces cerevisiae (strain AWRI1631) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=545124;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AWRI1631;
RX PubMed=18778279; DOI=10.1111/j.1567-1364.2008.00434.x;
RA Borneman A.R., Forgan A.H., Pretorius I.S., Chambers P.J.;
RT "Comparative genome analysis of a Saccharomyces cerevisiae wine strain.";
RL FEMS Yeast Res. 8:1185-1195(2008).
CC -!- FUNCTION: Serine/threonine protein kinase required for cell-type-
CC specific transcription and signal transduction in yeast. It is thought
CC that it phosphorylates the STE7 protein kinase which itself,
CC phosphorylates the FUS3 and or KSS1 kinases (By similarity).
CC {ECO:0000250}.
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=2.7.11.25;
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=2.7.11.25;
CC -!- SUBUNIT: Homodimer. Interacts (via SAM domain) with STE50 (via SAM
CC domain). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase kinase subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDZ70440.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; ABSV01001686; EDZ70440.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; B5VNQ3; -.
DR BMRB; B5VNQ3; -.
DR SMR; B5VNQ3; -.
DR Proteomes; UP000008988; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0019236; P:response to pheromone; IEA:UniProtKB-KW.
DR CDD; cd09534; SAM_Ste11_fungal; 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR029458; Ras-bd_By2.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR11584:SF369; APOPTOTIC SIGNAL-REGULATING KINASE 1, ISOFORM C; 1.
DR PANTHER; PTHR11584; SERINE/THREONINE PROTEIN KINASE; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF14847; Ras_bdg_2; 1.
DR Pfam; PF07647; SAM_2; 1.
DR SMART; SM01304; Ras_bdg_2; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Pheromone response;
KW Phosphoprotein; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..717
FT /note="Serine/threonine-protein kinase STE11"
FT /id="PRO_0000377640"
FT DOMAIN 20..84
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 415..712
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 453..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..479
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 579
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 421..429
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 444
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23561"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23561"
SQ SEQUENCE 717 AA; 80681 MW; 75B5CC70114DE08C CRC64;
MEQTQTAEGT DLLIGDEKTN DLPFVQLFLE EIGCTQYLDS FIQCNLVTEE EIKYLDKDIL
IALGVNKIGD RLKILRKSKS FQRDKRIEQV NRLKNLMEKV SSLSTATLSM NSELIPEKHC
VIFILNDGSA KKVNVNGCFN ADSIKKRLIR RLPHELLATN SNGEVTKMVQ DYDVFVLDYT
KNVLHLLYDV ELVTICHAND RVEKNRLIFV SKDQTPSDKA ISTSKKLYLR TLSALSQVGP
SSSNLLAQNK GISHNNAEGK LRIDNTEKDR IRQIFNQRPP SEFISTNLAG YFPHTDMKRL
QKTMRESFRH SARLSIAQRR PLSAESNNIG DILLKHSNAV DMALLQGLDQ TRLSSKLDTT
KIPKLAHKRP EDNDAISNQL ELLSVESGEE EDHDFFGEDS DIVSLPTKIA TPKNWLKGAC
IGSGSFGSVY LGMNAHTGEL MAVKQVEIKN NNIGVSTDNN KQANSDENNE QEEQQEKIED
VGAVSHPKTN QNIHRKMVDA LQHEMNLLKE LHHENIVTYY GASQEGGNLN IFLEYVPGGS
VSSMLNNYGP FEESLITNFT RQILIGVAYL HKKKIIHRDI KGANILIDIK GCVKITDFGI
SKKLSPLNKK QNKRASLQGS VFWMSPEVVK QSATTAKADI WSTGCVVIEM FTGKHPFPDF
SQMQAIFKIG TNTTPEIPSW ATSEGKNFLR KAFELDYQYR PGALELLQHP WLDAHII
//
