STE20_CANGA
ID STE20_CANGA Reviewed; 915 AA.
AC Q6FN53;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Serine/threonine-protein kinase STE20;
DE EC=2.7.11.1;
GN Name=STE20; OrderedLocusNames=CAGL0K02673g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
RN [2]
RP FUNCTION.
RX PubMed=15164359; DOI=10.1002/yea.1125;
RA Calcagno A.-M., Bignell E., Rogers T.R., Canedo M., Muehlschlegel F.A.,
RA Haynes K.;
RT "Candida glabrata Ste20 is involved in maintaining cell wall integrity and
RT adaptation to hypertonic stress, and is required for wild-type levels of
RT virulence.";
RL Yeast 21:557-568(2004).
CC -!- FUNCTION: MAP4K component of the MAPK pathway required for the mating
CC pheromone response and the regulation of cell polarity and cell cycle.
CC Phosphorylates histone H2B to form H2BS10ph (By similarity). Involved
CC in cell wall integrity, hypertonic stress adaptation and virulence.
CC {ECO:0000250, ECO:0000269|PubMed:15164359}.
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=2.7.11.1;
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=2.7.11.1;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000305}.
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DR EMBL; CR380957; CAG61302.1; -; Genomic_DNA.
DR RefSeq; XP_448341.1; XM_448341.1.
DR AlphaFoldDB; Q6FN53; -.
DR SMR; Q6FN53; -.
DR STRING; 5478.XP_448341.1; -.
DR PRIDE; Q6FN53; -.
DR EnsemblFungi; CAG61302; CAG61302; CAGL0K02673g.
DR GeneID; 2890268; -.
DR KEGG; cgr:CAGL0K02673g; -.
DR CGD; CAL0134517; STE20.
DR VEuPathDB; FungiDB:CAGL0K02673g; -.
DR eggNOG; KOG0578; Eukaryota.
DR HOGENOM; CLU_000288_26_3_1; -.
DR InParanoid; Q6FN53; -.
DR OMA; PKEWQRM; -.
DR Proteomes; UP000002428; Chromosome K.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000131; C:incipient cellular bud site; IEA:EnsemblFungi.
DR GO; GO:0043332; C:mating projection tip; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019899; F:enzyme binding; IEA:EnsemblFungi.
DR GO; GO:0044025; F:histone kinase activity (H2B-S14 specific); IEA:EnsemblFungi.
DR GO; GO:0008349; F:MAP kinase kinase kinase kinase activity; IGI:CGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0007121; P:bipolar cellular bud site selection; IEA:EnsemblFungi.
DR GO; GO:0007118; P:budding cell apical bud growth; IEA:EnsemblFungi.
DR GO; GO:0071470; P:cellular response to osmotic stress; IMP:CGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:CGD.
DR GO; GO:0001403; P:invasive growth in response to glucose limitation; IEA:EnsemblFungi.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:EnsemblFungi.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR GO; GO:0007232; P:osmosensory signaling pathway via Sho1 osmosensor; IEA:EnsemblFungi.
DR GO; GO:0000750; P:pheromone-dependent signal transduction involved in conjugation with cellular fusion; IEA:EnsemblFungi.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:EnsemblFungi.
DR GO; GO:0007124; P:pseudohyphal growth; IEA:EnsemblFungi.
DR GO; GO:0007096; P:regulation of exit from mitosis; IEA:EnsemblFungi.
DR GO; GO:0001402; P:signal transduction involved in filamentous growth; IGI:CGD.
DR GO; GO:0035376; P:sterol import; IEA:EnsemblFungi.
DR GO; GO:0034063; P:stress granule assembly; IEA:EnsemblFungi.
DR GO; GO:0000011; P:vacuole inheritance; IEA:EnsemblFungi.
DR CDD; cd01093; CRIB_PAK_like; 1.
DR Gene3D; 3.90.810.10; -; 1.
DR InterPro; IPR000095; CRIB_dom.
DR InterPro; IPR036936; CRIB_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR033923; PAK_BD.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00786; PBD; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00285; PBD; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50108; CRIB; 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; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
KW Pheromone response; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..915
FT /note="Serine/threonine-protein kinase STE20"
FT /id="PRO_0000237628"
FT DOMAIN 335..348
FT /note="CRIB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT DOMAIN 620..871
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 73..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 894..915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..572
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 739
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 626..634
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 649
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 915 AA; 100411 MW; 4CC3CBE4C4CCC0EA CRC64;
MSNANQKENV PSLGLPRTHG TLNVNALKAT DILKHKGKLN EVNSDQSTTN ENDEVQEEAV
FLDDPVHFTR VSSSSELSAA LSVNTTEQEQ DEEKGTEHAE LEPAEEDTVE VDTIRNNGDK
TYSTIRESAS DFETTNNTLI EISKNSSTYS STEFLNNNNN GISNSNRATI DSESKLRMNK
LREGSSTSLS NDSNGFNGMI SSNQASTVLS TPSQKPSSTT NTITKANNGG STRAQKEKHT
SPKLPSTVTA PSSHRKSADL SKTNKLPSTT AKRTPKQAVT SSSPKEPAKR KSSTSKMKGM
FSSLVQNMKR NSSDNRKSAS SLSSVSSSSS STLKISTPYN PKHIYHVGVD ARTGEYTGLP
EEWERLLASS GISRKEQQQN MQAVIDIVNF YQDVADHTGE EKVIKTFDPK KQNPLVRDSL
SKYEQVDDNR TSYASGGTPT LEQNGFHTSS TPRSRTSLTS PTAGYSMIST PPMATQEKYI
PTRPAPKPPG QQTPSSNASL TPKMQNATMS PIKENISSPV TKSEVDDELL LSKKNASLPK
LPSDDSSSHK KSATDSAPTS VETDTETVKV PPIPKTTPTV PAKASRRSNE KKKEERERNK
KLLYAKLTEI CSPGDPKSKY RDLIKIGQGA SGGVYIAHDT ESEDSVAIKQ MNLEKQPKKE
LILNEILVMR ESKHSNIVNF IDSYLAKGDL WIVMEYMEGG SLTDVVTHCL LSEGQIGAVC
RETLKGLQFL HSKGVLHRDI KSDNILLSLK GNIKLTDFGF CAQINENNLK RTTMVGTPYW
MAPEVVSRKE YGPKVDIWSL GIMIIEMIEG EPPYLNETPL RALYLIATNG TPKLKEPEAL
SDTLTKFLDW CLKVDPSERA TATELLDDPF ITEIAEDNSS LSPLVKLARI KKLEEQEEDA
GTDETEPETT PDTTI
