ID   STE20_ASHGO             Reviewed;         970 AA.
AC   Q75DK7;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 2.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Serine/threonine-protein kinase STE20;
DE            EC=2.7.11.1;
GN   Name=STE20; OrderedLocusNames=ABR014W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 200; 212; 230; 282; 907; 914
RP   AND 917-931.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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).
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=2.7.11.1;
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; AE016815; AAS50784.2; -; Genomic_DNA.
DR   RefSeq; NP_982960.2; NM_208313.2.
DR   AlphaFoldDB; Q75DK7; -.
DR   SMR; Q75DK7; -.
DR   STRING; 33169.AAS50784; -.
DR   EnsemblFungi; AAS50784; AAS50784; AGOS_ABR014W.
DR   GeneID; 4619052; -.
DR   KEGG; ago:AGOS_ABR014W; -.
DR   eggNOG; KOG0578; Eukaryota.
DR   HOGENOM; CLU_000288_26_3_1; -.
DR   InParanoid; Q75DK7; -.
DR   OMA; TPYNATH; -.
DR   Proteomes; UP000000591; Chromosome II.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
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:0035556; P:intracellular signal transduction; IBA:GO_Central.
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:0006468; P:protein phosphorylation; IBA:GO_Central.
DR   GO; GO:0007124; P:pseudohyphal growth; IEA:EnsemblFungi.
DR   GO; GO:0007096; P:regulation of exit from mitosis; IEA:EnsemblFungi.
DR   GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
DR   GO; GO:0001402; P:signal transduction involved in filamentous growth; IEA:EnsemblFungi.
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..970
FT                   /note="Serine/threonine-protein kinase STE20"
FT                   /id="PRO_0000237625"
FT   DOMAIN          380..393
FT                   /note="CRIB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT   DOMAIN          683..934
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          86..185
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          236..284
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          311..351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          499..551
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          592..663
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..127
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        164..185
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        236..277
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        311..345
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        531..551
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        609..627
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        628..663
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        802
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         689..697
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         712
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   970 AA;  105431 MW;  83C78E0A8BA3FBE2 CRC64;
     MSKVSGANET LQGALAPLSH MGGGGDATLL KDEGQVELPR GPGVLNVQVL PEEGHAHLQD
     LEGYKSMDPR QSESASTDVS EMLQHTASLD DPIQFTRVST SSVTSNSSSD PRESGDTQET
     GSRRGCSTEE QAPAGAERVS GQDQDSWDVE EVVAEPRSGI DVTPVGDVTN STIRASGRSA
     ESTSHYLDEY SDTRYSSSSP SSGSRKLSTT IITPEKNVVA QALHCYADNY ESPLNDLMSS
     GDERSSSVRE TSFENASSDT NANLNGGRAS TGESMRSPPP ATGLPNGFVH TQASAPALPV
     LPAKSPFRAV QSPFSGTRKS RNSANLAELS LPRTSTSSAS SMEQRKSRGG RMKVVLSSFV
     QNIRRNSQGE KRRSGTAMKI STPYNATHVH HVGVDSRTGE YTGLPEEWER LLASSGISKK
     EQQQHPQAVM DIVKFYQDVT GTSGEDKVFK TFNVSSTNAC ELSSSPSFKT PSLSSITRFE
     GSHEAYNSAY HSPMLQSPMG FHDPQHDEKF IPSRPAPRPP GGAAPKTDFT SPLAYDSQSA
     TATPKNQRFS NQSSGFFSLA RKATLNKNKQ QLPPIPSAAA ASAPITQPGS TANIPYIKPA
     ENPVSAPSKS IPPSLPAVPT PPPPIEKDPP LRDLERERER EHSSAKQGQL ALERKREEKR
     RRNQKLQAKL AEICSPGDPS KIYRNLVKIG QGASGGVYTA YEIGTNASVA IKQMNLEKQP
     KKELIINEIL VMKGSRHNNI VNFIDSYLLK GDLWVIMEYM EGGSLTDVVT HCILTEGQIA
     AVSRETLRGL HFLHSKGVIH RDIKSDNILL SMDGNIKLTD FGFCAQINET NLKRTTMVGT
     PYWMAPEVVS RKEYGPKVDI WSLGIMIIEM IEGEPPYLNE TPLRALYLIA TNGTPKLKDA
     DSLSPVLKRF LSWCLQVSPN DRATAMELLY DKFIVEVAEA NASLAPLVKL ARMKKLAEKM
     DADSDDNRTD