ID   STE20_DEBHA             Reviewed;        1079 AA.
AC   Q6BNF3;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Serine/threonine-protein kinase STE20;
DE            EC=2.7.11.1;
GN   Name=STE20; OrderedLocusNames=DEHA2E22220g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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).
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; CR382137; CAG88548.2; -; Genomic_DNA.
DR   RefSeq; XP_460267.2; XM_460267.1.
DR   AlphaFoldDB; Q6BNF3; -.
DR   SMR; Q6BNF3; -.
DR   STRING; 4959.XP_460267.2; -.
DR   EnsemblFungi; CAG88548; CAG88548; DEHA2E22220g.
DR   GeneID; 2902125; -.
DR   KEGG; dha:DEHA2E22220g; -.
DR   VEuPathDB; FungiDB:DEHA2E22220g; -.
DR   eggNOG; KOG0578; Eukaryota.
DR   HOGENOM; CLU_000288_26_0_1; -.
DR   InParanoid; Q6BNF3; -.
DR   OMA; RKFLAWC; -.
DR   OrthoDB; 757766at2759; -.
DR   Proteomes; UP000000599; Chromosome E.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0019236; P:response to pheromone; IEA:UniProtKB-KW.
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..1079
FT                   /note="Serine/threonine-protein kinase STE20"
FT                   /id="PRO_0000237629"
FT   DOMAIN          422..435
FT                   /note="CRIB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT   DOMAIN          801..1053
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          21..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          79..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          148..220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          261..323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          339..389
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          501..766
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..36
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        164..208
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        501..562
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        564..592
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        593..709
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        731..757
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        921
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         807..815
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         831
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   1079 AA;  119392 MW;  EF484D1A4C577D4A CRC64;
     MYKAKDTEYK LGSPIHEKIP SFEIGSDRRL DIDDNEGEEV SARDEHDDDE DYEYKRIIEE
     EFENDREFKD EHGFEIGVVD NDENNDQDCE ADTSKSIGSL PRMPGTYDFS GLKSDDNQYN
     ELTETLNQDD GNQSNDIAVG KLGDEASHTY KSTLDPGKPL QNPPPSNLNI DSILKSQLEN
     NKSEGSIGQR IDSISRKTTN SSGGPNIMKD NTLDRIPTHD YENIDDNNVF NRAGDPKIRG
     GLNASNDASI NDNIADISQS TIQTSTDAGE SINKGNGDIT KGLSNVDVND TSVNKSKQRN
     ISSGSVIRNP PSASQANQSN QSYHQTRAIT PVMNQMNKFQ GSNSEASSPR EHLGMGINNS
     APSTGANSNT SSPMNGSYPN SIAKSRRSGN RVKGVFSNMF SKNKTSTSVT SSPETHAINM
     KISTPFNAKH VAHVGVDDNG SYTGLPIEWE RLLSASGISK KEQQQHPQAV MDIVAFYQDT
     NDDNPDENAF KKFHYDNDSS HSSIYNATPP STPGIPSTYN ATPLQSEKQL QRQQSQKSQS
     SHPVQVQSTP KTPNNNYENQ FIPSRPAPKP PSSSIPSTKT IKPPPVPPSP STNTNISPAS
     KKNSFMGRSF SSKSIKALRN SNRKISEPPK APQSKISDSN TEMGIPKSKS HSNSLSTQSE
     VEPTKGSTTA PVSSTAKFNS TTINNINGHN IIEEEKNNNT LLSNPKQREQ KPDSTIEKRD
     TPPSPSQSRV SEEESTKKET SEKYNNKEND IPKKSSQQPV RDAKQAALLA QKKREDKKRK
     NQQIISKLQQ ICSEGDPNEL YKDLMKIGQG ASGGVYIAHD VNHRSQTVAI KQMNLEQQPK
     KELIINEILV MKGSKHENIV NFIDSYLLRG DLWVVMEYME GGSLTEIVTH SVMTEGQIGA
     VCRETLKGLR FLHSKGVIHR DIKSDNILLN IDGNIKMTDF GFCAQINEIN LKRTTMVGTP
     YWMAPEVVSR KEYGPKVDVW SLGIMIIEMI EGEPPYLNET PLRALYLIAT NGTPKLKEPE
     ALSYDIRKFL SWCLQVDFNK RGNADQLLND KFILEADDVE SLSPLVKIAA MKKATELDE