ID   STE20_KLULA             Reviewed;         989 AA.
AC   Q6CVA2;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Serine/threonine-protein kinase STE20;
DE            EC=2.7.11.1;
GN   Name=STE20; OrderedLocusNames=KLLA0B13607g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382122; CAH02530.1; -; Genomic_DNA.
DR   RefSeq; XP_452137.1; XM_452137.1.
DR   AlphaFoldDB; Q6CVA2; -.
DR   SMR; Q6CVA2; -.
DR   STRING; 28985.XP_452137.1; -.
DR   PRIDE; Q6CVA2; -.
DR   EnsemblFungi; CAH02530; CAH02530; KLLA0_B13607g.
DR   GeneID; 2897018; -.
DR   KEGG; kla:KLLA0_B13607g; -.
DR   eggNOG; KOG0578; Eukaryota.
DR   HOGENOM; CLU_000288_26_3_1; -.
DR   InParanoid; Q6CVA2; -.
DR   OMA; AYADPPK; -.
DR   Proteomes; UP000000598; Chromosome B.
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: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: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; 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..989
FT                   /note="Serine/threonine-protein kinase STE20"
FT                   /id="PRO_0000237631"
FT   DOMAIN          404..417
FT                   /note="CRIB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT   DOMAIN          698..949
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          265..400
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          567..588
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          620..681
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..38
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..74
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        275..295
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        306..360
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        574..588
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        621..635
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        664..681
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        817
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         704..712
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         727
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   989 AA;  108623 MW;  47CD34A2B4A6AF37 CRC64;
     MTDTGYTEEL LPGTFDALSV RENGGNTESD TSSIRKSQNQ DSKQEDVHRE NLSVQTLEDH
     TEVTETREQS VSKDLFDLPR APASLDVKGL QESDEDHYVK DLSDYKSMDP GKPGTVPTNV
     SEIFNSNQPT LDEPIQFTRV SSSSVLSESI SEGDADLISH LEGKVEEGNN LTSKETPGTI
     ESIVGDKTMS TIEGSSQNIG RISTGGRMTP DLSLMGGALE TSSDFLNSTQ TSNSPKITTP
     ITEVDANDVY ESPLNEILSS TDSFNKASTA SADHSKHVSV HEVIPEEEPH PETTNEDPPI
     KTPVMVNNFF ENQTPVSESR SPFRTISSPF SSLRKNVKSQ HGTPDHSQRN SNSSTSSNDV
     KRKTGTKKKG VFSTFVQNIK RNSHSEKRIS SGSGNGSGNN AFKISTPYNA KHVYHVGVDS
     KTGEYTGLPN EWEKLLTSSG ISMKEQQQHP QAVMDIVKFY QDVTENSGEE KVFKTFKVGG
     GSGANIASTP SFRTPSTASV QKFETPQMQT DATFPNENND TPYSSNLQGP LLTNDFSETV
     NNEKFIPTRP APKPQGSSTV SRRVEIPSPI NSLGHGTPKV QRSDTQSSSI FSFKKMPTLK
     SEQPLPPIPK AAEKPANLLP ARAAPTPPKP AIPTTPEQSS IPAIPSGLAV EVKEESNTSN
     VQTRKAQEKK REERKRKNQQ IQSKLTEICT TGDPSKLYKN LIKIGQGASG GVYTAYELGT
     NASVAIKQMN LEKQPKKELI VNEILVMKGS KHNNIVNFID SYLFRGDLWV VMEYMEGGSL
     TDVVTHCILT EGQIGAVSRE TLKGLQFLHS KGVIHRDIKS DNILLSMNGD IKLTDFGFCA
     QINEVNLKRT TMVGTPYWMA PEVVSRKEYG PKVDIWSLGI MIIEMIEGEP PYLNETPLRA
     LYLIATNGTP KLKDPGNLSH KMAMFLNWCL MVDPEDRGTA ADLLEDPFIT EIAEENTSLA
     PLVKLARMKK LAESMEDDEN DEDKYDEQS