ID   STE20_MAGO7             Reviewed;         914 AA.
AC   Q7Z8E9; A4R8E8; G4N6Y2;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-JAN-2012, sequence version 3.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Serine/threonine-protein kinase MST20;
DE            EC=2.7.11.1;
GN   Name=MST20; Synonyms=STE20; ORFNames=MGG_12821;
OS   Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Pyricularia oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=242507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=Guyane 11;
RX   PubMed=15141959; DOI=10.1094/mpmi.2004.17.5.547;
RA   Li L., Xue C., Bruno K., Nishimura M., Xu J.-R.;
RT   "Two PAK kinase genes, CHM1 and MST20, have distinct functions in
RT   Magnaporthe grisea.";
RL   Mol. Plant Microbe Interact. 17:547-556(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX   PubMed=15846337; DOI=10.1038/nature03449;
RA   Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA   Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA   Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA   Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA   Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA   Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL   Nature 434:980-986(2005).
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). Is
CC       involved in conidiation, aerial hyphal growth and infection-related
CC       morphogenesis. {ECO:0000250, ECO:0000269|PubMed:15141959}.
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; AY332225; AAP93639.1; -; Genomic_DNA.
DR   EMBL; CM001234; EHA50746.1; -; Genomic_DNA.
DR   RefSeq; XP_003717065.1; XM_003717017.1.
DR   AlphaFoldDB; Q7Z8E9; -.
DR   SMR; Q7Z8E9; -.
DR   STRING; 318829.MGG_12821T0; -.
DR   EnsemblFungi; MGG_12821T0; MGG_12821T0; MGG_12821.
DR   GeneID; 5050191; -.
DR   KEGG; mgr:MGG_12821; -.
DR   VEuPathDB; FungiDB:MGG_12821; -.
DR   eggNOG; KOG0578; Eukaryota.
DR   HOGENOM; CLU_000288_26_1_1; -.
DR   InParanoid; Q7Z8E9; -.
DR   OMA; PKEWQRM; -.
DR   OrthoDB; 757766at2759; -.
DR   PHI-base; PHI:518; -.
DR   Proteomes; UP000009058; Chromosome 4.
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:0051094; P:positive regulation of developmental process; IEA:UniProt.
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..914
FT                   /note="Serine/threonine-protein kinase MST20"
FT                   /id="PRO_0000237633"
FT   DOMAIN          306..319
FT                   /note="CRIB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT   DOMAIN          634..885
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..140
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          156..184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          251..286
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          408..615
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..34
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..105
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        270..284
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        509..597
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        753
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         640..648
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         663
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   VARIANT         253
FT                   /note="S -> R (in strain: Guyane 11)"
SQ   SEQUENCE   914 AA;  100249 MW;  B3B7BD5763E4D523 CRC64;
     MDGHSNFTQP SDTSHASHTI PSSSSSQRRR LTKKPPPSTS ARHHHSSLSI DSRVDAQSLV
     GKRSSTSLRR APSAPPARTP TSTHASNSSS PRNPSSSTRL NNHSPIIPAA SEFAASSLSP
     SARDRDSDPA RNDHGHQLQN NNNYYYSAFT NAHHHNQYSA ASHRRSNSYG HPHGPQSSNS
     LTFNHSEDFI GAPFDGSAIL NRIEATKASP TLGSGAFPHI SNPIPVGAAA PAQYSRGSPA
     LEQSFTFPSA AMSEKSQQVR GMEAQLPTSK RYSDETKEPK PGVLRKKSGF SGFMSGLVGT
     PKKPLISAPE NPVHVTHVGY DSATGQFTGL PKEWQRLISE SGITEKERRE NPETLVNVIK
     FYKETTEKPA EDQVLEKFHD ARPGLPSAPS AGSMISPGLA PHHYNPMSPM ISPPASPRFP
     QVGHEGNFEN PRSPPPVPKN KDVTLMPSRP APRPPVSLPT RTAPHAPYAA KDSGIDMPPQ
     HDDLTPTTYQ PPKESQPILP EEHRSRSNSR VNGNTAYPAS QQSPAVQAAY QQQLMQQQQE
     QALAQAQASM SGSMSRAPSK RQPQAQQPTP PQSQHQYSRP TDANGAQQTQ RPQQPQIGPV
     PQSRPRHRSR QSNGLDVVAA LKRICSEGDP REIYRSFTKI GQGASGGVYT GHERGSNRLV
     AIKQMNLEQQ PKKDLIINEI LVMKDSSHPN IVNFIDSYLC GGELWVVMEF MEGGSLTDVV
     TFNIMTEGQI ASVCRETLLG LQHLHSKGVI HRDIKSDNIL LSMEGNIKLT DFGFCATINE
     AQNKRTTMVG TPYWMAPEVV TRKEYGRKVD IWSLGIMAIE MIEGEPPYLT ESPLRALWLI
     ATNGTPQIKD EGNMSPVFRD FLYFALKVDP DKRASAHDLL RHEFMNLCVD LSHLSPLVRA
     AREARAQEKA RKGQ