MST11_MAGO7
ID MST11_MAGO7 Reviewed; 915 AA.
AC G4N7X0;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Mitogen-activated protein kinase kinae kinase MST11 {ECO:0000303|PubMed:15749760};
DE Short=MAPKKK MST11 {ECO:0000303|PubMed:15749760};
DE EC=2.7.11.24 {ECO:0000305|PubMed:15749760};
DE AltName: Full=MEKK MST11 {ECO:0000303|PubMed:15749760};
GN Name=MST11 {ECO:0000303|PubMed:15749760}; ORFNames=MGG_14847;
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 [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).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, DOMAIN, AND INTERACTION WITH MST50.
RX PubMed=15749760; DOI=10.1105/tpc.104.029116;
RA Zhao X., Kim Y., Park G., Xu J.R.;
RT "A mitogen-activated protein kinase cascade regulating infection-related
RT morphogenesis in Magnaporthe grisea.";
RL Plant Cell 17:1317-1329(2005).
RN [3]
RP FUNCTION.
RX PubMed=21283781; DOI=10.1371/journal.ppat.1001261;
RA Liu W., Zhou X., Li G., Li L., Kong L., Wang C., Zhang H., Xu J.R.;
RT "Multiple plant surface signals are sensed by different mechanisms in the
RT rice blast fungus for appressorium formation.";
RL PLoS Pathog. 7:e1001261-e1001261(2011).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23454094; DOI=10.1016/j.gep.2013.02.003;
RA Jin Q., Li C., Li Y., Shang J., Li D., Chen B., Dong H.;
RT "Complexity of roles and regulation of the PMK1-MAPK pathway in mycelium
RT development, conidiation and appressorium formation in Magnaporthe
RT oryzae.";
RL Gene Expr. Patterns 13:133-141(2013).
CC -!- FUNCTION: Mitogen-activated protein kinase kinase kinase; part of the
CC MST11-MST7-PMK1 MAP kinase (MAPK) cascade that is essential for
CC appressorium formation, penetration and invasive growth
CC (PubMed:15749760, PubMed:23454094). The MST11-MST7-PMK1 MAP kinase
CC cascade transduces signals from the cell surface sensors MDB2 and SHO1
CC that recognize various surface signals such as surface hydrophobicity,
CC cutin monomers, and rice leaf waxes (PubMed:21283781). MST11 acts as
CC the upstream MAPKKK that directly phosphorylates MAPKK MST7 (Probable).
CC MST11 but not MST7 may also be involved in the OSM1 MAPK pathway in
CC response to osmotic stresses (PubMed:15749760).
CC {ECO:0000269|PubMed:15749760, ECO:0000269|PubMed:21283781,
CC ECO:0000269|PubMed:23454094, ECO:0000305|PubMed:15749760}.
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=2.7.11.24;
CC Evidence={ECO:0000305|PubMed:15749760};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000305|PubMed:15749760};
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=2.7.11.24; Evidence={ECO:0000305|PubMed:15749760};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC Evidence={ECO:0000305|PubMed:15749760};
CC -!- SUBUNIT: Interacts with the adapter protein MST50.
CC {ECO:0000269|PubMed:15749760}.
CC -!- DOMAIN: The N-terminal sterile alpha motif (SAM) domain, but not the
CC Ras-associating (RA) domain, is essential for the function.
CC {ECO:0000269|PubMed:15749760}.
CC -!- DISRUPTION PHENOTYPE: Produces much less aerial hyphae and conidia and
CC shows weakened cell walls and higher sensitivity to cell wall-degrading
CC enzymes (PubMed:15749760). Impairs the formation of appressoria and the
CC ability to infect rice plants (PubMed:15749760, PubMed:23454094).
CC {ECO:0000269|PubMed:15749760, ECO:0000269|PubMed:23454094}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase kinase subfamily.
CC {ECO:0000305}.
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DR EMBL; CM001234; EHA50924.1; -; Genomic_DNA.
DR RefSeq; XP_003717243.1; XM_003717195.1.
DR AlphaFoldDB; G4N7X0; -.
DR SMR; G4N7X0; -.
DR STRING; 318829.MGG_14847T0; -.
DR EnsemblFungi; MGG_14847T0; MGG_14847T0; MGG_14847.
DR GeneID; 5048863; -.
DR KEGG; mgr:MGG_14847; -.
DR VEuPathDB; FungiDB:MGG_14847; -.
DR eggNOG; KOG0198; Eukaryota.
DR HOGENOM; CLU_003051_0_1_1; -.
DR InParanoid; G4N7X0; -.
DR OMA; FIGAHPF; -.
DR OrthoDB; 1290401at2759; -.
DR PHI-base; PHI:2119; -.
DR PHI-base; PHI:418; -.
DR PHI-base; PHI:8262; -.
DR Proteomes; UP000009058; Chromosome 4.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004707; F:MAP kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0051094; P:positive regulation of developmental process; IEA:UniProt.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 1.10.150.50; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR029458; Ras-bd_By2.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF14847; Ras_bdg_2; 1.
DR Pfam; PF07647; SAM_2; 1.
DR SMART; SM01304; Ras_bdg_2; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50200; RA; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase;
KW Virulence.
FT CHAIN 1..915
FT /note="Mitogen-activated protein kinase kinae kinase MST11"
FT /id="PRO_0000453097"
FT DOMAIN 65..128
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 263..353
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT DOMAIN 641..911
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 647..655
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 670
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 915 AA; 101021 MW; D5D67F423E255DB2 CRC64;
MAMLASKSPF PAPLATSGSG MMAGTAQASY PPSRRAPAVP PASQSFSPTE SEFSDSDDHD
SPKHWDEDKV CEYLRSVRCG EYEKLFRKNH INGENLLEMD KDVLKEMGIE KVGDRVRLFL
SIKKLRTKAI AGQKKRNRDS FAGHESMYTP VSESPSKPFH SSSRVMPNPS VNKRYSRQID
LSGMAYDPSR PTTSSRPTSP LPSADFRTAR TRNPYVGQQP TPTGSLRGLG SPPDSQANSR
PVLTHTRTDS GMDGSLMAAL PQNQDVIRVI STGGVTKVVK IADCNTCEEV MRVTLRKFAL
REDHERNYCF WVLSGLDPDP KQCRRLGDTE LWRVIKDQKR PERNRLILRR VPAGEPGQSE
LERAAAIAME EAQQSHSRAM DNVGARSQIK VQKVLGENWD NLQPPLSPVL YQDRERNVYN
AARDLERPEP LDSGRLQPRR KVLRSFGGLR PPSELIASDL TTYFPDHPRE DIDRTARLSM
RRSARLSKVN SRLSVASSFS MASSIQDAPP IPTIADSWLQ STPLPKARPR DLQSRLQHGY
RDSVASSMLD TLQEEGSPIE PNRKSYVSFA DSGSDSAAVS VTDPDGNIVR HSYFDEGSTI
GSGSGSGSFG DVSKALNEDG EDADEDLQSF LSGESWDDSK WMKGALIGQG SFGCVYLALH
AITGELLAVK QVEAPSPGAN SQNDARKKSM IEALKREISL LRDLRHPNIV QYLGCGSSAE
YLNIFLEYVP GGSVQTMLNS YGALPEPLVR SFVRQILNGL SYLHEREIIH RDIKGANILV
DNKGTIKISD FGISKKIEAT NLLNGANNNK HRPSLQGSVF WMAPEVVKQT SYTRKADIWS
LGCLVVEMMT GTHPFPDCTQ LQAIFKIGGG KATPTIPEDA STEAKAFLAQ TFEMDHNKRP
SADDLMLSPF LTPIT
