MST7_MAGO7
ID MST7_MAGO7 Reviewed; 415 AA.
AC G4NEB8;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Mitogen-activated protein kinase kinae MST7 {ECO:0000303|PubMed:15749760};
DE Short=MAPKK MST7 {ECO:0000303|PubMed:15749760};
DE EC=2.7.11.24 {ECO:0000269|PubMed:15749760};
DE AltName: Full=MEK MST7 {ECO:0000303|PubMed:15749760};
GN Name=MST7 {ECO:0000303|PubMed:15749760}; ORFNames=MGG_00800;
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, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, MUTAGENESIS OF SER-212
RP AND THR-216, 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).
RN [5]
RP FUNCTION, INTERACTION WITH TRX2, SUBUNIT, AND MUTAGENESIS OF CYS-114;
RP CYS-136; CYS-201 AND CYS-305.
RX PubMed=27059015; DOI=10.1111/1462-2920.13315;
RA Zhang S., Jiang C., Zhang Q., Qi L., Li C., Xu J.R.;
RT "Thioredoxins are involved in the activation of the PMK1 MAP kinase pathway
RT during appressorium penetration and invasive growth in Magnaporthe
RT oryzae.";
RL Environ. Microbiol. 18:3768-3784(2016).
CC -!- FUNCTION: Mitogen-activated protein kinase kinase; part of the MST11-
CC MST7-PMK1 MAP kinase (MAPK) cascade that is essential for appressorium
CC formation, penetration and invasive growth (PubMed:15749760,
CC PubMed:21283781, PubMed:23454094, PubMed:27059015). The MST11-MST7-PMK1
CC MAP kinase cascade transduces signals from the cell surface sensors
CC MDB2 and SHO1 that recognize various surface signals such as surface
CC hydrophobicity, cutin monomers, and rice leaf waxes (PubMed:21283781).
CC MST7 acts as the upstream MAPKK that directly phosphorylates MAP kinase
CC PMK1 (PubMed:15749760). {ECO:0000269|PubMed:15749760,
CC ECO:0000269|PubMed:21283781, ECO:0000269|PubMed:23454094,
CC ECO:0000269|PubMed:27059015}.
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:0000269|PubMed:15749760};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000269|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:0000269|PubMed:15749760};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC Evidence={ECO:0000269|PubMed:15749760};
CC -!- SUBUNIT: Homodimer (PubMed:27059015). Interacts with the adapter
CC protein MST50 (PubMed:15749760). Interacts with TRX2 (PubMed:27059015).
CC {ECO:0000269|PubMed:15749760, ECO:0000269|PubMed:27059015}.
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 subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM001235; EHA48601.1; -; Genomic_DNA.
DR RefSeq; XP_003718185.1; XM_003718137.1.
DR AlphaFoldDB; G4NEB8; -.
DR SMR; G4NEB8; -.
DR STRING; 318829.MGG_00800T0; -.
DR EnsemblFungi; MGG_00800T0; MGG_00800T0; MGG_00800.
DR GeneID; 2675190; -.
DR KEGG; mgr:MGG_00800; -.
DR VEuPathDB; FungiDB:MGG_00800; -.
DR eggNOG; KOG0581; Eukaryota.
DR HOGENOM; CLU_000288_63_23_1; -.
DR InParanoid; G4NEB8; -.
DR OMA; LEAWAVS; -.
DR OrthoDB; 688282at2759; -.
DR PHI-base; PHI:2120; -.
DR PHI-base; PHI:417; -.
DR Proteomes; UP000009058; Chromosome 5.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004707; F:MAP kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004708; F:MAP kinase kinase activity; IDA:GO_Central.
DR GO; GO:0000165; P:MAPK cascade; IDA:GO_Central.
DR GO; GO:0075018; P:positive regulation of appressorium formation; IMP:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 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.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Virulence.
FT CHAIN 1..415
FT /note="Mitogen-activated protein kinase kinae MST7"
FT /id="PRO_0000453095"
FT DOMAIN 61..326
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 67..75
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 90
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 114
FT /note="C->A: Does not affect appressorium formation and
FT plant infection."
FT /evidence="ECO:0000269|PubMed:27059015"
FT MUTAGEN 136
FT /note="C->A: Does not affect appressorium formation and
FT plant infection."
FT /evidence="ECO:0000269|PubMed:27059015"
FT MUTAGEN 201
FT /note="C->A: Does not affect appressorium formation and
FT plant infection."
FT /evidence="ECO:0000269|PubMed:27059015"
FT MUTAGEN 212
FT /note="S->D: Leads to constitutive activity; when
FT associated with Glu-216."
FT /evidence="ECO:0000269|PubMed:15749760"
FT MUTAGEN 216
FT /note="T->E: Leads to constitutive activity; when
FT associated with Asp-212."
FT /evidence="ECO:0000269|PubMed:15749760"
FT MUTAGEN 305
FT /note="C->A: Impairs appressorium formation and
FT pathogenicity."
FT /evidence="ECO:0000269|PubMed:27059015"
SQ SEQUENCE 415 AA; 46171 MW; F9036A416DB661EB CRC64;
MADPFAPRTM KRRNVKGLAL TPAAPKPPPT AENAPIHRDS DQHAQLEIGI EFNLDLRPED
LEVIKDLGSG NGGTVSKVRH IPTNTVMARK VIHVEAKREM RKRIVRELQI MHSCNSEYIV
TFYGAFLNEN NDVIMCMEYA DVGSLDRVSR VFGPIRVDVL GKIAEATLGG LTYLYAKHHI
MHRDIKPSNI LVNSRGSIKL CDFGVSGELI NSIADTFVGT STYMAPERIQ GEKYTVKSDV
WSFGLSIMEL AIGKFPFAAS EQLSDAESAP AGILDLLQQI VHEPAPKLPK SDAFPQILED
MIQKCLYKNP DDRPTPEELF ERDPFVQAAK RTPVDLREWA FGLMERDNRK SHLAPQLSPA
TADLLRSSDS PTATYHGDDR PLETPTSAYR VDPRRGPAEG SAGLADQVDR LYIRD
