PMK1_MAGO7
ID PMK1_MAGO7 Reviewed; 356 AA.
AC G4N0Z0;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Mitogen-activated protein kinase PMK11 {ECO:0000303|PubMed:8946911};
DE Short=MAPK PMK1 {ECO:0000303|PubMed:8946911};
DE EC=2.7.11.24 {ECO:0000269|PubMed:8946911};
GN Name=PMK1 {ECO:0000303|PubMed:8946911}; ORFNames=MGG_09565;
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, AND DISRUPTION PHENOTYPE.
RX PubMed=8946911; DOI=10.1101/gad.10.21.2696;
RA Xu J.R., Hamer J.E.;
RT "MAP kinase and cAMP signaling regulate infection structure formation and
RT pathogenic growth in the rice blast fungus Magnaporthe grisea.";
RL Genes Dev. 10:2696-2706(1996).
RN [3]
RP FUNCTION.
RX PubMed=11952120; DOI=10.1094/mpmi.2002.15.3.183;
RA Park G., Xue C., Zheng L., Lam S., Xu J.R.;
RT "MST12 regulates infectious growth but not appressorium formation in the
RT rice blast fungus Magnaporthe grisea.";
RL Mol. Plant Microbe Interact. 15:183-192(2002).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12215509; DOI=10.1105/tpc.003426;
RA Xue C., Park G., Choi W., Zheng L., Dean R.A., Xu J.R.;
RT "Two novel fungal virulence genes specifically expressed in appressoria of
RT the rice blast fungus.";
RL Plant Cell 14:2107-2119(2002).
RN [5]
RP FUNCTION, AND PHOSPHORYLATION.
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 [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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 [7]
RP REVIEW ON FUNCTION.
RX PubMed=23085322; DOI=10.1016/j.mib.2012.09.004;
RA Li G., Zhou X., Xu J.R.;
RT "Genetic control of infection-related development in Magnaporthe oryzae.";
RL Curr. Opin. Microbiol. 15:678-684(2012).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23591122; DOI=10.1016/j.fgb.2013.03.006;
RA Kong L.A., Li G.T., Liu Y., Liu M.G., Zhang S.J., Yang J., Zhou X.Y.,
RA Peng Y.L., Xu J.R.;
RT "Differences between appressoria formed by germ tubes and appressorium-like
RT structures developed by hyphal tips in Magnaporthe oryzae.";
RL Fungal Genet. Biol. 56:33-41(2013).
RN [9]
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 [10]
RP FUNCTION.
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).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=29567712; DOI=10.1126/science.aaq0892;
RA Sakulkoo W., Oses-Ruiz M., Oliveira Garcia E., Soanes D.M.,
RA Littlejohn G.R., Hacker C., Correia A., Valent B., Talbot N.J.;
RT "A single fungal MAP kinase controls plant cell-to-cell invasion by the
RT rice blast fungus.";
RL Science 359:1399-1403(2018).
CC -!- FUNCTION: Mitogen-activated protein kinase; part of the MST11-MST7-PMK1
CC MAP kinase (MAPK) cascade that is essential for appressorium formation,
CC penetration and invasive growth (PubMed:8946911, PubMed:11952120,
CC PubMed:15749760, PubMed:21283781, PubMed:23085322, PubMed:23454094,
CC PubMed:27059015). Central regulator of appressorium development that
CC acts downstream of the cAMP signal (PubMed:8946911, PubMed:23591122).
CC The MST11-MST7-PMK1 MAP kinase cascade transduces signals from the cell
CC surface sensors MDB2 and SHO1 that recognize various surface signals
CC such as surface hydrophobicity, cutin monomers, and rice leaf waxes
CC (PubMed:21283781). Regulates expression of secreted fungal effector
CC proteins implicated of host immune defenses, preventing reactive oxygen
CC species generation and excessive callose deposition at plasmodesmata
CC (PubMed:29567712). Furthermore, controls the hyphal constriction
CC required for fungal growth from one rice cell to the neighboring cell,
CC enabling host tissue colonization and blast disease (PubMed:29567712).
CC Targets downstream of the PMK1-MAPK pathway include transcription
CC factor MST12 and pathogenicity-related genes GAS1 and GAS2, both of
CC which are expressed during appressorium formation, even if regulation
CC of MST12 is not associated with expression of GAS1 or GAS2
CC (PubMed:12215509, PubMed:11952120, PubMed:23454094).
CC {ECO:0000269|PubMed:11952120, ECO:0000269|PubMed:12215509,
CC ECO:0000269|PubMed:15749760, ECO:0000269|PubMed:21283781,
CC ECO:0000269|PubMed:23085322, ECO:0000269|PubMed:23454094,
CC ECO:0000269|PubMed:23591122, ECO:0000269|PubMed:27059015,
CC ECO:0000269|PubMed:29567712, ECO:0000269|PubMed:8946911}.
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:8946911};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000269|PubMed:8946911};
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:8946911};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC Evidence={ECO:0000269|PubMed:8946911};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|RuleBase:RU361165};
CC -!- PTM: Phosphorylated by MST7. {ECO:0000269|PubMed:15749760}.
CC -!- DISRUPTION PHENOTYPE: Impairs the formation of appressoria and the
CC ability to infect rice plants, even when inoculated onto wounded leaves
CC (PubMed:8946911, PubMed:23591122, PubMed:23454094). Leads to decreased
CC transcription of the cell surface sensors MSB2 and SHO1
CC (PubMed:21283781). Blocks the transcription of both virulence genes
CC GAS1 and GAS2 during appressorium formation (PubMed:12215509).
CC {ECO:0000269|PubMed:12215509, ECO:0000269|PubMed:21283781,
CC ECO:0000269|PubMed:23454094, ECO:0000269|PubMed:23591122,
CC ECO:0000269|PubMed:8946911}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. MAP kinase subfamily. {ECO:0000305}.
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DR EMBL; CM001233; EHA52368.1; -; Genomic_DNA.
DR RefSeq; XP_003712175.1; XM_003712127.1.
DR AlphaFoldDB; G4N0Z0; -.
DR SMR; G4N0Z0; -.
DR STRING; 318829.MGG_09565T0; -.
DR EnsemblFungi; MGG_09565T0; MGG_09565T0; MGG_09565.
DR GeneID; 2680463; -.
DR KEGG; mgr:MGG_09565; -.
DR VEuPathDB; FungiDB:MGG_09565; -.
DR eggNOG; KOG0660; Eukaryota.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; G4N0Z0; -.
DR OMA; SFFDFDY; -.
DR OrthoDB; 741207at2759; -.
DR PHI-base; PHI:2163; -.
DR Proteomes; UP000009058; Chromosome 3.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004707; F:MAP kinase activity; IDA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0106259; P:cell-to-cell migration in host; IMP:PHI-base.
DR GO; GO:0030448; P:hyphal growth; IMP:PHI-base.
DR GO; GO:0000165; P:MAPK cascade; IDA:GO_Central.
DR GO; GO:0075018; P:positive regulation of appressorium formation; IDA:PHI-base.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0000921; P:septin ring assembly; IMP:PHI-base.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003527; MAP_kinase_CS.
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; PS01351; MAPK; 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; Magnesium; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Virulence.
FT CHAIN 1..356
FT /note="Mitogen-activated protein kinase PMK11"
FT /id="PRO_0000453091"
FT DOMAIN 24..312
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 30..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 356 AA; 41303 MW; 797412E03557B15F CRC64;
MSRANPPSNS SGSRKISFNV SEQYDIQDVV GEGAYGVVCS AIHKPSGQKV AIKKITPFDH
SMFCLRTLRE MKLLRYFNHE NIISILDIQK PRSYETFNEV YLIQELMETD MHRVIRTQDL
SDDHCQYFIY QTLRALKAMH SANVLHRDLK PSNLLLNANC DLKVCDFGLA RSAASQEDNS
GFMTEYVATR WYRAPEIMLT FKEYTKAIDV WSVGCILAEM LSGKPLFPGK DYHHQLTLIL
DVLGTPTMED YYGIKSRRAR EYIRSLPFKK KVPFRTLFPK TSDLALDLLE KLLAFNPVKR
ITVEEALKHP YLEPYHDPDD EPTAPPIPEE FFDFDKHKDN LSKEQLKQFI YQEIMR
