MKK2_MAGO7
ID MKK2_MAGO7 Reviewed; 527 AA.
AC G4N6Z6; G4N6Z7;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Mitogen-activated protein kinase kinae MKK2 {ECO:0000303|PubMed:28244240};
DE Short=MAPKK MKK2 {ECO:0000303|PubMed:28244240};
DE EC=2.7.11.24 {ECO:0000305|PubMed:28244240};
DE AltName: Full=MEK MKK2 {ECO:0000303|PubMed:28244240};
GN Name=MKK2 {ECO:0000303|PubMed:28244240}; ORFNames=MGG_06482;
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, AND INTERACTION WITH MTS50.
RX PubMed=28244240; DOI=10.1111/1462-2920.13710;
RA Li G., Zhang X., Tian H., Choi Y.E., Tao W.A., Xu J.R.;
RT "MST50 is involved in multiple MAP kinase signaling pathways in Magnaporthe
RT oryzae.";
RL Environ. Microbiol. 19:1959-1974(2017).
RN [3]
RP FUNCTION.
RX PubMed=28799700; DOI=10.1111/1462-2920.13884;
RA Zhang X., Liu W., Li Y., Li G., Xu J.R.;
RT "Expression of HopAI interferes with MAP kinase signalling in Magnaporthe
RT oryzae.";
RL Environ. Microbiol. 19:4190-4204(2017).
CC -!- FUNCTION: Mitogen-activated protein kinase kinase; part of the MCK1-
CC MKK2-MPS1 MAP kinase (MAPK) signal transduction cascade that is
CC essential for appressorium formation, penetration and invasive growth
CC (PubMed:28244240). Beside its role in pathogenesis, the MPS1 cascade is
CC active in conidiation and cellular stress responses (By similarity).
CC Targets downstream of the the MPS1-MAPK pathway include transcription
CC factors MIG1 and SWI6, as well as GSK1 and MPG1 (PubMed:28244240).
CC {ECO:0000250|UniProtKB:G4N0Z0, ECO:0000269|PubMed:28244240}.
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:28244240};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000305|PubMed:28244240};
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:28244240};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC Evidence={ECO:0000305|PubMed:28244240};
CC -!- SUBUNIT: Interacts with the adapter protein MST50.
CC {ECO:0000269|PubMed:28244240}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EHA50760.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CM001234; EHA50760.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CM001234; EHA50761.1; -; Genomic_DNA.
DR RefSeq; XP_003717079.1; XM_003717031.1.
DR RefSeq; XP_003717080.1; XM_003717032.1.
DR AlphaFoldDB; G4N6Z6; -.
DR SMR; G4N6Z6; -.
DR STRING; 318829.MGG_06482T0; -.
DR EnsemblFungi; MGG_06482T0; MGG_06482T0; MGG_06482.
DR EnsemblFungi; MGG_06482T1; MGG_06482T1; MGG_06482.
DR GeneID; 2684637; -.
DR KEGG; mgr:MGG_06482; -.
DR VEuPathDB; FungiDB:MGG_06482; -.
DR eggNOG; KOG0581; Eukaryota.
DR HOGENOM; CLU_000288_63_23_1; -.
DR InParanoid; G4N6Z6; -.
DR OrthoDB; 688282at2759; -.
DR Proteomes; UP000009058; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IEA:EnsemblFungi.
DR GO; GO:0000935; C:division septum; IEA:EnsemblFungi.
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:0000196; P:cell wall integrity MAPK cascade; IEA:EnsemblFungi.
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:0050850; P:positive regulation of calcium-mediated signaling; IEA:EnsemblFungi.
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; Transferase;
KW Virulence.
FT CHAIN 1..527
FT /note="Mitogen-activated protein kinase kinae MKK2"
FT /id="PRO_0000453096"
FT DOMAIN 227..497
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 233..241
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 256
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 527 AA; 56415 MW; 2D9BFB513DDD9C39 CRC64;
MHDQEAANGG ETATNPISSL DVPTPPATTI PTLSSPAPLL RPAIPGARSA GARTPRLGLA
IPPSPNVKPV GGAPGRPPLP TLHLATPMGS SVTPHEQPPG RPSIVTQQGQ SASGGSESSA
AHSRSGSFGP LDGRTSNPTS AGSQYSALSF ASHFGIGSTR PQGTPDPASA VGSIYSERSD
GGAGMDKDGN LKGLENFDKL TIDKARTADV EDLDVEGWKI ASMEKRIVEL GGLGEGAGGA
VTRCKLTGGK TVFALKVITA NPDPDVKKQI MRELDFNIQC ASEHICRYYG AFEDPSTATI
SIAMEFCEGG SLDSIYKEVK RLGGRTGEKV LGKIAEGVLR GLTYLNSKKI IHRDIKPSNI
LLCRNGDVKL CDFGVSGDFG TKGEANTFIG TSYYMAPERI TGQSYTITSD VWSTGVTLLE
VAQHRFPFPA DGTEMAPRAG LIDLLTYIVR QPIPKLKDEP SAQISWSENF KYFIECCLEK
DPQRRASPWR MLEHPWMVDM KSKRVNMTRY LAQVWGWDDK GEAKPAE
