ID B8QN51_MAIZE Unreviewed; 397 AA.
AC B8QN51;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=Mitogen-activated protein kinase {ECO:0000256|RuleBase:RU361165};
DE EC=2.7.11.24 {ECO:0000256|RuleBase:RU361165};
GN Name=MPK7 {ECO:0000313|EMBL:ACF35309.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:ACF35309.1};
RN [1] {ECO:0000313|EMBL:ACF35309.1}
RP NUCLEOTIDE SEQUENCE.
RA Wang J., Jiang M., Ding H.;
RT "Abscisic Acid Activates Mitogen-Activated Protein Kinase in Maize.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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:0000256|RuleBase:RU361165};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU361165};
CC -!- ACTIVITY REGULATION: Activated by threonine and tyrosine
CC phosphorylation. {ECO:0000256|RuleBase:RU361165}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. MAP kinase subfamily.
CC {ECO:0000256|ARBA:ARBA00008832}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. MAP kinase subfamily. {ECO:0000256|RuleBase:RU361165}.
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; EU616650; ACF35309.1; -; mRNA.
DR RefSeq; NP_001152745.1; NM_001159273.1.
DR AlphaFoldDB; B8QN51; -.
DR GeneID; 100286386; -.
DR KEGG; zma:100286386; -.
DR OrthoDB; 5474493at2759; -.
DR ExpressionAtlas; B8QN51; baseline and differential.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004707; F:MAP kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd07858; STKc_TEY_MAPK; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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 PANTHER; PTHR24055; MITOGEN-ACTIVATED PROTEIN KINASE; 1.
DR PANTHER; PTHR24055:SF553; MITOGEN-ACTIVATED PROTEIN KINASE 10; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU361165};
KW Magnesium {ECO:0000256|RuleBase:RU361165};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU000304};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361165}.
FT DOMAIN 66..351
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 397 AA; 44935 MW; 3F9E9A3F2F452998 CRC64;
MDGGGQPPDT EMTDAGAGGG GQPSPPQQPA SGAGMMENIH ATLSHGGRFI QYNIFGNVFE
VTSKYKPPIL PIGKGAYGIV CSALNSETAE QVAIKKIANA FDNKIDAKRT LREIKLLRHM
DHENIVAIRD IIPPPLREAF NDVYIAYELM DTDLHQIIRS NQALSEEHCQ YFLYQILRGL
KYIHSANVLH RDLKPSNLLL NANCDLKICD FGLARTTSET DFMTEYVVTR WYRAPELLLN
SSEYTAAIDV WSVGCIFMEL MDRKPLFPGR DHVHQLRLLM ELIGTPNEAD LDFVNENARR
YIRQLPCHAR QSFPEKFPHV QPLAIDLVEK MLTFDPRQRI TVEGALAHPY LASLHDISDE
PVCSMPFSFD FEQHALSEEQ MKDLIYQEAL AFNPDYQ
//
