ID D1MFM1_MALDO Unreviewed; 394 AA. AC D1MFM1; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 07-APR-2021, entry version 59. DE RecName: Full=Mitogen-activated protein kinase {ECO:0000256|ARBA:ARBA00012411, ECO:0000256|RuleBase:RU361165}; DE EC=2.7.11.24 {ECO:0000256|ARBA:ARBA00012411, ECO:0000256|RuleBase:RU361165}; GN Name=MPK1 {ECO:0000313|EMBL:ACY82513.1}; OS Malus domestica (Apple) (Pyrus malus). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus. OX NCBI_TaxID=3750 {ECO:0000313|EMBL:ACY82513.1}; RN [1] {ECO:0000313|EMBL:ACY82513.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Fruit {ECO:0000313|EMBL:ACY82513.1}; RA Wang X.-J., Zhu S.-Y., Lu Y.-F., Zhang D.-P.; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ACY82513.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Fruit {ECO:0000313|EMBL:ACY82513.1}; RX PubMed=20360020; DOI=10.1093/pcp/pcq037; RA Wang X.J., Zhu S.Y., Lu Y.F., Zhao R., Xin Q., Wang X.F., Zhang D.P.; RT "Two coupled components of the mitogen-activated protein kinase cascade RT MdMPK1 and MdMKK1 from apple function in ABA signal transduction."; RL Plant Cell Physiol. 51:754-766(2010). 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:0000256|ARBA:ARBA00000494}; 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|ARBA:ARBA00000088, CC 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. 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; GU139791; ACY82513.1; -; mRNA. DR RefSeq; NP_001280856.1; NM_001293927.1. DR GeneID; 103456346; -. DR KEGG; mdm:103456346; -. DR OrthoDB; 741207at2759; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004707; F:MAP kinase activity; IEA:UniProtKB-EC. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0106311; F:protein threonine kinase activity; IEA:RHEA. 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 2: Evidence at transcript level; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU10141, ECO:0000256|RuleBase:RU000304}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU361165, KW ECO:0000313|EMBL:ACY82513.1}; Magnesium {ECO:0000256|RuleBase:RU361165}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141, ECO:0000256|RuleBase:RU000304}; KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527, KW ECO:0000256|RuleBase:RU000304}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361165}. FT DOMAIN 61..346 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 1..29 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..15 FT /note="Polar" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 91 FT /note="ATP" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 394 AA; 44892 MW; 3B2F316DA53414CC CRC64; MDGSAPQTDT VMSDAAAGQQ PAPPPLPMAG VESIPATLSH GGRFIQYNIF GNVFEVTAKY KPPIMPIGKG AYGIVCSALN SETNEHVAIK KIANAFDNKI DAKRTLREIK LLRHMDHENV VAIRDIIPPP QRNSFNDVYI AYGLMDTDLH QIIRSNQALS EEHCQYFLYQ ILRGLKYIHS ANVLHRDLKP SNLLLNANCD LKICDFGLAR VTSETDFMTE YVVTRWYRAP ELLLNSSDYT AAIDVWSVGC IFMELMDRKP LFPGRDHVHQ LRLLLELIGT PSEAELQFLN ENAKRYIRQL PLYRRQSFTE KFPHVHPSAI DLVEKMLTFD PTQRITVEDA LAHPYLTSLH DISDEPVCTT PFSFDFEQHA LSEEQMKELI YREALAFNPE YQLQ //