ID A0A1S3BTE3_CUCME Unreviewed; 492 AA. AC A0A1S3BTE3; DT 12-APR-2017, integrated into UniProtKB/TrEMBL. DT 12-APR-2017, sequence version 1. DT 10-JUN-2026, entry version 43. DE RecName: Full=mitogen-activated protein kinase {ECO:0000256|ARBA:ARBA00012411}; DE EC=2.7.11.24 {ECO:0000256|ARBA:ARBA00012411}; GN Name=LOC103492960 {ECO:0000313|RefSeq:XP_008451774.1}; OS Cucumis melo (Muskmelon). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis. OX NCBI_TaxID=3656 {ECO:0000313|Proteomes:UP001652600, ECO:0000313|RefSeq:XP_008451774.1}; RN [1] {ECO:0000313|RefSeq:XP_008451774.1} RP IDENTIFICATION. RC TISSUE=Stem {ECO:0000313|RefSeq:XP_008451774.1}; RG RefSeq; RL Submitted (JAN-2026) to UniProtKB. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + CC H(+); 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:ARBA00048312}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + CC ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA- CC COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.24; CC Evidence={ECO:0000256|ARBA:ARBA00047592}; CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr CC protein kinase family. MAP kinase subfamily. CC {ECO:0000256|ARBA:ARBA00008832}. 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 RefSeq; XP_008451774.1; XM_008453552.3. DR AlphaFoldDB; A0A1S3BTE3; -. DR SMR; A0A1S3BTE3; -. DR GeneID; 103492960; -. DR KEGG; cmo:103492960; -. DR eggNOG; KOG0660; Eukaryota. DR InParanoid; A0A1S3BTE3; -. DR OrthoDB; 661390at71240; -. DR Proteomes; UP001652600; Chromosome 7. 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 CDD; cd07859; STKc_TDY_MAPK; 1. DR FunFam; 1.10.510.10:FF:000017; Mitogen-activated protein kinase; 1. DR FunFam; 3.30.200.20:FF:000046; Mitogen-activated protein kinase; 1. DR Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 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; IPR050117; MAPK. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR PANTHER; PTHR24055; MITOGEN-ACTIVATED PROTEIN KINASE; 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. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Reference proteome {ECO:0000313|Proteomes:UP001652600}; KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 25..316 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 437..461 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 54 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 492 AA; 56591 MW; 78CB6224B11DE97E CRC64; MPQDHPKKEA KEVNFFTEYG DANRYKILEV VGRGSYGVVC SAIDMQTGEK VAIKRIHDIF DHASDAIRIL REVKLLRLLR HPDIVDIKRI MLPPSKKEFR DIYVVFELME SDLHQVIKAN DDLTREHHQF FLYQMLRALK FMHTANVYHR DLKPKNILAN ANCKLKICDF GLARVAFSDT PTTVFWTDYV ATRWYRAPEL CGSFCSKYTP AIDIWSVGCI FAEVLMGKPL FPGKSVAHQL DLITDLLGTP SLETIAGVRN EKVRKYLTEM KKKSAVPFSQ RFPKADPTAI RLLERLLAFN PKDRPSAVEA LADPYFKGLA KVEREPSCQP ISRSEFEFER QKLTKDDVRE LLYREILEYH PQIREDYLNG TETTKLHYPS VTGHFKSQFT FHKENNGKSA PVLPLERKHF SLPRSTVCTN LVSPDHESVR RNPKVCNNSM GLPDRTFGNP SKAYHPPKVP TGRVAGPILP YEHRNIKDVY SKLTSQIRSL DF //