ID A0A914ZP63_PARUN Unreviewed; 369 AA. AC A0A914ZP63; DT 22-FEB-2023, integrated into UniProtKB/TrEMBL. DT 22-FEB-2023, sequence version 1. DT 27-NOV-2024, entry version 11. 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}; OS Parascaris univalens (Nematode worm). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Parascaris. OX NCBI_TaxID=6257 {ECO:0000313|Proteomes:UP000887569, ECO:0000313|WBParaSite:PgB10_g072_t01}; RN [1] {ECO:0000313|WBParaSite:PgB10_g072_t01} RP IDENTIFICATION. RG WormBaseParasite; RL Submitted (NOV-2022) 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:ARBA00000494}; 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:ARBA00000088, CC ECO:0000256|RuleBase:RU361165}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946, CC 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 WBParaSite; PgB10_g072_t01; PgB10_g072_t01; PgB10_g072. DR Proteomes; UP000887569; Unplaced. DR GO; GO:0005737; C:cytoplasm; IEA:UniProt. DR GO; GO:0005634; C:nucleus; IEA:TreeGrafter. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004707; F:MAP kinase activity; IEA:InterPro. DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro. DR CDD; cd07849; STKc_ERK1_2_like; 1. DR FunFam; 1.10.510.10:FF:000624; Mitogen-activated protein kinase; 1. DR FunFam; 3.30.200.20:FF:000373; Mitogen-activated protein kinase 1; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR050117; MAP_kinase. DR InterPro; IPR003527; MAP_kinase_CS. DR InterPro; IPR008349; MAPK_ERK1/2. 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:SF596; MITOGEN-ACTIVATED PROTEIN KINASE ERK-A; 1. DR Pfam; PF00069; Pkinase; 1. DR PRINTS; PR01770; ERK1ERK2MAPK. 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 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Cell cycle {ECO:0000256|ARBA:ARBA00023306}; 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}; Reference proteome {ECO:0000313|Proteomes:UP000887569}; KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527, KW ECO:0000256|RuleBase:RU000304}; KW Transferase {ECO:0000256|RuleBase:RU361165}. FT DOMAIN 26..314 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT BINDING 56 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 369 AA; 42836 MW; 4324AB2F57F3E2EA CRC64; MTTLEAQTRN AVEEVHGQVF EVGPRYVSLS YIGEGAYGMV VSAMDVETHD RVAIKKISPF EHQTFCQRTL REIKILTRFK HENIINIQEI IRAPSVEQMK DIYIVQCLME TDLYKLLKTQ KLSNDHICYF LYQILRGLKY IHSANVIHRD LKPSNLLLNT TCDLKICDFG LARVTDPGHD HTGFLTEYVA TRWYRAPEIM LNSKGYTKSI DVWSVGCILA EMLNNRPLFP GKHYLDQLNL ILAVIGSPSQ EDLQCIINEK ARSYLLSLPH KVKQPWLRMY PSADPRALDL LDKMLTFNPS KRINIEDALA HPYLEQYYDP NDEPVCEEPF TLEMELDDLP KETLKELIFQ ETENHYKRMQ EAKLQNAQQ //