ID A0A0G4PWR1_PENC3 Unreviewed; 352 AA. AC A0A0G4PWR1; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 02-OCT-2024, entry version 53. 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 ORFNames=PCAMFM013_S063g000013 {ECO:0000313|EMBL:CRL30907.1}; OS Penicillium camemberti (strain FM 013). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium. OX NCBI_TaxID=1429867 {ECO:0000313|EMBL:CRL30907.1, ECO:0000313|Proteomes:UP000053732}; RN [1] {ECO:0000313|EMBL:CRL30907.1, ECO:0000313|Proteomes:UP000053732} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FM 013 {ECO:0000313|Proteomes:UP000053732}; RX PubMed=24407037; DOI=10.1038/ncomms3876; RA Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A., RA Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A., RA Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.; RT "Multiple recent horizontal transfers of a large genomic region in cheese RT making fungi."; RL Nat. Commun. 5:2876-2876(2014). 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|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. 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; HG793196; CRL30907.1; -; Genomic_DNA. DR AlphaFoldDB; A0A0G4PWR1; -. DR STRING; 1429867.A0A0G4PWR1; -. DR Proteomes; UP000053732; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter. 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:UniProtKB-EC. DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:TreeGrafter. DR GO; GO:0007231; P:osmosensory signaling pathway; IEA:TreeGrafter. DR GO; GO:0051403; P:stress-activated MAPK cascade; IEA:TreeGrafter. 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; 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:SF158; MITOGEN-ACTIVATED PROTEIN KINASE P38A-RELATED; 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 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU10141}; KW Kinase {ECO:0000256|RuleBase:RU361165, ECO:0000313|EMBL:CRL30907.1}; KW Magnesium {ECO:0000256|RuleBase:RU361165}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000053732}; KW Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU000304}; KW Transferase {ECO:0000256|RuleBase:RU361165}. FT DOMAIN 20..299 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT BINDING 50 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 352 AA; 40293 MW; 03BADC44E6385E75 CRC64; MANFTQLQIF GTTFEITSRY LNLQPVGIGA FGLVCSARDQ LTGQPVAVKK IMKPFSSSVL SKRTFRELKL LKHLRHDNVI SLSDVFISPL EDIYFVTELL GTDLHRLLTS RSRQAQFIQY FVYQIFRGLK YVHSAGVVHR DLKPSNILIN ENCDLKICDF GLARTEDPQM TGYVSTRYYR APEIMLNWQK YDVEVDIWSA GCVFAEMFEG KPLFPGTDHV NQFSIITDLL GTPPDDVIQT IGSESTLRFV KSLPKRKRHP LADKFRNADA DAVDLLERIF VFNPTERIQA AEVLAHKYLA PYHDPMDEPV AQEKFDWSFT NLDVPVDTWK IMMYSESIDF HNIDQGNVAP VN //