ID A0A0G4PWR1_PENCA Unreviewed; 352 AA. AC A0A0G4PWR1; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 16-OCT-2019, entry version 31. DE RecName: Full=Mitogen-activated protein kinase {ECO:0000256|RuleBase:RU361165, ECO:0000256|SAAS:SAAS00574127}; DE EC=2.7.11.24 {ECO:0000256|RuleBase:RU361165, ECO:0000256|SAAS:SAAS00574127}; GN ORFNames=PCAMFM013_S063g000013 {ECO:0000313|EMBL:CRL30907.1}; OS Penicillium camemberti 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|Proteomes:UP000053732} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FM 013 {ECO:0000313|Proteomes:UP000053732}; 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., RA Goarin A., Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., RA Brygoo Y.; RT "Multiple recent horizontal transfers of a large genomic region in RT cheesemaking fungi."; RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {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., RA Goarin A., Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., RA Brygoo Y.; RT "Multiple recent horizontal transfers of a large genomic region in RT cheese making fungi."; RL Nat. Commun. 5:2876-2876(2014). 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, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; CC EC=2.7.11.24; Evidence={ECO:0000256|SAAS:SAAS01125144}; 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 ECO:0000256|SAAS:SAAS01125154}; 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 CC protein kinase family. MAP kinase subfamily. CC {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 EnsemblFungi; CRL30907; CRL30907; PCAMFM013_S063g000013. DR Proteomes; UP000053732; Unassembled WGS sequence. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004707; F:MAP kinase activity; IEA:UniProtKB-EC. 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 3: Inferred from homology; KW ATP-binding {ECO:0000256|RuleBase:RU000304, KW ECO:0000256|SAAS:SAAS00574094}; KW Complete proteome {ECO:0000313|Proteomes:UP000053732}; KW Kinase {ECO:0000256|RuleBase:RU361165, ECO:0000256|SAAS:SAAS00574086, KW ECO:0000313|EMBL:CRL30907.1}; KW Magnesium {ECO:0000256|RuleBase:RU361165}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU000304, KW ECO:0000256|SAAS:SAAS00574135}; KW Reference proteome {ECO:0000313|Proteomes:UP000053732}; KW Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU000304, KW ECO:0000256|SAAS:SAAS00574114}; KW Transferase {ECO:0000256|RuleBase:RU361165, KW ECO:0000256|SAAS:SAAS00574095}. FT DOMAIN 20 299 Protein kinase. {ECO:0000259|PROSITE: FT PS50011}. 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 //