ID A0A0G4PWR1_PENCA Unreviewed; 352 AA. AC A0A0G4PWR1; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 17-FEB-2016, entry version 6. DE RecName: Full=Mitogen-activated protein kinase {ECO:0000256|RuleBase:RU361165, ECO:0000256|SAAS:SAAS00388444}; DE EC=2.7.11.24 {ECO:0000256|RuleBase:RU361165, ECO:0000256|SAAS:SAAS00388444}; GN ORFNames=PCAMFM013_S063g000013 {ECO:0000313|EMBL:CRL30907.1}; OS Penicillium camembertii. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium. OX NCBI_TaxID=5075 {ECO:0000313|EMBL:CRL30907.1}; RN [1] {ECO:0000313|EMBL:CRL30907.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FM013 {ECO:0000313|EMBL:CRL30907.1}; 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: ATP + a protein = ADP + a phosphoprotein. CC {ECO:0000256|RuleBase:RU361165, ECO:0000256|SAAS:SAAS00095926}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|RuleBase:RU361165}; CC -!- ENZYME 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 -!- SIMILARITY: Contains 1 protein kinase domain. 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 GO; GO:0005622; C:intracellular; IEA:GOC. 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. DR InterPro; IPR003527; MAP_kinase_CS. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR002290; Ser/Thr_dual-sp_kinase. 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:SAAS00465584}; KW Kinase {ECO:0000256|RuleBase:RU361165, ECO:0000256|SAAS:SAAS00465575, KW ECO:0000313|EMBL:CRL30907.1}; KW Magnesium {ECO:0000256|RuleBase:RU361165}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU000304, KW ECO:0000256|SAAS:SAAS00465633}; KW Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU361165, KW ECO:0000256|SAAS:SAAS00465625}; KW Transferase {ECO:0000256|RuleBase:RU361165, KW ECO:0000256|SAAS:SAAS00465635}. 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 //