ID MPKC_ASPOR Reviewed; 344 AA. AC Q2U469; DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 29-MAY-2007, sequence version 2. DT 27-MAR-2024, entry version 96. DE RecName: Full=Mitogen-activated protein kinase mpkC; DE Short=MAP kinase C; DE EC=2.7.11.24; GN Name=mpkC; ORFNames=AO090020000466; OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Circumdati. OX NCBI_TaxID=510516; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 42149 / RIB 40; RX PubMed=16372010; DOI=10.1038/nature04300; RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E., RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., RA Kikuchi H.; RT "Genome sequencing and analysis of Aspergillus oryzae."; RL Nature 438:1157-1161(2005). CC -!- FUNCTION: Mitogen-activated protein kinase required for growth on media CC where sorbitol or mannitol is the sole carbon source. {ECO:0000250}. 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, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24; 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; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- ACTIVITY REGULATION: Activated by tyrosine and threonine CC phosphorylation. {ECO:0000250}. CC -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues CC whose phosphorylation activates the MAP kinases. CC -!- PTM: Dually phosphorylated on Thr-170 and Tyr-172, which activates the CC enzyme. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein CC kinase family. MAP kinase subfamily. HOG1 sub-subfamily. CC {ECO:0000255|PROSITE-ProRule:PRU00159}. CC -!- SEQUENCE CAUTION: CC Sequence=BAE63646.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; 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; AP007167; BAE63646.1; ALT_SEQ; Genomic_DNA. DR AlphaFoldDB; Q2U469; -. DR SMR; Q2U469; -. DR STRING; 510516.Q2U469; -. DR OrthoDB; 158564at2759; -. DR Proteomes; UP000006564; Chromosome 6. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004707; F:MAP kinase activity; IEA:UniProtKB-EC. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. 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; 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; Kinase; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Serine/threonine-protein kinase; Transferase. FT CHAIN 1..344 FT /note="Mitogen-activated protein kinase mpkC" FT /id="PRO_0000289715" FT DOMAIN 19..298 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOTIF 170..172 FT /note="TXY" FT ACT_SITE 140 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 25..33 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 48 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 170 FT /note="Phosphothreonine" FT /evidence="ECO:0000250" FT MOD_RES 172 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250" SQ SEQUENCE 344 AA; 39188 MW; 66631F37777D796E CRC64; MEFIRAEILG TTFETTSRYA NVQPVGLGAF GLVCSAYDQI TQQHVAVKKM MNPFANASIA KRTYREVKLL KQLRHENLIG LCDIFISPLE DIYLVTELLG TDLGRLLRAR PLDNKFAQYF MYQILRGLKY IHSAGVIHRD LKPSNLLVNE NCDLKICDFG LARVQEPQMT GYVSTRYYRA PEIMLTWQRY GKMVDIWSAG CILAEMLRGK PLFPGKDHIH QFFLITEVLG NPPPEVVQKI TSGNTQRVVN SLPNQEPRPL RAVFHEFDND VISLLEQLLL FDPDKRLTAE TALQHPYLAP YHDPDDEPAA LEKFDWSFND ADLPIDTWKL MMCVAIGSAK CAPN //