ID MPKC_NEOFI Reviewed; 377 AA. AC A1DES4; DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 29-MAY-2007, sequence version 2. DT 27-MAR-2024, entry version 87. DE RecName: Full=Mitogen-activated protein kinase mpkC; DE Short=MAP kinase C; DE EC=2.7.11.24; GN Name=mpkc; ORFNames=NFIA_078210; OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Fumigati. OX NCBI_TaxID=331117; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / RC NRRL 181 / WB 181; RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046; RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J., RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H., RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M., RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J., RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C., RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.; RT "Genomic islands in the pathogenic filamentous fungus Aspergillus RT fumigatus."; RL PLoS Genet. 4:E1000046-E1000046(2008). 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-171 and Tyr-173, 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=EAW17881.1; 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; DS027696; EAW17881.1; ALT_SEQ; Genomic_DNA. DR RefSeq; XP_001259778.1; XM_001259777.1. DR AlphaFoldDB; A1DES4; -. DR SMR; A1DES4; -. DR STRING; 331117.A1DES4; -. DR GeneID; 4586381; -. DR KEGG; nfi:NFIA_078210; -. DR VEuPathDB; FungiDB:NFIA_078210; -. DR eggNOG; KOG0660; Eukaryota. DR OrthoDB; 158564at2759; -. DR Proteomes; UP000006702; 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 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..377 FT /note="Mitogen-activated protein kinase mpkC" FT /id="PRO_0000289718" FT DOMAIN 20..299 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOTIF 171..173 FT /note="TXY" FT ACT_SITE 141 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 26..34 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 49 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 171 FT /note="Phosphothreonine" FT /evidence="ECO:0000250" FT MOD_RES 173 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250" SQ SEQUENCE 377 AA; 42913 MW; 9799CB428A4F547C CRC64; MAEFVRAEIL GTKFEYTTRY VNPQPIGMGS FGLVCSAFDQ ITQQPVALKK IMKPFDSSSL AKRTYREIRL LKYLRHENLI CLRDIFISPL EDIYIATELL GTDLGRLLSI KPLDSKFSQY FIYQILRGLK YIHSANVIHR DLKPTNILIN ENCDLKICDF GLARLQEPQM TGYVATRYYR APEIMLTWQR YGVQVDVWSA GCILAEMLRG KPLFPGKDHV HQFHLITNVL GNPPDAVIEK ITSKNTVNFV KSLPSREPRD LSTVIMTHTS IAIDLLKKML VIDPDTRISA QDALRHPYLA PYHDPTDEPA ASGPFDWSFD SADFPKETWK IMIYSEVLDY LNVGNPADPA PFDPSTPFDP SALEREFSEF LSDSGQI //