MKC1_CANAX
ID MKC1_CANAX Reviewed; 501 AA.
AC P43068;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Mitogen-activated protein kinase MKC1;
DE Short=MAP kinase MKC1;
DE EC=2.7.11.24;
GN Name=MKC1;
OS Candida albicans (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5476;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 64385 / 1001;
RX PubMed=7891715; DOI=10.1128/mcb.15.4.2197;
RA Navarro-Garcia F., Sanchez M., Pla J., Nombela C.;
RT "Functional characterization of the MKC1 gene of Candida albicans, which
RT encodes a mitogen-activated protein kinase homolog related to cell
RT integrity.";
RL Mol. Cell. Biol. 15:2197-2206(1995).
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-211 and Tyr-213, which activates the
CC enzyme. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. MAP kinase subfamily. {ECO:0000305}.
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DR EMBL; X76708; CAA54129.1; -; Genomic_DNA.
DR AlphaFoldDB; P43068; -.
DR SMR; P43068; -.
DR VEuPathDB; FungiDB:CAWG_01373; -.
DR VEuPathDB; FungiDB:CR_00120C_A; -.
DR PHI-base; PHI:67; -.
DR PHI-base; PHI:6843; -.
DR GO; GO:0005737; C:cytoplasm; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0000196; P:cell wall integrity MAPK cascade; IEA:EnsemblFungi.
DR GO; GO:1902660; P:negative regulation of glucose mediated signaling pathway; IEA:EnsemblFungi.
DR GO; GO:1902413; P:negative regulation of mitotic cytokinesis; IEA:EnsemblFungi.
DR GO; GO:1905665; P:positive regulation of calcium ion import across plasma membrane; IEA:EnsemblFungi.
DR GO; GO:0050850; P:positive regulation of calcium-mediated signaling; IEA:EnsemblFungi.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003527; MAP_kinase_CS.
DR InterPro; IPR008352; MAPK_p38-like.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR01773; P38MAPKINASE.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS01351; MAPK; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell cycle; Kinase; Nucleotide-binding; Phosphoprotein;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..501
FT /note="Mitogen-activated protein kinase MKC1"
FT /id="PRO_0000186334"
FT DOMAIN 28..339
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 400..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 211..213
FT /note="TXY"
FT COMPBIAS 400..419
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 174
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 34..42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 74
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 211
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 213
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 501 AA; 58192 MW; 0EA9F8B6CB97AB07 CRC64;
MDQQEAPIYY GRSVNKVYNQ EFIIDSRFKI VKELGHGAYG IVCSAKYDNG SKKVPDSNNG
NASSSANASF VAIKKITNIF SKNILCKRAL RELKLLQFFR GHKNITCLYD LDIIPNPMTG
EFNEIYLYEE LMECDMHQII RSGQPLSDQH YQSFIYQVLC GLNFIHSADV LHRDLKPGNL
LVNADCELKI CDFGLARGFS ENPDENAGFM TEYVATRWYR APEIMLSFTN YTKAIDIWSV
GCILAELLGG KPLFRGKDYV DQLNQILMIL GTPPESTLQR IGSHRAQNYV RSLPITRKAS
YEELFPDANP LALDLLERML TLDPRERITV RDALNHKYLE LWHDPKEEIE CQVKFDFKSF
ETVDGLDEMK QLIMDEVQKF REFVRKPIEE QQRIQMQLHM QKREEQRQEE EEKELLEQQR
QFPAQESMDI SQTPYNNLET NIGTPQVEDD YPRPQELDEF TFSNLESSSS MNLFQDMAKP
SGEEYIKLEE ELGFGLDWCY V
