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KKCCC_EMEND
ID   KKCCC_EMEND             Reviewed;         518 AA.
AC   Q9Y898;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Calcium/calmodulin-dependent protein kinase kinase cmkC {ECO:0000305};
DE            EC=2.7.11.17 {ECO:0000269|PubMed:10988293};
DE   AltName: Full=CaMK kinase C {ECO:0000303|PubMed:10988293};
DE            Short=CaMKK C {ECO:0000303|PubMed:10988293};
DE   AltName: Full=CaMKK alpha/beta homolog {ECO:0000303|PubMed:10988293};
GN   Name=cmkC {ECO:0000303|PubMed:10988293};
OS   Emericella nidulans (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=162425 {ECO:0000312|EMBL:AAD38851.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=GR5;
RX   PubMed=10988293; DOI=10.1074/jbc.m006422200;
RA   Joseph J.D., Means A.R.;
RT   "Identification and characterization of two Ca2+/CaM-dependent protein
RT   kinases required for normal nuclear division in Aspergillus nidulans.";
RL   J. Biol. Chem. 275:38230-38238(2000).
CC   -!- FUNCTION: Calcium/calmodulin-dependent protein kinase that operates in
CC       the calcium-triggered CaMKK-CaMK1 signaling cascade. Phosphorylates and
CC       activates cmkB in vitro. Required in G1-phase of the cell cycle for
CC       proper timing of the initial nuclear division after germination as well
CC       as for subsequent nuclear division cycles. Required for the normal
CC       temporal regulation of nimX activity. {ECO:0000269|PubMed:10988293}.
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=2.7.11.17;
CC         Evidence={ECO:0000269|PubMed:10988293};
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=2.7.11.17; Evidence={ECO:0000269|PubMed:10988293};
CC   -!- ACTIVITY REGULATION: Activated by Ca(2+)/calmodulin. Binding of
CC       calmodulin may relieve intrasteric autoinhibition.
CC       {ECO:0000250|UniProtKB:P97756}.
CC   -!- DOMAIN: The autoinhibitory domain overlaps with the calmodulin binding
CC       region and may be involved in intrasteric autoinhibition.
CC       {ECO:0000250|UniProtKB:P97756}.
CC   -!- DISRUPTION PHENOTYPE: Not lethal, but spores germinate with delayed
CC       kinetics and this lag corresponds to a delay in the G1-phase activation
CC       of the cyclin-dependent kinase nimX. Does not activate cmkB.
CC       {ECO:0000269|PubMed:10988293}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; AF156028; AAD38851.1; -; mRNA.
DR   AlphaFoldDB; Q9Y898; -.
DR   SMR; Q9Y898; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004683; F:calmodulin-dependent protein 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:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
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; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Calmodulin-binding; Cell cycle; Cell division; Kinase;
KW   Nucleotide-binding; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..518
FT                   /note="Calcium/calmodulin-dependent protein kinase kinase
FT                   cmkC"
FT                   /id="PRO_0000440634"
FT   DOMAIN          81..376
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          119..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          404..409
FT                   /note="Autoinhibitory domain"
FT                   /evidence="ECO:0000250|UniProtKB:P97756, ECO:0000305"
FT   REGION          407..431
FT                   /note="Calmodulin-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P97756, ECO:0000305"
FT   REGION          453..472
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        243
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         87..95
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         109
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   518 AA;  59153 MW;  5F9AF1CFDE340C00 CRC64;
     MANEGAGSLQ QDASPGSSAR PEPYPRPSPA RYASTPSFES PQRHHRRNPI ARRPVKETLN
     ARSEYTLSQD DGTADDRINQ YVIKQEIGRG SFGAVHVAVD QYGNEYAVKE FSKARLRKRA
     KSQLLRQSRG PKRSSRWPKL PFSSPGTGTW RRRDEKCSLF YQRRNCHYEE VTPQQSSILD
     RGTGRPDPRF SYMVMEMCKK GVVMKVTLEE RADPYDDERC RCWFRDLILG IEYLHAQGIV
     HRDIKPDNCL ITNDDVLKVV DFGVSEMFVL NSDMFTAKSA GSPAFLPPEL CVVKHGDVSG
     KAADIWSMGV TLYCLRYGKL PFEEHSIIEL YDAIKNRPIV CDGETDEVFK DLMLRILEKD
     PAKRIQMDEL REHPWVTKNG MDPLLPKSEN TAEIVDLPTE EEMFSAITKN FGHVLAVMKA
     AKKFKSLQGP TRASTPIQSI LGQEYETHFV EPPTQMDPEE SVSLPSPLPY KKTQSLNTYN
     RRAWERDDVV KGYHPQRRKL SLVLRQRAAN RVLRTALF
 
 
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