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
