KCC1B_EMEND
ID KCC1B_EMEND Reviewed; 404 AA.
AC Q9Y899;
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 cmkB {ECO:0000303|PubMed:10988293};
DE Short=CaMK B {ECO:0000303|PubMed:10988293};
DE EC=2.7.11.17 {ECO:0000269|PubMed:10988293};
DE AltName: Full=CaMKI/IV homolog {ECO:0000303|PubMed:10988293};
GN Name=cmkB {ECO:0000303|PubMed:10988293, ECO:0000312|EMBL:AAD38850.1};
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:AAD38850.1};
RN [1] {ECO:0000312|EMBL:AAD38850.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, DISRUPTION PHENOTYPE, MUTAGENESIS OF THR-179, AND
RP PHOSPHORYLATION AT THR-179.
RC STRAIN=GR5 {ECO:0000303|PubMed:10988293};
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. Required in G1-
CC phase of the cell cycle for proper timing of the initial nuclear
CC division after germination, but not for subsequent mitoses. Required
CC for the normal temporal regulation of nimX activity.
CC {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 results in conformational change that relieves intrasteric
CC autoinhibition and allows phosphorylation of Thr-179 within the
CC activation loop by cmkC. {ECO:0000269|PubMed:10988293}.
CC -!- DOMAIN: The autoinhibitory domain overlaps with the calmodulin binding
CC region and interacts in the inactive folded state with the catalytic
CC domain as a pseudosubstrate. {ECO:0000250|UniProtKB:Q63450}.
CC -!- PTM: Phosphorylated by cmkC on Thr-179. {ECO:0000269|PubMed:10988293}.
CC -!- DISRUPTION PHENOTYPE: Lethal. {ECO:0000269|PubMed:10988293}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. CaMK subfamily. {ECO:0000305}.
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DR EMBL; AF156027; AAD38850.1; -; mRNA.
DR AlphaFoldDB; Q9Y899; -.
DR SMR; Q9Y899; -.
DR iPTMnet; Q9Y899; -.
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 Allosteric enzyme; ATP-binding; Calmodulin-binding; Cell cycle;
KW Cell division; Kinase; Nucleotide-binding; Phosphoprotein;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..404
FT /note="Calcium/calmodulin-dependent protein kinase cmkB"
FT /id="PRO_0000440633"
FT DOMAIN 18..279
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 279..322
FT /note="Autoinhibitory domain"
FT /evidence="ECO:0000250|UniProtKB:Q63450"
FT REGION 301..323
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250|UniProtKB:Q63450"
FT REGION 336..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..368
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 141
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 24..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 179
FT /note="Phosphothreonine; by cmkC"
FT /evidence="ECO:0000305|PubMed:10988293"
FT MUTAGEN 179
FT /note="T->A: Loss of activation by cmkC."
FT /evidence="ECO:0000269|PubMed:10988293"
SQ SEQUENCE 404 AA; 45752 MW; 79715478C68FB2B4 CRC64;
MASQVQPGQK PKVQPCRYKT GKTLGAGLYS VVKECVHIDT GQYYAAKVIN KRLMVGREHM
VRNEIAILKQ VSTGHQNILT LVDYFETMNN LYLVTDLALG GELFDRICRK GSYYESDAAD
LVRAILSAVA YLHDHGIVHR DLKPENLLFR TPEDNADLLI ADFGLSRIMD EEQLHVLTTT
CGTPGYMAPE IFDKSGHGKP VDIWAIGLIT YFMLCGYTPF DRETNLEEVQ AIATANFSFT
PVEYWRGVSQ EARDFIKRCL TVNPKKRMTA HQALQHPWIN PPYDTTDDLG SGEDLLPNIK
KNFNARRTLH KAIDTVRAIN KLRENGGLMM DGIMSVDPKP EHVNGSEVVE DRTTPREREN
EDAMEIDSRS NARGQTEQQI REQERKVKET VAGLWSRTAP RSER
