ID Q064X6_9SYNE Unreviewed; 501 AA.
AC Q064X6;
DT 14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 1.
DT 24-JAN-2024, entry version 71.
DE RecName: Full=Circadian clock oscillator protein KaiC {ECO:0000256|HAMAP-Rule:MF_01836};
DE EC=2.7.11.1 {ECO:0000256|HAMAP-Rule:MF_01836};
DE EC=3.6.4.- {ECO:0000256|HAMAP-Rule:MF_01836};
GN Name=kaiC {ECO:0000256|HAMAP-Rule:MF_01836};
GN ORFNames=BL107_16380 {ECO:0000313|EMBL:EAU72402.1};
OS Synechococcus sp. BL107.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=313625 {ECO:0000313|EMBL:EAU72402.1, ECO:0000313|Proteomes:UP000004390};
RN [1] {ECO:0000313|EMBL:EAU72402.1, ECO:0000313|Proteomes:UP000004390}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BL107 {ECO:0000313|EMBL:EAU72402.1,
RC ECO:0000313|Proteomes:UP000004390};
RA Scanlan D., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the KaiC family. {ECO:0000256|HAMAP-
CC Rule:MF_01836}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01836}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAU72402.1}.
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; AATZ01000001; EAU72402.1; -; Genomic_DNA.
DR AlphaFoldDB; Q064X6; -.
DR STRING; 313625.BL107_16380; -.
DR eggNOG; COG0467; Bacteria.
DR HOGENOM; CLU_023669_4_1_3; -.
DR Proteomes; UP000004390; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0007623; P:circadian rhythm; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0042752; P:regulation of circadian rhythm; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd19485; KaiC-N; 1.
DR CDD; cd19484; KaiC_C; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR HAMAP; MF_01836; KaiC; 1.
DR InterPro; IPR013503; Circadian_KaiC_bact.
DR InterPro; IPR030665; KaiC.
DR InterPro; IPR014774; KaiC-like_dom.
DR InterPro; IPR047222; KaiC_C.
DR InterPro; IPR010624; KaiC_dom.
DR InterPro; IPR047221; KaiC_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR02655; circ_KaiC; 1.
DR PANTHER; PTHR42926; -; 1.
DR PANTHER; PTHR42926:SF1; KAIC-LIKE PROTEIN 2; 1.
DR Pfam; PF06745; ATPase; 2.
DR PIRSF; PIRSF039117; KaiC; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51146; KAIC; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01836};
KW Biological rhythms {ECO:0000256|HAMAP-Rule:MF_01836};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01836};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_01836};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01836};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01836};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01836};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|HAMAP-
KW Rule:MF_01836};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_01836};
KW Repressor {ECO:0000256|HAMAP-Rule:MF_01836};
KW Serine/threonine-protein kinase {ECO:0000256|HAMAP-Rule:MF_01836};
KW Transcription {ECO:0000256|HAMAP-Rule:MF_01836};
KW Transcription regulation {ECO:0000256|HAMAP-Rule:MF_01836};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01836}.
FT DOMAIN 4..245
FT /note="KaiC"
FT /evidence="ECO:0000259|PROSITE:PS51146"
FT DOMAIN 246..478
FT /note="KaiC"
FT /evidence="ECO:0000259|PROSITE:PS51146"
FT BINDING 34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /ligand_note="ligand shared between homodimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01836"
FT BINDING 36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /ligand_note="ligand shared between homodimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01836"
FT BINDING 37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /ligand_note="ligand shared between homodimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01836"
FT BINDING 38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /ligand_note="ligand shared between homodimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01836"
FT BINDING 38
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01836"
FT BINDING 74
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /ligand_note="ligand shared between homodimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01836"
FT BINDING 209
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /ligand_note="ligand shared between homodimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01836"
FT BINDING 210
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /ligand_note="ligand shared between homodimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01836"
FT BINDING 211
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /ligand_note="ligand shared between homodimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01836"
FT BINDING 213
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /ligand_note="ligand shared between homodimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01836"
FT BINDING 215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /ligand_note="ligand shared between homodimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01836"
FT BINDING 275
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /ligand_note="ligand shared between homodimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01836"
FT BINDING 276
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /ligand_note="ligand shared between homodimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01836"
FT BINDING 277
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /ligand_note="ligand shared between homodimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01836"
FT BINDING 278
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /ligand_note="ligand shared between homodimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01836"
FT BINDING 279
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /ligand_note="ligand shared between homodimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01836"
FT BINDING 280
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /ligand_note="ligand shared between homodimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01836"
FT BINDING 280
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01836"
FT BINDING 303
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01836"
FT BINDING 316
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /ligand_note="ligand shared between homodimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01836"
FT BINDING 436
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /ligand_note="ligand shared between homodimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01836"
FT BINDING 442
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /ligand_note="ligand shared between homodimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01836"
FT BINDING 443
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /ligand_note="ligand shared between homodimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01836"
FT BINDING 444
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /ligand_note="ligand shared between homodimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01836"
FT BINDING 446
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /ligand_note="ligand shared between homodimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01836"
FT BINDING 448
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /ligand_note="ligand shared between homodimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01836"
FT BINDING 450
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /ligand_note="ligand shared between homodimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01836"
FT MOD_RES 416
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01836"
FT MOD_RES 417
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01836"
SQ SEQUENCE 501 AA; 55822 MW; 12119BA032F8EC11 CRC64;
MQVQKLATGI EGFDDVCHGG LPIGRSTLIS GTSGSGKTVL SLHFLHNGIK HFEEPGIFVT
FEESPLDILR NAASFGWNLQ EMVEQDKLFI LDASPDPDGQ DVAGSFDLSG LIERINYAIR
KYKAKRVVID SITAVFQQYD AVFVVRREIF RLIARLKEIG VTTVMTTERI DEYGPIARYG
VEEFVSDNVV ILRNVLEGER RRRTVEILKL RGTTHMKGEF PFTMGAHGIS IFPLGAMRLT
QRSSNVRVSS GVPRLDEMCG GGFFKDSIIL ATGATGTGKT MLVSKFIEDA CRNKERAILF
AYEESRAQLM RNGTSWGIDF EQMEQDGLLK IICAYPESTG LEDHLQIIKT EISEFKPSRM
AIDSLSALAR GVSHNAFRQF VIGVTGYAKQ EEIAGFFTNT SEEFMGSHSI TDSHISTITD
TILLLQYVEI RGEMARALNV FKMRGSWHDK GIREFVITGN GPQIKDSFSN FERIISGVPH
RVSTDERSEL SRIAKSVSSD D
//