ID A0A2T1LXW3_9CHRO Unreviewed; 519 AA.
AC A0A2T1LXW3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
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 ECO:0000313|EMBL:PSF37228.1};
GN ORFNames=C7H19_10935 {ECO:0000313|EMBL:PSF37228.1};
OS Aphanothece hegewaldii CCALA 016.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Aphanothecaceae; Aphanothece.
OX NCBI_TaxID=2107694 {ECO:0000313|EMBL:PSF37228.1, ECO:0000313|Proteomes:UP000239001};
RN [1] {ECO:0000313|EMBL:PSF37228.1, ECO:0000313|Proteomes:UP000239001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCALA 016 {ECO:0000313|EMBL:PSF37228.1,
RC ECO:0000313|Proteomes:UP000239001};
RA Moore K.R., Magnabosco C., Momper L., Gold D.A., Bosak T., Fournier G.P.;
RT "The ancient ancestry and fast evolution of plastids.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PSF37228.1, ECO:0000313|Proteomes:UP000239001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCALA 016 {ECO:0000313|EMBL:PSF37228.1,
RC ECO:0000313|Proteomes:UP000239001};
RA Keele B.F.;
RL Submitted (MAR-2018) 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:PSF37228.1}.
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DR EMBL; PXOH01000010; PSF37228.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T1LXW3; -.
DR OrthoDB; 9787927at2; -.
DR Proteomes; UP000239001; 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 PRINTS; PR01874; DNAREPAIRADA.
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}; Reference proteome {ECO:0000313|Proteomes:UP000239001};
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 19..260
FT /note="KaiC"
FT /evidence="ECO:0000259|PROSITE:PS51146"
FT DOMAIN 261..493
FT /note="KaiC"
FT /evidence="ECO:0000259|PROSITE:PS51146"
FT BINDING 49
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 50
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 51
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 52
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 53
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 53
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01836"
FT BINDING 54
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 89
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 224
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 225
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 226
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 228
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 230
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 290
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 291
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 292
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 293
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 294
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 295
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 295
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01836"
FT BINDING 296
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 318
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01836"
FT BINDING 331
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 451
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 457
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 458
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 459
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 461
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 463
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 465
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 431
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01836"
FT MOD_RES 432
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01836"
SQ SEQUENCE 519 AA; 58410 MW; 829EFF86BB55F075 CRC64;
MSQQIPNGKQ KQIYPLGVRK IRTMIEGFDE ISHGGLPAGR TTLISGTSGT GKTLMAIQFL
YHGIKYFDFP GLFVTFEESP IDIIQNAYSF GWDLPALIEE GKLFILDASP DPEGQEVVGS
FDLSALIERI QYAIQKYKAK LVSVDSVTAV FQQYEAASVV RREIFRLVAR LKKLEVTSIM
TTERVEEYGQ VARFGVEEFV SDNVVIFRNV LEGERRRRTA EILKLRGTTH MKGEYPFTMT
NDGINIFPLG AMRLTQRSSN ARISSGVKTL DEMCGGGFFK DSIILATGAT GTGKTLLVSK
FLEEGCRRGE RAILFAYEES RAQLSRNAFS WGIDFEEMEK KGLLKLLCSY PESAGLEDHL
QMIKSEIAEF KPSRIAIDSL SALARGVSNN AFRQFVIGVT GFAKQEEITG FFTNTTDQFM
GAHSITESHI STITDTILML QYVEIKGEMS RALNVFKMRG SWHDKGIREY TINQDGPEIR
DSFRNYERII SGSPTRITVD EKTELSRIMR NMKEKTQDE
//
