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Circadian clock protein kinase KaiC (EC 2.7.11.1)

 Q1PJG6_PROMR            Unreviewed;       513 AA.
Q1PJG6;
16-MAY-2006, integrated into UniProtKB/TrEMBL.
16-MAY-2006, sequence version 1.
27-SEP-2017, entry version 43.
RecName: Full=Circadian clock protein kinase KaiC {ECO:0000256|HAMAP-Rule:MF_01836};
EC=2.7.11.1 {ECO:0000256|HAMAP-Rule:MF_01836};
Name=kaiC {ECO:0000256|HAMAP-Rule:MF_01836,
ECO:0000313|EMBL:ABE11415.1};
ORFNames=HOT0M-1A11_0021 {ECO:0000313|EMBL:ABE11415.1};
uncultured Prochlorococcus marinus clone HOT0M-1A11.
Bacteria; Cyanobacteria; Synechococcales; Prochloraceae;
Prochlorococcus.
NCBI_TaxID=379386 {ECO:0000313|EMBL:ABE11415.1};
[1] {ECO:0000313|EMBL:ABE11415.1}
NUCLEOTIDE SEQUENCE.
PubMed=16556843; DOI=10.1126/science.1122050;
Coleman M.L., Sullivan M.B., Martiny A.C., Steglich C., Barry K.,
Delong E.F., Chisholm S.W.;
"Genomic islands and the ecology and evolution of Prochlorococcus.";
Science 311:1768-1770(2006).
[2] {ECO:0000313|EMBL:ABE11415.1}
NUCLEOTIDE SEQUENCE.
US DOE Joint Genome Institute (JGI);
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
Hammon N., Israni S., Richardson P.;
"Sequencing of the draft fosmids and assembly of Prochlorococcus
marinus environmental genome fragment.";
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Core component of the KaiBC clock protein complex, which
constitutes the main circadian regulator in cyanobacteria. Binds
to DNA. The KaiBC complex may act as a promoter-nonspecific
transcription regulator that represses transcription, possibly by
acting on the state of chromosome compaction. {ECO:0000256|HAMAP-
Rule:MF_01836}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000256|HAMAP-Rule:MF_01836}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_01836};
-!- SUBUNIT: Homohexamer; hexamerization is dependent on ATP-binding.
Component of the KaiBC complex with KaiB. Interacts directly with
SasA. {ECO:0000256|HAMAP-Rule:MF_01836}.
-!- PTM: Phosphorylated on serine/threonine residues by autocatalysis.
Both phosphorylated and unphosphorylated forms exist. Can probably
autophosphorylate and autodephosphorylate. Phosphorylated form
correlates with clock speed. {ECO:0000256|HAMAP-Rule:MF_01836}.
-!- SIMILARITY: Belongs to the KaiC family. {ECO:0000256|HAMAP-
Rule:MF_01836}.
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EMBL; DQ366734; ABE11415.1; -; Genomic_DNA.
ProteinModelPortal; Q1PJG6; -.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-UniRule.
GO; GO:0007623; P:circadian rhythm; IEA:UniProtKB-UniRule.
GO; GO:0042752; P:regulation of circadian rhythm; IEA:InterPro.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
HAMAP; MF_01836; KaiC; 1.
InterPro; IPR013503; Circadian_KaiC_bact.
InterPro; IPR030665; KaiC.
InterPro; IPR014774; KaiC-like_dom.
InterPro; IPR010624; KaiC_dom.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF06745; ATPase; 2.
PIRSF; PIRSF039117; KaiC; 1.
SUPFAM; SSF52540; SSF52540; 2.
TIGRFAMs; TIGR02655; circ_KaiC; 1.
PROSITE; PS51146; KAIC; 2.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_01836};
Biological rhythms {ECO:0000256|HAMAP-Rule:MF_01836};
DNA-binding {ECO:0000256|HAMAP-Rule:MF_01836};
Kinase {ECO:0000256|HAMAP-Rule:MF_01836};
Magnesium {ECO:0000256|HAMAP-Rule:MF_01836};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01836};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01836};
Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_01836};
Repeat {ECO:0000256|HAMAP-Rule:MF_01836};
Repressor {ECO:0000256|HAMAP-Rule:MF_01836};
Serine/threonine-protein kinase {ECO:0000256|HAMAP-Rule:MF_01836};
Transcription {ECO:0000256|HAMAP-Rule:MF_01836};
Transcription regulation {ECO:0000256|HAMAP-Rule:MF_01836};
Transferase {ECO:0000256|HAMAP-Rule:MF_01836}.
DOMAIN 19 260 KaiC. {ECO:0000259|PROSITE:PS51146}.
DOMAIN 261 493 KaiC. {ECO:0000259|PROSITE:PS51146}.
NP_BIND 46 53 ATP. {ECO:0000256|HAMAP-Rule:MF_01836}.
NP_BIND 288 295 ATP. {ECO:0000256|HAMAP-Rule:MF_01836}.
METAL 295 295 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01836}.
METAL 318 318 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01836}.
METAL 319 319 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01836}.
METAL 378 378 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01836}.
MOD_RES 432 432 Phosphothreonine; by autocatalysis.
{ECO:0000256|HAMAP-Rule:MF_01836}.
SEQUENCE 513 AA; 57368 MW; 78C78D80DEB3A21D CRC64;
MNKTMKDKKF GKSNKMQVQK LPTGIEGFDD VCRGGLPVSR STLVSGTSGT GKTVFSLQYL
HHGICNFDEP GIFVTFEESP LDIIRNAASF GWDLQDLIDQ NKLFILDASP DPDGQDVAGN
FDLSGLIERI SYAIRKYKAK RVAIDSITAV FQQYDAIYVV RREIFRLIAR LKEIGVTTVM
TTERVDDYGP IARYGVEEFV SDNVVLLRNV LESEKRRRTL EVLKLRGTVH MKGEYPFTMG
ADGISVFALG AMRLTQSSSN IRISSGVKDL DDMCGGGYFQ DSIILATGAT GTGKTMLVSK
FVEDAYSNNE RAILFAYEES RAQLLRNATS WGIDFEKMES DGLLKIICAY PESTGLEDHL
QIIKTQINQF KPKRMAIDSL SALARGVSLN AFRQFVIAVT GYTKQEEIAG FFTNTAEEFM
GSHSITDSHI STITDTILLL QYVEIKGEMA RALNVFKMRG SWHDKRIREF IITNRGPEIK
DSFSNFEQIF SGAPHRVVPD QNVQNVFKGL DNN


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