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Protein

Circadian clock protein kinase KaiC

Gene

kaiC

Organism
Synechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Core component of the KaiABC clock protein complex, which constitutes the main circadian regulator in cyanobacteria. Binds to DNA. The KaiABC complex may act as a promoter-nonspecific transcription regulator that represses transcription, possibly by acting on the state of chromosome compaction.2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Mg2+1 Publication

Enzyme regulationi

The interaction with KaiA enhances its phosphorylation status, while the interaction with KaiB decreases it. A KaiA dimer is sufficient to enhance KaiC phosphorylation.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi295Magnesium1
Metal bindingi318Magnesium1
Metal bindingi319Magnesium1
Metal bindingi378Magnesium1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi46 – 53ATP8
Nucleotide bindingi288 – 295ATP8

GO - Molecular functioni

GO - Biological processi

  • circadian rhythm Source: UniProtKB-HAMAP
  • entrainment of circadian clock Source: UniProtKB
  • negative regulation of circadian rhythm Source: UniProtKB
  • regulation of phosphorelay signal transduction system Source: CACAO
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Repressor, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Biological rhythms, Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, DNA-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciSYNEL:SYNPCC7942_1216-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Circadian clock protein kinase KaiC (EC:2.7.11.1)
Gene namesi
Name:kaiC
Ordered Locus Names:Synpcc7942_1216
ORF Names:see0011
OrganismiSynechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2)
Taxonomic identifieri1140 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaSynechococcalesSynechococcaceaeSynechococcus
Proteomesi
  • UP000002717 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi52K → A: Induces an arrhythmic phenotype. 1 Publication1
Mutagenesisi71G → A: Lowers the amplitude and distords the waveform of the circadian rhythm. 1 Publication1
Mutagenesisi87A → V in kaiC1; shortens the period of the circadian rhythm to 22 hours. 1
Mutagenesisi114G → A: Extends the period of the circadian rhythm to 27 hours. 1 Publication1
Mutagenesisi115Q → A: Abolishes the circadian rhythm. 1 Publication1
Mutagenesisi157S → C in kaiC2; extends the period of the circadian rhythm to 29 hours. 1
Mutagenesisi215R → C in kaiC3; shortens the period of the circadian rhythm to 16 hours and decreases the interaction with KaiA. 1
Mutagenesisi236P → S in kaiC4; extends the period of the circadian rhythm to 28 hours. 1
Mutagenesisi248P → L in kaiC6; induces a low amplitude phenotype and decreases the interaction with KaiA. 1
Mutagenesisi248P → S in kaiC5; induces an arrhythmic phenotype. 1
Mutagenesisi253R → H in kaiC7; extends the period of the circadian rhythm to 40 hours. 1
Mutagenesisi273M → I in kaiC8; extends the period of the circadian rhythm to 37 hours. 1
Mutagenesisi294K → A: Induces a long period phenotype. 1 Publication1
Mutagenesisi321R → Q in kaiC9; shortens the period of the circadian rhythm to 21 hours. 1
Mutagenesisi409T → A in kaiC10; extends the period of the circadian rhythm to 27 hours. 1
Mutagenesisi421G → R in kaiC11; extends the period of the circadian rhythm to 44 hours and increases the interaction with KaiA. 1
Mutagenesisi422A → T in kaiC15; able to suppress the kaiA2 extended phenotype. 1
Mutagenesisi432T → A: Loss of function. 1 Publication1
Mutagenesisi442Y → H in kaiC12; extends the period of the circadian rhythm to 60 hours and increases the interaction with KaiA. 1
Mutagenesisi460G → E in kaiC13; induces an arrhythmic phenotype. 1
Mutagenesisi495T → A in kaiC14; induces an arrhythmic phenotype. 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002177821 – 519Circadian clock protein kinase KaiCAdd BLAST519

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei432Phosphothreonine; by autocatalysis1 Publication1

Post-translational modificationi

Phosphorylated on serine/threonine residues by autocatalysis. Both phosphorylated and unphosphorylated forms exist. Can probably autophosphorylate and autodephosphorylate. Phosphorylated form correlates with clock speed.3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiQ79PF4.

PTM databases

iPTMnetiQ79PF4.

Expressioni

Developmental stagei

Accumulates in a circadian fashion, peaking at circadian time (CT) 15-18.1 Publication

Inductioni

Down-regulated by itself.1 Publication

Interactioni

Subunit structurei

Homohexamer; hexamerization is dependent on ATP-binding. Core component of the KaiABC complex, at least composed of a KaiC homohexamer, a KaiB dimer and two KaiA dimers. Interacts directly with SasA.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself9EBI-592287,EBI-592287
kaiAQ79PF617EBI-592287,EBI-592281
kaiBQ79PF510EBI-592287,EBI-619150
sasAQ069046EBI-592287,EBI-626872

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

DIPiDIP-33330N.
IntActiQ79PF4. 3 interactors.
MINTiMINT-8094424.
STRINGi1140.Synpcc7942_1216.

Structurei

Secondary structure

1519
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi28 – 31Combined sources4
Beta strandi34 – 37Combined sources4
Beta strandi40 – 47Combined sources8
Helixi52 – 67Combined sources16
Beta strandi71 – 78Combined sources8
Helixi80 – 87Combined sources8
Helixi88 – 90Combined sources3
Helixi94 – 99Combined sources6
Beta strandi102 – 107Combined sources6
Beta strandi119 – 121Combined sources3
Helixi123 – 137Combined sources15
Beta strandi140 – 145Combined sources6
Helixi147 – 153Combined sources7
Helixi157 – 174Combined sources18
Beta strandi177 – 183Combined sources7
Beta strandi187 – 189Combined sources3
Beta strandi191 – 195Combined sources5
Helixi197 – 200Combined sources4
Beta strandi202 – 212Combined sources11
Beta strandi215 – 225Combined sources11
Beta strandi233 – 240Combined sources8
Beta strandi243 – 246Combined sources4
Turni249 – 251Combined sources3
Helixi268 – 273Combined sources6
Beta strandi276 – 281Combined sources6
Beta strandi283 – 288Combined sources6
Helixi294 – 306Combined sources13
Turni307 – 309Combined sources3
Beta strandi312 – 319Combined sources8
Helixi321 – 329Combined sources9
Turni330 – 332Combined sources3
Helixi335 – 340Combined sources6
Beta strandi343 – 346Combined sources4
Helixi351 – 353Combined sources3
Helixi356 – 368Combined sources13
Beta strandi373 – 378Combined sources6
Helixi380 – 383Combined sources4
Beta strandi385 – 387Combined sources3
Helixi389 – 405Combined sources17
Beta strandi409 – 415Combined sources7
Beta strandi417 – 420Combined sources4
Beta strandi423 – 429Combined sources7
Turni431 – 433Combined sources3
Beta strandi435 – 445Combined sources11
Beta strandi448 – 461Combined sources14
Beta strandi468 – 472Combined sources5
Beta strandi477 – 482Combined sources6
Beta strandi486 – 488Combined sources3
Helixi489 – 491Combined sources3
Helixi501 – 512Combined sources12
Beta strandi514 – 516Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TF7X-ray2.80A/B/C/D/E/F1-519[»]
1U9IX-ray2.80A/B/C/D/E/F1-519[»]
2GBLX-ray2.80A/B/C/D/E/F1-519[»]
3DVLX-ray2.80A/B/C/D/E/F1-519[»]
3JZMX-ray2.90A/B/C/D/E/F1-519[»]
3K09X-ray3.20A/B/C/D/E/F1-519[»]
3K0AX-ray3.00A/B/C/D/E/F1-519[»]
3K0CX-ray3.30A/B/C/D/E/F1-519[»]
3K0EX-ray3.20A/B/C/D/E/F1-519[»]
3K0FX-ray3.00A/B/C/D/E/F1-519[»]
3S1AX-ray3.00A/B/C/D/E/F1-519[»]
4DUGX-ray3.30A/B/C/D/E/F1-519[»]
4IJMX-ray3.35A/B/C/D/E/F14-519[»]
4TL6X-ray1.76A/B/C1-253[»]
4TL7X-ray1.94A/B/C/D/E/F1-253[»]
4TL8X-ray1.86A/B/C/D/E/F1-253[»]
4TL9X-ray1.82A/B/C/D/E/F1-253[»]
4TLAX-ray1.80A/B/C/D/E/F1-253[»]
4TLBX-ray1.98A/B/C/D/E/F1-253[»]
4TLCX-ray2.09A/B/C/D/E/F1-253[»]
4TLDX-ray1.95A/B/C/D/E/F1-253[»]
4TLEX-ray1.94A/B/C/D/E/F1-253[»]
5C5EX-ray2.82G/H500-519[»]
ProteinModelPortaliQ79PF4.
SMRiQ79PF4.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ79PF4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini19 – 260KaiC 1Add BLAST242
Domaini261 – 493KaiC 2Add BLAST233

Domaini

The KaiC domains mediate the interaction with KaiA.

Sequence similaritiesi

Belongs to the KaiC family.Curated
Contains 2 kaiC domains.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG4105EHU. Bacteria.
COG0467. LUCA.
HOGENOMiHOG000230416.
KOiK08482.
OrthoDBiPOG091H0SAA.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
HAMAPiMF_01836. KaiC. 1 hit.
InterProiIPR013503. Circadian_KaiC_bact.
IPR030665. KaiC.
IPR014774. KaiC-like_dom.
IPR010624. KaiC_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF06745. ATPase. 2 hits.
[Graphical view]
PIRSFiPIRSF039117. KaiC. 1 hit.
SUPFAMiSSF52540. SSF52540. 2 hits.
TIGRFAMsiTIGR02655. circ_KaiC. 1 hit.
PROSITEiPS51146. KAIC. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q79PF4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSAEMTSPN NNSEHQAIAK MRTMIEGFDD ISHGGLPIGR STLVSGTSGT
60 70 80 90 100
GKTLFSIQFL YNGIIEFDEP GVFVTFEETP QDIIKNARSF GWDLAKLVDE
110 120 130 140 150
GKLFILDASP DPEGQEVVGG FDLSALIERI NYAIQKYRAR RVSIDSVTSV
160 170 180 190 200
FQQYDASSVV RRELFRLVAR LKQIGATTVM TTERIEEYGP IARYGVEEFV
210 220 230 240 250
SDNVVILRNV LEGERRRRTL EILKLRGTSH MKGEYPFTIT DHGINIFPLG
260 270 280 290 300
AMRLTQRSSN VRVSSGVVRL DEMCGGGFFK DSIILATGAT GTGKTLLVSR
310 320 330 340 350
FVENACANKE RAILFAYEES RAQLLRNAYS WGMDFEEMER QNLLKIVCAY
360 370 380 390 400
PESAGLEDHL QIIKSEINDF KPARIAIDSL SALARGVSNN AFRQFVIGVT
410 420 430 440 450
GYAKQEEITG LFTNTSDQFM GAHSITDSHI STITDTIILL QYVEIRGEMS
460 470 480 490 500
RAINVFKMRG SWHDKAIREF MISDKGPDIK DSFRNFERII SGSPTRITVD
510
EKSELSRIVR GVQEKGPES
Length:519
Mass (Da):58,003
Last modified:July 5, 2004 - v1
Checksum:i855DFE131EFFF3CF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB010691 Genomic DNA. Translation: BAA37103.1.
AY120853 Genomic DNA. Translation: AAM82686.1.
CP000100 Genomic DNA. Translation: ABB57246.1.
PIRiT44269.
RefSeqiWP_011242648.1. NC_007604.1.

Genome annotation databases

EnsemblBacteriaiABB57246; ABB57246; Synpcc7942_1216.
KEGGisyf:Synpcc7942_1216.
PATRICi23787739. VBISynElo51371_1398.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB010691 Genomic DNA. Translation: BAA37103.1.
AY120853 Genomic DNA. Translation: AAM82686.1.
CP000100 Genomic DNA. Translation: ABB57246.1.
PIRiT44269.
RefSeqiWP_011242648.1. NC_007604.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TF7X-ray2.80A/B/C/D/E/F1-519[»]
1U9IX-ray2.80A/B/C/D/E/F1-519[»]
2GBLX-ray2.80A/B/C/D/E/F1-519[»]
3DVLX-ray2.80A/B/C/D/E/F1-519[»]
3JZMX-ray2.90A/B/C/D/E/F1-519[»]
3K09X-ray3.20A/B/C/D/E/F1-519[»]
3K0AX-ray3.00A/B/C/D/E/F1-519[»]
3K0CX-ray3.30A/B/C/D/E/F1-519[»]
3K0EX-ray3.20A/B/C/D/E/F1-519[»]
3K0FX-ray3.00A/B/C/D/E/F1-519[»]
3S1AX-ray3.00A/B/C/D/E/F1-519[»]
4DUGX-ray3.30A/B/C/D/E/F1-519[»]
4IJMX-ray3.35A/B/C/D/E/F14-519[»]
4TL6X-ray1.76A/B/C1-253[»]
4TL7X-ray1.94A/B/C/D/E/F1-253[»]
4TL8X-ray1.86A/B/C/D/E/F1-253[»]
4TL9X-ray1.82A/B/C/D/E/F1-253[»]
4TLAX-ray1.80A/B/C/D/E/F1-253[»]
4TLBX-ray1.98A/B/C/D/E/F1-253[»]
4TLCX-ray2.09A/B/C/D/E/F1-253[»]
4TLDX-ray1.95A/B/C/D/E/F1-253[»]
4TLEX-ray1.94A/B/C/D/E/F1-253[»]
5C5EX-ray2.82G/H500-519[»]
ProteinModelPortaliQ79PF4.
SMRiQ79PF4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-33330N.
IntActiQ79PF4. 3 interactors.
MINTiMINT-8094424.
STRINGi1140.Synpcc7942_1216.

PTM databases

iPTMnetiQ79PF4.

Proteomic databases

PRIDEiQ79PF4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABB57246; ABB57246; Synpcc7942_1216.
KEGGisyf:Synpcc7942_1216.
PATRICi23787739. VBISynElo51371_1398.

Phylogenomic databases

eggNOGiENOG4105EHU. Bacteria.
COG0467. LUCA.
HOGENOMiHOG000230416.
KOiK08482.
OrthoDBiPOG091H0SAA.

Enzyme and pathway databases

BioCyciSYNEL:SYNPCC7942_1216-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ79PF4.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
HAMAPiMF_01836. KaiC. 1 hit.
InterProiIPR013503. Circadian_KaiC_bact.
IPR030665. KaiC.
IPR014774. KaiC-like_dom.
IPR010624. KaiC_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF06745. ATPase. 2 hits.
[Graphical view]
PIRSFiPIRSF039117. KaiC. 1 hit.
SUPFAMiSSF52540. SSF52540. 2 hits.
TIGRFAMsiTIGR02655. circ_KaiC. 1 hit.
PROSITEiPS51146. KAIC. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiKAIC_SYNE7
AccessioniPrimary (citable) accession number: Q79PF4
Secondary accession number(s): Q31NX3, Q9Z3H2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: July 5, 2004
Last modified: November 2, 2016
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

'Kai' means 'cycle' in Japanese.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.