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Q79PF6

- KAIA_SYNE7

UniProt

Q79PF6 - KAIA_SYNE7

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Protein

Circadian clock protein KaiA

Gene

kaiA

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

Functioni

Component of the KaiABC clock protein complex, which constitutes the main circadian regulator in cyanobacteria. The KaiABC complex may act as a promoter-nonspecific transcription regulator that represses transcription, possibly by acting on the state of chromosome compaction. In the complex, it enhances the phosphorylation status of KaiC. In contrast, the presence of KaiB in the complex decreases the phosphorylation status of KaiC, suggesting that KaiB acts by antagonizing the interaction between KaiA and KaiC. A KaiA dimer is sufficient to enhance KaiC hexamer phosphorylation.4 Publications

GO - Molecular functioni

  1. identical protein binding Source: IntAct

GO - Biological processi

  1. circadian rhythm Source: InterPro
  2. entrainment of circadian clock Source: UniProtKB
  3. negative regulation of protein dephosphorylation Source: CACAO
  4. positive regulation of circadian rhythm Source: UniProtKB
  5. protein phosphorylation Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Biological rhythms

Enzyme and pathway databases

BioCyciSYNEL:SYNPCC7942_1218-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Circadian clock protein KaiA
Gene namesi
Name:kaiA
Ordered Locus Names:Synpcc7942_1218
ORF Names:see0009
OrganismiSynechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2)
Taxonomic identifieri1140 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus
ProteomesiUP000002717: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi9 – 91I → T: Extends the period of the circadian rhythm to 29 hours. 1 Publication
Mutagenesisi16 – 161I → F: Extends the period of the circadian rhythm to 27 hours. 1 Publication
Mutagenesisi31 – 311L → P: Extends the period of the circadian rhythm to 27 hours. 1 Publication
Mutagenesisi36 – 361S → P: Extends the period of the circadian rhythm to 29 hours. 1 Publication
Mutagenesisi53 – 531C → S: Induces an arrhythmic phenotype. 1 Publication
Mutagenesisi76 – 761V → G: Extends the period of the circadian rhythm to 28 hours. 1 Publication
Mutagenesisi103 – 1031E → K in kaiA1; extends the period of the circadian rhythm to 33 hours and increases the interaction with KaiB.
Mutagenesisi113 – 1131Q → R: Extends the period of the circadian rhythm to 33 hours. 1 Publication
Mutagenesisi117 – 1171Q → L: Extends the period of the circadian rhythm to 26 hours. 1 Publication
Mutagenesisi119 – 1191D → E: Extends the period of the circadian rhythm to 30 hours. 1 Publication
Mutagenesisi119 – 1191D → G: Extends the period of the circadian rhythm to 26 hours. 1 Publication
Mutagenesisi131 – 1311V → A: Extends the period of the circadian rhythm to 28 hours. 1 Publication
Mutagenesisi136 – 1361D → V: Extends the period of the circadian rhythm to 30 hours. 1 Publication
Mutagenesisi136 – 1361D → Y: Extends the period of the circadian rhythm to 29 hours. 1 Publication
Mutagenesisi166 – 1661Y → C in kaiA3; induces an arrhythmic phenotype and reduces the interaction with KaiC.
Mutagenesisi178 – 1781F → S or I: Induces an arrhythmic phenotype. 1 Publication
Mutagenesisi180 – 1801R → H: Extends the period of the circadian rhythm to 26 hours. 1 Publication
Mutagenesisi194 – 1941M → T: Extends the period of the circadian rhythm to 26 hours. 1 Publication
Mutagenesisi224 – 2241F → S: Induces an arrhythmic phenotype. 1 Publication
Mutagenesisi225 – 2251F → S: Induces an arrhythmic phenotype. 1 Publication
Mutagenesisi239 – 2391E → G: Extends the period of the circadian rhythm to 28 hours. 1 Publication
Mutagenesisi241 – 2411M → T: Extends the period of the circadian rhythm to 38 hours. 1 Publication
Mutagenesisi242 – 2421D → V or G: Extends the period of the circadian rhythm to 27 hours. 1 Publication
Mutagenesisi243 – 2431E → A: Extends the period of the circadian rhythm to 34 hours. 1 Publication
Mutagenesisi244 – 2441F → V: Extends the period of the circadian rhythm to 26 hours. 1 Publication
Mutagenesisi245 – 2451A → D: Extends the period of the circadian rhythm to 26 hours. 1 Publication
Mutagenesisi249 – 2491R → H in kaiA1; extends the period of the circadian rhythm to 30 hours.
Mutagenesisi266 – 2661I → V: Extends the period of the circadian rhythm to 27 hours. 1 Publication
Mutagenesisi273 – 2731C → Y: Extends the period of the circadian rhythm to 30 hours. 1 Publication
Mutagenesisi274 – 2741E → K in kaiA3; induces an arrhythmic phenotype.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 284284Circadian clock protein KaiAPRO_0000217871Add
BLAST

Expressioni

Developmental stagei

Expressed constantly throughout the circadian cycle.1 Publication

Interactioni

Subunit structurei

Homodimer. Component of the KaiABC complex, at least composed of a KaiC homohexamer, a KaiB dimer and two KaiA dimers. The KaiABC complex also interacts with SasA.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-592281,EBI-592281
kaiBQ79PF59EBI-592281,EBI-619150
kaiCQ79PF417EBI-592281,EBI-592287
ldpAQ8GLI42EBI-592281,EBI-626836

Protein-protein interaction databases

DIPiDIP-33329N.
IntActiQ79PF6. 4 interactions.
STRINGi1140.Synpcc7942_1218.

Structurei

Secondary structure

1
284
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 106
Helixi14 – 2310
Beta strandi29 – 346
Helixi37 – 4610
Turni47 – 493
Beta strandi52 – 576
Helixi63 – 7210
Beta strandi79 – 835
Beta strandi87 – 893
Beta strandi98 – 1003
Beta strandi104 – 1063
Helixi108 – 1103
Helixi111 – 1133
Helixi114 – 12815
Turni134 – 1363
Beta strandi138 – 1403
Turni144 – 1474
Helixi149 – 1513
Helixi152 – 16413
Beta strandi165 – 1717
Helixi175 – 1773
Turni179 – 1813
Helixi184 – 20522
Helixi212 – 22514
Helixi230 – 24920
Turni250 – 2523
Helixi257 – 2615
Helixi262 – 27918

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M2ENMR-A1-135[»]
1M2FNMR-A1-135[»]
1R8JX-ray2.03A/B2-284[»]
4G86X-ray2.39A/B2-284[»]
ProteinModelPortaliQ79PF6.
SMRiQ79PF6. Positions 1-282.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ79PF6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 164164KaiA N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini174 – 282109KaiA C-terminalPROSITE-ProRule annotationAdd
BLAST

Domaini

The N-terminal part (1-102), which is also called pseudo-receiver domain, does not enhance KaiC autophosphorylation. It may have an amplitude-amplifier function and may be involved in transducing input signals to the KaiABC complex. This domain is not conserved in other species.1 Publication
The KaiA domain mediates the interaction with KaiC, the homodimerization, and is responsible for the clock oscillation function.1 Publication

Sequence similaritiesi

Contains 1 kaiA C-terminal domain.PROSITE-ProRule annotation
Contains 1 kaiA N-terminal domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG123092.
HOGENOMiHOG000276784.
KOiK08480.
OrthoDBiEOG65QWP2.

Family and domain databases

Gene3Di1.10.1240.30. 1 hit.
InterProiIPR011006. CheY-like_superfamily.
IPR011648. Circadian_clock_KaiA.
IPR020844. Circadian_clock_KaiA_N.
IPR020856. Circadian_clock_protein_KaiA_C.
IPR017944. KaiA/RbsU_helical_domain.
[Graphical view]
PfamiPF07688. KaiA. 1 hit.
[Graphical view]
SUPFAMiSSF101215. SSF101215. 1 hit.
SSF52172. SSF52172. 1 hit.
PROSITEiPS51431. KAIA_C. 1 hit.
PS51430. KAIA_N. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q79PF6 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLSQIAICIW VESTAILQDC QRALSADRYQ LQVCESGEML LEYAQTHRDQ
60 70 80 90 100
IDCLILVAAN PSFRAVVQQL CFEGVVVPAI VVGDRDSEDP DEPAKEQLYH
110 120 130 140 150
SAELHLGIHQ LEQLPYQVDA ALAEFLRLAP VETMADHIML MGANHDPELS
160 170 180 190 200
SQQRDLAQRL QERLGYLGVY YKRDPDRFLR NLPAYESQKL HQAMQTSYRE
210 220 230 240 250
IVLSYFSPNS NLNQSIDNFV NMAFFADVPV TKVVEIHMEL MDEFAKKLRV
260 270 280
EGRSEDILLD YRLTLIDVIA HLCEMYRRSI PRET
Length:284
Mass (Da):32,632
Last modified:July 5, 2004 - v1
Checksum:i7C4F3B79FFDF59A2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB010691 Genomic DNA. Translation: BAA37101.1.
AY120853 Genomic DNA. Translation: AAM82684.1.
CP000100 Genomic DNA. Translation: ABB57248.1.
PIRiT44267.
RefSeqiYP_400235.1. NC_007604.1.

Genome annotation databases

EnsemblBacteriaiABB57248; ABB57248; Synpcc7942_1218.
GeneIDi3773506.
KEGGisyf:Synpcc7942_1218.
PATRICi23787743. VBISynElo51371_1400.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB010691 Genomic DNA. Translation: BAA37101.1 .
AY120853 Genomic DNA. Translation: AAM82684.1 .
CP000100 Genomic DNA. Translation: ABB57248.1 .
PIRi T44267.
RefSeqi YP_400235.1. NC_007604.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1M2E NMR - A 1-135 [» ]
1M2F NMR - A 1-135 [» ]
1R8J X-ray 2.03 A/B 2-284 [» ]
4G86 X-ray 2.39 A/B 2-284 [» ]
ProteinModelPortali Q79PF6.
SMRi Q79PF6. Positions 1-282.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-33329N.
IntActi Q79PF6. 4 interactions.
STRINGi 1140.Synpcc7942_1218.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABB57248 ; ABB57248 ; Synpcc7942_1218 .
GeneIDi 3773506.
KEGGi syf:Synpcc7942_1218.
PATRICi 23787743. VBISynElo51371_1400.

Phylogenomic databases

eggNOGi NOG123092.
HOGENOMi HOG000276784.
KOi K08480.
OrthoDBi EOG65QWP2.

Enzyme and pathway databases

BioCyci SYNEL:SYNPCC7942_1218-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q79PF6.

Family and domain databases

Gene3Di 1.10.1240.30. 1 hit.
InterProi IPR011006. CheY-like_superfamily.
IPR011648. Circadian_clock_KaiA.
IPR020844. Circadian_clock_KaiA_N.
IPR020856. Circadian_clock_protein_KaiA_C.
IPR017944. KaiA/RbsU_helical_domain.
[Graphical view ]
Pfami PF07688. KaiA. 1 hit.
[Graphical view ]
SUPFAMi SSF101215. SSF101215. 1 hit.
SSF52172. SSF52172. 1 hit.
PROSITEi PS51431. KAIA_C. 1 hit.
PS51430. KAIA_N. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Expression of a gene cluster kaiABC as a circadian feedback process in cyanobacteria."
    Ishiura M., Kutsuna S., Aoki S., Iwasaki H., Andersson C.R., Tanabe A., Golden S.S., Johnson C.H., Kondo T.
    Science 281:1519-1523(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, MUTANTS KAIA1; KAIA2 AND KAIA3.
  2. "Synechococcus elongatus PCC7942 cosmid 7G3."
    Holtman C.K., Sandoval P., Chen Y., Socias T., Mohler B.J., McMurtry S., Gonzalez A., Salinas I., Golden S.S., Youderian P.
    Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942."
    US DOE Joint Genome Institute
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PCC 7942.
  4. "Physical interactions among circadian clock proteins KaiA, KaiB and KaiC in cyanobacteria."
    Iwasaki H., Taniguchi Y., Ishiura M., Kondo T.
    EMBO J. 18:1137-1145(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KAIC AND KAIB, MUTANT KAIA1.
  5. "Two KaiA-binding domains of cyanobacterial circadian clock protein KaiC."
    Taniguchi Y., Yamaguchi A., Hijikata A., Iwasaki H., Kamagata K., Ishiura M., Go M., Kondo T.
    FEBS Lett. 496:86-90(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KAIC, MUTANTS KAIA2 AND KAIA4.
  6. "Mutations in KaiA, a clock protein, extend the period of circadian rhythm in the cyanobacterium Synechococcus elongatus PCC 7942."
    Nishimura H., Nakahira Y., Imai K., Tsuruhara A., Kondo H., Hayashi H., Hirai M., Saito H., Kondo T.
    Microbiology 148:2903-2909(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ILE-9; ILE-16; LEU-31; SER-36; CYS-53; VAL-76; GLN-113; GLN-117; ASP-119; VAL-131; ASP-136; PHE-178; ARG-180; MET-194; PHE-224; PHE-225; GLU-239; MET-241; ASP-242; GLU-243; PHE-244; ALA-245; ILE-266 AND CYS-273.
  7. "KaiA-stimulated KaiC phosphorylation in circadian timing loops in cyanobacteria."
    Iwasaki H., Nishiwaki T., Kitayama Y., Nakajima M., Kondo T.
    Proc. Natl. Acad. Sci. U.S.A. 99:15788-15793(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Cyanobacterial circadian clockwork: roles of KaiA, KaiB and the kaiBC promoter in regulating KaiC."
    Xu Y., Mori T., Johnson C.H.
    EMBO J. 22:2117-2126(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "KaiB functions as an attenuator of KaiC phosphorylation in the cyanobacterial circadian clock system."
    Kitayama Y., Iwasaki H., Nishiwaki T., Kondo T.
    EMBO J. 22:2127-2134(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DEVELOPMENTAL STAGE.
  10. "Stoichiometric interactions between cyanobacterial clock proteins KaiA and KaiC."
    Hayashi F., Ito H., Fujita M., Iwase R., Uzumaki T., Ishiura M.
    Biochem. Biophys. Res. Commun. 316:195-202(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STOICHIOMETRY OF THE COMPLEX FORMED WITH KAIC.
  11. "Structure and function from the circadian clock protein KaiA of Synechococcus elongatus: a potential clock input mechanism."
    Williams S.B., Vakonakis I., Golden S.S., LiWang A.C.
    Proc. Natl. Acad. Sci. U.S.A. 99:15357-15362(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-135.
  12. Erratum
    Williams S.B., Vakonakis I., Golden S.S., LiWang A.C.
    Proc. Natl. Acad. Sci. U.S.A. 100:763-763(2003)
  13. "Crystal structure of circadian clock protein KaiA from Synechococcus elongatus."
    Ye S., Vakonakis I., Ioerger T.R., LiWang A.C., Sacchettini J.C.
    J. Biol. Chem. 279:20511-20518(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 2-284, HOMODIMERIZATION, DOMAIN.

Entry informationi

Entry nameiKAIA_SYNE7
AccessioniPrimary (citable) accession number: Q79PF6
Secondary accession number(s): Q31NX1, Q9Z3H4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: July 5, 2004
Last modified: October 29, 2014
This is version 76 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.

Caution

PubMed:15007067 structure is derived from this sequence and not from the one of S.elongatus.Curated

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

External Data

Dasty 3