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Protein data for KAIC_ANASP:

Description:
Circadian clock protein kinase kaiC (EC 2.7.1.37).

Molecular weight: 57920

View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):

DNA repair( GO:0006281 )


Important dates:
11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
07-MAR-2006, entry version 20.

Phylogenetic order:
Bacteria Cyanobacteria Nostocales Nostocaceae Nostoc.

To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html

Links to references in other databases for protein KAIC_ANASP:

DatabasePointerAdd. info#1Add. info#2
EMBLAB071284BAB85869.1-
EMBLBA000019BAB74585.1-
PIRAG2166AG2166.
SMRQ8YT4016-496.1
GenomeReviewsBA000019_GRalr2886.1
BioCycNSP103690:ALR2886-MONOMER-.1
HAMAPMF_01836-1.
InterProIPR010624KaiC.
InterProIPR004504RadA.
PfamPF06745KaiC2.
PRINTSPR01874DNAREPAIRADA.
PROSITEPS51146KAIC2.

General information about the databases mentioned above

Keywords:
ATP-binding; Biological rhythms; Complete proteome; DNA-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding; Phosphorylation; Repeat; Repressor; Serine/threonine-protein kinase; Transcription; Transcription regulation; Transferase.

References:
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15170179; DOI=10.1038/nsmb781;
RA Uzumaki T., Fujita M., Nakatsu T., Hayashi F., Shibata H., Itoh N.,
RA Kato H., Ishiura M.;
RT "Crystal structure of the C-terminal clock-oscillator domain of the
RT cyanobacterial KaiA protein.";
RL Nat. Struct. Mol. Biol. 11:623-631(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX MEDLINE=21595285; PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S.,
RA Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T.,
RA Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
RA Nakazaki N., Shimpo S., Sugimoto M., Takazawa M., Yamada M.,
RA Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).

Feature:
CHAIN 1 519 Circadian clock protein kinase kaiC.
/FTId=PRO_0000217775.
DOMAIN 18 259 KaiC 1.
DOMAIN 260 492 KaiC 2.
NP_BIND 45 52 ATP (By similarity).
NP_BIND 287 294 ATP (By similarity).
METAL 294 294 Magnesium (By similarity).
METAL 317 317 Magnesium (By similarity).
METAL 318 318 Magnesium (By similarity).
METAL 377 377 Magnesium (By similarity).
MOD_RES 431 431 Phosphothreonine (by autocatalysis) (By
similarity).

Comments:
-!- FUNCTION: 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 (By similarity).
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR: Magnesium (By similarity).
-!- ENZYME REGULATION: The interaction with kaiA enhances its
phosphorylation status, while the interaction with kaiB decreases
it. A kaiA dimer is sufficient to enhance kaiC phosphorylation (By
similarity).
-!- SUBUNIT: 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 (By similarity).
-!- DOMAIN: The kaiC domains mediate the interaction with kaiA (By
similarity).
-!- 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 (By similarity).
-!- SIMILARITY: Belongs to the kaiC family.
-!- SIMILARITY: Contains 2 kaiC domains.
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Sequence length: 519

     MSEKEQQEQQ NTSGNGVEKI RTMIEGFDDI SHGGLPVGRT TLVSGTSGTG KTLLSLQFLF
     NGISFFDEPG VFVTFEESPS DIIKNAHIFG WNLQRLINEG KLFILDASPD PEGQDIVGNF
     DLSALIERLQ YAIRKYKAKR VSIDSITAVF QQYEAVGVVR REIFRLVARL KQLNVTTIIT
     TERSEEYGPV ASFGVEEFVS DNVVIARNVL EGERRRRTIE ILKLRGTTHM KGEYPFTITN
     DGVNIFPLGA MRLTQRSSNV RVSSGVKTLD GMCGGGFFKD SIILATGATG TGKTLLVSKF
     LQNGCVNNER AILFAYEESR AQLSRNAYSW GIDFEELESQ GLLKIICTYP ESTGLEDHLQ
     IIKSEIAYFK PARIAIDSLS ALARGVSNNA FRQFVIGVTG YAKQEEITGF FTNTTDQFMG
     SHSITDSHIS TITDTILMLQ YVEIRGEMSR AINVFKMRGS WHDKGIREYN ITADGPEIQD
     SFRNYERIVS GSPTRVSIDE KAELSRIVRR FEDKQGSDS

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