Summary: KaiB domain
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This is the Wikipedia entry entitled "Cyanobacterial clock proteins". More...
Cyanobacterial clock proteins Edit Wikipedia article
| KaiA domain | |||||||||
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| crystal structure of circadian clock protein kaia from synechococcus elongatus | |||||||||
| Identifiers | |||||||||
| Symbol | KaiA | ||||||||
| Pfam | PF07688 | ||||||||
| InterPro | IPR011648 | ||||||||
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| KaiB domain | |||||||||
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| solution structure of the n-terminal domain of synechococcus elongatus sasa (average minimized structure) | |||||||||
| Identifiers | |||||||||
| Symbol | KaiB | ||||||||
| Pfam | PF07689 | ||||||||
| Pfam clan | CL0172 | ||||||||
| InterPro | IPR011649 | ||||||||
| CDD | cd02978 | ||||||||
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| KaiC | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| crystal structure of full length circadian clock protein kaic with phosphorylation sites | |||||||||
| Identifiers | |||||||||
| Symbol | KaiC | ||||||||
| Pfam | PF06745 | ||||||||
| Pfam clan | CL0023 | ||||||||
| InterPro | IPR014774 | ||||||||
| CDD | cd01124 | ||||||||
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In molecular biology, the cyanobacterial clock proteins are the main circadian regulator in cyanobacteria. The cyanobacterial clock proteins comprise three proteins: kiaA, kiaB and kiaC. 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, KaiA 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 antagonising the interaction between kaiA and kaiC. The activity of KaiA activates kaiBC expression, while KaiC represses it. The overall fold of the KaiA monomer is that of a four-helix bundle, which forms a dimer in the known structure.[1] KaiA functions as a homodimer. Each monomer is composed of three functional domains: the N-terminal amplitude-amplifier domain, the central period-adjuster domain and the C-terminal clock-oscillator domain. The N-terminal domain of KaiA, from cyanobacteria, acts as a pseudo-receiver domain, but lacks the conserved aspartyl residue required for phosphotransfer in response regulators.[2] The C-terminal domain is responsible for dimer formation, binding to KaiC, enhancing KaiC phosphorylation and generating the circadian oscillations.[3] The KaiA protein from Anabaena sp. (strain PCC 7120) lacks the N-terminal CheY-like domain.
KaiB adopts an alpha-beta meander motif and is found to be a dimer or a tetramer.[1][4]
KaiC belongs to a larger family of proteins; it performs autophosphorylation and acts as its own transcriptional repressor. It binds ATP.[5]
Also in the KiaC family is RadA/Sms, a highly conserved eubacterial protein that shares sequence similarity with both RecA strand transferase and lon protease. The RadA/Sms family are probable ATP-dependent proteases involved in both DNA repair and degradation of proteins, peptides, glycopeptides. They are classified in as non-peptidase homologues and unassigned peptidases in MEROPS peptidase family S16 (lon protease family, clan SJ). RadA/Sms is involved in recombination and recombinational repair, most likely involving the stabilisation or processing of branched DNA molecules or blocked replication forks because of its genetic redundancy with RecG and RuvABC.[6]
[edit] References
- ^ a b Garces RG, Wu N, Gillon W, Pai EF (April 2004). "Anabaena circadian clock proteins KaiA and KaiB reveal a potential common binding site to their partner KaiC". EMBO J. 23 (8): 1688â98. doi:10.1038/sj.emboj.7600190. PMC 394244. PMID 15071498. //www.ncbi.nlm.nih.gov/pmc/articles/PMC394244/.
- ^ Williams SB, Vakonakis I, Golden SS, LiWang AC (November 2002). "Structure and function from the circadian clock protein KaiA of Synechococcus elongatus: a potential clock input mechanism". Proc. Natl. Acad. Sci. U.S.A. 99 (24): 15357â62. doi:10.1073/pnas.232517099. PMC 137721. PMID 12438647. //www.ncbi.nlm.nih.gov/pmc/articles/PMC137721/.
- ^ Uzumaki T, Fujita M, Nakatsu T, Hayashi F, Shibata H, Itoh N, Kato H, Ishiura M (July 2004). "Crystal structure of the C-terminal clock-oscillator domain of the cyanobacterial KaiA protein". Nat. Struct. Mol. Biol. 11 (7): 623â31. doi:10.1038/nsmb781. PMID 15170179.
- ^ Hitomi K, Oyama T, Han S, Arvai AS, Getzoff ED (2005). "Tetrameric architecture of the circadian clock protein KaiB. A novel interface for intermolecular interactions and its impact on the circadian rhythm.". J Biol Chem 280 (19): 19127â35. doi:10.1074/jbc.M411284200. PMID 15716274. http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=15716274.
- ^ Pattanayek R, Wang J, Mori T, Xu Y, Johnson CH, Egli M (2004). "Visualizing a circadian clock protein: crystal structure of KaiC and functional insights.". Mol Cell 15 (3): 375â88. doi:10.1016/j.molcel.2004.07.013. PMID 15304218. http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=15304218.
- ^ Beam CE, Saveson CJ, Lovett ST (December 2002). "Role for radA/sms in recombination intermediate processing in Escherichia coli". J. Bacteriol. 184 (24): 6836â44. PMC 135464. PMID 12446634. //www.ncbi.nlm.nih.gov/pmc/articles/PMC135464/.
This article incorporates text from the public domain Pfam and InterPro IPR011648
This article incorporates text from the public domain Pfam and InterPro IPR011649
This article incorporates text from the public domain Pfam and InterPro IPR014774
This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.
This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
KaiB domain Provide feedback
The cyanobacterial clock proteins KaiA and KaiB are proposed as regulators of the circadian rhythm in cyanobacteria. Mutations in both proteins have been reported to alter or abolish circadian rhythmicity. KaiB adopts an alpha-beta meander motif and is found to be a dimer [1].
Literature references
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Garces RG, Wu N, Gillon W, Pai EF; , EMBO J 2004;23:1688-1698.: Anabaena circadian clock proteins KaiA and KaiB reveal a potential common binding site to their partner KaiC. PUBMED:15071498 EPMC:15071498
External database links
| PANDIT: | PF07689 |
| Pseudofam: | PF07689 |
| SYSTERS: | KaiB |
This tab holds annotation information from the InterPro database.
InterPro entry IPR011649
The cyanobacterial clock proteins KaiA and KaiB are proposed as regulators of the circadian rhythm in cyanobacteria. Mutations in both proteins have been reported to alter or abolish circadian rhythmicity. KaiB adopts an alpha-beta meander motif and is found to be a dimer [PUBMED:15071498].Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Biological process | rhythmic process (GO:0048511) |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Pfam Clan
This family is a member of clan Thioredoxin (CL0172), which contains the following 45 members:
2Fe-2S_thioredx AhpC-TSA AhpC-TSA_2 ArsC ArsD Calsequestrin DIM1 DSBA DUF1525 DUF1687 DUF2703 DUF4174 DUF836 DUF899 DUF953 ERp29_N Glutaredoxin GSHPx GST_N GST_N_2 GST_N_3 HyaE KaiB MRP-S23 MRP-S25 OST3_OST6 Phosducin Redoxin SCO1-SenC SelP_N SH3BGR T4_deiodinase Thioredox_DsbH Thioredoxin Thioredoxin_2 Thioredoxin_3 Thioredoxin_4 Thioredoxin_5 Thioredoxin_6 Thioredoxin_7 Thioredoxin_8 Thioredoxin_9 Tom37 TraF YtfJ_HI0045Alignments
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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
| Seed (16) |
Full (352) |
Representative proteomes | NCBI (572) |
Meta (244) |
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| RP15 (31) |
RP35 (86) |
RP55 (113) |
RP75 (129) |
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| Jalview | ||||||||
| HTML | ||||||||
| PP/heatmap | 1 | |||||||
| Pfam viewer | ||||||||
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
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| Seed (16) |
Full (352) |
Representative proteomes | NCBI (572) |
Meta (244) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (31) |
RP35 (86) |
RP55 (113) |
RP75 (129) |
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| Raw Stockholm | ||||||||
| Gzipped | ||||||||
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.
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Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
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Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
| Seed source: | Bateman A |
| Previous IDs: | none |
| Type: | Domain |
| Author: | Bateman A |
| Number in seed: | 16 |
| Number in full: | 352 |
| Average length of the domain: | 80.00 aa |
| Average identity of full alignment: | 41 % |
| Average coverage of the sequence by the domain: | 45.47 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 82 | ||||||||||||
| Family (HMM) version: | 7 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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Interactions
There is 1 interaction for this family. More...
KaiBStructures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the KaiB domain has been found. There are 18 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence