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44  structures 1070  species 0  interactions 4642  sequences 302  architectures

Family: BRCT_2 (PF16589)

Summary: BRCT domain, a BRCA1 C-terminus domain

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This is the Wikipedia entry entitled "BRCT domain". More...

BRCT domain Edit Wikipedia article

BRCA1 C Terminus (BRCT) domain
PDB 1cdz EBI.jpg
Structure of an XRCC1 BRCT domain.[1]
Identifiers
Symbol BRCT
Pfam PF00533
InterPro IPR001357
SCOP 1cdz
SUPERFAMILY 1cdz
CDD cd00027

BRCA1 C Terminus (BRCT) domain is a family of evolutionarily related proteins.

The BRCT domain (after the C_terminal domain of a breast cancer susceptibility protein) is found predominantly in proteins involved in cell cycle checkpoint functions responsive to DNA damage,[2] for example as found in the breast cancer DNA-repair protein BRCA1. The domain is an approximately 100 amino acid tandem repeat, which appears to act as a phospho-protein binding domain.[3]

Examples

Human proteins containing this domain include:

References

  1. ^ Zhang X, Moréra S, Bates PA, et al. (November 1998). "Structure of an XRCC1 BRCT domain: a new protein-protein interaction module". EMBO J. 17 (21): 6404–11. PMC 1170965Freely accessible. PMID 9799248. doi:10.1093/emboj/17.21.6404. 
  2. ^ Bork P, Hofmann K, Koonin EV, Bucher P, Neuwald AF, Altschul SF (1997). "A superfamily of conserved domains in DNA damage-responsive cell cycle checkpoint proteins". FASEB J. 11 (1): 68–76. PMID 9034168. 
  3. ^ Yu X, Chini CC, He M, Mer G, Chen J (2003). "The BRCT domain is a phospho-protein binding domain". Science. 302 (5645): 639–642. PMID 14576433. doi:10.1126/science.1088753. 

External links

This article incorporates text from the public domain Pfam and InterPro IPR001357


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.

BRCT domain, a BRCA1 C-terminus domain Provide feedback

This BRCT domain, a BRCA1 C-terminus region, is found on many RAP1 proteins, usually at the very N-terminus. The function in human at least of a BRCT is to contribute to the heterogeneity of the telomere DNA length, but that may not be its general function, which remains unknown [1,2].

Literature references

  1. Chen Y, Rai R, Zhou ZR, Kanoh J, Ribeyre C, Yang Y, Zheng H, Damay P, Wang F, Tsujii H, Hiraoka Y, Shore D, Hu HY, Chang S, Lei M;, Nat Struct Mol Biol. 2011;18:213-221.: A conserved motif within RAP1 has diversified roles in telomere protection and regulation in different organisms. PUBMED:21217703 EPMC:21217703

  2. Fujita I, Tanaka M, Kanoh J;, PLoS One. 2012;7:e49151.: Identification of the functional domains of the telomere protein Rap1 in Schizosaccharomyces pombe. PUBMED:23133674 EPMC:23133674


Internal database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR001357

The breast cancer susceptibility gene contains at its C terminus two copies of a conserved domain that was named BRCT for BRCA1 C terminus. This domain of about 95 amino acids is found in a large variety of proteins involved in DNA repair, recombination and cell cycle control [PUBMED:8673121, PUBMED:9034168, PUBMED:9000507]. The BRCT domain is not limited to the C-terminal of protein sequences and can be found in multiple copies or in a single copy as in RAP1 and TdT. Some data [PUBMED:9799248] indicate that the BRCT domain functions as a protein-protein interaction module.

The structure of the first of the two C-terminal BRCT domains of the human DNA repair protein XRCC1 has recently been determined by X-ray crystallography [PUBMED:9799248].

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 BRCT-like (CL0459), which has the following description:

The BRCT domain is found predominantly in proteins involved in cell cycle checkpoint functions responsive to DNA damage.

The clan contains the following 9 members:

BRCT BRCT_2 BRCT_3 Dfp1_Him1_M LIG3_BRCT NIBRIN_BRCT_II PTCB-BRCT RTT107_BRCT_5 RTT107_BRCT_6

Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the UniProtKB sequence database, the NCBI sequence database, and our metagenomics sequence database. More...

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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
(95)
Full
(4642)
Representative proteomes UniProt
(6638)
NCBI
(11573)
Meta
(9)
RP15
(1303)
RP35
(2569)
RP55
(3599)
RP75
(4382)
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PP/heatmap 1 View               

1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(95)
Full
(4642)
Representative proteomes UniProt
(6638)
NCBI
(11573)
Meta
(9)
RP15
(1303)
RP35
(2569)
RP55
(3599)
RP75
(4382)
Alignment:
Format:
Order:
Sequence:
Gaps:
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(95)
Full
(4642)
Representative proteomes UniProt
(6638)
NCBI
(11573)
Meta
(9)
RP15
(1303)
RP35
(2569)
RP55
(3599)
RP75
(4382)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download   Download   Download  

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

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.

Note: You can also download the data file for the tree.

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 View help on the curation process

Seed source: Manual
Previous IDs: none
Type: Family
Sequence Ontology: SO:0100021
Author: Coggill P
Number in seed: 95
Number in full: 4642
Average length of the domain: 91.40 aa
Average identity of full alignment: 20 %
Average coverage of the sequence by the domain: 11.39 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 45638612 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 27.3 27.3
Trusted cut-off 27.3 27.3
Noise cut-off 27.2 27.2
Model length: 85
Family (HMM) version: 5
Download: download the raw HMM for this family

Species distribution

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Structures

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 BRCT_2 domain has been found. There are 44 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 sequence.

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