Summary
BRCA1 C Terminus (BRCT) domain
The BRCT domain is found predominantly in proteins involved in cell cycle checkpoint functions responsive to DNA damage. The BRCT domain of XRCC1 forms a homodimer in the crystal structure. This suggests that pairs of BRCT domains associate as homo- or heterodimers. BRCT domains are often found as tandem-repeat pairs [2]. Structures of the BRCA1 BRCT domains revealed a basis for a widely utilised head-to-tail BRCT-BRCT oligomerisation mode [3]. This conserved tandem BRCT architecture facilitates formation of the canonical BRCT phospho-peptide interaction cleft at a groove between the BRCT domains. Disease associated missense and nonsense mutations in the BRCA1 BRCT domains disrupt peptide binding by directly occluding this peptide binding groove, or by disrupting key conserved BRCT core folding determinants [5].
Literature references
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Koonin EV, Altschul SF, Bork P; , Nature Genet 1996;13:266-268.: BRCA1 protein products ...Functional motifs... PUBMED:8673121
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Glover JN, Williams RS, Lee MS; , Trends Biochem Sci. 2004;29:579-585.: Interactions between BRCT repeats and phosphoproteins: tangled up in two. PUBMED:15501676
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Williams RS, Green R, Glover JN; , Nat Struct Biol. 2001;8:838-842.: Crystal structure of the BRCT repeat region from the breast cancer-associated protein BRCA1. PUBMED:11573086
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Williams RS, Lee MS, Hau DD, Glover JN; , Nat Struct Mol Biol. 2004;11:519-525.: Structural basis of phosphopeptide recognition by the BRCT domain of BRCA1. PUBMED:15133503
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Williams RS, Chasman DI, Hau DD, Hui B, Lau AY, Glover JN; , J Biol Chem. 2003;278:53007-53016.: Detection of protein folding defects caused by BRCA1-BRCT truncation and missense mutations. PUBMED:14534301
InterPro entry IPR001357
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 PUBMED:9034168, 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 PUBMED:14576433.
A chitin biosynthesis protein from yeast also seems to belong to this group.
Gene Ontology
| Cellular component | intracellular (GO:0005622) |
External database links
| HOMSTRAD: | BRCT |
| PANDIT: | PF00533 |
| SCOP: | 1cdz |
| SYSTERS: | BRCT |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Alignments
There are various ways to view or download the sequence alignments that we store. You can use a sequence viewer to look at either the seed or full alignment for the family, or you can look at a plain text version of the sequence in a variety of different formats. More...
View options
Formatting options
Download options
Very large alignments can often cause problems for the formatting tool above. If you find that downloading or viewing a large alignment is problematic, you can also download a gzip-compressed, Stockholm-format file containing the seed or full alignment for this family.
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
The main seed and full alignments are generated using sequences from the UniProt sequence database. However, we also generate alignments using sequences from the NCBI sequence database and the "metaseq" metagenomics dataset.
You can view alignments from these two additional datasets using the form above, or you can download alignments of NCBI or metagenomics sequences, as gzip-compressed files.
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 HMMER2.
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. 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 or full alignments.
Note: You can also download the data files for the seed, full, NCBI or metagenomics trees.
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: | [3] |
| Previous IDs: | none |
| Type: | Family |
| Author: | Bateman A |
| Number in seed: | 114 |
| Number in full: | 3710 |
| Average length of the domain: | 78.20 aa |
| Average identity of full alignment: | 22 % |
| Average coverage of the sequence by the domain: | 9.95 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 9421015 -E 1000 HMM pfamseq
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| Model details: |
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| Model length: | 78 | ||||||||||||
| Family (HMM) version: | 19 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
Tree controls
HideThe tree shows the occurrence of this domain across different species. More...
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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 MSD 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 domain has been found.
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