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19  structures 323  species 1  interaction 445  sequences 10  architectures

Family: TRF (PF08558)

Summary: Telomere repeat binding factor (TRF)

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Telomere repeat binding factor (TRF) Provide feedback

Telomere repeat binding factor (TRF) family proteins are important for the regulation of telomere stability. The two related human TRF proteins hTRF1 and hTRF2 form homodimers and bind directly to telomeric TTAGGG repeats via the myb DNA binding domain PF00249 at the carboxy terminus [1]. TRF1 is implicated in telomere length regulation and TRF2 in telomere protection [1]. Other telomere complex associated proteins are recruited through their interaction with either TRF1 or TRF2. The fission yeast protein Taz1p (telomere-associated in Schizosaccharomyces pombe) has similarity to both hTRF1 and hTRF2 and may perform the dual functions of TRF1 and TRF2 at fission yeast telomeres [2]. This domain is composed of multiple alpha helices [3] arranged in a solenoid conformation similar to TPR repeats. The fungal members have now also been found to carry two double strand telomeric repeat binding factors [4].

Literature references

  1. Ye JZ, Donigian JR, van Overbeek M, Loayza D, Luo Y, Krutchinsky AN, Chait BT, de Lange T; , J Biol Chem 2004;279:47264-47271.: TIN2 binds TRF1 and TRF2 simultaneously and stabilizes the TRF2 complex on telomeres. PUBMED:15316005 EPMC:15316005

  2. Cooper JP, Nimmo ER, Allshire RC, Cech TR; , Nature 1997;385:744-747.: Regulation of telomere length and function by a Myb-domain protein in fission yeast. PUBMED:9034194 EPMC:9034194

  3. Fairall L, Chapman L, Moss H, de Lange T, Rhodes D; , Mol Cell 2001;8:351-361.: Structure of the TRFH dimerization domain of the human telomeric proteins TRF1 and TRF2. PUBMED:11545737 EPMC:11545737

  4. Pitt CW, Valente LP, Rhodes D, Simonsson T; , J Biol Chem. 2008;283:2693-2701.: Identification and characterization of an essential telomeric repeat binding factor in fission yeast. PUBMED:17977837 EPMC:17977837


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR013867

Telomeres function to shield chromosome ends from degradation and end-to-end fusions, as well as preventing the activation of DNA damage checkpoints. Telomeric repeat binding factor (TRF) proteins TRF1 and TRF2 are major components of vertebrate telomeres required for regulation of telomere stability. TRF1 and TRF2 bind to telomeric DNA as homodimers. Dimerisation involves the TRF homology (TRFH) subdomain contained within the dimerisation domain. The TRFH subdomain is important not only for dimerisation, but for DNA binding, telomere localisation, and interactions with other telomeric proteins. The dimerisation domains of TRF1 and TRF2 show the same multi-helical structure, arranged in a solenoid conformation similar to TPR repeats, which can be divided into an alpha-alpha superhelix and a long alpha hairpin [PUBMED:11545737].

The two related human TRF proteins hTRF1 and hTRF2 form homodimers and bind directly to telomeric TTAGGG repeats via the myb DNA binding domain INTERPRO at the carboxy terminus [PUBMED:15316005]. TRF1 is implicated in telomere length regulation and TRF2 in telomere protection [PUBMED:15316005]. Other telomere complex associated proteins are recruited through their interaction with either TRF1 or TRF2. The fission yeast protein Taz1p (telomere-associated in Schizosaccharomyces pombe (Fission yeast) has similarity to both hTRF1 and hTRF2 and may perform the dual functions of TRF1 and TRF2 at fission yeast telomeres [PUBMED:9034194].

This entry represents dimerisation domain.

Gene Ontology

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Domain organisation

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Alignments

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(27)
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RP75
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  Seed
(27)
Full
(445)
Representative proteomes UniProt
(629)
NCBI
(1232)
Meta
(0)
RP15
(45)
RP35
(162)
RP55
(286)
RP75
(418)
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  Seed
(27)
Full
(445)
Representative proteomes UniProt
(629)
NCBI
(1232)
Meta
(0)
RP15
(45)
RP35
(162)
RP55
(286)
RP75
(418)
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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

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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

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Curation View help on the curation process

Seed source: Pfam-B_8956 (release 18.0)
Previous IDs: none
Type: Domain
Author: Daub J, Wood V
Number in seed: 27
Number in full: 445
Average length of the domain: 213.60 aa
Average identity of full alignment: 22 %
Average coverage of the sequence by the domain: 34.04 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 26740544 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 25.0 25.0
Trusted cut-off 25.3 25.5
Noise cut-off 24.3 24.6
Model length: 239
Family (HMM) version: 9
Download: download the raw HMM for this family

Species distribution

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Interactions

There is 1 interaction for this family. More...

TRF

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 TRF domain has been found. There are 19 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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