Summary: GYF domain
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GYF domain Edit Wikipedia article
| the crystal structure of a binary u5 snrnp complex | |||||||||
| Identifiers | |||||||||
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| Symbol | GYF | ||||||||
| Pfam | PF02213 | ||||||||
| InterPro | IPR003169 | ||||||||
| SMART | GYF | ||||||||
| SCOP | 1gyf | ||||||||
| SUPERFAMILY | 1gyf | ||||||||
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In molecular biology, the GYF domain (glycine-tyrosine-phenylalanine domain) is an approximately 60-amino acid protein domain which contains a conserved GP[YF]xxxx[MV]xxWxxx[GN]YF motif. It was identified in the human intracellular protein termed CD2 binding protein 2 (CD2BP2), which binds to a site containing two tandem PPPGHR segments within the cytoplasmic region of CD2. Binding experiments and mutational analyses have demonstrated the critical importance of the GYF tripeptide in ligand binding. A GYF domain is also found in several other eukaryotic proteins of unknown function.[1] It has been proposed that the GYF domain found in these proteins could also be involved in proline-rich sequence recognition.[2] Resolution of the structure of the CD2BP2 GYF domain by NMR spectroscopy revealed a compact domain with a beta-beta-alpha-beta-beta topology, where the single alpha-helix is tilted away from the twisted, anti-parallel beta-sheet. The conserved residues of the GYF domain create a contiguous patch of predominantly hydrophobic nature which forms an integral part of the ligand-binding site.[2] There is limited homology within the C-terminal 20-30 amino acids of various GYF domains, supporting the idea that this part of the domain is structurally but not functionally important.[3]
[edit] References
- ^ Nishizawa K, Freund C, Li J, Wagner G, Reinherz EL (December 1998). "Identification of a proline-binding motif regulating CD2-triggered T lymphocyte activation". Proc. Natl. Acad. Sci. U.S.A. 95 (25): 14897902. doi:10.1073/pnas.95.25.14897. PMC 24547. PMID 9843987. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=24547.
- ^ a b Freund C, Dotsch V, Nishizawa K, Reinherz EL, Wagner G (July 1999). "The GYF domain is a novel structural fold that is involved in lymphoid signaling through proline-rich sequences". Nat. Struct. Biol. 6 (7): 65660. doi:10.1038/10712. PMID 10404223.
- ^ Freund C, Kuhne R, Yang H, Park S, Reinherz EL, Wagner G (November 2002). "Dynamic interaction of CD2 with the GYF and the SH3 domain of compartmentalized effector molecules". EMBO J. 21 (22): 598595. doi:10.1093/emboj/cdf602. PMC 137194. PMID 12426371. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=137194.
This article incorporates text from the public domain Pfam and InterPro IPR003169
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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.
GYF domain Provide feedback
The GYF domain is named because of the presence of Gly-Tyr-Phe residues. The GYF domain is a proline-binding domain in CD2-binding protein O95400.
Literature references
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Freund C, Dotsch V, Nishizawa K, Reinherz EL, Wagner G; , Nat Struct Biol 1999;6:656-660.: The GYF domain is a novel structural fold that is involved in lymphoid signaling through proline-rich sequences. PUBMED:10404223 EPMC:10404223
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Nishizawa K, Freund C, Li J, Wagner G, Reinherz EL; , Proc Natl Acad Sci U S A 1998;95:14897-14902.: Identification of a proline-binding motif regulating CD2-triggered T lymphocyte activation. PUBMED:9843987 EPMC:9843987
Internal database links
| Similarity to PfamA using HHSearch: | DUF4339 |
External database links
| PANDIT: | PF02213 |
| Pseudofam: | PF02213 |
| SCOP: | 1gyf |
| SMART: | GYF |
| SYSTERS: | GYF |
This tab holds annotation information from the InterPro database.
InterPro entry IPR003169
The glycine-tyrosine-phenylalanine (GYF) domain is an around 60-amino acid domain which contains a conserved GP[YF]xxxx[MV]xxWxxx[GN]YF motif. It was identified in the human intracellular protein termed CD2 binding protein 2 (CD2BP2), which binds to a site containing two tandem PPPGHR segments within the cytoplasmic region of CD2. Binding experiments and mutational analyses have demonstrated the critical importance of the GYF tripeptide in ligand binding. A GYF domain is also found in several other eukaryotic proteins of unknown function [PUBMED:9843987]. It has been proposed that the GYF domain found in these proteins could also be involved in proline-rich sequence recognition [PUBMED:10404223]. Resolution of the structure of the CD2BP2 GYF domain by NMR spectroscopy revealed a compact domain with a beta-beta-alpha-beta-beta topology, where the single alpha-helix is tilted away from the twisted, anti-parallel beta-sheet. The conserved residues of the GYF domain create a contiguous patch of predominantly hydrophobic nature which forms an integral part of the ligand-binding site [PUBMED:10404223]. There is limited homology within the C-terminal 20-30 amino acids of various GYF domains, supporting the idea that this part of the domain is structurally but not functionally important [PUBMED:12426371].
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Molecular function | protein binding (GO:0005515) |
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
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 using the family HMM. We also generate alignments using four representative proteomes (RP) sets, 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 (79) |
Full (823) |
Representative proteomes | NCBI (801) |
Meta (13) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (187) |
RP35 (316) |
RP55 (466) |
RP75 (564) |
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| Jalview | ||||||||
| HTML | ||||||||
| PP/heatmap | 1 | |||||||
| Pfam viewer | ||||||||
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
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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 (79) |
Full (823) |
Representative proteomes | NCBI (801) |
Meta (13) |
||||
|---|---|---|---|---|---|---|---|---|
| RP15 (187) |
RP35 (316) |
RP55 (466) |
RP75 (564) |
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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.
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
| Seed source: | Alignment kindly provided by SMART |
| Previous IDs: | none |
| Type: | Domain |
| Author: | SMART |
| Number in seed: | 79 |
| Number in full: | 823 |
| Average length of the domain: | 55.40 aa |
| Average identity of full alignment: | 30 % |
| Average coverage of the sequence by the domain: | 6.25 % |
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: | 57 | ||||||||||||
| Family (HMM) version: | 11 | ||||||||||||
| 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 GYF domain has been found. There are 12 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