Summary: GATA zinc finger
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GATA zinc finger Edit Wikipedia article
| zinc fingers as protein recognition motifs: structural basis for the gata-1/friend of gata interaction | |||||||||
| Identifiers | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Symbol | GATA | ||||||||
| Pfam | PF00320 | ||||||||
| Pfam clan | CL0167 | ||||||||
| InterPro | IPR000679 | ||||||||
| PROSITE | PDOC00300 | ||||||||
| SCOP | 1gat | ||||||||
| SUPERFAMILY | 1gat | ||||||||
| CDD | cd00202 | ||||||||
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In molecular biology, GATA zinc fingers are zinc-containing domains found in a number of transcription factors (including erythroid-specific transcription factor and nitrogen regulatory proteins). They specifically bind the DNA sequence (A/T)GATA(A/G) in the regulatory regions of genes.[1] They are consequently termed GATA-binding transcription factors. The interactions occur via highly-conserved zinc finger (Znf) domains in which the zinc ion is coordinated by 4 cysteine residues.[2][3] NMR studies have shown the core of the Znf to comprise 2 irregular anti-parallel beta-sheets and an alpha-helix, followed by a long loop to the C-terminal end of the finger. The N-terminal part, which includes the helix, is similar in structure, but not sequence, to the N-terminal zinc module of the glucocorticoid receptor DNA-binding domain. The helix and the loop connecting the 2 beta-sheets interact with the major groove of the DNA, while the C-terminal tail wraps around into the minor groove. It is this tail that is the essential determinant of specific binding. Interactions between the Znf and DNA are mainly hydrophobic, explaining the preponderance of thymines in the binding site; a large number of interactions with the phosphate backbone have also been observed.[3] Two GATA zinc fingers are found in the GATA transcription factors. However there are several proteins which only contains a single copy of the domain.
[edit] References
- ^ Yamamoto M, Ko LJ, Leonard MW, Beug H, Orkin SH, Engel JD (October 1990). "Activity and tissue-specific expression of the transcription factor NF-E1 multigene family". Genes Dev. 4 (10): 165062. PMID 2249770.
- ^ Evans T, Felsenfeld G (September 1989). "The erythroid-specific transcription factor Eryf1: a new finger protein". Cell 58 (5): 87785. doi:10.1016/0092-8674(89)90940-9. PMID 2776214.
- ^ a b Omichinski JG, Clore GM, Schaad O, Felsenfeld G, Trainor C, Appella E, Stahl SJ, Gronenborn AM (July 1993). "NMR structure of a specific DNA complex of Zn-containing DNA binding domain of GATA-1". Science 261 (5120): 43846. doi:10.1126/science.8332909. PMID 8332909.
This article incorporates text from the public domain Pfam and InterPro IPR000679
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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.
GATA zinc finger Provide feedback
This domain uses four cysteine residues to coordinate a zinc ion. This domain binds to DNA. Two GATA zinc fingers are found in the GATA transcription factors. However there are several proteins which only contains a single copy of the domain.
Literature references
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Omichinski JG, Clore GM, Schaad O, Felsenfeld G, Trainor C, Appella E, Stahl SJ, Gronenborn AM; , Science 1993;261:438-446.: NMR structure of a specific DNA complex of Zn-containing DNA binding domain of GATA-1. PUBMED:8332909 EPMC:8332909
Internal database links
| SCOOP: | ZZ |
External database links
| HOMSTRAD: | GATA |
| PANDIT: | PF00320 |
| PRINTS: | PR00619 |
| PROSITE: | PDOC00300 |
| Pseudofam: | PF00320 |
| SCOP: | 1gat |
| SYSTERS: | GATA |
This tab holds annotation information from the InterPro database.
InterPro entry IPR000679
Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. Some of these domains bind zinc, but many do not; instead binding other metals such as iron, or no metal at all. For example, some family members form salt bridges to stabilise the finger-like folds. They were first identified as a DNA-binding motif in transcription factor TFIIIA from Xenopus laevis (African clawed frog), however they are now recognised to bind DNA, RNA, protein and/or lipid substrates [PUBMED:10529348, PUBMED:15963892, PUBMED:15718139, PUBMED:17210253, PUBMED:12665246]. Their binding properties depend on the amino acid sequence of the finger domains and of the linker between fingers, as well as on the higher-order structures and the number of fingers. Znf domains are often found in clusters, where fingers can have different binding specificities. There are many superfamilies of Znf motifs, varying in both sequence and structure. They display considerable versatility in binding modes, even between members of the same class (e.g. some bind DNA, others protein), suggesting that Znf motifs are stable scaffolds that have evolved specialised functions. For example, Znf-containing proteins function in gene transcription, translation, mRNA trafficking, cytoskeleton organisation, epithelial development, cell adhesion, protein folding, chromatin remodelling and zinc sensing, to name but a few [PUBMED:11179890]. Zinc-binding motifs are stable structures, and they rarely undergo conformational changes upon binding their target.
This entry represents GATA-type zinc fingers (Znf). A number of transcription factors (including erythroid-specific transcription factor and nitrogen regulatory proteins), specifically bind the DNA sequence (A/T)GATA(A/G) [PUBMED:2249770] in the regulatory regions of genes. They are consequently termed GATA-binding transcription factors. The interactions occur via highly-conserved Znf domains in which the zinc ion is coordinated by 4 cysteine residues [PUBMED:2776214, PUBMED:8332909]. NMR studies have shown the core of the Znf to comprise 2 irregular anti-parallel beta-sheets and an alpha-helix, followed by a long loop to the C-terminal end of the finger. The N-terminal part, which includes the helix, is similar in structure, but not sequence, to the N-terminal zinc module of the glucocorticoid receptor DNA-binding domain. The helix and the loop connecting the 2 beta-sheets interact with the major groove of the DNA, while the C-terminal tail wraps around into the minor groove. It is this tail that is the essential determinant of specific binding. Interactions between the Znf and DNA are mainly hydrophobic, explaining the preponderance of thymines in the binding site; a large number of interactions with the phosphate backbone have also been observed [PUBMED:8332909]. Two GATA zinc fingers are found in the GATA transcription factors. However there are several proteins which only contains a single copy of the domain.
More information about these proteins can be found at Protein of the Month: Zinc Fingers [PUBMED:].
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Molecular function | sequence-specific DNA binding (GO:0043565) |
| zinc ion binding (GO:0008270) | |
| sequence-specific DNA binding transcription factor activity (GO:0003700) | |
| Biological process | regulation of transcription, DNA-dependent (GO:0006355) |
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 Zn_Beta_Ribbon (CL0167), which contains the following 50 members:
A2L_zn_ribbon Auto_anti-p27 Baculo_LEF5_C DNA_RNApol_7kD DUF1610 DUF1936 DUF2116 DUF2180 DUF2387 DZR Elf1 GATA NinF NOB1_Zn_bind Ogr_Delta OrfB_Zn_ribbon PhnA_Zn_Ribbon Prim_Zn_Ribbon Ribosomal_L32p Ribosomal_L37ae Ribosomal_S27 Ribosomal_S27e RNA_POL_M_15KD RRN7 Spt4 TF_Zn_Ribbon TFIIS_C Tnp_zf-ribbon_2 Topo_Zn_Ribbon Toprim_Crpt Trm112p UPF0547 zf-C4_Topoisom zf-CHC2 zf-DHHC zf-dskA_traR zf-FPG_IleRS zf-GRF zf-NADH-PPase zf-RanBP zf-ribbon_3 zf-TFIIB zinc-ribbons_6 zinc_ribbon_2 zinc_ribbon_4 zinc_ribbon_5 Zn-ribbon_8 Zn_ribbon_recom Zn_Tnp_IS1 Zn_Tnp_IS1595Alignments
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...
View options
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 (69) |
Full (3798) |
Representative proteomes | NCBI (3654) |
Meta (15) |
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| RP15 (638) |
RP35 (1149) |
RP55 (1789) |
RP75 (2299) |
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| Jalview | ||||||||
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| PP/heatmap | 1 | |||||||
| Pfam viewer | ||||||||
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
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Format an alignment
Download options
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 (69) |
Full (3798) |
Representative proteomes | NCBI (3654) |
Meta (15) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (638) |
RP35 (1149) |
RP55 (1789) |
RP75 (2299) |
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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: | Prosite |
| Previous IDs: | none |
| Type: | Domain |
| Author: | Finn RD |
| Number in seed: | 69 |
| Number in full: | 3798 |
| Average length of the domain: | 35.30 aa |
| Average identity of full alignment: | 45 % |
| Average coverage of the sequence by the domain: | 8.26 % |
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: | 36 | ||||||||||||
| Family (HMM) version: | 22 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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Interactions
There is 1 interaction for this family. More...
zf-C2H2Structures
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 GATA domain has been found. There are 40 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