Summary
MYM-type Zinc finger with FCS sequence motif
MYM-type zinc fingers were identified in MYM family proteins [1]. Human protein Q14202 is involved in a chromosomal translocation and may be responsible for X-linked retardation in XQ13.1 [2]. Q9UBW7 is also involved in disease. In myeloproliferative disorders it is fused to FGF receptor 1 [3]; in atypical myeloproliferative disorders it is rearranged [4]. Members of the family generally are involved in development. This Zn-finger domain functions as a transcriptional trans-activator of late vaccinia viral genes, and orthologues are also found in all nucleocytoplasmic large DNA viruses, NCLDV. This domain is also found fused to the C termini of recombinases from certain prokaryotic transposons [5].
Literature references
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Reiter A, Sohal J, Kulkarni S, Chase A, Macdonald DH, Aguiar RC, Goncalves C, Hernandez JM, Jennings BA, Goldman JM, Cross NC; , Blood 1998;92:1735-1742.: Consistent fusion of ZNF198 to the fibroblast growth factor receptor-1 in the t(8;13)(p11;q12) myeloproliferative syndrome. PUBMED:9716603
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van der Maarel SM, Scholten IH, Huber I, Philippe C, Suijkerbuijk RF, Gilgenkrantz S, Kere J, Cremers FP, Ropers HH; , Hum Mol Genet 1996;5:887-897.: Cloning and characterization of DXS6673E, a candidate gene for X-linked mental retardation in Xq13.1. PUBMED:8817323
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Popovici C, Adelaide J, Ollendorff V, Chaffanet M, Guasch G, Jacrot M, Leroux D, Birnbaum D, Pebusque MJ; , Proc Natl Acad Sci U S A 1998;95:5712-5717.: Fibroblast growth factor receptor 1 is fused to FIM in stem-cell myeloproliferative disorder with t(8;13). PUBMED:9576949
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Still IH, Cowell JK; , Blood 1998;92:1456-1458.: The t(8;13) atypical myeloproliferative disorder: further analysis of the ZNF198 gene and lack of evidence for multiple genes disrupted on chromosome 13. PUBMED:9694738
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Iyer LM, Aravind L, Koonin EV; , J Virol. 2001;75:11720-11734.: Common origin of four diverse families of large eukaryotic DNA viruses. PUBMED:11689653
InterPro entry IPR010507
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.
MYM-type zinc fingers were identified in MYM family proteins PUBMED:9716603. Human protein is involved in a chromosomal translocation and may be responsible for X-linked retardation in XQ13.1 PUBMED:8817323. is also involved in disease. In myeloproliferative disorders it is fused to FGF receptor 1 PUBMED:9576949; in atypical myeloproliferative disorders it is rearranged PUBMED:9694738. Members of the family generally are involved in development. This Zn-finger domain functions as a transcriptional trans-activator of late vaccinia viral genes, and orthologues are also found in all nucleocytoplasmic large DNA viruses, NCLDV. This domain is also found fused to the C termini of recombinases from certain prokaryotic transposons PUBMED:9716603.
More information about these proteins can be found at Protein of the Month: Zinc Fingers PUBMED:.
Clan
This family is a member of clan TRASH (CL0175), which contains the following 10 members:
Arc_trans_TRASH ATPase-cat_bd DUF2256 DUF329 DUF581 Ribosomal_L24e YHS zf-FCS zf-HIT zf-MYNDGene Ontology
| Cellular component | nucleus (GO:0005634) |
| Molecular function | zinc ion binding (GO:0008270) |
External database links
| PANDIT: | PF06467 |
| SYSTERS: | zf-FCS |
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...
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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: | ADDA_4806, Iyer L |
| Previous IDs: | zf_MYM; zf-MYM; |
| Type: | Domain |
| Author: | Yeats C |
| Number in seed: | 56 |
| Number in full: | 436 |
| Average length of the domain: | 41.80 aa |
| Average identity of full alignment: | 24 % |
| Average coverage of the sequence by the domain: | 4.73 % |
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: | 43 | ||||||||||||
| Family (HMM) version: | 7 | ||||||||||||
| 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 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 zf-FCS domain has been found.
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