Summary: MYM-type Zinc finger with FCS sequence motif
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MYM-type Zinc finger with FCS sequence motif Provide feedback
MYM-type zinc fingers were identified in MYM family proteins . Human protein Q14202 is involved in a chromosomal translocation and may be responsible for X-linked retardation in XQ13.1 . Q9UBW7 is also involved in disease. In myeloproliferative disorders it is fused to FGF receptor 1 ; in atypical myeloproliferative disorders it is rearranged . 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 .
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 EPMC:9716603
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 EPMC:8817323
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 EPMC:9576949
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 EPMC:9694738
External database links
This tab holds annotation information from the InterPro database.
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 SWISSPROT is involved in a chromosomal translocation and may be responsible for X-linked retardation in XQ13.1 [PUBMED:8817323]. SWISSPROT 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:].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||zinc ion binding (GO:0008270)|
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TRASH-like domains contain well-conserved cysteine residues that are thought to be involved in metal coordination. These domains are thus expected to be involved in metal trafficking and heavy-metal resistance. It has been suggested that the members adopt a 'treble-clef' fold, with 3/4 beta strands preceding a C-terminal alpha helix .
The clan contains the following 11 members:Arc_trans_TRASH ATPase-cat_bd DUF2256 DUF329 DUF581 Ribosomal_L24e YHS zf-FCS zf-HIT zf-Mss51 zf-MYND
We make a range of alignments for each Pfam-A family:
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Curation and family details
|Seed source:||ADDA_4806, Iyer L|
|Previous IDs:||zf_MYM; zf-MYM;|
|Number in seed:||56|
|Number in full:||1780|
|Average length of the domain:||41.30 aa|
|Average identity of full alignment:||25 %|
|Average coverage of the sequence by the domain:||16.45 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||9|
|Download:||download the raw HMM for this family|
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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. There are 2 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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