The domain within your query sequence starts at position 527 and ends at position 569; the E-value for the zf-FCS domain shown below is 1.8e-9.

EKYGKLTTCTGCRTQCRFFDMTQCIGPNGYMEPYCSTACMNSH

zf-FCS

zf-FCS
PFAM accession number:PF06467
Interpro abstract (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 Q14202 is involved in a chromosomal translocation and may be responsible for X-linked retardation in XQ13.1 [ (PUBMED:8817323) ]. Q9UBW7 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) ].

GO function:zinc ion binding (GO:0008270)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry zf-FCS