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68  structures 1546  species 0  interactions 25769  sequences 735  architectures

Family: zf-MYND (PF01753)

Summary: MYND finger

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This is the Wikipedia entry entitled "MYND zinc finger". More...

MYND zinc finger Edit Wikipedia article

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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.

MYND finger Provide feedback

No Pfam abstract.

Literature references

  1. Gross CT, McGinnis W; , EMBO J 1996;15:1961-1970.: DEAF-1, a novel protein that binds an essential region in a Deformed response element. PUBMED:8617243 EPMC:8617243

  2. LeBoeuf RD, Ban EM, Green MM, Stone AS, Propst SM, Blalock JE, Tauber JD; , J Biol Chem 1998;273:361-368.: Molecular cloning, sequence analysis, expression, and tissue distribution of suppressin, a novel suppressor of cell cycle entry. PUBMED:9417089 EPMC:9417089

Internal database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR002893

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 MYND-type zinc finger domains. The MYND domain (myeloid, Nervy, and DEAF-1) is present in a large group of proteins that includes RP-8 (PDCD2), Nervy, and predicted proteins from Drosophila, mammals, Caenorhabditis elegans, yeast, and plants [ PUBMED:7498738 , PUBMED:8617243 , PUBMED:2072913 ]. The MYND domain consists of a cluster of cysteine and histidine residues, arranged with an invariant spacing to form a potential zinc-binding motif [ PUBMED:8617243 ]. Mutating conserved cysteine residues in the DEAF-1 MYND domain does not abolish DNA binding, which suggests that the MYND domain might be involved in protein-protein interactions [ PUBMED:8617243 ]. Indeed, the MYND domain of ETO/MTG8 interacts directly with the N-CoR and SMRT co-repressors [ PUBMED:9584201 , PUBMED:9819404 ]. Aberrant recruitment of co-repressor complexes and inappropriate transcriptional repression is believed to be a general mechanism of leukemogenesis caused by the t(8;21) translocations that fuse ETO with the acute myelogenous leukemia 1 (AML1) protein. ETO has been shown to be a co-repressor recruited by the promyelocytic leukemia zinc finger (PLZF) protein [ PUBMED:10688654 ]. A divergent MYND domain present in the adenovirus E1A binding protein BS69 was also shown to interact with N-CoR and mediate transcriptional repression [ PUBMED:10734313 ]. The current evidence suggests that the MYND motif in mammalian proteins constitutes a protein-protein interaction domain that functions as a co-repressor-recruiting interface.

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 TRASH (CL0175), which has the following description:

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 [1].

The clan contains the following 13 members:

Arc_trans_TRASH ATPase-cat_bd DUF2256 NosL Ribosomal_L24e YacG YHS zf-C6H2 zf-FCS zf-FLZ zf-HIT zf-Mss51 zf-MYND


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 (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB 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.

Representative proteomes UniProt
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available

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Representative proteomes UniProt

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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.

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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

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...


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 View help on the curation process

Seed source: Bateman A
Previous IDs: none
Type: Domain
Sequence Ontology: SO:0000417
Author: Bateman A
Number in seed: 126
Number in full: 25769
Average length of the domain: 41.40 aa
Average identity of full alignment: 36 %
Average coverage of the sequence by the domain: 7.47 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 22.7 22.7
Trusted cut-off 22.7 22.7
Noise cut-off 22.6 22.6
Model length: 40
Family (HMM) version: 21
Download: download the raw HMM for this family

Species distribution

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Colour assignments

Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence


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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

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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-MYND domain has been found. There are 68 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 sequence.

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AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
A0A096MJU8 View 3D Structure Click here
A0A0G2K0G0 View 3D Structure Click here
A0A0G2K8N6 View 3D Structure Click here
A0A0P0WFA2 View 3D Structure Click here
A0A0P0XPE6 View 3D Structure Click here
A0A0R0HLZ8 View 3D Structure Click here
A0A0R0JEG4 View 3D Structure Click here
A0A0R0JI11 View 3D Structure Click here
A0A0R0K284 View 3D Structure Click here
A0A0R4IVE6 View 3D Structure Click here
A0A0R4IXV4 View 3D Structure Click here
A0A0R4J368 View 3D Structure Click here
A0A1D6DWM5 View 3D Structure Click here
A0A1D6ECT9 View 3D Structure Click here
A0A1D6EI12 View 3D Structure Click here
A0A1D6GJT5 View 3D Structure Click here
A0A1D6H5U8 View 3D Structure Click here
A0A1D6H8A4 View 3D Structure Click here
A0A1D6I638 View 3D Structure Click here
A0A1D6IBH0 View 3D Structure Click here
A0A1D6JZS7 View 3D Structure Click here
A0A1D6KLE9 View 3D Structure Click here
A0A1D6KLG8 View 3D Structure Click here
A0A1D6LQJ2 View 3D Structure Click here
A0A1D6MRF4 View 3D Structure Click here
A0A1D6N2W7 View 3D Structure Click here
A0A1D6PCF3 View 3D Structure Click here
A0A1D6Q1V8 View 3D Structure Click here
A0A1D6QPL2 View 3D Structure Click here
A0A1D8PKL7 View 3D Structure Click here
A0A2R8QV03 View 3D Structure Click here
A0A2R8RHK9 View 3D Structure Click here
A0A2R8RJM1 View 3D Structure Click here
A0A2R8RUH3 View 3D Structure Click here
A1Z7W1 View 3D Structure Click here
A1Z8L3 View 3D Structure Click here
A2BGJ5 View 3D Structure Click here
A4HSK2 View 3D Structure Click here
A4HSS1 View 3D Structure Click here
A4I6U2 View 3D Structure Click here