Summary: Class II histone deacetylase complex subunits 2 and 3
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Class II histone deacetylase complex subunits 2 and 3 Provide feedback
This family of class II histone deacetylase complex subunits HDA2 and HDA3 is found in fungi, The member from S. pombe is referred to as Ccq1 in Q10432. These proteins associate with HDA1 to generate the activity of the HDA1 histone deacetylase complex. HDA1 interacts with itself and with the HDA2-HDA3 subcomplex to form a probable tetramer and these interactions are necessary for catalytic activity. The HDA1 histone deacetylase complex is responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. HDA2 and HDA3 have a conserved coiled-coil domain towards their C-terminus .
Wu J, Carmen AA, Kobayashi R, Suka N, Grunstein M; , Proc Natl Acad Sci U S A. 2001;98:4391-4396.: HDA2 and HDA3 are related proteins that interact with and are essential for the activity of the yeast histone deacetylase HDA1. PUBMED:11287668 EPMC:11287668
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This tab holds annotation information from the InterPro database.
InterPro entry IPR021006
This entry contains the class II histone deacetylase complex subunits HDA2 and HDA3 is found in fungi. The member from Schizosaccharomyces pombe (Fission yeast) is referred to as Ccq1 in SWISSPROT. These proteins associate with HDA1 to generate the activity of the HDA1 histone deacetylase complex. HDA1 interacts with itself and with the HDA2-HDA3 subcomplex to form a probable tetramer and these interactions are necessary for catalytic activity. The HDA1 histone deacetylase complex is responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. HDA2 and HDA3 have a conserved coiled-coil domain towards their C terminus [PUBMED:11287668].
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Curation and family details
|Seed source:||Chahwan C|
|Author:||Wood V, Coggill P|
|Number in seed:||26|
|Number in full:||146|
|Average length of the domain:||269.30 aa|
|Average identity of full alignment:||22 %|
|Average coverage of the sequence by the domain:||34.08 %|
|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:||3|
|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 HDA2-3 domain has been found. There are 6 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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