Summary: E3 ubiquitin ligase EDD
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E3 ubiquitin ligase EDD Provide feedback
EDD, the ER ubiquitin ligase from the HECT ligases, contains an N-terminal ubiquitin-associated domain which binds ubiquitin. Ubiquitin is recognised by helices alpha-1 and -3 in in the UBA domain. EDD is involved in DNA damage repair pathways and binds to mono-ubiquitinated proteins .
Kozlov G, Nguyen L, Lin T, De Crescenzo G, Park M, Gehring K; , J Biol Chem. 2007;282:35787-35795.: Structural basis of ubiquitin recognition by the ubiquitin-associated (UBA) domain of the ubiquitin ligase EDD. PUBMED:17897937 EPMC:17897937
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This tab holds annotation information from the InterPro database.
InterPro entry IPR024725
EDD, the ER ubiquitin ligase from the HECT ligases, contains an N-terminal ubiquitin-associated (UBA) domain which binds ubiquitin. Ubiquitin is recognised by helices alpha-1 and -3 in in the UBA domain. EDD is involved in DNA damage repair pathways and binds to mono-ubiquitinated proteins [PUBMED:17897937].
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|Molecular function||ubiquitin binding (GO:0043130)|
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Curation and family details
|Number in seed:||3|
|Number in full:||94|
|Average length of the domain:||52.30 aa|
|Average identity of full alignment:||84 %|
|Average coverage of the sequence by the domain:||2.12 %|
|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|
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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 E3_UbLigase_EDD domain has been found. There are 4 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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