Summary: DmpG-like communication domain
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DmpG-like communication domain Edit Wikipedia article
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|DmpG-like communication domain|
crystal structure of a bifunctional aldolase-dehydrogenase : sequestering a reactive and volatile intermediate
In molecular biology, the DmpG-like communication domain is a protein domain found towards the C-terminal region of various aldolase enzymes. It consists of five alpha-helices, four of which form an antiparallel helical bundle that plugs the C terminus of the N-terminal TIM barrel domain. The communication domain is thought to play an important role in the heterodimerisation of the enzyme.
DmpG-like communication domain Provide feedback
This domain is found towards the C-terminal region of various aldolase enzymes. It consists of five alpha-helices, four of which form an antiparallel helical bundle that plugs the C-terminus of the N-terminal TIM barrel domain . The communication domain is thought to play an important role in the heterodimerisation of the enzyme .
Manjasetty BA, Powlowski J, Vrielink A; , Proc Natl Acad Sci U S A 2003;100:6992-6997.: Crystal structure of a bifunctional aldolase-dehydrogenase: sequestering a reactive and volatile intermediate. PUBMED:12764229 EPMC:12764229
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR012425
This domain is found towards the C-terminal region of various aldolase enzymes. It consists of five alpha-helices, four of which form an antiparallel helical bundle that plugs the C terminus of the N-terminal TIM barrel domain [PUBMED:12764229]. The communication domain is thought to play an important role in the heterodimerisation of the enzyme [PUBMED:12764229].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||oxo-acid-lyase activity (GO:0016833)|
|Biological process||aromatic compound catabolic process (GO:0019439)|
- the number of sequences which exhibit this architecture
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This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
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We make a range of alignments for each Pfam-A family:
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key: available, not generated, — not available.
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Curation and family details
|Seed source:||Pfam-B_1675 (release 14.0)|
|Number in seed:||66|
|Number in full:||4495|
|Average length of the domain:||62.90 aa|
|Average identity of full alignment:||65 %|
|Average coverage of the sequence by the domain:||18.54 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||7|
|Download:||download the raw HMM for this family|
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The tree shows the occurrence of this domain across different species. More...
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There are 3 interactions for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
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 DmpG_comm domain has been found. There are 9 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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