Summary: MetRS-N binding domain
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MetRS-N binding domain Provide feedback
The MetRS-N domain binds an Arc1-P domain in a tetrameric complex resembling a classical GST homo-dimer. Domain-swapping between symmetrically related MetRS-N and Arc1p-N domains generates a 2:2 tetramer held together by van der Waals forces. This domain is necessary for formation of the aminoacyl-tRNA synthetase complex necessary for tRNA nuclear export and shuttling as part of the translational apparatus. The domain is associated with PF09334.
Simader H, Hothorn M, Kohler C, Basquin J, Simos G, Suck D; , Nucleic Acids Res. 2006;34:3968-3979.: Structural basis of yeast aminoacyl-tRNA synthetase complex formation revealed by crystal structures of two binary sub-complexes. PUBMED:16914447 EPMC:16914447
Internal database links
|SCOOP:||GST_N_2 GST_N_3 GST_N_4|
This tab holds annotation information from the InterPro database.
InterPro entry IPR018285
This entry represents the N-terminal domain of methionyl-tRNA synthetase (MetRS). This N-terminal appended domain mediates non-catalytic complex formation through its interaction with a domain in the tRNA aminoacylation cofactor Arc1p. The interacting domains of MetRS, GluRS (glutamyl-tRNA synthetase) and Arc1p form a ternary complex resembling a classical GST homo-dimer [PUBMED:16914447]. Domain-swapping between symmetrically related MetRS-N and Arc1p-N domains generates a 2:2 tetramer held together by van der Waals forces. This domain is necessary for formation of the aminoacyl-tRNA synthetase complex necessary for tRNA nuclear export and shuttling as part of the translational apparatus.
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Curation and family details
|Number in seed:||5|
|Number in full:||39|
|Average length of the domain:||115.20 aa|
|Average identity of full alignment:||32 %|
|Average coverage of the sequence by the domain:||15.49 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 11927849 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||7|
|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 MetRS-N domain has been found. There are 1 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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