Summary: Catalytic cysteine-containing C-terminus of GTPase, MnmE
Catalytic cysteine-containing C-terminus of GTPase, MnmE Provide feedback
This short C-terminal region contains the only cysteine present in these proteins. It is proposed that MnmE is a tRNA-modifying enzyme and that Cys-451 functions as a catalytic residue in the modification reaction.
Yim L, Martinez-Vicente M, Villarroya M, Aguado C, Knecht E, Armengod ME;, J Biol Chem. 2003;278:28378-28387.: The GTPase activity and C-terminal cysteine of the Escherichia coli MnmE protein are essential for its tRNA modifying function. PUBMED:12730230 EPMC:12730230
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This tab holds annotation information from the InterPro database.
InterPro entry IPR025867
This entry represents the short C-terminal domain of MnmE, containing the only cysteine present in these proteins. It is proposed that MnmE is a tRNA-modifying enzyme [PUBMED:10601028] and that Cys-451 functions as a catalytic residue in the modification reaction.
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Curation and family details
|Seed source:||Pfam-B_102 (release 24.0)|
|Number in seed:||534|
|Number in full:||4286|
|Average length of the domain:||72.50 aa|
|Average identity of full alignment:||33 %|
|Average coverage of the sequence by the domain:||15.93 %|
|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:||2|
|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 GTPase_Cys_C domain has been found. There are 8 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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