Summary: Prolyl-tRNA synthetase, C-terminal
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Prolyl-tRNA synthetase, C-terminal Provide feedback
Members of this family are predominantly found in prokaryotic prolyl-tRNA synthetase. They contain a zinc binding site, and adopt a structure consisting of alpha helices and antiparallel beta sheets arranged in 2 layers, in a beta-alpha-beta-alpha-beta motif .
Kamtekar S, Kennedy WD, Wang J, Stathopoulos C, Soll D, Steitz TA; , Proc Natl Acad Sci U S A. 2003;100:1673-1678.: The structural basis of cysteine aminoacylation of tRNAPro by prolyl-tRNA synthetases. PUBMED:12578991 EPMC:12578991
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR015264
The aminoacyl-tRNA synthetases (EC) catalyse the attachment of an amino acid to its cognate transfer RNA molecule in a highly specific two-step reaction. These proteins differ widely in size and oligomeric state, and have limited sequence homology [PUBMED:2203971]. The 20 aminoacyl-tRNA synthetases are divided into two classes, I and II. Class I aminoacyl-tRNA synthetases contain a characteristic Rossman fold catalytic domain and are mostly monomeric [PUBMED:10673435]. Class II aminoacyl-tRNA synthetases share an anti-parallel beta-sheet fold flanked by alpha-helices [PUBMED:8364025], and are mostly dimeric or multimeric, containing at least three conserved regions [PUBMED:8274143, PUBMED:2053131, PUBMED:1852601]. However, tRNA binding involves an alpha-helical structure that is conserved between class I and class II synthetases. In reactions catalysed by the class I aminoacyl-tRNA synthetases, the aminoacyl group is coupled to the 2'-hydroxyl of the tRNA, while, in class II reactions, the 3'-hydroxyl site is preferred. The synthetases specific for arginine, cysteine, glutamic acid, glutamine, isoleucine, leucine, methionine, tyrosine, tryptophan and valine belong to class I synthetases. The synthetases specific for alanine, asparagine, aspartic acid, glycine, histidine, lysine, phenylalanine, proline, serine, and threonine belong to class-II synthetases [PUBMED:]. Based on their mode of binding to the tRNA acceptor stem, both classes of tRNA synthetases have been subdivided into three subclasses, designated 1a, 1b, 1c and 2a, 2b, 2c.
This domain is found predominantly found in prolyl-tRNA synthetases from archaeal Methanococci species. It contains a zinc binding site, and adopts a structure consisting of alpha helices and antiparallel beta sheets arranged in 2 layers, in a beta-alpha-beta-alpha-beta motif [PUBMED:12578991].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||cytoplasm (GO:0005737)|
|Molecular function||ATP binding (GO:0005524)|
|nucleotide binding (GO:0000166)|
|proline-tRNA ligase activity (GO:0004827)|
|Biological process||prolyl-tRNA aminoacylation (GO:0006433)|
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|Number in seed:||4|
|Number in full:||16|
|Average length of the domain:||65.10 aa|
|Average identity of full alignment:||57 %|
|Average coverage of the sequence by the domain:||14.15 %|
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build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||5|
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