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His/Gly/Thr/Pro-type tRNA ligase C-terminal domain-containing protein
This HMM hits a C-terminal region, thought to be the anticodin-binding domain, of tRNA ligases for amino acids His, Gly, Thr, and Pro. Proteins named by this HMM are mostly partials, scoring below cutoffs of more specific models because incomplete sequences generate insufficient scores.
aminoacyl--tRNA ligase-related protein
This HMM finds multiple types of aminoacyl--tRNA ligase, such as those for Thr, Pro, His, and Ser in Escherichia coli. Because equivalog-level HMMs exist to identify full-length members of the tRNA ligase families, any protein receiving annotation from this HMM is most likely to be either a partial sequence or a tRNA ligase-related protein involved in some process other than protein translation on the ribosome.
proline--tRNA ligase
Catalyzes the formation of prolyl-tRNA(Pro) from proline and tRNA(Pro)
proline--tRNA ligase catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro)
Prolyl-tRNA synthetase is a class II tRNA synthetase and is recognized by pfam HMM tRNA-synt_2b, which recognizes tRNA synthetases for Gly, His, Ser, and Pro. The prolyl-tRNA synthetases are divided into two widely divergent groups. This group includes enzymes from Escherichia coli, Bacillus subtilis, Aquifex aeolicus, the spirochete Treponema pallidum, Synechocystis PCC6803, and one of the two prolyL-tRNA synthetases of Saccharomyces cerevisiae. The other group includes the Pro-specific domain of a human multifunctional tRNA ligase and the prolyl-tRNA synthetases from the Archaea, the Mycoplasmas, and the spirochete Borrelia burgdorferi.
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