The domain within your query sequence starts at position 21 and ends at position 198; the E-value for the PTS_2-RNA domain shown below is 2.6e-67.

DRNVQLSKALSYALRHGALKLGLPMRADGFVPLQALLQLPQFHSFSIEDVQLVVNTNEKQ
RFTLQPGEPSTGLLIRANQGHSLQVPELELTPLETPQALPLTLVHGTFWKHWPSILLKGL
SRQGRTHIHLASGLPGDPGVISGIRPNCEVAVFIDGPLALTDGIPFFCSANGVILTPG

PTS_2-RNA

PTS_2-RNA
PFAM accession number:PF01885
Interpro abstract (IPR002745):

The final step of tRNA splicing in Saccharomyces cerevisiae (Baker's yeast) requires 2'-phosphotransferase (Tpt1) to transfer the 2'-phosphate from ligated tRNA to NAD, producing mature tRNA and ADP ribose-1' '-2' '-cyclic phosphate. Yeast and Mus musculus (Mouse) Tpt1 protein and bacterial KptA protein can catalyze the conversion of the generated intermediate to both product and the original substrate, these enzymes likely use the same reaction mechanism. Step 1 of this reaction is strikingly similar to the ADP-ribosylation of proteins catalyzed by a number of bacterial toxins.

KptA, a functional Tpt1 protein homologue from Escherichia coli is strikingly similar to yeast Tpt1 in its kinetic parameters, although E. coli is not known to have a 2'-phosphorylated RNA substrate [(PUBMED:9915792),(PUBMED:11705403)].

GO process:tRNA splicing, via endonucleolytic cleavage and ligation (GO:0006388)
GO function:transferase activity, transferring phosphorus-containing groups (GO:0016772)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry PTS_2-RNA