The domain within your query sequence starts at position 35 and ends at position 164; the E-value for the Thg1 domain shown below is 1e-53.



PFAM accession number:PF04446
Interpro abstract (IPR024956):

The Thg1 protein from Saccharomyces cerevisiae is responsible for adding a GMP residue to the 5' end of tRNA His [(PUBMED:14633974)]. The catalytic domain of Thg1 contains a RRM (ferredoxin) fold palm domain, just like the viral RNA-dependent RNA polymerases, reverse transcriptases, family A and B DNA polymerases, adenylyl cyclases, diguanylate cyclases (GGDEF domain) and the predicted polymerase of the CRISPR system [(PUBMED:20591188)]. Thg1 possesses an active site with three acidic residues that chelate Mg++ cations [(PUBMED:20591188)]. Thg1 likely catalyses polymerisation using a similar mechanism to the 5'-3' polymerases [(PUBMED:20591188), (PUBMED:21059936)].

GO process:tRNA modification (GO:0006400)
GO function:magnesium ion binding (GO:0000287), tRNA guanylyltransferase activity (GO:0008193)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Thg1