The domain within your query sequence starts at position 2 and ends at position 104; the E-value for the Thg1 domain shown below is 2.1e-37.
TSRFAEEHNFAKPNDSRALHLMTKCAQTVMEELEDIVIAYGQSDEYSFVFRKKSNWFKRR ASKFMTLVASQFASSYVFYWRDYFEDQPLRYPPGFDGRVVLYP
Thg1 |
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| PFAM accession number: | PF04446 |
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| 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