tRNAHis guanylyltransferase catalytic domain (IPR024956)

Short name: tRNAHis_GuaTrfase_cat

Overlapping homologous superfamilies

Domain relationships



The Thg1 protein from Saccharomyces cerevisiae is responsible for adding a GMP residue to the 5' end of tRNA His [PMID: 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 [PMID: 20591188]. Thg1 possesses an active site with three acidic residues that chelate Mg++ cations [PMID: 20591188]. Thg1 likely catalyses polymerisation using a similar mechanism to the 5'-3' polymerases [PMID: 20591188, PMID: 21059936].

GO terms

Biological Process

GO:0006400 tRNA modification

Molecular Function

GO:0000287 magnesium ion binding
GO:0008193 tRNA guanylyltransferase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.