{"metadata":{"accession":"PF04446","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR024956","hierarchy":null,"name":{"name":"tRNAHis guanylyltransferase","short":"Thg1"},"description":[{"text":"<p>The Thg1 protein from Saccharomyces cerevisiae is responsible for adding a GMP residue to the 5' end of tRNA His [[cite:PUB00020433]]. The catalytic domain 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 [[cite:PUB00057251]]. Thg1 possesses an active site with three  acidic residues that chelate Mg++ cations [[cite:PUB00057251]]. Thg1 catalyzes  polymerization similar to the 5'-3' polymerases [[cite:PUB00057251]][[cite:PUB00057252]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00057252":{"PMID":21059936,"ISBN":null,"volume":"107","issue":"47","year":2010,"title":"tRNA(His) guanylyltransferase (THG1), a unique 3'-5' nucleotidyl transferase, shares unexpected structural homology with canonical 5'-3' DNA polymerases.","URL":null,"raw_pages":"20305-10","medline_journal":"Proc Natl Acad Sci U S A","ISO_journal":"Proc. Natl. Acad. Sci. U.S.A.","authors":["Hyde SJ","Eckenroth BE","Smith BA","Eberley WA","Heintz NH","Jackman JE","Doublie S."],"DOI_URL":"http://dx.doi.org/10.1073/pnas.1010436107"},"PUB00020433":{"PMID":14633974,"ISBN":null,"volume":"17","issue":"23","year":2003,"title":"tRNAHis maturation: an essential yeast protein catalyzes addition of a guanine nucleotide to the 5' end of tRNAHis.","URL":null,"raw_pages":"2889-901","medline_journal":"Genes Dev","ISO_journal":"Genes Dev.","authors":["Gu W","Jackman JE","Lohan AJ","Gray MW","Phizicky EM."],"DOI_URL":"http://dx.doi.org/10.1101/gad.1148603"},"PUB00057251":{"PMID":20591188,"ISBN":null,"volume":"5","issue":null,"year":2010,"title":"Presence of a classical RRM-fold palm domain in Thg1-type 3'- 5'nucleic acid polymerases and the origin of the GGDEF and CRISPR polymerase domains.","URL":null,"raw_pages":"43","medline_journal":"Biol Direct","ISO_journal":"Biol. Direct","authors":["Anantharaman V","Iyer LM","Aravind L."],"DOI_URL":"http://dx.doi.org/10.1186/1745-6150-5-43"}},"set_info":null,"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":102,"interactions":0,"matches":5546,"pathways":0,"proteins":4888,"proteomes":3738,"sets":0,"structural_models":{"alphafold":3998},"structures":16,"taxa":9628},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":152,"alignment:full":3920},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}