Summary: tRNAHis guanylyltransferase
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tRNAHis guanylyltransferase Provide feedback
The Thg1 protein from Saccharomyces cerevisiae is responsible for adding a GMP residue to the 5' end of tRNA His [1]. 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 [2]. Thg1 possesses an active site with three acidic residues that chelate Mg++ cations [2]. Thg1 catalyzes polymerization similar to the 5'-3' polymerases [2].
Literature references
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Gu W, Jackman JE, Lohan AJ, Gray MW, Phizicky EM; , 17;0:0-0.: tRNAHis maturation: An essential yeast protein catalyzes addition of a guanine nucleotide to the 5' end of tRNAHis. PUBMED:14633974 EPMC:14633974
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Anantharaman V, Iyer LM, Aravind L;, Biol Direct. 2010;5:43.: 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. PUBMED:20591188 EPMC:20591188
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Hyde SJ, Eckenroth BE, Smith BA, Eberley WA, Heintz NH, Jackman JE, Doublie S;, Proc Natl Acad Sci U S A. 2010;107:20305-20310.: tRNA(His) guanylyltransferase (THG1), a unique 3'-5' nucleotidyl transferase, shares unexpected structural homology with canonical 5'-3' DNA polymerases. PUBMED:21059936 EPMC:21059936
This tab holds annotation information from the InterPro database.
InterPro entry 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].
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
Molecular function | magnesium ion binding (GO:0000287) |
tRNA guanylyltransferase activity (GO:0008193) | |
Biological process | tRNA modification (GO:0006400) |
Domain organisation
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Alignments
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Seed (171) |
Full (1880) |
Representative proteomes | UniProt (3546) |
NCBI (4439) |
Meta (18) |
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RP15 (310) |
RP35 (857) |
RP55 (1446) |
RP75 (2035) |
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PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
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Seed (171) |
Full (1880) |
Representative proteomes | UniProt (3546) |
NCBI (4439) |
Meta (18) |
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RP15 (310) |
RP35 (857) |
RP55 (1446) |
RP75 (2035) |
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Raw Stockholm | |||||||||
Gzipped |
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
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Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
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Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
Seed source: | Manual |
Previous IDs: | DUF549; |
Type: | Domain |
Sequence Ontology: | SO:0000417 |
Author: |
Anantharaman V |
Number in seed: | 171 |
Number in full: | 1880 |
Average length of the domain: | 124.00 aa |
Average identity of full alignment: | 42 % |
Average coverage of the sequence by the domain: | 38.31 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 47079205 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 126 | ||||||||||||
Family (HMM) version: | 13 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Thg1 domain has been found. There are 30 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.
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