probable tRNA(His) guanylyltransferase isoform 3 [Homo sapiens]
Thg1 and Thg1C domain-containing protein( domain architecture ID 13563479)
Thg1 and Thg1C domain-containing protein
List of domain hits
Name | Accession | Description | Interval | E-value | |||
Thg1C | pfam14413 | Thg1 C terminal domain; Thg1 polymerases contain an additional region of conservation ... |
42-158 | 1.91e-77 | |||
Thg1 C terminal domain; Thg1 polymerases contain an additional region of conservation C-terminal to the core palm domain that comprise of 5 helices and two strands. This region has several well-conserved charged residues including a basic residue found towards the end of the first helix of this unit might contribute to the Thg1-specific active site. This C-terminal module of Thg1 is predicted to form a helical bundle that functions equivalently to the fingers of the other nucleic acid polymerases, probably in interacting with the template HtRNA. : Pssm-ID: 464167 Cd Length: 116 Bit Score: 226.25 E-value: 1.91e-77
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Thg1 super family | cl37709 | tRNAHis guanylyltransferase; The Thg1 protein from Saccharomyces cerevisiae is responsible for ... |
1-39 | 1.08e-15 | |||
tRNAHis guanylyltransferase; The Thg1 protein from Saccharomyces cerevisiae is responsible for adding a GMP residue to the 5' end of tRNA His. 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. Thg1 possesses an active site with three acidic residues that chelate Mg++ cations. Thg1 catalyzes polymerization similar to the 5'-3' polymerases. The actual alignment was detected with superfamily member pfam04446: Pssm-ID: 461314 Cd Length: 130 Bit Score: 69.44 E-value: 1.08e-15
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Name | Accession | Description | Interval | E-value | |||
Thg1C | pfam14413 | Thg1 C terminal domain; Thg1 polymerases contain an additional region of conservation ... |
42-158 | 1.91e-77 | |||
Thg1 C terminal domain; Thg1 polymerases contain an additional region of conservation C-terminal to the core palm domain that comprise of 5 helices and two strands. This region has several well-conserved charged residues including a basic residue found towards the end of the first helix of this unit might contribute to the Thg1-specific active site. This C-terminal module of Thg1 is predicted to form a helical bundle that functions equivalently to the fingers of the other nucleic acid polymerases, probably in interacting with the template HtRNA. Pssm-ID: 464167 Cd Length: 116 Bit Score: 226.25 E-value: 1.91e-77
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Thg1 | COG4021 | tRNA(His) 5'-end guanylyltransferase [Translation, ribosomal structure and biogenesis]; tRNA ... |
31-146 | 1.90e-19 | |||
tRNA(His) 5'-end guanylyltransferase [Translation, ribosomal structure and biogenesis]; tRNA(His) 5'-end guanylyltransferase is part of the Pathway/BioSystem: tRNA modification Pssm-ID: 443199 [Multi-domain] Cd Length: 235 Bit Score: 81.83 E-value: 1.90e-19
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Thg1 | pfam04446 | tRNAHis guanylyltransferase; The Thg1 protein from Saccharomyces cerevisiae is responsible for ... |
1-39 | 1.08e-15 | |||
tRNAHis guanylyltransferase; The Thg1 protein from Saccharomyces cerevisiae is responsible for adding a GMP residue to the 5' end of tRNA His. 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. Thg1 possesses an active site with three acidic residues that chelate Mg++ cations. Thg1 catalyzes polymerization similar to the 5'-3' polymerases. Pssm-ID: 461314 Cd Length: 130 Bit Score: 69.44 E-value: 1.08e-15
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Name | Accession | Description | Interval | E-value | |||
Thg1C | pfam14413 | Thg1 C terminal domain; Thg1 polymerases contain an additional region of conservation ... |
42-158 | 1.91e-77 | |||
Thg1 C terminal domain; Thg1 polymerases contain an additional region of conservation C-terminal to the core palm domain that comprise of 5 helices and two strands. This region has several well-conserved charged residues including a basic residue found towards the end of the first helix of this unit might contribute to the Thg1-specific active site. This C-terminal module of Thg1 is predicted to form a helical bundle that functions equivalently to the fingers of the other nucleic acid polymerases, probably in interacting with the template HtRNA. Pssm-ID: 464167 Cd Length: 116 Bit Score: 226.25 E-value: 1.91e-77
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Thg1 | COG4021 | tRNA(His) 5'-end guanylyltransferase [Translation, ribosomal structure and biogenesis]; tRNA ... |
31-146 | 1.90e-19 | |||
tRNA(His) 5'-end guanylyltransferase [Translation, ribosomal structure and biogenesis]; tRNA(His) 5'-end guanylyltransferase is part of the Pathway/BioSystem: tRNA modification Pssm-ID: 443199 [Multi-domain] Cd Length: 235 Bit Score: 81.83 E-value: 1.90e-19
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Thg1 | pfam04446 | tRNAHis guanylyltransferase; The Thg1 protein from Saccharomyces cerevisiae is responsible for ... |
1-39 | 1.08e-15 | |||
tRNAHis guanylyltransferase; The Thg1 protein from Saccharomyces cerevisiae is responsible for adding a GMP residue to the 5' end of tRNA His. 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. Thg1 possesses an active site with three acidic residues that chelate Mg++ cations. Thg1 catalyzes polymerization similar to the 5'-3' polymerases. Pssm-ID: 461314 Cd Length: 130 Bit Score: 69.44 E-value: 1.08e-15
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Blast search parameters | ||||
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