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Conserved domains on  [gi|961349606|ref|NP_001304753|]
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probable tRNA(His) guanylyltransferase isoform 2 [Homo sapiens]

Protein Classification

Thg1C domain-containing protein( domain architecture ID 10627615)

Thg1C domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Thg1C pfam14413
Thg1 C terminal domain; Thg1 polymerases contain an additional region of conservation ...
35-151 2.11e-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: 225.86  E-value: 2.11e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961349606   35 QTLKDYLSWRQADCHINNLYNTVFWALIQQSGLTPVQAQGRLQGTLAADKNEILFSEFNINYNNELPMYRKGTVLIWQKV 114
Cdd:pfam14413   1 KNLRDYLSWRQVDCHINNLYNTTFWALVQKGGLTPTEAEERLKGTVSADKNEILFSEFGINYNNEPEIFRKGSVLVREEV 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 961349606  115 DEVMTKEIKLPtEMEGKKMAVTRTRTKPVPLHCDIIG 151
Cdd:pfam14413  81 EETVTKPTELS-KTQKEKEEKKRKKAKIVVLHCDIIG 116
 
Name Accession Description Interval E-value
Thg1C pfam14413
Thg1 C terminal domain; Thg1 polymerases contain an additional region of conservation ...
35-151 2.11e-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: 225.86  E-value: 2.11e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961349606   35 QTLKDYLSWRQADCHINNLYNTVFWALIQQSGLTPVQAQGRLQGTLAADKNEILFSEFNINYNNELPMYRKGTVLIWQKV 114
Cdd:pfam14413   1 KNLRDYLSWRQVDCHINNLYNTTFWALVQKGGLTPTEAEERLKGTVSADKNEILFSEFGINYNNEPEIFRKGSVLVREEV 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 961349606  115 DEVMTKEIKLPtEMEGKKMAVTRTRTKPVPLHCDIIG 151
Cdd:pfam14413  81 EETVTKPTELS-KTQKEKEEKKRKKAKIVVLHCDIIG 116
Thg1 COG4021
tRNA(His) 5'-end guanylyltransferase [Translation, ribosomal structure and biogenesis]; tRNA ...
16-139 4.70e-20

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: 82.99  E-value: 4.70e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961349606  16 IGLKEEPGFDGRVVVYPSNQTLkDYLSWRQADCHINNLYNTVFWALIQQsGLTPVQAQGRLQGTLAADKNEILFsEFNIN 95
Cdd:COG4021  103 LALGEPVAFDCRIIPLPNELVV-DYFRWRQEEAWRNALNAYCYWTLRKE-GMSPREAAARLKGMKVAEKHELLF-QRGIN 179
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 961349606  96 YnNELPMY-RKGTVLIWqkvdEVMTKEIKLPteMEGKKMAVTRTR 139
Cdd:COG4021  180 F-NDLPAWqRRGIGVYW----EEYEKEGYNP--VTGEKVLTTRRR 217
 
Name Accession Description Interval E-value
Thg1C pfam14413
Thg1 C terminal domain; Thg1 polymerases contain an additional region of conservation ...
35-151 2.11e-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: 225.86  E-value: 2.11e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961349606   35 QTLKDYLSWRQADCHINNLYNTVFWALIQQSGLTPVQAQGRLQGTLAADKNEILFSEFNINYNNELPMYRKGTVLIWQKV 114
Cdd:pfam14413   1 KNLRDYLSWRQVDCHINNLYNTTFWALVQKGGLTPTEAEERLKGTVSADKNEILFSEFGINYNNEPEIFRKGSVLVREEV 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 961349606  115 DEVMTKEIKLPtEMEGKKMAVTRTRTKPVPLHCDIIG 151
Cdd:pfam14413  81 EETVTKPTELS-KTQKEKEEKKRKKAKIVVLHCDIIG 116
Thg1 COG4021
tRNA(His) 5'-end guanylyltransferase [Translation, ribosomal structure and biogenesis]; tRNA ...
16-139 4.70e-20

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: 82.99  E-value: 4.70e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961349606  16 IGLKEEPGFDGRVVVYPSNQTLkDYLSWRQADCHINNLYNTVFWALIQQsGLTPVQAQGRLQGTLAADKNEILFsEFNIN 95
Cdd:COG4021  103 LALGEPVAFDCRIIPLPNELVV-DYFRWRQEEAWRNALNAYCYWTLRKE-GMSPREAAARLKGMKVAEKHELLF-QRGIN 179
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 961349606  96 YnNELPMY-RKGTVLIWqkvdEVMTKEIKLPteMEGKKMAVTRTR 139
Cdd:COG4021  180 F-NDLPAWqRRGIGVYW----EEYEKEGYNP--VTGEKVLTTRRR 217
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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