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Conserved domains on  [gi|1898583686|ref|XP_035863657|]
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probable tRNA(His) guanylyltransferase isoform X3 [Sander lucioperca]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Thg1 pfam04446
tRNAHis guanylyltransferase; The Thg1 protein from Saccharomyces cerevisiae is responsible for ...
 32-161 9.58e-80

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: 237.39  E-value: 9.58e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898583686  32 FEYVRNFETDDTCLRNCYIVVRLDGRNFHKFAEQHEFTKPNDDRALGLMSRSARSVMEELEDIVIAYGQSDEFSFVFKRT 111
Cdd:pfam04446   1 YEYVKSFEQDDKLLPNTWIVVRIDGRGFHKFSKKHGFEKPNDERALDLMNEAAKDVMEEFPDIVLAYGQSDEYSFVFRKS 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1898583686 112 STWFKRRASKLMTHVASQFSSSYVFYWKEFFGEQPLLYPPGFDGRVVLYP 161
Cdd:pfam04446  81 TTLFNRRVSKLVSLVASLFSSSYVFLWSKFFPDKPLLYPPSFDGRAVLYP 130
Thg1C pfam14413
Thg1 C terminal domain; Thg1 polymerases contain an additional region of conservation ...
 165-279 3.54e-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: 230.49  E-value: 3.54e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898583686 165 NLRDYLSWRQADCHINNLYNTVFWTLVQKGGLTTAQAEDRLKGTLAADKNEILFSEFHINYNTEPAVHRKGTTLIWEKRD 244
Cdd:pfam14413   2 NLRDYLSWRQVDCHINNLYNTTFWALVQKGGLTPTEAEERLKGTVSADKNEILFSEFGINYNNEPEIFRKGSVLVREEVE 81

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1898583686 245 ETVLKRMKLPNEEEKDVAVTRSRRRVQAHHCDIIG 279
Cdd:pfam14413  82 ETVTKPTELSKTQKEKEEKKRKKAKIVVLHCDIIG 116
 
Name Accession Description Interval E-value
Thg1 pfam04446
tRNAHis guanylyltransferase; The Thg1 protein from Saccharomyces cerevisiae is responsible for ...
 32-161 9.58e-80

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: 237.39  E-value: 9.58e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898583686  32 FEYVRNFETDDTCLRNCYIVVRLDGRNFHKFAEQHEFTKPNDDRALGLMSRSARSVMEELEDIVIAYGQSDEFSFVFKRT 111
Cdd:pfam04446   1 YEYVKSFEQDDKLLPNTWIVVRIDGRGFHKFSKKHGFEKPNDERALDLMNEAAKDVMEEFPDIVLAYGQSDEYSFVFRKS 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1898583686 112 STWFKRRASKLMTHVASQFSSSYVFYWKEFFGEQPLLYPPGFDGRVVLYP 161
Cdd:pfam04446  81 TTLFNRRVSKLVSLVASLFSSSYVFLWSKFFPDKPLLYPPSFDGRAVLYP 130
Thg1C pfam14413
Thg1 C terminal domain; Thg1 polymerases contain an additional region of conservation ...
 165-279 3.54e-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: 230.49  E-value: 3.54e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898583686 165 NLRDYLSWRQADCHINNLYNTVFWTLVQKGGLTTAQAEDRLKGTLAADKNEILFSEFHINYNTEPAVHRKGTTLIWEKRD 244
Cdd:pfam14413   2 NLRDYLSWRQVDCHINNLYNTTFWALVQKGGLTPTEAEERLKGTVSADKNEILFSEFGINYNNEPEIFRKGSVLVREEVE 81

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1898583686 245 ETVLKRMKLPNEEEKDVAVTRSRRRVQAHHCDIIG 279
Cdd:pfam14413  82 ETVTKPTELSKTQKEKEEKKRKKAKIVVLHCDIIG 116
Thg1 COG4021
tRNA(His) 5'-end guanylyltransferase [Translation, ribosomal structure and biogenesis]; tRNA ...
 36-270 1.68e-43

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: 148.47  E-value: 1.68e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898583686  36 RNFET--DDTCLRNCYIVVRLDGRNFHKFAEQHEFTKPNDDRALGLMSRSARSVMEELE-DIVIAYGQSDEFSFVFKRTS 112
Cdd:COG4021     2 RVREIfhDLRVLPGLPVVVRLDGRGFTRLTKELGFEKPFDERFRDAMVETAEHLMKESGfSPVYAYTFSDEISLLFDELP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898583686 113 twFKRRASKLMTHVASQFSSSYVFYWKEffgeqpllyPPGFDGRVVLYPSNhNLRDYLSWRQADCHINNLYNTVFWTLVq 192
Cdd:COG4021    82 --FDRRVEKLDSVLAGEASAAFTLALGE---------PVAFDCRIIPLPNE-LVVDYFRWRQEEAWRNALNAYCYWTLR- 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1898583686 193 KGGLTTAQAEDRLKGTLAADKNEILFsEFHINYNTEPAVHRKGTTLIWEKRDetvlKRMKLPNEEEKdVAVTRSRRRV 270
Cdd:COG4021   149 KEGMSPREAAARLKGMKVAEKHELLF-QRGINFNDLPAWQRRGIGVYWEEYE----KEGYNPVTGEK-VLTTRRRLVV 220
 
Name Accession Description Interval E-value
Thg1 pfam04446
tRNAHis guanylyltransferase; The Thg1 protein from Saccharomyces cerevisiae is responsible for ...
 32-161 9.58e-80

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: 237.39  E-value: 9.58e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898583686  32 FEYVRNFETDDTCLRNCYIVVRLDGRNFHKFAEQHEFTKPNDDRALGLMSRSARSVMEELEDIVIAYGQSDEFSFVFKRT 111
Cdd:pfam04446   1 YEYVKSFEQDDKLLPNTWIVVRIDGRGFHKFSKKHGFEKPNDERALDLMNEAAKDVMEEFPDIVLAYGQSDEYSFVFRKS 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1898583686 112 STWFKRRASKLMTHVASQFSSSYVFYWKEFFGEQPLLYPPGFDGRVVLYP 161
Cdd:pfam04446  81 TTLFNRRVSKLVSLVASLFSSSYVFLWSKFFPDKPLLYPPSFDGRAVLYP 130
Thg1C pfam14413
Thg1 C terminal domain; Thg1 polymerases contain an additional region of conservation ...
 165-279 3.54e-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: 230.49  E-value: 3.54e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898583686 165 NLRDYLSWRQADCHINNLYNTVFWTLVQKGGLTTAQAEDRLKGTLAADKNEILFSEFHINYNTEPAVHRKGTTLIWEKRD 244
Cdd:pfam14413   2 NLRDYLSWRQVDCHINNLYNTTFWALVQKGGLTPTEAEERLKGTVSADKNEILFSEFGINYNNEPEIFRKGSVLVREEVE 81

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1898583686 245 ETVLKRMKLPNEEEKDVAVTRSRRRVQAHHCDIIG 279
Cdd:pfam14413  82 ETVTKPTELSKTQKEKEEKKRKKAKIVVLHCDIIG 116
Thg1 COG4021
tRNA(His) 5'-end guanylyltransferase [Translation, ribosomal structure and biogenesis]; tRNA ...
 36-270 1.68e-43

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: 148.47  E-value: 1.68e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898583686  36 RNFET--DDTCLRNCYIVVRLDGRNFHKFAEQHEFTKPNDDRALGLMSRSARSVMEELE-DIVIAYGQSDEFSFVFKRTS 112
Cdd:COG4021     2 RVREIfhDLRVLPGLPVVVRLDGRGFTRLTKELGFEKPFDERFRDAMVETAEHLMKESGfSPVYAYTFSDEISLLFDELP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898583686 113 twFKRRASKLMTHVASQFSSSYVFYWKEffgeqpllyPPGFDGRVVLYPSNhNLRDYLSWRQADCHINNLYNTVFWTLVq 192
Cdd:COG4021    82 --FDRRVEKLDSVLAGEASAAFTLALGE---------PVAFDCRIIPLPNE-LVVDYFRWRQEEAWRNALNAYCYWTLR- 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1898583686 193 KGGLTTAQAEDRLKGTLAADKNEILFsEFHINYNTEPAVHRKGTTLIWEKRDetvlKRMKLPNEEEKdVAVTRSRRRV 270
Cdd:COG4021   149 KEGMSPREAAARLKGMKVAEKHELLF-QRGINFNDLPAWQRRGIGVYWEEYE----KEGYNPVTGEK-VLTTRRRLVV 220
 
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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