NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|320545101|ref|NP_001188815|]
View 

tRNA-histidine guanylyltransferase, isoform B [Drosophila melanogaster]

Protein Classification

tRNA(His) guanylyltransferase( domain architecture ID 10517154)

tRNA(His) guanylyltransferase adds a GMP to the 5'-end of tRNA(His) after transcription and RNase P cleavage

EC:  2.7.7.79
Gene Ontology:  GO:0008193|GO:0006400
PubMed:  28623126

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Thg1 pfam04446
tRNAHis guanylyltransferase; The Thg1 protein from Saccharomyces cerevisiae is responsible for ...
 6-134 7.00e-81

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: 240.09  E-value: 7.00e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545101    6 FEYVKSFEQDDSILPNVWIVIRIDGKKFHKFSKTHDFEKPNDENALNVMNAAATAVMQEFRDIVLAYGQSDEYSFVFRKE 85
Cdd:pfam04446   1 YEYVKSFEQDDKLLPNTWIVVRIDGRGFHKFSKKHGFEKPNDERALDLMNEAAKDVMEEFPDIVLAYGQSDEYSFVFRKS 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 320545101   86 TAAFKRRSAKLLTYVTSLFSSSYVMQWSKWM-NLPLAYAPCFDGRVVLYP 134
Cdd:pfam04446  81 TTLFNRRVSKLVSLVASLFSSSYVFLWSKFFpDKPLLYPPSFDGRAVLYP 130
Thg1C pfam14413
Thg1 C terminal domain; Thg1 polymerases contain an additional region of conservation ...
 137-234 4.21e-56

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: 176.56  E-value: 4.21e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545101  137 QNLKDYLSWRQADVHVNNLYNTAFWKLVLEKGLTNQQAEAKLRGTFSADKNELLFQEFGINYNNLPAMYRKGTILLRKRV 216
Cdd:pfam14413   1 KNLRDYLSWRQVDCHINNLYNTTFWALVQKGGLTPTEAEERLKGTVSADKNEILFSEFGINYNNEPEIFRKGSVLVREEV 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 320545101  217 ILGE-----------------KSRQAVVPLHEDLI 234
Cdd:pfam14413  81 EETVtkptelsktqkekeekkRKKAKIVVLHCDII 115
 
Name Accession Description Interval E-value
Thg1 pfam04446
tRNAHis guanylyltransferase; The Thg1 protein from Saccharomyces cerevisiae is responsible for ...
 6-134 7.00e-81

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: 240.09  E-value: 7.00e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545101    6 FEYVKSFEQDDSILPNVWIVIRIDGKKFHKFSKTHDFEKPNDENALNVMNAAATAVMQEFRDIVLAYGQSDEYSFVFRKE 85
Cdd:pfam04446   1 YEYVKSFEQDDKLLPNTWIVVRIDGRGFHKFSKKHGFEKPNDERALDLMNEAAKDVMEEFPDIVLAYGQSDEYSFVFRKS 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 320545101   86 TAAFKRRSAKLLTYVTSLFSSSYVMQWSKWM-NLPLAYAPCFDGRVVLYP 134
Cdd:pfam04446  81 TTLFNRRVSKLVSLVASLFSSSYVFLWSKFFpDKPLLYPPSFDGRAVLYP 130
Thg1C pfam14413
Thg1 C terminal domain; Thg1 polymerases contain an additional region of conservation ...
 137-234 4.21e-56

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: 176.56  E-value: 4.21e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545101  137 QNLKDYLSWRQADVHVNNLYNTAFWKLVLEKGLTNQQAEAKLRGTFSADKNELLFQEFGINYNNLPAMYRKGTILLRKRV 216
Cdd:pfam14413   1 KNLRDYLSWRQVDCHINNLYNTTFWALVQKGGLTPTEAEERLKGTVSADKNEILFSEFGINYNNEPEIFRKGSVLVREEV 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 320545101  217 ILGE-----------------KSRQAVVPLHEDLI 234
Cdd:pfam14413  81 EETVtkptelsktqkekeekkRKKAKIVVLHCDII 115
Thg1 COG4021
tRNA(His) 5'-end guanylyltransferase [Translation, ribosomal structure and biogenesis]; tRNA ...
 10-221 2.27e-45

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: 153.09  E-value: 2.27e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545101  10 KSFEQ--DDSILPNVWIVIRIDGKKFHKFSKTHDFEKPNDENALNVMNAAATAVMQE--FRdIVLAYGQSDEYSFVFRKE 85
Cdd:COG4021    2 RVREIfhDLRVLPGLPVVVRLDGRGFTRLTKELGFEKPFDERFRDAMVETAEHLMKEsgFS-PVYAYTFSDEISLLFDEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545101  86 TaaFKRRSAKLLTYVTSLFSSSyvmqwskwMNLPLAYAPCFDGRVVLYPSEQnLKDYLSWRQADVHVNNLYNTAFWKLVL 165
Cdd:COG4021   81 P--FDRRVEKLDSVLAGEASAA--------FTLALGEPVAFDCRIIPLPNEL-VVDYFRWRQEEAWRNALNAYCYWTLRK 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 320545101 166 EkGLTNQQAEAKLRGTFSADKNELLFQeFGINYNNLPAMYRKGTILLRKRV-------ILGEK 221
Cdd:COG4021  150 E-GMSPREAAARLKGMKVAEKHELLFQ-RGINFNDLPAWQRRGIGVYWEEYekegynpVTGEK 210
 
Name Accession Description Interval E-value
Thg1 pfam04446
tRNAHis guanylyltransferase; The Thg1 protein from Saccharomyces cerevisiae is responsible for ...
 6-134 7.00e-81

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: 240.09  E-value: 7.00e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545101    6 FEYVKSFEQDDSILPNVWIVIRIDGKKFHKFSKTHDFEKPNDENALNVMNAAATAVMQEFRDIVLAYGQSDEYSFVFRKE 85
Cdd:pfam04446   1 YEYVKSFEQDDKLLPNTWIVVRIDGRGFHKFSKKHGFEKPNDERALDLMNEAAKDVMEEFPDIVLAYGQSDEYSFVFRKS 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 320545101   86 TAAFKRRSAKLLTYVTSLFSSSYVMQWSKWM-NLPLAYAPCFDGRVVLYP 134
Cdd:pfam04446  81 TTLFNRRVSKLVSLVASLFSSSYVFLWSKFFpDKPLLYPPSFDGRAVLYP 130
Thg1C pfam14413
Thg1 C terminal domain; Thg1 polymerases contain an additional region of conservation ...
 137-234 4.21e-56

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: 176.56  E-value: 4.21e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545101  137 QNLKDYLSWRQADVHVNNLYNTAFWKLVLEKGLTNQQAEAKLRGTFSADKNELLFQEFGINYNNLPAMYRKGTILLRKRV 216
Cdd:pfam14413   1 KNLRDYLSWRQVDCHINNLYNTTFWALVQKGGLTPTEAEERLKGTVSADKNEILFSEFGINYNNEPEIFRKGSVLVREEV 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 320545101  217 ILGE-----------------KSRQAVVPLHEDLI 234
Cdd:pfam14413  81 EETVtkptelsktqkekeekkRKKAKIVVLHCDII 115
Thg1 COG4021
tRNA(His) 5'-end guanylyltransferase [Translation, ribosomal structure and biogenesis]; tRNA ...
 10-221 2.27e-45

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: 153.09  E-value: 2.27e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545101  10 KSFEQ--DDSILPNVWIVIRIDGKKFHKFSKTHDFEKPNDENALNVMNAAATAVMQE--FRdIVLAYGQSDEYSFVFRKE 85
Cdd:COG4021    2 RVREIfhDLRVLPGLPVVVRLDGRGFTRLTKELGFEKPFDERFRDAMVETAEHLMKEsgFS-PVYAYTFSDEISLLFDEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545101  86 TaaFKRRSAKLLTYVTSLFSSSyvmqwskwMNLPLAYAPCFDGRVVLYPSEQnLKDYLSWRQADVHVNNLYNTAFWKLVL 165
Cdd:COG4021   81 P--FDRRVEKLDSVLAGEASAA--------FTLALGEPVAFDCRIIPLPNEL-VVDYFRWRQEEAWRNALNAYCYWTLRK 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 320545101 166 EkGLTNQQAEAKLRGTFSADKNELLFQeFGINYNNLPAMYRKGTILLRKRV-------ILGEK 221
Cdd:COG4021  150 E-GMSPREAAARLKGMKVAEKHELLFQ-RGINFNDLPAWQRRGIGVYWEEYekegynpVTGEK 210
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH