NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|961349610|ref|NP_001304755|]
View 

probable tRNA(His) guanylyltransferase isoform 4 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Thg1C pfam14413
Thg1 C terminal domain; Thg1 polymerases contain an additional region of conservation ...
 105-221 7.77e-76

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: 224.71  E-value: 7.77e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961349610  105 QTLKDYLSWRQADCHINNLYNTVFWALIQQSGLTPVQAQGRLQGTLAADKNEILFSEFNINYNNELPMYRKGTVLIWQKV 184
Cdd:pfam14413   1 KNLRDYLSWRQVDCHINNLYNTTFWALVQKGGLTPTEAEERLKGTVSADKNEILFSEFGINYNNEPEIFRKGSVLVREEV 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 961349610  185 DEVMTKEIKLPtEMEGKKMAVTRTRTKPVPLHCDIIG 221
Cdd:pfam14413  81 EETVTKPTELS-KTQKEKEEKKRKKAKIVVLHCDIIG 116
Thg1 pfam04446
tRNAHis guanylyltransferase; The Thg1 protein from Saccharomyces cerevisiae is responsible for ...
 2-102 7.69e-58

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: 179.61  E-value: 7.69e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961349610    2 RFAEKHNFAKPNDSRALQLMTKCAQTVMEELEDIVIAYGQSDEYSFVFKRKTNWFKRRASKFMTHVASQFASSYVFYWRD 81
Cdd:pfam04446  30 KFSKKHGFEKPNDERALDLMNEAAKDVMEEFPDIVLAYGQSDEYSFVFRKSTTLFNRRVSKLVSLVASLFSSSYVFLWSK 109

                          90       100
                  ....*....|....*....|.
gi 961349610   82 YFEDQPLLYPPGFDGRVVVYP 102
Cdd:pfam04446 110 FFPDKPLLYPPSFDGRAVLYP 130
 
Name Accession Description Interval E-value
Thg1C pfam14413
Thg1 C terminal domain; Thg1 polymerases contain an additional region of conservation ...
 105-221 7.77e-76

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: 224.71  E-value: 7.77e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961349610  105 QTLKDYLSWRQADCHINNLYNTVFWALIQQSGLTPVQAQGRLQGTLAADKNEILFSEFNINYNNELPMYRKGTVLIWQKV 184
Cdd:pfam14413   1 KNLRDYLSWRQVDCHINNLYNTTFWALVQKGGLTPTEAEERLKGTVSADKNEILFSEFGINYNNEPEIFRKGSVLVREEV 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 961349610  185 DEVMTKEIKLPtEMEGKKMAVTRTRTKPVPLHCDIIG 221
Cdd:pfam14413  81 EETVTKPTELS-KTQKEKEEKKRKKAKIVVLHCDIIG 116
Thg1 pfam04446
tRNAHis guanylyltransferase; The Thg1 protein from Saccharomyces cerevisiae is responsible for ...
 2-102 7.69e-58

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: 179.61  E-value: 7.69e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961349610    2 RFAEKHNFAKPNDSRALQLMTKCAQTVMEELEDIVIAYGQSDEYSFVFKRKTNWFKRRASKFMTHVASQFASSYVFYWRD 81
Cdd:pfam04446  30 KFSKKHGFEKPNDERALDLMNEAAKDVMEEFPDIVLAYGQSDEYSFVFRKSTTLFNRRVSKLVSLVASLFSSSYVFLWSK 109

                          90       100
                  ....*....|....*....|.
gi 961349610   82 YFEDQPLLYPPGFDGRVVVYP 102
Cdd:pfam04446 110 FFPDKPLLYPPSFDGRAVLYP 130
Thg1 COG4021
tRNA(His) 5'-end guanylyltransferase [Translation, ribosomal structure and biogenesis]; tRNA ...
 2-209 3.82e-30

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: 111.88  E-value: 3.82e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961349610   2 RFAEKHNFAKPNDSRALQLMTKCAQTVMEELE-DIVIAYGQSDEYSFVFKRKTnwFKRRASKFMTHVASqFASSYVFYwr 80
Cdd:COG4021   29 RLTKELGFEKPFDERFRDAMVETAEHLMKESGfSPVYAYTFSDEISLLFDELP--FDRRVEKLDSVLAG-EASAAFTL-- 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961349610  81 dyfedqpLLYPPG-FDGRVVVYPSNQTLkDYLSWRQADCHINNLYNTVFWALIQQsGLTPVQAQGRLQGTLAADKNEILF 159
Cdd:COG4021  104 -------ALGEPVaFDCRIIPLPNELVV-DYFRWRQEEAWRNALNAYCYWTLRKE-GMSPREAAARLKGMKVAEKHELLF 174

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 961349610 160 sEFNINYnNELPMY-RKGTVLIWqkvdEVMTKEIKLPteMEGKKMAVTRTR 209
Cdd:COG4021  175 -QRGINF-NDLPAWqRRGIGVYW----EEYEKEGYNP--VTGEKVLTTRRR 217
 
Name Accession Description Interval E-value
Thg1C pfam14413
Thg1 C terminal domain; Thg1 polymerases contain an additional region of conservation ...
 105-221 7.77e-76

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: 224.71  E-value: 7.77e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961349610  105 QTLKDYLSWRQADCHINNLYNTVFWALIQQSGLTPVQAQGRLQGTLAADKNEILFSEFNINYNNELPMYRKGTVLIWQKV 184
Cdd:pfam14413   1 KNLRDYLSWRQVDCHINNLYNTTFWALVQKGGLTPTEAEERLKGTVSADKNEILFSEFGINYNNEPEIFRKGSVLVREEV 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 961349610  185 DEVMTKEIKLPtEMEGKKMAVTRTRTKPVPLHCDIIG 221
Cdd:pfam14413  81 EETVTKPTELS-KTQKEKEEKKRKKAKIVVLHCDIIG 116
Thg1 pfam04446
tRNAHis guanylyltransferase; The Thg1 protein from Saccharomyces cerevisiae is responsible for ...
 2-102 7.69e-58

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: 179.61  E-value: 7.69e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961349610    2 RFAEKHNFAKPNDSRALQLMTKCAQTVMEELEDIVIAYGQSDEYSFVFKRKTNWFKRRASKFMTHVASQFASSYVFYWRD 81
Cdd:pfam04446  30 KFSKKHGFEKPNDERALDLMNEAAKDVMEEFPDIVLAYGQSDEYSFVFRKSTTLFNRRVSKLVSLVASLFSSSYVFLWSK 109

                          90       100
                  ....*....|....*....|.
gi 961349610   82 YFEDQPLLYPPGFDGRVVVYP 102
Cdd:pfam04446 110 FFPDKPLLYPPSFDGRAVLYP 130
Thg1 COG4021
tRNA(His) 5'-end guanylyltransferase [Translation, ribosomal structure and biogenesis]; tRNA ...
 2-209 3.82e-30

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: 111.88  E-value: 3.82e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961349610   2 RFAEKHNFAKPNDSRALQLMTKCAQTVMEELE-DIVIAYGQSDEYSFVFKRKTnwFKRRASKFMTHVASqFASSYVFYwr 80
Cdd:COG4021   29 RLTKELGFEKPFDERFRDAMVETAEHLMKESGfSPVYAYTFSDEISLLFDELP--FDRRVEKLDSVLAG-EASAAFTL-- 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961349610  81 dyfedqpLLYPPG-FDGRVVVYPSNQTLkDYLSWRQADCHINNLYNTVFWALIQQsGLTPVQAQGRLQGTLAADKNEILF 159
Cdd:COG4021  104 -------ALGEPVaFDCRIIPLPNELVV-DYFRWRQEEAWRNALNAYCYWTLRKE-GMSPREAAARLKGMKVAEKHELLF 174

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 961349610 160 sEFNINYnNELPMY-RKGTVLIWqkvdEVMTKEIKLPteMEGKKMAVTRTR 209
Cdd:COG4021  175 -QRGINF-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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH