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Conserved domains on  [gi|238479418|ref|NP_001154545|]
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tRNAHis guanylyltransferase [Arabidopsis thaliana]

Protein Classification

Thg1 and Thg1C domain-containing protein( domain architecture ID 11149964)

protein containing domains PLN00220, Thg1, and Thg1C

Graphical summary

 Zoom to residue level

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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 ...
 280-408 4.15e-74

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: 230.84  E-value: 4.15e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479418  280 DYVKSFQFESRLLPLTWVVVRIDGCHFHRFSEVHEFEKPNDEQALKLMNSCAVAVLEEFQDIAFAYGVSDEFSFVLKNKS 359
Cdd:pfam04446   2 EYVKSFEQDDKLLPNTWIVVRIDGRGFHKFSKKHGFEKPNDERALDLMNEAAKDVMEEFPDIVLAYGQSDEYSFVFRKST 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 238479418  360 ELYKRQSSKIISAVVSFFTSTYMMRWGDFFPHKKLKYPPSFDGRAVCYP 408
Cdd:pfam04446  82 TLFNRRVSKLVSLVASLFSSSYVFLWSKFFPDKPLLYPPSFDGRAVLYP 130
Thg1 pfam04446
tRNAHis guanylyltransferase; The Thg1 protein from Saccharomyces cerevisiae is responsible for ...
 6-132 5.10e-63

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: 201.95  E-value: 5.10e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479418    6 YEYVKSFEVEDEVMFPNLIIIRIDGRDFSRFSQVHKFEKPNDETSLNLMNSCASSVLVEYPDIVFAYGYSDEYSFVFKKA 85
Cdd:pfam04446   1 YEYVKSFEQDDKLLPNTWIVVRIDGRGFHKFSKKHGFEKPNDERALDLMNEAAKDVMEEFPDIVLAYGQSDEYSFVFRKS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 238479418   86 SRFYQRRASKILSLVASFFAAVYVTKWKEFFPHTKLEYAPSFASKVV 132
Cdd:pfam04446  81 TTLFNRRVSKLVSLVASLFSSSYVFLWSKFFPDKPLLYPPSFDGRAV 127
Thg1C pfam14413
Thg1 C terminal domain; Thg1 polymerases contain an additional region of conservation ...
 412-517 2.36e-47

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: 160.38  E-value: 2.36e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479418  412 ILLDYLAWRQVDCHINNQYNTCFWMLV-KSGKSKIQAQDYLKGTQTREKNELLSQQFGIEYNSLPVIFRMGSSVFRLKTQ 490
Cdd:pfam14413   2 NLRDYLSWRQVDCHINNLYNTTFWALVqKGGLTPTEAEERLKGTVSADKNEILFSEFGINYNNEPEIFRKGSVLVREEVE 81

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 238479418  491 EGVTEEnGEVSGKQVE--------AEVGVDYSNII 517
Cdd:pfam14413  82 ETVTKP-TELSKTQKEkeekkrkkAKIVVLHCDII 115
Thg1C super family cl16863
Thg1 C terminal domain; Thg1 polymerases contain an additional region of conservation ...
 138-247 8.87e-34

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.


The actual alignment was detected with superfamily member pfam14413:

Pssm-ID: 464167  Cd Length: 116  Bit Score: 123.79  E-value: 8.87e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479418  138 EVLQAYLAWRQHDCHISNQYDTCLWMLV-KSGKTLSETQEILKDTQKQQRNELLFQQFGINYKMLPVLFRQGSCLFKTKK 216
Cdd:pfam14413   1 KNLRDYLSWRQVDCHINNLYNTTFWALVqKGGLTPTEAEERLKGTVSADKNEILFSEFGINYNNEPEIFRKGSVLVREEV 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 238479418  217 SKSFQLLEETVKHDENGKPVKRLRRRETLVH 247
Cdd:pfam14413  81 EETVTKPTELSKTQKEKEEKKRKKAKIVVLH 111
 
Name Accession Description Interval E-value
Thg1 pfam04446
tRNAHis guanylyltransferase; The Thg1 protein from Saccharomyces cerevisiae is responsible for ...
 280-408 4.15e-74

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: 230.84  E-value: 4.15e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479418  280 DYVKSFQFESRLLPLTWVVVRIDGCHFHRFSEVHEFEKPNDEQALKLMNSCAVAVLEEFQDIAFAYGVSDEFSFVLKNKS 359
Cdd:pfam04446   2 EYVKSFEQDDKLLPNTWIVVRIDGRGFHKFSKKHGFEKPNDERALDLMNEAAKDVMEEFPDIVLAYGQSDEYSFVFRKST 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 238479418  360 ELYKRQSSKIISAVVSFFTSTYMMRWGDFFPHKKLKYPPSFDGRAVCYP 408
Cdd:pfam04446  82 TLFNRRVSKLVSLVASLFSSSYVFLWSKFFPDKPLLYPPSFDGRAVLYP 130
Thg1 pfam04446
tRNAHis guanylyltransferase; The Thg1 protein from Saccharomyces cerevisiae is responsible for ...
 6-132 5.10e-63

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: 201.95  E-value: 5.10e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479418    6 YEYVKSFEVEDEVMFPNLIIIRIDGRDFSRFSQVHKFEKPNDETSLNLMNSCASSVLVEYPDIVFAYGYSDEYSFVFKKA 85
Cdd:pfam04446   1 YEYVKSFEQDDKLLPNTWIVVRIDGRGFHKFSKKHGFEKPNDERALDLMNEAAKDVMEEFPDIVLAYGQSDEYSFVFRKS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 238479418   86 SRFYQRRASKILSLVASFFAAVYVTKWKEFFPHTKLEYAPSFASKVV 132
Cdd:pfam04446  81 TTLFNRRVSKLVSLVASLFSSSYVFLWSKFFPDKPLLYPPSFDGRAV 127
Thg1C pfam14413
Thg1 C terminal domain; Thg1 polymerases contain an additional region of conservation ...
 412-517 2.36e-47

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: 160.38  E-value: 2.36e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479418  412 ILLDYLAWRQVDCHINNQYNTCFWMLV-KSGKSKIQAQDYLKGTQTREKNELLSQQFGIEYNSLPVIFRMGSSVFRLKTQ 490
Cdd:pfam14413   2 NLRDYLSWRQVDCHINNLYNTTFWALVqKGGLTPTEAEERLKGTVSADKNEILFSEFGINYNNEPEIFRKGSVLVREEVE 81

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 238479418  491 EGVTEEnGEVSGKQVE--------AEVGVDYSNII 517
Cdd:pfam14413  82 ETVTKP-TELSKTQKEkeekkrkkAKIVVLHCDII 115
Thg1 COG4021
tRNA(His) 5'-end guanylyltransferase [Translation, ribosomal structure and biogenesis]; tRNA ...
 290-499 4.82e-34

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: 128.83  E-value: 4.82e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479418 290 RLLPLTWVVVRIDGCHFHRFSEVHEFEKPNDEQALKLMNSCAVAVLEE--FQdIAFAYGVSDEFSFVLKNksELYKRQSS 367
Cdd:COG4021   11 RVLPGLPVVVRLDGRGFTRLTKELGFEKPFDERFRDAMVETAEHLMKEsgFS-PVYAYTFSDEISLLFDE--LPFDRRVE 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479418 368 KIISAVVSFFTSTYMMrwgdffphkKLKYPPSFDGRAVCYPTSDIlLDYLAWRQVDCHIN--NQYntCFWMLVKSGKSKI 445
Cdd:COG4021   88 KLDSVLAGEASAAFTL---------ALGEPVAFDCRIIPLPNELV-VDYFRWRQEEAWRNalNAY--CYWTLRKEGMSPR 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 238479418 446 QAQDYLKGTQTREKNELLSqQFGIEYNSLPVIFRMGSSVFRLKTQ-EGVTEENGE 499
Cdd:COG4021  156 EAAARLKGMKVAEKHELLF-QRGINFNDLPAWQRRGIGVYWEEYEkEGYNPVTGE 209
Thg1C pfam14413
Thg1 C terminal domain; Thg1 polymerases contain an additional region of conservation ...
 138-247 8.87e-34

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: 123.79  E-value: 8.87e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479418  138 EVLQAYLAWRQHDCHISNQYDTCLWMLV-KSGKTLSETQEILKDTQKQQRNELLFQQFGINYKMLPVLFRQGSCLFKTKK 216
Cdd:pfam14413   1 KNLRDYLSWRQVDCHINNLYNTTFWALVqKGGLTPTEAEERLKGTVSADKNEILFSEFGINYNNEPEIFRKGSVLVREEV 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 238479418  217 SKSFQLLEETVKHDENGKPVKRLRRRETLVH 247
Cdd:pfam14413  81 EETVTKPTELSKTQKEKEEKKRKKAKIVVLH 111
 
Name Accession Description Interval E-value
Thg1 pfam04446
tRNAHis guanylyltransferase; The Thg1 protein from Saccharomyces cerevisiae is responsible for ...
 280-408 4.15e-74

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: 230.84  E-value: 4.15e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479418  280 DYVKSFQFESRLLPLTWVVVRIDGCHFHRFSEVHEFEKPNDEQALKLMNSCAVAVLEEFQDIAFAYGVSDEFSFVLKNKS 359
Cdd:pfam04446   2 EYVKSFEQDDKLLPNTWIVVRIDGRGFHKFSKKHGFEKPNDERALDLMNEAAKDVMEEFPDIVLAYGQSDEYSFVFRKST 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 238479418  360 ELYKRQSSKIISAVVSFFTSTYMMRWGDFFPHKKLKYPPSFDGRAVCYP 408
Cdd:pfam04446  82 TLFNRRVSKLVSLVASLFSSSYVFLWSKFFPDKPLLYPPSFDGRAVLYP 130
Thg1 pfam04446
tRNAHis guanylyltransferase; The Thg1 protein from Saccharomyces cerevisiae is responsible for ...
 6-132 5.10e-63

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: 201.95  E-value: 5.10e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479418    6 YEYVKSFEVEDEVMFPNLIIIRIDGRDFSRFSQVHKFEKPNDETSLNLMNSCASSVLVEYPDIVFAYGYSDEYSFVFKKA 85
Cdd:pfam04446   1 YEYVKSFEQDDKLLPNTWIVVRIDGRGFHKFSKKHGFEKPNDERALDLMNEAAKDVMEEFPDIVLAYGQSDEYSFVFRKS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 238479418   86 SRFYQRRASKILSLVASFFAAVYVTKWKEFFPHTKLEYAPSFASKVV 132
Cdd:pfam04446  81 TTLFNRRVSKLVSLVASLFSSSYVFLWSKFFPDKPLLYPPSFDGRAV 127
Thg1C pfam14413
Thg1 C terminal domain; Thg1 polymerases contain an additional region of conservation ...
 412-517 2.36e-47

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: 160.38  E-value: 2.36e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479418  412 ILLDYLAWRQVDCHINNQYNTCFWMLV-KSGKSKIQAQDYLKGTQTREKNELLSQQFGIEYNSLPVIFRMGSSVFRLKTQ 490
Cdd:pfam14413   2 NLRDYLSWRQVDCHINNLYNTTFWALVqKGGLTPTEAEERLKGTVSADKNEILFSEFGINYNNEPEIFRKGSVLVREEVE 81

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 238479418  491 EGVTEEnGEVSGKQVE--------AEVGVDYSNII 517
Cdd:pfam14413  82 ETVTKP-TELSKTQKEkeekkrkkAKIVVLHCDII 115
Thg1 COG4021
tRNA(His) 5'-end guanylyltransferase [Translation, ribosomal structure and biogenesis]; tRNA ...
 290-499 4.82e-34

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: 128.83  E-value: 4.82e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479418 290 RLLPLTWVVVRIDGCHFHRFSEVHEFEKPNDEQALKLMNSCAVAVLEE--FQdIAFAYGVSDEFSFVLKNksELYKRQSS 367
Cdd:COG4021   11 RVLPGLPVVVRLDGRGFTRLTKELGFEKPFDERFRDAMVETAEHLMKEsgFS-PVYAYTFSDEISLLFDE--LPFDRRVE 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479418 368 KIISAVVSFFTSTYMMrwgdffphkKLKYPPSFDGRAVCYPTSDIlLDYLAWRQVDCHIN--NQYntCFWMLVKSGKSKI 445
Cdd:COG4021   88 KLDSVLAGEASAAFTL---------ALGEPVAFDCRIIPLPNELV-VDYFRWRQEEAWRNalNAY--CYWTLRKEGMSPR 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 238479418 446 QAQDYLKGTQTREKNELLSqQFGIEYNSLPVIFRMGSSVFRLKTQ-EGVTEENGE 499
Cdd:COG4021  156 EAAARLKGMKVAEKHELLF-QRGINFNDLPAWQRRGIGVYWEEYEkEGYNPVTGE 209
Thg1C pfam14413
Thg1 C terminal domain; Thg1 polymerases contain an additional region of conservation ...
 138-247 8.87e-34

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: 123.79  E-value: 8.87e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479418  138 EVLQAYLAWRQHDCHISNQYDTCLWMLV-KSGKTLSETQEILKDTQKQQRNELLFQQFGINYKMLPVLFRQGSCLFKTKK 216
Cdd:pfam14413   1 KNLRDYLSWRQVDCHINNLYNTTFWALVqKGGLTPTEAEERLKGTVSADKNEILFSEFGINYNNEPEIFRKGSVLVREEV 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 238479418  217 SKSFQLLEETVKHDENGKPVKRLRRRETLVH 247
Cdd:pfam14413  81 EETVTKPTELSKTQKEKEEKKRKKAKIVVLH 111
Thg1 COG4021
tRNA(His) 5'-end guanylyltransferase [Translation, ribosomal structure and biogenesis]; tRNA ...
 24-242 6.51e-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: 117.27  E-value: 6.51e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479418  24 IIIRIDGRDFSRFSQVHKFEKPNDETSLNLMNSCASSVLVEYP-DIVFAYGYSDEYSFVFKKASrfYQRRASKILSLVAS 102
Cdd:COG4021   18 VVVRLDGRGFTRLTKELGFEKPFDERFRDAMVETAEHLMKESGfSPVYAYTFSDEISLLFDELP--FDRRVEKLDSVLAG 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479418 103 FFAAVyvtkwkefFPHtKLEYAPSFASKVVSCASVEVLQaYLAWRQHD---CHIsNQYdtCLWMLVKSGKTLSETQEILK 179
Cdd:COG4021   96 EASAA--------FTL-ALGEPVAFDCRIIPLPNELVVD-YFRWRQEEawrNAL-NAY--CYWTLRKEGMSPREAAARLK 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 238479418 180 DTQKQQRNELLFqQFGINYKMLPVLFRQGSCLFKtkksksfqllEETVKHDEN---GKPVKRLRRR 242
Cdd:COG4021  163 GMKVAEKHELLF-QRGINFNDLPAWQRRGIGVYW----------EEYEKEGYNpvtGEKVLTTRRR 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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