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Conserved domains on  [gi|186504734|ref|NP_180791|]
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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

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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 ...
 273-401 2.67e-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: 231.23  E-value: 2.67e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186504734  273 DYVKSFQFESRLLPLTWVVVRIDGCHFHRFSEVHEFEKPNDEQALKLMNSCAVAVLEEFQDIAFAYGVSDEFSFVLKNKS 352
Cdd:pfam04446   2 EYVKSFEQDDKLLPNTWIVVRIDGRGFHKFSKKHGFEKPNDERALDLMNEAAKDVMEEFPDIVLAYGQSDEYSFVFRKST 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 186504734  353 ELYKRQSSKIISAVVSFFTSTYMMRWGDFFPHKKLKYPPSFDGRAVCYP 401
Cdd:pfam04446  82 TLFNRRVSKLVSLVASLFSSSYVFLWSKFFPDKPLLYPPSFDGRAVLYP 130
Thg1 pfam04446
tRNAHis guanylyltransferase; The Thg1 protein from Saccharomyces cerevisiae is responsible for ...
 6-132 3.45e-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: 202.34  E-value: 3.45e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186504734    6 YEYVKSFEVEDEVMFPNLIIIRIDGRDFSRFSQVHKFEKPNDETSLNLMNSCASSVLVEYPDIVFAYGYSDEYSFVFKKA 85
Cdd:pfam04446   1 YEYVKSFEQDDKLLPNTWIVVRIDGRGFHKFSKKHGFEKPNDERALDLMNEAAKDVMEEFPDIVLAYGQSDEYSFVFRKS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 186504734   86 SRFYQRRASKILSLVASFFAAVYVTKWKEFFPHTKLEYAPSFASKVV 132
Cdd:pfam04446  81 TTLFNRRVSKLVSLVASLFSSSYVFLWSKFFPDKPLLYPPSFDGRAV 127
Thg1C pfam14413
Thg1 C terminal domain; Thg1 polymerases contain an additional region of conservation ...
 405-510 1.85e-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: 1.85e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186504734  405 ILLDYLAWRQVDCHINNQYNTCFWMLV-KSGKSKIQAQDYLKGTQTREKNELLSQQFGIEYNSLPVIFRMGSSVFRLKTQ 483
Cdd:pfam14413   2 NLRDYLSWRQVDCHINNLYNTTFWALVqKGGLTPTEAEERLKGTVSADKNEILFSEFGINYNNEPEIFRKGSVLVREEVE 81

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 186504734  484 EGVTEEnGEVSGKQVE--------AEVGVDYSNII 510
Cdd:pfam14413  82 ETVTKP-TELSKTQKEkeekkrkkAKIVVLHCDII 115
Thg1C super family cl16863
Thg1 C terminal domain; Thg1 polymerases contain an additional region of conservation ...
 138-240 2.00e-33

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: 123.02  E-value: 2.00e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186504734  138 EVLQAYLAWRQHDCHISNQYDTCLWMLV-KSGKTLSETQEILKDTQKQQRNELLFQQFGINYKMLPVLFRQGSCLFKTKL 216
Cdd:pfam14413   1 KNLRDYLSWRQVDCHINNLYNTTFWALVqKGGLTPTEAEERLKGTVSADKNEILFSEFGINYNNEPEIFRKGSVLVREEV 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 186504734  217 EETV-------KHDENGKPVKRLRRRETLVH 240
Cdd:pfam14413  81 EETVtkptelsKTQKEKEEKKRKKAKIVVLH 111
 
Name Accession Description Interval E-value
Thg1 pfam04446
tRNAHis guanylyltransferase; The Thg1 protein from Saccharomyces cerevisiae is responsible for ...
 273-401 2.67e-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: 231.23  E-value: 2.67e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186504734  273 DYVKSFQFESRLLPLTWVVVRIDGCHFHRFSEVHEFEKPNDEQALKLMNSCAVAVLEEFQDIAFAYGVSDEFSFVLKNKS 352
Cdd:pfam04446   2 EYVKSFEQDDKLLPNTWIVVRIDGRGFHKFSKKHGFEKPNDERALDLMNEAAKDVMEEFPDIVLAYGQSDEYSFVFRKST 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 186504734  353 ELYKRQSSKIISAVVSFFTSTYMMRWGDFFPHKKLKYPPSFDGRAVCYP 401
Cdd:pfam04446  82 TLFNRRVSKLVSLVASLFSSSYVFLWSKFFPDKPLLYPPSFDGRAVLYP 130
Thg1 pfam04446
tRNAHis guanylyltransferase; The Thg1 protein from Saccharomyces cerevisiae is responsible for ...
 6-132 3.45e-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: 202.34  E-value: 3.45e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186504734    6 YEYVKSFEVEDEVMFPNLIIIRIDGRDFSRFSQVHKFEKPNDETSLNLMNSCASSVLVEYPDIVFAYGYSDEYSFVFKKA 85
Cdd:pfam04446   1 YEYVKSFEQDDKLLPNTWIVVRIDGRGFHKFSKKHGFEKPNDERALDLMNEAAKDVMEEFPDIVLAYGQSDEYSFVFRKS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 186504734   86 SRFYQRRASKILSLVASFFAAVYVTKWKEFFPHTKLEYAPSFASKVV 132
Cdd:pfam04446  81 TTLFNRRVSKLVSLVASLFSSSYVFLWSKFFPDKPLLYPPSFDGRAV 127
Thg1C pfam14413
Thg1 C terminal domain; Thg1 polymerases contain an additional region of conservation ...
 405-510 1.85e-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: 1.85e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186504734  405 ILLDYLAWRQVDCHINNQYNTCFWMLV-KSGKSKIQAQDYLKGTQTREKNELLSQQFGIEYNSLPVIFRMGSSVFRLKTQ 483
Cdd:pfam14413   2 NLRDYLSWRQVDCHINNLYNTTFWALVqKGGLTPTEAEERLKGTVSADKNEILFSEFGINYNNEPEIFRKGSVLVREEVE 81

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 186504734  484 EGVTEEnGEVSGKQVE--------AEVGVDYSNII 510
Cdd:pfam14413  82 ETVTKP-TELSKTQKEkeekkrkkAKIVVLHCDII 115
Thg1 COG4021
tRNA(His) 5'-end guanylyltransferase [Translation, ribosomal structure and biogenesis]; tRNA ...
 283-492 4.33e-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: 4.33e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186504734 283 RLLPLTWVVVRIDGCHFHRFSEVHEFEKPNDEQALKLMNSCAVAVLEE--FQdIAFAYGVSDEFSFVLKNksELYKRQSS 360
Cdd:COG4021   11 RVLPGLPVVVRLDGRGFTRLTKELGFEKPFDERFRDAMVETAEHLMKEsgFS-PVYAYTFSDEISLLFDE--LPFDRRVE 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186504734 361 KIISAVVSFFTSTYMMrwgdffphkKLKYPPSFDGRAVCYPTSDIlLDYLAWRQVDCHIN--NQYntCFWMLVKSGKSKI 438
Cdd:COG4021   88 KLDSVLAGEASAAFTL---------ALGEPVAFDCRIIPLPNELV-VDYFRWRQEEAWRNalNAY--CYWTLRKEGMSPR 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 186504734 439 QAQDYLKGTQTREKNELLSqQFGIEYNSLPVIFRMGSSVFRLKTQ-EGVTEENGE 492
Cdd:COG4021  156 EAAARLKGMKVAEKHELLF-QRGINFNDLPAWQRRGIGVYWEEYEkEGYNPVTGE 209
Thg1C pfam14413
Thg1 C terminal domain; Thg1 polymerases contain an additional region of conservation ...
 138-240 2.00e-33

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: 123.02  E-value: 2.00e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186504734  138 EVLQAYLAWRQHDCHISNQYDTCLWMLV-KSGKTLSETQEILKDTQKQQRNELLFQQFGINYKMLPVLFRQGSCLFKTKL 216
Cdd:pfam14413   1 KNLRDYLSWRQVDCHINNLYNTTFWALVqKGGLTPTEAEERLKGTVSADKNEILFSEFGINYNNEPEIFRKGSVLVREEV 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 186504734  217 EETV-------KHDENGKPVKRLRRRETLVH 240
Cdd:pfam14413  81 EETVtkptelsKTQKEKEEKKRKKAKIVVLH 111
Thg1 COG4021
tRNA(His) 5'-end guanylyltransferase [Translation, ribosomal structure and biogenesis]; tRNA ...
 24-235 1.86e-31

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: 121.51  E-value: 1.86e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186504734  24 IIIRIDGRDFSRFSQVHKFEKPNDETSLNLMNSCASSVLVEYP-DIVFAYGYSDEYSFVFKKASrfYQRRASKILSLVAS 102
Cdd:COG4021   18 VVVRLDGRGFTRLTKELGFEKPFDERFRDAMVETAEHLMKESGfSPVYAYTFSDEISLLFDELP--FDRRVEKLDSVLAG 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186504734 103 FFAAVyvtkwkefFPHtKLEYAPSFASKVVSCASVEVLQaYLAWRQHD---CHIsNQYdtCLWMLVKSGKTLSETQEILK 179
Cdd:COG4021   96 EASAA--------FTL-ALGEPVAFDCRIIPLPNELVVD-YFRWRQEEawrNAL-NAY--CYWTLRKEGMSPREAAARLK 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 186504734 180 DTQKQQRNELLFqQFGINYKMLPVLFRQGSCLFKTKLEETVKHDENGKPVKRLRRR 235
Cdd:COG4021  163 GMKVAEKHELLF-QRGINFNDLPAWQRRGIGVYWEEYEKEGYNPVTGEKVLTTRRR 217
 
Name Accession Description Interval E-value
Thg1 pfam04446
tRNAHis guanylyltransferase; The Thg1 protein from Saccharomyces cerevisiae is responsible for ...
 273-401 2.67e-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: 231.23  E-value: 2.67e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186504734  273 DYVKSFQFESRLLPLTWVVVRIDGCHFHRFSEVHEFEKPNDEQALKLMNSCAVAVLEEFQDIAFAYGVSDEFSFVLKNKS 352
Cdd:pfam04446   2 EYVKSFEQDDKLLPNTWIVVRIDGRGFHKFSKKHGFEKPNDERALDLMNEAAKDVMEEFPDIVLAYGQSDEYSFVFRKST 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 186504734  353 ELYKRQSSKIISAVVSFFTSTYMMRWGDFFPHKKLKYPPSFDGRAVCYP 401
Cdd:pfam04446  82 TLFNRRVSKLVSLVASLFSSSYVFLWSKFFPDKPLLYPPSFDGRAVLYP 130
Thg1 pfam04446
tRNAHis guanylyltransferase; The Thg1 protein from Saccharomyces cerevisiae is responsible for ...
 6-132 3.45e-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: 202.34  E-value: 3.45e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186504734    6 YEYVKSFEVEDEVMFPNLIIIRIDGRDFSRFSQVHKFEKPNDETSLNLMNSCASSVLVEYPDIVFAYGYSDEYSFVFKKA 85
Cdd:pfam04446   1 YEYVKSFEQDDKLLPNTWIVVRIDGRGFHKFSKKHGFEKPNDERALDLMNEAAKDVMEEFPDIVLAYGQSDEYSFVFRKS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 186504734   86 SRFYQRRASKILSLVASFFAAVYVTKWKEFFPHTKLEYAPSFASKVV 132
Cdd:pfam04446  81 TTLFNRRVSKLVSLVASLFSSSYVFLWSKFFPDKPLLYPPSFDGRAV 127
Thg1C pfam14413
Thg1 C terminal domain; Thg1 polymerases contain an additional region of conservation ...
 405-510 1.85e-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: 1.85e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186504734  405 ILLDYLAWRQVDCHINNQYNTCFWMLV-KSGKSKIQAQDYLKGTQTREKNELLSQQFGIEYNSLPVIFRMGSSVFRLKTQ 483
Cdd:pfam14413   2 NLRDYLSWRQVDCHINNLYNTTFWALVqKGGLTPTEAEERLKGTVSADKNEILFSEFGINYNNEPEIFRKGSVLVREEVE 81

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 186504734  484 EGVTEEnGEVSGKQVE--------AEVGVDYSNII 510
Cdd:pfam14413  82 ETVTKP-TELSKTQKEkeekkrkkAKIVVLHCDII 115
Thg1 COG4021
tRNA(His) 5'-end guanylyltransferase [Translation, ribosomal structure and biogenesis]; tRNA ...
 283-492 4.33e-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: 4.33e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186504734 283 RLLPLTWVVVRIDGCHFHRFSEVHEFEKPNDEQALKLMNSCAVAVLEE--FQdIAFAYGVSDEFSFVLKNksELYKRQSS 360
Cdd:COG4021   11 RVLPGLPVVVRLDGRGFTRLTKELGFEKPFDERFRDAMVETAEHLMKEsgFS-PVYAYTFSDEISLLFDE--LPFDRRVE 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186504734 361 KIISAVVSFFTSTYMMrwgdffphkKLKYPPSFDGRAVCYPTSDIlLDYLAWRQVDCHIN--NQYntCFWMLVKSGKSKI 438
Cdd:COG4021   88 KLDSVLAGEASAAFTL---------ALGEPVAFDCRIIPLPNELV-VDYFRWRQEEAWRNalNAY--CYWTLRKEGMSPR 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 186504734 439 QAQDYLKGTQTREKNELLSqQFGIEYNSLPVIFRMGSSVFRLKTQ-EGVTEENGE 492
Cdd:COG4021  156 EAAARLKGMKVAEKHELLF-QRGINFNDLPAWQRRGIGVYWEEYEkEGYNPVTGE 209
Thg1C pfam14413
Thg1 C terminal domain; Thg1 polymerases contain an additional region of conservation ...
 138-240 2.00e-33

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: 123.02  E-value: 2.00e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186504734  138 EVLQAYLAWRQHDCHISNQYDTCLWMLV-KSGKTLSETQEILKDTQKQQRNELLFQQFGINYKMLPVLFRQGSCLFKTKL 216
Cdd:pfam14413   1 KNLRDYLSWRQVDCHINNLYNTTFWALVqKGGLTPTEAEERLKGTVSADKNEILFSEFGINYNNEPEIFRKGSVLVREEV 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 186504734  217 EETV-------KHDENGKPVKRLRRRETLVH 240
Cdd:pfam14413  81 EETVtkptelsKTQKEKEEKKRKKAKIVVLH 111
Thg1 COG4021
tRNA(His) 5'-end guanylyltransferase [Translation, ribosomal structure and biogenesis]; tRNA ...
 24-235 1.86e-31

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: 121.51  E-value: 1.86e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186504734  24 IIIRIDGRDFSRFSQVHKFEKPNDETSLNLMNSCASSVLVEYP-DIVFAYGYSDEYSFVFKKASrfYQRRASKILSLVAS 102
Cdd:COG4021   18 VVVRLDGRGFTRLTKELGFEKPFDERFRDAMVETAEHLMKESGfSPVYAYTFSDEISLLFDELP--FDRRVEKLDSVLAG 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186504734 103 FFAAVyvtkwkefFPHtKLEYAPSFASKVVSCASVEVLQaYLAWRQHD---CHIsNQYdtCLWMLVKSGKTLSETQEILK 179
Cdd:COG4021   96 EASAA--------FTL-ALGEPVAFDCRIIPLPNELVVD-YFRWRQEEawrNAL-NAY--CYWTLRKEGMSPREAAARLK 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 186504734 180 DTQKQQRNELLFqQFGINYKMLPVLFRQGSCLFKTKLEETVKHDENGKPVKRLRRR 235
Cdd:COG4021  163 GMKVAEKHELLF-QRGINFNDLPAWQRRGIGVYWEEYEKEGYNPVTGEKVLTTRRR 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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