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Conserved domains on  [gi|15238631|ref|NP_197866|]
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tRNA (guanine-N-7) methyltransferase [Arabidopsis thaliana]

Protein Classification

tRNA (guanine-N(7)-)-methyltransferase( domain architecture ID 10493262)

tRNA (guanine-N(7)-)-methyltransferase which catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Methyltransf_4 pfam02390
Putative methyltransferase; This is a family of putative methyltransferases. The aligned ...
63-242 3.52e-64

Putative methyltransferase; This is a family of putative methyltransferases. The aligned region contains the GXGXG S-AdoMet binding site suggesting a putative methyltransferase activity.


:

Pssm-ID: 367068  Cd Length: 173  Bit Score: 197.90  E-value: 3.52e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238631    63 KKVEFADIGCGFGGLLISLATLFPDTLMIGMELRDKVTEYVKERILALRrtssegqYENISVVRTNSMKYIPNYFEKGQL 142
Cdd:pfam02390   1 DAPVFLEIGCGMGGFLVAMAKANPDKNFIGIEIRVPGVAKALKKIDALG-------LQNLRILCGNALDVLPNYFPPGSL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238631   143 SKMFFLFPDPHFKEKNHRRRVISTHLLDEYAYVLRAGGIIYTITDVEELGEWMKSCLEKHPMFESLTQEELVSDPVVELL 222
Cdd:pfam02390  74 QKIFINFPDPWPKKRHHKRRLLQPEFLKEYARVLKPGGVLHLATDVEEYAEEMLKHLAEHPLFERLDLENDLAPGPLSPL 153
                         170       180
                  ....*....|....*....|
gi 15238631   223 CSATEEGQKVARNGGQTFRA 242
Cdd:pfam02390 154 RPATEYEQKVQRLGGPIYRL 173
 
Name Accession Description Interval E-value
Methyltransf_4 pfam02390
Putative methyltransferase; This is a family of putative methyltransferases. The aligned ...
63-242 3.52e-64

Putative methyltransferase; This is a family of putative methyltransferases. The aligned region contains the GXGXG S-AdoMet binding site suggesting a putative methyltransferase activity.


Pssm-ID: 367068  Cd Length: 173  Bit Score: 197.90  E-value: 3.52e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238631    63 KKVEFADIGCGFGGLLISLATLFPDTLMIGMELRDKVTEYVKERILALRrtssegqYENISVVRTNSMKYIPNYFEKGQL 142
Cdd:pfam02390   1 DAPVFLEIGCGMGGFLVAMAKANPDKNFIGIEIRVPGVAKALKKIDALG-------LQNLRILCGNALDVLPNYFPPGSL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238631   143 SKMFFLFPDPHFKEKNHRRRVISTHLLDEYAYVLRAGGIIYTITDVEELGEWMKSCLEKHPMFESLTQEELVSDPVVELL 222
Cdd:pfam02390  74 QKIFINFPDPWPKKRHHKRRLLQPEFLKEYARVLKPGGVLHLATDVEEYAEEMLKHLAEHPLFERLDLENDLAPGPLSPL 153
                         170       180
                  ....*....|....*....|
gi 15238631   223 CSATEEGQKVARNGGQTFRA 242
Cdd:pfam02390 154 RPATEYEQKVQRLGGPIYRL 173
TIGR00091 TIGR00091
tRNA (guanine-N(7)-)-methyltransferase; This predicted S-adenosylmethionine-dependent ...
46-247 3.64e-47

tRNA (guanine-N(7)-)-methyltransferase; This predicted S-adenosylmethionine-dependent methyltransferase is found in a single copy in most Bacteria. It is also found, with a short amino-terminal extension in eukaryotes. Its function is unknown. In E. coli, this protein flanks the DNA repair protein MutY, also called micA. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 161703  Cd Length: 194  Bit Score: 155.21  E-value: 3.64e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238631    46 DYSLHFPKFVEADNKfiKKVEFADIGCGFGGLLISLATLFPDTLMIGMELRDKVteyvkerILALRRTSSEGQYENISVV 125
Cdd:TIGR00091   1 DYSLDKPDFATVFGN--KAPLHLEIGCGKGRFLIDMAKQNPDKNFLGIEIHTPI-------VLAANNKANKLGLKNLHVL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238631   126 RTNSMKYIPNYFEKGQLSKMFFLFPDPHFKEKNHRRRVISTHLLDEYAYVLRAGGIIYTITDVEELGEWMKSCLEKHPMF 205
Cdd:TIGR00091  72 CGDANELLDKFFPDGSLSKVFLNFPDPWPKKRHNKRRITQPHFLKEYANVLKKGGVIHFKTDNEPLFEDMLKVLSENDLF 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 15238631   206 ESLTQEELVSDPVVELLCSATEEGQKVARNGGQTFRAVFRRI 247
Cdd:TIGR00091 152 ENTSKSTDLNNSPLSRPRNMTEYEQRFERLGHPVFDLCFERL 193
TrmB COG0220
tRNA G46 N7-methylase TrmB [Translation, ribosomal structure and biogenesis]; tRNA G46 ...
69-208 1.35e-27

tRNA G46 N7-methylase TrmB [Translation, ribosomal structure and biogenesis]; tRNA G46 N7-methylase TrmB is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 439990  Cd Length: 204  Bit Score: 104.83  E-value: 1.35e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238631  69 DIGCGFGGLLISLATLFPDTLMIGMELRdkvteyvKERILALRRTSSEGQYENISVVRTNsMKYIPNYFEKGQLSKMFFL 148
Cdd:COG0220  38 EIGFGKGEFLVELAAANPDINFIGIEVH-------EPGVAKALKKAEEEGLTNVRLLRGD-AVELLELFPDGSLDRIYLN 109
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238631 149 FPDPHFKEKNHRRRVISTHLLDEYAYVLRAGGIIYTITDVEELGEWMKSCLEKHPMFESL 208
Cdd:COG0220 110 FPDPWPKKRHHKRRLVQPEFLALLARVLKPGGELHLATDWEDYAEEMLEVLSAHPGFENL 169
trmB PRK00121
tRNA (guanine-N(7)-)-methyltransferase; Reviewed
69-217 2.63e-27

tRNA (guanine-N(7)-)-methyltransferase; Reviewed


Pssm-ID: 234649  Cd Length: 202  Bit Score: 104.09  E-value: 2.63e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238631   69 DIGCGFGGLLISLATLFPDTLMIGMELRdkvteyvKERILALRRTSSEGQYENISVVRTNSMKYIPNYFEKGQLSKMFFL 148
Cdd:PRK00121  46 EIGFGKGEFLVEMAKANPDINFIGIEVH-------EPGVGKALKKIEEEGLTNLRLLCGDAVEVLLDMFPDGSLDRIYLN 118
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15238631  149 FPDPHFKEKNHRRRVISTHLLDEYAYVLRAGGIIYTITDVEELGEWMKSCLEKHPMFESLTQEELVSDP 217
Cdd:PRK00121 119 FPDPWPKKRHHKRRLVQPEFLALYARKLKPGGEIHFATDWEGYAEYMLEVLSAEGGFLVSEAGDYVPRP 187
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
67-185 2.19e-05

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 42.42  E-value: 2.19e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238631  67 FADIGCGFGGLLISLAtLFPDTLMIGMELRDKVTEYVKERILALRRtssegqyENISVVRTNSMKyiPNYFEKGQLSKMF 146
Cdd:cd02440   2 VLDLGCGTGALALALA-SGPGARVTGVDISPVALELARKAAAALLA-------DNVEVLKGDAEE--LPPEADESFDVII 71
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15238631 147 FLFPDPHFKEkNHRRrvisthLLDEYAYVLRAGGIIYTI 185
Cdd:cd02440  72 SDPPLHHLVE-DLAR------FLEEARRLLKPGGVLVLT 103
 
Name Accession Description Interval E-value
Methyltransf_4 pfam02390
Putative methyltransferase; This is a family of putative methyltransferases. The aligned ...
63-242 3.52e-64

Putative methyltransferase; This is a family of putative methyltransferases. The aligned region contains the GXGXG S-AdoMet binding site suggesting a putative methyltransferase activity.


Pssm-ID: 367068  Cd Length: 173  Bit Score: 197.90  E-value: 3.52e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238631    63 KKVEFADIGCGFGGLLISLATLFPDTLMIGMELRDKVTEYVKERILALRrtssegqYENISVVRTNSMKYIPNYFEKGQL 142
Cdd:pfam02390   1 DAPVFLEIGCGMGGFLVAMAKANPDKNFIGIEIRVPGVAKALKKIDALG-------LQNLRILCGNALDVLPNYFPPGSL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238631   143 SKMFFLFPDPHFKEKNHRRRVISTHLLDEYAYVLRAGGIIYTITDVEELGEWMKSCLEKHPMFESLTQEELVSDPVVELL 222
Cdd:pfam02390  74 QKIFINFPDPWPKKRHHKRRLLQPEFLKEYARVLKPGGVLHLATDVEEYAEEMLKHLAEHPLFERLDLENDLAPGPLSPL 153
                         170       180
                  ....*....|....*....|
gi 15238631   223 CSATEEGQKVARNGGQTFRA 242
Cdd:pfam02390 154 RPATEYEQKVQRLGGPIYRL 173
TIGR00091 TIGR00091
tRNA (guanine-N(7)-)-methyltransferase; This predicted S-adenosylmethionine-dependent ...
46-247 3.64e-47

tRNA (guanine-N(7)-)-methyltransferase; This predicted S-adenosylmethionine-dependent methyltransferase is found in a single copy in most Bacteria. It is also found, with a short amino-terminal extension in eukaryotes. Its function is unknown. In E. coli, this protein flanks the DNA repair protein MutY, also called micA. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 161703  Cd Length: 194  Bit Score: 155.21  E-value: 3.64e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238631    46 DYSLHFPKFVEADNKfiKKVEFADIGCGFGGLLISLATLFPDTLMIGMELRDKVteyvkerILALRRTSSEGQYENISVV 125
Cdd:TIGR00091   1 DYSLDKPDFATVFGN--KAPLHLEIGCGKGRFLIDMAKQNPDKNFLGIEIHTPI-------VLAANNKANKLGLKNLHVL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238631   126 RTNSMKYIPNYFEKGQLSKMFFLFPDPHFKEKNHRRRVISTHLLDEYAYVLRAGGIIYTITDVEELGEWMKSCLEKHPMF 205
Cdd:TIGR00091  72 CGDANELLDKFFPDGSLSKVFLNFPDPWPKKRHNKRRITQPHFLKEYANVLKKGGVIHFKTDNEPLFEDMLKVLSENDLF 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 15238631   206 ESLTQEELVSDPVVELLCSATEEGQKVARNGGQTFRAVFRRI 247
Cdd:TIGR00091 152 ENTSKSTDLNNSPLSRPRNMTEYEQRFERLGHPVFDLCFERL 193
TrmB COG0220
tRNA G46 N7-methylase TrmB [Translation, ribosomal structure and biogenesis]; tRNA G46 ...
69-208 1.35e-27

tRNA G46 N7-methylase TrmB [Translation, ribosomal structure and biogenesis]; tRNA G46 N7-methylase TrmB is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 439990  Cd Length: 204  Bit Score: 104.83  E-value: 1.35e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238631  69 DIGCGFGGLLISLATLFPDTLMIGMELRdkvteyvKERILALRRTSSEGQYENISVVRTNsMKYIPNYFEKGQLSKMFFL 148
Cdd:COG0220  38 EIGFGKGEFLVELAAANPDINFIGIEVH-------EPGVAKALKKAEEEGLTNVRLLRGD-AVELLELFPDGSLDRIYLN 109
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238631 149 FPDPHFKEKNHRRRVISTHLLDEYAYVLRAGGIIYTITDVEELGEWMKSCLEKHPMFESL 208
Cdd:COG0220 110 FPDPWPKKRHHKRRLVQPEFLALLARVLKPGGELHLATDWEDYAEEMLEVLSAHPGFENL 169
trmB PRK00121
tRNA (guanine-N(7)-)-methyltransferase; Reviewed
69-217 2.63e-27

tRNA (guanine-N(7)-)-methyltransferase; Reviewed


Pssm-ID: 234649  Cd Length: 202  Bit Score: 104.09  E-value: 2.63e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238631   69 DIGCGFGGLLISLATLFPDTLMIGMELRdkvteyvKERILALRRTSSEGQYENISVVRTNSMKYIPNYFEKGQLSKMFFL 148
Cdd:PRK00121  46 EIGFGKGEFLVEMAKANPDINFIGIEVH-------EPGVGKALKKIEEEGLTNLRLLCGDAVEVLLDMFPDGSLDRIYLN 118
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15238631  149 FPDPHFKEKNHRRRVISTHLLDEYAYVLRAGGIIYTITDVEELGEWMKSCLEKHPMFESLTQEELVSDP 217
Cdd:PRK00121 119 FPDPWPKKRHHKRRLVQPEFLALYARKLKPGGEIHFATDWEGYAEYMLEVLSAEGGFLVSEAGDYVPRP 187
PRK01544 PRK01544
bifunctional N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase/tRNA (m7G46) ...
51-206 3.32e-07

bifunctional N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase/tRNA (m7G46) methyltransferase; Reviewed


Pssm-ID: 234958 [Multi-domain]  Cd Length: 506  Bit Score: 50.63  E-value: 3.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238631   51 FPKFVEADNKFI--KKVEFADIGCGFGGLLISLATLFPDTLMIGMELrdkvteYVKERILALRRTSSEgqyeNIS--VVR 126
Cdd:PRK01544 333 LPKYLFSKEKLVneKRKVFLEIGFGMGEHFINQAKMNPDALFIGVEV------YLNGVANVLKLAGEQ----NITnfLLF 402
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238631  127 TNSMKYIPNYFEKGQLSKMFFLFPDPHFKEKNHRRRVISTHLLDEYAYVLRAGGIIYTITDVEELGEWMKSCLEKHPMFE 206
Cdd:PRK01544 403 PNNLDLILNDLPNNSLDGIYILFPDPWIKNKQKKKRIFNKERLKILQDKLKDNGNLVFASDIENYFYEAIELIQQNGNFE 482
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
67-185 2.19e-05

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 42.42  E-value: 2.19e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238631  67 FADIGCGFGGLLISLAtLFPDTLMIGMELRDKVTEYVKERILALRRtssegqyENISVVRTNSMKyiPNYFEKGQLSKMF 146
Cdd:cd02440   2 VLDLGCGTGALALALA-SGPGARVTGVDISPVALELARKAAAALLA-------DNVEVLKGDAEE--LPPEADESFDVII 71
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15238631 147 FLFPDPHFKEkNHRRrvisthLLDEYAYVLRAGGIIYTI 185
Cdd:cd02440  72 SDPPLHHLVE-DLAR------FLEEARRLLKPGGVLVLT 103
 
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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