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Conserved domains on  [gi|1034675346|ref|XP_016885354|]
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tRNA (uracil-5-)-methyltransferase homolog B isoform X3 [Homo sapiens]

Protein Classification

class I SAM-dependent RNA methyltransferase( domain architecture ID 11455144)

class I SAM-dependent RNA methyltransferase catalyzes the methylation of a specific RNA substrate using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor

EC:  2.1.1.-
Gene Ontology:  GO:0031167|GO:0046872
PubMed:  12826405|12504684

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
21-384 1.61e-59

tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure and biogenesis]; tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family is part of the Pathway/BioSystem: tRNA modification


:

Pssm-ID: 441866 [Multi-domain]  Cd Length: 377  Bit Score: 197.32  E-value: 1.61e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034675346  21 LHPIIPSPVINGYRNKSTFSVnrGPDGNPKTVGFYlgtwrdgnvvcvqsnhlknipEKHSqvaqyYEVFlrqsPLEPCLV 100
Cdd:COG2265   109 VEPIIGSPEPWGYRNRARLSV--RRTDGRLRLGFY---------------------ARGS-----HELV----DIDECPL 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034675346 101 FHEggywreltvrtnsqgHTMAIItfhpqklsqeelhvqkEIVKEFFIRGPGAACGLTSLyfqestMTRCshqqspyqll 180
Cdd:COG2265   157 LDP---------------ALNALL----------------PALRELLAELGARRGELRHL------VVRA---------- 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034675346 181 fGEPYIFEELLSLKIRISPDAFFQINTAGAEMLYRTVGELTGVNSDTILLDICCGTGVIGLSLAQHTSRVLGIELLEQAV 260
Cdd:COG2265   190 -GRDYLTERLGGLTFRISPGSFFQVNPEQAEALYAAALEWLDLTGGERVLDLYCGVGTFALPLARRAKKVIGVEIVPEAV 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034675346 261 EDARWTAAFNGITNSEFHTGQAEKILPGLLKSKE-DgqsiVAVVNPARAGLHYKVIQAIRNFRAiHTLVFVSCklhgest 339
Cdd:COG2265   269 EDARENARLNGLKNVEFVAGDLEEVLPELLWGGRpD----VVVLDPPRAGAGPEVLEALAALGP-RRIVYVSC------- 336
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1034675346 340 rnvielccppDPA------KKLLGEPFVLQQAVPVDLFPHTPHCELVLLFT 384
Cdd:COG2265   337 ----------NPAtlardlALLVEGGYRLEKVQPVDMFPHTHHVESVALLE 377
 
Name Accession Description Interval E-value
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
21-384 1.61e-59

tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure and biogenesis]; tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441866 [Multi-domain]  Cd Length: 377  Bit Score: 197.32  E-value: 1.61e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034675346  21 LHPIIPSPVINGYRNKSTFSVnrGPDGNPKTVGFYlgtwrdgnvvcvqsnhlknipEKHSqvaqyYEVFlrqsPLEPCLV 100
Cdd:COG2265   109 VEPIIGSPEPWGYRNRARLSV--RRTDGRLRLGFY---------------------ARGS-----HELV----DIDECPL 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034675346 101 FHEggywreltvrtnsqgHTMAIItfhpqklsqeelhvqkEIVKEFFIRGPGAACGLTSLyfqestMTRCshqqspyqll 180
Cdd:COG2265   157 LDP---------------ALNALL----------------PALRELLAELGARRGELRHL------VVRA---------- 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034675346 181 fGEPYIFEELLSLKIRISPDAFFQINTAGAEMLYRTVGELTGVNSDTILLDICCGTGVIGLSLAQHTSRVLGIELLEQAV 260
Cdd:COG2265   190 -GRDYLTERLGGLTFRISPGSFFQVNPEQAEALYAAALEWLDLTGGERVLDLYCGVGTFALPLARRAKKVIGVEIVPEAV 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034675346 261 EDARWTAAFNGITNSEFHTGQAEKILPGLLKSKE-DgqsiVAVVNPARAGLHYKVIQAIRNFRAiHTLVFVSCklhgest 339
Cdd:COG2265   269 EDARENARLNGLKNVEFVAGDLEEVLPELLWGGRpD----VVVLDPPRAGAGPEVLEALAALGP-RRIVYVSC------- 336
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1034675346 340 rnvielccppDPA------KKLLGEPFVLQQAVPVDLFPHTPHCELVLLFT 384
Cdd:COG2265   337 ----------NPAtlardlALLVEGGYRLEKVQPVDMFPHTHHVESVALLE 377
rumA TIGR00479
23S rRNA (uracil-5-)-methyltransferase RumA; This protein family was first proposed to be RNA ...
15-378 8.33e-31

23S rRNA (uracil-5-)-methyltransferase RumA; This protein family was first proposed to be RNA methyltransferases by homology to the TrmA family. The member from E. coli has now been shown to act as the 23S RNA methyltransferase for the conserved U1939. The gene is now designated rumA and was previously designated ygcA. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 129571 [Multi-domain]  Cd Length: 431  Bit Score: 121.85  E-value: 8.33e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034675346  15 ERLSCL-LHPIIPSPVIN----GYRNKSTFSVNRGPDGNPKtVGFY-LGTWR--DGNVVCVQSNHL-------KNIPEKH 79
Cdd:TIGR00479  90 ERIGKFvSEPIEDVPTIGddpwGYRNKARLSLGRSPSGQLQ-AGFYqKGSHDivDVKQCPVQAPALnallpkvRAILENF 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034675346  80 SQVAQYYEVflrqsplepclvfhEGGYWRELTVRTNSQGHTMAI--ITFHpqklsqEELHVQKEIVKEFFIRGP--GAAC 155
Cdd:TIGR00479 169 GASRYLEHK--------------ELGQARHGVLRIGRHTGELSSvdRTAL------ERFPHKEELDLYLQPDSPdvKSIC 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034675346 156 -----GLTSLYFQESTMTrcshqqspyqlLFGEPYIFEELLSLKIRISPDAFFQINTAGAEMLYRTVGELTGVNSDTILL 230
Cdd:TIGR00479 229 qninpEKTNVIFGEETEV-----------IAGEMPIYDKSGDLSFTFSARDFIQVNSGQNEKLVDRALEWLELQGEERVL 297
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034675346 231 DICCGTGVIGLSLAQHTSRVLGIELLEQAVEDARWTAAFNGITNSEFHTGQAEKILPgllKSKEDGQSI-VAVVNPARAG 309
Cdd:TIGR00479 298 DAYCGMGTFTLPLAKQAKSVVGVEGVPESVEKAQQNAELNGIANVTFYHGTLETVLP---KQPWAGNGFdKVLLDPPRKG 374
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034675346 310 LHYKVIQAIRNFRAIHtLVFVSCKlhgestrnvielccPPDPAKK---LLGEPFVLQQAVPVDLFPHTPHCE 378
Cdd:TIGR00479 375 CAAGVLRTIIKLKPER-IVYVSCN--------------PATLARDleaLCKAGYTIARVQPVDMFPHTGHVE 431
rumB PRK03522
23S rRNA (uracil(747)-C(5))-methyltransferase RlmC;
179-382 1.28e-18

23S rRNA (uracil(747)-C(5))-methyltransferase RlmC;


Pssm-ID: 235128 [Multi-domain]  Cd Length: 315  Bit Score: 85.69  E-value: 1.28e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034675346 179 LLFGEPYIFEELLSLKIRISPDAFFQINTAGAEMLYRT----VGELtGVNSdtiLLDICCGTGVIGLSLAQHTSRVLGIE 254
Cdd:PRK03522  127 FLTEQQALPERFNGVPLFIRPQSFFQTNPAVAAQLYATardwVREL-PPRS---MWDLFCGVGGFGLHCATPGMQLTGIE 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034675346 255 LLEQAVEDARWTAAFNGITNSEFH--------TGQAEKilPGLlkskedgqsivAVVNPARAGLHyKVIQAIRNFRAIHT 326
Cdd:PRK03522  203 ISAEAIACAKQSAAELGLTNVQFQaldstqfaTAQGEV--PDL-----------VLVNPPRRGIG-KELCDYLSQMAPRF 268
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034675346 327 LVFVSCklhgestrNVIELccppdpAKKLLGEP-FVLQQAVPVDLFPHTPHCE-LVLL 382
Cdd:PRK03522  269 ILYSSC--------NAQTM------AKDLAHLPgYRIERVQLFDMFPHTAHYEvLTLL 312
tRNA_U5-meth_tr pfam05958
tRNA (Uracil-5-)-methyltransferase; This family consists of (Uracil-5-)-methyltransferases EC: ...
178-385 3.22e-10

tRNA (Uracil-5-)-methyltransferase; This family consists of (Uracil-5-)-methyltransferases EC:2.1.1.35 from bacteria, archaea and eukaryotes. A 5-methyluridine (m(5)U) residue at position 54 is a conserved feature of bacterial and eukaryotic tRNAs. The methylation of U54 is catalyzed by the tRNA(m5U54)methyltransferase, which in Saccharomyces cerevisiae is encoded by the nonessential TRM2 gene. It is thought that tRNA modification enzymes might have a role in tRNA maturation not necessarily linked to their known catalytic activity.


Pssm-ID: 428692  Cd Length: 357  Bit Score: 60.92  E-value: 3.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034675346 178 QLLFGEPYIFEEL----LSLKIRISPDAFFQINTAGAEMLYRTVGELTGvNSDTILLDICCGTGVIGLSLAQHTSRVLGI 253
Cdd:pfam05958 151 KIVLDQDYVDETLpvagREFIYRQVENSFTQPNAAVNIKMLEWACDVTQ-GSKGDLLELYCGNGNFSLALARNFRKVLAT 229
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034675346 254 ELLEQAVEDARWTAAFNGITNSEFHTGQAEKILPGLLKSKE----------DGQSIVAVVNPARAGLHYKVIQAIRNFRA 323
Cdd:pfam05958 230 EIAKPSVAAAQYNIAANNIDNVQIIRMSAEEFTQAMNGVREfnrlkgidlkSYNCSTIFVDPPRAGLDPETLKLVQAYPR 309
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034675346 324 IhtlVFVSCklhgestrNVIELCcppdpaKKL--LGEPFVLQQAVPVDLFPHTPHCELVLLFTR 385
Cdd:pfam05958 310 I---LYISC--------NPETLC------ANLeqLSKTHRVERFALFDQFPYTHHMECGVLLEK 356
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
229-322 1.02e-04

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: 41.26  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034675346 229 LLDICCGTGVIGLSLAQHTS-RVLGIELLEQAVEDARWTAAFNGITNSEFHTGQAEKILPgllksKEDGQSIVAVVNPAR 307
Cdd:cd02440     2 VLDLGCGTGALALALASGPGaRVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPP-----EADESFDVIISDPPL 76
                          90
                  ....*....|....*
gi 1034675346 308 AGLHYKVIQAIRNFR 322
Cdd:cd02440    77 HHLVEDLARFLEEAR 91
 
Name Accession Description Interval E-value
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
21-384 1.61e-59

tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure and biogenesis]; tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441866 [Multi-domain]  Cd Length: 377  Bit Score: 197.32  E-value: 1.61e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034675346  21 LHPIIPSPVINGYRNKSTFSVnrGPDGNPKTVGFYlgtwrdgnvvcvqsnhlknipEKHSqvaqyYEVFlrqsPLEPCLV 100
Cdd:COG2265   109 VEPIIGSPEPWGYRNRARLSV--RRTDGRLRLGFY---------------------ARGS-----HELV----DIDECPL 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034675346 101 FHEggywreltvrtnsqgHTMAIItfhpqklsqeelhvqkEIVKEFFIRGPGAACGLTSLyfqestMTRCshqqspyqll 180
Cdd:COG2265   157 LDP---------------ALNALL----------------PALRELLAELGARRGELRHL------VVRA---------- 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034675346 181 fGEPYIFEELLSLKIRISPDAFFQINTAGAEMLYRTVGELTGVNSDTILLDICCGTGVIGLSLAQHTSRVLGIELLEQAV 260
Cdd:COG2265   190 -GRDYLTERLGGLTFRISPGSFFQVNPEQAEALYAAALEWLDLTGGERVLDLYCGVGTFALPLARRAKKVIGVEIVPEAV 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034675346 261 EDARWTAAFNGITNSEFHTGQAEKILPGLLKSKE-DgqsiVAVVNPARAGLHYKVIQAIRNFRAiHTLVFVSCklhgest 339
Cdd:COG2265   269 EDARENARLNGLKNVEFVAGDLEEVLPELLWGGRpD----VVVLDPPRAGAGPEVLEALAALGP-RRIVYVSC------- 336
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1034675346 340 rnvielccppDPA------KKLLGEPFVLQQAVPVDLFPHTPHCELVLLFT 384
Cdd:COG2265   337 ----------NPAtlardlALLVEGGYRLEKVQPVDMFPHTHHVESVALLE 377
rumA TIGR00479
23S rRNA (uracil-5-)-methyltransferase RumA; This protein family was first proposed to be RNA ...
15-378 8.33e-31

23S rRNA (uracil-5-)-methyltransferase RumA; This protein family was first proposed to be RNA methyltransferases by homology to the TrmA family. The member from E. coli has now been shown to act as the 23S RNA methyltransferase for the conserved U1939. The gene is now designated rumA and was previously designated ygcA. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 129571 [Multi-domain]  Cd Length: 431  Bit Score: 121.85  E-value: 8.33e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034675346  15 ERLSCL-LHPIIPSPVIN----GYRNKSTFSVNRGPDGNPKtVGFY-LGTWR--DGNVVCVQSNHL-------KNIPEKH 79
Cdd:TIGR00479  90 ERIGKFvSEPIEDVPTIGddpwGYRNKARLSLGRSPSGQLQ-AGFYqKGSHDivDVKQCPVQAPALnallpkvRAILENF 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034675346  80 SQVAQYYEVflrqsplepclvfhEGGYWRELTVRTNSQGHTMAI--ITFHpqklsqEELHVQKEIVKEFFIRGP--GAAC 155
Cdd:TIGR00479 169 GASRYLEHK--------------ELGQARHGVLRIGRHTGELSSvdRTAL------ERFPHKEELDLYLQPDSPdvKSIC 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034675346 156 -----GLTSLYFQESTMTrcshqqspyqlLFGEPYIFEELLSLKIRISPDAFFQINTAGAEMLYRTVGELTGVNSDTILL 230
Cdd:TIGR00479 229 qninpEKTNVIFGEETEV-----------IAGEMPIYDKSGDLSFTFSARDFIQVNSGQNEKLVDRALEWLELQGEERVL 297
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034675346 231 DICCGTGVIGLSLAQHTSRVLGIELLEQAVEDARWTAAFNGITNSEFHTGQAEKILPgllKSKEDGQSI-VAVVNPARAG 309
Cdd:TIGR00479 298 DAYCGMGTFTLPLAKQAKSVVGVEGVPESVEKAQQNAELNGIANVTFYHGTLETVLP---KQPWAGNGFdKVLLDPPRKG 374
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034675346 310 LHYKVIQAIRNFRAIHtLVFVSCKlhgestrnvielccPPDPAKK---LLGEPFVLQQAVPVDLFPHTPHCE 378
Cdd:TIGR00479 375 CAAGVLRTIIKLKPER-IVYVSCN--------------PATLARDleaLCKAGYTIARVQPVDMFPHTGHVE 431
rumB PRK03522
23S rRNA (uracil(747)-C(5))-methyltransferase RlmC;
179-382 1.28e-18

23S rRNA (uracil(747)-C(5))-methyltransferase RlmC;


Pssm-ID: 235128 [Multi-domain]  Cd Length: 315  Bit Score: 85.69  E-value: 1.28e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034675346 179 LLFGEPYIFEELLSLKIRISPDAFFQINTAGAEMLYRT----VGELtGVNSdtiLLDICCGTGVIGLSLAQHTSRVLGIE 254
Cdd:PRK03522  127 FLTEQQALPERFNGVPLFIRPQSFFQTNPAVAAQLYATardwVREL-PPRS---MWDLFCGVGGFGLHCATPGMQLTGIE 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034675346 255 LLEQAVEDARWTAAFNGITNSEFH--------TGQAEKilPGLlkskedgqsivAVVNPARAGLHyKVIQAIRNFRAIHT 326
Cdd:PRK03522  203 ISAEAIACAKQSAAELGLTNVQFQaldstqfaTAQGEV--PDL-----------VLVNPPRRGIG-KELCDYLSQMAPRF 268
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034675346 327 LVFVSCklhgestrNVIELccppdpAKKLLGEP-FVLQQAVPVDLFPHTPHCE-LVLL 382
Cdd:PRK03522  269 ILYSSC--------NAQTM------AKDLAHLPgYRIERVQLFDMFPHTAHYEvLTLL 312
rumA PRK13168
23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD;
173-385 7.13e-12

23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD;


Pssm-ID: 237291 [Multi-domain]  Cd Length: 443  Bit Score: 66.33  E-value: 7.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034675346 173 QQSPYQLLFGepyifeellsLKIRISPDAFFQINTAGAEMLYRTVGELTGVNSDTILLDICCGTGVIGLSLAQHTSRVLG 252
Cdd:PRK13168  255 QLSYYLPEFG----------LRLAFSPRDFIQVNAQVNQKMVARALEWLDPQPGDRVLDLFCGLGNFTLPLARQAAEVVG 324
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034675346 253 IELLEQAVEDARWTAAFNGITNSEFHTGQAEKILPGLLKSKedgQSIVAV-VNPARAGLhYKVIQAIRNFRAIhTLVFVS 331
Cdd:PRK13168  325 VEGVEAMVERARENARRNGLDNVTFYHANLEEDFTDQPWAL---GGFDKVlLDPPRAGA-AEVMQALAKLGPK-RIVYVS 399
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034675346 332 CklhgestrnvielccppDPA------KKLLGEPFVLQQAVPVDLFPHTPHCELVLLFTR 385
Cdd:PRK13168  400 C-----------------NPAtlardaGVLVEAGYRLKRAGMLDMFPHTGHVESMALFER 442
tRNA_U5-meth_tr pfam05958
tRNA (Uracil-5-)-methyltransferase; This family consists of (Uracil-5-)-methyltransferases EC: ...
178-385 3.22e-10

tRNA (Uracil-5-)-methyltransferase; This family consists of (Uracil-5-)-methyltransferases EC:2.1.1.35 from bacteria, archaea and eukaryotes. A 5-methyluridine (m(5)U) residue at position 54 is a conserved feature of bacterial and eukaryotic tRNAs. The methylation of U54 is catalyzed by the tRNA(m5U54)methyltransferase, which in Saccharomyces cerevisiae is encoded by the nonessential TRM2 gene. It is thought that tRNA modification enzymes might have a role in tRNA maturation not necessarily linked to their known catalytic activity.


Pssm-ID: 428692  Cd Length: 357  Bit Score: 60.92  E-value: 3.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034675346 178 QLLFGEPYIFEEL----LSLKIRISPDAFFQINTAGAEMLYRTVGELTGvNSDTILLDICCGTGVIGLSLAQHTSRVLGI 253
Cdd:pfam05958 151 KIVLDQDYVDETLpvagREFIYRQVENSFTQPNAAVNIKMLEWACDVTQ-GSKGDLLELYCGNGNFSLALARNFRKVLAT 229
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034675346 254 ELLEQAVEDARWTAAFNGITNSEFHTGQAEKILPGLLKSKE----------DGQSIVAVVNPARAGLHYKVIQAIRNFRA 323
Cdd:pfam05958 230 EIAKPSVAAAQYNIAANNIDNVQIIRMSAEEFTQAMNGVREfnrlkgidlkSYNCSTIFVDPPRAGLDPETLKLVQAYPR 309
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034675346 324 IhtlVFVSCklhgestrNVIELCcppdpaKKL--LGEPFVLQQAVPVDLFPHTPHCELVLLFTR 385
Cdd:pfam05958 310 I---LYISC--------NPETLC------ANLeqLSKTHRVERFALFDQFPYTHHMECGVLLEK 356
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
223-274 4.17e-08

tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 53.61  E-value: 4.17e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034675346 223 VNSDTILL-------------DICCGTGVIGLSLAQHTS--RVLGIELLEQAVEDARWTAAFNGITN 274
Cdd:COG4123    22 FGTDAVLLaafapvkkggrvlDLGTGTGVIALMLAQRSPgaRITGVEIQPEAAELARRNVALNGLED 88
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
229-280 5.83e-08

16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA G1207 methylase RsmC is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 442062 [Multi-domain]  Cd Length: 191  Bit Score: 52.50  E-value: 5.83e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034675346 229 LLDICCGTGVIGLSLAQHT--SRVLGIELLEQAVEDARWTAAFNGITNSEFHTG 280
Cdd:COG2813    53 VLDLGCGYGVIGLALAKRNpeARVTLVDVNARAVELARANAAANGLENVEVLWS 106
PRK05031 PRK05031
tRNA (uracil-5-)-methyltransferase; Validated
179-382 3.31e-07

tRNA (uracil-5-)-methyltransferase; Validated


Pssm-ID: 235332  Cd Length: 362  Bit Score: 51.75  E-value: 3.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034675346 179 LLFGEPYIFEEL----LSLKIRISPDAFFQINTAGAE-MLYRTVGELTGVNSDtiLLDICCGTGVIGLSLAQHTSRVLGI 253
Cdd:PRK05031  157 IVLDQDYVDERLpvagREFIYRQVENSFTQPNAAVNEkMLEWALDATKGSKGD--LLELYCGNGNFTLALARNFRRVLAT 234
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034675346 254 ELLEQAVEDARWTAAFNGITNSEFHTGQAEKILPGLLKSKE------------DGQSIvaVVNPARAGLHYKVIQAIRNF 321
Cdd:PRK05031  235 EISKPSVAAAQYNIAANGIDNVQIIRMSAEEFTQAMNGVREfnrlkgidlksyNFSTI--FVDPPRAGLDDETLKLVQAY 312
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034675346 322 RAIhtlVFVSCK---LHgestRNVIELCCPPDPAKkllgepFVLqqavpVDLFPHTPHCEL-VLL 382
Cdd:PRK05031  313 ERI---LYISCNpetLC----ENLETLSQTHKVER------FAL-----FDQFPYTHHMECgVLL 359
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
230-285 1.18e-06

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 46.40  E-value: 1.18e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034675346 230 LDICCGTGVIGLSLAQHT-SRVLGIELLEQAVEDARWTAAFNGItNSEFHTGQAEKI 285
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGgARVTGVDLSPEMLERARERAAEAGL-NVEFVQGDAEDL 57
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
213-285 2.17e-06

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 46.91  E-value: 2.17e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034675346 213 LYRTVGELTGVNSDTILLDICCGTGVIGLSLAQHTSRVLGIELLEQAVEDARWTAAFNGItNSEFHTGQAEKI 285
Cdd:COG2226    10 GREALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGL-NVEFVVGDAEDL 81
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
182-280 4.37e-06

Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 47.84  E-value: 4.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034675346 182 GEP--YI--FEELLSLKIRISPDAFfqI---NTagaEMLYRTVGELTGVNSDTILLDICCGTGVIGLSLAQH--TSRVLG 252
Cdd:COG2890    67 GEPlaYIlgEAEFYGLEFKVDPGVL--IprpET---EELVELALALLPAGAPPRVLDLGTGSGAIALALAKErpDARVTA 141
                          90       100
                  ....*....|....*....|....*....
gi 1034675346 253 IELLEQAVEDARWTAAFNGITNS-EFHTG 280
Cdd:COG2890   142 VDISPDALAVARRNAERLGLEDRvRFLQG 170
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
224-285 7.92e-06

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 45.49  E-value: 7.92e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034675346 224 NSDTILLDICCGTGVIGLSLAQHT---SRVLGIELLEQAVEDARWTAAFNGITNSEFHTGQAEKI 285
Cdd:pfam13847   2 DKGMRVLDLGCGTGHLSFELAEELgpnAEVVGIDISEEAIEKARENAQKLGFDNVEFEQGDIEEL 66
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
230-280 1.39e-05

N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 46.31  E-value: 1.39e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034675346 230 LDICCGTGVIGLSLAQH--TSRVLGIELLEQAVEDARWTAAFNGITNSEFHTG 280
Cdd:PRK09328  113 LDLGTGSGAIALALAKErpDAEVTAVDISPEALAVARRNAKHGLGARVEFLQG 165
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
229-285 2.67e-05

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 43.47  E-value: 2.67e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034675346 229 LLDICCGTGVIGLSLAQHTSRVLGIELLEQAVEDARWTAAFNGItnsEFHTGQAEKI 285
Cdd:COG2227    28 VLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAELNV---DFVQGDLEDL 81
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
230-287 3.98e-05

SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 44.14  E-value: 3.98e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034675346 230 LDICCGTGVIGLSLAQHT-SRVLGIELLEQAVEDARWTAAFNGITNSEFHTGQAEKILP 287
Cdd:COG0500    31 LDLGCGTGRNLLALAARFgGRVIGIDLSPEAIALARARAAKAGLGNVEFLVADLAELDP 89
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
230-318 9.03e-05

Methyltransferase small domain; This domain is found in ribosomal RNA small subunit methyltransferase C as well as other methyltransferases.


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 42.58  E-value: 9.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034675346 230 LDICCGTGVIGLSLAQHTSRVlGIELLE---QAVEDARWTAAFNGITNSEFHTGQaekilpgLLKSKEDGQSIVAVVNPA 306
Cdd:pfam05175  36 LDLGCGAGVLGAALAKESPDA-ELTMVDinaRALESARENLAANGLENGEVVASD-------VYSGVEDGKFDLIISNPP 107
                          90
                  ....*....|....*
gi 1034675346 307 -RAGLH--YKVIQAI 318
Cdd:pfam05175 108 fHAGLAttYNVAQRF 122
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
229-322 1.02e-04

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: 41.26  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034675346 229 LLDICCGTGVIGLSLAQHTS-RVLGIELLEQAVEDARWTAAFNGITNSEFHTGQAEKILPgllksKEDGQSIVAVVNPAR 307
Cdd:cd02440     2 VLDLGCGTGALALALASGPGaRVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPP-----EADESFDVIISDPPL 76
                          90
                  ....*....|....*
gi 1034675346 308 AGLHYKVIQAIRNFR 322
Cdd:cd02440    77 HHLVEDLARFLEEAR 91
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
223-301 1.14e-04

Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal protein L11 methyltransferase (EC:2.1.1.-) sequences.


Pssm-ID: 428888 [Multi-domain]  Cd Length: 294  Bit Score: 43.41  E-value: 1.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034675346 223 VNSDTILLDICCGTGVigLSLAQH---TSRVLGIELLEQAVEDARWTAAFNGITNsefhtgQAEKILPG-LLKSKEDGqs 298
Cdd:pfam06325 159 VKPGESVLDVGCGSGI--LAIAALklgAKKVVGVDIDPVAVRAAKENAELNGVEA------RLEVYLPGdLPKEKADV-- 228

                  ...
gi 1034675346 299 IVA 301
Cdd:pfam06325 229 VVA 231
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
230-264 1.42e-04

Predicted methyltransferase, contains TPR repeat [General function prediction only];


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 42.29  E-value: 1.42e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1034675346 230 LDICCGTGVIGLSLAQHTSRVLGIELLEQAVEDAR 264
Cdd:COG4976    51 LDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAR 85
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
215-285 1.02e-03

tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 N-methylase Trm11 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440663 [Multi-domain]  Cd Length: 172  Bit Score: 39.55  E-value: 1.02e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034675346 215 RTVGELTGVNSDTILLDICCGTGVI---GLSLAqhtSRVLGIELLEQAVEDARWTAAFNGITNSEFHTGQAEKI 285
Cdd:COG1041    16 RALVNLAGAKEGDTVLDPFCGTGTIlieAGLLG---RRVIGSDIDPKMVEGARENLEHYGYEDADVIRGDARDL 86
PRK14968 PRK14968
putative methyltransferase; Provisional
230-274 1.83e-03

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 39.11  E-value: 1.83e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1034675346 230 LDICCGTGVIGLSLAQHTSRVLGIELLEQAVEDARWTAAFNGITN 274
Cdd:PRK14968   28 LEVGTGSGIVAIVAAKNGKKVVGVDINPYAVECAKCNAKLNNIRN 72
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
230-288 2.63e-03

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 37.11  E-value: 2.63e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034675346 230 LDICCGTGVIGLSLAQHT--SRVLGIELLEQAVEDARwtAAFNGITnseFHTGQAEKILPG 288
Cdd:COG4106     6 LDLGCGTGRLTALLAERFpgARVTGVDLSPEMLARAR--ARLPNVR---FVVADLRDLDPP 61
 
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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