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Conserved domains on  [gi|530422192|ref|XP_005262258|]
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tRNA (uracil-5-)-methyltransferase homolog B isoform X4 [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

CATH:  2.20.25.110
EC:  2.1.1.-
Gene Ontology:  GO:0001510|GO:0046872|GO:0008757|GO:1904047
PubMed:  12826405|12504684
SCOP:  3000118

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 ...
 62-264 3.85e-57

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: 186.92  E-value: 3.85e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422192  62 GEPYIFEELLSLKIRISPDAFFQINTAGAEMLYRTVGELTGVNSDTILLDICCGTGVIGLSLAQHTSRVLGIELLEQAVE 141
Cdd:COG2265  190 GRDYLTERLGGLTFRISPGSFFQVNPEQAEALYAAALEWLDLTGGERVLDLYCGVGTFALPLARRAKKVIGVEIVPEAVE 269

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422192 142 DARWTAAFNGITNSEFHTGQAEKILPGLLKSKE-DgqsiVAVVNPARAGLHYKVIQAIRNFRAiHTLVFVSCklhgestr 220
Cdd:COG2265  270 DARENARLNGLKNVEFVAGDLEEVLPELLWGGRpD----VVVLDPPRAGAGPEVLEALAALGP-RRIVYVSC-------- 336

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 530422192 221 nvielccppDPA------KKLLGEPFVLQQAVPVDLFPHTPHCELVLLFT 264
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 ...
 62-264 3.85e-57

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: 186.92  E-value: 3.85e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422192  62 GEPYIFEELLSLKIRISPDAFFQINTAGAEMLYRTVGELTGVNSDTILLDICCGTGVIGLSLAQHTSRVLGIELLEQAVE 141
Cdd:COG2265  190 GRDYLTERLGGLTFRISPGSFFQVNPEQAEALYAAALEWLDLTGGERVLDLYCGVGTFALPLARRAKKVIGVEIVPEAVE 269

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422192 142 DARWTAAFNGITNSEFHTGQAEKILPGLLKSKE-DgqsiVAVVNPARAGLHYKVIQAIRNFRAiHTLVFVSCklhgestr 220
Cdd:COG2265  270 DARENARLNGLKNVEFVAGDLEEVLPELLWGGRpD----VVVLDPPRAGAGPEVLEALAALGP-RRIVYVSC-------- 336

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 530422192 221 nvielccppDPA------KKLLGEPFVLQQAVPVDLFPHTPHCELVLLFT 264
Cdd:COG2265  337 ---------NPAtlardlALLVEGGYRLEKVQPVDMFPHTHHVESVALLE 377
rumA TIGR00479
23S rRNA (uracil-5-)-methyltransferase RumA; This protein family was first proposed to be RNA ...
 60-258 3.90e-30

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: 116.84  E-value: 3.90e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422192   60 LFGEPYIFEELLSLKIRISPDAFFQINTAGAEMLYRTVGELTGVNSDTILLDICCGTGVIGLSLAQHTSRVLGIELLEQA 139
Cdd:TIGR00479 247 IAGEMPIYDKSGDLSFTFSARDFIQVNSGQNEKLVDRALEWLELQGEERVLDAYCGMGTFTLPLAKQAKSVVGVEGVPES 326

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422192  140 VEDARWTAAFNGITNSEFHTGQAEKILPgllKSKEDGQSI-VAVVNPARAGLHYKVIQAIRNFRAIHtLVFVSCKlhges 218
Cdd:TIGR00479 327 VEKAQQNAELNGIANVTFYHGTLETVLP---KQPWAGNGFdKVLLDPPRKGCAAGVLRTIIKLKPER-IVYVSCN----- 397

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 530422192  219 trnvielccPPDPAKK---LLGEPFVLQQAVPVDLFPHTPHCE 258
Cdd:TIGR00479 398 ---------PATLARDleaLCKAGYTIARVQPVDMFPHTGHVE 431
rumB PRK03522
23S rRNA (uracil(747)-C(5))-methyltransferase RlmC;
59-262 8.34e-19

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


Pssm-ID: 235128 [Multi-domain]  Cd Length: 315  Bit Score: 83.76  E-value: 8.34e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422192  59 LLFGEPYIFEELLSLKIRISPDAFFQINTAGAEMLYRT----VGELtGVNSdtiLLDICCGTGVIGLSLAQHTSRVLGIE 134
Cdd:PRK03522 127 FLTEQQALPERFNGVPLFIRPQSFFQTNPAVAAQLYATardwVREL-PPRS---MWDLFCGVGGFGLHCATPGMQLTGIE 202

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422192 135 LLEQAVEDARWTAAFNGITNSEFHTGQAekilPGLLKSKEDGQSIVaVVNPARAGLHyKVIQAIRNFRAIHTLVFVSCkl 214
Cdd:PRK03522 203 ISAEAIACAKQSAAELGLTNVQFQALDS----TQFATAQGEVPDLV-LVNPPRRGIG-KELCDYLSQMAPRFILYSSC-- 274

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 530422192 215 hgestrNVIELccppdpAKKLLGEP-FVLQQAVPVDLFPHTPHCE-LVLL 262
Cdd:PRK03522 275 ------NAQTM------AKDLAHLPgYRIERVQLFDMFPHTAHYEvLTLL 312
tRNA_U5-meth_tr pfam05958
tRNA (Uracil-5-)-methyltransferase; This family consists of (Uracil-5-)-methyltransferases EC: ...
 58-265 1.33e-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: 1.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422192   58 QLLFGEPYIFEEL----LSLKIRISPDAFFQINTAGAEMLYRTVGELTGvNSDTILLDICCGTGVIGLSLAQHTSRVLGI 133
Cdd:pfam05958 151 KIVLDQDYVDETLpvagREFIYRQVENSFTQPNAAVNIKMLEWACDVTQ-GSKGDLLELYCGNGNFSLALARNFRKVLAT 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422192  134 ELLEQAVEDARWTAAFNGITNSEFHTGQAEKILPGLLKSKE----------DGQSIVAVVNPARAGLHYKVIQAIRNFRA 203
Cdd:pfam05958 230 EIAKPSVAAAQYNIAANNIDNVQIIRMSAEEFTQAMNGVREfnrlkgidlkSYNCSTIFVDPPRAGLDPETLKLVQAYPR 309

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530422192  204 IhtlVFVSCklhgestrNVIELCcppdpaKKL--LGEPFVLQQAVPVDLFPHTPHCELVLLFTR 265
Cdd:pfam05958 310 I---LYISC--------NPETLC------ANLeqLSKTHRVERFALFDQFPYTHHMECGVLLEK 356
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 109-202 1.82e-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: 40.11  E-value: 1.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422192 109 LLDICCGTGVIGLSLAQHTS-RVLGIELLEQAVEDARWTAAFNGITNSEFHTGQAEKILPgllksKEDGQSIVAVVNPAR 187
Cdd:cd02440    2 VLDLGCGTGALALALASGPGaRVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPP-----EADESFDVIISDPPL 76

                         90
                 ....*....|....*
gi 530422192 188 AGLHYKVIQAIRNFR 202
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 ...
 62-264 3.85e-57

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: 186.92  E-value: 3.85e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422192  62 GEPYIFEELLSLKIRISPDAFFQINTAGAEMLYRTVGELTGVNSDTILLDICCGTGVIGLSLAQHTSRVLGIELLEQAVE 141
Cdd:COG2265  190 GRDYLTERLGGLTFRISPGSFFQVNPEQAEALYAAALEWLDLTGGERVLDLYCGVGTFALPLARRAKKVIGVEIVPEAVE 269

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422192 142 DARWTAAFNGITNSEFHTGQAEKILPGLLKSKE-DgqsiVAVVNPARAGLHYKVIQAIRNFRAiHTLVFVSCklhgestr 220
Cdd:COG2265  270 DARENARLNGLKNVEFVAGDLEEVLPELLWGGRpD----VVVLDPPRAGAGPEVLEALAALGP-RRIVYVSC-------- 336

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 530422192 221 nvielccppDPA------KKLLGEPFVLQQAVPVDLFPHTPHCELVLLFT 264
Cdd:COG2265  337 ---------NPAtlardlALLVEGGYRLEKVQPVDMFPHTHHVESVALLE 377
rumA TIGR00479
23S rRNA (uracil-5-)-methyltransferase RumA; This protein family was first proposed to be RNA ...
 60-258 3.90e-30

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: 116.84  E-value: 3.90e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422192   60 LFGEPYIFEELLSLKIRISPDAFFQINTAGAEMLYRTVGELTGVNSDTILLDICCGTGVIGLSLAQHTSRVLGIELLEQA 139
Cdd:TIGR00479 247 IAGEMPIYDKSGDLSFTFSARDFIQVNSGQNEKLVDRALEWLELQGEERVLDAYCGMGTFTLPLAKQAKSVVGVEGVPES 326

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422192  140 VEDARWTAAFNGITNSEFHTGQAEKILPgllKSKEDGQSI-VAVVNPARAGLHYKVIQAIRNFRAIHtLVFVSCKlhges 218
Cdd:TIGR00479 327 VEKAQQNAELNGIANVTFYHGTLETVLP---KQPWAGNGFdKVLLDPPRKGCAAGVLRTIIKLKPER-IVYVSCN----- 397

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 530422192  219 trnvielccPPDPAKK---LLGEPFVLQQAVPVDLFPHTPHCE 258
Cdd:TIGR00479 398 ---------PATLARDleaLCKAGYTIARVQPVDMFPHTGHVE 431
rumB PRK03522
23S rRNA (uracil(747)-C(5))-methyltransferase RlmC;
59-262 8.34e-19

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


Pssm-ID: 235128 [Multi-domain]  Cd Length: 315  Bit Score: 83.76  E-value: 8.34e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422192  59 LLFGEPYIFEELLSLKIRISPDAFFQINTAGAEMLYRT----VGELtGVNSdtiLLDICCGTGVIGLSLAQHTSRVLGIE 134
Cdd:PRK03522 127 FLTEQQALPERFNGVPLFIRPQSFFQTNPAVAAQLYATardwVREL-PPRS---MWDLFCGVGGFGLHCATPGMQLTGIE 202

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422192 135 LLEQAVEDARWTAAFNGITNSEFHTGQAekilPGLLKSKEDGQSIVaVVNPARAGLHyKVIQAIRNFRAIHTLVFVSCkl 214
Cdd:PRK03522 203 ISAEAIACAKQSAAELGLTNVQFQALDS----TQFATAQGEVPDLV-LVNPPRRGIG-KELCDYLSQMAPRFILYSSC-- 274

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 530422192 215 hgestrNVIELccppdpAKKLLGEP-FVLQQAVPVDLFPHTPHCE-LVLL 262
Cdd:PRK03522 275 ------NAQTM------AKDLAHLPgYRIERVQLFDMFPHTAHYEvLTLL 312
rumA PRK13168
23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD;
53-265 4.18e-12

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


Pssm-ID: 237291 [Multi-domain]  Cd Length: 443  Bit Score: 65.56  E-value: 4.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422192  53 QQSPYQLLFGepyifeellsLKIRISPDAFFQINTAGAEMLYRTVGELTGVNSDTILLDICCGTGVIGLSLAQHTSRVLG 132
Cdd:PRK13168 255 QLSYYLPEFG----------LRLAFSPRDFIQVNAQVNQKMVARALEWLDPQPGDRVLDLFCGLGNFTLPLARQAAEVVG 324

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422192 133 IELLEQAVEDARWTAAFNGITNSEFHTGQAEKILPGLLKSKedgQSIVAV-VNPARAGLhYKVIQAIRNFRAIhTLVFVS 211
Cdd:PRK13168 325 VEGVEAMVERARENARRNGLDNVTFYHANLEEDFTDQPWAL---GGFDKVlLDPPRAGA-AEVMQALAKLGPK-RIVYVS 399

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422192 212 CklhgestrnvielccppDPA------KKLLGEPFVLQQAVPVDLFPHTPHCELVLLFTR 265
Cdd:PRK13168 400 C-----------------NPAtlardaGVLVEAGYRLKRAGMLDMFPHTGHVESMALFER 442
tRNA_U5-meth_tr pfam05958
tRNA (Uracil-5-)-methyltransferase; This family consists of (Uracil-5-)-methyltransferases EC: ...
 58-265 1.33e-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: 1.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422192   58 QLLFGEPYIFEEL----LSLKIRISPDAFFQINTAGAEMLYRTVGELTGvNSDTILLDICCGTGVIGLSLAQHTSRVLGI 133
Cdd:pfam05958 151 KIVLDQDYVDETLpvagREFIYRQVENSFTQPNAAVNIKMLEWACDVTQ-GSKGDLLELYCGNGNFSLALARNFRKVLAT 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422192  134 ELLEQAVEDARWTAAFNGITNSEFHTGQAEKILPGLLKSKE----------DGQSIVAVVNPARAGLHYKVIQAIRNFRA 203
Cdd:pfam05958 230 EIAKPSVAAAQYNIAANNIDNVQIIRMSAEEFTQAMNGVREfnrlkgidlkSYNCSTIFVDPPRAGLDPETLKLVQAYPR 309

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530422192  204 IhtlVFVSCklhgestrNVIELCcppdpaKKL--LGEPFVLQQAVPVDLFPHTPHCELVLLFTR 265
Cdd:pfam05958 310 I---LYISC--------NPETLC------ANLeqLSKTHRVERFALFDQFPYTHHMECGVLLEK 356
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 109-160 3.04e-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: 3.04e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530422192 109 LLDICCGTGVIGLSLAQHT--SRVLGIELLEQAVEDARWTAAFNGITNSEFHTG 160
Cdd:COG2813   53 VLDLGCGYGVIGLALAKRNpeARVTLVDVNARAVELARANAAANGLENVEVLWS 106
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 109-154 4.53e-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: 52.45  E-value: 4.53e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 530422192 109 LLDICCGTGVIGLSLAQHTS--RVLGIELLEQAVEDARWTAAFNGITN 154
Cdd:COG4123   41 VLDLGTGTGVIALMLAQRSPgaRITGVEIQPEAAELARRNVALNGLED 88
PRK05031 PRK05031
tRNA (uracil-5-)-methyltransferase; Validated
 59-262 3.14e-07

tRNA (uracil-5-)-methyltransferase; Validated


Pssm-ID: 235332  Cd Length: 362  Bit Score: 50.60  E-value: 3.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422192  59 LLFGEPYIFEEL----LSLKIRISPDAFFQINTAGAE-MLYRTVGELTGVNSDtiLLDICCGTGVIGLSLAQHTSRVLGI 133
Cdd:PRK05031 157 IVLDQDYVDERLpvagREFIYRQVENSFTQPNAAVNEkMLEWALDATKGSKGD--LLELYCGNGNFTLALARNFRRVLAT 234

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422192 134 ELLEQAVEDARWTAAFNGITNSEFHTGQAEKILPGLLKSKE------------DGQSIvaVVNPARAGLHYKVIQAIRNF 201
Cdd:PRK05031 235 EISKPSVAAAQYNIAANGIDNVQIIRMSAEEFTQAMNGVREfnrlkgidlksyNFSTI--FVDPPRAGLDDETLKLVQAY 312

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530422192 202 RAIhtlVFVSCK---LHgestRNVIELCCPPDPAKkllgepFVLqqavpVDLFPHTPHCEL-VLL 262
Cdd:PRK05031 313 ERI---LYISCNpetLC----ENLETLSQTHKVER------FAL-----FDQFPYTHHMECgVLL 359
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 110-165 8.91e-07

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 46.02  E-value: 8.91e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 530422192  110 LDICCGTGVIGLSLAQHT-SRVLGIELLEQAVEDARWTAAFNGItNSEFHTGQAEKI 165
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGgARVTGVDLSPEMLERARERAAEAGL-NVEFVQGDAEDL 57
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 93-165 1.94e-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: 46.14  E-value: 1.94e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530422192  93 LYRTVGELTGVNSDTILLDICCGTGVIGLSLAQHTSRVLGIELLEQAVEDARWTAAFNGItNSEFHTGQAEKI 165
Cdd:COG2226   10 GREALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGL-NVEFVVGDAEDL 81
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 62-160 4.29e-06

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 47.07  E-value: 4.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422192  62 GEP--YI--FEELLSLKIRISPDAFfqI---NTagaEMLYRTVGELTGVNSDTILLDICCGTGVIGLSLAQH--TSRVLG 132
Cdd:COG2890   67 GEPlaYIlgEAEFYGLEFKVDPGVL--IprpET---EELVELALALLPAGAPPRVLDLGTGSGAIALALAKErpDARVTA 141

                         90       100
                 ....*....|....*....|....*....
gi 530422192 133 IELLEQAVEDARWTAAFNGITNS-EFHTG 160
Cdd:COG2890  142 VDISPDALAVARRNAERLGLEDRvRFLQG 170
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 104-165 1.09e-05

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 44.33  E-value: 1.09e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530422192  104 NSDTILLDICCGTGVIGLSLAQHT---SRVLGIELLEQAVEDARWTAAFNGITNSEFHTGQAEKI 165
Cdd:pfam13847   2 DKGMRVLDLGCGTGHLSFELAEELgpnAEVVGIDISEEAIEKARENAQKLGFDNVEFEQGDIEEL 66
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 110-160 1.34e-05

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 45.54  E-value: 1.34e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530422192 110 LDICCGTGVIGLSLAQH--TSRVLGIELLEQAVEDARWTAAFNGITNSEFHTG 160
Cdd:PRK09328 113 LDLGTGSGAIALALAKErpDAEVTAVDISPEALAVARRNAKHGLGARVEFLQG 165
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 109-165 2.00e-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: 43.08  E-value: 2.00e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 530422192 109 LLDICCGTGVIGLSLAQHTSRVLGIELLEQAVEDARWTAAFNGItnsEFHTGQAEKI 165
Cdd:COG2227   28 VLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAELNV---DFVQGDLEDL 81
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 110-167 5.06e-05

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 42.98  E-value: 5.06e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 530422192 110 LDICCGTGVIGLSLAQHT-SRVLGIELLEQAVEDARWTAAFNGITNSEFHTGQAEKILP 167
Cdd:COG0500   31 LDLGCGTGRNLLALAARFgGRVIGIDLSPEAIALARARAAKAGLGNVEFLVADLAELDP 89
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 110-198 6.85e-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: 42.19  E-value: 6.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422192  110 LDICCGTGVIGLSLAQHTSRVlGIELLE---QAVEDARWTAAFNGITNSEFHTGQaekilpgLLKSKEDGQSIVAVVNPA 186
Cdd:pfam05175  36 LDLGCGAGVLGAALAKESPDA-ELTMVDinaRALESARENLAANGLENGEVVASD-------VYSGVEDGKFDLIISNPP 107

                          90
                  ....*....|....*
gi 530422192  187 -RAGLH--YKVIQAI 198
Cdd:pfam05175 108 fHAGLAttYNVAQRF 122
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 103-181 7.17e-05

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: 7.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422192  103 VNSDTILLDICCGTGVigLSLAQH---TSRVLGIELLEQAVEDARWTAAFNGITNsefhtgQAEKILPG-LLKSKEDGqs 178
Cdd:pfam06325 159 VKPGESVLDVGCGSGI--LAIAALklgAKKVVGVDIDPVAVRAAKENAELNGVEA------RLEVYLPGdLPKEKADV-- 228


                  ...
gi 530422192  179 IVA 181
Cdd:pfam06325 229 VVA 231
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
110-144 1.03e-04

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 41.91  E-value: 1.03e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 530422192 110 LDICCGTGVIGLSLAQHTSRVLGIELLEQAVEDAR 144
Cdd:COG4976   51 LDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAR 85
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 109-202 1.82e-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: 40.11  E-value: 1.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530422192 109 LLDICCGTGVIGLSLAQHTS-RVLGIELLEQAVEDARWTAAFNGITNSEFHTGQAEKILPgllksKEDGQSIVAVVNPAR 187
Cdd:cd02440    2 VLDLGCGTGALALALASGPGaRVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPP-----EADESFDVIISDPPL 76

                         90
                 ....*....|....*
gi 530422192 188 AGLHYKVIQAIRNFR 202
Cdd:cd02440   77 HHLVEDLARFLEEAR 91
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 95-165 6.02e-04

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: 6.02e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530422192  95 RTVGELTGVNSDTILLDICCGTGVI---GLSLAqhtSRVLGIELLEQAVEDARWTAAFNGITNSEFHTGQAEKI 165
Cdd:COG1041   16 RALVNLAGAKEGDTVLDPFCGTGTIlieAGLLG---RRVIGSDIDPKMVEGARENLEHYGYEDADVIRGDARDL 86
PRK14968 PRK14968
putative methyltransferase; Provisional
 110-154 1.06e-03

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 39.11  E-value: 1.06e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 530422192 110 LDICCGTGVIGLSLAQHTSRVLGIELLEQAVEDARWTAAFNGITN 154
Cdd:PRK14968  28 LEVGTGSGIVAIVAAKNGKKVVGVDINPYAVECAKCNAKLNNIRN 72
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
110-168 2.31e-03

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 36.73  E-value: 2.31e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530422192 110 LDICCGTGVIGLSLAQHT--SRVLGIELLEQAVEDARwtAAFNGITnseFHTGQAEKILPG 168
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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