|
Name |
Accession |
Description |
Interval |
E-value |
| meth_trns_rumB |
TIGR02085 |
23S rRNA (uracil-5-)-methyltransferase RumB; This family consists of RNA methyltransferases ... |
2-374 |
0e+00 |
|
23S rRNA (uracil-5-)-methyltransferase RumB; This family consists of RNA methyltransferases designated RumB, formerly YbjF. Members act on 23S rRNA U747 and the equivalent position in other proteobacterial species. This family is homologous to the other 23S rRNA methyltransferase RumA and to the tRNA methyltransferase TrmA. [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 131140 Cd Length: 374 Bit Score: 736.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447072511 2 QCALYDAGRCRSCQWITQPIPQQLSAKTADLKNLLA-DFPVVEWCAPVSGPEQGFRNKAKMVVSGSVEKPLLGMLHRDGT 80
Cdd:TIGR02085 1 QCAFYIQGRCRSCQWLAQPYSEQLTNKQQHLKELLApNATVVQWLAPVTSAEQAFRNKAKMVVSGSVERPILGILHRDGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447072511 81 PEDLCDCPLYPASFAPVFAALKPFIARAGLTPYNVARKRGELKYILLTESQSDGGMMLRFVLRSDTKLAQLRKALPWLHE 160
Cdd:TIGR02085 81 PLDLCDCPLYPQSFQPVFAYLKNFIARAGLTPYNVAKKKGELKFILLTESENSGQLMLRFVLRSETKLAQIRRALPWLIE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447072511 161 QLPQLKVITVNIQPVHMAIMEGETEIYLTEQQALAERFNDVPLWIRPQSFFQTNPAVASQLYATARDWVRQLPVKHMWDL 240
Cdd:TIGR02085 161 QLPQLEVISVNIQPVHMAILEGEEEIFLTEQQALPERFNDVPLVIRPQSFFQTNPKVAAQLYATARQWVREIPVTQMWDL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447072511 241 FCGVGGFGLHCATPDMQLTGIEIASEAIACAKQSAAELGLTRLQFQALDSTQFATAQGDVPELVLVNPPRRGIGKPLCDY 320
Cdd:TIGR02085 241 FCGVGGFGLHCAGPDTQLTGIEIESEAIACAQQSAQMLGLDNLSFAALDSAKFATAQMSAPELVLVNPPRRGIGKELCDY 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 447072511 321 LSTMAPRFIIYSSCNAQTMAKDIRELPGFRIERVQLFDMFPHTAHYEVLTLLVK 374
Cdd:TIGR02085 321 LSQMAPKFILYSSCNAQTMAKDIAELSGYQIERVQLFDMFPHTSHYEVLTLLVR 374
|
|
| rumB |
PRK03522 |
23S rRNA (uracil(747)-C(5))-methyltransferase RlmC; |
61-375 |
0e+00 |
|
23S rRNA (uracil(747)-C(5))-methyltransferase RlmC;
Pssm-ID: 235128 [Multi-domain] Cd Length: 315 Bit Score: 675.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447072511 61 MVVSGSVEKPLLGMLHRDGTPEDLCDCPLYPASFAPVFAALKPFIARAGLTPYNVARKRGELKYILLTESQSDGGMMLRF 140
Cdd:PRK03522 1 MVVSGSVERPLLGILHRDGTPVDLCDCPLYPASFAPVFAALKPFIARAGLTPYNVARKRGELKYILLTESQSDGELMLRF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447072511 141 VLRSDTKLAQLRKALPWLHEQLPQLKVITVNIQPVHMAIMEGETEIYLTEQQALAERFNDVPLWIRPQSFFQTNPAVASQ 220
Cdd:PRK03522 81 VLRSETKLARLRRALPWLQAQLPQLKVISVNIQPVHMAILEGEEEIFLTEQQALPERFNGVPLFIRPQSFFQTNPAVAAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447072511 221 LYATARDWVRQLPVKHMWDLFCGVGGFGLHCATPDMQLTGIEIASEAIACAKQSAAELGLTRLQFQALDSTQFATAQGDV 300
Cdd:PRK03522 161 LYATARDWVRELPPRSMWDLFCGVGGFGLHCATPGMQLTGIEISAEAIACAKQSAAELGLTNVQFQALDSTQFATAQGEV 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447072511 301 PELVLVNPPRRGIGKPLCDYLSTMAPRFIIYSSCNAQTMAKDIRELPGFRIERVQLFDMFPHTAHYEVLTLLVKQ 375
Cdd:PRK03522 241 PDLVLVNPPRRGIGKELCDYLSQMAPRFILYSSCNAQTMAKDLAHLPGYRIERVQLFDMFPHTAHYEVLTLLVRQ 315
|
|
| TrmA |
COG2265 |
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ... |
3-373 |
1.28e-102 |
|
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: 307.87 E-value: 1.28e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447072511 3 CALYdaGRCRSCQWITQPIPQQLSAKTADLKNLL---ADFPVVEWcAPV--SGPEQGFRNKAKMVVSGSVEKPLLGMlHR 77
Cdd:COG2265 67 CPHF--GRCGGCQLQHLSYEAQLELKQRVVREALeriGGLPEVEV-EPIigSPEPWGYRNRARLSVRRTDGRLRLGF-YA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447072511 78 DGTPE--DLCDCPLYPASFAPVFAALKPFIARAGltpynvaRKRGELKYILLTEsqsdggmmlrfvlrsdtklaqlrkal 155
Cdd:COG2265 143 RGSHElvDIDECPLLDPALNALLPALRELLAELG-------ARRGELRHLVVRA-------------------------- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447072511 156 pwlheqlpqlkvitvniqpvhmaimegeteiyltEQQALAERFNDVPLWIRPQSFFQTNPAVASQLYATARDWVRQLPVK 235
Cdd:COG2265 190 ----------------------------------GRDYLTERLGGLTFRISPGSFFQVNPEQAEALYAAALEWLDLTGGE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447072511 236 HMWDLFCGVGGFGLHCATPDMQLTGIEIASEAIACAKQSAAELGLTRLQFQALDSTQFATAQ--GDVPELVLVNPPRRGI 313
Cdd:COG2265 236 RVLDLYCGVGTFALPLARRAKKVIGVEIVPEAVEDARENARLNGLKNVEFVAGDLEEVLPELlwGGRPDVVVLDPPRAGA 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447072511 314 GKPLCDYLSTMAPRFIIYSSCNAQTMAKDIRELP--GFRIERVQLFDMFPHTAHYEVLTLLV 373
Cdd:COG2265 316 GPEVLEALAALGPRRIVYVSCNPATLARDLALLVegGYRLEKVQPVDMFPHTHHVESVALLE 377
|
|
| tRNA_U5-meth_tr |
pfam05958 |
tRNA (Uracil-5-)-methyltransferase; This family consists of (Uracil-5-)-methyltransferases EC: ... |
209-374 |
1.17e-17 |
|
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: 83.26 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447072511 209 SFFQTNPAVASQLYATARDwVRQLPVKHMWDLFCGVGGFGLHCATPDMQLTGIEIASEAIACAKQSAAELGLTRLQFQAL 288
Cdd:pfam05958 178 SFTQPNAAVNIKMLEWACD-VTQGSKGDLLELYCGNGNFSLALARNFRKVLATEIAKPSVAAAQYNIAANNIDNVQIIRM 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447072511 289 DSTQFATAQGDVPEL---------------VLVNPPRRGIGKPLCDyLSTMAPRfIIYSSCNAQTMAKDIRELP-GFRIE 352
Cdd:pfam05958 257 SAEEFTQAMNGVREFnrlkgidlksyncstIFVDPPRAGLDPETLK-LVQAYPR-ILYISCNPETLCANLEQLSkTHRVE 334
|
170 180
....*....|....*....|..
gi 447072511 353 RVQLFDMFPHTAHYEVLTLLVK 374
Cdd:pfam05958 335 RFALFDQFPYTHHMECGVLLEK 356
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
238-309 |
5.99e-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: 41.65 E-value: 5.99e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447072511 238 WDLFCGVGGFGLHCA-TPDMQLTGIEIASEAIACAKQSAAELGLTRLQFQALDSTQFATAQGDVPELVLVNPP 309
Cdd:cd02440 3 LDLGCGTGALALALAsGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPEADESFDVIISDPP 75
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| meth_trns_rumB |
TIGR02085 |
23S rRNA (uracil-5-)-methyltransferase RumB; This family consists of RNA methyltransferases ... |
2-374 |
0e+00 |
|
23S rRNA (uracil-5-)-methyltransferase RumB; This family consists of RNA methyltransferases designated RumB, formerly YbjF. Members act on 23S rRNA U747 and the equivalent position in other proteobacterial species. This family is homologous to the other 23S rRNA methyltransferase RumA and to the tRNA methyltransferase TrmA. [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 131140 Cd Length: 374 Bit Score: 736.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447072511 2 QCALYDAGRCRSCQWITQPIPQQLSAKTADLKNLLA-DFPVVEWCAPVSGPEQGFRNKAKMVVSGSVEKPLLGMLHRDGT 80
Cdd:TIGR02085 1 QCAFYIQGRCRSCQWLAQPYSEQLTNKQQHLKELLApNATVVQWLAPVTSAEQAFRNKAKMVVSGSVERPILGILHRDGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447072511 81 PEDLCDCPLYPASFAPVFAALKPFIARAGLTPYNVARKRGELKYILLTESQSDGGMMLRFVLRSDTKLAQLRKALPWLHE 160
Cdd:TIGR02085 81 PLDLCDCPLYPQSFQPVFAYLKNFIARAGLTPYNVAKKKGELKFILLTESENSGQLMLRFVLRSETKLAQIRRALPWLIE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447072511 161 QLPQLKVITVNIQPVHMAIMEGETEIYLTEQQALAERFNDVPLWIRPQSFFQTNPAVASQLYATARDWVRQLPVKHMWDL 240
Cdd:TIGR02085 161 QLPQLEVISVNIQPVHMAILEGEEEIFLTEQQALPERFNDVPLVIRPQSFFQTNPKVAAQLYATARQWVREIPVTQMWDL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447072511 241 FCGVGGFGLHCATPDMQLTGIEIASEAIACAKQSAAELGLTRLQFQALDSTQFATAQGDVPELVLVNPPRRGIGKPLCDY 320
Cdd:TIGR02085 241 FCGVGGFGLHCAGPDTQLTGIEIESEAIACAQQSAQMLGLDNLSFAALDSAKFATAQMSAPELVLVNPPRRGIGKELCDY 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 447072511 321 LSTMAPRFIIYSSCNAQTMAKDIRELPGFRIERVQLFDMFPHTAHYEVLTLLVK 374
Cdd:TIGR02085 321 LSQMAPKFILYSSCNAQTMAKDIAELSGYQIERVQLFDMFPHTSHYEVLTLLVR 374
|
|
| rumB |
PRK03522 |
23S rRNA (uracil(747)-C(5))-methyltransferase RlmC; |
61-375 |
0e+00 |
|
23S rRNA (uracil(747)-C(5))-methyltransferase RlmC;
Pssm-ID: 235128 [Multi-domain] Cd Length: 315 Bit Score: 675.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447072511 61 MVVSGSVEKPLLGMLHRDGTPEDLCDCPLYPASFAPVFAALKPFIARAGLTPYNVARKRGELKYILLTESQSDGGMMLRF 140
Cdd:PRK03522 1 MVVSGSVERPLLGILHRDGTPVDLCDCPLYPASFAPVFAALKPFIARAGLTPYNVARKRGELKYILLTESQSDGELMLRF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447072511 141 VLRSDTKLAQLRKALPWLHEQLPQLKVITVNIQPVHMAIMEGETEIYLTEQQALAERFNDVPLWIRPQSFFQTNPAVASQ 220
Cdd:PRK03522 81 VLRSETKLARLRRALPWLQAQLPQLKVISVNIQPVHMAILEGEEEIFLTEQQALPERFNGVPLFIRPQSFFQTNPAVAAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447072511 221 LYATARDWVRQLPVKHMWDLFCGVGGFGLHCATPDMQLTGIEIASEAIACAKQSAAELGLTRLQFQALDSTQFATAQGDV 300
Cdd:PRK03522 161 LYATARDWVRELPPRSMWDLFCGVGGFGLHCATPGMQLTGIEISAEAIACAKQSAAELGLTNVQFQALDSTQFATAQGEV 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447072511 301 PELVLVNPPRRGIGKPLCDYLSTMAPRFIIYSSCNAQTMAKDIRELPGFRIERVQLFDMFPHTAHYEVLTLLVKQ 375
Cdd:PRK03522 241 PDLVLVNPPRRGIGKELCDYLSQMAPRFILYSSCNAQTMAKDLAHLPGYRIERVQLFDMFPHTAHYEVLTLLVRQ 315
|
|
| TrmA |
COG2265 |
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ... |
3-373 |
1.28e-102 |
|
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: 307.87 E-value: 1.28e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447072511 3 CALYdaGRCRSCQWITQPIPQQLSAKTADLKNLL---ADFPVVEWcAPV--SGPEQGFRNKAKMVVSGSVEKPLLGMlHR 77
Cdd:COG2265 67 CPHF--GRCGGCQLQHLSYEAQLELKQRVVREALeriGGLPEVEV-EPIigSPEPWGYRNRARLSVRRTDGRLRLGF-YA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447072511 78 DGTPE--DLCDCPLYPASFAPVFAALKPFIARAGltpynvaRKRGELKYILLTEsqsdggmmlrfvlrsdtklaqlrkal 155
Cdd:COG2265 143 RGSHElvDIDECPLLDPALNALLPALRELLAELG-------ARRGELRHLVVRA-------------------------- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447072511 156 pwlheqlpqlkvitvniqpvhmaimegeteiyltEQQALAERFNDVPLWIRPQSFFQTNPAVASQLYATARDWVRQLPVK 235
Cdd:COG2265 190 ----------------------------------GRDYLTERLGGLTFRISPGSFFQVNPEQAEALYAAALEWLDLTGGE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447072511 236 HMWDLFCGVGGFGLHCATPDMQLTGIEIASEAIACAKQSAAELGLTRLQFQALDSTQFATAQ--GDVPELVLVNPPRRGI 313
Cdd:COG2265 236 RVLDLYCGVGTFALPLARRAKKVIGVEIVPEAVEDARENARLNGLKNVEFVAGDLEEVLPELlwGGRPDVVVLDPPRAGA 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447072511 314 GKPLCDYLSTMAPRFIIYSSCNAQTMAKDIRELP--GFRIERVQLFDMFPHTAHYEVLTLLV 373
Cdd:COG2265 316 GPEVLEALAALGPRRIVYVSCNPATLARDLALLVegGYRLEKVQPVDMFPHTHHVESVALLE 377
|
|
| rumA |
TIGR00479 |
23S rRNA (uracil-5-)-methyltransferase RumA; This protein family was first proposed to be RNA ... |
3-367 |
3.26e-52 |
|
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: 179.25 E-value: 3.26e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447072511 3 CALYDagRCRSCQWITQPIPQQLSAKTADLKNLLA-----DFPVVEWCAPVSGPEQGFRNKAKMVVSGSVEKPLLGMLHR 77
Cdd:TIGR00479 58 CPHFG--QCGGCQLQHLSYELQLRSKQQQVIALLErigkfVSEPIEDVPTIGDDPWGYRNKARLSLGRSPSGQLQAGFYQ 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447072511 78 DGTPE--DLCDCPLYPASFAPVFAALKPFIARAGLTPYNVARKRGELKYILLTESQSDGGMMLRFVLRSDtKLAQLRKAL 155
Cdd:TIGR00479 136 KGSHDivDVKQCPVQAPALNALLPKVRAILENFGASRYLEHKELGQARHGVLRIGRHTGELSSVDRTALE-RFPHKEELD 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447072511 156 PWLHEQLPQLKVITVNIQPVHMAIMEGETEIYLTEQQALAERFNDVPLWIRPQSFFQTNPAVASQLYATARDWVRQLPVK 235
Cdd:TIGR00479 215 LYLQPDSPDVKSICQNINPEKTNVIFGEETEVIAGEMPIYDKSGDLSFTFSARDFIQVNSGQNEKLVDRALEWLELQGEE 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447072511 236 HMWDLFCGVGGFGLHCATPDMQLTGIEIASEAIACAKQSAAELGLTRLQFQALDSTQFATAQ---GDVPELVLVNPPRRG 312
Cdd:TIGR00479 295 RVLDAYCGMGTFTLPLAKQAKSVVGVEGVPESVEKAQQNAELNGIANVTFYHGTLETVLPKQpwaGNGFDKVLLDPPRKG 374
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 447072511 313 IGKPLCDYLSTMAPRFIIYSSCNAQTMAKDIREL--PGFRIERVQLFDMFPHTAHYE 367
Cdd:TIGR00479 375 CAAGVLRTIIKLKPERIVYVSCNPATLARDLEALckAGYTIARVQPVDMFPHTGHVE 431
|
|
| rumA |
PRK13168 |
23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD; |
3-371 |
6.78e-25 |
|
23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD;
Pssm-ID: 237291 [Multi-domain] Cd Length: 443 Bit Score: 105.24 E-value: 6.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447072511 3 CALYdaGRCRSCQwiTQ--PIPQQLSAKTADLKNLLADFPVVE---WCAPVSGPEQGFRNKAKMVVSgSVEKP---LLGm 74
Cdd:PRK13168 80 CPHF--GVCGGCQ--LQhlSIDAQIASKQRALEDLLKHLAGVEpeeVLPPIAGPPWGYRRRARLSVR-YVPKKgqlLVG- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447072511 75 LHRDGTPE--DLCDCPLYPASFAPVFAALKPFIARagLTpynvARKRgeLKYILLTesQSDGGMMLrfVLR-----SDTK 147
Cdd:PRK13168 154 FREKNSSDivDIDQCPVLVPPLSALLPPLRALLSS--LS----AKRR--LGHVELA--QGDNGTAL--VLRhleplSEAD 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447072511 148 LAQLRK-ALpwlHEQLpQLKVitvniQPvhmaimEGETEIYLTEQQALAERF----NDVPLWIRPQSFFQTNPAVASQLY 222
Cdd:PRK13168 222 RAKLRAfAE---QHGL-QLYL-----QP------KGPDLVHLLGPADAQLSYylpeFGLRLAFSPRDFIQVNAQVNQKMV 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447072511 223 ATARDWVRQLPVKHMWDLFCGVGGFGLHCATPDMQLTGIEIASEAIACAKQSAAELGLTRLQFQALD-----STQFATAQ 297
Cdd:PRK13168 287 ARALEWLDPQPGDRVLDLFCGLGNFTLPLARQAAEVVGVEGVEAMVERARENARRNGLDNVTFYHANleedfTDQPWALG 366
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447072511 298 G-DvpeLVLVNPPRRG-IGkpLCDYLSTMAPRFIIYSSCNAQTMAKDIREL--PGFRIERVQLFDMFPHTAHYEVLTL 371
Cdd:PRK13168 367 GfD---KVLLDPPRAGaAE--VMQALAKLGPKRIVYVSCNPATLARDAGVLveAGYRLKRAGMLDMFPHTGHVESMAL 439
|
|
| tRNA_U5-meth_tr |
pfam05958 |
tRNA (Uracil-5-)-methyltransferase; This family consists of (Uracil-5-)-methyltransferases EC: ... |
209-374 |
1.17e-17 |
|
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: 83.26 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447072511 209 SFFQTNPAVASQLYATARDwVRQLPVKHMWDLFCGVGGFGLHCATPDMQLTGIEIASEAIACAKQSAAELGLTRLQFQAL 288
Cdd:pfam05958 178 SFTQPNAAVNIKMLEWACD-VTQGSKGDLLELYCGNGNFSLALARNFRKVLATEIAKPSVAAAQYNIAANNIDNVQIIRM 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447072511 289 DSTQFATAQGDVPEL---------------VLVNPPRRGIGKPLCDyLSTMAPRfIIYSSCNAQTMAKDIRELP-GFRIE 352
Cdd:pfam05958 257 SAEEFTQAMNGVREFnrlkgidlksyncstIFVDPPRAGLDPETLK-LVQAYPR-ILYISCNPETLCANLEQLSkTHRVE 334
|
170 180
....*....|....*....|..
gi 447072511 353 RVQLFDMFPHTAHYEVLTLLVK 374
Cdd:pfam05958 335 RFALFDQFPYTHHMECGVLLEK 356
|
|
| PRK05031 |
PRK05031 |
tRNA (uracil-5-)-methyltransferase; Validated |
209-374 |
5.25e-17 |
|
tRNA (uracil-5-)-methyltransferase; Validated
Pssm-ID: 235332 Cd Length: 362 Bit Score: 81.41 E-value: 5.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447072511 209 SFFQTNPAVASQLYATARDWVRQLPvKHMWDLFCGVGGFGLHCATPDMQLTGIEIASEAIACAKQSAAELGLTRLQF--- 285
Cdd:PRK05031 183 SFTQPNAAVNEKMLEWALDATKGSK-GDLLELYCGNGNFTLALARNFRRVLATEISKPSVAAAQYNIAANGIDNVQIirm 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447072511 286 ------QA--------------LDSTQFATaqgdvpelVLVNPPRRGIGKPLCDylstMAPRF--IIYSSCNAQTMAKDI 343
Cdd:PRK05031 262 saeeftQAmngvrefnrlkgidLKSYNFST--------IFVDPPRAGLDDETLK----LVQAYerILYISCNPETLCENL 329
|
170 180 190
....*....|....*....|....*....|..
gi 447072511 344 RELP-GFRIERVQLFDMFPHTAHYEVLTLLVK 374
Cdd:PRK05031 330 ETLSqTHKVERFALFDQFPYTHHMECGVLLEK 361
|
|
| TrmN6 |
COG4123 |
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ... |
227-309 |
1.19e-07 |
|
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: 52.07 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447072511 227 DWVRQLPVKHMWDLFCGVGGFGLHCA--TPDMQLTGIEIASEAIACAKQSAAELGLT-RLQFQALDSTQFATAQGDVP-E 302
Cdd:COG4123 31 AFAPVKKGGRVLDLGTGTGVIALMLAqrSPGARITGVEIQPEAAELARRNVALNGLEdRITVIHGDLKEFAAELPPGSfD 110
|
....*..
gi 447072511 303 LVLVNPP 309
Cdd:COG4123 111 LVVSNPP 117
|
|
| RsmC |
COG2813 |
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ... |
239-309 |
3.30e-05 |
|
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: 44.03 E-value: 3.30e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447072511 239 DLFCGVGGFGLHCAT--PDMQLTGIEIASEAIACAKQSAAELGLTRLQFQALDSTQfataqgDVPE----LVLVNPP 309
Cdd:COG2813 55 DLGCGYGVIGLALAKrnPEARVTLVDVNARAVELARANAAANGLENVEVLWSDGLS------GVPDgsfdLILSNPP 125
|
|
| Methyltransf_31 |
pfam13847 |
Methyltransferase domain; This family appears to have methyltransferase activity. |
239-299 |
4.83e-05 |
|
Methyltransferase domain; This family appears to have methyltransferase activity.
Pssm-ID: 463998 [Multi-domain] Cd Length: 150 Bit Score: 43.17 E-value: 4.83e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447072511 239 DLFCGVGGFGLHCAT---PDMQLTGIEIASEAIACAKQSAAELGLTRLQFQALDSTQFATAQGD 299
Cdd:pfam13847 9 DLGCGTGHLSFELAEelgPNAEVVGIDISEEAIEKARENAQKLGFDNVEFEQGDIEELPELLED 72
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
238-309 |
5.99e-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: 41.65 E-value: 5.99e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447072511 238 WDLFCGVGGFGLHCA-TPDMQLTGIEIASEAIACAKQSAAELGLTRLQFQALDSTQFATAQGDVPELVLVNPP 309
Cdd:cd02440 3 LDLGCGTGALALALAsGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPEADESFDVIISDPP 75
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
239-293 |
2.44e-04 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 41.83 E-value: 2.44e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 447072511 239 DLFCGVGGFGLHCA-TPDMQLTGIEIASEAIACAKQSAAELGLTRLQFQALDSTQF 293
Cdd:COG0500 32 DLGCGTGRNLLALAaRFGGRVIGIDLSPEAIALARARAAKAGLGNVEFLVADLAEL 87
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
223-289 |
5.07e-04 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 40.30 E-value: 5.07e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447072511 223 ATARDWVRQLPVK---HMWDLFCGVGGFGLHCA-TPDMQLTGIEIASEAIACAKQSAAELGLT-RLQFQALD 289
Cdd:COG2230 38 AKLDLILRKLGLKpgmRVLDIGCGWGGLALYLArRYGVRVTGVTLSPEQLEYARERAAEAGLAdRVEVRLAD 109
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
218-300 |
7.34e-04 |
|
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: 39.59 E-value: 7.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447072511 218 ASQLYATARDWVRQLPVK---HMWDLFCGVGGFGLHCATPDMQLTGIEIASEAIACAKQSAAELGLtRLQFQALDSTQ-- 292
Cdd:COG2226 4 VAARYDGREALLAALGLRpgaRVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGL-NVEFVVGDAEDlp 82
|
....*...
gi 447072511 293 FATAQGDV 300
Cdd:COG2226 83 FPDGSFDL 90
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
239-298 |
1.09e-03 |
|
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: 38.46 E-value: 1.09e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447072511 239 DLFCGVGGFGLHCATPDMQLTGIEIASEAIACAKQSAAELgltRLQFQALDSTQFATAQG 298
Cdd:COG2227 30 DVGCGTGRLALALARRGADVTGVDISPEALEIARERAAEL---NVDFVQGDLEDLPLEDG 86
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
239-298 |
1.81e-03 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 37.16 E-value: 1.81e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447072511 239 DLFCGVGGFGLHCAT-PDMQLTGIEIASEAIACAKQSAAELGLtRLQFQALDSTQFATAQG 298
Cdd:pfam13649 3 DLGCGTGRLTLALARrGGARVTGVDLSPEMLERARERAAEAGL-NVEFVQGDAEDLPFPDG 62
|
|
| |
