|
Name |
Accession |
Description |
Interval |
E-value |
| rumA |
PRK13168 |
23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD; |
1-253 |
8.93e-154 |
|
23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD;
Pssm-ID: 237291 [Multi-domain] Cd Length: 443 Bit Score: 435.35 E-value: 8.93e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940131713 1 MLKSFSKPQALGHVELFSG-VATAVLLRHTAPLAEADLALLQAFCSKHGAQLWLHGDG---ELQPASPGDTLGYRLEPWN 76
Cdd:PRK13168 185 LLSSLSAKRRLGHVELAQGdNGTALVLRHLEPLSEADRAKLRAFAEQHGLQLYLQPKGpdlVHLLGPADAQLSYYLPEFG 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940131713 77 LQLAWRPGDFIQVNAAVNTAMIEQALQWLAPAKDERVMDLFCGLGNFALPLAGLAKEVVAVEGVATMVERAAVNAMSNDL 156
Cdd:PRK13168 265 LRLAFSPRDFIQVNAQVNQKMVARALEWLDPQPGDRVLDLFCGLGNFTLPLARQAAEVVGVEGVEAMVERARENARRNGL 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940131713 157 HNVQFFQADLSQPLTHADWAAEGFSAVLLDPPRDGAFEVVRQIRKTGARRLLYVSCNPATLARDTVELISQGYRLKRAGI 236
Cdd:PRK13168 345 DNVTFYHANLEEDFTDQPWALGGFDKVLLDPPRAGAAEVMQALAKLGPKRIVYVSCNPATLARDAGVLVEAGYRLKRAGM 424
|
250
....*....|....*..
gi 940131713 237 LDMFPQTAHVEAMALFE 253
Cdd:PRK13168 425 LDMFPHTGHVESMALFE 441
|
|
| TrmA |
COG2265 |
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ... |
30-253 |
2.18e-85 |
|
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: 258.95 E-value: 2.18e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940131713 30 APLAEADLALLQAFCSKHGAQlwlhgDGELQP---ASPGDTLGYRLEpwNLQLAWRPGDFIQVNAAVNTAMIEQALQWLA 106
Cdd:COG2265 158 DPALNALLPALRELLAELGAR-----RGELRHlvvRAGRDYLTERLG--GLTFRISPGSFFQVNPEQAEALYAAALEWLD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940131713 107 PAKDERVMDLFCGLGNFALPLAGLAKEVVAVEGVATMVERAAVNAMSNDLHNVQFFQADLSQPLTHADWaAEGFSAVLLD 186
Cdd:COG2265 231 LTGGERVLDLYCGVGTFALPLARRAKKVIGVEIVPEAVEDARENARLNGLKNVEFVAGDLEEVLPELLW-GGRPDVVVLD 309
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 940131713 187 PPRDGA-FEVVRQIRKTGARRLLYVSCNPATLARDTVELISQGYRLKRAGILDMFPQTAHVEAMALFE 253
Cdd:COG2265 310 PPRAGAgPEVLEALAALGPRRIVYVSCNPATLARDLALLVEGGYRLEKVQPVDMFPHTHHVESVALLE 377
|
|
| rumA |
TIGR00479 |
23S rRNA (uracil-5-)-methyltransferase RumA; This protein family was first proposed to be RNA ... |
2-247 |
2.39e-64 |
|
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: 206.60 E-value: 2.39e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940131713 2 LKSFSKPQALGHVELfsGVA---TAVLLRHTAPLAEADLALLQAFCSKHGAQLWLHGD--------GELQPASPGDTLGY 70
Cdd:TIGR00479 165 LENFGASRYLEHKEL--GQArhgVLRIGRHTGELSSVDRTALERFPHKEELDLYLQPDspdvksicQNINPEKTNVIFGE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940131713 71 RLE------PW-----NLQLAWRPGDFIQVNAAVNTAMIEQALQWLAPAKDERVMDLFCGLGNFALPLAGLAKEVVAVEG 139
Cdd:TIGR00479 243 ETEviagemPIydksgDLSFTFSARDFIQVNSGQNEKLVDRALEWLELQGEERVLDAYCGMGTFTLPLAKQAKSVVGVEG 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940131713 140 VATMVERAAVNAMSNDLHNVQFFQADLSQPLTHADWAAEGFSAVLLDPPRDG-AFEVVRQIRKTGARRLLYVSCNPATLA 218
Cdd:TIGR00479 323 VPESVEKAQQNAELNGIANVTFYHGTLETVLPKQPWAGNGFDKVLLDPPRKGcAAGVLRTIIKLKPERIVYVSCNPATLA 402
|
250 260
....*....|....*....|....*....
gi 940131713 219 RDTVELISQGYRLKRAGILDMFPQTAHVE 247
Cdd:TIGR00479 403 RDLEALCKAGYTIARVQPVDMFPHTGHVE 431
|
|
| tRNA_U5-meth_tr |
pfam05958 |
tRNA (Uracil-5-)-methyltransferase; This family consists of (Uracil-5-)-methyltransferases EC: ... |
84-253 |
1.19e-26 |
|
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: 105.98 E-value: 1.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940131713 84 GDFIQVNAAVNTAMIEQALQWLAPAKDErVMDLFCGLGNFALPLAGLAKEVVAVEGVATMVERAAVNAMSNDLHNVQFFQ 163
Cdd:pfam05958 177 NSFTQPNAAVNIKMLEWACDVTQGSKGD-LLELYCGNGNFSLALARNFRKVLATEIAKPSVAAAQYNIAANNIDNVQIIR 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940131713 164 ---ADLSQPLTHA---------DWAAEGFSAVLLDPPRDGA-FEVVRQIRKTGarRLLYVSCNPATLARDTVELiSQGYR 230
Cdd:pfam05958 256 msaEEFTQAMNGVrefnrlkgiDLKSYNCSTIFVDPPRAGLdPETLKLVQAYP--RILYISCNPETLCANLEQL-SKTHR 332
|
170 180
....*....|....*....|...
gi 940131713 231 LKRAGILDMFPQTAHVEAMALFE 253
Cdd:pfam05958 333 VERFALFDQFPYTHHMECGVLLE 355
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
112-207 |
1.13e-10 |
|
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: 57.05 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940131713 112 RVMDLFCGLGNFALPLA-GLAKEVVAVEGVATMVERAAVNAMSNDLHNVQFFQADLSQPLTHADwaaEGFSAVLLDPPRD 190
Cdd:cd02440 1 RVLDLGCGTGALALALAsGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPEAD---ESFDVIISDPPLH 77
|
90
....*....|....*..
gi 940131713 191 GAFEVVRQIRKTGARRL 207
Cdd:cd02440 78 HLVEDLARFLEEARRLL 94
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| rumA |
PRK13168 |
23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD; |
1-253 |
8.93e-154 |
|
23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD;
Pssm-ID: 237291 [Multi-domain] Cd Length: 443 Bit Score: 435.35 E-value: 8.93e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940131713 1 MLKSFSKPQALGHVELFSG-VATAVLLRHTAPLAEADLALLQAFCSKHGAQLWLHGDG---ELQPASPGDTLGYRLEPWN 76
Cdd:PRK13168 185 LLSSLSAKRRLGHVELAQGdNGTALVLRHLEPLSEADRAKLRAFAEQHGLQLYLQPKGpdlVHLLGPADAQLSYYLPEFG 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940131713 77 LQLAWRPGDFIQVNAAVNTAMIEQALQWLAPAKDERVMDLFCGLGNFALPLAGLAKEVVAVEGVATMVERAAVNAMSNDL 156
Cdd:PRK13168 265 LRLAFSPRDFIQVNAQVNQKMVARALEWLDPQPGDRVLDLFCGLGNFTLPLARQAAEVVGVEGVEAMVERARENARRNGL 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940131713 157 HNVQFFQADLSQPLTHADWAAEGFSAVLLDPPRDGAFEVVRQIRKTGARRLLYVSCNPATLARDTVELISQGYRLKRAGI 236
Cdd:PRK13168 345 DNVTFYHANLEEDFTDQPWALGGFDKVLLDPPRAGAAEVMQALAKLGPKRIVYVSCNPATLARDAGVLVEAGYRLKRAGM 424
|
250
....*....|....*..
gi 940131713 237 LDMFPQTAHVEAMALFE 253
Cdd:PRK13168 425 LDMFPHTGHVESMALFE 441
|
|
| TrmA |
COG2265 |
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ... |
30-253 |
2.18e-85 |
|
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: 258.95 E-value: 2.18e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940131713 30 APLAEADLALLQAFCSKHGAQlwlhgDGELQP---ASPGDTLGYRLEpwNLQLAWRPGDFIQVNAAVNTAMIEQALQWLA 106
Cdd:COG2265 158 DPALNALLPALRELLAELGAR-----RGELRHlvvRAGRDYLTERLG--GLTFRISPGSFFQVNPEQAEALYAAALEWLD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940131713 107 PAKDERVMDLFCGLGNFALPLAGLAKEVVAVEGVATMVERAAVNAMSNDLHNVQFFQADLSQPLTHADWaAEGFSAVLLD 186
Cdd:COG2265 231 LTGGERVLDLYCGVGTFALPLARRAKKVIGVEIVPEAVEDARENARLNGLKNVEFVAGDLEEVLPELLW-GGRPDVVVLD 309
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 940131713 187 PPRDGA-FEVVRQIRKTGARRLLYVSCNPATLARDTVELISQGYRLKRAGILDMFPQTAHVEAMALFE 253
Cdd:COG2265 310 PPRAGAgPEVLEALAALGPRRIVYVSCNPATLARDLALLVEGGYRLEKVQPVDMFPHTHHVESVALLE 377
|
|
| rumA |
TIGR00479 |
23S rRNA (uracil-5-)-methyltransferase RumA; This protein family was first proposed to be RNA ... |
2-247 |
2.39e-64 |
|
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: 206.60 E-value: 2.39e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940131713 2 LKSFSKPQALGHVELfsGVA---TAVLLRHTAPLAEADLALLQAFCSKHGAQLWLHGD--------GELQPASPGDTLGY 70
Cdd:TIGR00479 165 LENFGASRYLEHKEL--GQArhgVLRIGRHTGELSSVDRTALERFPHKEELDLYLQPDspdvksicQNINPEKTNVIFGE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940131713 71 RLE------PW-----NLQLAWRPGDFIQVNAAVNTAMIEQALQWLAPAKDERVMDLFCGLGNFALPLAGLAKEVVAVEG 139
Cdd:TIGR00479 243 ETEviagemPIydksgDLSFTFSARDFIQVNSGQNEKLVDRALEWLELQGEERVLDAYCGMGTFTLPLAKQAKSVVGVEG 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940131713 140 VATMVERAAVNAMSNDLHNVQFFQADLSQPLTHADWAAEGFSAVLLDPPRDG-AFEVVRQIRKTGARRLLYVSCNPATLA 218
Cdd:TIGR00479 323 VPESVEKAQQNAELNGIANVTFYHGTLETVLPKQPWAGNGFDKVLLDPPRKGcAAGVLRTIIKLKPERIVYVSCNPATLA 402
|
250 260
....*....|....*....|....*....
gi 940131713 219 RDTVELISQGYRLKRAGILDMFPQTAHVE 247
Cdd:TIGR00479 403 RDLEALCKAGYTIARVQPVDMFPHTGHVE 431
|
|
| rumB |
PRK03522 |
23S rRNA (uracil(747)-C(5))-methyltransferase RlmC; |
82-253 |
2.40e-31 |
|
23S rRNA (uracil(747)-C(5))-methyltransferase RlmC;
Pssm-ID: 235128 [Multi-domain] Cd Length: 315 Bit Score: 117.66 E-value: 2.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940131713 82 RPGDFIQVNAAVNTAMIEQALQWLAPAKDERVMDLFCGLGNFALPLAGLAKEVVAVEGVATMVERAAVNAMSNDLHNVQF 161
Cdd:PRK03522 146 RPQSFFQTNPAVAAQLYATARDWVRELPPRSMWDLFCGVGGFGLHCATPGMQLTGIEISAEAIACAKQSAAELGLTNVQF 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940131713 162 FQADLSQPLTHADWAAEgfsAVLLDPPRDG-AFEVVRQIRKTGARRLLYVSCNPATLARDTVELisQGYRLKRAGILDMF 240
Cdd:PRK03522 226 QALDSTQFATAQGEVPD---LVLVNPPRRGiGKELCDYLSQMAPRFILYSSCNAQTMAKDLAHL--PGYRIERVQLFDMF 300
|
170
....*....|...
gi 940131713 241 PQTAHVEAMALFE 253
Cdd:PRK03522 301 PHTAHYEVLTLLV 313
|
|
| PRK05031 |
PRK05031 |
tRNA (uracil-5-)-methyltransferase; Validated |
86-248 |
1.38e-28 |
|
tRNA (uracil-5-)-methyltransferase; Validated
Pssm-ID: 235332 Cd Length: 362 Bit Score: 111.07 E-value: 1.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940131713 86 FIQVNAAVNTAMIEQALQWLAPAKDErVMDLFCGLGNFALPLAGLAKEVVAVEGVATMVERAAVNAMSNDLHNVQFFQ-- 163
Cdd:PRK05031 184 FTQPNAAVNEKMLEWALDATKGSKGD-LLELYCGNGNFTLALARNFRRVLATEISKPSVAAAQYNIAANGIDNVQIIRms 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940131713 164 -ADLSQPLT---------HADWAAEGFSAVLLDPPRDGA-FEVVRQIRktGARRLLYVSCNPATLARDtVELISQGYRLK 232
Cdd:PRK05031 263 aEEFTQAMNgvrefnrlkGIDLKSYNFSTIFVDPPRAGLdDETLKLVQ--AYERILYISCNPETLCEN-LETLSQTHKVE 339
|
170
....*....|....*.
gi 940131713 233 RAGILDMFPQTAHVEA 248
Cdd:PRK05031 340 RFALFDQFPYTHHMEC 355
|
|
| tRNA_U5-meth_tr |
pfam05958 |
tRNA (Uracil-5-)-methyltransferase; This family consists of (Uracil-5-)-methyltransferases EC: ... |
84-253 |
1.19e-26 |
|
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: 105.98 E-value: 1.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940131713 84 GDFIQVNAAVNTAMIEQALQWLAPAKDErVMDLFCGLGNFALPLAGLAKEVVAVEGVATMVERAAVNAMSNDLHNVQFFQ 163
Cdd:pfam05958 177 NSFTQPNAAVNIKMLEWACDVTQGSKGD-LLELYCGNGNFSLALARNFRKVLATEIAKPSVAAAQYNIAANNIDNVQIIR 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940131713 164 ---ADLSQPLTHA---------DWAAEGFSAVLLDPPRDGA-FEVVRQIRKTGarRLLYVSCNPATLARDTVELiSQGYR 230
Cdd:pfam05958 256 msaEEFTQAMNGVrefnrlkgiDLKSYNCSTIFVDPPRAGLdPETLKLVQAYP--RILYISCNPETLCANLEQL-SKTHR 332
|
170 180
....*....|....*....|...
gi 940131713 231 LKRAGILDMFPQTAHVEAMALFE 253
Cdd:pfam05958 333 VERFALFDQFPYTHHMECGVLLE 355
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
112-207 |
1.13e-10 |
|
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: 57.05 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940131713 112 RVMDLFCGLGNFALPLA-GLAKEVVAVEGVATMVERAAVNAMSNDLHNVQFFQADLSQPLTHADwaaEGFSAVLLDPPRD 190
Cdd:cd02440 1 RVLDLGCGTGALALALAsGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPEAD---ESFDVIISDPPLH 77
|
90
....*....|....*..
gi 940131713 191 GAFEVVRQIRKTGARRL 207
Cdd:cd02440 78 HLVEDLARFLEEARRLL 94
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
99-185 |
7.52e-09 |
|
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: 53.07 E-value: 7.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940131713 99 EQALQWLAPAKDERVMDLFCGLGNFALPLAGLAKEVVAVEGVATMVERAAVNAMSNDLhNVQFFQADlsqpLTHADWAAE 178
Cdd:COG2226 12 EALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGL-NVEFVVGD----AEDLPFPDG 86
|
....*..
gi 940131713 179 GFSAVLL 185
Cdd:COG2226 87 SFDLVIS 93
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
109-241 |
5.41e-07 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 48.76 E-value: 5.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940131713 109 KDERVMDLFCGLGNFALPLAGLAKE-VVAVEGVATMVERAAVNAMSNDLHNVQFFQADLSQPLthaDWAAEGFSAVL--- 184
Cdd:COG0500 26 KGGRVLDLGCGTGRNLLALAARFGGrVIGIDLSPEAIALARARAAKAGLGNVEFLVADLAELD---PLPAESFDLVVafg 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 940131713 185 ----LDP-PRDGAFEVVRQIRKTGARrlLYVSCNPATLARDTVELISQGYRLKRAGILDMFP 241
Cdd:COG0500 103 vlhhLPPeEREALLRELARALKPGGV--LLLSASDAAAALSLARLLLLATASLLELLLLLRL 162
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
94-185 |
1.04e-06 |
|
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: 46.55 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940131713 94 NTAMIEQALQWLAPAKdeRVMDLFCGLGNFALPLAGLAKEVVAVEGVATMVERAAVNAmsnDLHNVQFFQADlsqpLTHA 173
Cdd:COG2227 11 DRRLAALLARLLPAGG--RVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERA---AELNVDFVQGD----LEDL 81
|
90
....*....|..
gi 940131713 174 DWAAEGFSAVLL 185
Cdd:COG2227 82 PLEDGSFDLVIC 93
|
|
| Pcm |
COG2518 |
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ... |
102-185 |
1.22e-06 |
|
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442008 [Multi-domain] Cd Length: 197 Bit Score: 47.78 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940131713 102 LQWLAPAKDERVMDLFCGLG-NFALpLAGLAKEVVAVEGVATMVERAAVNAMSNDLHNVQFFQADLSQPlthadWAAEG- 179
Cdd:COG2518 59 LEALDLKPGDRVLEIGTGSGyQAAV-LARLAGRVYSVERDPELAERARERLAALGYDNVTVRVGDGALG-----WPEHAp 132
|
....*.
gi 940131713 180 FSAVLL 185
Cdd:COG2518 133 FDRIIV 138
|
|
| COG4976 |
COG4976 |
Predicted methyltransferase, contains TPR repeat [General function prediction only]; |
97-181 |
1.93e-06 |
|
Predicted methyltransferase, contains TPR repeat [General function prediction only];
Pssm-ID: 444001 [Multi-domain] Cd Length: 181 Bit Score: 46.92 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940131713 97 MIEQALQWLAPAKDERVMDLFCGLGNFALPLAGLAKEVVAVEGVATMVERAAVNAMSNDLHNVQFfqADLSQPLTHAD-- 174
Cdd:COG4976 34 LAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAREKGVYDRLLVADL--ADLAEPDGRFDli 111
|
....*..
gi 940131713 175 WAAEGFS 181
Cdd:COG4976 112 VAADVLT 118
|
|
| Methyltransf_31 |
pfam13847 |
Methyltransferase domain; This family appears to have methyltransferase activity. |
109-165 |
5.67e-06 |
|
Methyltransferase domain; This family appears to have methyltransferase activity.
Pssm-ID: 463998 [Multi-domain] Cd Length: 150 Bit Score: 45.10 E-value: 5.67e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 940131713 109 KDERVMDLFCGLGNFALPLAGLA---KEVVAVEGVATMVERAAVNAMSNDLHNVQFFQAD 165
Cdd:pfam13847 3 KGMRVLDLGCGTGHLSFELAEELgpnAEVVGIDISEEAIEKARENAQKLGFDNVEFEQGD 62
|
|
| PRK07580 |
PRK07580 |
Mg-protoporphyrin IX methyl transferase; Validated |
97-168 |
7.30e-06 |
|
Mg-protoporphyrin IX methyl transferase; Validated
Pssm-ID: 236059 [Multi-domain] Cd Length: 230 Bit Score: 45.60 E-value: 7.30e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 940131713 97 MIEQALQWLaPA----KDERVMDLFCGLGNFALPLAGLAKEVVAVEGVATMVERAAVNA-MSNDLHNVQFFQADLSQ 168
Cdd:PRK07580 48 MRDTVLSWL-PAdgdlTGLRILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEARERApEAGLAGNITFEVGDLES 123
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
113-184 |
1.04e-05 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 42.94 E-value: 1.04e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 940131713 113 VMDLFCGLGNFALPLAGLAK-EVVAVEGVATMVERAAVNAMSNDLhNVQFFQADlsqpLTHADWAAEGFSAVL 184
Cdd:pfam13649 1 VLDLGCGTGRLTLALARRGGaRVTGVDLSPEMLERARERAAEAGL-NVEFVQGD----AEDLPFPDGSFDLVV 68
|
|
| PRK08317 |
PRK08317 |
hypothetical protein; Provisional |
99-203 |
1.17e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 181382 [Multi-domain] Cd Length: 241 Bit Score: 45.31 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940131713 99 EQALQWLAPAKDERVMDLFCGLGNFALPLAGL---AKEVVAVEGVATMVERAAvNAMSNDLHNVQFFQADlsqpLTHADW 175
Cdd:PRK08317 9 ARTFELLAVQPGDRVLDVGCGPGNDARELARRvgpEGRVVGIDRSEAMLALAK-ERAAGLGPNVEFVRGD----ADGLPF 83
|
90 100 110
....*....|....*....|....*....|....*.
gi 940131713 176 AAEGFSAV--------LLDPPRdGAFEVVRQIRKTG 203
Cdd:PRK08317 84 PDGSFDAVrsdrvlqhLEDPAR-ALAEIARVLRPGG 118
|
|
| Trm5 |
COG2520 |
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 ... |
110-165 |
2.41e-05 |
|
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 N-methylase Trm5 is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 442010 [Multi-domain] Cd Length: 333 Bit Score: 44.85 E-value: 2.41e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 940131713 110 DERVMDLFCGLGNFALPLAGL-AKEVVAVE----GVATMVEraavNAMSNDL-HNVQFFQAD 165
Cdd:COG2520 181 GERVLDMFAGVGPFSIPIAKRsGAKVVAIDinpdAVEYLKE----NIRLNKVeDRVTPILGD 238
|
|
| MTS |
pfam05175 |
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ... |
102-207 |
1.13e-04 |
|
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: 41.42 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940131713 102 LQWLAPAKDERVMDLFCGLGNFALPLAGLAK--EVVAVEGVATMVERAAVNAMSNDLHNVQFFQADLsqpltHADWAAEG 179
Cdd:pfam05175 24 LEHLPKDLSGKVLDLGCGAGVLGAALAKESPdaELTMVDINARALESARENLAANGLENGEVVASDV-----YSGVEDGK 98
|
90 100 110
....*....|....*....|....*....|..
gi 940131713 180 FSAVLLDPP----RDGAFEVVRQIRKTGARRL 207
Cdd:pfam05175 99 FDLIISNPPfhagLATTYNVAQRFIADAKRHL 130
|
|
| PRK14968 |
PRK14968 |
putative methyltransferase; Provisional |
109-188 |
3.25e-04 |
|
putative methyltransferase; Provisional
Pssm-ID: 237872 [Multi-domain] Cd Length: 188 Bit Score: 40.65 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940131713 109 KDERVMDLFCGLGNFALPLAGLAKEVVAVEGVATMVERAAVNAMSNDLHN--VQFFQADLSQPLthadwAAEGFSAVLLD 186
Cdd:PRK14968 23 KGDRVLEVGTGSGIVAIVAAKNGKKVVGVDINPYAVECAKCNAKLNNIRNngVEVIRSDLFEPF-----RGDKFDVILFN 97
|
..
gi 940131713 187 PP 188
Cdd:PRK14968 98 PP 99
|
|
| Trm11 |
COG1041 |
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ... |
91-188 |
1.20e-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: 38.78 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940131713 91 AAVNTAMIEqalqwlapaKDERVMDLFCGLGNFALPLAGLAKEVVAVEGVATMVERAAVNAMSNDLHNVQFFQADlsqpL 170
Cdd:COG1041 17 ALVNLAGAK---------EGDTVLDPFCGTGTILIEAGLLGRRVIGSDIDPKMVEGARENLEHYGYEDADVIRGD----A 83
|
90
....*....|....*...
gi 940131713 171 THADWAAEGFSAVLLDPP 188
Cdd:COG1041 84 RDLPLADESVDAIVTDPP 101
|
|
| PRK15128 |
PRK15128 |
23S rRNA (cytosine(1962)-C(5))-methyltransferase RlmI; |
108-189 |
4.94e-03 |
|
23S rRNA (cytosine(1962)-C(5))-methyltransferase RlmI;
Pssm-ID: 185082 [Multi-domain] Cd Length: 396 Bit Score: 37.89 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940131713 108 AKDERVMDLFCGLGNFALP-LAGLAKEVVAVEGVATMVERAAVNAMSN--DLHNVQFFQADLSQPLTHADWAAEGFSAVL 184
Cdd:PRK15128 219 VENKRVLNCFSYTGGFAVSaLMGGCSQVVSVDTSQEALDIARQNVELNklDLSKAEFVRDDVFKLLRTYRDRGEKFDVIV 298
|
....*
gi 940131713 185 LDPPR 189
Cdd:PRK15128 299 MDPPK 303
|
|
| Methyltransf_23 |
pfam13489 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
98-174 |
9.65e-03 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 404385 [Multi-domain] Cd Length: 162 Bit Score: 35.87 E-value: 9.65e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 940131713 98 IEQALQWLAPAKDE--RVMDLFCGLGNFALPLAGLAKEVVAVEGVATMVERAAVNAmsndlHNVQFFQADLSQPLTHAD 174
Cdd:pfam13489 9 LADLLLRLLPKLPSpgRVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERALLNV-----RFDQFDEQEAAVPAGKFD 82
|
|
| |
