|
Name |
Accession |
Description |
Interval |
E-value |
| TrmA |
COG2265 |
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ... |
245-447 |
3.74e-58 |
|
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: 195.39 E-value: 3.74e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011295 245 GEPHIFEDLLGLKIRISPDAFFQINTAGAEMLYRIIGELSGVNSESLLLDICCGTGVIGLSVAQRASQVHGIELVEQAVE 324
Cdd:COG2265 190 GRDYLTERLGGLTFRISPGSFFQVNPEQAEALYAAALEWLDLTGGERVLDLYCGVGTFALPLARRAKKVIGVEIVPEAVE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011295 325 DARWTAAFNGVTNCEFHAGRAETILPQLLksqKDEKLTVAVVNPARAGLHYRVVRAIRNCRtIHTLVFVSCKPhgeST-- 402
Cdd:COG2265 270 DARENARLNGLKNVEFVAGDLEEVLPELL---WGGRPDVVVLDPPRAGAGPEVLEALAALG-PRRIVYVSCNP---ATla 342
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 569011295 403 RNfielccppnsAKQLLGDPFVLREAVPVDLFPHTPHCELVLLFT 447
Cdd:COG2265 343 RD----------LALLVEGGYRLEKVQPVDMFPHTHHVESVALLE 377
|
|
| rumA |
TIGR00479 |
23S rRNA (uracil-5-)-methyltransferase RumA; This protein family was first proposed to be RNA ... |
95-441 |
1.90e-33 |
|
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: 130.33 E-value: 1.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011295 95 GYRNKSTFSVYRSPDGNPKTVGYYLGTWKDGNVVCLPCNH---------LKNIPEKHSQVAQYYEVflrqssvepcllfh 165
Cdd:TIGR00479 112 GYRNKARLSLGRSPSGQLQAGFYQKGSHDIVDVKQCPVQApalnallpkVRAILENFGASRYLEHK-------------- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011295 166 EGGHWRELVVRTNRQGHTMAIV--TFHpQGLSEEEVCVQKVTlKDFftKGPGAIC-----ELTSLYFQESTMTrcshqqs 238
Cdd:TIGR00479 178 ELGQARHGVLRIGRHTGELSSVdrTAL-ERFPHKEELDLYLQ-PDS--PDVKSICqninpEKTNVIFGEETEV------- 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011295 239 pyqlLFGEPHIFEDLLGLKIRISPDAFFQINTAGAEMLYRIIGELSGVNSESLLLDICCGTGVIGLSVAQRASQVHGIEL 318
Cdd:TIGR00479 247 ----IAGEMPIYDKSGDLSFTFSARDFIQVNSGQNEKLVDRALEWLELQGEERVLDAYCGMGTFTLPLAKQAKSVVGVEG 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011295 319 VEQAVEDARWTAAFNGVTNCEFHAGRAETILPQLlkSQKDEKLTVAVVNPARAGLHYRVVRAIRNCRTIHtLVFVSCKPh 398
Cdd:TIGR00479 323 VPESVEKAQQNAELNGIANVTFYHGTLETVLPKQ--PWAGNGFDKVLLDPPRKGCAAGVLRTIIKLKPER-IVYVSCNP- 398
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 569011295 399 GESTRNfielccppnsAKQLLGDPFVLREAVPVDLFPHTPHCE 441
Cdd:TIGR00479 399 ATLARD----------LEALCKAGYTIARVQPVDMFPHTGHVE 431
|
|
| rumB |
PRK03522 |
23S rRNA (uracil(747)-C(5))-methyltransferase RlmC; |
245-445 |
6.18e-17 |
|
23S rRNA (uracil(747)-C(5))-methyltransferase RlmC;
Pssm-ID: 235128 [Multi-domain] Cd Length: 315 Bit Score: 81.07 E-value: 6.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011295 245 GEPHIF--------EDLLGLKIRISPDAFFQINTAGAEMLYRI----IGELsGVNSeslLLDICCGTGVIGLSVAQRASQ 312
Cdd:PRK03522 122 GEEEIFlteqqalpERFNGVPLFIRPQSFFQTNPAVAAQLYATardwVREL-PPRS---MWDLFCGVGGFGLHCATPGMQ 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011295 313 VHGIELVEQAVEDARWTAAFNGVTNCEFHAGRAETILpqllkSQKDEKLTVAVVNPARAGLHYRVVRAIrNCRTIHTLVF 392
Cdd:PRK03522 198 LTGIEISAEAIACAKQSAAELGLTNVQFQALDSTQFA-----TAQGEVPDLVLVNPPRRGIGKELCDYL-SQMAPRFILY 271
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 569011295 393 VSCKPHgestrnfielccppNSAKQLLGDP-FVLREAVPVDLFPHTPHCE-LVLL 445
Cdd:PRK03522 272 SSCNAQ--------------TMAKDLAHLPgYRIERVQLFDMFPHTAHYEvLTLL 312
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
293-385 |
1.81e-08 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 51.80 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011295 293 LDICCGTGVIGLSVAQRA-SQVHGIELVEQAVEDARWTAAFNGVtNCEFHAGRAETIlpqllkSQKDEKLTVAVvnpARA 371
Cdd:pfam13649 2 LDLGCGTGRLTLALARRGgARVTGVDLSPEMLERARERAAEAGL-NVEFVQGDAEDL------PFPDGSFDLVV---SSG 71
|
90
....*....|....*...
gi 569011295 372 GLHY----RVVRAIRNCR 385
Cdd:pfam13649 72 VLHHlpdpDLEAALREIA 89
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
292-385 |
1.95e-08 |
|
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: 52.05 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011295 292 LLDICCGTGVIGLSVAQR-ASQVHGIELVEQAVEDARWTAAFNGVTNCEFHAGRAETILPqllksQKDEKLTVAVVNPAR 370
Cdd:cd02440 2 VLDLGCGTGALALALASGpGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPP-----EADESFDVIISDPPL 76
|
90
....*....|....*
gi 569011295 371 AGLHYRVVRAIRNCR 385
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 ... |
245-447 |
3.74e-58 |
|
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: 195.39 E-value: 3.74e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011295 245 GEPHIFEDLLGLKIRISPDAFFQINTAGAEMLYRIIGELSGVNSESLLLDICCGTGVIGLSVAQRASQVHGIELVEQAVE 324
Cdd:COG2265 190 GRDYLTERLGGLTFRISPGSFFQVNPEQAEALYAAALEWLDLTGGERVLDLYCGVGTFALPLARRAKKVIGVEIVPEAVE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011295 325 DARWTAAFNGVTNCEFHAGRAETILPQLLksqKDEKLTVAVVNPARAGLHYRVVRAIRNCRtIHTLVFVSCKPhgeST-- 402
Cdd:COG2265 270 DARENARLNGLKNVEFVAGDLEEVLPELL---WGGRPDVVVLDPPRAGAGPEVLEALAALG-PRRIVYVSCNP---ATla 342
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 569011295 403 RNfielccppnsAKQLLGDPFVLREAVPVDLFPHTPHCELVLLFT 447
Cdd:COG2265 343 RD----------LALLVEGGYRLEKVQPVDMFPHTHHVESVALLE 377
|
|
| rumA |
TIGR00479 |
23S rRNA (uracil-5-)-methyltransferase RumA; This protein family was first proposed to be RNA ... |
95-441 |
1.90e-33 |
|
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: 130.33 E-value: 1.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011295 95 GYRNKSTFSVYRSPDGNPKTVGYYLGTWKDGNVVCLPCNH---------LKNIPEKHSQVAQYYEVflrqssvepcllfh 165
Cdd:TIGR00479 112 GYRNKARLSLGRSPSGQLQAGFYQKGSHDIVDVKQCPVQApalnallpkVRAILENFGASRYLEHK-------------- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011295 166 EGGHWRELVVRTNRQGHTMAIV--TFHpQGLSEEEVCVQKVTlKDFftKGPGAIC-----ELTSLYFQESTMTrcshqqs 238
Cdd:TIGR00479 178 ELGQARHGVLRIGRHTGELSSVdrTAL-ERFPHKEELDLYLQ-PDS--PDVKSICqninpEKTNVIFGEETEV------- 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011295 239 pyqlLFGEPHIFEDLLGLKIRISPDAFFQINTAGAEMLYRIIGELSGVNSESLLLDICCGTGVIGLSVAQRASQVHGIEL 318
Cdd:TIGR00479 247 ----IAGEMPIYDKSGDLSFTFSARDFIQVNSGQNEKLVDRALEWLELQGEERVLDAYCGMGTFTLPLAKQAKSVVGVEG 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011295 319 VEQAVEDARWTAAFNGVTNCEFHAGRAETILPQLlkSQKDEKLTVAVVNPARAGLHYRVVRAIRNCRTIHtLVFVSCKPh 398
Cdd:TIGR00479 323 VPESVEKAQQNAELNGIANVTFYHGTLETVLPKQ--PWAGNGFDKVLLDPPRKGCAAGVLRTIIKLKPER-IVYVSCNP- 398
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 569011295 399 GESTRNfielccppnsAKQLLGDPFVLREAVPVDLFPHTPHCE 441
Cdd:TIGR00479 399 ATLARD----------LEALCKAGYTIARVQPVDMFPHTGHVE 431
|
|
| rumB |
PRK03522 |
23S rRNA (uracil(747)-C(5))-methyltransferase RlmC; |
245-445 |
6.18e-17 |
|
23S rRNA (uracil(747)-C(5))-methyltransferase RlmC;
Pssm-ID: 235128 [Multi-domain] Cd Length: 315 Bit Score: 81.07 E-value: 6.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011295 245 GEPHIF--------EDLLGLKIRISPDAFFQINTAGAEMLYRI----IGELsGVNSeslLLDICCGTGVIGLSVAQRASQ 312
Cdd:PRK03522 122 GEEEIFlteqqalpERFNGVPLFIRPQSFFQTNPAVAAQLYATardwVREL-PPRS---MWDLFCGVGGFGLHCATPGMQ 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011295 313 VHGIELVEQAVEDARWTAAFNGVTNCEFHAGRAETILpqllkSQKDEKLTVAVVNPARAGLHYRVVRAIrNCRTIHTLVF 392
Cdd:PRK03522 198 LTGIEISAEAIACAKQSAAELGLTNVQFQALDSTQFA-----TAQGEVPDLVLVNPPRRGIGKELCDYL-SQMAPRFILY 271
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 569011295 393 VSCKPHgestrnfielccppNSAKQLLGDP-FVLREAVPVDLFPHTPHCE-LVLL 445
Cdd:PRK03522 272 SSCNAQ--------------TMAKDLAHLPgYRIERVQLFDMFPHTAHYEvLTLL 312
|
|
| RsmC |
COG2813 |
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ... |
292-381 |
9.08e-12 |
|
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: 63.67 E-value: 9.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011295 292 LLDICCGTGVIGLSVAQRA--SQVHGIELVEQAVEDARWTAAFNGVTNCEFHAgraetilPQLLKSQKDEKLTVAVVN-P 368
Cdd:COG2813 53 VLDLGCGYGVIGLALAKRNpeARVTLVDVNARAVELARANAAANGLENVEVLW-------SDGLSGVPDGSFDLILSNpP 125
|
90
....*....|....*
gi 569011295 369 ARAGL--HYRVVRAI 381
Cdd:COG2813 126 FHAGRavDKEVAHAL 140
|
|
| TrmN6 |
COG4123 |
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ... |
292-368 |
1.09e-09 |
|
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: 58.62 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011295 292 LLDICCGTGVIGLSVAQR--ASQVHGIELVEQAVEDARWTAAFNGVTN-CEFHAGRaetiLPQLLKSQKDEKLTVAVVNP 368
Cdd:COG4123 41 VLDLGTGTGVIALMLAQRspGARITGVEIQPEAAELARRNVALNGLEDrITVIHGD----LKEFAAELPPGSFDLVVSNP 116
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
293-385 |
1.81e-08 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 51.80 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011295 293 LDICCGTGVIGLSVAQRA-SQVHGIELVEQAVEDARWTAAFNGVtNCEFHAGRAETIlpqllkSQKDEKLTVAVvnpARA 371
Cdd:pfam13649 2 LDLGCGTGRLTLALARRGgARVTGVDLSPEMLERARERAAEAGL-NVEFVQGDAEDL------PFPDGSFDLVV---SSG 71
|
90
....*....|....*...
gi 569011295 372 GLHY----RVVRAIRNCR 385
Cdd:pfam13649 72 VLHHlpdpDLEAALREIA 89
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
292-385 |
1.95e-08 |
|
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: 52.05 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011295 292 LLDICCGTGVIGLSVAQR-ASQVHGIELVEQAVEDARWTAAFNGVTNCEFHAGRAETILPqllksQKDEKLTVAVVNPAR 370
Cdd:cd02440 2 VLDLGCGTGALALALASGpGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPP-----EADESFDVIISDPPL 76
|
90
....*....|....*
gi 569011295 371 AGLHYRVVRAIRNCR 385
Cdd:cd02440 77 HHLVEDLARFLEEAR 91
|
|
| MTS |
pfam05175 |
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ... |
293-381 |
2.53e-08 |
|
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: 53.36 E-value: 2.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011295 293 LDICCGTGVIGLSVAQRASQVHgIELVE---QAVEDARWTAAFNGVTNCEFHAGraetilpQLLKSQKDEKLTVAVVNPA 369
Cdd:pfam05175 36 LDLGCGAGVLGAALAKESPDAE-LTMVDinaRALESARENLAANGLENGEVVAS-------DVYSGVEDGKFDLIISNPP 107
|
90
....*....|....*
gi 569011295 370 -RAGLH--YRVVRAI 381
Cdd:pfam05175 108 fHAGLAttYNVAQRF 122
|
|
| Methyltransf_31 |
pfam13847 |
Methyltransferase domain; This family appears to have methyltransferase activity. |
292-357 |
2.62e-08 |
|
Methyltransferase domain; This family appears to have methyltransferase activity.
Pssm-ID: 463998 [Multi-domain] Cd Length: 150 Bit Score: 52.80 E-value: 2.62e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569011295 292 LLDICCGTGVIGLSVAQRA---SQVHGIELVEQAVEDARWTAAFNGVTNCEFHAGRAETiLPQLLKSQK 357
Cdd:pfam13847 7 VLDLGCGTGHLSFELAEELgpnAEVVGIDISEEAIEKARENAQKLGFDNVEFEQGDIEE-LPELLEDDK 74
|
|
| tRNA_U5-meth_tr |
pfam05958 |
tRNA (Uracil-5-)-methyltransferase; This family consists of (Uracil-5-)-methyltransferases EC: ... |
263-448 |
1.35e-07 |
|
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: 53.21 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011295 263 DAFFQINTAGAE-ML---YRIIGelsgvNSESLLLDICCGTGVIGLSVAQRASQVHGIELVEQAVEDARWTAAFNGVTNC 338
Cdd:pfam05958 177 NSFTQPNAAVNIkMLewaCDVTQ-----GSKGDLLELYCGNGNFSLALARNFRKVLATEIAKPSVAAAQYNIAANNIDNV 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011295 339 EFHAGRAETiLPQLLKSQ-----------KDEKLTVAVVNPARAGLHYRVVRAIRNCRTIhtlVFVSCKPHgestrnfiE 407
Cdd:pfam05958 252 QIIRMSAEE-FTQAMNGVrefnrlkgidlKSYNCSTIFVDPPRAGLDPETLKLVQAYPRI---LYISCNPE--------T 319
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 569011295 408 LCcppNSAKQLLGDPFVLREAVpVDLFPHTPHCELVLLFTR 448
Cdd:pfam05958 320 LC---ANLEQLSKTHRVERFAL-FDQFPYTHHMECGVLLEK 356
|
|
| PRK09328 |
PRK09328 |
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional |
293-368 |
6.58e-07 |
|
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
Pssm-ID: 236467 [Multi-domain] Cd Length: 275 Bit Score: 50.55 E-value: 6.58e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569011295 293 LDICCGTGVIGLSVAQR--ASQVHGIELVEQAVEDARWTAAFNGVTNCEFHAGRaetilpqLLKSQKDEKLTVAVVNP 368
Cdd:PRK09328 113 LDLGTGSGAIALALAKErpDAEVTAVDISPEALAVARRNAKHGLGARVEFLQGD-------WFEPLPGGRFDLIVSNP 183
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
292-348 |
1.19e-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: 47.68 E-value: 1.19e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 569011295 292 LLDICCGTGVIGLSVAQRASQVHGIELVEQAVEDARWTAAFNGVtNCEFHAGRAETI 348
Cdd:COG2226 26 VLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGL-NVEFVVGDAEDL 81
|
|
| HemK |
COG2890 |
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ... |
239-343 |
1.57e-06 |
|
Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];
Pssm-ID: 442135 [Multi-domain] Cd Length: 282 Bit Score: 49.38 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011295 239 PYQLLFGEphifEDLLGLKIRISPDAFfqI---NTAgaEMLYRIIGELSGvNSESLLLDICCGTGVIGLSVAQR--ASQV 313
Cdd:COG2890 69 PLAYILGE----AEFYGLEFKVDPGVL--IprpETE--ELVELALALLPA-GAPPRVLDLGTGSGAIALALAKErpDARV 139
|
90 100 110
....*....|....*....|....*....|.
gi 569011295 314 HGIELVEQAVEDARWTAAFNGVTN-CEFHAG 343
Cdd:COG2890 140 TAVDISPDALAVARRNAERLGLEDrVRFLQG 170
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
293-350 |
9.33e-06 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 46.45 E-value: 9.33e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 569011295 293 LDICCGTGVIGLSVAQRA-SQVHGIELVEQAVEDARWTAAFNGVTNCEFHAGRAETILP 350
Cdd:COG0500 31 LDLGCGTGRNLLALAARFgGRVIGIDLSPEAIALARARAAKAGLGNVEFLVADLAELDP 89
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
292-348 |
1.19e-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: 44.62 E-value: 1.19e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 569011295 292 LLDICCGTGVIGLSVAQRASQVHGIELVEQAVEDARWTAAFNGVtncEFHAGRAETI 348
Cdd:COG2227 28 VLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAELNV---DFVQGDLEDL 81
|
|
| PRK05031 |
PRK05031 |
tRNA (uracil-5-)-methyltransferase; Validated |
263-445 |
5.99e-05 |
|
tRNA (uracil-5-)-methyltransferase; Validated
Pssm-ID: 235332 Cd Length: 362 Bit Score: 44.82 E-value: 5.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011295 263 DAFFQINTAGAE-MLYRIIGELSgvNSESLLLDICCGTGVIGLSVAQRASQVHGIELVEQAVEDARWTAAFNGVTNCEFH 341
Cdd:PRK05031 182 NSFTQPNAAVNEkMLEWALDATK--GSKGDLLELYCGNGNFTLALARNFRRVLATEISKPSVAAAQYNIAANGIDNVQII 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011295 342 AGRAETiLPQLLKSQ------KDEKL------TVaVVNPARAGLHYRVVRAIRNCRTIhtlVFVSCKPHgesT--RNFIE 407
Cdd:PRK05031 260 RMSAEE-FTQAMNGVrefnrlKGIDLksynfsTI-FVDPPRAGLDDETLKLVQAYERI---LYISCNPE---TlcENLET 331
|
170 180 190
....*....|....*....|....*....|....*....
gi 569011295 408 LCcppNSAKqllgdpfVLREAVpVDLFPHTPHCEL-VLL 445
Cdd:PRK05031 332 LS---QTHK-------VERFAL-FDQFPYTHHMECgVLL 359
|
|
| Tam |
COG4106 |
Trans-aconitate methyltransferase [Energy production and conversion]; |
293-351 |
6.39e-05 |
|
Trans-aconitate methyltransferase [Energy production and conversion];
Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 41.73 E-value: 6.39e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569011295 293 LDICCGTGVIGLSVAQR--ASQVHGIELVEQAVEDARwtaafNGVTNCEFHAGRAETILPQ 351
Cdd:COG4106 6 LDLGCGTGRLTALLAERfpGARVTGVDLSPEMLARAR-----ARLPNVRFVVADLRDLDPP 61
|
|
| COG4976 |
COG4976 |
Predicted methyltransferase, contains TPR repeat [General function prediction only]; |
293-327 |
1.52e-04 |
|
Predicted methyltransferase, contains TPR repeat [General function prediction only];
Pssm-ID: 444001 [Multi-domain] Cd Length: 181 Bit Score: 42.29 E-value: 1.52e-04
10 20 30
....*....|....*....|....*....|....*
gi 569011295 293 LDICCGTGVIGLSVAQRASQVHGIELVEQAVEDAR 327
Cdd:COG4976 51 LDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAR 85
|
|
| PRK14968 |
PRK14968 |
putative methyltransferase; Provisional |
293-368 |
3.05e-04 |
|
putative methyltransferase; Provisional
Pssm-ID: 237872 [Multi-domain] Cd Length: 188 Bit Score: 41.42 E-value: 3.05e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569011295 293 LDICCGTGVIGLSVAQRASQVHGIELVEQAVEDARWTAAFNGVTNCEFHAGRAEtilpqLLKSQKDEKLTVAVVNP 368
Cdd:PRK14968 28 LEVGTGSGIVAIVAAKNGKKVVGVDINPYAVECAKCNAKLNNIRNNGVEVIRSD-----LFEPFRGDKFDVILFNP 98
|
|
| COG4076 |
COG4076 |
Predicted RNA methylase [General function prediction only]; |
286-351 |
5.95e-04 |
|
Predicted RNA methylase [General function prediction only];
Pssm-ID: 443253 [Multi-domain] Cd Length: 230 Bit Score: 41.18 E-value: 5.95e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569011295 286 VNSESLLLDICCGTGVIG-LSVAQRASQVHGIELVEQAVEDARWTAAFNGVT-NCEFHAGRAETILPQ 351
Cdd:COG4076 33 VKPGDVVLDIGTGSGLLSmLAARAGAKKVYAVEVNPDIAAVARRIIAANGLSdRITVINADATDLDLP 100
|
|
| CobL |
COG2242 |
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ... |
290-352 |
6.88e-04 |
|
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 441843 [Multi-domain] Cd Length: 403 Bit Score: 41.69 E-value: 6.88e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569011295 290 SLLLDICCGTGVIGLSVAQRA--SQVHGIELVEQAVEDARWTA-AFnGVTNCEFHAGRAETILPQL 352
Cdd:COG2242 249 DVLWDIGAGSGSVSIEAARLApgGRVYAIERDPERAALIRANArRF-GVPNVEVVEGEAPEALADL 313
|
|
| Methyltransf_11 |
pfam08241 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
293-399 |
2.84e-03 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 462406 [Multi-domain] Cd Length: 94 Bit Score: 36.87 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011295 293 LDICCGTGVIGLSVAQRASQVHGIELVEQAVEDARWTAAFNGVTnceFHAGRAETiLPqllksQKDEKLTVAVvnpARAG 372
Cdd:pfam08241 1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREGLT---FVVGDAED-LP-----FPDNSFDLVL---SSEV 68
|
90 100
....*....|....*....|....*....
gi 569011295 373 LHY--RVVRAIRNCRTIhtlvfvsCKPHG 399
Cdd:pfam08241 69 LHHveDPERALREIARV-------LKPGG 90
|
|
| COG2263 |
COG2263 |
Predicted RNA methylase [General function prediction only]; |
273-327 |
4.15e-03 |
|
Predicted RNA methylase [General function prediction only];
Pssm-ID: 441864 [Multi-domain] Cd Length: 199 Bit Score: 38.35 E-value: 4.15e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 569011295 273 AEMLY--RIIGELSGvnseSLLLDICCGTGVIGLSVAQR-ASQVHGIELVEQAVEDAR 327
Cdd:COG2263 32 AELLHlaYLRGDIEG----KTVLDLGCGTGMLAIGAALLgAKKVVGVDIDPEALEIAR 85
|
|
| PrmA |
COG2264 |
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis]; |
292-357 |
5.85e-03 |
|
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441865 [Multi-domain] Cd Length: 284 Bit Score: 38.62 E-value: 5.85e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569011295 292 LLDICCGTGVigLSVA---QRASQVHGIELVEQAVEDARWTAAFNGVtncefhAGRAETILPQLLKSQK 357
Cdd:COG2264 152 VLDVGCGSGI--LAIAaakLGAKRVLAVDIDPVAVEAARENAELNGV------EDRIEVVLGDLLEDGP 212
|
|
| Trm11 |
COG1041 |
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ... |
278-368 |
6.44e-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: 37.62 E-value: 6.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569011295 278 RIIGELSGVNSESLLLDICCGTGVIGLSVAQRASQVHGIELVEQAVEDARWTAAFNGVTNCEFHAGRAETIlpqllkSQK 357
Cdd:COG1041 16 RALVNLAGAKEGDTVLDPFCGTGTILIEAGLLGRRVIGSDIDPKMVEGARENLEHYGYEDADVIRGDARDL------PLA 89
|
90
....*....|.
gi 569011295 358 DEKLTVAVVNP 368
Cdd:COG1041 90 DESVDAIVTDP 100
|
|
|