|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05031 |
PRK05031 |
tRNA (uracil-5-)-methyltransferase; Validated |
1-366 |
0e+00 |
|
tRNA (uracil-5-)-methyltransferase; Validated
Pssm-ID: 235332 Cd Length: 362 Bit Score: 750.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777846 1 MTPEHLPTEQYDAQLAEKVVRLQSMMTPFNAPVPEVFRSPVSHYRMRAEFRIWHDGDDLYHIIFDQQTKSRIRVDSFPAA 80
Cdd:PRK05031 1 MTPECLPPEQYEAQLAEKVARLKELFAPFSAPEPEVFRSPPSHYRMRAEFRIWHEGDDLYYAMFDQQTKQRIRIDQFPIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777846 81 SELINQLMTLMMEGVRNNPVLRHKLFQIDYLTTQSNQAIVSLLYHKALNDEWREQAEALRDALRaqniNVHLIGRATKTK 160
Cdd:PRK05031 81 SELINALMPALLAALRANPVLRHKLFQVDFLSTLSGEILVSLLYHKKLDEEWEQAAKALRDALF----NVHLIGRSRKQK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777846 161 IMLDQDYIDERLPVAGKEMVYRQVENSFTQPNAAMNVQMLEWALKATEGSTGDLLELYCGNGNFSLALARNFDRVLATEI 240
Cdd:PRK05031 157 IVLDQDYVDERLPVAGREFIYRQVENSFTQPNAAVNEKMLEWALDATKGSKGDLLELYCGNGNFTLALARNFRRVLATEI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777846 241 AKPSVAAAQYNIAANHIDNVQIIRMAAEEFTQAMNGVRAFNRLEGIDLKSYQCETIFVDPPRSGLDSETEKMVQAYPRIL 320
Cdd:PRK05031 237 SKPSVAAAQYNIAANGIDNVQIIRMSAEEFTQAMNGVREFNRLKGIDLKSYNFSTIFVDPPRAGLDDETLKLVQAYERIL 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 829777846 321 YISCNPETLCKNLETLGQTHKVERLALFDQFPYTHHMECGVLLTAK 366
Cdd:PRK05031 317 YISCNPETLCENLETLSQTHKVERFALFDQFPYTHHMECGVLLEKK 362
|
|
| trmA_only |
TIGR02143 |
tRNA (uracil(54)-C(5))-methyltransferase; This family consists exclusively of proteins ... |
10-366 |
0e+00 |
|
tRNA (uracil(54)-C(5))-methyltransferase; This family consists exclusively of proteins believed to act as tRNA (uracil-5-)-methyltransferase. All members of far are proteobacterial. The seed alignment was taken directly from pfam05958 in Pfam 12.0, but higher cutoffs are used to select only functionally equivalent proteins. Homologous proteins excluded by the higher cutoff scores of this model include other uracil methyltransferases, such as RumA, active on rRNA. [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 131198 Cd Length: 353 Bit Score: 702.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777846 10 QYDAQLAEKVVRLQSMMTPFNAPVPEVFRSPVSHYRMRAEFRIWHDGDDLYHIIFDQQTKSRIRVDSFPAASELINQLMT 89
Cdd:TIGR02143 1 QYTAQLAEKVSRLKDLFAPFDAPEPEVFESPDKHYRMRAEFRIWHEGDDLYYAMFDQQTKSKIRVDQFPAASELINRLMP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777846 90 LMMEGVRNNPVLRHKLFQIDYLTTQSNQAIVSLLYHKALNDEWREQAEALRDalraQNINVHLIGRATKTKIMLDQDYID 169
Cdd:TIGR02143 81 ALIAALRQNPALRHKLFQVDFLTTLSGEALVSLLYHKQLDDEWRQAAEALKD----IKLNVNLIGRARKKKIVLDQDYVD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777846 170 ERLPVAGKEMVYRQVENSFTQPNAAMNVQMLEWALKATEGSTGDLLELYCGNGNFSLALARNFDRVLATEIAKPSVAAAQ 249
Cdd:TIGR02143 157 ETLPVAGREFIYRQVENSFTQPNAAVNIKMLEWACEVTQGSKGDLLELYCGNGNFSLALAQNFRRVLATEIAKPSVNAAQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777846 250 YNIAANHIDNVQIIRMAAEEFTQAMNGVRAFNRLEGIDLKSYQCETIFVDPPRSGLDSETEKMVQAYPRILYISCNPETL 329
Cdd:TIGR02143 237 YNIAANNIDNVQIIRMSAEEFTQAMNGVREFRRLKGIDLKSYNCSTIFVDPPRAGLDPDTCKLVQAYERILYISCNPETL 316
|
330 340 350
....*....|....*....|....*....|....*..
gi 829777846 330 CKNLETLGQTHKVERLALFDQFPYTHHMECGVLLTAK 366
Cdd:TIGR02143 317 KANLEQLSETHRVERFALFDQFPYTHHMECGVLLERK 353
|
|
| tRNA_U5-meth_tr |
pfam05958 |
tRNA (Uracil-5-)-methyltransferase; This family consists of (Uracil-5-)-methyltransferases EC: ... |
10-366 |
0e+00 |
|
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: 699.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777846 10 QYDAQLAEKVVRLQSMMTPFNAPVPEVFRSPVSHYRMRAEFRIWHDGDDLYHIIFDQQTKSRIRVDSFPAASELINQLMT 89
Cdd:pfam05958 1 QYDAQLAEKKSRLKALFAPFYAPDPEVFASPDKHYRMRAEFRIWHEGDDLYYAMFDQQTKSRIRVDQFPAASELINELMP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777846 90 LMMEGVRNNPVLRHKLFQIDYLTTQSNQAIVSLLYHKALNDEWREQAEALRDALRAQNINVHLIGRATKTKIMLDQDYID 169
Cdd:pfam05958 81 ALIAALRQDPALRHKLFQVDFLTTLSGEALVSLLYHKQLDDEWRQAAEALRDALRAQGLDVNLIGRARKQKIVLDQDYVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777846 170 ERLPVAGKEMVYRQVENSFTQPNAAMNVQMLEWALKATEGSTGDLLELYCGNGNFSLALARNFDRVLATEIAKPSVAAAQ 249
Cdd:pfam05958 161 ETLPVAGREFIYRQVENSFTQPNAAVNIKMLEWACDVTQGSKGDLLELYCGNGNFSLALARNFRKVLATEIAKPSVAAAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777846 250 YNIAANHIDNVQIIRMAAEEFTQAMNGVRAFNRLEGIDLKSYQCETIFVDPPRSGLDSETEKMVQAYPRILYISCNPETL 329
Cdd:pfam05958 241 YNIAANNIDNVQIIRMSAEEFTQAMNGVREFNRLKGIDLKSYNCSTIFVDPPRAGLDPETLKLVQAYPRILYISCNPETL 320
|
330 340 350
....*....|....*....|....*....|....*..
gi 829777846 330 CKNLETLGQTHKVERLALFDQFPYTHHMECGVLLTAK 366
Cdd:pfam05958 321 CANLEQLSKTHRVERFALFDQFPYTHHMECGVLLEKK 357
|
|
| TrmA |
COG2265 |
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ... |
5-364 |
9.77e-63 |
|
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: 205.02 E-value: 9.77e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777846 5 HLPteqYDAQLAEK--VVR--LQSMMTPFNAPVPEVFRSPV-SHYRMRAEFRIWHDGDDLYHIIFDQQTKSRIRVDSFPA 79
Cdd:COG2265 80 HLS---YEAQLELKqrVVReaLERIGGLPEVEVEPIIGSPEpWGYRNRARLSVRRTDGRLRLGFYARGSHELVDIDECPL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777846 80 ASELINQLMtlmmegvrnnPVLRhklfqidylttqsnqaivsllyhkalndEWREQAEALRDALRaqninvHLIGRAtkt 159
Cdd:COG2265 157 LDPALNALL----------PALR----------------------------ELLAELGARRGELR------HLVVRA--- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777846 160 kimlDQDYIDERLpvAGKEMVYRqvENSFTQPNAAMNVQMLEWALKATEGSTGD-LLELYCGNGNFSLALARNFDRVLAT 238
Cdd:COG2265 190 ----GRDYLTERL--GGLTFRIS--PGSFFQVNPEQAEALYAAALEWLDLTGGErVLDLYCGVGTFALPLARRAKKVIGV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777846 239 EIAKPSVAAAQYNIAANHIDNVQIIRMAAEEFTQAMNGVRAFNrlegidlksyqceTIFVDPPRSGLDSET-EKMVQAYP 317
Cdd:COG2265 262 EIVPEAVEDARENARLNGLKNVEFVAGDLEEVLPELLWGGRPD-------------VVVLDPPRAGAGPEVlEALAALGP 328
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 829777846 318 -RILYISCNPETLCKNLETL-GQTHKVERLALFDQFPYTHHMECGVLLT 364
Cdd:COG2265 329 rRIVYVSCNPATLARDLALLvEGGYRLEKVQPVDMFPHTHHVESVALLE 377
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
213-320 |
7.94e-06 |
|
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: 44.34 E-value: 7.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777846 213 DLLELYCGNGNFSLALAR-NFDRVLATEIAKPSVAAAQYNIAANHIDNVQIIRMAAEEFTqamngvraFNRLEGIDLksy 291
Cdd:cd02440 1 RVLDLGCGTGALALALASgPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELP--------PEADESFDV--- 69
|
90 100
....*....|....*....|....*....
gi 829777846 292 qcetIFVDPPRSGLDSETEKMVQAYPRIL 320
Cdd:cd02440 70 ----IISDPPLHHLVEDLARFLEEARRLL 94
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05031 |
PRK05031 |
tRNA (uracil-5-)-methyltransferase; Validated |
1-366 |
0e+00 |
|
tRNA (uracil-5-)-methyltransferase; Validated
Pssm-ID: 235332 Cd Length: 362 Bit Score: 750.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777846 1 MTPEHLPTEQYDAQLAEKVVRLQSMMTPFNAPVPEVFRSPVSHYRMRAEFRIWHDGDDLYHIIFDQQTKSRIRVDSFPAA 80
Cdd:PRK05031 1 MTPECLPPEQYEAQLAEKVARLKELFAPFSAPEPEVFRSPPSHYRMRAEFRIWHEGDDLYYAMFDQQTKQRIRIDQFPIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777846 81 SELINQLMTLMMEGVRNNPVLRHKLFQIDYLTTQSNQAIVSLLYHKALNDEWREQAEALRDALRaqniNVHLIGRATKTK 160
Cdd:PRK05031 81 SELINALMPALLAALRANPVLRHKLFQVDFLSTLSGEILVSLLYHKKLDEEWEQAAKALRDALF----NVHLIGRSRKQK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777846 161 IMLDQDYIDERLPVAGKEMVYRQVENSFTQPNAAMNVQMLEWALKATEGSTGDLLELYCGNGNFSLALARNFDRVLATEI 240
Cdd:PRK05031 157 IVLDQDYVDERLPVAGREFIYRQVENSFTQPNAAVNEKMLEWALDATKGSKGDLLELYCGNGNFTLALARNFRRVLATEI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777846 241 AKPSVAAAQYNIAANHIDNVQIIRMAAEEFTQAMNGVRAFNRLEGIDLKSYQCETIFVDPPRSGLDSETEKMVQAYPRIL 320
Cdd:PRK05031 237 SKPSVAAAQYNIAANGIDNVQIIRMSAEEFTQAMNGVREFNRLKGIDLKSYNFSTIFVDPPRAGLDDETLKLVQAYERIL 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 829777846 321 YISCNPETLCKNLETLGQTHKVERLALFDQFPYTHHMECGVLLTAK 366
Cdd:PRK05031 317 YISCNPETLCENLETLSQTHKVERFALFDQFPYTHHMECGVLLEKK 362
|
|
| trmA_only |
TIGR02143 |
tRNA (uracil(54)-C(5))-methyltransferase; This family consists exclusively of proteins ... |
10-366 |
0e+00 |
|
tRNA (uracil(54)-C(5))-methyltransferase; This family consists exclusively of proteins believed to act as tRNA (uracil-5-)-methyltransferase. All members of far are proteobacterial. The seed alignment was taken directly from pfam05958 in Pfam 12.0, but higher cutoffs are used to select only functionally equivalent proteins. Homologous proteins excluded by the higher cutoff scores of this model include other uracil methyltransferases, such as RumA, active on rRNA. [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 131198 Cd Length: 353 Bit Score: 702.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777846 10 QYDAQLAEKVVRLQSMMTPFNAPVPEVFRSPVSHYRMRAEFRIWHDGDDLYHIIFDQQTKSRIRVDSFPAASELINQLMT 89
Cdd:TIGR02143 1 QYTAQLAEKVSRLKDLFAPFDAPEPEVFESPDKHYRMRAEFRIWHEGDDLYYAMFDQQTKSKIRVDQFPAASELINRLMP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777846 90 LMMEGVRNNPVLRHKLFQIDYLTTQSNQAIVSLLYHKALNDEWREQAEALRDalraQNINVHLIGRATKTKIMLDQDYID 169
Cdd:TIGR02143 81 ALIAALRQNPALRHKLFQVDFLTTLSGEALVSLLYHKQLDDEWRQAAEALKD----IKLNVNLIGRARKKKIVLDQDYVD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777846 170 ERLPVAGKEMVYRQVENSFTQPNAAMNVQMLEWALKATEGSTGDLLELYCGNGNFSLALARNFDRVLATEIAKPSVAAAQ 249
Cdd:TIGR02143 157 ETLPVAGREFIYRQVENSFTQPNAAVNIKMLEWACEVTQGSKGDLLELYCGNGNFSLALAQNFRRVLATEIAKPSVNAAQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777846 250 YNIAANHIDNVQIIRMAAEEFTQAMNGVRAFNRLEGIDLKSYQCETIFVDPPRSGLDSETEKMVQAYPRILYISCNPETL 329
Cdd:TIGR02143 237 YNIAANNIDNVQIIRMSAEEFTQAMNGVREFRRLKGIDLKSYNCSTIFVDPPRAGLDPDTCKLVQAYERILYISCNPETL 316
|
330 340 350
....*....|....*....|....*....|....*..
gi 829777846 330 CKNLETLGQTHKVERLALFDQFPYTHHMECGVLLTAK 366
Cdd:TIGR02143 317 KANLEQLSETHRVERFALFDQFPYTHHMECGVLLERK 353
|
|
| tRNA_U5-meth_tr |
pfam05958 |
tRNA (Uracil-5-)-methyltransferase; This family consists of (Uracil-5-)-methyltransferases EC: ... |
10-366 |
0e+00 |
|
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: 699.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777846 10 QYDAQLAEKVVRLQSMMTPFNAPVPEVFRSPVSHYRMRAEFRIWHDGDDLYHIIFDQQTKSRIRVDSFPAASELINQLMT 89
Cdd:pfam05958 1 QYDAQLAEKKSRLKALFAPFYAPDPEVFASPDKHYRMRAEFRIWHEGDDLYYAMFDQQTKSRIRVDQFPAASELINELMP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777846 90 LMMEGVRNNPVLRHKLFQIDYLTTQSNQAIVSLLYHKALNDEWREQAEALRDALRAQNINVHLIGRATKTKIMLDQDYID 169
Cdd:pfam05958 81 ALIAALRQDPALRHKLFQVDFLTTLSGEALVSLLYHKQLDDEWRQAAEALRDALRAQGLDVNLIGRARKQKIVLDQDYVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777846 170 ERLPVAGKEMVYRQVENSFTQPNAAMNVQMLEWALKATEGSTGDLLELYCGNGNFSLALARNFDRVLATEIAKPSVAAAQ 249
Cdd:pfam05958 161 ETLPVAGREFIYRQVENSFTQPNAAVNIKMLEWACDVTQGSKGDLLELYCGNGNFSLALARNFRKVLATEIAKPSVAAAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777846 250 YNIAANHIDNVQIIRMAAEEFTQAMNGVRAFNRLEGIDLKSYQCETIFVDPPRSGLDSETEKMVQAYPRILYISCNPETL 329
Cdd:pfam05958 241 YNIAANNIDNVQIIRMSAEEFTQAMNGVREFNRLKGIDLKSYNCSTIFVDPPRAGLDPETLKLVQAYPRILYISCNPETL 320
|
330 340 350
....*....|....*....|....*....|....*..
gi 829777846 330 CKNLETLGQTHKVERLALFDQFPYTHHMECGVLLTAK 366
Cdd:pfam05958 321 CANLEQLSKTHRVERFALFDQFPYTHHMECGVLLEKK 357
|
|
| TrmA |
COG2265 |
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ... |
5-364 |
9.77e-63 |
|
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: 205.02 E-value: 9.77e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777846 5 HLPteqYDAQLAEK--VVR--LQSMMTPFNAPVPEVFRSPV-SHYRMRAEFRIWHDGDDLYHIIFDQQTKSRIRVDSFPA 79
Cdd:COG2265 80 HLS---YEAQLELKqrVVReaLERIGGLPEVEVEPIIGSPEpWGYRNRARLSVRRTDGRLRLGFYARGSHELVDIDECPL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777846 80 ASELINQLMtlmmegvrnnPVLRhklfqidylttqsnqaivsllyhkalndEWREQAEALRDALRaqninvHLIGRAtkt 159
Cdd:COG2265 157 LDPALNALL----------PALR----------------------------ELLAELGARRGELR------HLVVRA--- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777846 160 kimlDQDYIDERLpvAGKEMVYRqvENSFTQPNAAMNVQMLEWALKATEGSTGD-LLELYCGNGNFSLALARNFDRVLAT 238
Cdd:COG2265 190 ----GRDYLTERL--GGLTFRIS--PGSFFQVNPEQAEALYAAALEWLDLTGGErVLDLYCGVGTFALPLARRAKKVIGV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777846 239 EIAKPSVAAAQYNIAANHIDNVQIIRMAAEEFTQAMNGVRAFNrlegidlksyqceTIFVDPPRSGLDSET-EKMVQAYP 317
Cdd:COG2265 262 EIVPEAVEDARENARLNGLKNVEFVAGDLEEVLPELLWGGRPD-------------VVVLDPPRAGAGPEVlEALAALGP 328
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 829777846 318 -RILYISCNPETLCKNLETL-GQTHKVERLALFDQFPYTHHMECGVLLT 364
Cdd:COG2265 329 rRIVYVSCNPATLARDLALLvEGGYRLEKVQPVDMFPHTHHVESVALLE 377
|
|
| rumA |
TIGR00479 |
23S rRNA (uracil-5-)-methyltransferase RumA; This protein family was first proposed to be RNA ... |
4-358 |
2.04e-28 |
|
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: 114.92 E-value: 2.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777846 4 EHLPteqYDAQLAEK---VVRLQSMMTPFN----APVPEVFRSPVShYRMRAEFRIWHDGDDLYHIIFDQQTKSRI-RVD 75
Cdd:TIGR00479 70 QHLS---YELQLRSKqqqVIALLERIGKFVsepiEDVPTIGDDPWG-YRNKARLSLGRSPSGQLQAGFYQKGSHDIvDVK 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777846 76 SFPAASELINQLMTLMMEGVRNNPVLRH----KLFQIDYLTTQ-----SNQAIVSLLYHKALNDEwREQAEALRDALRAQ 146
Cdd:TIGR00479 146 QCPVQAPALNALLPKVRAILENFGASRYlehkELGQARHGVLRigrhtGELSSVDRTALERFPHK-EELDLYLQPDSPDV 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777846 147 NINVHLIGRATKTKImldqdYIDERLPVAGkEMVYRQV---------ENSFTQPNAAMNVQMLEWALKATEGSTGD-LLE 216
Cdd:TIGR00479 225 KSICQNINPEKTNVI-----FGEETEVIAG-EMPIYDKsgdlsftfsARDFIQVNSGQNEKLVDRALEWLELQGEErVLD 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777846 217 LYCGNGNFSLALARNFDRVLATEIAKPSVAAAQYNIAANHIDNVQIIRMAAEEF--TQAMNGVRAfnrlegidlksyqcE 294
Cdd:TIGR00479 299 AYCGMGTFTLPLAKQAKSVVGVEGVPESVEKAQQNAELNGIANVTFYHGTLETVlpKQPWAGNGF--------------D 364
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 829777846 295 TIFVDPPRSGLDSET-EKMVQAYP-RILYISCNPETLCKNLETL-GQTHKVERLALFDQFPYTHHME 358
Cdd:TIGR00479 365 KVLLDPPRKGCAAGVlRTIIKLKPeRIVYVSCNPATLARDLEALcKAGYTIARVQPVDMFPHTGHVE 431
|
|
| rumA |
PRK13168 |
23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD; |
5-358 |
7.75e-26 |
|
23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD;
Pssm-ID: 237291 [Multi-domain] Cd Length: 443 Bit Score: 107.55 E-value: 7.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777846 5 HLPteqYDAQLAEKVVRLQSMMTPFNAPVPEVFRSPVS----HYRMRAEFRIWHDGD-DLYHIIFDQQtKSR--IRVDS- 76
Cdd:PRK13168 93 HLS---IDAQIASKQRALEDLLKHLAGVEPEEVLPPIAgppwGYRRRARLSVRYVPKkGQLLVGFREK-NSSdiVDIDQc 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777846 77 ---FPAASELINQLMTLM--MEGVRNnpvLRH-KLFQIDylttqsnQAIVSLLYH-KALNDEWREqaeALRDALRAQNIN 149
Cdd:PRK13168 169 pvlVPPLSALLPPLRALLssLSAKRR---LGHvELAQGD-------NGTALVLRHlEPLSEADRA---KLRAFAEQHGLQ 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777846 150 VHLIGRATKTKIMLDQDY--IDERLPVAGKEMVYRqvENSFTQPNAAMNVQM----LEW-ALKATEgstgDLLELYCGNG 222
Cdd:PRK13168 236 LYLQPKGPDLVHLLGPADaqLSYYLPEFGLRLAFS--PRDFIQVNAQVNQKMvaraLEWlDPQPGD----RVLDLFCGLG 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777846 223 NFSLALARNFDRVLATEIAKPSVAAAQYNIAANHIDNVQIirMAA---EEFTQAMNGVRAFNRlegidlksyqcetIFVD 299
Cdd:PRK13168 310 NFTLPLARQAAEVVGVEGVEAMVERARENARRNGLDNVTF--YHAnleEDFTDQPWALGGFDK-------------VLLD 374
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 829777846 300 PPRSG----LDSETEKMVQaypRILYISCNPETLCKNLETL-GQTHKVERLALFDQFPYTHHME 358
Cdd:PRK13168 375 PPRAGaaevMQALAKLGPK---RIVYVSCNPATLARDAGVLvEAGYRLKRAGMLDMFPHTGHVE 435
|
|
| rumB |
PRK03522 |
23S rRNA (uracil(747)-C(5))-methyltransferase RlmC; |
187-364 |
2.83e-19 |
|
23S rRNA (uracil(747)-C(5))-methyltransferase RlmC;
Pssm-ID: 235128 [Multi-domain] Cd Length: 315 Bit Score: 87.23 E-value: 2.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777846 187 SFTQPN----AAMNVQMLEWALKATEGSTGDLlelYCGNGNFSLALARNFDRVLATEIAKPSVAAAQYNIAANHIDNVQI 262
Cdd:PRK03522 149 SFFQTNpavaAQLYATARDWVRELPPRSMWDL---FCGVGGFGLHCATPGMQLTGIEISAEAIACAKQSAAELGLTNVQF 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777846 263 IRMAAEEFTQAMNGVRafnrlegiDLksyqcetIFVDPPRSGLDSE----TEKMvqAYPRILYISCNPETLCKNLETLgQ 338
Cdd:PRK03522 226 QALDSTQFATAQGEVP--------DL-------VLVNPPRRGIGKElcdyLSQM--APRFILYSSCNAQTMAKDLAHL-P 287
|
170 180
....*....|....*....|....*.
gi 829777846 339 THKVERLALFDQFPYTHHMECGVLLT 364
Cdd:PRK03522 288 GYRIERVQLFDMFPHTAHYEVLTLLV 313
|
|
| RsmC |
COG2813 |
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ... |
211-320 |
3.46e-06 |
|
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: 47.11 E-value: 3.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777846 211 TGDLLELYCGNGNFSLALARNFD--RVLATEIAKPSVAAAQYNIAANHIDNVQiirmaaeeftqamngVRAFNRLEGIDL 288
Cdd:COG2813 50 GGRVLDLGCGYGVIGLALAKRNPeaRVTLVDVNARAVELARANAAANGLENVE---------------VLWSDGLSGVPD 114
|
90 100 110
....*....|....*....|....*....|....*.
gi 829777846 289 KSYQceTIFVDPP-RSGL---DSETEKMVQAYPRIL 320
Cdd:COG2813 115 GSFD--LILSNPPfHAGRavdKEVAHALIADAARHL 148
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
213-320 |
7.94e-06 |
|
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: 44.34 E-value: 7.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777846 213 DLLELYCGNGNFSLALAR-NFDRVLATEIAKPSVAAAQYNIAANHIDNVQIIRMAAEEFTqamngvraFNRLEGIDLksy 291
Cdd:cd02440 1 RVLDLGCGTGALALALASgPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELP--------PEADESFDV--- 69
|
90 100
....*....|....*....|....*....
gi 829777846 292 qcetIFVDPPRSGLDSETEKMVQAYPRIL 320
Cdd:cd02440 70 ----IISDPPLHHLVEDLARFLEEARRLL 94
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
198-270 |
1.14e-05 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 45.68 E-value: 1.14e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 829777846 198 QMLEWALKATEGSTGDLLELYCGNGNFSLALA-RNFDRVLATEIAKPSVAAAQYNIAANHIDNVQIIRMAAEEF 270
Cdd:COG0500 14 LAALLALLERLPKGGRVLDLGCGTGRNLLALAaRFGGRVIGIDLSPEAIALARARAAKAGLGNVEFLVADLAEL 87
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
203-269 |
5.24e-05 |
|
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: 42.67 E-value: 5.24e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 829777846 203 ALKATEGSTgdLLELYCGNGNFSLALARNFDRVLATEIAKPSVAAAQYNIAANHIdNVQIIRMAAEE 269
Cdd:COG2226 17 ALGLRPGAR--VLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGL-NVEFVVGDAED 80
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
200-270 |
6.28e-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: 42.31 E-value: 6.28e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 829777846 200 LEWALKATEGSTGDLLELYCGNGNFSLALARNFDRVLATEIAKPSVAAAQYNIAANhidNVQIIRMAAEEF 270
Cdd:COG2227 14 LAALLARLLPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAEL---NVDFVQGDLEDL 81
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
215-270 |
1.85e-04 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 40.24 E-value: 1.85e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 829777846 215 LELYCGNGNFSLALARNFD-RVLATEIAKPSVAAAQYNIAANHIdNVQIIRMAAEEF 270
Cdd:pfam13649 2 LDLGCGTGRLTLALARRGGaRVTGVDLSPEMLERARERAAEAGL-NVEFVQGDAEDL 57
|
|
| Methyltransf_11 |
pfam08241 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
215-261 |
3.87e-04 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 462406 [Multi-domain] Cd Length: 94 Bit Score: 39.19 E-value: 3.87e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 829777846 215 LELYCGNGNFSLALARNFDRVLATEIAKPSVAAAQYNIAANHIDNVQ 261
Cdd:pfam08241 1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREGLTFVV 47
|
|
| TrmN6 |
COG4123 |
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ... |
214-274 |
6.51e-04 |
|
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: 40.90 E-value: 6.51e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 829777846 214 LLELYCGNGNFSLALARNFD--RVLATEIAKPSVAAAQYNIAANHIDN-VQIIRMAAEEFTQAM 274
Cdd:COG4123 41 VLDLGTGTGVIALMLAQRSPgaRITGVEIQPEAAELARRNVALNGLEDrITVIHGDLKEFAAEL 104
|
|
| trmB |
PRK00121 |
tRNA (guanine-N(7)-)-methyltransferase; Reviewed |
215-274 |
5.93e-03 |
|
tRNA (guanine-N(7)-)-methyltransferase; Reviewed
Pssm-ID: 234649 Cd Length: 202 Bit Score: 37.45 E-value: 5.93e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 829777846 215 LELYCGNGNFSLALA-----RNFdrvLATEIAKPSVAAAQYNIAANHIDNVQIIRMAAEEFTQAM 274
Cdd:PRK00121 45 LEIGFGKGEFLVEMAkanpdINF---IGIEVHEPGVGKALKKIEEEGLTNLRLLCGDAVEVLLDM 106
|
|
| Tam |
COG4106 |
Trans-aconitate methyltransferase [Energy production and conversion]; |
215-271 |
7.03e-03 |
|
Trans-aconitate methyltransferase [Energy production and conversion];
Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 35.57 E-value: 7.03e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 829777846 215 LELYCGNGNFSLALARNFD--RVLATEIAKPSVAAAQyniaaNHIDNVQIIRMAAEEFT 271
Cdd:COG4106 6 LDLGCGTGRLTALLAERFPgaRVTGVDLSPEMLARAR-----ARLPNVRFVVADLRDLD 59
|
|
| |
