|
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: 761.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745595550 1 MTPEHLPTEQYEAQLAEKVVRLQSMMAPFSDLVPEVFRSPVSHYRMRAEFRIWHDGDDLYHIIFDQQTKSRIRVDSFPAA 80
Cdd:PRK05031 1 MTPECLPPEQYEAQLAEKVARLKELFAPFSAPEPEVFRSPPSHYRMRAEFRIWHEGDDLYYAMFDQQTKQRIRIDQFPIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745595550 81 SELINQLMTAMIAGVRNNPVLRHKLFQIDYLTTLSNQAVVSLLYHKKLDDEWRQEAEALRDALRaqnlNVHLIGRATKTK 160
Cdd:PRK05031 81 SELINALMPALLAALRANPVLRHKLFQVDFLSTLSGEILVSLLYHKKLDEEWEQAAKALRDALF----NVHLIGRSRKQK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745595550 161 IALDQDYIDERLPVAGKEMIYRQVENSFTQPNAAMNIQMLEWALDVTKGSKGDLLELYCGNGNFSLALARNFDRVLATEI 240
Cdd:PRK05031 157 IVLDQDYVDERLPVAGREFIYRQVENSFTQPNAAVNEKMLEWALDATKGSKGDLLELYCGNGNFTLALARNFRRVLATEI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745595550 241 AKPSVAAAQYNIAANHIDNVQIIRMAAEEFTQAMNGVREFNRLQGIDLKSYQCETIFVDPPRSGLDSETEKMVQAYPRIL 320
Cdd:PRK05031 237 SKPSVAAAQYNIAANGIDNVQIIRMSAEEFTQAMNGVREFNRLKGIDLKSYNFSTIFVDPPRAGLDDETLKLVQAYERIL 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1745595550 321 YISCNPETLCKNLETLSQTHKVERLALFDQFPYTHHMECGVLLTAK 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: 722.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745595550 10 QYEAQLAEKVVRLQSMMAPFSDLVPEVFRSPVSHYRMRAEFRIWHDGDDLYHIIFDQQTKSRIRVDSFPAASELINQLMT 89
Cdd:TIGR02143 1 QYTAQLAEKVSRLKDLFAPFDAPEPEVFESPDKHYRMRAEFRIWHEGDDLYYAMFDQQTKSKIRVDQFPAASELINRLMP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745595550 90 AMIAGVRNNPVLRHKLFQIDYLTTLSNQAVVSLLYHKKLDDEWRQEAEALRDalraQNLNVHLIGRATKTKIALDQDYID 169
Cdd:TIGR02143 81 ALIAALRQNPALRHKLFQVDFLTTLSGEALVSLLYHKQLDDEWRQAAEALKD----IKLNVNLIGRARKKKIVLDQDYVD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745595550 170 ERLPVAGKEMIYRQVENSFTQPNAAMNIQMLEWALDVTKGSKGDLLELYCGNGNFSLALARNFDRVLATEIAKPSVAAAQ 249
Cdd:TIGR02143 157 ETLPVAGREFIYRQVENSFTQPNAAVNIKMLEWACEVTQGSKGDLLELYCGNGNFSLALAQNFRRVLATEIAKPSVNAAQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745595550 250 YNIAANHIDNVQIIRMAAEEFTQAMNGVREFNRLQGIDLKSYQCETIFVDPPRSGLDSETEKMVQAYPRILYISCNPETL 329
Cdd:TIGR02143 237 YNIAANNIDNVQIIRMSAEEFTQAMNGVREFRRLKGIDLKSYNCSTIFVDPPRAGLDPDTCKLVQAYERILYISCNPETL 316
|
330 340 350
....*....|....*....|....*....|....*..
gi 1745595550 330 CKNLETLSQTHKVERLALFDQFPYTHHMECGVLLTAK 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: 719.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745595550 10 QYEAQLAEKVVRLQSMMAPFSDLVPEVFRSPVSHYRMRAEFRIWHDGDDLYHIIFDQQTKSRIRVDSFPAASELINQLMT 89
Cdd:pfam05958 1 QYDAQLAEKKSRLKALFAPFYAPDPEVFASPDKHYRMRAEFRIWHEGDDLYYAMFDQQTKSRIRVDQFPAASELINELMP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745595550 90 AMIAGVRNNPVLRHKLFQIDYLTTLSNQAVVSLLYHKKLDDEWRQEAEALRDALRAQNLNVHLIGRATKTKIALDQDYID 169
Cdd:pfam05958 81 ALIAALRQDPALRHKLFQVDFLTTLSGEALVSLLYHKQLDDEWRQAAEALRDALRAQGLDVNLIGRARKQKIVLDQDYVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745595550 170 ERLPVAGKEMIYRQVENSFTQPNAAMNIQMLEWALDVTKGSKGDLLELYCGNGNFSLALARNFDRVLATEIAKPSVAAAQ 249
Cdd:pfam05958 161 ETLPVAGREFIYRQVENSFTQPNAAVNIKMLEWACDVTQGSKGDLLELYCGNGNFSLALARNFRKVLATEIAKPSVAAAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745595550 250 YNIAANHIDNVQIIRMAAEEFTQAMNGVREFNRLQGIDLKSYQCETIFVDPPRSGLDSETEKMVQAYPRILYISCNPETL 329
Cdd:pfam05958 241 YNIAANNIDNVQIIRMSAEEFTQAMNGVREFNRLKGIDLKSYNCSTIFVDPPRAGLDPETLKLVQAYPRILYISCNPETL 320
|
330 340 350
....*....|....*....|....*....|....*..
gi 1745595550 330 CKNLETLSQTHKVERLALFDQFPYTHHMECGVLLTAK 366
Cdd:pfam05958 321 CANLEQLSKTHRVERFALFDQFPYTHHMECGVLLEKK 357
|
|
| TrmA |
COG2265 |
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ... |
5-364 |
1.15e-61 |
|
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: 201.94 E-value: 1.15e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745595550 5 HLPteqYEAQLAEKVVRLQSMMAPFSDL----VPEVFRSPV-SHYRMRAEFRIWHDGDDLYHIIFDQQTKSRIRVDSFPA 79
Cdd:COG2265 80 HLS---YEAQLELKQRVVREALERIGGLpeveVEPIIGSPEpWGYRNRARLSVRRTDGRLRLGFYARGSHELVDIDECPL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745595550 80 ASELINQLMtamiagvrnnPVLRhklfqidylttlsnqavvsllyhkklddEWRQEAEALRDALRaqnlnvHLIgratkt 159
Cdd:COG2265 157 LDPALNALL----------PALR----------------------------ELLAELGARRGELR------HLV------ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745595550 160 kIALDQDYIDERLpvAGKEMIYRqvENSFTQPNAAMNIQMLEWALDVTKGSKGD-LLELYCGNGNFSLALARNFDRVLAT 238
Cdd:COG2265 187 -VRAGRDYLTERL--GGLTFRIS--PGSFFQVNPEQAEALYAAALEWLDLTGGErVLDLYCGVGTFALPLARRAKKVIGV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745595550 239 EIAKPSVAAAQYNIAANHIDNVQIIRMAAEEFTQAMNGVREFNrlqgidlksyqceTIFVDPPRSGLDSET-EKMVQAYP 317
Cdd:COG2265 262 EIVPEAVEDARENARLNGLKNVEFVAGDLEEVLPELLWGGRPD-------------VVVLDPPRAGAGPEVlEALAALGP 328
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1745595550 318 -RILYISCNPETLCKNLETL-SQTHKVERLALFDQFPYTHHMECGVLLT 364
Cdd:COG2265 329 rRIVYVSCNPATLARDLALLvEGGYRLEKVQPVDMFPHTHHVESVALLE 377
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
213-270 |
1.09e-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: 43.96 E-value: 1.09e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1745595550 213 DLLELYCGNGNFSLALAR-NFDRVLATEIAKPSVAAAQYNIAANHIDNVQIIRMAAEEF 270
Cdd:cd02440 1 RVLDLGCGTGALALALASgPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEEL 59
|
|
| |
|
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: 761.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745595550 1 MTPEHLPTEQYEAQLAEKVVRLQSMMAPFSDLVPEVFRSPVSHYRMRAEFRIWHDGDDLYHIIFDQQTKSRIRVDSFPAA 80
Cdd:PRK05031 1 MTPECLPPEQYEAQLAEKVARLKELFAPFSAPEPEVFRSPPSHYRMRAEFRIWHEGDDLYYAMFDQQTKQRIRIDQFPIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745595550 81 SELINQLMTAMIAGVRNNPVLRHKLFQIDYLTTLSNQAVVSLLYHKKLDDEWRQEAEALRDALRaqnlNVHLIGRATKTK 160
Cdd:PRK05031 81 SELINALMPALLAALRANPVLRHKLFQVDFLSTLSGEILVSLLYHKKLDEEWEQAAKALRDALF----NVHLIGRSRKQK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745595550 161 IALDQDYIDERLPVAGKEMIYRQVENSFTQPNAAMNIQMLEWALDVTKGSKGDLLELYCGNGNFSLALARNFDRVLATEI 240
Cdd:PRK05031 157 IVLDQDYVDERLPVAGREFIYRQVENSFTQPNAAVNEKMLEWALDATKGSKGDLLELYCGNGNFTLALARNFRRVLATEI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745595550 241 AKPSVAAAQYNIAANHIDNVQIIRMAAEEFTQAMNGVREFNRLQGIDLKSYQCETIFVDPPRSGLDSETEKMVQAYPRIL 320
Cdd:PRK05031 237 SKPSVAAAQYNIAANGIDNVQIIRMSAEEFTQAMNGVREFNRLKGIDLKSYNFSTIFVDPPRAGLDDETLKLVQAYERIL 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1745595550 321 YISCNPETLCKNLETLSQTHKVERLALFDQFPYTHHMECGVLLTAK 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: 722.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745595550 10 QYEAQLAEKVVRLQSMMAPFSDLVPEVFRSPVSHYRMRAEFRIWHDGDDLYHIIFDQQTKSRIRVDSFPAASELINQLMT 89
Cdd:TIGR02143 1 QYTAQLAEKVSRLKDLFAPFDAPEPEVFESPDKHYRMRAEFRIWHEGDDLYYAMFDQQTKSKIRVDQFPAASELINRLMP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745595550 90 AMIAGVRNNPVLRHKLFQIDYLTTLSNQAVVSLLYHKKLDDEWRQEAEALRDalraQNLNVHLIGRATKTKIALDQDYID 169
Cdd:TIGR02143 81 ALIAALRQNPALRHKLFQVDFLTTLSGEALVSLLYHKQLDDEWRQAAEALKD----IKLNVNLIGRARKKKIVLDQDYVD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745595550 170 ERLPVAGKEMIYRQVENSFTQPNAAMNIQMLEWALDVTKGSKGDLLELYCGNGNFSLALARNFDRVLATEIAKPSVAAAQ 249
Cdd:TIGR02143 157 ETLPVAGREFIYRQVENSFTQPNAAVNIKMLEWACEVTQGSKGDLLELYCGNGNFSLALAQNFRRVLATEIAKPSVNAAQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745595550 250 YNIAANHIDNVQIIRMAAEEFTQAMNGVREFNRLQGIDLKSYQCETIFVDPPRSGLDSETEKMVQAYPRILYISCNPETL 329
Cdd:TIGR02143 237 YNIAANNIDNVQIIRMSAEEFTQAMNGVREFRRLKGIDLKSYNCSTIFVDPPRAGLDPDTCKLVQAYERILYISCNPETL 316
|
330 340 350
....*....|....*....|....*....|....*..
gi 1745595550 330 CKNLETLSQTHKVERLALFDQFPYTHHMECGVLLTAK 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: 719.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745595550 10 QYEAQLAEKVVRLQSMMAPFSDLVPEVFRSPVSHYRMRAEFRIWHDGDDLYHIIFDQQTKSRIRVDSFPAASELINQLMT 89
Cdd:pfam05958 1 QYDAQLAEKKSRLKALFAPFYAPDPEVFASPDKHYRMRAEFRIWHEGDDLYYAMFDQQTKSRIRVDQFPAASELINELMP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745595550 90 AMIAGVRNNPVLRHKLFQIDYLTTLSNQAVVSLLYHKKLDDEWRQEAEALRDALRAQNLNVHLIGRATKTKIALDQDYID 169
Cdd:pfam05958 81 ALIAALRQDPALRHKLFQVDFLTTLSGEALVSLLYHKQLDDEWRQAAEALRDALRAQGLDVNLIGRARKQKIVLDQDYVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745595550 170 ERLPVAGKEMIYRQVENSFTQPNAAMNIQMLEWALDVTKGSKGDLLELYCGNGNFSLALARNFDRVLATEIAKPSVAAAQ 249
Cdd:pfam05958 161 ETLPVAGREFIYRQVENSFTQPNAAVNIKMLEWACDVTQGSKGDLLELYCGNGNFSLALARNFRKVLATEIAKPSVAAAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745595550 250 YNIAANHIDNVQIIRMAAEEFTQAMNGVREFNRLQGIDLKSYQCETIFVDPPRSGLDSETEKMVQAYPRILYISCNPETL 329
Cdd:pfam05958 241 YNIAANNIDNVQIIRMSAEEFTQAMNGVREFNRLKGIDLKSYNCSTIFVDPPRAGLDPETLKLVQAYPRILYISCNPETL 320
|
330 340 350
....*....|....*....|....*....|....*..
gi 1745595550 330 CKNLETLSQTHKVERLALFDQFPYTHHMECGVLLTAK 366
Cdd:pfam05958 321 CANLEQLSKTHRVERFALFDQFPYTHHMECGVLLEKK 357
|
|
| TrmA |
COG2265 |
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ... |
5-364 |
1.15e-61 |
|
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: 201.94 E-value: 1.15e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745595550 5 HLPteqYEAQLAEKVVRLQSMMAPFSDL----VPEVFRSPV-SHYRMRAEFRIWHDGDDLYHIIFDQQTKSRIRVDSFPA 79
Cdd:COG2265 80 HLS---YEAQLELKQRVVREALERIGGLpeveVEPIIGSPEpWGYRNRARLSVRRTDGRLRLGFYARGSHELVDIDECPL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745595550 80 ASELINQLMtamiagvrnnPVLRhklfqidylttlsnqavvsllyhkklddEWRQEAEALRDALRaqnlnvHLIgratkt 159
Cdd:COG2265 157 LDPALNALL----------PALR----------------------------ELLAELGARRGELR------HLV------ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745595550 160 kIALDQDYIDERLpvAGKEMIYRqvENSFTQPNAAMNIQMLEWALDVTKGSKGD-LLELYCGNGNFSLALARNFDRVLAT 238
Cdd:COG2265 187 -VRAGRDYLTERL--GGLTFRIS--PGSFFQVNPEQAEALYAAALEWLDLTGGErVLDLYCGVGTFALPLARRAKKVIGV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745595550 239 EIAKPSVAAAQYNIAANHIDNVQIIRMAAEEFTQAMNGVREFNrlqgidlksyqceTIFVDPPRSGLDSET-EKMVQAYP 317
Cdd:COG2265 262 EIVPEAVEDARENARLNGLKNVEFVAGDLEEVLPELLWGGRPD-------------VVVLDPPRAGAGPEVlEALAALGP 328
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1745595550 318 -RILYISCNPETLCKNLETL-SQTHKVERLALFDQFPYTHHMECGVLLT 364
Cdd:COG2265 329 rRIVYVSCNPATLARDLALLvEGGYRLEKVQPVDMFPHTHHVESVALLE 377
|
|
| rumA |
PRK13168 |
23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD; |
5-358 |
2.81e-27 |
|
23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD;
Pssm-ID: 237291 [Multi-domain] Cd Length: 443 Bit Score: 111.79 E-value: 2.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745595550 5 HLPteqYEAQLAEKVVRLQSMMAPFSDLVPEVFRSPVS----HYRMRAEFRIWHDGD-DLYHIIFDQQtKSR--IRVDS- 76
Cdd:PRK13168 93 HLS---IDAQIASKQRALEDLLKHLAGVEPEEVLPPIAgppwGYRRRARLSVRYVPKkGQLLVGFREK-NSSdiVDIDQc 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745595550 77 ---FPAASELINQLmTAMIAGVRNNPVLRH-KLFQIDylttlsnQAVVSLLYH-KKLDDEWRQeaeALRDALRAQNLNVH 151
Cdd:PRK13168 169 pvlVPPLSALLPPL-RALLSSLSAKRRLGHvELAQGD-------NGTALVLRHlEPLSEADRA---KLRAFAEQHGLQLY 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745595550 152 LIGRATKTKIALDQDY--IDERLPVAGKEMIYRqvENSFTQPNAAMNIQM----LEWaLDVTKGSKgdLLELYCGNGNFS 225
Cdd:PRK13168 238 LQPKGPDLVHLLGPADaqLSYYLPEFGLRLAFS--PRDFIQVNAQVNQKMvaraLEW-LDPQPGDR--VLDLFCGLGNFT 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745595550 226 LALARNFDRVLATEIAKPSVAAAQYNIAANHIDNVQIirMAA---EEFTQAMNGVREFNRlqgidlksyqcetIFVDPPR 302
Cdd:PRK13168 313 LPLARQAAEVVGVEGVEAMVERARENARRNGLDNVTF--YHAnleEDFTDQPWALGGFDK-------------VLLDPPR 377
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1745595550 303 SG----LDSETEKMVQaypRILYISCNPETLCKNLETL-SQTHKVERLALFDQFPYTHHME 358
Cdd:PRK13168 378 AGaaevMQALAKLGPK---RIVYVSCNPATLARDAGVLvEAGYRLKRAGMLDMFPHTGHVE 435
|
|
| rumA |
TIGR00479 |
23S rRNA (uracil-5-)-methyltransferase RumA; This protein family was first proposed to be RNA ... |
9-358 |
4.57e-27 |
|
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: 111.07 E-value: 4.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745595550 9 EQYEAQLAEKVVRLQSmmAPFSDlVPEVFRSPVShYRMRAEFRIWHDGDDLYHIIFDQQTKSRI-RVDSFPAASELINQL 87
Cdd:TIGR00479 82 QQQVIALLERIGKFVS--EPIED-VPTIGDDPWG-YRNKARLSLGRSPSGQLQAGFYQKGSHDIvDVKQCPVQAPALNAL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745595550 88 MTAMIAGVRNNPVLRH----KLFQIDYLTTL-----SNQAVVSLLYHKKLDDEWRQEAEALRDALRAQNLNVHLIGRATk 158
Cdd:TIGR00479 158 LPKVRAILENFGASRYlehkELGQARHGVLRigrhtGELSSVDRTALERFPHKEELDLYLQPDSPDVKSICQNINPEKT- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745595550 159 tkialDQDYIDERLPVAGKEMIYRQVE--------NSFTQPNAAMNIQMLEWALDVTKGSKGD-LLELYCGNGNFSLALA 229
Cdd:TIGR00479 237 -----NVIFGEETEVIAGEMPIYDKSGdlsftfsaRDFIQVNSGQNEKLVDRALEWLELQGEErVLDAYCGMGTFTLPLA 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745595550 230 RNFDRVLATEIAKPSVAAAQYNIAANHIDNVQIIRMAAEEF--TQAMNGVReFNrlqgidlksyqceTIFVDPPRSGLDS 307
Cdd:TIGR00479 312 KQAKSVVGVEGVPESVEKAQQNAELNGIANVTFYHGTLETVlpKQPWAGNG-FD-------------KVLLDPPRKGCAA 377
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1745595550 308 ET-EKMVQAYP-RILYISCNPETLCKNLETLSQ-THKVERLALFDQFPYTHHME 358
Cdd:TIGR00479 378 GVlRTIIKLKPeRIVYVSCNPATLARDLEALCKaGYTIARVQPVDMFPHTGHVE 431
|
|
| rumB |
PRK03522 |
23S rRNA (uracil(747)-C(5))-methyltransferase RlmC; |
187-364 |
3.76e-20 |
|
23S rRNA (uracil(747)-C(5))-methyltransferase RlmC;
Pssm-ID: 235128 [Multi-domain] Cd Length: 315 Bit Score: 89.54 E-value: 3.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745595550 187 SFTQPN----AAMNIQMLEWALDVTKGSKGDLlelYCGNGNFSLALARNFDRVLATEIAKPSVAAAQYNIAANHIDNVQI 262
Cdd:PRK03522 149 SFFQTNpavaAQLYATARDWVRELPPRSMWDL---FCGVGGFGLHCATPGMQLTGIEISAEAIACAKQSAAELGLTNVQF 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745595550 263 IRMAAEEFTQAMNGVREFnrlqgidlksyqcetIFVDPPRSGLDSE----TEKMvqAYPRILYISCNPETLCKNLETLSQ 338
Cdd:PRK03522 226 QALDSTQFATAQGEVPDL---------------VLVNPPRRGIGKElcdyLSQM--APRFILYSSCNAQTMAKDLAHLPG 288
|
170 180
....*....|....*....|....*.
gi 1745595550 339 tHKVERLALFDQFPYTHHMECGVLLT 364
Cdd:PRK03522 289 -YRIERVQLFDMFPHTAHYEVLTLLV 313
|
|
| RsmC |
COG2813 |
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ... |
211-264 |
2.95e-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: 2.95e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1745595550 211 KGDLLELYCGNGNFSLALARNFD--RVLATEIAKPSVAAAQYNIAANHIDNVQIIR 264
Cdd:COG2813 50 GGRVLDLGCGYGVIGLALAKRNPeaRVTLVDVNARAVELARANAAANGLENVEVLW 105
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
213-270 |
1.09e-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: 43.96 E-value: 1.09e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1745595550 213 DLLELYCGNGNFSLALAR-NFDRVLATEIAKPSVAAAQYNIAANHIDNVQIIRMAAEEF 270
Cdd:cd02440 1 RVLDLGCGTGALALALASgPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEEL 59
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
212-270 |
1.76e-05 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 45.29 E-value: 1.76e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745595550 212 GDLLELYCGNGNFSLALA-RNFDRVLATEIAKPSVAAAQYNIAANHIDNVQIIRMAAEEF 270
Cdd:COG0500 28 GRVLDLGCGTGRNLLALAaRFGGRVIGIDLSPEAIALARARAAKAGLGNVEFLVADLAEL 87
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
203-269 |
3.34e-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: 43.44 E-value: 3.34e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1745595550 203 ALDVTKGSKgdLLELYCGNGNFSLALARNFDRVLATEIAKPSVAAAQYNIAANHIdNVQIIRMAAEE 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 |
9.50e-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: 41.54 E-value: 9.50e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1745595550 200 LEWALDVTKGSKGDLLELYCGNGNFSLALARNFDRVLATEIAKPSVAAAQYNIAANhidNVQIIRMAAEEF 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 1745595550 215 LELYCGNGNFSLALARNFD-RVLATEIAKPSVAAAQYNIAANHIdNVQIIRMAAEEF 270
Cdd:pfam13649 2 LDLGCGTGRLTLALARRGGaRVTGVDLSPEMLERARERAAEAGL-NVEFVQGDAEDL 57
|
|
| TrmN6 |
COG4123 |
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ... |
190-274 |
3.60e-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: 41.67 E-value: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745595550 190 QPNAAMNIQM----LEWALDVTKGSKgdLLELYCGNGNFSLALARNFD--RVLATEIAKPSVAAAQYNIAANHIDN-VQI 262
Cdd:COG4123 15 QPRCGYRFGTdavlLAAFAPVKKGGR--VLDLGTGTGVIALMLAQRSPgaRITGVEIQPEAAELARRNVALNGLEDrITV 92
|
90
....*....|..
gi 1745595550 263 IRMAAEEFTQAM 274
Cdd:COG4123 93 IHGDLKEFAAEL 104
|
|
| Methyltransf_11 |
pfam08241 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
215-261 |
4.31e-04 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 462406 [Multi-domain] Cd Length: 94 Bit Score: 38.80 E-value: 4.31e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1745595550 215 LELYCGNGNFSLALARNFDRVLATEIAKPSVAAAQYNIAANHIDNVQ 261
Cdd:pfam08241 1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREGLTFVV 47
|
|
| trmB |
PRK00121 |
tRNA (guanine-N(7)-)-methyltransferase; Reviewed |
215-288 |
4.33e-03 |
|
tRNA (guanine-N(7)-)-methyltransferase; Reviewed
Pssm-ID: 234649 Cd Length: 202 Bit Score: 37.83 E-value: 4.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1745595550 215 LELYCGNGNFSLALA-----RNFdrvLATEIAKPSVAAAQYNIAANHIDNVQIIRMAAEEFTQAMngvreF--NRLQGID 287
Cdd:PRK00121 45 LEIGFGKGEFLVEMAkanpdINF---IGIEVHEPGVGKALKKIEEEGLTNLRLLCGDAVEVLLDM-----FpdGSLDRIY 116
|
.
gi 1745595550 288 L 288
Cdd:PRK00121 117 L 117
|
|
| Tam |
COG4106 |
Trans-aconitate methyltransferase [Energy production and conversion]; |
215-271 |
7.74e-03 |
|
Trans-aconitate methyltransferase [Energy production and conversion];
Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 35.57 E-value: 7.74e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1745595550 215 LELYCGNGNFSLALARNFD--RVLATEIAKPSVAAAQyniaaNHIDNVQIIRMAAEEFT 271
Cdd:COG4106 6 LDLGCGTGRLTALLAERFPgaRVTGVDLSPEMLARAR-----ARLPNVRFVVADLRDLD 59
|
|
| |
