|
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: 755.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972098 1 MTPEHLPTEQYEAQLAEKVVRLQTMMAPFAAPVPEVFRSPVSHYRMRAEFRLWHDGDDLYHIIFDQQTRSRIRVDSFPAA 80
Cdd:PRK05031 1 MTPECLPPEQYEAQLAEKVARLKELFAPFSAPEPEVFRSPPSHYRMRAEFRIWHEGDDLYYAMFDQQTKQRIRIDQFPIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972098 81 SALINQLMTAMLEGVRNNPVLRQKLFQIDYLTTLSNQAVVSLLYHKKLDDAWREQAEALRDALRaqglNVHLIGRATKTK 160
Cdd:PRK05031 81 SELINALMPALLAALRANPVLRHKLFQVDFLSTLSGEILVSLLYHKKLDEEWEQAAKALRDALF----NVHLIGRSRKQK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972098 161 IELDQDYIDERLPVGGREMIYRQVENSFTQPNAAMNIQMLEWALDVTKGATGDLLELYCGNGNFSLALARNFDRVLATEI 240
Cdd:PRK05031 157 IVLDQDYVDERLPVAGREFIYRQVENSFTQPNAAVNEKMLEWALDATKGSKGDLLELYCGNGNFTLALARNFRRVLATEI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972098 241 AKPSVAAAQYNIAANHIDNVQIIRMAAEEFTQAMNGVRQFNRLQGIDLHSYQCETIFVDPPRSGLDSETEKMVQAYPRIL 320
Cdd:PRK05031 237 SKPSVAAAQYNIAANGIDNVQIIRMSAEEFTQAMNGVREFNRLKGIDLKSYNFSTIFVDPPRAGLDDETLKLVQAYERIL 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 488972098 321 YISCNPETLCRNLETLSQTHNVTRLALFDQFPYTHHMECGVLLTRK 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: 707.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972098 10 QYEAQLAEKVVRLQTMMAPFAAPVPEVFRSPVSHYRMRAEFRLWHDGDDLYHIIFDQQTRSRIRVDSFPAASALINQLMT 89
Cdd:TIGR02143 1 QYTAQLAEKVSRLKDLFAPFDAPEPEVFESPDKHYRMRAEFRIWHEGDDLYYAMFDQQTKSKIRVDQFPAASELINRLMP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972098 90 AMLEGVRNNPVLRQKLFQIDYLTTLSNQAVVSLLYHKKLDDAWREQAEALRDalraQGLNVHLIGRATKTKIELDQDYID 169
Cdd:TIGR02143 81 ALIAALRQNPALRHKLFQVDFLTTLSGEALVSLLYHKQLDDEWRQAAEALKD----IKLNVNLIGRARKKKIVLDQDYVD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972098 170 ERLPVGGREMIYRQVENSFTQPNAAMNIQMLEWALDVTKGATGDLLELYCGNGNFSLALARNFDRVLATEIAKPSVAAAQ 249
Cdd:TIGR02143 157 ETLPVAGREFIYRQVENSFTQPNAAVNIKMLEWACEVTQGSKGDLLELYCGNGNFSLALAQNFRRVLATEIAKPSVNAAQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972098 250 YNIAANHIDNVQIIRMAAEEFTQAMNGVRQFNRLQGIDLHSYQCETIFVDPPRSGLDSETEKMVQAYPRILYISCNPETL 329
Cdd:TIGR02143 237 YNIAANNIDNVQIIRMSAEEFTQAMNGVREFRRLKGIDLKSYNCSTIFVDPPRAGLDPDTCKLVQAYERILYISCNPETL 316
|
330 340 350
....*....|....*....|....*....|....*..
gi 488972098 330 CRNLETLSQTHNVTRLALFDQFPYTHHMECGVLLTRK 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: 704.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972098 10 QYEAQLAEKVVRLQTMMAPFAAPVPEVFRSPVSHYRMRAEFRLWHDGDDLYHIIFDQQTRSRIRVDSFPAASALINQLMT 89
Cdd:pfam05958 1 QYDAQLAEKKSRLKALFAPFYAPDPEVFASPDKHYRMRAEFRIWHEGDDLYYAMFDQQTKSRIRVDQFPAASELINELMP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972098 90 AMLEGVRNNPVLRQKLFQIDYLTTLSNQAVVSLLYHKKLDDAWREQAEALRDALRAQGLNVHLIGRATKTKIELDQDYID 169
Cdd:pfam05958 81 ALIAALRQDPALRHKLFQVDFLTTLSGEALVSLLYHKQLDDEWRQAAEALRDALRAQGLDVNLIGRARKQKIVLDQDYVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972098 170 ERLPVGGREMIYRQVENSFTQPNAAMNIQMLEWALDVTKGATGDLLELYCGNGNFSLALARNFDRVLATEIAKPSVAAAQ 249
Cdd:pfam05958 161 ETLPVAGREFIYRQVENSFTQPNAAVNIKMLEWACDVTQGSKGDLLELYCGNGNFSLALARNFRKVLATEIAKPSVAAAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972098 250 YNIAANHIDNVQIIRMAAEEFTQAMNGVRQFNRLQGIDLHSYQCETIFVDPPRSGLDSETEKMVQAYPRILYISCNPETL 329
Cdd:pfam05958 241 YNIAANNIDNVQIIRMSAEEFTQAMNGVREFNRLKGIDLKSYNCSTIFVDPPRAGLDPETLKLVQAYPRILYISCNPETL 320
|
330 340 350
....*....|....*....|....*....|....*..
gi 488972098 330 CRNLETLSQTHNVTRLALFDQFPYTHHMECGVLLTRK 366
Cdd:pfam05958 321 CANLEQLSKTHRVERFALFDQFPYTHHMECGVLLEKK 357
|
|
| TrmA |
COG2265 |
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ... |
5-364 |
3.21e-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: 200.79 E-value: 3.21e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972098 5 HLPteqYEAQLAEK--VVR--LQTMMAPFAAPVPEVFRSPV-SHYRMRAEFRLWHDGDDLYHIIFDQQTRSRIRVDSFPA 79
Cdd:COG2265 80 HLS---YEAQLELKqrVVReaLERIGGLPEVEVEPIIGSPEpWGYRNRARLSVRRTDGRLRLGFYARGSHELVDIDECPL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972098 80 ASALINQLMtamlegvrnnPVLRQklfqidylttlsnqavvsllyhkklddaWREQAEALRDALRaqglnvHLIGRAtkt 159
Cdd:COG2265 157 LDPALNALL----------PALRE----------------------------LLAELGARRGELR------HLVVRA--- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972098 160 kielDQDYIDERLpvGGREMIYRqvENSFTQPNAAMNIQMLEWALDVTKGATGD-LLELYCGNGNFSLALARNFDRVLAT 238
Cdd:COG2265 190 ----GRDYLTERL--GGLTFRIS--PGSFFQVNPEQAEALYAAALEWLDLTGGErVLDLYCGVGTFALPLARRAKKVIGV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972098 239 EIAKPSVAAAQYNIAANHIDNVQIIRMAAEEFTQAMNGVRQFNrlqgidlhsyqceTIFVDPPRSGLDSET-EKMVQAYP 317
Cdd:COG2265 262 EIVPEAVEDARENARLNGLKNVEFVAGDLEEVLPELLWGGRPD-------------VVVLDPPRAGAGPEVlEALAALGP 328
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 488972098 318 -RILYISCNPETLCRNLETL-SQTHNVTRLALFDQFPYTHHMECGVLLT 364
Cdd:COG2265 329 rRIVYVSCNPATLARDLALLvEGGYRLEKVQPVDMFPHTHHVESVALLE 377
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
213-320 |
8.75e-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: 8.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972098 213 DLLELYCGNGNFSLALAR-NFDRVLATEIAKPSVAAAQYNIAANHIDNVQIIRMAAEEFtqamngvrQFNRLQGIDLhsy 291
Cdd:cd02440 1 RVLDLGCGTGALALALASgPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEEL--------PPEADESFDV--- 69
|
90 100
....*....|....*....|....*....
gi 488972098 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: 755.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972098 1 MTPEHLPTEQYEAQLAEKVVRLQTMMAPFAAPVPEVFRSPVSHYRMRAEFRLWHDGDDLYHIIFDQQTRSRIRVDSFPAA 80
Cdd:PRK05031 1 MTPECLPPEQYEAQLAEKVARLKELFAPFSAPEPEVFRSPPSHYRMRAEFRIWHEGDDLYYAMFDQQTKQRIRIDQFPIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972098 81 SALINQLMTAMLEGVRNNPVLRQKLFQIDYLTTLSNQAVVSLLYHKKLDDAWREQAEALRDALRaqglNVHLIGRATKTK 160
Cdd:PRK05031 81 SELINALMPALLAALRANPVLRHKLFQVDFLSTLSGEILVSLLYHKKLDEEWEQAAKALRDALF----NVHLIGRSRKQK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972098 161 IELDQDYIDERLPVGGREMIYRQVENSFTQPNAAMNIQMLEWALDVTKGATGDLLELYCGNGNFSLALARNFDRVLATEI 240
Cdd:PRK05031 157 IVLDQDYVDERLPVAGREFIYRQVENSFTQPNAAVNEKMLEWALDATKGSKGDLLELYCGNGNFTLALARNFRRVLATEI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972098 241 AKPSVAAAQYNIAANHIDNVQIIRMAAEEFTQAMNGVRQFNRLQGIDLHSYQCETIFVDPPRSGLDSETEKMVQAYPRIL 320
Cdd:PRK05031 237 SKPSVAAAQYNIAANGIDNVQIIRMSAEEFTQAMNGVREFNRLKGIDLKSYNFSTIFVDPPRAGLDDETLKLVQAYERIL 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 488972098 321 YISCNPETLCRNLETLSQTHNVTRLALFDQFPYTHHMECGVLLTRK 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: 707.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972098 10 QYEAQLAEKVVRLQTMMAPFAAPVPEVFRSPVSHYRMRAEFRLWHDGDDLYHIIFDQQTRSRIRVDSFPAASALINQLMT 89
Cdd:TIGR02143 1 QYTAQLAEKVSRLKDLFAPFDAPEPEVFESPDKHYRMRAEFRIWHEGDDLYYAMFDQQTKSKIRVDQFPAASELINRLMP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972098 90 AMLEGVRNNPVLRQKLFQIDYLTTLSNQAVVSLLYHKKLDDAWREQAEALRDalraQGLNVHLIGRATKTKIELDQDYID 169
Cdd:TIGR02143 81 ALIAALRQNPALRHKLFQVDFLTTLSGEALVSLLYHKQLDDEWRQAAEALKD----IKLNVNLIGRARKKKIVLDQDYVD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972098 170 ERLPVGGREMIYRQVENSFTQPNAAMNIQMLEWALDVTKGATGDLLELYCGNGNFSLALARNFDRVLATEIAKPSVAAAQ 249
Cdd:TIGR02143 157 ETLPVAGREFIYRQVENSFTQPNAAVNIKMLEWACEVTQGSKGDLLELYCGNGNFSLALAQNFRRVLATEIAKPSVNAAQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972098 250 YNIAANHIDNVQIIRMAAEEFTQAMNGVRQFNRLQGIDLHSYQCETIFVDPPRSGLDSETEKMVQAYPRILYISCNPETL 329
Cdd:TIGR02143 237 YNIAANNIDNVQIIRMSAEEFTQAMNGVREFRRLKGIDLKSYNCSTIFVDPPRAGLDPDTCKLVQAYERILYISCNPETL 316
|
330 340 350
....*....|....*....|....*....|....*..
gi 488972098 330 CRNLETLSQTHNVTRLALFDQFPYTHHMECGVLLTRK 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: 704.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972098 10 QYEAQLAEKVVRLQTMMAPFAAPVPEVFRSPVSHYRMRAEFRLWHDGDDLYHIIFDQQTRSRIRVDSFPAASALINQLMT 89
Cdd:pfam05958 1 QYDAQLAEKKSRLKALFAPFYAPDPEVFASPDKHYRMRAEFRIWHEGDDLYYAMFDQQTKSRIRVDQFPAASELINELMP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972098 90 AMLEGVRNNPVLRQKLFQIDYLTTLSNQAVVSLLYHKKLDDAWREQAEALRDALRAQGLNVHLIGRATKTKIELDQDYID 169
Cdd:pfam05958 81 ALIAALRQDPALRHKLFQVDFLTTLSGEALVSLLYHKQLDDEWRQAAEALRDALRAQGLDVNLIGRARKQKIVLDQDYVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972098 170 ERLPVGGREMIYRQVENSFTQPNAAMNIQMLEWALDVTKGATGDLLELYCGNGNFSLALARNFDRVLATEIAKPSVAAAQ 249
Cdd:pfam05958 161 ETLPVAGREFIYRQVENSFTQPNAAVNIKMLEWACDVTQGSKGDLLELYCGNGNFSLALARNFRKVLATEIAKPSVAAAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972098 250 YNIAANHIDNVQIIRMAAEEFTQAMNGVRQFNRLQGIDLHSYQCETIFVDPPRSGLDSETEKMVQAYPRILYISCNPETL 329
Cdd:pfam05958 241 YNIAANNIDNVQIIRMSAEEFTQAMNGVREFNRLKGIDLKSYNCSTIFVDPPRAGLDPETLKLVQAYPRILYISCNPETL 320
|
330 340 350
....*....|....*....|....*....|....*..
gi 488972098 330 CRNLETLSQTHNVTRLALFDQFPYTHHMECGVLLTRK 366
Cdd:pfam05958 321 CANLEQLSKTHRVERFALFDQFPYTHHMECGVLLEKK 357
|
|
| TrmA |
COG2265 |
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ... |
5-364 |
3.21e-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: 200.79 E-value: 3.21e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972098 5 HLPteqYEAQLAEK--VVR--LQTMMAPFAAPVPEVFRSPV-SHYRMRAEFRLWHDGDDLYHIIFDQQTRSRIRVDSFPA 79
Cdd:COG2265 80 HLS---YEAQLELKqrVVReaLERIGGLPEVEVEPIIGSPEpWGYRNRARLSVRRTDGRLRLGFYARGSHELVDIDECPL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972098 80 ASALINQLMtamlegvrnnPVLRQklfqidylttlsnqavvsllyhkklddaWREQAEALRDALRaqglnvHLIGRAtkt 159
Cdd:COG2265 157 LDPALNALL----------PALRE----------------------------LLAELGARRGELR------HLVVRA--- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972098 160 kielDQDYIDERLpvGGREMIYRqvENSFTQPNAAMNIQMLEWALDVTKGATGD-LLELYCGNGNFSLALARNFDRVLAT 238
Cdd:COG2265 190 ----GRDYLTERL--GGLTFRIS--PGSFFQVNPEQAEALYAAALEWLDLTGGErVLDLYCGVGTFALPLARRAKKVIGV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972098 239 EIAKPSVAAAQYNIAANHIDNVQIIRMAAEEFTQAMNGVRQFNrlqgidlhsyqceTIFVDPPRSGLDSET-EKMVQAYP 317
Cdd:COG2265 262 EIVPEAVEDARENARLNGLKNVEFVAGDLEEVLPELLWGGRPD-------------VVVLDPPRAGAGPEVlEALAALGP 328
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 488972098 318 -RILYISCNPETLCRNLETL-SQTHNVTRLALFDQFPYTHHMECGVLLT 364
Cdd:COG2265 329 rRIVYVSCNPATLARDLALLvEGGYRLEKVQPVDMFPHTHHVESVALLE 377
|
|
| rumA |
PRK13168 |
23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD; |
5-358 |
4.58e-27 |
|
23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD;
Pssm-ID: 237291 [Multi-domain] Cd Length: 443 Bit Score: 111.02 E-value: 4.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972098 5 HLPteqYEAQLAEKVVRLQTMMAPFAAPVPEVFRSPVS----HYRMRAEFRLWHDGD-DLYHIIFDQQTRSRI-RVDS-- 76
Cdd:PRK13168 93 HLS---IDAQIASKQRALEDLLKHLAGVEPEEVLPPIAgppwGYRRRARLSVRYVPKkGQLLVGFREKNSSDIvDIDQcp 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972098 77 --FPAASALINQLmTAMLEGVRNnpvlRQKLFQIDYltTLSNQAVVSLLYH-KKLDDAWREqaeALRDALRAQGLNVHLI 153
Cdd:PRK13168 170 vlVPPLSALLPPL-RALLSSLSA----KRRLGHVEL--AQGDNGTALVLRHlEPLSEADRA---KLRAFAEQHGLQLYLQ 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972098 154 GRATKTKIELDQDY--IDERLPVGGREMIYRqvENSFTQPNAAMNIQM----LEWaLDVTKGatgD-LLELYCGNGNFSL 226
Cdd:PRK13168 240 PKGPDLVHLLGPADaqLSYYLPEFGLRLAFS--PRDFIQVNAQVNQKMvaraLEW-LDPQPG---DrVLDLFCGLGNFTL 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972098 227 ALARNFDRVLATEIAKPSVAAAQYNIAANHIDNVQiirMAAEEFTQAMngVRQFNRLQGIDLhsyqcetIFVDPPRSG-- 304
Cdd:PRK13168 314 PLARQAAEVVGVEGVEAMVERARENARRNGLDNVT---FYHANLEEDF--TDQPWALGGFDK-------VLLDPPRAGaa 381
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 488972098 305 --LDSETEKMVQaypRILYISCNPETLCRNLETL-SQTHNVTRLALFDQFPYTHHME 358
Cdd:PRK13168 382 evMQALAKLGPK---RIVYVSCNPATLARDAGVLvEAGYRLKRAGMLDMFPHTGHVE 435
|
|
| rumA |
TIGR00479 |
23S rRNA (uracil-5-)-methyltransferase RumA; This protein family was first proposed to be RNA ... |
9-358 |
5.78e-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: 110.68 E-value: 5.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972098 9 EQYEAQLAEKVVRLQTMMApfaAPVPEVFRSPVShYRMRAEFRLWHDGDDLYHIIFDQQTRSRI-RVDSFPAASALINQL 87
Cdd:TIGR00479 82 QQQVIALLERIGKFVSEPI---EDVPTIGDDPWG-YRNKARLSLGRSPSGQLQAGFYQKGSHDIvDVKQCPVQAPALNAL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972098 88 MTAMLEGVRNNPVLRQ----KLFQIDYLTTL-----SNQAVVSLLYHKKLDDAwREQAEALRDALRAQGLNVHLIGRATK 158
Cdd:TIGR00479 158 LPKVRAILENFGASRYlehkELGQARHGVLRigrhtGELSSVDRTALERFPHK-EELDLYLQPDSPDVKSICQNINPEKT 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972098 159 TKIeldqdYIDERLPVGGREMIYRQVE--------NSFTQPNAAMNIQMLEWALDVTKGATGD-LLELYCGNGNFSLALA 229
Cdd:TIGR00479 237 NVI-----FGEETEVIAGEMPIYDKSGdlsftfsaRDFIQVNSGQNEKLVDRALEWLELQGEErVLDAYCGMGTFTLPLA 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972098 230 RNFDRVLATEIAKPSVAAAQYNIAANHIDNVQIIRMAAEEFTqamngVRQFNRLQGIDlhsyqceTIFVDPPRSGLDSET 309
Cdd:TIGR00479 312 KQAKSVVGVEGVPESVEKAQQNAELNGIANVTFYHGTLETVL-----PKQPWAGNGFD-------KVLLDPPRKGCAAGV 379
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 488972098 310 -EKMVQAYP-RILYISCNPETLCRNLETLSQ-THNVTRLALFDQFPYTHHME 358
Cdd:TIGR00479 380 lRTIIKLKPeRIVYVSCNPATLARDLEALCKaGYTIARVQPVDMFPHTGHVE 431
|
|
| rumB |
PRK03522 |
23S rRNA (uracil(747)-C(5))-methyltransferase RlmC; |
187-366 |
4.52e-20 |
|
23S rRNA (uracil(747)-C(5))-methyltransferase RlmC;
Pssm-ID: 235128 [Multi-domain] Cd Length: 315 Bit Score: 89.54 E-value: 4.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972098 187 SFTQPN----AAMNIQMLEWALDVtkgATGDLLELYCGNGNFSLALARNFDRVLATEIAKPSVAAAQYNIAANHIDNVQI 262
Cdd:PRK03522 149 SFFQTNpavaAQLYATARDWVREL---PPRSMWDLFCGVGGFGLHCATPGMQLTGIEISAEAIACAKQSAAELGLTNVQF 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972098 263 IRMAAEEFTQAMNGVRqfnrlqgiDLhsyqcetIFVDPPRSGLDSE----TEKMvqAYPRILYISCNPETLCRNLETLSQ 338
Cdd:PRK03522 226 QALDSTQFATAQGEVP--------DL-------VLVNPPRRGIGKElcdyLSQM--APRFILYSSCNAQTMAKDLAHLPG 288
|
170 180
....*....|....*....|....*...
gi 488972098 339 THnVTRLALFDQFPYTHHMECGVLLTRK 366
Cdd:PRK03522 289 YR-IERVQLFDMFPHTAHYEVLTLLVRQ 315
|
|
| RsmC |
COG2813 |
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ... |
210-264 |
3.83e-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: 3.83e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 488972098 210 ATGDLLELYCGNGNFSLALARNFD--RVLATEIAKPSVAAAQYNIAANHIDNVQIIR 264
Cdd:COG2813 49 LGGRVLDLGCGYGVIGLALAKRNPeaRVTLVDVNARAVELARANAAANGLENVEVLW 105
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
213-320 |
8.75e-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: 8.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972098 213 DLLELYCGNGNFSLALAR-NFDRVLATEIAKPSVAAAQYNIAANHIDNVQIIRMAAEEFtqamngvrQFNRLQGIDLhsy 291
Cdd:cd02440 1 RVLDLGCGTGALALALASgPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEEL--------PPEADESFDV--- 69
|
90 100
....*....|....*....|....*....
gi 488972098 292 qcetIFVDPPRSGLDSETEKMVQAYPRIL 320
Cdd:cd02440 70 ----IISDPPLHHLVEDLARFLEEARRLL 94
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
186-270 |
2.12e-05 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 44.91 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972098 186 NSFTQPNAAMNIQMLEwaldvTKGATGDLLELYCGNGNFSLALA-RNFDRVLATEIAKPSVAAAQYNIAANHIDNVQIIR 264
Cdd:COG0500 7 SDELLPGLAALLALLE-----RLPKGGRVLDLGCGTGRNLLALAaRFGGRVIGIDLSPEAIALARARAAKAGLGNVEFLV 81
|
....*.
gi 488972098 265 MAAEEF 270
Cdd:COG0500 82 ADLAEL 87
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
203-269 |
4.05e-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: 43.06 E-value: 4.05e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488972098 203 ALDVTKGATgdLLELYCGNGNFSLALARNFDRVLATEIAKPSVAAAQYNIAANHIdNVQIIRMAAEE 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 |
1.40e-04 |
|
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: 41.16 E-value: 1.40e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488972098 200 LEWALDVTKGATGDLLELYCGNGNFSLALARNFDRVLATEIAKPSVAAAQYNIAANhidNVQIIRMAAEEF 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 488972098 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 |
4.71e-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: 4.71e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 488972098 215 LELYCGNGNFSLALARNFDRVLATEIAKPSVAAAQYNIAANHIDNVQ 261
Cdd:pfam08241 1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREGLTFVV 47
|
|
| TrmN6 |
COG4123 |
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ... |
190-274 |
5.33e-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: 5.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972098 190 QPNAAMNIQM----LEWALDVTKGATgdLLELYCGNGNFSLALARNFD--RVLATEIAKPSVAAAQYNIAANHIDN-VQI 262
Cdd:COG4123 15 QPRCGYRFGTdavlLAAFAPVKKGGR--VLDLGTGTGVIALMLAQRSPgaRITGVEIQPEAAELARRNVALNGLEDrITV 92
|
90
....*....|..
gi 488972098 263 IRMAAEEFTQAM 274
Cdd:COG4123 93 IHGDLKEFAAEL 104
|
|
| trmB |
PRK00121 |
tRNA (guanine-N(7)-)-methyltransferase; Reviewed |
215-288 |
4.37e-03 |
|
tRNA (guanine-N(7)-)-methyltransferase; Reviewed
Pssm-ID: 234649 Cd Length: 202 Bit Score: 37.83 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972098 215 LELYCGNGNFSLALA-----RNFdrvLATEIAKPSVAAAQYNIAANHIDNVQIIRMAAEEFTQAMngvrqF--NRLQGID 287
Cdd:PRK00121 45 LEIGFGKGEFLVEMAkanpdINF---IGIEVHEPGVGKALKKIEEEGLTNLRLLCGDAVEVLLDM-----FpdGSLDRIY 116
|
.
gi 488972098 288 L 288
Cdd:PRK00121 117 L 117
|
|
| |
