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Conserved domains on  [gi|16130692|ref|NP_417265|]
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23S rRNA m(5)U1939 methyltransferase [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD( domain architecture ID 11486451)

23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD catalyzes the formation of 5-methyl-uridine at position 1939 (m5U1939) in 23S rRNA

EC:  2.1.1.190
Gene Ontology:  GO:0003723|GO:0070475

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
rumA PRK13168
23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD;
2-431 0e+00

23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD;


:

Pssm-ID: 237291 [Multi-domain]  Cd Length: 443  Bit Score: 792.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692    2 AQFYSAKRRTTTRQIITVSVNDLDSFGQGVARHNGKTLFIPGLLPQENAEVTVTEDKKQYARAKVVRRLSDSPERETPRC 81
Cdd:PRK13168   1 AQFYSPKRRVTTRQIITVTIESLDHDGRGVARHNGKTVFIEGALPGERVEVQVTEDKKQYARAKVVRILKPSPERVTPRC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692   82 PHFGVCGGCQQQHASVDLQQRSKSAALARLMKH-------DVSEVIADVPWGYRRRARLSLNYLPKTQQLQMGFRKAGSS 154
Cdd:PRK13168  81 PHFGVCGGCQLQHLSIDAQIASKQRALEDLLKHlagvepeEVLPPIAGPPWGYRRRARLSVRYVPKKGQLLVGFREKNSS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692  155 DIVDVKQCPILAPQLEALLPKVRACLGSLQAMRHLGHVELVQATSGTLMILRHTAPLSSADREKLERFSHSEGLDLYLAP 234
Cdd:PRK13168 161 DIVDIDQCPVLVPPLSALLPPLRALLSSLSAKRRLGHVELAQGDNGTALVLRHLEPLSEADRAKLRAFAEQHGLQLYLQP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692  235 DSEILETVSGEM-----PWYDSNGLRLTFSPRDFIQVNAGVNQKMVARALEWLDVQPEDRVLDLFCGMGNFTLPLATQAA 309
Cdd:PRK13168 241 KGPDLVHLLGPAdaqlsYYLPEFGLRLAFSPRDFIQVNAQVNQKMVARALEWLDPQPGDRVLDLFCGLGNFTLPLARQAA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692  310 SVVGVEGVPALVEKGQQNARLNGLQNVTFYHENLEEDVTKQPWAKNGFDKVLLDPARAGAAGVMQQIIKLEPIRIVYVSC 389
Cdd:PRK13168 321 EVVGVEGVEAMVERARENARRNGLDNVTFYHANLEEDFTDQPWALGGFDKVLLDPPRAGAAEVMQALAKLGPKRIVYVSC 400
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 16130692  390 NPATLARDSEALLKAGYTIARLAMLDMFPHTGHLESMVLFSR 431
Cdd:PRK13168 401 NPATLARDAGVLVEAGYRLKRAGMLDMFPHTGHVESMALFER 442
 
Name Accession Description Interval E-value
rumA PRK13168
23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD;
2-431 0e+00

23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD;


Pssm-ID: 237291 [Multi-domain]  Cd Length: 443  Bit Score: 792.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692    2 AQFYSAKRRTTTRQIITVSVNDLDSFGQGVARHNGKTLFIPGLLPQENAEVTVTEDKKQYARAKVVRRLSDSPERETPRC 81
Cdd:PRK13168   1 AQFYSPKRRVTTRQIITVTIESLDHDGRGVARHNGKTVFIEGALPGERVEVQVTEDKKQYARAKVVRILKPSPERVTPRC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692   82 PHFGVCGGCQQQHASVDLQQRSKSAALARLMKH-------DVSEVIADVPWGYRRRARLSLNYLPKTQQLQMGFRKAGSS 154
Cdd:PRK13168  81 PHFGVCGGCQLQHLSIDAQIASKQRALEDLLKHlagvepeEVLPPIAGPPWGYRRRARLSVRYVPKKGQLLVGFREKNSS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692  155 DIVDVKQCPILAPQLEALLPKVRACLGSLQAMRHLGHVELVQATSGTLMILRHTAPLSSADREKLERFSHSEGLDLYLAP 234
Cdd:PRK13168 161 DIVDIDQCPVLVPPLSALLPPLRALLSSLSAKRRLGHVELAQGDNGTALVLRHLEPLSEADRAKLRAFAEQHGLQLYLQP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692  235 DSEILETVSGEM-----PWYDSNGLRLTFSPRDFIQVNAGVNQKMVARALEWLDVQPEDRVLDLFCGMGNFTLPLATQAA 309
Cdd:PRK13168 241 KGPDLVHLLGPAdaqlsYYLPEFGLRLAFSPRDFIQVNAQVNQKMVARALEWLDPQPGDRVLDLFCGLGNFTLPLARQAA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692  310 SVVGVEGVPALVEKGQQNARLNGLQNVTFYHENLEEDVTKQPWAKNGFDKVLLDPARAGAAGVMQQIIKLEPIRIVYVSC 389
Cdd:PRK13168 321 EVVGVEGVEAMVERARENARRNGLDNVTFYHANLEEDFTDQPWALGGFDKVLLDPPRAGAAEVMQALAKLGPKRIVYVSC 400
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 16130692  390 NPATLARDSEALLKAGYTIARLAMLDMFPHTGHLESMVLFSR 431
Cdd:PRK13168 401 NPATLARDAGVLVEAGYRLKRAGMLDMFPHTGHVESMALFER 442
rumA TIGR00479
23S rRNA (uracil-5-)-methyltransferase RumA; This protein family was first proposed to be RNA ...
24-424 0e+00

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: 634.55  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692    24 LDSFGQGVARHNGKTLFIPGLLPQENAEVTVTEDKKQYARAKVVRRLSDSPERETPRCPHFGVCGGCQQQHASVDLQQRS 103
Cdd:TIGR00479   1 LDHQGEGVARFNGKTVFVPGALPGEKAEVRVTEVKKQYARARVKKILEDSPERTTPPCPHFGQCGGCQLQHLSYELQLRS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692   104 KS---AALARLMKHDVSEVIADVP------WGYRRRARLSLNYLPKTQqLQMGFRKAGSSDIVDVKQCPILAPQLEALLP 174
Cdd:TIGR00479  81 KQqqvIALLERIGKFVSEPIEDVPtigddpWGYRNKARLSLGRSPSGQ-LQAGFYQKGSHDIVDVKQCPVQAPALNALLP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692   175 KVRACLGSLQAMRHLGHVELVQATSGTLMILRHTAPLSSADREKLERFSHSEGLDLYLAPDS------------------ 236
Cdd:TIGR00479 160 KVRAILENFGASRYLEHKELGQARHGVLRIGRHTGELSSVDRTALERFPHKEELDLYLQPDSpdvksicqninpektnvi 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692   237 --EILETVSGEMPWYD-SNGLRLTFSPRDFIQVNAGVNQKMVARALEWLDVQPEDRVLDLFCGMGNFTLPLATQAASVVG 313
Cdd:TIGR00479 240 fgEETEVIAGEMPIYDkSGDLSFTFSARDFIQVNSGQNEKLVDRALEWLELQGEERVLDAYCGMGTFTLPLAKQAKSVVG 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692   314 VEGVPALVEKGQQNARLNGLQNVTFYHENLEEDVTKQPWAKNGFDKVLLDPARAG-AAGVMQQIIKLEPIRIVYVSCNPA 392
Cdd:TIGR00479 320 VEGVPESVEKAQQNAELNGIANVTFYHGTLETVLPKQPWAGNGFDKVLLDPPRKGcAAGVLRTIIKLKPERIVYVSCNPA 399
                         410       420       430
                  ....*....|....*....|....*....|..
gi 16130692   393 TLARDSEALLKAGYTIARLAMLDMFPHTGHLE 424
Cdd:TIGR00479 400 TLARDLEALCKAGYTIARVQPVDMFPHTGHVE 431
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
15-430 1.57e-163

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: 465.03  E-value: 1.57e-163
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692  15 QIITVSVNDLDSFGQGVARHNGKTLFIPGLLPQENAEVTVTEDKKQYARAKVVRRLSDSPERETPRCPHFGVCGGCQQQH 94
Cdd:COG2265   1 EILELTIEDLAHGGDGVARHDGKVVFVPGALPGERVRVRVTKVKKSFARAKLVEVLEPSPDRVEPPCPHFGRCGGCQLQH 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692  95 ASVDLQQRSKSAALARLMKH-------DVSEVI-ADVPWGYRRRARLSLNYlpKTQQLQMGFRKAGSSDIVDVKQCPILA 166
Cdd:COG2265  81 LSYEAQLELKQRVVREALERigglpevEVEPIIgSPEPWGYRNRARLSVRR--TDGRLRLGFYARGSHELVDIDECPLLD 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692 167 PQLEALLPKVRACLGSLQAMR-HLGHVELvqatsgtlmilrhtaplssadreklerfshsegldlyLAPDSEILETVsge 245
Cdd:COG2265 159 PALNALLPALRELLAELGARRgELRHLVV-------------------------------------RAGRDYLTERL--- 198
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692 246 mpwydsNGLRLTFSPRDFIQVNAGVNQKMVARALEWLDVQPEDRVLDLFCGMGNFTLPLATQAASVVGVEGVPALVEKGQ 325
Cdd:COG2265 199 ------GGLTFRISPGSFFQVNPEQAEALYAAALEWLDLTGGERVLDLYCGVGTFALPLARRAKKVIGVEIVPEAVEDAR 272
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692 326 QNARLNGLQNVTFYHENLEEDVTKQPWaKNGFDKVLLDPARAGA-AGVMQQIIKLEPIRIVYVSCNPATLARDSEALLKA 404
Cdd:COG2265 273 ENARLNGLKNVEFVAGDLEEVLPELLW-GGRPDVVVLDPPRAGAgPEVLEALAALGPRRIVYVSCNPATLARDLALLVEG 351
                       410       420
                ....*....|....*....|....*.
gi 16130692 405 GYTIARLAMLDMFPHTGHLESMVLFS 430
Cdd:COG2265 352 GYRLEKVQPVDMFPHTHHVESVALLE 377
tRNA_U5-meth_tr pfam05958
tRNA (Uracil-5-)-methyltransferase; This family consists of (Uracil-5-)-methyltransferases EC: ...
98-432 9.92e-30

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: 118.31  E-value: 9.92e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692    98 DLQQRSKSAALARLMKH---DVSEVIADVPWGYRRRARLSLNYLPKTQQLQMgFRKAGSSDIVdVKQCPILAPQLEALLP 174
Cdd:pfam05958   3 DAQLAEKKSRLKALFAPfyaPDPEVFASPDKHYRMRAEFRIWHEGDDLYYAM-FDQQTKSRIR-VDQFPAASELINELMP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692   175 KVRACLGSLQAMRH-LGHVELVQATSGTLMI-LRHTAPLSSADREKLERFS---HSEGLDLYLAPDSE----ILET--VS 243
Cdd:pfam05958  81 ALIAALRQDPALRHkLFQVDFLTTLSGEALVsLLYHKQLDDEWRQAAEALRdalRAQGLDVNLIGRARkqkiVLDQdyVD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692   244 GEMPWYDSNgLRLTFSPRDFIQVNAGVNQKMVARALEWLDVQPEDrVLDLFCGMGNFTLPLATQAASVVGVEGVPALVEK 323
Cdd:pfam05958 161 ETLPVAGRE-FIYRQVENSFTQPNAAVNIKMLEWACDVTQGSKGD-LLELYCGNGNFSLALARNFRKVLATEIAKPSVAA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692   324 GQQNARLNGLQNVTFYHENLEEdVTKqpwAKNG----------------FDKVLLDPARAGAAGVMQQIIKLEPiRIVYV 387
Cdd:pfam05958 239 AQYNIAANNIDNVQIIRMSAEE-FTQ---AMNGvrefnrlkgidlksynCSTIFVDPPRAGLDPETLKLVQAYP-RILYI 313
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 16130692   388 SCNPATLARDSEALLKAgYTIARLAMLDMFPHTGHLESMVLFSRV 432
Cdd:pfam05958 314 SCNPETLCANLEQLSKT-HRVERFALFDQFPYTHHMECGVLLEKK 357
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
289-378 9.32e-14

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: 67.07  E-value: 9.32e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692 289 RVLDLFCGMGNFTLPLA-TQAASVVGVEGVPALVEKGQQNARLNGLQNVTFYHENLEEDvtkQPWAKNGFDKVLLDPARA 367
Cdd:cd02440   1 RVLDLGCGTGALALALAsGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEEL---PPEADESFDVIISDPPLH 77
                        90
                ....*....|.
gi 16130692 368 GAAGVMQQIIK 378
Cdd:cd02440  78 HLVEDLARFLE 88
rADc smart00650
Ribosomal RNA adenine dimethylases;
274-360 2.03e-07

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 50.59  E-value: 2.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692    274 MVARALEWLDVQPEDRVLDLFCGMGNFTLPLATQAASVVGVEGVPALVEKgqqnarlngLQNVTFYHENLE---EDVTKQ 350
Cdd:smart00650   1 VIDKIVRAANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRLAPR---------LREKFAAADNLTvihGDALKF 71
                           90
                   ....*....|
gi 16130692    351 PWAKNGFDKV 360
Cdd:smart00650  72 DLPKLQPYKV 81
 
Name Accession Description Interval E-value
rumA PRK13168
23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD;
2-431 0e+00

23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD;


Pssm-ID: 237291 [Multi-domain]  Cd Length: 443  Bit Score: 792.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692    2 AQFYSAKRRTTTRQIITVSVNDLDSFGQGVARHNGKTLFIPGLLPQENAEVTVTEDKKQYARAKVVRRLSDSPERETPRC 81
Cdd:PRK13168   1 AQFYSPKRRVTTRQIITVTIESLDHDGRGVARHNGKTVFIEGALPGERVEVQVTEDKKQYARAKVVRILKPSPERVTPRC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692   82 PHFGVCGGCQQQHASVDLQQRSKSAALARLMKH-------DVSEVIADVPWGYRRRARLSLNYLPKTQQLQMGFRKAGSS 154
Cdd:PRK13168  81 PHFGVCGGCQLQHLSIDAQIASKQRALEDLLKHlagvepeEVLPPIAGPPWGYRRRARLSVRYVPKKGQLLVGFREKNSS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692  155 DIVDVKQCPILAPQLEALLPKVRACLGSLQAMRHLGHVELVQATSGTLMILRHTAPLSSADREKLERFSHSEGLDLYLAP 234
Cdd:PRK13168 161 DIVDIDQCPVLVPPLSALLPPLRALLSSLSAKRRLGHVELAQGDNGTALVLRHLEPLSEADRAKLRAFAEQHGLQLYLQP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692  235 DSEILETVSGEM-----PWYDSNGLRLTFSPRDFIQVNAGVNQKMVARALEWLDVQPEDRVLDLFCGMGNFTLPLATQAA 309
Cdd:PRK13168 241 KGPDLVHLLGPAdaqlsYYLPEFGLRLAFSPRDFIQVNAQVNQKMVARALEWLDPQPGDRVLDLFCGLGNFTLPLARQAA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692  310 SVVGVEGVPALVEKGQQNARLNGLQNVTFYHENLEEDVTKQPWAKNGFDKVLLDPARAGAAGVMQQIIKLEPIRIVYVSC 389
Cdd:PRK13168 321 EVVGVEGVEAMVERARENARRNGLDNVTFYHANLEEDFTDQPWALGGFDKVLLDPPRAGAAEVMQALAKLGPKRIVYVSC 400
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 16130692  390 NPATLARDSEALLKAGYTIARLAMLDMFPHTGHLESMVLFSR 431
Cdd:PRK13168 401 NPATLARDAGVLVEAGYRLKRAGMLDMFPHTGHVESMALFER 442
rumA TIGR00479
23S rRNA (uracil-5-)-methyltransferase RumA; This protein family was first proposed to be RNA ...
24-424 0e+00

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: 634.55  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692    24 LDSFGQGVARHNGKTLFIPGLLPQENAEVTVTEDKKQYARAKVVRRLSDSPERETPRCPHFGVCGGCQQQHASVDLQQRS 103
Cdd:TIGR00479   1 LDHQGEGVARFNGKTVFVPGALPGEKAEVRVTEVKKQYARARVKKILEDSPERTTPPCPHFGQCGGCQLQHLSYELQLRS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692   104 KS---AALARLMKHDVSEVIADVP------WGYRRRARLSLNYLPKTQqLQMGFRKAGSSDIVDVKQCPILAPQLEALLP 174
Cdd:TIGR00479  81 KQqqvIALLERIGKFVSEPIEDVPtigddpWGYRNKARLSLGRSPSGQ-LQAGFYQKGSHDIVDVKQCPVQAPALNALLP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692   175 KVRACLGSLQAMRHLGHVELVQATSGTLMILRHTAPLSSADREKLERFSHSEGLDLYLAPDS------------------ 236
Cdd:TIGR00479 160 KVRAILENFGASRYLEHKELGQARHGVLRIGRHTGELSSVDRTALERFPHKEELDLYLQPDSpdvksicqninpektnvi 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692   237 --EILETVSGEMPWYD-SNGLRLTFSPRDFIQVNAGVNQKMVARALEWLDVQPEDRVLDLFCGMGNFTLPLATQAASVVG 313
Cdd:TIGR00479 240 fgEETEVIAGEMPIYDkSGDLSFTFSARDFIQVNSGQNEKLVDRALEWLELQGEERVLDAYCGMGTFTLPLAKQAKSVVG 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692   314 VEGVPALVEKGQQNARLNGLQNVTFYHENLEEDVTKQPWAKNGFDKVLLDPARAG-AAGVMQQIIKLEPIRIVYVSCNPA 392
Cdd:TIGR00479 320 VEGVPESVEKAQQNAELNGIANVTFYHGTLETVLPKQPWAGNGFDKVLLDPPRKGcAAGVLRTIIKLKPERIVYVSCNPA 399
                         410       420       430
                  ....*....|....*....|....*....|..
gi 16130692   393 TLARDSEALLKAGYTIARLAMLDMFPHTGHLE 424
Cdd:TIGR00479 400 TLARDLEALCKAGYTIARVQPVDMFPHTGHVE 431
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
15-430 1.57e-163

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: 465.03  E-value: 1.57e-163
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692  15 QIITVSVNDLDSFGQGVARHNGKTLFIPGLLPQENAEVTVTEDKKQYARAKVVRRLSDSPERETPRCPHFGVCGGCQQQH 94
Cdd:COG2265   1 EILELTIEDLAHGGDGVARHDGKVVFVPGALPGERVRVRVTKVKKSFARAKLVEVLEPSPDRVEPPCPHFGRCGGCQLQH 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692  95 ASVDLQQRSKSAALARLMKH-------DVSEVI-ADVPWGYRRRARLSLNYlpKTQQLQMGFRKAGSSDIVDVKQCPILA 166
Cdd:COG2265  81 LSYEAQLELKQRVVREALERigglpevEVEPIIgSPEPWGYRNRARLSVRR--TDGRLRLGFYARGSHELVDIDECPLLD 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692 167 PQLEALLPKVRACLGSLQAMR-HLGHVELvqatsgtlmilrhtaplssadreklerfshsegldlyLAPDSEILETVsge 245
Cdd:COG2265 159 PALNALLPALRELLAELGARRgELRHLVV-------------------------------------RAGRDYLTERL--- 198
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692 246 mpwydsNGLRLTFSPRDFIQVNAGVNQKMVARALEWLDVQPEDRVLDLFCGMGNFTLPLATQAASVVGVEGVPALVEKGQ 325
Cdd:COG2265 199 ------GGLTFRISPGSFFQVNPEQAEALYAAALEWLDLTGGERVLDLYCGVGTFALPLARRAKKVIGVEIVPEAVEDAR 272
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692 326 QNARLNGLQNVTFYHENLEEDVTKQPWaKNGFDKVLLDPARAGA-AGVMQQIIKLEPIRIVYVSCNPATLARDSEALLKA 404
Cdd:COG2265 273 ENARLNGLKNVEFVAGDLEEVLPELLW-GGRPDVVVLDPPRAGAgPEVLEALAALGPRRIVYVSCNPATLARDLALLVEG 351
                       410       420
                ....*....|....*....|....*.
gi 16130692 405 GYTIARLAMLDMFPHTGHLESMVLFS 430
Cdd:COG2265 352 GYRLEKVQPVDMFPHTHHVESVALLE 377
PRK05031 PRK05031
tRNA (uracil-5-)-methyltransferase; Validated
87-431 2.46e-37

tRNA (uracil-5-)-methyltransferase; Validated


Pssm-ID: 235332  Cd Length: 362  Bit Score: 139.19  E-value: 2.46e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692   87 CGGCQQQHASVDLQQRSKSAALARLMKH---DVSEVIADVPWGYRRRA--RL-----SLNYLpktqqlqMgFRKaGSSDI 156
Cdd:PRK05031   1 MTPECLPPEQYEAQLAEKVARLKELFAPfsaPEPEVFRSPPSHYRMRAefRIwhegdDLYYA-------M-FDQ-QTKQR 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692  157 VDVKQCPILAPQLEALLPKVRACLGSLQAMRH-LGHVELVQATSGTLMI--LRHTaPLSSADREKLERFSHS-EGLDL-- 230
Cdd:PRK05031  72 IRIDQFPIASELINALMPALLAALRANPVLRHkLFQVDFLSTLSGEILVslLYHK-KLDEEWEQAAKALRDAlFNVHLig 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692  231 ------YLAPDSEILETVsgempwyDSNGLRLTFSPRD--FIQVNAGVNQKMvaraLEW-LDV--QPEDRVLDLFCGMGN 299
Cdd:PRK05031 151 rsrkqkIVLDQDYVDERL-------PVAGREFIYRQVEnsFTQPNAAVNEKM----LEWaLDAtkGSKGDLLELYCGNGN 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692  300 FTLPLATQAASVVGVEGVPALVEKGQQNARLNGLQNVTFYHENLEEdVTKqpwAKNG----------------FDKVLLD 363
Cdd:PRK05031 220 FTLALARNFRRVLATEISKPSVAAAQYNIAANGIDNVQIIRMSAEE-FTQ---AMNGvrefnrlkgidlksynFSTIFVD 295
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130692  364 PARAGA-AGVMQQIIKLEpiRIVYVSCNPATLARDSEALLKaGYTIARLAMLDMFPHTGHLESMVLFSR 431
Cdd:PRK05031 296 PPRAGLdDETLKLVQAYE--RILYISCNPETLCENLETLSQ-THKVERFALFDQFPYTHHMECGVLLEK 361
rumB PRK03522
23S rRNA (uracil(747)-C(5))-methyltransferase RlmC;
157-431 4.52e-31

23S rRNA (uracil(747)-C(5))-methyltransferase RlmC;


Pssm-ID: 235128 [Multi-domain]  Cd Length: 315  Bit Score: 121.13  E-value: 4.52e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692  157 VDVKQCPILAPQLEALLPKVRACLGSLQ------AMRH--LGHVELVQAT-SGTLM---ILRHTAPLSSADREK---LER 221
Cdd:PRK03522  22 VDLCDCPLYPASFAPVFAALKPFIARAGltpynvARKRgeLKYILLTESQsDGELMlrfVLRSETKLARLRRALpwlQAQ 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692  222 FSHSEGLDLYLAP--------DSEIL--ETVSGEMPWydsNGLRLTFSPRDFIQVNAGVNQKMVARALEWLDVQPEDRVL 291
Cdd:PRK03522 102 LPQLKVISVNIQPvhmailegEEEIFltEQQALPERF---NGVPLFIRPQSFFQTNPAVAAQLYATARDWVRELPPRSMW 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692  292 DLFCGMGNFTLPLATQAASVVGVEGVPALVEKGQQNARLNGLQNVTFyhenLEEDVTKqpWAKNGFDK---VLLDPARAG 368
Cdd:PRK03522 179 DLFCGVGGFGLHCATPGMQLTGIEISAEAIACAKQSAAELGLTNVQF----QALDSTQ--FATAQGEVpdlVLVNPPRRG 252
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130692  369 -AAGVMQQIIKLEPIRIVYVSCNPATLARDSEALlkAGYTIARLAMLDMFPHTGHLESMVLFSR 431
Cdd:PRK03522 253 iGKELCDYLSQMAPRFILYSSCNAQTMAKDLAHL--PGYRIERVQLFDMFPHTAHYEVLTLLVR 314
tRNA_U5-meth_tr pfam05958
tRNA (Uracil-5-)-methyltransferase; This family consists of (Uracil-5-)-methyltransferases EC: ...
98-432 9.92e-30

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: 118.31  E-value: 9.92e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692    98 DLQQRSKSAALARLMKH---DVSEVIADVPWGYRRRARLSLNYLPKTQQLQMgFRKAGSSDIVdVKQCPILAPQLEALLP 174
Cdd:pfam05958   3 DAQLAEKKSRLKALFAPfyaPDPEVFASPDKHYRMRAEFRIWHEGDDLYYAM-FDQQTKSRIR-VDQFPAASELINELMP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692   175 KVRACLGSLQAMRH-LGHVELVQATSGTLMI-LRHTAPLSSADREKLERFS---HSEGLDLYLAPDSE----ILET--VS 243
Cdd:pfam05958  81 ALIAALRQDPALRHkLFQVDFLTTLSGEALVsLLYHKQLDDEWRQAAEALRdalRAQGLDVNLIGRARkqkiVLDQdyVD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692   244 GEMPWYDSNgLRLTFSPRDFIQVNAGVNQKMVARALEWLDVQPEDrVLDLFCGMGNFTLPLATQAASVVGVEGVPALVEK 323
Cdd:pfam05958 161 ETLPVAGRE-FIYRQVENSFTQPNAAVNIKMLEWACDVTQGSKGD-LLELYCGNGNFSLALARNFRKVLATEIAKPSVAA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692   324 GQQNARLNGLQNVTFYHENLEEdVTKqpwAKNG----------------FDKVLLDPARAGAAGVMQQIIKLEPiRIVYV 387
Cdd:pfam05958 239 AQYNIAANNIDNVQIIRMSAEE-FTQ---AMNGvrefnrlkgidlksynCSTIFVDPPRAGLDPETLKLVQAYP-RILYI 313
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 16130692   388 SCNPATLARDSEALLKAgYTIARLAMLDMFPHTGHLESMVLFSRV 432
Cdd:pfam05958 314 SCNPETLCANLEQLSKT-HRVERFALFDQFPYTHHMECGVLLEKK 357
meth_trns_rumB TIGR02085
23S rRNA (uracil-5-)-methyltransferase RumB; This family consists of RNA methyltransferases ...
85-431 7.77e-28

23S rRNA (uracil-5-)-methyltransferase RumB; This family consists of RNA methyltransferases designated RumB, formerly YbjF. Members act on 23S rRNA U747 and the equivalent position in other proteobacterial species. This family is homologous to the other 23S rRNA methyltransferase RumA and to the tRNA methyltransferase TrmA. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 131140  Cd Length: 374  Bit Score: 113.40  E-value: 7.77e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692    85 GVCGGCQQQHASVDLQQRSKSAALARLM--KHDVSEVIADV---PWGYRRRARLSLNYLPKTQQLQMGFRKAGSSDIVDv 159
Cdd:TIGR02085   8 GRCRSCQWLAQPYSEQLTNKQQHLKELLapNATVVQWLAPVtsaEQAFRNKAKMVVSGSVERPILGILHRDGTPLDLCD- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692   160 kqCPILAPQLEALLPKV-----RACLGSLQAMRHLGHVELVQAT----SGTLM---ILRHTAPLSSADREK---LERFSH 224
Cdd:TIGR02085  87 --CPLYPQSFQPVFAYLknfiaRAGLTPYNVAKKKGELKFILLTesenSGQLMlrfVLRSETKLAQIRRALpwlIEQLPQ 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692   225 SEGLDLYLAP--------DSEILETVSGEMPwYDSNGLRLTFSPRDFIQVNAGVNQKMVARALEWLDVQPEDRVLDLFCG 296
Cdd:TIGR02085 165 LEVISVNIQPvhmailegEEEIFLTEQQALP-ERFNDVPLVIRPQSFFQTNPKVAAQLYATARQWVREIPVTQMWDLFCG 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692   297 MGNFTLPLATQAASVVGVEGVPALVEKGQQNARLNGLQNVTFYhenlEEDVTKQPWAKNGF-DKVLLDPARAG-AAGVMQ 374
Cdd:TIGR02085 244 VGGFGLHCAGPDTQLTGIEIESEAIACAQQSAQMLGLDNLSFA----ALDSAKFATAQMSApELVLVNPPRRGiGKELCD 319
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 16130692   375 QIIKLEPIRIVYVSCNPATLARDSEALlkAGYTIARLAMLDMFPHTGHLESMVLFSR 431
Cdd:TIGR02085 320 YLSQMAPKFILYSSCNAQTMAKDIAEL--SGYQIERVQLFDMFPHTSHYEVLTLLVR 374
TRAM pfam01938
TRAM domain; This small domain has no known function. However it may perform a nucleic acid ...
10-67 3.82e-14

TRAM domain; This small domain has no known function. However it may perform a nucleic acid binding role (Bateman A. unpublished observation).


Pssm-ID: 396497 [Multi-domain]  Cd Length: 59  Bit Score: 66.47  E-value: 3.82e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 16130692    10 RTTTRQIITVSVNDLDSFGQGVARH-NGKTLFIPGLLPQENAEVTVTEDKKQYARAKVV 67
Cdd:pfam01938   1 RRYVGQTQEVLVEGLSSNGEGIGRTdNGKVVFVPGALPGEFVEVKITKVKRNYLRGELL 59
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
289-378 9.32e-14

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: 67.07  E-value: 9.32e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692 289 RVLDLFCGMGNFTLPLA-TQAASVVGVEGVPALVEKGQQNARLNGLQNVTFYHENLEEDvtkQPWAKNGFDKVLLDPARA 367
Cdd:cd02440   1 RVLDLGCGTGALALALAsGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEEL---PPEADESFDVIISDPPLH 77
                        90
                ....*....|.
gi 16130692 368 GAAGVMQQIIK 378
Cdd:cd02440  78 HLVEDLARFLE 88
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
276-407 9.82e-14

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: 68.10  E-value: 9.82e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692 276 ARALEWLDVQPEDRVLDLFCGMGNFTLPLATQAASVVGVEGVPALVEKGQQNARLNGLqNVTFyhenLEEDVTKQPWAKN 355
Cdd:COG2226  12 EALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGL-NVEF----VVGDAEDLPFPDG 86
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130692 356 GFDKVLL--------DPARAgaagvMQQIIK-LEP-IRIVYVSCNPATLARDSEALLKAGYT 407
Cdd:COG2226  87 SFDLVISsfvlhhlpDPERA-----LAEIARvLKPgGRLVVVDFSPPDLAELEELLAEAGFE 143
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
289-395 8.68e-12

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 62.82  E-value: 8.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692   289 RVLDLFCGMGNFTLPLATQA---ASVVGVEGVPALVEKGQQNARLNGLQNVTFYHENLEEdvTKQPWAKNGFDKVLLDPA 365
Cdd:pfam13847   6 RVLDLGCGTGHLSFELAEELgpnAEVVGIDISEEAIEKARENAQKLGFDNVEFEQGDIEE--LPELLEDDKFDVVISNCV 83
                          90       100       110
                  ....*....|....*....|....*....|...
gi 16130692   366 RAGAA---GVMQQIIKLEPIRIVYVSCNPATLA 395
Cdd:pfam13847  84 LNHIPdpdKVLQEILRVLKPGGRLIISDPDSLA 116
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
273-372 3.61e-10

Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 59.33  E-value: 3.61e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692 273 KMVARALEWLDVQPEDRVLDLFCGMGNFTLPLATQAASVVGVEGVPALVEKGQQNARLNGLQNVTFYHENLEedvtkQPW 352
Cdd:COG2518  53 YIVARMLEALDLKPGDRVLEIGTGSGYQAAVLARLAGRVYSVERDPELAERARERLAALGYDNVTVRVGDGA-----LGW 127
                        90       100
                ....*....|....*....|.
gi 16130692 353 AKNG-FDKVLLDparAGAAGV 372
Cdd:COG2518 128 PEHApFDRIIVT---AAAPEV 145
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
290-361 1.53e-09

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 54.88  E-value: 1.53e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130692   290 VLDLFCGMGNFTLPLATQA-ASVVGVEGVPALVEKGQQNARLNGLqNVTFYHenleEDVTKQPWAKNGFDKVL 361
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGgARVTGVDLSPEMLERARERAAEAGL-NVEFVQ----GDAEDLPFPDGSFDLVV 68
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
272-361 2.32e-09

Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 56.09  E-value: 2.32e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692 272 QKMVARALEWLDVQPEDRVLDLFCGMGNFTLPLATQA-ASVVGVEGVPALVEKGQQNARLNGLQN-VTFYHENLEEDVTK 349
Cdd:COG2230  37 EAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYgVRVTGVTLSPEQLEYARERAAEAGLADrVEVRLADYRDLPAD 116
                        90
                ....*....|..
gi 16130692 350 QPwakngFDKVL 361
Cdd:COG2230 117 GQ-----FDAIV 123
COG3269 COG3269
Predicted RNA-binding protein, contains TRAM domain [General function prediction only];
15-70 6.79e-09

Predicted RNA-binding protein, contains TRAM domain [General function prediction only];


Pssm-ID: 442500 [Multi-domain]  Cd Length: 129  Bit Score: 53.90  E-value: 6.79e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 16130692  15 QIITVSVNDLDSFGQGVARHNGKTLFIPGLLPQENAEVTVTEDKKQYARAKVVRRL 70
Cdd:COG3269  74 EEYEVEIEDIGKKGDGIARVEGFVIFVPGAEVGDRVKVKITKVKRNFAFAEVVERL 129
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
255-340 9.25e-09

Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 55.07  E-value: 9.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692   255 RLTFSPRDF-----------IQVNAGVNQ-KMVARALEWLDVQPEDRVLDLFCGMGNFTLPLAT---QAASVVGVEGVPA 319
Cdd:pfam01135  30 REEFVPESFksyayediplsIGYGQTISApHMHAMMLELLELKPGMRVLEIGSGSGYLTACFARmvgEVGRVVSIEHIPE 109
                          90       100
                  ....*....|....*....|.
gi 16130692   320 LVEKGQQNARLNGLQNVTFYH 340
Cdd:pfam01135 110 LVEIARRNLEKLGLENVIVVV 130
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
272-346 9.74e-09

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 55.61  E-value: 9.74e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130692  272 QKMVARALEWL--DVQPED-RVLDLFCGMGNFTLPLATQAASVVGVEGVPALVEKGQQNARLNGL-QNVTFYHENLEED 346
Cdd:PRK07580  46 QRMRDTVLSWLpaDGDLTGlRILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEARERAPEAGLaGNITFEVGDLESL 124
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
289-362 1.17e-07

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: 50.40  E-value: 1.17e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130692 289 RVLDLFCGMGNFTLPLATQAASVVGVEGVPALVEKGQQNARlngLQNVTFYHENLEEDvtkqPWAKNGFDKVLL 362
Cdd:COG2227  27 RVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAA---ELNVDFVQGDLEDL----PLEDGSFDLVIC 93
rADc smart00650
Ribosomal RNA adenine dimethylases;
274-360 2.03e-07

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 50.59  E-value: 2.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692    274 MVARALEWLDVQPEDRVLDLFCGMGNFTLPLATQAASVVGVEGVPALVEKgqqnarlngLQNVTFYHENLE---EDVTKQ 350
Cdd:smart00650   1 VIDKIVRAANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRLAPR---------LREKFAAADNLTvihGDALKF 71
                           90
                   ....*....|
gi 16130692    351 PWAKNGFDKV 360
Cdd:smart00650  72 DLPKLQPYKV 81
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
289-404 2.11e-07

SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 51.07  E-value: 2.11e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692 289 RVLDLFCGMGNFTLPLATQAAS-VVGVEGVPALVEKGQQNARLNGLQNVTFYHENLEEDvtkQPWAKNGFDKVL------ 361
Cdd:COG0500  29 RVLDLGCGTGRNLLALAARFGGrVIGIDLSPEAIALARARAAKAGLGNVEFLVADLAEL---DPLPAESFDLVVafgvlh 105
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 16130692 362 -LDPARAGAagVMQQIIK-LEPIRIVYVSCNPATLARDSEALLKA 404
Cdd:COG0500 106 hLPPEEREA--LLRELARaLKPGGVLLLSASDAAAALSLARLLLL 148
PRK08317 PRK08317
hypothetical protein; Provisional
276-367 4.46e-07

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 50.71  E-value: 4.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692  276 ARALEWLDVQPEDRVLDLFCGMGNFTLPLATQ---AASVVGVEGVPALVEkGQQNARLNGLQNVTFYHenleEDVTKQPW 352
Cdd:PRK08317   9 ARTFELLAVQPGDRVLDVGCGPGNDARELARRvgpEGRVVGIDRSEAMLA-LAKERAAGLGPNVEFVR----GDADGLPF 83
                         90       100
                 ....*....|....*....|...
gi 16130692  353 AKNGFDKV--------LLDPARA 367
Cdd:PRK08317  84 PDGSFDAVrsdrvlqhLEDPARA 106
Trm5 COG2520
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 ...
258-363 7.13e-07

tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 N-methylase Trm5 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442010 [Multi-domain]  Cd Length: 333  Bit Score: 50.63  E-value: 7.13e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692 258 FSPRdfiqvNAGVNQKMVARalewldVQPEDRVLDLFCGMGNFTLPLAT-QAASVVGVEGVPALVEKGQQNARLNGLQ-N 335
Cdd:COG2520 163 FSPR-----LATERLRIAEL------VKPGERVLDMFAGVGPFSIPIAKrSGAKVVAIDINPDAVEYLKENIRLNKVEdR 231
                        90       100
                ....*....|....*....|....*....
gi 16130692 336 VTFYHenleEDVTK-QPWAKNGFDKVLLD 363
Cdd:COG2520 232 VTPIL----GDAREvAPELEGKADRIIMN 256
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
272-391 1.13e-06

Predicted methyltransferase, contains TPR repeat [General function prediction only];


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 48.46  E-value: 1.13e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692 272 QKMVARALEWLDVQPEDRVLDLFCGMGNFTLPLATQAASVVGVEGVPALVEKgqqnARLNGLQnVTFYHenleEDVTKQP 351
Cdd:COG4976  32 ALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAK----AREKGVY-DRLLV----ADLADLA 102
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 16130692 352 WAKNGFDKVLldparagAAGVMQQIIKLEPI-RIVYVSCNP 391
Cdd:COG4976 103 EPDGRFDLIV-------AADVLTYLGDLAAVfAGVARALKP 136
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
281-358 1.54e-06

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: 48.99  E-value: 1.54e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692 281 WLDVQPEDRVLDLFCGMGnfTLPLA----TQAASVVGVEGVPALVEKGQQNARLNGLQN-VTFYHENLEEdvTKQPWAKN 355
Cdd:COG4123  32 FAPVKKGGRVLDLGTGTG--VIALMlaqrSPGARITGVEIQPEAAELARRNVALNGLEDrITVIHGDLKE--FAAELPPG 107

                ...
gi 16130692 356 GFD 358
Cdd:COG4123 108 SFD 110
RrnaAD pfam00398
Ribosomal RNA adenine dimethylase;
270-342 2.15e-06

Ribosomal RNA adenine dimethylase;


Pssm-ID: 395321 [Multi-domain]  Cd Length: 263  Bit Score: 48.90  E-value: 2.15e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130692   270 VNQKMVARALEWLDVQPEDRVLDLFCGMGNFTLPLATQAASVVGVEGVPALVEKGQqnARLNGLQNVTFYHEN 342
Cdd:pfam00398  14 KDPKVINEIVDKANLRESDTVLEIGPGKGALTVILAKRAKQVVAIEIDPRLAKLLQ--KKLSLDENLTVIHQD 84
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
279-378 3.43e-06

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: 46.81  E-value: 3.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692   279 LEWLDVQPEDRVLDLFCGMGNFTLPLA--TQAASVVGVEGVPALVEKGQQNARLNGLQNVTFYHENLEEDVtkqpwAKNG 356
Cdd:pfam05175  24 LEHLPKDLSGKVLDLGCGAGVLGAALAkeSPDAELTMVDINARALESARENLAANGLENGEVVASDVYSGV-----EDGK 98
                          90       100
                  ....*....|....*....|....*.
gi 16130692   357 FDKVLLDPA-RAGAA---GVMQQIIK 378
Cdd:pfam05175  99 FDLIISNPPfHAGLAttyNVAQRFIA 124
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
279-378 4.66e-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: 4.66e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692 279 LEWLDVQPEDRVLDLFCGMGnftlPLATQAA------SVVGVEGVPALVEKGQQNARLNGLQNVTFYHENLEEDVTKQPw 352
Cdd:COG2813  42 LEHLPEPLGGRVLDLGCGYG----VIGLALAkrnpeaRVTLVDVNARAVELARANAAANGLENVEVLWSDGLSGVPDGS- 116
                        90       100       110
                ....*....|....*....|....*....|
gi 16130692 353 akngFDKVLLD-PARAGAA---GVMQQIIK 378
Cdd:COG2813 117 ----FDLILSNpPFHAGRAvdkEVAHALIA 142
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
291-367 5.40e-06

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 44.58  E-value: 5.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692   291 LDLFCGMGNFTLPLATQAASVVGVEGVPALVEKGQQNARLNGLQNVtfyhenlEEDVTKQPWAKNGFDKVLL-------- 362
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREGLTFV-------VGDAEDLPFPDNSFDLVLSsevlhhve 73

                  ....*
gi 16130692   363 DPARA 367
Cdd:pfam08241  74 DPERA 78
RlmK COG1092
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ...
289-364 6.14e-06

23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure and biogenesis]; 23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 440709 [Multi-domain]  Cd Length: 392  Bit Score: 48.25  E-value: 6.14e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692 289 RVLDLFCGMGNFTLPLATQ-AASVVGVEGVPALVEKGQQNARLNGLQ-NVTFYHEN----LEEdvtkqpWAKNG--FDKV 360
Cdd:COG1092 219 RVLNLFSYTGGFSVHAAAGgAKSVTSVDLSATALEWAKENAALNGLDdRHEFVQADafdwLRE------LAREGerFDLI 292

                ....
gi 16130692 361 LLDP 364
Cdd:COG1092 293 ILDP 296
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
284-342 1.02e-05

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 46.57  E-value: 1.02e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130692 284 VQPEDRVLDLFCGMGNFTLpLATQ--AASVVGVEGVPALVEKGQQNARLNGL-QNVTFYHEN 342
Cdd:COG4076  33 VKPGDVVLDIGTGSGLLSM-LAARagAKKVYAVEVNPDIAAVARRIIAANGLsDRITVINAD 93
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
277-358 1.40e-05

bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 46.30  E-value: 1.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692  277 RALEWLDVQPEDRVLDLFCGMGNFTLPLATQA---ASVVGVEGVPALVEKGQQNARLNGLQ-NVTFyhenLEEDVTKQPW 352
Cdd:PRK00216  42 KTIKWLGVRPGDKVLDLACGTGDLAIALAKAVgktGEVVGLDFSEGMLAVGREKLRDLGLSgNVEF----VQGDAEALPF 117

                 ....*.
gi 16130692  353 AKNGFD 358
Cdd:PRK00216 118 PDNSFD 123
pcm PRK00312
protein-L-isoaspartate(D-aspartate) O-methyltransferase;
274-340 2.29e-05

protein-L-isoaspartate(D-aspartate) O-methyltransferase;


Pssm-ID: 178974 [Multi-domain]  Cd Length: 212  Bit Score: 45.20  E-value: 2.29e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130692  274 MVARALEWLDVQPEDRVLDLFCGMGNFTLPLATQAASVVGVEGVPALVEKGQQNARLNGLQNVTFYH 340
Cdd:PRK00312  66 MVARMTELLELKPGDRVLEIGTGSGYQAAVLAHLVRRVFSVERIKTLQWEAKRRLKQLGLHNVSVRH 132
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
284-364 4.22e-05

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: 43.78  E-value: 4.22e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692 284 VQPEDRVLDLFCGMGNFTLPLATQAASVVGVEGVPALVEKGQQNARLNGLQNVTFYHenleEDVTKQPWAKNGFDKVLLD 363
Cdd:COG1041  24 AKEGDTVLDPFCGTGTILIEAGLLGRRVIGSDIDPKMVEGARENLEHYGYEDADVIR----GDARDLPLADESVDAIVTD 99

                .
gi 16130692 364 P 364
Cdd:COG1041 100 P 100
Cons_hypoth95 pfam03602
Conserved hypothetical protein 95;
289-364 2.53e-04

Conserved hypothetical protein 95;


Pssm-ID: 427391 [Multi-domain]  Cd Length: 179  Bit Score: 41.84  E-value: 2.53e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130692   289 RVLDLFCGMGNFTL-PLATQAASVVGVEGVPALVEKGQQNARLNGLQNVTFYHENLeEDVTKQPWAKNGFDKVLLDP 364
Cdd:pfam03602  44 RVLDLFAGSGALGLeALSRGAKRVTLVEKDKRAVQILKENLQLLGLPGAVLVMDAL-LALLRLAGKGPVFDIVFLDP 119
PRK14968 PRK14968
putative methyltransferase; Provisional
279-364 3.51e-04

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 41.42  E-value: 3.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692  279 LEWLDVQPEDRVLDLFCGMGNFTLPLATQAASVVGVEGVPALVEKGQQNARLNGLQN--VTFYHENLEEdvtkqPWAKNG 356
Cdd:PRK14968  16 AENAVDKKGDRVLEVGTGSGIVAIVAAKNGKKVVGVDINPYAVECAKCNAKLNNIRNngVEVIRSDLFE-----PFRGDK 90

                 ....*...
gi 16130692  357 FDKVLLDP 364
Cdd:PRK14968  91 FDVILFNP 98
arsM PRK11873
arsenite methyltransferase;
285-345 4.64e-04

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 41.86  E-value: 4.64e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130692  285 QPEDRVLDLFCGMGNFTLpLATQA----ASVVGVEGVPALVEKGQQNARLNGLQNVTFYHENLEE 345
Cdd:PRK11873  76 KPGETVLDLGSGGGFDCF-LAARRvgptGKVIGVDMTPEMLAKARANARKAGYTNVEFRLGEIEA 139
Methyltr_RsmB-F pfam01189
16S rRNA methyltransferase RsmB/F; This is the catalytic core of this SAM-dependent 16S ...
281-363 1.14e-03

16S rRNA methyltransferase RsmB/F; This is the catalytic core of this SAM-dependent 16S ribosomal methyltransferase RsmB/F enzyme. There is a catalytic cysteine residue at 180 in UniProtKB:Q5SII2, with another highly conserved cysteine at residue 230. It methylates the C(5) position of cytosine 2870 (m5C2870) in 25S rRNA.


Pssm-ID: 426109 [Multi-domain]  Cd Length: 199  Bit Score: 40.10  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692   281 WLDVQPEDRVLDLFCGMGNFT---LPLATQAASVVGVEGVPALVEKGQQNARLNGLQNVTFYHENLEEdvTKQPWAKNGF 357
Cdd:pfam01189   3 LLAPQEGETILDMCAAPGGKTthiAELMKNQGTVVAVDINKHRLKRVAENIHRLGVTNTIILNGDGRQ--PDQWLGGVLF 80

                  ....*.
gi 16130692   358 DKVLLD 363
Cdd:pfam01189  81 DRILLD 86
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
279-332 1.57e-03

Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal protein L11 methyltransferase (EC:2.1.1.-) sequences.


Pssm-ID: 428888 [Multi-domain]  Cd Length: 294  Bit Score: 40.33  E-value: 1.57e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 16130692   279 LEWLD--VQPEDRVLDLFCGMGnfTLPLA---TQAASVVGVEGVPALVEKGQQNARLNG 332
Cdd:pfam06325 152 LEALErlVKPGESVLDVGCGSG--ILAIAalkLGAKKVVGVDIDPVAVRAAKENAELNG 208
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
279-346 2.62e-03

Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 39.39  E-value: 2.62e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692 279 LEWLD--VQPEDRVLDLFCG----------MGnftlplatqAASVVGVEGVPALVEKGQQNARLNGLQN-VTFYHENLEE 345
Cdd:COG2264 139 LEALEklLKPGKTVLDVGCGsgilaiaaakLG---------AKRVLAVDIDPVAVEAARENAELNGVEDrIEVVLGDLLE 209

                .
gi 16130692 346 D 346
Cdd:COG2264 210 D 210
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
285-350 2.78e-03

HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. Both E. coli and H. influenzae have two members rather than one. The members from the Mycoplasmas have an additional C-terminal domain. [Protein fate, Protein modification and repair]


Pssm-ID: 273125 [Multi-domain]  Cd Length: 284  Bit Score: 39.26  E-value: 2.78e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130692   285 QPEDRVLDLFCGMGNFTLPLAT--QAASVVGVEGVPALVEKGQQNARLNGL-QNVTFYHENLEEDVTKQ 350
Cdd:TIGR00536 113 PPILHILDLGTGSGCIALALAYefPNAEVIAVDISPDALAVAEENAEKNQLeHRVEFIQSNLFEPLAGQ 181
YtxK COG0827
Adenine-specific DNA N6-methylase [Replication, recombination and repair];
274-342 5.44e-03

Adenine-specific DNA N6-methylase [Replication, recombination and repair];


Pssm-ID: 440589 [Multi-domain]  Cd Length: 327  Bit Score: 38.78  E-value: 5.44e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130692 274 MVARALEWLDVQPEDRVLDLFCGMGNF---TLPLATQAASVVGVEGVPALVEKGQQNARLNGlQNVTFYHEN 342
Cdd:COG0827 103 LIGYLVEKFTKKEGLRILDPAVGTGNLlttVLNQLKKKVNAYGVEVDDLLIRLAAVLANLQG-HPVELFHQD 173
RsmB COG0144
16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and ...
274-363 6.17e-03

16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and biogenesis]; 16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 439914 [Multi-domain]  Cd Length: 441  Bit Score: 38.84  E-value: 6.17e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130692 274 MVARALewlDVQPEDRVLDLFCGMGNFTLPLATQA---ASVVGVEGVPALVEKGQQNARLNGLQNVTFyhenLEEDVTK- 349
Cdd:COG0144 240 LVALLL---DPKPGERVLDLCAAPGGKTLHLAELMgnkGRVVAVDISEHRLKRLRENLARLGLSNVEV----VVADAREl 312
                        90
                ....*....|....
gi 16130692 350 QPWAKNGFDKVLLD 363
Cdd:COG0144 313 LEWLPGKFDRVLLD 326
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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