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Conserved domains on  [gi|505384625|ref|WP_015571727|]
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MULTISPECIES: 23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD [Enterobacter]

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;
2-432 0e+00

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


:

Pssm-ID: 237291 [Multi-domain]  Cd Length: 443  Bit Score: 765.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625   2 AQFYSAKRRVTTRQIITVEATDLDPFGQGVARHKGKTLFITGLLPGERADITLTEEKRQYARGQVKRRLNDSPERVMPRC 81
Cdd:PRK13168   1 AQFYSPKRRVTTRQIITVTIESLDHDGRGVARHNGKTVFIEGALPGERVEVQVTEDKKQYARAKVVRILKPSPERVTPRC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625  82 PHFGVCGGCQQQHASTELQQKSKSSALARLVGH-------DVNDIIADRPWGYRRRARLSLSYQPKTERLEMGFRKAGSS 154
Cdd:PRK13168  81 PHFGVCGGCQLQHLSIDAQIASKQRALEDLLKHlagvepeEVLPPIAGPPWGYRRRARLSVRYVPKKGQLLVGFREKNSS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625 155 DIVSVTQCPVLVPHLEALLPDVHHCLASLDGVRSLGHVELVLANSGPLMVLRHTAPLSKADREKLERFSHSHELALFLAP 234
Cdd:PRK13168 161 DIVDIDQCPVLVPPLSALLPPLRALLSSLSAKRRLGHVELAQGDNGTALVLRHLEPLSEADRAKLRAFAEQHGLQLYLQP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625 235 QSEILEQVSGEA-----PWYASDGLRLTFSPRDFIQVNDGVNQQMVANALAWLDVQPTDRVLDLFCGMGNFTLPLARKAA 309
Cdd:PRK13168 241 KGPDLVHLLGPAdaqlsYYLPEFGLRLAFSPRDFIQVNAQVNQKMVARALEWLDPQPGDRVLDLFCGLGNFTLPLARQAA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625 310 SVVGVEGVEALVVKGQENAQQNGLQNVTFFHQNLEDDVTQQPWAKQGFDKILLDPARAGAPGVMQHIIKLAPERVVYVSC 389
Cdd:PRK13168 321 EVVGVEGVEAMVERARENARRNGLDNVTFYHANLEEDFTDQPWALGGFDKVLLDPPRAGAAEVMQALAKLGPKRIVYVSC 400
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 505384625 390 NPATLARDSEALLSGGYQIRRLAMLDMFPHTGHLESMVLFEHI 432
Cdd:PRK13168 401 NPATLARDAGVLVEAGYRLKRAGMLDMFPHTGHVESMALFERG 443
 
Name Accession Description Interval E-value
rumA PRK13168
23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD;
2-432 0e+00

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


Pssm-ID: 237291 [Multi-domain]  Cd Length: 443  Bit Score: 765.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625   2 AQFYSAKRRVTTRQIITVEATDLDPFGQGVARHKGKTLFITGLLPGERADITLTEEKRQYARGQVKRRLNDSPERVMPRC 81
Cdd:PRK13168   1 AQFYSPKRRVTTRQIITVTIESLDHDGRGVARHNGKTVFIEGALPGERVEVQVTEDKKQYARAKVVRILKPSPERVTPRC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625  82 PHFGVCGGCQQQHASTELQQKSKSSALARLVGH-------DVNDIIADRPWGYRRRARLSLSYQPKTERLEMGFRKAGSS 154
Cdd:PRK13168  81 PHFGVCGGCQLQHLSIDAQIASKQRALEDLLKHlagvepeEVLPPIAGPPWGYRRRARLSVRYVPKKGQLLVGFREKNSS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625 155 DIVSVTQCPVLVPHLEALLPDVHHCLASLDGVRSLGHVELVLANSGPLMVLRHTAPLSKADREKLERFSHSHELALFLAP 234
Cdd:PRK13168 161 DIVDIDQCPVLVPPLSALLPPLRALLSSLSAKRRLGHVELAQGDNGTALVLRHLEPLSEADRAKLRAFAEQHGLQLYLQP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625 235 QSEILEQVSGEA-----PWYASDGLRLTFSPRDFIQVNDGVNQQMVANALAWLDVQPTDRVLDLFCGMGNFTLPLARKAA 309
Cdd:PRK13168 241 KGPDLVHLLGPAdaqlsYYLPEFGLRLAFSPRDFIQVNAQVNQKMVARALEWLDPQPGDRVLDLFCGLGNFTLPLARQAA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625 310 SVVGVEGVEALVVKGQENAQQNGLQNVTFFHQNLEDDVTQQPWAKQGFDKILLDPARAGAPGVMQHIIKLAPERVVYVSC 389
Cdd:PRK13168 321 EVVGVEGVEAMVERARENARRNGLDNVTFYHANLEEDFTDQPWALGGFDKVLLDPPRAGAAEVMQALAKLGPKRIVYVSC 400
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 505384625 390 NPATLARDSEALLSGGYQIRRLAMLDMFPHTGHLESMVLFEHI 432
Cdd:PRK13168 401 NPATLARDAGVLVEAGYRLKRAGMLDMFPHTGHVESMALFERG 443
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: 539.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625   24 LDPFGQGVARHKGKTLFITGLLPGERADITLTEEKRQYARGQVKRRLNDSPERVMPRCPHFGVCGGCQQQHASTELQQKS 103
Cdd:TIGR00479   1 LDHQGEGVARFNGKTVFVPGALPGEKAEVRVTEVKKQYARARVKKILEDSPERTTPPCPHFGQCGGCQLQHLSYELQLRS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625  104 KS---SALARLVGHDVNDIIADRP------WGYRRRARLSLSYQPKTErLEMGFRKAGSSDIVSVTQCPVLVPHLEALLP 174
Cdd:TIGR00479  81 KQqqvIALLERIGKFVSEPIEDVPtigddpWGYRNKARLSLGRSPSGQ-LQAGFYQKGSHDIVDVKQCPVQAPALNALLP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625  175 DVHHCLASLDGVRSLGHVELVLANSGPLMVLRHTAPLSKADREKLERFSHSHELALFLAPQS------------------ 236
Cdd:TIGR00479 160 KVRAILENFGASRYLEHKELGQARHGVLRIGRHTGELSSVDRTALERFPHKEELDLYLQPDSpdvksicqninpektnvi 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625  237 --EILEQVSGEAPWY-ASDGLRLTFSPRDFIQVNDGVNQQMVANALAWLDVQPTDRVLDLFCGMGNFTLPLARKAASVVG 313
Cdd:TIGR00479 240 fgEETEVIAGEMPIYdKSGDLSFTFSARDFIQVNSGQNEKLVDRALEWLELQGEERVLDAYCGMGTFTLPLAKQAKSVVG 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625  314 VEGVEALVVKGQENAQQNGLQNVTFFHQNLEDDVTQQPWAKQGFDKILLDPARAG-APGVMQHIIKLAPERVVYVSCNPA 392
Cdd:TIGR00479 320 VEGVPESVEKAQQNAELNGIANVTFYHGTLETVLPKQPWAGNGFDKVLLDPPRKGcAAGVLRTIIKLKPERIVYVSCNPA 399
                         410       420       430
                  ....*....|....*....|....*....|..
gi 505384625  393 TLARDSEALLSGGYQIRRLAMLDMFPHTGHLE 424
Cdd:TIGR00479 400 TLARDLEALCKAGYTIARVQPVDMFPHTGHVE 431
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
15-430 9.33e-157

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: 447.70  E-value: 9.33e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625  15 QIITVEATDLDPFGQGVARHKGKTLFITGLLPGERADITLTEEKRQYARGQVKRRLNDSPERVMPRCPHFGVCGGCQQQH 94
Cdd:COG2265    1 EILELTIEDLAHGGDGVARHDGKVVFVPGALPGERVRVRVTKVKKSFARAKLVEVLEPSPDRVEPPCPHFGRCGGCQLQH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625  95 ASTELQQKSKSS----ALARLVGHD---VNDII-ADRPWGYRRRARLSLSYqpKTERLEMGFRKAGSSDIVSVTQCPVLV 166
Cdd:COG2265   81 LSYEAQLELKQRvvreALERIGGLPeveVEPIIgSPEPWGYRNRARLSVRR--TDGRLRLGFYARGSHELVDIDECPLLD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625 167 PHLEALLPDVHHCLASLDGVR-SLGHVELvlansgplmvlrhtaplskadreklerfshshelalfLAPQSEILEQVsge 245
Cdd:COG2265  159 PALNALLPALRELLAELGARRgELRHLVV-------------------------------------RAGRDYLTERL--- 198
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625 246 apwyasDGLRLTFSPRDFIQVNDGVNQQMVANALAWLDVQPTDRVLDLFCGMGNFTLPLARKAASVVGVEGVEALVVKGQ 325
Cdd:COG2265  199 ------GGLTFRISPGSFFQVNPEQAEALYAAALEWLDLTGGERVLDLYCGVGTFALPLARRAKKVIGVEIVPEAVEDAR 272
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625 326 ENAQQNGLQNVTFFHQNLEDDVTQQPWaKQGFDKILLDPARAGA-PGVMQHIIKLAPERVVYVSCNPATLARDSEALLSG 404
Cdd:COG2265  273 ENARLNGLKNVEFVAGDLEEVLPELLW-GGRPDVVVLDPPRAGAgPEVLEALAALGPRRIVYVSCNPATLARDLALLVEG 351
                        410       420
                 ....*....|....*....|....*.
gi 505384625 405 GYQIRRLAMLDMFPHTGHLESMVLFE 430
Cdd:COG2265  352 GYRLEKVQPVDMFPHTHHVESVALLE 377
tRNA_U5-meth_tr pfam05958
tRNA (Uracil-5-)-methyltransferase; This family consists of (Uracil-5-)-methyltransferases EC: ...
263-430 1.33e-23

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: 101.36  E-value: 1.33e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625  263 FIQVNDGVNQQMVANALAWLDVQPTDrVLDLFCGMGNFTLPLARKAASVVGVEGVEALVVKGQENAQQNGLQNVTFFHQN 342
Cdd:pfam05958 179 FTQPNAAVNIKMLEWACDVTQGSKGD-LLELYCGNGNFSLALARNFRKVLATEIAKPSVAAAQYNIAANNIDNVQIIRMS 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625  343 LEdDVTQQPWAKQGFDK-------------ILLDPARAgapGVMQHIIKLAP--ERVVYVSCNPATLaRDSEALLSGGYQ 407
Cdd:pfam05958 258 AE-EFTQAMNGVREFNRlkgidlksyncstIFVDPPRA---GLDPETLKLVQayPRILYISCNPETL-CANLEQLSKTHR 332
                         170       180
                  ....*....|....*....|...
gi 505384625  408 IRRLAMLDMFPHTGHLESMVLFE 430
Cdd:pfam05958 333 VERFALFDQFPYTHHMECGVLLE 355
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
289-389 1.44e-13

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: 66.68  E-value: 1.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625 289 RVLDLFCGMGNFTLPLAR-KAASVVGVEGVEALVVKGQENAQQNGLQNVTFFHQNLEDDvtqQPWAKQGFDKILLDPARA 367
Cdd:cd02440    1 RVLDLGCGTGALALALASgPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEEL---PPEADESFDVIISDPPLH 77
                         90       100
                 ....*....|....*....|....*..
gi 505384625 368 GAPGVMQHIIK-----LAPERVVYVSC 389
Cdd:cd02440   78 HLVEDLARFLEearrlLKPGGVLVLTL 104
rADc smart00650
Ribosomal RNA adenine dimethylases;
282-360 6.79e-06

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 45.96  E-value: 6.79e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625   282 LDVQPTDRVLDLFCGMGNFTLPLARKAASVVGVEGVEALVvkgqenaqqNGLQNVTFFHQNLE---DDVTQQPWAKQGFD 358
Cdd:smart00650   9 ANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRLA---------PRLREKFAAADNLTvihGDALKFDLPKLQPY 79

                   ..
gi 505384625   359 KI 360
Cdd:smart00650  80 KV 81
 
Name Accession Description Interval E-value
rumA PRK13168
23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD;
2-432 0e+00

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


Pssm-ID: 237291 [Multi-domain]  Cd Length: 443  Bit Score: 765.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625   2 AQFYSAKRRVTTRQIITVEATDLDPFGQGVARHKGKTLFITGLLPGERADITLTEEKRQYARGQVKRRLNDSPERVMPRC 81
Cdd:PRK13168   1 AQFYSPKRRVTTRQIITVTIESLDHDGRGVARHNGKTVFIEGALPGERVEVQVTEDKKQYARAKVVRILKPSPERVTPRC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625  82 PHFGVCGGCQQQHASTELQQKSKSSALARLVGH-------DVNDIIADRPWGYRRRARLSLSYQPKTERLEMGFRKAGSS 154
Cdd:PRK13168  81 PHFGVCGGCQLQHLSIDAQIASKQRALEDLLKHlagvepeEVLPPIAGPPWGYRRRARLSVRYVPKKGQLLVGFREKNSS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625 155 DIVSVTQCPVLVPHLEALLPDVHHCLASLDGVRSLGHVELVLANSGPLMVLRHTAPLSKADREKLERFSHSHELALFLAP 234
Cdd:PRK13168 161 DIVDIDQCPVLVPPLSALLPPLRALLSSLSAKRRLGHVELAQGDNGTALVLRHLEPLSEADRAKLRAFAEQHGLQLYLQP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625 235 QSEILEQVSGEA-----PWYASDGLRLTFSPRDFIQVNDGVNQQMVANALAWLDVQPTDRVLDLFCGMGNFTLPLARKAA 309
Cdd:PRK13168 241 KGPDLVHLLGPAdaqlsYYLPEFGLRLAFSPRDFIQVNAQVNQKMVARALEWLDPQPGDRVLDLFCGLGNFTLPLARQAA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625 310 SVVGVEGVEALVVKGQENAQQNGLQNVTFFHQNLEDDVTQQPWAKQGFDKILLDPARAGAPGVMQHIIKLAPERVVYVSC 389
Cdd:PRK13168 321 EVVGVEGVEAMVERARENARRNGLDNVTFYHANLEEDFTDQPWALGGFDKVLLDPPRAGAAEVMQALAKLGPKRIVYVSC 400
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 505384625 390 NPATLARDSEALLSGGYQIRRLAMLDMFPHTGHLESMVLFEHI 432
Cdd:PRK13168 401 NPATLARDAGVLVEAGYRLKRAGMLDMFPHTGHVESMALFERG 443
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: 539.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625   24 LDPFGQGVARHKGKTLFITGLLPGERADITLTEEKRQYARGQVKRRLNDSPERVMPRCPHFGVCGGCQQQHASTELQQKS 103
Cdd:TIGR00479   1 LDHQGEGVARFNGKTVFVPGALPGEKAEVRVTEVKKQYARARVKKILEDSPERTTPPCPHFGQCGGCQLQHLSYELQLRS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625  104 KS---SALARLVGHDVNDIIADRP------WGYRRRARLSLSYQPKTErLEMGFRKAGSSDIVSVTQCPVLVPHLEALLP 174
Cdd:TIGR00479  81 KQqqvIALLERIGKFVSEPIEDVPtigddpWGYRNKARLSLGRSPSGQ-LQAGFYQKGSHDIVDVKQCPVQAPALNALLP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625  175 DVHHCLASLDGVRSLGHVELVLANSGPLMVLRHTAPLSKADREKLERFSHSHELALFLAPQS------------------ 236
Cdd:TIGR00479 160 KVRAILENFGASRYLEHKELGQARHGVLRIGRHTGELSSVDRTALERFPHKEELDLYLQPDSpdvksicqninpektnvi 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625  237 --EILEQVSGEAPWY-ASDGLRLTFSPRDFIQVNDGVNQQMVANALAWLDVQPTDRVLDLFCGMGNFTLPLARKAASVVG 313
Cdd:TIGR00479 240 fgEETEVIAGEMPIYdKSGDLSFTFSARDFIQVNSGQNEKLVDRALEWLELQGEERVLDAYCGMGTFTLPLAKQAKSVVG 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625  314 VEGVEALVVKGQENAQQNGLQNVTFFHQNLEDDVTQQPWAKQGFDKILLDPARAG-APGVMQHIIKLAPERVVYVSCNPA 392
Cdd:TIGR00479 320 VEGVPESVEKAQQNAELNGIANVTFYHGTLETVLPKQPWAGNGFDKVLLDPPRKGcAAGVLRTIIKLKPERIVYVSCNPA 399
                         410       420       430
                  ....*....|....*....|....*....|..
gi 505384625  393 TLARDSEALLSGGYQIRRLAMLDMFPHTGHLE 424
Cdd:TIGR00479 400 TLARDLEALCKAGYTIARVQPVDMFPHTGHVE 431
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
15-430 9.33e-157

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: 447.70  E-value: 9.33e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625  15 QIITVEATDLDPFGQGVARHKGKTLFITGLLPGERADITLTEEKRQYARGQVKRRLNDSPERVMPRCPHFGVCGGCQQQH 94
Cdd:COG2265    1 EILELTIEDLAHGGDGVARHDGKVVFVPGALPGERVRVRVTKVKKSFARAKLVEVLEPSPDRVEPPCPHFGRCGGCQLQH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625  95 ASTELQQKSKSS----ALARLVGHD---VNDII-ADRPWGYRRRARLSLSYqpKTERLEMGFRKAGSSDIVSVTQCPVLV 166
Cdd:COG2265   81 LSYEAQLELKQRvvreALERIGGLPeveVEPIIgSPEPWGYRNRARLSVRR--TDGRLRLGFYARGSHELVDIDECPLLD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625 167 PHLEALLPDVHHCLASLDGVR-SLGHVELvlansgplmvlrhtaplskadreklerfshshelalfLAPQSEILEQVsge 245
Cdd:COG2265  159 PALNALLPALRELLAELGARRgELRHLVV-------------------------------------RAGRDYLTERL--- 198
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625 246 apwyasDGLRLTFSPRDFIQVNDGVNQQMVANALAWLDVQPTDRVLDLFCGMGNFTLPLARKAASVVGVEGVEALVVKGQ 325
Cdd:COG2265  199 ------GGLTFRISPGSFFQVNPEQAEALYAAALEWLDLTGGERVLDLYCGVGTFALPLARRAKKVIGVEIVPEAVEDAR 272
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625 326 ENAQQNGLQNVTFFHQNLEDDVTQQPWaKQGFDKILLDPARAGA-PGVMQHIIKLAPERVVYVSCNPATLARDSEALLSG 404
Cdd:COG2265  273 ENARLNGLKNVEFVAGDLEEVLPELLW-GGRPDVVVLDPPRAGAgPEVLEALAALGPRRIVYVSCNPATLARDLALLVEG 351
                        410       420
                 ....*....|....*....|....*.
gi 505384625 405 GYQIRRLAMLDMFPHTGHLESMVLFE 430
Cdd:COG2265  352 GYRLEKVQPVDMFPHTHHVESVALLE 377
rumB PRK03522
23S rRNA (uracil(747)-C(5))-methyltransferase RlmC;
231-430 1.12e-32

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


Pssm-ID: 235128 [Multi-domain]  Cd Length: 315  Bit Score: 125.37  E-value: 1.12e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625 231 FLAPQSEILEQVsgeapwyasDGLRLTFSPRDFIQVNDGVNQQMVANALAWLDVQPTDRVLDLFCGMGNFTLPLARKAAS 310
Cdd:PRK03522 127 FLTEQQALPERF---------NGVPLFIRPQSFFQTNPAVAAQLYATARDWVRELPPRSMWDLFCGVGGFGLHCATPGMQ 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625 311 VVGVEGVEALVVKGQENAQQNGLQNVTFfhQNLedDVTQQPWAKQGF-DKILLDPARAG-APGVMQHIIKLAPERVVYVS 388
Cdd:PRK03522 198 LTGIEISAEAIACAKQSAAELGLTNVQF--QAL--DSTQFATAQGEVpDLVLVNPPRRGiGKELCDYLSQMAPRFILYSS 273
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 505384625 389 CNPATLARDSEALlsGGYQIRRLAMLDMFPHTGHLESMVLFE 430
Cdd:PRK03522 274 CNAQTMAKDLAHL--PGYRIERVQLFDMFPHTAHYEVLTLLV 313
PRK05031 PRK05031
tRNA (uracil-5-)-methyltransferase; Validated
263-430 1.80e-29

tRNA (uracil-5-)-methyltransferase; Validated


Pssm-ID: 235332  Cd Length: 362  Bit Score: 117.62  E-value: 1.80e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625 263 FIQVNDGVNQQMvanaLAW-LDV--QPTDRVLDLFCGMGNFTLPLARKAASVVGVE----GVEALvvkgQENAQQNGLQN 335
Cdd:PRK05031 184 FTQPNAAVNEKM----LEWaLDAtkGSKGDLLELYCGNGNFTLALARNFRRVLATEiskpSVAAA----QYNIAANGIDN 255
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625 336 VTFFHQNLEDdVTQqpwAKQG----------------FDKILLDPARAGapgVMQHIIKLAP--ERVVYVSCNPATLARD 397
Cdd:PRK05031 256 VQIIRMSAEE-FTQ---AMNGvrefnrlkgidlksynFSTIFVDPPRAG---LDDETLKLVQayERILYISCNPETLCEN 328
                        170       180       190
                 ....*....|....*....|....*....|...
gi 505384625 398 SEALlSGGYQIRRLAMLDMFPHTGHLESMVLFE 430
Cdd:PRK05031 329 LETL-SQTHKVERFALFDQFPYTHHMECGVLLE 360
meth_trns_rumB TIGR02085
23S rRNA (uracil-5-)-methyltransferase RumB; This family consists of RNA methyltransferases ...
85-430 4.05e-27

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: 111.47  E-value: 4.05e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625   85 GVCGGCQQQHASTELQQKSKSSALARLV--GHDVNDIIA---DRPWGYRRRARLSLSyqPKTERLEMGFRKAgSSDIVSV 159
Cdd:TIGR02085   8 GRCRSCQWLAQPYSEQLTNKQQHLKELLapNATVVQWLApvtSAEQAFRNKAKMVVS--GSVERPILGILHR-DGTPLDL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625  160 TQCPVLVPHLEALLPDVHHCLA-----SLDGVRSLGHVELVL----ANSGPLM---VLRHTAPLSKADREK---LERFSH 224
Cdd:TIGR02085  85 CDCPLYPQSFQPVFAYLKNFIAragltPYNVAKKKGELKFILltesENSGQLMlrfVLRSETKLAQIRRALpwlIEQLPQ 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625  225 SHELALFLAPQ-SEILEqvsGEAPWYASD---------GLRLTFSPRDFIQVNDGVNQQMVANALAWLDVQPTDRVLDLF 294
Cdd:TIGR02085 165 LEVISVNIQPVhMAILE---GEEEIFLTEqqalperfnDVPLVIRPQSFFQTNPKVAAQLYATARQWVREIPVTQMWDLF 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625  295 CGMGNFTLPLARKAASVVGVEGVEALVVKGQENAQQNGLQNVTFfhQNLedDVTQQPWAK-QGFDKILLDPARAG-APGV 372
Cdd:TIGR02085 242 CGVGGFGLHCAGPDTQLTGIEIESEAIACAQQSAQMLGLDNLSF--AAL--DSAKFATAQmSAPELVLVNPPRRGiGKEL 317
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 505384625  373 MQHIIKLAPERVVYVSCNPATLARDSEALlsGGYQIRRLAMLDMFPHTGHLESMVLFE 430
Cdd:TIGR02085 318 CDYLSQMAPKFILYSSCNAQTMAKDIAEL--SGYQIERVQLFDMFPHTSHYEVLTLLV 373
tRNA_U5-meth_tr pfam05958
tRNA (Uracil-5-)-methyltransferase; This family consists of (Uracil-5-)-methyltransferases EC: ...
263-430 1.33e-23

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: 101.36  E-value: 1.33e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625  263 FIQVNDGVNQQMVANALAWLDVQPTDrVLDLFCGMGNFTLPLARKAASVVGVEGVEALVVKGQENAQQNGLQNVTFFHQN 342
Cdd:pfam05958 179 FTQPNAAVNIKMLEWACDVTQGSKGD-LLELYCGNGNFSLALARNFRKVLATEIAKPSVAAAQYNIAANNIDNVQIIRMS 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625  343 LEdDVTQQPWAKQGFDK-------------ILLDPARAgapGVMQHIIKLAP--ERVVYVSCNPATLaRDSEALLSGGYQ 407
Cdd:pfam05958 258 AE-EFTQAMNGVREFNRlkgidlksyncstIFVDPPRA---GLDPETLKLVQayPRILYISCNPETL-CANLEQLSKTHR 332
                         170       180
                  ....*....|....*....|...
gi 505384625  408 IRRLAMLDMFPHTGHLESMVLFE 430
Cdd:pfam05958 333 VERFALFDQFPYTHHMECGVLLE 355
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
289-389 1.44e-13

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: 66.68  E-value: 1.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625 289 RVLDLFCGMGNFTLPLAR-KAASVVGVEGVEALVVKGQENAQQNGLQNVTFFHQNLEDDvtqQPWAKQGFDKILLDPARA 367
Cdd:cd02440    1 RVLDLGCGTGALALALASgPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEEL---PPEADESFDVIISDPPLH 77
                         90       100
                 ....*....|....*....|....*..
gi 505384625 368 GAPGVMQHIIK-----LAPERVVYVSC 389
Cdd:cd02440   78 HLVEDLARFLEearrlLKPGGVLVLTL 104
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
289-395 2.19e-12

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 64.36  E-value: 2.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625  289 RVLDLFCGMGNFTLPLARKA---ASVVGVEGVEALVVKGQENAQQNGLQNVTFFHQNLEDdvTQQPWAKQGFDKILLDPA 365
Cdd:pfam13847   6 RVLDLGCGTGHLSFELAEELgpnAEVVGIDISEEAIEKARENAQKLGFDNVEFEQGDIEE--LPELLEDDKFDVVISNCV 83
                          90       100       110
                  ....*....|....*....|....*....|...
gi 505384625  366 RAGAP---GVMQHIIKLAPERVVYVSCNPATLA 395
Cdd:pfam13847  84 LNHIPdpdKVLQEILRVLKPGGRLIISDPDSLA 116
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
278-367 4.20e-12

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: 63.47  E-value: 4.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625 278 ALAWLDVQPTDRVLDLFCGMGNFTLPLARKAASVVGVEGVEALVVKGQENAQQNGLqNVTFFHQnledDVTQQPWAKQGF 357
Cdd:COG2226   14 LLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGL-NVEFVVG----DAEDLPFPDGSF 88
                         90
                 ....*....|....*...
gi 505384625 358 DKILL--------DPARA 367
Cdd:COG2226   89 DLVISsfvlhhlpDPERA 106
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
272-386 1.92e-11

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 63.70  E-value: 1.92e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625 272 QQMVANALAWL--DVQPTD-RVLDLFCGMGNFTLPLARKAASVVGVEGVEALVVKGQENAQQNGL-QNVTFFHQNLEDDv 347
Cdd:PRK07580  46 QRMRDTVLSWLpaDGDLTGlRILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEARERAPEAGLaGNITFEVGDLESL- 124
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 505384625 348 tqqpwaKQGFDK-ILLD-----PArAGAPGVMQHIIKLAPERVVY 386
Cdd:PRK07580 125 ------LGRFDTvVCLDvlihyPQ-EDAARMLAHLASLTRGSLIF 162
TRAM pfam01938
TRAM domain; This small domain has no known function. However it may perform a nucleic acid ...
10-67 3.30e-11

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: 58.38  E-value: 3.30e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 505384625   10 RVTTRQIITVEATDLDPFGQGVARH-KGKTLFITGLLPGERADITLTEEKRQYARGQVK 67
Cdd:pfam01938   1 RRYVGQTQEVLVEGLSSNGEGIGRTdNGKVVFVPGALPGEFVEVKITKVKRNYLRGELL 59
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
274-381 4.60e-10

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


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 58.95  E-value: 4.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625 274 MVANALAWLDVQPTDRVLDLFCGMGNFTLPLARKAASVVGVEGVEALVVKGQENAQQNGLQNVTFFHQNLEddvtqQPWA 353
Cdd:COG2518   54 IVARMLEALDLKPGDRVLEIGTGSGYQAAVLARLAGRVYSVERDPELAERARERLAALGYDNVTVRVGDGA-----LGWP 128
                         90       100       110
                 ....*....|....*....|....*....|
gi 505384625 354 KQG-FDKILLDparAGAPGVMQHIIK-LAP 381
Cdd:COG2518  129 EHApFDRIIVT---AAAPEVPEALLEqLAP 155
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
272-361 3.15e-09

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 55.71  E-value: 3.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625 272 QQMVANALAWLDVQPTDRVLDLFCGMGNFTLPLARKA-ASVVGVEGVEALVVKGQENAQQNGLQN-VTFFHQNLEDDVTQ 349
Cdd:COG2230   37 EAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYgVRVTGVTLSPEQLEYARERAAEAGLADrVEVRLADYRDLPAD 116
                         90
                 ....*....|..
gi 505384625 350 QPwakqgFDKIL 361
Cdd:COG2230  117 GQ-----FDAIV 123
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
290-376 3.59e-09

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 53.72  E-value: 3.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625  290 VLDLFCGMGNFTLPLARKA-ASVVGVEGVEALVVKGQENAQQNGLqNVTFFHQnledDVTQQPWAKQGFDKILldparag 368
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGgARVTGVDLSPEMLERARERAAEAGL-NVEFVQG----DAEDLPFPDGSFDLVV------- 68

                  ....*...
gi 505384625  369 APGVMQHI 376
Cdd:pfam13649  69 SSGVLHHL 76
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
289-404 9.33e-09

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 54.92  E-value: 9.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625 289 RVLDLFCGMGNFTLPLA-RKAASVVGVEGVEALVVKGQENAQQNGLQNVTFFHQNLEDDvtqQPWAKQGFDKIL------ 361
Cdd:COG0500   29 RVLDLGCGTGRNLLALAaRFGGRVIGIDLSPEAIALARARAAKAGLGNVEFLVADLAEL---DPLPAESFDLVVafgvlh 105
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 505384625 362 -LDPARAGApgVMQHIIK-LAPERVVYVSCNPATLARDSEALLSG 404
Cdd:COG0500  106 hLPPEEREA--LLRELARaLKPGGVLLLSASDAAAALSLARLLLL 148
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
289-376 1.57e-08

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: 52.71  E-value: 1.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625 289 RVLDLFCGMGNFTLPLARKAASVVGVEGVEALVVKGQENAQQnglQNVTFFHQNLEDDvtqqPWAKQGFDKILldparag 368
Cdd:COG2227   27 RVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAE---LNVDFVQGDLEDL----PLEDGSFDLVI------- 92

                 ....*...
gi 505384625 369 APGVMQHI 376
Cdd:COG2227   93 CSEVLEHL 100
PRK08317 PRK08317
hypothetical protein; Provisional
276-367 9.89e-08

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 52.63  E-value: 9.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625 276 ANALAWLDVQPTDRVLDLFCGMGNFTLPLAR---KAASVVGVEGVEALVVKGQENAQQNGLQnvTFFHQnleDDVTQQPW 352
Cdd:PRK08317   9 ARTFELLAVQPGDRVLDVGCGPGNDARELARrvgPEGRVVGIDRSEAMLALAKERAAGLGPN--VEFVR---GDADGLPF 83
                         90       100
                 ....*....|....*....|...
gi 505384625 353 AKQGFDKI--------LLDPARA 367
Cdd:PRK08317  84 PDGSFDAVrsdrvlqhLEDPARA 106
COG3269 COG3269
Predicted RNA-binding protein, contains TRAM domain [General function prediction only];
11-70 1.34e-07

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


Pssm-ID: 442500 [Multi-domain]  Cd Length: 129  Bit Score: 50.05  E-value: 1.34e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625  11 VTTRQIITVEATDLDPFGQGVARHKGKTLFITGLLPGERADITLTEEKRQYARGQVKRRL 70
Cdd:COG3269   70 VEEGEEYEVEIEDIGKKGDGIARVEGFVIFVPGAEVGDRVKVKITKVKRNFAFAEVVERL 129
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
282-383 3.89e-07

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: 49.90  E-value: 3.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625  282 LDVQPTDRVLDLFCGMGNFTLPLARKA--ASVVGVEGVEALVVKGQENAQQNGLQNVTFFHQNLEDDVtqqpwAKQGFDK 359
Cdd:pfam05175  27 LPKDLSGKVLDLGCGAGVLGAALAKESpdAELTMVDINARALESARENLAANGLENGEVVASDVYSGV-----EDGKFDL 101
                          90       100
                  ....*....|....*....|....*...
gi 505384625  360 ILLDP----ARAGAPGVMQHIIKLAPER 383
Cdd:pfam05175 102 IISNPpfhaGLATTYNVAQRFIADAKRH 129
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
282-383 4.43e-07

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: 49.80  E-value: 4.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625 282 LDVQPTDRVLDLFCGMGNFTLPLARKA--ASVVGVEgVEALVVK-GQENAQQNGLQNVTFFHQNLEDDVTQQPwakqgFD 358
Cdd:COG2813   45 LPEPLGGRVLDLGCGYGVIGLALAKRNpeARVTLVD-VNARAVElARANAAANGLENVEVLWSDGLSGVPDGS-----FD 118
                         90       100
                 ....*....|....*....|....*....
gi 505384625 359 KILLD-PARAGA---PGVMQHIIKLAPER 383
Cdd:COG2813  119 LILSNpPFHAGRavdKEVAHALIADAARH 147
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
274-381 5.07e-07

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


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 50.06  E-value: 5.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625  274 MVANALAWLDVQPTDRVLDLFCGMGNFTLPLAR---KAASVVGVEGVEALVVKGQENAQQNGLQNVTFFHqnleDDVTQQ 350
Cdd:pfam01135  61 MHAMMLELLELKPGMRVLEIGSGSGYLTACFARmvgEVGRVVSIEHIPELVEIARRNLEKLGLENVIVVV----GDGRQG 136
                          90       100       110
                  ....*....|....*....|....*....|..
gi 505384625  351 PWAKQGFDKILLDparAGAPGVMQHII-KLAP 381
Cdd:pfam01135 137 WPEFAPYDAIHVG---AAAPEIPEALIdQLKE 165
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
203-358 9.77e-07

Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 50.15  E-value: 9.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625 203 MVLRHTAPLSKADREKLERFSHSHElalflapQSEILEQVSGEAPWYasdGLRLtfsprdfiQVNDGV------NQQMVA 276
Cdd:COG2890   41 LLLHPDRPLTEEELARLEALVARRA-------AGEPLAYILGEAEFY---GLEF--------KVDPGVliprpeTEELVE 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625 277 NALAWLDVQPTDRVLDLFCGMGN--FTLPLARKAASVVGVE-GVEALVVkGQENAQQNGLQN-VTFFHQNLEDDVTqqpw 352
Cdd:COG2890  103 LALALLPAGAPPRVLDLGTGSGAiaLALAKERPDARVTAVDiSPDALAV-ARRNAERLGLEDrVRFLQGDLFEPLP---- 177

                 ....*.
gi 505384625 353 AKQGFD 358
Cdd:COG2890  178 GDGRFD 183
pcm PRK00312
protein-L-isoaspartate(D-aspartate) O-methyltransferase;
274-379 1.62e-06

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


Pssm-ID: 178974 [Multi-domain]  Cd Length: 212  Bit Score: 48.66  E-value: 1.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625 274 MVANALAWLDVQPTDRVLDLFCGMGNFTLPLARKAASVVGVEGVEALVVKGQENAQQNGLQNVTFFHqnleDDvTQQPWA 353
Cdd:PRK00312  66 MVARMTELLELKPGDRVLEIGTGSGYQAAVLAHLVRRVFSVERIKTLQWEAKRRLKQLGLHNVSVRH----GD-GWKGWP 140
                         90       100
                 ....*....|....*....|....*..
gi 505384625 354 KQG-FDKILLDparAGAPGVMQHIIKL 379
Cdd:PRK00312 141 AYApFDRILVT---AAAPEIPRALLEQ 164
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
280-358 2.24e-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: 48.60  E-value: 2.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625 280 AWLDVQPTDRVLDLFCGMGNFTLPLARK--AASVVGVEGVEALVVKGQENAQQNGLQN-VTFFHQNLEDdvTQQPWAKQG 356
Cdd:COG4123   31 AFAPVKKGGRVLDLGTGTGVIALMLAQRspGARITGVEIQPEAAELARRNVALNGLEDrITVIHGDLKE--FAAELPPGS 108

                 ..
gi 505384625 357 FD 358
Cdd:COG4123  109 FD 110
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
272-381 3.04e-06

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 47.30  E-value: 3.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625 272 QQMVANALAWLDVQPTDRVLDLFCGMGNFTLPLARKAASVVGVEGVEALVVKgqenAQQNGLQnVTFFHQnledDVTQQP 351
Cdd:COG4976   32 ALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAK----AREKGVY-DRLLVA----DLADLA 102
                         90       100       110
                 ....*....|....*....|....*....|
gi 505384625 352 WAKQGFDKILldparagAPGVMQHIIKLAP 381
Cdd:COG4976  103 EPDGRFDLIV-------AADVLTYLGDLAA 125
rADc smart00650
Ribosomal RNA adenine dimethylases;
282-360 6.79e-06

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 45.96  E-value: 6.79e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625   282 LDVQPTDRVLDLFCGMGNFTLPLARKAASVVGVEGVEALVvkgqenaqqNGLQNVTFFHQNLE---DDVTQQPWAKQGFD 358
Cdd:smart00650   9 ANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRLA---------PRLREKFAAADNLTvihGDALKFDLPKLQPY 79

                   ..
gi 505384625   359 KI 360
Cdd:smart00650  80 KV 81
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
278-358 1.28e-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: 1.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625 278 ALAWLDVQPTDRVLDLFCGMGNFTLPLARKA---ASVVGVEGVEALVVKGQENAQQNGLQ-NVTFfhqnLEDDVTQQPWA 353
Cdd:PRK00216  43 TIKWLGVRPGDKVLDLACGTGDLAIALAKAVgktGEVVGLDFSEGMLAVGREKLRDLGLSgNVEF----VQGDAEALPFP 118

                 ....*
gi 505384625 354 KQGFD 358
Cdd:PRK00216 119 DNSFD 123
Cons_hypoth95 pfam03602
Conserved hypothetical protein 95;
289-387 2.16e-05

Conserved hypothetical protein 95;


Pssm-ID: 427391 [Multi-domain]  Cd Length: 179  Bit Score: 44.92  E-value: 2.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625  289 RVLDLFCGMGNFTL-PLARKAASVVGVEGVEALVVKGQENAQQNGLQNVTFFHQNLEdDVTQQPWAKQGFDKILLDP--A 365
Cdd:pfam03602  44 RVLDLFAGSGALGLeALSRGAKRVTLVEKDKRAVQILKENLQLLGLPGAVLVMDALL-ALLRLAGKGPVFDIVFLDPpyA 122
                          90       100
                  ....*....|....*....|....*
gi 505384625  366 RAGAPGVMQHIIK---LAPERVVYV 387
Cdd:pfam03602 123 KGLIEEVLDLLAEkgwLKPNALIYV 147
Trm5 COG2520
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 ...
284-340 5.18e-05

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: 44.85  E-value: 5.18e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505384625 284 VQPTDRVLDLFCGMGNFTLPLARK-AASVVGVE----GVEALvvkgQENAQQNGLQ-NVTFFH 340
Cdd:COG2520  178 VKPGERVLDMFAGVGPFSIPIAKRsGAKVVAIDinpdAVEYL----KENIRLNKVEdRVTPIL 236
RlmK COG1092
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ...
289-364 6.54e-05

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: 44.79  E-value: 6.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625 289 RVLDLFCGMGNFTLPLARK-AASVVGVEGVE-ALVVkGQENAQQNGLQNVtffHQNLEDDV----TQQPWAKQGFDKILL 362
Cdd:COG1092  219 RVLNLFSYTGGFSVHAAAGgAKSVTSVDLSAtALEW-AKENAALNGLDDR---HEFVQADAfdwlRELAREGERFDLIIL 294

                 ..
gi 505384625 363 DP 364
Cdd:COG1092  295 DP 296
arsM PRK11873
arsenite methyltransferase;
278-338 1.60e-04

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 43.01  E-value: 1.60e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505384625 278 ALAWLdvQPTDRVLDLFCGMGNFTLpLARKA----ASVVGVEGVEALVVKGQENAQQNGLQNVTF 338
Cdd:PRK11873  71 ALAEL--KPGETVLDLGSGGGFDCF-LAARRvgptGKVIGVDMTPEMLAKARANARKAGYTNVEF 132
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
284-364 1.73e-04

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: 41.86  E-value: 1.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625 284 VQPTDRVLDLFCGMGNFTLPLARKAASVVGVEgVEALVVKG-QENAQQNGLQNVTFFHQnledDVTQQPWAKQGFDKILL 362
Cdd:COG1041   24 AKEGDTVLDPFCGTGTILIEAGLLGRRVIGSD-IDPKMVEGaRENLEHYGYEDADVIRG----DARDLPLADESVDAIVT 98

                 ..
gi 505384625 363 DP 364
Cdd:COG1041   99 DP 100
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
244-364 2.92e-04

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: 42.34  E-value: 2.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625  244 GEAPWYASDglrltfsprdfIQVNDGV------NQQMVANALAWLDVQPT-DRVLDLFCGMGNFTLPLA--RKAASVVGV 314
Cdd:TIGR00536  76 GSKEFYGLE-----------FFVNEHVliprpeTEELVEKALASLISQPPiLHILDLGTGSGCIALALAyeFPNAEVIAV 144
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 505384625  315 E-GVEALVVkGQENAQQNGLQNVTFFHQ-NLEDDVtqqpwAKQGFDKILLDP 364
Cdd:TIGR00536 145 DiSPDALAV-AEENAEKNQLEHRVEFIQsNLFEPL-----AGQKIDIIVSNP 190
RsmB COG0144
16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and ...
198-363 3.76e-04

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: 42.69  E-value: 3.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625 198 NSGPLMVLRhtAPLSKADREKLErfshshelalflapqsEILEQ--VSGEAPWYASDGLRLTFSPRdfIQVNDGVNQ--- 272
Cdd:COG0144  172 NEPPPLDLR--VNTLKASREELL----------------ARLAEegIEAEPTPLSPDGLRLEGPGP--VTALPGFREglf 231
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625 273 -------QMVANALawlDVQPTDRVLDLFCGMGNFTLPLARKA---ASVVGVEGVEALVVKGQENAQQNGLQNVTFFHQn 342
Cdd:COG0144  232 svqdeasQLVALLL---DPKPGERVLDLCAAPGGKTLHLAELMgnkGRVVAVDISEHRLKRLRENLARLGLSNVEVVVA- 307
                        170       180
                 ....*....|....*....|..
gi 505384625 343 ledDVTQ-QPWAKQGFDKILLD 363
Cdd:COG0144  308 ---DARElLEWLPGKFDRVLLD 326
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
289-410 1.38e-03

16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA G966 N2-methylase RsmD is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 440505 [Multi-domain]  Cd Length: 183  Bit Score: 39.68  E-value: 1.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625 289 RVLDLFCGMGNFTL-PLARKAASVVGVEG----VEALvvkgQENAQQNGLQ-NVTFFHQnledDVTQ--QPWAKQGFDKI 360
Cdd:COG0742   44 RVLDLFAGSGALGLeALSRGAASVVFVEKdrkaAAVI----RKNLEKLGLEdRARVIRG----DALRflKRLAGEPFDLV 115
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 505384625 361 LLDP--ARAGAPGVMQHIIK---LAPERVVYVSCNpatlARDSEALLSGGYQIRR 410
Cdd:COG0742  116 FLDPpyAKGLLEKALELLAEnglLAPGGLIVVEHS----KREELPELPAGLELLK 166
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
291-367 1.69e-03

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 37.64  E-value: 1.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625  291 LDLFCGMGNFTLPLARKAASVVGVEGVEALVVKGQENAQQNGLQNVTFfhqnledDVTQQPWAKQGFDKILL-------- 362
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREGLTFVVG-------DAEDLPFPDNSFDLVLSsevlhhve 73

                  ....*
gi 505384625  363 DPARA 367
Cdd:pfam08241  74 DPERA 78
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
284-342 2.70e-03

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 39.25  E-value: 2.70e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505384625 284 VQPTDRVLDLFCGMGNFTLPLARK-AASVVGVEGVEALVVKGQENAQQNGL-QNVTFFHQN 342
Cdd:COG4076   33 VKPGDVVLDIGTGSGLLSMLAARAgAKKVYAVEVNPDIAAVARRIIAANGLsDRITVINAD 93
Methyltr_RsmB-F pfam01189
16S rRNA methyltransferase RsmB/F; This is the catalytic core of this SAM-dependent 16S ...
281-363 5.17e-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: 38.17  E-value: 5.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384625  281 WLDVQPTDRVLDLFCGMGNFT---LPLARKAASVVGVEGVEALVVKGQENAQQNGLQNVTFfhqnLEDDVTQQP-W-AKQ 355
Cdd:pfam01189   3 LLAPQEGETILDMCAAPGGKTthiAELMKNQGTVVAVDINKHRLKRVAENIHRLGVTNTII----LNGDGRQPDqWlGGV 78

                  ....*...
gi 505384625  356 GFDKILLD 363
Cdd:pfam01189  79 LFDRILLD 86
 
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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