|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00175 |
PTZ00175 |
diphthine synthase; Provisional |
1-272 |
1.55e-164 |
|
diphthine synthase; Provisional
Pssm-ID: 185500 Cd Length: 270 Bit Score: 457.11 E-value: 1.55e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62945254 1 MLYLIGLGLGDAKDITVKGLEVVRRCSRVYLEAYTSVL-TVGKEALEEFYGRKLILADREEVEQEADNIFKDADVSDVAF 79
Cdd:PTZ00175 2 MLYIIGLGLGDEKDITVKGLEAVKSADVVYLESYTSILiNSNKEKLEEFYGKPVIEADREMVEEGCDEILEEAKEKNVAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62945254 80 LVVGDPFGATTHSDLILRATKLGIPYQVIHNASIMNAVGCCGLQLYRFGETVSIVFWTDTWRPESFFDKVKKNRENGMHT 159
Cdd:PTZ00175 82 LVVGDPFCATTHTDLYLRAKKKGIEVEVIHNASIMNAIGCTGLQLYRFGETVSIPFFTETWKPDSFYDKIKANRDNGLHT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62945254 160 LCLLDIKVKEQSLENLIRGRKIYEPPRYMSVNQAAQQLLEIVQNHRARgeapAITEETLCVGLARVGAEDQKIAAGTLQQ 239
Cdd:PTZ00175 162 LCLLDIKVKERSVENLMKGRKIYEPPRYMTINQAIEQLLEVEEKKGGG----VIAEDTLVVGVARVGSDDQQIVSGTLED 237
|
250 260 270
....*....|....*....|....*....|...
gi 62945254 240 MCTVSLGEPLHSLVITGGNLHPLEMEMLSLFSI 272
Cdd:PTZ00175 238 LLDVDFGPPLHSLVICAPTLHDIEEEFFELYRI 270
|
|
| DHP5_DphB |
cd11647 |
diphthine methyl ester synthase and diphthine synthase; Eukaryotic diphthine methyl ester ... |
1-256 |
5.62e-138 |
|
diphthine methyl ester synthase and diphthine synthase; Eukaryotic diphthine methyl ester synthase (DHP5) and archaeal diphthamide synthase (DphB) participate in the second step of the biosynthetic pathway of diphthamide. The eukaryotic enzyme catalyzes four methylations of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine methyl ester; the archaeal enzyme, catalyzes only 3 methylations, producing diphthine. Diphtheria toxin ADP-ribosylates diphthamide leading to inhibition of protein synthesis in the eukaryotic host cells.
Pssm-ID: 381174 Cd Length: 241 Bit Score: 388.70 E-value: 5.62e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62945254 1 MLYLIGLGLGDAKDITVKGLEVVRRCSRVYLEAYTSVLTVGK-EALEEFYGRKLILADREEVEQEADNIFKDADVSDVAF 79
Cdd:cd11647 1 MLYLIGLGLGDEKDITLEGLEALKKADKVYLEAYTSILPGSKlEELEKLIGKKIILLDREDLEEESEEILEEAKKKDVAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62945254 80 LVVGDPFGATTHSDLILRATKLGIPYQVIHNASIMNAVGCC-GLQLYRFGETVSIVFWTDTWRPESFFDKVKKNRENGMH 158
Cdd:cd11647 81 LVPGDPLIATTHIDLRLEAKKRGIKVKVIHNASILSAAGSTsGLQLYKFGRTVTIPFPEENYKPESPYDVIKENLKRGLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62945254 159 TLCLLDIKVkeqslenlirgrkiyEPPRYMSVNQAAQQLLEIVQNHRARgeapAITEETLCVGLARVGAEDQKIAAGTLQ 238
Cdd:cd11647 161 TLLLLDIKV---------------EEGRFMTINEAIEILLEIEEKRKEG----VITEDTLVVGLARLGSDDQKIVAGTLK 221
|
250
....*....|....*...
gi 62945254 239 QMCTVSLGEPLHSLVITG 256
Cdd:cd11647 222 ELLKEDFGPPPHSLIIPG 239
|
|
| DPH5 |
COG1798 |
Diphthamide biosynthesis methyltransferase [Translation, ribosomal structure and biogenesis]; |
1-271 |
5.18e-106 |
|
Diphthamide biosynthesis methyltransferase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441403 Cd Length: 255 Bit Score: 308.27 E-value: 5.18e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62945254 1 MLYLIGLGLGDAKDITVKGLEVVRRCSRVYLEAYTSVLT-VGKEALEEFYGRKLILADREEVEQEADNIFKDADVSDVAF 79
Cdd:COG1798 1 MLTFVGLGLSDERDITLKGLEALRSADKVYAEFYTSRLIgTDLEKLEELIGKEIVVLDREDVEDNPEEILEEAKEKDVVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62945254 80 LVVGDPFGATTHSDLILRATKLGIPYQVIHNASIMNAV-GCCGLQLYRFGETVSIVFWTDTWRPESFFDKVKKNRENGMH 158
Cdd:COG1798 81 LTAGDPMIATTHVDLRLRAKRRGIETRVIHGVSIVSAAiGLTGLQNYKFGKTVTIPFPYEGFVPTSPYDTIKENLERGLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62945254 159 TLCLLDIKVKEQslenlirgrkiyeppRYMSVNQAAQQLLEIvQNHRARGEapaITEETLCVGLARVGAEDQKIAAGTLQ 238
Cdd:COG1798 161 TLVLLDIKADKN---------------RYMTANEALELLLEI-EKKRREGV---ISDDTLAVVVARAGSPDPKIVAGKLS 221
|
250 260 270
....*....|....*....|....*....|...
gi 62945254 239 QMCTVSLGEPLHSLVITgGNLHPLEMEMLSLFS 271
Cdd:COG1798 222 ELANYDFGEPPHSLIIP-GRLHFMEAEALKALA 253
|
|
| dph5 |
TIGR00522 |
diphthine synthase; Alternate name: diphthamide biosynthesis S-adenosylmethionine-dependent ... |
1-271 |
2.02e-98 |
|
diphthine synthase; Alternate name: diphthamide biosynthesis S-adenosylmethionine-dependent methyltransferase. This protein participates in the modification of a specific His of elongation factor 2 of eukarotes and Archaea to diphthamide. The protein was characterized in Saccharomyces cerevisiae and designated DPH5. [Protein fate, Protein modification and repair]
Pssm-ID: 273117 Cd Length: 257 Bit Score: 289.02 E-value: 2.02e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62945254 1 MLYLIGLGLGDAKDITVKGLEVVRRCSRVYLEAYTSVLTVGK-EALEEFYGRKLILADREEVEQEADNIFKDADVSDVAF 79
Cdd:TIGR00522 1 MLYLIGLGLYDENDISVKGLEAIKKADEVYAEFYTSKLLGSSiEEIEEFFGKRVVVLERSDVEENSFRLIERAKSKDVAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62945254 80 LVVGDPFGATTHSDLILRATKLGIPYQVIHNASIMNAV-GCCGLQLYRFGETVSIVFWTDTWRPESFFDKVKKNRENGMH 158
Cdd:TIGR00522 81 LVAGDPMVATTHTDLKLEAKRKGIETRIIHGASISSAVcGLTGLQLYKFGKTATIVFFTDNYRPQTPYNVIKENRKIGLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62945254 159 TLCLLDIKVKEqslenlirgrkiyepPRYMSVNQAAQQLLEIvqnhRARGEAPAITEETLCVGLARVGAEDQKIAAGTLQ 238
Cdd:TIGR00522 161 TLVLLDIHPKE---------------NRAMTIGEGLENLLEE----EEKRKTGAITPDTYAVVIARAGSGKPVVKCDKIE 221
|
250 260 270
....*....|....*....|....*....|...
gi 62945254 239 QMCTVSLGEPLHSLVITGGNLHPLEMEMLSLFS 271
Cdd:TIGR00522 222 NLKNYDFGEPLHCLVVLAKTLHFMEFEYLREFA 254
|
|
| TP_methylase |
pfam00590 |
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ... |
1-240 |
6.22e-24 |
|
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of diverse substrates. This family includes a related group of bacterial proteins of unknown function. This family includes the methylase Dipthine synthase.
Pssm-ID: 425769 [Multi-domain] Cd Length: 209 Bit Score: 96.26 E-value: 6.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62945254 1 MLYLIGLGLGDAKDITVKGLEVVRRCSRVYLE---AYTSVLTVGKEALeeFYGRKLILADREEVEQEADNIFKDA--DVS 75
Cdd:pfam00590 1 KLYLVGVGPGDPDLLTLRALRALKEADVVLGDdsrALEILLDLLPEDL--YFPMTEDKEPLEEAYEEIAEALAAAlrAGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62945254 76 DVAFLVVGDPFGATTHSDLILRATKLGIPYQVIHNASIMNAVGCC-GLQLYRFGETVSIVFWTDT-WRPESFFDKVKKNR 153
Cdd:pfam00590 79 DVARLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARlGIPLTEGGEVLSVLFLPGLaRIELRLLEALLANG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62945254 154 engmHTLCLLDIKVKeqslenlirgrkiyepprymsVNQAAQQLLEivqnhrargeapAITEETLCVGLARVGAEDQKIA 233
Cdd:pfam00590 159 ----DTVVLLYGPRR---------------------LAELAELLLE------------LYPDTTPVAVVERAGTPDEKVV 201
|
....*..
gi 62945254 234 AGTLQQM 240
Cdd:pfam00590 202 RGTLGEL 208
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00175 |
PTZ00175 |
diphthine synthase; Provisional |
1-272 |
1.55e-164 |
|
diphthine synthase; Provisional
Pssm-ID: 185500 Cd Length: 270 Bit Score: 457.11 E-value: 1.55e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62945254 1 MLYLIGLGLGDAKDITVKGLEVVRRCSRVYLEAYTSVL-TVGKEALEEFYGRKLILADREEVEQEADNIFKDADVSDVAF 79
Cdd:PTZ00175 2 MLYIIGLGLGDEKDITVKGLEAVKSADVVYLESYTSILiNSNKEKLEEFYGKPVIEADREMVEEGCDEILEEAKEKNVAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62945254 80 LVVGDPFGATTHSDLILRATKLGIPYQVIHNASIMNAVGCCGLQLYRFGETVSIVFWTDTWRPESFFDKVKKNRENGMHT 159
Cdd:PTZ00175 82 LVVGDPFCATTHTDLYLRAKKKGIEVEVIHNASIMNAIGCTGLQLYRFGETVSIPFFTETWKPDSFYDKIKANRDNGLHT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62945254 160 LCLLDIKVKEQSLENLIRGRKIYEPPRYMSVNQAAQQLLEIVQNHRARgeapAITEETLCVGLARVGAEDQKIAAGTLQQ 239
Cdd:PTZ00175 162 LCLLDIKVKERSVENLMKGRKIYEPPRYMTINQAIEQLLEVEEKKGGG----VIAEDTLVVGVARVGSDDQQIVSGTLED 237
|
250 260 270
....*....|....*....|....*....|...
gi 62945254 240 MCTVSLGEPLHSLVITGGNLHPLEMEMLSLFSI 272
Cdd:PTZ00175 238 LLDVDFGPPLHSLVICAPTLHDIEEEFFELYRI 270
|
|
| DHP5_DphB |
cd11647 |
diphthine methyl ester synthase and diphthine synthase; Eukaryotic diphthine methyl ester ... |
1-256 |
5.62e-138 |
|
diphthine methyl ester synthase and diphthine synthase; Eukaryotic diphthine methyl ester synthase (DHP5) and archaeal diphthamide synthase (DphB) participate in the second step of the biosynthetic pathway of diphthamide. The eukaryotic enzyme catalyzes four methylations of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine methyl ester; the archaeal enzyme, catalyzes only 3 methylations, producing diphthine. Diphtheria toxin ADP-ribosylates diphthamide leading to inhibition of protein synthesis in the eukaryotic host cells.
Pssm-ID: 381174 Cd Length: 241 Bit Score: 388.70 E-value: 5.62e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62945254 1 MLYLIGLGLGDAKDITVKGLEVVRRCSRVYLEAYTSVLTVGK-EALEEFYGRKLILADREEVEQEADNIFKDADVSDVAF 79
Cdd:cd11647 1 MLYLIGLGLGDEKDITLEGLEALKKADKVYLEAYTSILPGSKlEELEKLIGKKIILLDREDLEEESEEILEEAKKKDVAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62945254 80 LVVGDPFGATTHSDLILRATKLGIPYQVIHNASIMNAVGCC-GLQLYRFGETVSIVFWTDTWRPESFFDKVKKNRENGMH 158
Cdd:cd11647 81 LVPGDPLIATTHIDLRLEAKKRGIKVKVIHNASILSAAGSTsGLQLYKFGRTVTIPFPEENYKPESPYDVIKENLKRGLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62945254 159 TLCLLDIKVkeqslenlirgrkiyEPPRYMSVNQAAQQLLEIVQNHRARgeapAITEETLCVGLARVGAEDQKIAAGTLQ 238
Cdd:cd11647 161 TLLLLDIKV---------------EEGRFMTINEAIEILLEIEEKRKEG----VITEDTLVVGLARLGSDDQKIVAGTLK 221
|
250
....*....|....*...
gi 62945254 239 QMCTVSLGEPLHSLVITG 256
Cdd:cd11647 222 ELLKEDFGPPPHSLIIPG 239
|
|
| DPH5 |
COG1798 |
Diphthamide biosynthesis methyltransferase [Translation, ribosomal structure and biogenesis]; |
1-271 |
5.18e-106 |
|
Diphthamide biosynthesis methyltransferase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441403 Cd Length: 255 Bit Score: 308.27 E-value: 5.18e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62945254 1 MLYLIGLGLGDAKDITVKGLEVVRRCSRVYLEAYTSVLT-VGKEALEEFYGRKLILADREEVEQEADNIFKDADVSDVAF 79
Cdd:COG1798 1 MLTFVGLGLSDERDITLKGLEALRSADKVYAEFYTSRLIgTDLEKLEELIGKEIVVLDREDVEDNPEEILEEAKEKDVVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62945254 80 LVVGDPFGATTHSDLILRATKLGIPYQVIHNASIMNAV-GCCGLQLYRFGETVSIVFWTDTWRPESFFDKVKKNRENGMH 158
Cdd:COG1798 81 LTAGDPMIATTHVDLRLRAKRRGIETRVIHGVSIVSAAiGLTGLQNYKFGKTVTIPFPYEGFVPTSPYDTIKENLERGLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62945254 159 TLCLLDIKVKEQslenlirgrkiyeppRYMSVNQAAQQLLEIvQNHRARGEapaITEETLCVGLARVGAEDQKIAAGTLQ 238
Cdd:COG1798 161 TLVLLDIKADKN---------------RYMTANEALELLLEI-EKKRREGV---ISDDTLAVVVARAGSPDPKIVAGKLS 221
|
250 260 270
....*....|....*....|....*....|...
gi 62945254 239 QMCTVSLGEPLHSLVITgGNLHPLEMEMLSLFS 271
Cdd:COG1798 222 ELANYDFGEPPHSLIIP-GRLHFMEAEALKALA 253
|
|
| dph5 |
TIGR00522 |
diphthine synthase; Alternate name: diphthamide biosynthesis S-adenosylmethionine-dependent ... |
1-271 |
2.02e-98 |
|
diphthine synthase; Alternate name: diphthamide biosynthesis S-adenosylmethionine-dependent methyltransferase. This protein participates in the modification of a specific His of elongation factor 2 of eukarotes and Archaea to diphthamide. The protein was characterized in Saccharomyces cerevisiae and designated DPH5. [Protein fate, Protein modification and repair]
Pssm-ID: 273117 Cd Length: 257 Bit Score: 289.02 E-value: 2.02e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62945254 1 MLYLIGLGLGDAKDITVKGLEVVRRCSRVYLEAYTSVLTVGK-EALEEFYGRKLILADREEVEQEADNIFKDADVSDVAF 79
Cdd:TIGR00522 1 MLYLIGLGLYDENDISVKGLEAIKKADEVYAEFYTSKLLGSSiEEIEEFFGKRVVVLERSDVEENSFRLIERAKSKDVAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62945254 80 LVVGDPFGATTHSDLILRATKLGIPYQVIHNASIMNAV-GCCGLQLYRFGETVSIVFWTDTWRPESFFDKVKKNRENGMH 158
Cdd:TIGR00522 81 LVAGDPMVATTHTDLKLEAKRKGIETRIIHGASISSAVcGLTGLQLYKFGKTATIVFFTDNYRPQTPYNVIKENRKIGLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62945254 159 TLCLLDIKVKEqslenlirgrkiyepPRYMSVNQAAQQLLEIvqnhRARGEAPAITEETLCVGLARVGAEDQKIAAGTLQ 238
Cdd:TIGR00522 161 TLVLLDIHPKE---------------NRAMTIGEGLENLLEE----EEKRKTGAITPDTYAVVIARAGSGKPVVKCDKIE 221
|
250 260 270
....*....|....*....|....*....|...
gi 62945254 239 QMCTVSLGEPLHSLVITGGNLHPLEMEMLSLFS 271
Cdd:TIGR00522 222 NLKNYDFGEPLHCLVVLAKTLHFMEFEYLREFA 254
|
|
| TP_methylase |
pfam00590 |
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ... |
1-240 |
6.22e-24 |
|
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of diverse substrates. This family includes a related group of bacterial proteins of unknown function. This family includes the methylase Dipthine synthase.
Pssm-ID: 425769 [Multi-domain] Cd Length: 209 Bit Score: 96.26 E-value: 6.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62945254 1 MLYLIGLGLGDAKDITVKGLEVVRRCSRVYLE---AYTSVLTVGKEALeeFYGRKLILADREEVEQEADNIFKDA--DVS 75
Cdd:pfam00590 1 KLYLVGVGPGDPDLLTLRALRALKEADVVLGDdsrALEILLDLLPEDL--YFPMTEDKEPLEEAYEEIAEALAAAlrAGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62945254 76 DVAFLVVGDPFGATTHSDLILRATKLGIPYQVIHNASIMNAVGCC-GLQLYRFGETVSIVFWTDT-WRPESFFDKVKKNR 153
Cdd:pfam00590 79 DVARLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARlGIPLTEGGEVLSVLFLPGLaRIELRLLEALLANG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62945254 154 engmHTLCLLDIKVKeqslenlirgrkiyepprymsVNQAAQQLLEivqnhrargeapAITEETLCVGLARVGAEDQKIA 233
Cdd:pfam00590 159 ----DTVVLLYGPRR---------------------LAELAELLLE------------LYPDTTPVAVVERAGTPDEKVV 201
|
....*..
gi 62945254 234 AGTLQQM 240
Cdd:pfam00590 202 RGTLGEL 208
|
|
| TP_methylase |
cd09815 |
S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet ... |
5-254 |
4.74e-21 |
|
S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet (S-adenosyl-L-methionine or SAM) in the methylation of diverse substrates. Most members catalyze various methylation steps in cobalamin (vitamin B12) biosynthesis. There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. The enzymes involved in the aerobic pathway are prefixed Cob and those of the anaerobic pathway Cbi. Most of the enzymes are shared by both pathways and a few enzymes are pathway-specific. Diphthine synthase and ribosomal RNA small subunit methyltransferase I (RsmI) are two superfamily members that are not involved in cobalamin biosynthesis. Diphthine synthase participates in the posttranslational modification of a specific histidine residue in elongation factor 2 (EF-2) of eukaryotes and archaea to diphthamide. RsmI catalyzes the 2-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA. Other superfamily members not involved in cobalamin biosynthesis include the N-terminal tetrapyrrole methylase domain of Bacillus subtilis YabN whose specific function is unknown, and Omphalotus olearius omphalotin methyltransferase which catalyzes the automethylation of its own C-terminus; this C terminus is subsequently released and macrocyclized to give Omphalotin A, a potent nematicide.
Pssm-ID: 381167 [Multi-domain] Cd Length: 219 Bit Score: 88.60 E-value: 4.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62945254 5 IGLGLGDAKDITVKGLEVVRRCSRVYLEAYTSVLTVGKEALEEFYG-RKLILADREEVEQEADNIFKDADVS-DVAFLVV 82
Cdd:cd09815 1 VGVGPGDPDLLTLRALEILRAADVVVAEDKDSKLLSLVLRAILKDGkRIYDLHDPNVEEEMAELLLEEARQGkDVAFLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62945254 83 GDPFGATTHSDLILRATKLGIPYQVIHNASIMNAVGC-CGLQLYRFGETVSIVFWTDTWRpesfFDKVKKNRENGMHTLC 161
Cdd:cd09815 81 GDPGVAGTGAELVERAEREGVEVKVIPGVSAADAAAAaLGIDLGESFLFVTASDLLENPR----LLVLKALAKERRHLVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62945254 162 LLDIKVKEQSLENLIrgrKIYEPPrymsvnqaaqqlleivqnhrargeapaiteETLCVGLARVGAEDQKIAAGTLQQMC 241
Cdd:cd09815 157 FLDGHRFLKALERLL---KELGED------------------------------DTPVVLVANAGSEGEVIRTGTVKELR 203
|
250
....*....|....*
gi 62945254 242 TV--SLGEPLHSLVI 254
Cdd:cd09815 204 AErtERGKPLTTILV 218
|
|
| TP_methylase |
cd11724 |
uncharacterized family of the tetrapyrrole methylase superfamily; Members of this superfamily ... |
2-87 |
4.61e-08 |
|
uncharacterized family of the tetrapyrrole methylase superfamily; Members of this superfamily use S-AdoMet (S-adenosyl-L-methionine or SAM) in the methylation of diverse substrates. Most members catalyze various methylation steps in cobalamin (vitamin B12) biosynthesis. There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. The enzymes involved in the aerobic pathway are prefixed Cob and those of the anaerobic pathway Cbi. Most of the enzymes are shared by both pathways and a few enzymes are pathway-specific. Diphthine synthase and Ribosomal RNA small subunit methyltransferase I (RsmI) are two superfamily members that are not involved in cobalamin biosynthesis. Diphthine synthase participates in the posttranslational modification of a specific histidine residue in elongation factor 2 (EF-2) of eukaryotes and archaea to diphthamide. RsmI catalyzes the 2-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA. Other superfamily members not involved in cobalamin biosynthesis include the N-terminal tetrapyrrole methylase domain of Bacillus subtilis YabN whose specific function is unknown, and Omphalotus olearius omphalotin methyltransferase which catalyzes the automethylation of its own C-terminus; this C terminus is subsequently released and macrocyclized to give Omphalotin A, a potent nematicide.
Pssm-ID: 381178 [Multi-domain] Cd Length: 243 Bit Score: 52.56 E-value: 4.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62945254 2 LYLIGLGLGDAKDITVKGLEVVRR-----CSRVYLEAYTSVLTvGKEALE------EFYGRKliLADREEVEQEADNIFK 70
Cdd:cd11724 2 LYLVGVGPGDPDLITLRALKAIKKadvvfAPPDLRKRFAEYLA-GKEVLDdphglfTYYGKK--CSPLEEAEKECEELEK 78
|
90 100 110
....*....|....*....|....*....|.
gi 62945254 71 --DADVS----------DVAFLVVGDP--FG 87
Cdd:cd11724 79 qrAEIVQkirealaqgkNVALLDSGDPtiYG 109
|
|
| YabN_N_like |
cd11723 |
N-terminal S-AdoMet-dependent tetrapyrrole methylase domain of Bacillus subtilis YabN and ... |
2-124 |
2.94e-07 |
|
N-terminal S-AdoMet-dependent tetrapyrrole methylase domain of Bacillus subtilis YabN and similar domains; This family includes the S-AdoMet (S-adenosyl-L-methionine or SAM)-dependent tetrapyrrole methylase (TP-methylase) domain of Bacillus subtilis YabN, and similar domains. YabN is a fusion of an N-terminal TP-methylase and a C-terminal MazG-type nucleotide pyrophosphohydrolase domain. MazG-like NTP-PPases have been implicated in house-cleaning functions such as degrading abnormal (d)NTPs. TP-methylases use S-AdoMet in the methylation of diverse substrates. Most TP-methylase family members catalyze various methylation steps in cobalamin (vitamin B12) biosynthesis, other members like diphthine synthase and ribosomal RNA small subunit methyltransferase I (RsmI) act on other substrates. The specific function of YabN's TP-methylase domain is not known.
Pssm-ID: 381177 Cd Length: 218 Bit Score: 50.18 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62945254 2 LYLIGLGLGDAKDITVKGLEVVRRCSRVYL-----EAYTSVLTVGK--EALEEFYGRKlilADREEVEQE-ADNIFKDAD 73
Cdd:cd11723 1 ITIVGLGPGDPDLLTLGALEALKSADKVYLrtarhPVVEELKEEGIefESFDDLYEEA---EDFEEVYEAiAERLLEAAE 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 62945254 74 VSDVAFLVVGDPFGATTHSDLILRATKLGIPYQVIHNAS----IMNAVGCC---GLQL 124
Cdd:cd11723 78 HGDVVYAVPGHPLVAERTVQLLLERAEEGIEVEIIPGVSfldaALAALGIDpieGLQI 135
|
|
| PRK05576 |
PRK05576 |
cobalt-factor II C(20)-methyltransferase; |
1-108 |
3.64e-07 |
|
cobalt-factor II C(20)-methyltransferase;
Pssm-ID: 235512 [Multi-domain] Cd Length: 229 Bit Score: 49.91 E-value: 3.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62945254 1 MLYLIGLGLGDAKDITVKGLEVVRRCSRVYleAYTSVLTVGKEAL---EEFYGRKLIL--------ADREEVEQE----A 65
Cdd:PRK05576 3 KLYGIGLGPGDPELLTVKAARILEEADVVY--APASRKGGGSLALnivRPYLKEETEIvelhfpmsKDEEEKEAVwkenA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 62945254 66 DNIFKDA-DVSDVAFLVVGDPFGATTHSDLILRATKLGIPYQVI 108
Cdd:PRK05576 81 EEIAAEAeEGKNVAFITLGDPNLYSTFSHLLEYLKCHDIEVETV 124
|
|
| CobF |
COG2243 |
Precorrin-2 methylase [Coenzyme transport and metabolism]; Precorrin-2 methylase is part of ... |
2-108 |
9.91e-07 |
|
Precorrin-2 methylase [Coenzyme transport and metabolism]; Precorrin-2 methylase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 441844 [Multi-domain] Cd Length: 229 Bit Score: 48.56 E-value: 9.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62945254 2 LYLIGLGLGDAKDITVKGLEVVRRCSRV-------------------YLEAYTSV-----LTVGKEALEEFYgrkliLAD 57
Cdd:COG2243 5 LYGVGVGPGDPELLTLKAVRALREADVIaypakgagkaslareivapYLPPARIVelvfpMTTDYEALVAAW-----DEA 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 62945254 58 REEVEQEADnifkdaDVSDVAFLVVGDPF--GATTHsdLILRATKLGIPYQVI 108
Cdd:COG2243 80 AARIAEELE------AGRDVAFLTEGDPSlySTFMY--LLERLRERGFEVEVI 124
|
|
| cobI_cbiL |
TIGR01467 |
precorrin-2 C(20)-methyltransferase; This model represents precorrin-2 C(20)-methyltransferase, ... |
1-117 |
1.19e-05 |
|
precorrin-2 C(20)-methyltransferase; This model represents precorrin-2 C(20)-methyltransferase, one of several closely related S-adenosylmethionine-dependent methyltransferases involved in cobalamin (vitamin B12) biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
Pssm-ID: 273642 [Multi-domain] Cd Length: 230 Bit Score: 45.38 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62945254 1 MLYLIGLGLGDAKDITVKGLEVVRRCSRVYLEAytsvltvgKEALEEFYGRKLIL------------------ADREEVE 62
Cdd:TIGR01467 2 KLYGVGVGPGDPELITVKALEALRSADVIAVPA--------SKKGRESLARKIVEdylkpndtrilelvfpmtKDRDELE 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 62945254 63 QEADNIFKD--ADVS---DVAFLVVGDPFGATTHSDLILRATKLGIPYQVIHNASIMNAV 117
Cdd:TIGR01467 74 KAWDEAAEAvaAELEegrDVAFLTLGDPSLYSTFSYLLQRLQGMGIEVEVVPGITSFAAC 133
|
|
| PRK05787 |
PRK05787 |
cobalt-precorrin-7 (C(5))-methyltransferase; |
1-85 |
1.34e-04 |
|
cobalt-precorrin-7 (C(5))-methyltransferase;
Pssm-ID: 235609 [Multi-domain] Cd Length: 210 Bit Score: 42.16 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62945254 1 MLYLIGLGLGDAKDITVKGLEVVRRCSRVYleaytsvltVGKEALEEFygRKLILADREEV----EQEADNIFKDADVSD 76
Cdd:PRK05787 1 MIYIVGIGPGDPEYLTLKALEAIRKADVVV---------GSKRVLELF--PELIDGEAFVLtaglRDLLEWLELAAKGKN 69
|
....*....
gi 62945254 77 VAFLVVGDP 85
Cdd:PRK05787 70 VVVLSTGDP 78
|
|
| Precorrin_2_C20_MT |
cd11645 |
Precorrin-2 C20-methyltransferase, also named CobI or CbiL; Precorrin-2 C20-methyltransferase ... |
5-86 |
8.24e-04 |
|
Precorrin-2 C20-methyltransferase, also named CobI or CbiL; Precorrin-2 C20-methyltransferase (also known as S-adenosyl-L-methionine--precorrin-2 methyltransferase) participates in the pathway toward the biosynthesis of cobalamin (vitamin B12). There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. Precorrin-2 C20-methyltransferase catalyzes methylation at the C-20 position of a cyclic tetrapyrrole ring of precorrin-2 using S-adenosylmethionine as a methyl group source to produce precorrin-3A. In the anaerobic pathway, cobalt is inserted into precorrin-2 by CbiK to generate cobalt-precorrin-2, which is the substrate for CbiL, a C20 methyltransferase. In Clostridium difficile, CbiK and CbiL are fused into a bifunctional enzyme. In the aerobic pathway, the precorrin-2 C20-methyltransferase is named CobI. This family includes CbiL and CobI precorrin-2 C20-methyltransferases, both as stand-alone enzymes and when CbiL forms part of a bifunctional enzyme.
Pssm-ID: 381172 [Multi-domain] Cd Length: 223 Bit Score: 39.80 E-value: 8.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62945254 5 IGLGLGDAKDITVKGLEVVRRCSRVyleaYTSVLTVGKEALEEFYGRKLILADREEVE-----------------QEADN 67
Cdd:cd11645 1 VGVGPGDPELLTLKAVRILKEADVI----FVPVSKGGEGSAALIIAAALLIPDKEIIPlefpmtkdreeleeawdEAAEE 76
|
90 100
....*....|....*....|
gi 62945254 68 IFKDADVS-DVAFLVVGDPF 86
Cdd:cd11645 77 IAEELKEGkDVAFLTLGDPS 96
|
|
| Precorrin-4_C11-MT |
cd11641 |
Precorrin-4 C11-methyltransferase (CbiF/CobM); Precorrin-4 C11-methyltransferase participates ... |
5-108 |
5.65e-03 |
|
Precorrin-4 C11-methyltransferase (CbiF/CobM); Precorrin-4 C11-methyltransferase participates in the pathway toward the biosynthesis of cobalamin (vitamin B12). There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. In the aerobic pathway, CobM catalyzes the methylation of precorrin-4 at C-11 to yield precorrin-5. In the anaerobic pathway, CibF catalyzes the methylation of cobalt-precorrin-4 to cobalt-precorrin-5. Both CibF and CobM, which are homologous, are included in this model. There are about 30 enzymes involved in vitamin B12 synthetic pathway. The enzymes involved in the aerobic pathway are prefixed Cob and those of the anaerobic pathway Cbi. Most of the enzymes are shared in both pathways and several of these enzymes are pathway-specific.
Pssm-ID: 381168 [Multi-domain] Cd Length: 225 Bit Score: 37.37 E-value: 5.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62945254 5 IGLGLGDAKDITVKGLEVVRRCSRVYleaYTSVLtVGKEALEEFYGRKLILA----DREEVEQeadnIFKDA--DVSDVA 78
Cdd:cd11641 1 VGAGPGDPELITVKGARLLEEADVVI---YAGSL-VPPELLAYAKPGAEIVDsagmTLEEIIE----VMREAarEGKDVV 72
|
90 100 110
....*....|....*....|....*....|..
gi 62945254 79 FLVVGDP--FGATthSDLILRATKLGIPYQVI 108
Cdd:cd11641 73 RLHTGDPslYGAI--REQIDALDKLGIPYEVV 102
|
|
| |
