|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00175 |
PTZ00175 |
diphthine synthase; Provisional |
1-272 |
1.45e-164 |
|
diphthine synthase; Provisional
Pssm-ID: 185500 Cd Length: 270 Bit Score: 457.11 E-value: 1.45e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872880 1 MLYLIGLGLGDAKDITVKGLEAVRRCSRVYLEAYTSVL-TVGKEALEEFYGRKLILADREEVEQEADNILKDADISDVAF 79
Cdd:PTZ00175 2 MLYIIGLGLGDEKDITVKGLEAVKSADVVYLESYTSILiNSNKEKLEEFYGKPVIEADREMVEEGCDEILEEAKEKNVAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872880 80 LVVGDPFGATTHSDLVLRATKLGIPYRVIHNASIMNAVGCCGLQLYKFGETVSIVFWTDTWRPESFFDKVKKNRQNGMHT 159
Cdd:PTZ00175 82 LVVGDPFCATTHTDLYLRAKKKGIEVEVIHNASIMNAIGCTGLQLYRFGETVSIPFFTETWKPDSFYDKIKANRDNGLHT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872880 160 LCLLDIKVKEQSLENLIKGRKIYEPPRYMSVNQAAQQLLEIIQNQRirgeEPAITEETLCVGLARVGADDQKIAAGTLQQ 239
Cdd:PTZ00175 162 LCLLDIKVKERSVENLMKGRKIYEPPRYMTINQAIEQLLEVEEKKG----GGVIAEDTLVVGVARVGSDDQQIVSGTLED 237
|
250 260 270
....*....|....*....|....*....|...
gi 383872880 240 MCTVDLGEPLHSLIITGGSIHPIEMEMLNLFSI 272
Cdd:PTZ00175 238 LLDVDFGPPLHSLVICAPTLHDIEEEFFELYRI 270
|
|
| DHP5_DphB |
cd11647 |
diphthine methyl ester synthase and diphthine synthase; Eukaryotic diphthine methyl ester ... |
1-256 |
2.01e-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: 389.85 E-value: 2.01e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872880 1 MLYLIGLGLGDAKDITVKGLEAVRRCSRVYLEAYTSVLTVGK-EALEEFYGRKLILADREEVEQEADNILKDADISDVAF 79
Cdd:cd11647 1 MLYLIGLGLGDEKDITLEGLEALKKADKVYLEAYTSILPGSKlEELEKLIGKKIILLDREDLEEESEEILEEAKKKDVAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872880 80 LVVGDPFGATTHSDLVLRATKLGIPYRVIHNASIMNAVGCC-GLQLYKFGETVSIVFWTDTWRPESFFDKVKKNRQNGMH 158
Cdd:cd11647 81 LVPGDPLIATTHIDLRLEAKKRGIKVKVIHNASILSAAGSTsGLQLYKFGRTVTIPFPEENYKPESPYDVIKENLKRGLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872880 159 TLCLLDIKVkeqslenlikgrkiyEPPRYMSVNQAAQQLLEIIQNQRirgeEPAITEETLCVGLARVGADDQKIAAGTLQ 238
Cdd:cd11647 161 TLLLLDIKV---------------EEGRFMTINEAIEILLEIEEKRK----EGVITEDTLVVGLARLGSDDQKIVAGTLK 221
|
250
....*....|....*...
gi 383872880 239 QMCTVDLGEPLHSLIITG 256
Cdd:cd11647 222 ELLKEDFGPPPHSLIIPG 239
|
|
| DPH5 |
COG1798 |
Diphthamide biosynthesis methyltransferase [Translation, ribosomal structure and biogenesis]; |
1-267 |
8.79e-107 |
|
Diphthamide biosynthesis methyltransferase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441403 Cd Length: 255 Bit Score: 310.20 E-value: 8.79e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872880 1 MLYLIGLGLGDAKDITVKGLEAVRRCSRVYLEAYTSVLT-VGKEALEEFYGRKLILADREEVEQEADNILKDADISDVAF 79
Cdd:COG1798 1 MLTFVGLGLSDERDITLKGLEALRSADKVYAEFYTSRLIgTDLEKLEELIGKEIVVLDREDVEDNPEEILEEAKEKDVVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872880 80 LVVGDPFGATTHSDLVLRATKLGIPYRVIHNASIMNAV-GCCGLQLYKFGETVSIVFWTDTWRPESFFDKVKKNRQNGMH 158
Cdd:COG1798 81 LTAGDPMIATTHVDLRLRAKRRGIETRVIHGVSIVSAAiGLTGLQNYKFGKTVTIPFPYEGFVPTSPYDTIKENLERGLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872880 159 TLCLLDIKVKEQslenlikgrkiyeppRYMSVNQAAQQLLEIIQNQRirgeEPAITEETLCVGLARVGADDQKIAAGTLQ 238
Cdd:COG1798 161 TLVLLDIKADKN---------------RYMTANEALELLLEIEKKRR----EGVISDDTLAVVVARAGSPDPKIVAGKLS 221
|
250 260
....*....|....*....|....*....
gi 383872880 239 QMCTVDLGEPLHSLIITgGSIHPIEMEML 267
Cdd:COG1798 222 ELANYDFGEPPHSLIIP-GRLHFMEAEAL 249
|
|
| dph5 |
TIGR00522 |
diphthine synthase; Alternate name: diphthamide biosynthesis S-adenosylmethionine-dependent ... |
1-271 |
2.81e-100 |
|
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: 294.03 E-value: 2.81e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872880 1 MLYLIGLGLGDAKDITVKGLEAVRRCSRVYLEAYTSVLTVGK-EALEEFYGRKLILADREEVEQEADNILKDADISDVAF 79
Cdd:TIGR00522 1 MLYLIGLGLYDENDISVKGLEAIKKADEVYAEFYTSKLLGSSiEEIEEFFGKRVVVLERSDVEENSFRLIERAKSKDVAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872880 80 LVVGDPFGATTHSDLVLRATKLGIPYRVIHNASIMNAV-GCCGLQLYKFGETVSIVFWTDTWRPESFFDKVKKNRQNGMH 158
Cdd:TIGR00522 81 LVAGDPMVATTHTDLKLEAKRKGIETRIIHGASISSAVcGLTGLQLYKFGKTATIVFFTDNYRPQTPYNVIKENRKIGLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872880 159 TLCLLDIKVKEqslenlikgrkiyepPRYMSVNQAAQQLLEiIQNQRirgEEPAITEETLCVGLARVGADDQKIAAGTLQ 238
Cdd:TIGR00522 161 TLVLLDIHPKE---------------NRAMTIGEGLENLLE-EEEKR---KTGAITPDTYAVVIARAGSGKPVVKCDKIE 221
|
250 260 270
....*....|....*....|....*....|...
gi 383872880 239 QMCTVDLGEPLHSLIITGGSIHPIEMEMLNLFS 271
Cdd:TIGR00522 222 NLKNYDFGEPLHCLVVLAKTLHFMEFEYLREFA 254
|
|
| TP_methylase |
pfam00590 |
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ... |
1-240 |
1.31e-25 |
|
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: 100.49 E-value: 1.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872880 1 MLYLIGLGLGDAKDITVKGLEAVRRCSRVYLE---AYTSVLTVGKEALeeFYGRKLILADREEVEQEADNILKDA--DIS 75
Cdd:pfam00590 1 KLYLVGVGPGDPDLLTLRALRALKEADVVLGDdsrALEILLDLLPEDL--YFPMTEDKEPLEEAYEEIAEALAAAlrAGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872880 76 DVAFLVVGDPFGATTHSDLVLRATKLGIPYRVIHNASIMNAVGCC-GLQLYKFGETVSIVFWTDT-WRPESFFDKVKKNR 153
Cdd:pfam00590 79 DVARLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARlGIPLTEGGEVLSVLFLPGLaRIELRLLEALLANG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872880 154 qngmHTLCLLDIKVKeqslenlikgrkiyepprymsVNQAAQQLLEiiqnqrirgeepAITEETLCVGLARVGADDQKIA 233
Cdd:pfam00590 159 ----DTVVLLYGPRR---------------------LAELAELLLE------------LYPDTTPVAVVERAGTPDEKVV 201
|
....*..
gi 383872880 234 AGTLQQM 240
Cdd:pfam00590 202 RGTLGEL 208
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00175 |
PTZ00175 |
diphthine synthase; Provisional |
1-272 |
1.45e-164 |
|
diphthine synthase; Provisional
Pssm-ID: 185500 Cd Length: 270 Bit Score: 457.11 E-value: 1.45e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872880 1 MLYLIGLGLGDAKDITVKGLEAVRRCSRVYLEAYTSVL-TVGKEALEEFYGRKLILADREEVEQEADNILKDADISDVAF 79
Cdd:PTZ00175 2 MLYIIGLGLGDEKDITVKGLEAVKSADVVYLESYTSILiNSNKEKLEEFYGKPVIEADREMVEEGCDEILEEAKEKNVAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872880 80 LVVGDPFGATTHSDLVLRATKLGIPYRVIHNASIMNAVGCCGLQLYKFGETVSIVFWTDTWRPESFFDKVKKNRQNGMHT 159
Cdd:PTZ00175 82 LVVGDPFCATTHTDLYLRAKKKGIEVEVIHNASIMNAIGCTGLQLYRFGETVSIPFFTETWKPDSFYDKIKANRDNGLHT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872880 160 LCLLDIKVKEQSLENLIKGRKIYEPPRYMSVNQAAQQLLEIIQNQRirgeEPAITEETLCVGLARVGADDQKIAAGTLQQ 239
Cdd:PTZ00175 162 LCLLDIKVKERSVENLMKGRKIYEPPRYMTINQAIEQLLEVEEKKG----GGVIAEDTLVVGVARVGSDDQQIVSGTLED 237
|
250 260 270
....*....|....*....|....*....|...
gi 383872880 240 MCTVDLGEPLHSLIITGGSIHPIEMEMLNLFSI 272
Cdd:PTZ00175 238 LLDVDFGPPLHSLVICAPTLHDIEEEFFELYRI 270
|
|
| DHP5_DphB |
cd11647 |
diphthine methyl ester synthase and diphthine synthase; Eukaryotic diphthine methyl ester ... |
1-256 |
2.01e-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: 389.85 E-value: 2.01e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872880 1 MLYLIGLGLGDAKDITVKGLEAVRRCSRVYLEAYTSVLTVGK-EALEEFYGRKLILADREEVEQEADNILKDADISDVAF 79
Cdd:cd11647 1 MLYLIGLGLGDEKDITLEGLEALKKADKVYLEAYTSILPGSKlEELEKLIGKKIILLDREDLEEESEEILEEAKKKDVAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872880 80 LVVGDPFGATTHSDLVLRATKLGIPYRVIHNASIMNAVGCC-GLQLYKFGETVSIVFWTDTWRPESFFDKVKKNRQNGMH 158
Cdd:cd11647 81 LVPGDPLIATTHIDLRLEAKKRGIKVKVIHNASILSAAGSTsGLQLYKFGRTVTIPFPEENYKPESPYDVIKENLKRGLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872880 159 TLCLLDIKVkeqslenlikgrkiyEPPRYMSVNQAAQQLLEIIQNQRirgeEPAITEETLCVGLARVGADDQKIAAGTLQ 238
Cdd:cd11647 161 TLLLLDIKV---------------EEGRFMTINEAIEILLEIEEKRK----EGVITEDTLVVGLARLGSDDQKIVAGTLK 221
|
250
....*....|....*...
gi 383872880 239 QMCTVDLGEPLHSLIITG 256
Cdd:cd11647 222 ELLKEDFGPPPHSLIIPG 239
|
|
| DPH5 |
COG1798 |
Diphthamide biosynthesis methyltransferase [Translation, ribosomal structure and biogenesis]; |
1-267 |
8.79e-107 |
|
Diphthamide biosynthesis methyltransferase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441403 Cd Length: 255 Bit Score: 310.20 E-value: 8.79e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872880 1 MLYLIGLGLGDAKDITVKGLEAVRRCSRVYLEAYTSVLT-VGKEALEEFYGRKLILADREEVEQEADNILKDADISDVAF 79
Cdd:COG1798 1 MLTFVGLGLSDERDITLKGLEALRSADKVYAEFYTSRLIgTDLEKLEELIGKEIVVLDREDVEDNPEEILEEAKEKDVVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872880 80 LVVGDPFGATTHSDLVLRATKLGIPYRVIHNASIMNAV-GCCGLQLYKFGETVSIVFWTDTWRPESFFDKVKKNRQNGMH 158
Cdd:COG1798 81 LTAGDPMIATTHVDLRLRAKRRGIETRVIHGVSIVSAAiGLTGLQNYKFGKTVTIPFPYEGFVPTSPYDTIKENLERGLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872880 159 TLCLLDIKVKEQslenlikgrkiyeppRYMSVNQAAQQLLEIIQNQRirgeEPAITEETLCVGLARVGADDQKIAAGTLQ 238
Cdd:COG1798 161 TLVLLDIKADKN---------------RYMTANEALELLLEIEKKRR----EGVISDDTLAVVVARAGSPDPKIVAGKLS 221
|
250 260
....*....|....*....|....*....
gi 383872880 239 QMCTVDLGEPLHSLIITgGSIHPIEMEML 267
Cdd:COG1798 222 ELANYDFGEPPHSLIIP-GRLHFMEAEAL 249
|
|
| dph5 |
TIGR00522 |
diphthine synthase; Alternate name: diphthamide biosynthesis S-adenosylmethionine-dependent ... |
1-271 |
2.81e-100 |
|
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: 294.03 E-value: 2.81e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872880 1 MLYLIGLGLGDAKDITVKGLEAVRRCSRVYLEAYTSVLTVGK-EALEEFYGRKLILADREEVEQEADNILKDADISDVAF 79
Cdd:TIGR00522 1 MLYLIGLGLYDENDISVKGLEAIKKADEVYAEFYTSKLLGSSiEEIEEFFGKRVVVLERSDVEENSFRLIERAKSKDVAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872880 80 LVVGDPFGATTHSDLVLRATKLGIPYRVIHNASIMNAV-GCCGLQLYKFGETVSIVFWTDTWRPESFFDKVKKNRQNGMH 158
Cdd:TIGR00522 81 LVAGDPMVATTHTDLKLEAKRKGIETRIIHGASISSAVcGLTGLQLYKFGKTATIVFFTDNYRPQTPYNVIKENRKIGLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872880 159 TLCLLDIKVKEqslenlikgrkiyepPRYMSVNQAAQQLLEiIQNQRirgEEPAITEETLCVGLARVGADDQKIAAGTLQ 238
Cdd:TIGR00522 161 TLVLLDIHPKE---------------NRAMTIGEGLENLLE-EEEKR---KTGAITPDTYAVVIARAGSGKPVVKCDKIE 221
|
250 260 270
....*....|....*....|....*....|...
gi 383872880 239 QMCTVDLGEPLHSLIITGGSIHPIEMEMLNLFS 271
Cdd:TIGR00522 222 NLKNYDFGEPLHCLVVLAKTLHFMEFEYLREFA 254
|
|
| TP_methylase |
pfam00590 |
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ... |
1-240 |
1.31e-25 |
|
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: 100.49 E-value: 1.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872880 1 MLYLIGLGLGDAKDITVKGLEAVRRCSRVYLE---AYTSVLTVGKEALeeFYGRKLILADREEVEQEADNILKDA--DIS 75
Cdd:pfam00590 1 KLYLVGVGPGDPDLLTLRALRALKEADVVLGDdsrALEILLDLLPEDL--YFPMTEDKEPLEEAYEEIAEALAAAlrAGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872880 76 DVAFLVVGDPFGATTHSDLVLRATKLGIPYRVIHNASIMNAVGCC-GLQLYKFGETVSIVFWTDT-WRPESFFDKVKKNR 153
Cdd:pfam00590 79 DVARLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARlGIPLTEGGEVLSVLFLPGLaRIELRLLEALLANG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872880 154 qngmHTLCLLDIKVKeqslenlikgrkiyepprymsVNQAAQQLLEiiqnqrirgeepAITEETLCVGLARVGADDQKIA 233
Cdd:pfam00590 159 ----DTVVLLYGPRR---------------------LAELAELLLE------------LYPDTTPVAVVERAGTPDEKVV 201
|
....*..
gi 383872880 234 AGTLQQM 240
Cdd:pfam00590 202 RGTLGEL 208
|
|
| TP_methylase |
cd09815 |
S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet ... |
5-254 |
1.08e-22 |
|
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: 93.23 E-value: 1.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872880 5 IGLGLGDAKDITVKGLEAVRRCSRVYLEAYTSVLTVGKEALEEFYG-RKLILADREEVEQEADNILKDADIS-DVAFLVV 82
Cdd:cd09815 1 VGVGPGDPDLLTLRALEILRAADVVVAEDKDSKLLSLVLRAILKDGkRIYDLHDPNVEEEMAELLLEEARQGkDVAFLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872880 83 GDPFGATTHSDLVLRATKLGIPYRVIHNASIMNAVGC-CGLQLYKFGETVSIVFWTDTWRpesfFDKVKKNRQNGMHTLC 161
Cdd:cd09815 81 GDPGVAGTGAELVERAEREGVEVKVIPGVSAADAAAAaLGIDLGESFLFVTASDLLENPR----LLVLKALAKERRHLVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872880 162 LLDIKVKEQSLENLIkgrKIYEPPrymsvnqaaqqlleiiqnqrirgeepaiteETLCVGLARVGADDQKIAAGTLQQMC 241
Cdd:cd09815 157 FLDGHRFLKALERLL---KELGED------------------------------DTPVVLVANAGSEGEVIRTGTVKELR 203
|
250
....*....|....*
gi 383872880 242 TV--DLGEPLHSLII 254
Cdd:cd09815 204 AErtERGKPLTTILV 218
|
|
| YabN_N_like |
cd11723 |
N-terminal S-AdoMet-dependent tetrapyrrole methylase domain of Bacillus subtilis YabN and ... |
2-124 |
2.90e-08 |
|
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: 52.88 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872880 2 LYLIGLGLGDAKDITVKGLEAVRRCSRVYL-----EAYTSVLTVGK--EALEEFYGRKlilADREEVEQE-ADNILKDAD 73
Cdd:cd11723 1 ITIVGLGPGDPDLLTLGALEALKSADKVYLrtarhPVVEELKEEGIefESFDDLYEEA---EDFEEVYEAiAERLLEAAE 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 383872880 74 ISDVAFLVVGDPFGATTHSDLVLRATKLGIPYRVIHNAS----IMNAVGCC---GLQL 124
Cdd:cd11723 78 HGDVVYAVPGHPLVAERTVQLLLERAEEGIEVEIIPGVSfldaALAALGIDpieGLQI 135
|
|
| TP_methylase |
cd11724 |
uncharacterized family of the tetrapyrrole methylase superfamily; Members of this superfamily ... |
2-87 |
1.37e-07 |
|
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: 51.40 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872880 2 LYLIGLGLGDAKDITVKGLEAVRR-----CSRVYLEAYTSVLTvGKEALE------EFYGRKLILADREEVEQEADNILK 70
Cdd:cd11724 2 LYLVGVGPGDPDLITLRALKAIKKadvvfAPPDLRKRFAEYLA-GKEVLDdphglfTYYGKKCSPLEEAEKECEELEKQR 80
|
90 100
....*....|....*....|....*....
gi 383872880 71 DADIS----------DVAFLVVGDP--FG 87
Cdd:cd11724 81 AEIVQkirealaqgkNVALLDSGDPtiYG 109
|
|
| CobF |
COG2243 |
Precorrin-2 methylase [Coenzyme transport and metabolism]; Precorrin-2 methylase is part of ... |
2-108 |
3.11e-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: 50.10 E-value: 3.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872880 2 LYLIGLGLGDAKDITVKGLEAVRRCSRV-------------------YLEAYTSV-----LTVGKEALEEFYgrklilad 57
Cdd:COG2243 5 LYGVGVGPGDPELLTLKAVRALREADVIaypakgagkaslareivapYLPPARIVelvfpMTTDYEALVAAW-------- 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 383872880 58 reevEQEADNILKDADI-SDVAFLVVGDPF--GATTHsdLVLRATKLGIPYRVI 108
Cdd:COG2243 77 ----DEAAARIAEELEAgRDVAFLTEGDPSlySTFMY--LLERLRERGFEVEVI 124
|
|
| PRK05576 |
PRK05576 |
cobalt-factor II C(20)-methyltransferase; |
1-108 |
7.70e-07 |
|
cobalt-factor II C(20)-methyltransferase;
Pssm-ID: 235512 [Multi-domain] Cd Length: 229 Bit Score: 48.76 E-value: 7.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872880 1 MLYLIGLGLGDAKDITVKGLEAVRRCSRVYleAYTSVLTVGKEAL---EEFYGRKLIL--------ADREEVEQE----A 65
Cdd:PRK05576 3 KLYGIGLGPGDPELLTVKAARILEEADVVY--APASRKGGGSLALnivRPYLKEETEIvelhfpmsKDEEEKEAVwkenA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 383872880 66 DNILKDA-DISDVAFLVVGDPFGATTHSDLVLRATKLGIPYRVI 108
Cdd:PRK05576 81 EEIAAEAeEGKNVAFITLGDPNLYSTFSHLLEYLKCHDIEVETV 124
|
|
| cobI_cbiL |
TIGR01467 |
precorrin-2 C(20)-methyltransferase; This model represents precorrin-2 C(20)-methyltransferase, ... |
1-117 |
9.82e-06 |
|
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: 45.76 E-value: 9.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872880 1 MLYLIGLGLGDAKDITVKGLEAVRRCSRVYLEAytsvltvgKEALEEFYGRKLIL------------------ADREEVE 62
Cdd:TIGR01467 2 KLYGVGVGPGDPELITVKALEALRSADVIAVPA--------SKKGRESLARKIVEdylkpndtrilelvfpmtKDRDELE 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872880 63 Q---EADNILKDA--DISDVAFLVVGDPFGATTHSDLVLRATKLGIPYRVIHNASIMNAV 117
Cdd:TIGR01467 74 KawdEAAEAVAAEleEGRDVAFLTLGDPSLYSTFSYLLQRLQGMGIEVEVVPGITSFAAC 133
|
|
| PRK05787 |
PRK05787 |
cobalt-precorrin-7 (C(5))-methyltransferase; |
1-85 |
6.98e-05 |
|
cobalt-precorrin-7 (C(5))-methyltransferase;
Pssm-ID: 235609 [Multi-domain] Cd Length: 210 Bit Score: 42.93 E-value: 6.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872880 1 MLYLIGLGLGDAKDITVKGLEAVRRCSRVYleaytsvltVGKEALEEFygRKLILADREEV----EQEADNILKDADISD 76
Cdd:PRK05787 1 MIYIVGIGPGDPEYLTLKALEAIRKADVVV---------GSKRVLELF--PELIDGEAFVLtaglRDLLEWLELAAKGKN 69
|
....*....
gi 383872880 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 |
7.28e-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: 7.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872880 5 IGLGLGDAKDITVKGLEAVRRCSRVyleaYTSVLTVGKEALEEFYGRKLILADREEVE-----------------QEADN 67
Cdd:cd11645 1 VGVGPGDPELLTLKAVRILKEADVI----FVPVSKGGEGSAALIIAAALLIPDKEIIPlefpmtkdreeleeawdEAAEE 76
|
90 100
....*....|....*....|
gi 383872880 68 ILKDADIS-DVAFLVVGDPF 86
Cdd:cd11645 77 IAEELKEGkDVAFLTLGDPS 96
|
|
| Precorrin-6Y-MT |
cd11644 |
Precorrin-6Y methyltransferase (also named CbiE); CbiE (precorrin-6Y methyltransferase, also ... |
5-86 |
3.55e-03 |
|
Precorrin-6Y methyltransferase (also named CbiE); CbiE (precorrin-6Y methyltransferase, also known as cobalt-precorrin-7 C(5)-methyltransferase, also known as cobalt-precorrin-6Y C(5)-methyltransferase) catalyzes the methylation of C-5 in cobalt-precorrin-7 to form cobalt-precorrin-8. It 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. CbiE functions in the anaerobic pathway, it is a subunit of precorrin-6Y C5,15-methyltransferase, a bifunctional enzyme: cobalt-precorrin-7 C(5)-methyltransferase (CbiE)/cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating) (CbiT), that catalyzes two methylations (at C-5 and C-15) in precorrin-6Y, as well as the decarboxylation of the acetate side chain located in ring C, in order to generate precorrin-8X. CbiE and CbiT can be found fused (CbiET, also called CobL), or on separate protein chains (CbiE and CbiT). In the aerobic pathway, a single enzyme called CobL catalyzes the methylations at C-5 and C-15, and the decarboxylation of the C-12 acetate side chain of precorrin-6B.
Pssm-ID: 381171 [Multi-domain] Cd Length: 198 Bit Score: 37.86 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872880 5 IGLGLGDAKDITVKGLEAVRRCSRVYleAYTSVLtvgkEALEEFYGRKLILAdREEVEQEADNILKDADisDVAFLVVGD 84
Cdd:cd11644 1 IGIGPGGPEYLTPEAREAIEEADVVI--GAKRLL----ELFPDLGAEKIPLP-SEDIAELLEEIAEAGK--RVVVLASGD 71
|
..
gi 383872880 85 PF 86
Cdd:cd11644 72 PG 73
|
|
| PLN02625 |
PLN02625 |
uroporphyrin-III C-methyltransferase |
3-137 |
7.02e-03 |
|
uroporphyrin-III C-methyltransferase
Pssm-ID: 178232 [Multi-domain] Cd Length: 263 Bit Score: 37.30 E-value: 7.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383872880 3 YLIGLGLGDAKDITVKGLEAVRRCSRVYLE--AYTSVLTVGKEALEEFYGRKliLADREEVEQ-EADNILKD--ADISDV 77
Cdd:PLN02625 18 FLVGTGPGDPDLLTLKALRLLQTADVVLYDrlVSPDILDLVPPGAELLYVGK--RGGYHSRTQeEIHELLLSfaEAGKTV 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 383872880 78 AFLVVGDP--FGATTHSDLVLRatKLGIPYRVIhnASIMNAVGCC---GLQLYKFGETVSIVFWT 137
Cdd:PLN02625 96 VRLKGGDPlvFGRGGEEMDALR--KNGIPVTVV--PGITAAIGAPaelGIPLTHRGVATSVRFLT 156
|
|
| |
