|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00175 |
PTZ00175 |
diphthine synthase; Provisional |
1-271 |
2.59e-163 |
|
diphthine synthase; Provisional
Pssm-ID: 185500 Cd Length: 270 Bit Score: 454.03 E-value: 2.59e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117190324 1 MLYLIGLGLGDAKDITVKGLEVVRRCSRVYLEAYTSVL-TVGKEALEEFYGRKLVVADREEVEQEADNILKDADISDVAF 79
Cdd:PTZ00175 2 MLYIIGLGLGDEKDITVKGLEAVKSADVVYLESYTSILiNSNKEKLEEFYGKPVIEADREMVEEGCDEILEEAKEKNVAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117190324 80 LVVGDPFGATTHSDLVLRATKLGIPYRVIHNASIMNAVGCCGLQLYKFGETVSIVFWTDTWRPESFFDKVKKNRQNGMHT 159
Cdd:PTZ00175 82 LVVGDPFCATTHTDLYLRAKKKGIEVEVIHNASIMNAIGCTGLQLYRFGETVSIPFFTETWKPDSFYDKIKANRDNGLHT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117190324 160 LCLLDIKVKEQSLENLIKGRKIYEPPRYMSVNQAAQQLLEIVQNqriRGEEPVTEETLCVGLARVGADDQKIAAGTLRQM 239
Cdd:PTZ00175 162 LCLLDIKVKERSVENLMKGRKIYEPPRYMTINQAIEQLLEVEEK---KGGGVIAEDTLVVGVARVGSDDQQIVSGTLEDL 238
|
250 260 270
....*....|....*....|....*....|..
gi 117190324 240 CTVDLGEPLHSLIITGGSIHPMEMEMLSLFSI 271
Cdd:PTZ00175 239 LDVDFGPPLHSLVICAPTLHDIEEEFFELYRI 270
|
|
| DHP5_DphB |
cd11647 |
diphthine methyl ester synthase and diphthine synthase; Eukaryotic diphthine methyl ester ... |
1-255 |
1.28e-139 |
|
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: 392.94 E-value: 1.28e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117190324 1 MLYLIGLGLGDAKDITVKGLEVVRRCSRVYLEAYTSVLTVGK-EALEEFYGRKLVVADREEVEQEADNILKDADISDVAF 79
Cdd:cd11647 1 MLYLIGLGLGDEKDITLEGLEALKKADKVYLEAYTSILPGSKlEELEKLIGKKIILLDREDLEEESEEILEEAKKKDVAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117190324 80 LVVGDPFGATTHSDLVLRATKLGIPYRVIHNASIMNAVGCC-GLQLYKFGETVSIVFWTDTWRPESFFDKVKKNRQNGMH 158
Cdd:cd11647 81 LVPGDPLIATTHIDLRLEAKKRGIKVKVIHNASILSAAGSTsGLQLYKFGRTVTIPFPEENYKPESPYDVIKENLKRGLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117190324 159 TLCLLDIKVkeqslenlikgrkiyEPPRYMSVNQAAQQLLEIvqnQRIRGEEPVTEETLCVGLARVGADDQKIAAGTLRQ 238
Cdd:cd11647 161 TLLLLDIKV---------------EEGRFMTINEAIEILLEI---EEKRKEGVITEDTLVVGLARLGSDDQKIVAGTLKE 222
|
250
....*....|....*..
gi 117190324 239 MCTVDLGEPLHSLIITG 255
Cdd:cd11647 223 LLKEDFGPPPHSLIIPG 239
|
|
| DPH5 |
COG1798 |
Diphthamide biosynthesis methyltransferase [Translation, ribosomal structure and biogenesis]; |
1-270 |
1.50e-108 |
|
Diphthamide biosynthesis methyltransferase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441403 Cd Length: 255 Bit Score: 314.82 E-value: 1.50e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117190324 1 MLYLIGLGLGDAKDITVKGLEVVRRCSRVYLEAYTSVLT-VGKEALEEFYGRKLVVADREEVEQEADNILKDADISDVAF 79
Cdd:COG1798 1 MLTFVGLGLSDERDITLKGLEALRSADKVYAEFYTSRLIgTDLEKLEELIGKEIVVLDREDVEDNPEEILEEAKEKDVVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117190324 80 LVVGDPFGATTHSDLVLRATKLGIPYRVIHNASIMNAV-GCCGLQLYKFGETVSIVFWTDTWRPESFFDKVKKNRQNGMH 158
Cdd:COG1798 81 LTAGDPMIATTHVDLRLRAKRRGIETRVIHGVSIVSAAiGLTGLQNYKFGKTVTIPFPYEGFVPTSPYDTIKENLERGLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117190324 159 TLCLLDIKVKEQslenlikgrkiyeppRYMSVNQAAQQLLEIvqnQRIRGEEPVTEETLCVGLARVGADDQKIAAGTLRQ 238
Cdd:COG1798 161 TLVLLDIKADKN---------------RYMTANEALELLLEI---EKKRREGVISDDTLAVVVARAGSPDPKIVAGKLSE 222
|
250 260 270
....*....|....*....|....*....|..
gi 117190324 239 MCTVDLGEPLHSLIITgGSIHPMEMEMLSLFS 270
Cdd:COG1798 223 LANYDFGEPPHSLIIP-GRLHFMEAEALKALA 253
|
|
| dph5 |
TIGR00522 |
diphthine synthase; Alternate name: diphthamide biosynthesis S-adenosylmethionine-dependent ... |
1-270 |
6.49e-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: 292.87 E-value: 6.49e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117190324 1 MLYLIGLGLGDAKDITVKGLEVVRRCSRVYLEAYTSVLTVGK-EALEEFYGRKLVVADREEVEQEADNILKDADISDVAF 79
Cdd:TIGR00522 1 MLYLIGLGLYDENDISVKGLEAIKKADEVYAEFYTSKLLGSSiEEIEEFFGKRVVVLERSDVEENSFRLIERAKSKDVAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117190324 80 LVVGDPFGATTHSDLVLRATKLGIPYRVIHNASIMNAV-GCCGLQLYKFGETVSIVFWTDTWRPESFFDKVKKNRQNGMH 158
Cdd:TIGR00522 81 LVAGDPMVATTHTDLKLEAKRKGIETRIIHGASISSAVcGLTGLQLYKFGKTATIVFFTDNYRPQTPYNVIKENRKIGLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117190324 159 TLCLLDIKVKEqslenlikgrkiyepPRYMSVNQAAQQLLEIvQNQriRGEEPVTEETLCVGLARVGADDQKIAAGTLRQ 238
Cdd:TIGR00522 161 TLVLLDIHPKE---------------NRAMTIGEGLENLLEE-EEK--RKTGAITPDTYAVVIARAGSGKPVVKCDKIEN 222
|
250 260 270
....*....|....*....|....*....|..
gi 117190324 239 MCTVDLGEPLHSLIITGGSIHPMEMEMLSLFS 270
Cdd:TIGR00522 223 LKNYDFGEPLHCLVVLAKTLHFMEFEYLREFA 254
|
|
| TP_methylase |
pfam00590 |
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ... |
1-239 |
1.08e-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: 100.88 E-value: 1.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117190324 1 MLYLIGLGLGDAKDITVKGLEVVRRCSRVYLE---AYTSVLTVGKEALeeFYGRKLVVADREEVEQEADNILKDA--DIS 75
Cdd:pfam00590 1 KLYLVGVGPGDPDLLTLRALRALKEADVVLGDdsrALEILLDLLPEDL--YFPMTEDKEPLEEAYEEIAEALAAAlrAGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117190324 76 DVAFLVVGDPFGATTHSDLVLRATKLGIPYRVIHNASIMNAVGCC-GLQLYKFGETVSIVFWTDT-WRPESFFDKVKKNR 153
Cdd:pfam00590 79 DVARLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARlGIPLTEGGEVLSVLFLPGLaRIELRLLEALLANG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117190324 154 qngmHTLCLLDIKVKeqslenlikgrkiyepprymsVNQAAQQLLEIvqnqrirgeepVTEETLCVGLARVGADDQKIAA 233
Cdd:pfam00590 159 ----DTVVLLYGPRR---------------------LAELAELLLEL-----------YPDTTPVAVVERAGTPDEKVVR 202
|
....*.
gi 117190324 234 GTLRQM 239
Cdd:pfam00590 203 GTLGEL 208
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00175 |
PTZ00175 |
diphthine synthase; Provisional |
1-271 |
2.59e-163 |
|
diphthine synthase; Provisional
Pssm-ID: 185500 Cd Length: 270 Bit Score: 454.03 E-value: 2.59e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117190324 1 MLYLIGLGLGDAKDITVKGLEVVRRCSRVYLEAYTSVL-TVGKEALEEFYGRKLVVADREEVEQEADNILKDADISDVAF 79
Cdd:PTZ00175 2 MLYIIGLGLGDEKDITVKGLEAVKSADVVYLESYTSILiNSNKEKLEEFYGKPVIEADREMVEEGCDEILEEAKEKNVAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117190324 80 LVVGDPFGATTHSDLVLRATKLGIPYRVIHNASIMNAVGCCGLQLYKFGETVSIVFWTDTWRPESFFDKVKKNRQNGMHT 159
Cdd:PTZ00175 82 LVVGDPFCATTHTDLYLRAKKKGIEVEVIHNASIMNAIGCTGLQLYRFGETVSIPFFTETWKPDSFYDKIKANRDNGLHT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117190324 160 LCLLDIKVKEQSLENLIKGRKIYEPPRYMSVNQAAQQLLEIVQNqriRGEEPVTEETLCVGLARVGADDQKIAAGTLRQM 239
Cdd:PTZ00175 162 LCLLDIKVKERSVENLMKGRKIYEPPRYMTINQAIEQLLEVEEK---KGGGVIAEDTLVVGVARVGSDDQQIVSGTLEDL 238
|
250 260 270
....*....|....*....|....*....|..
gi 117190324 240 CTVDLGEPLHSLIITGGSIHPMEMEMLSLFSI 271
Cdd:PTZ00175 239 LDVDFGPPLHSLVICAPTLHDIEEEFFELYRI 270
|
|
| DHP5_DphB |
cd11647 |
diphthine methyl ester synthase and diphthine synthase; Eukaryotic diphthine methyl ester ... |
1-255 |
1.28e-139 |
|
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: 392.94 E-value: 1.28e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117190324 1 MLYLIGLGLGDAKDITVKGLEVVRRCSRVYLEAYTSVLTVGK-EALEEFYGRKLVVADREEVEQEADNILKDADISDVAF 79
Cdd:cd11647 1 MLYLIGLGLGDEKDITLEGLEALKKADKVYLEAYTSILPGSKlEELEKLIGKKIILLDREDLEEESEEILEEAKKKDVAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117190324 80 LVVGDPFGATTHSDLVLRATKLGIPYRVIHNASIMNAVGCC-GLQLYKFGETVSIVFWTDTWRPESFFDKVKKNRQNGMH 158
Cdd:cd11647 81 LVPGDPLIATTHIDLRLEAKKRGIKVKVIHNASILSAAGSTsGLQLYKFGRTVTIPFPEENYKPESPYDVIKENLKRGLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117190324 159 TLCLLDIKVkeqslenlikgrkiyEPPRYMSVNQAAQQLLEIvqnQRIRGEEPVTEETLCVGLARVGADDQKIAAGTLRQ 238
Cdd:cd11647 161 TLLLLDIKV---------------EEGRFMTINEAIEILLEI---EEKRKEGVITEDTLVVGLARLGSDDQKIVAGTLKE 222
|
250
....*....|....*..
gi 117190324 239 MCTVDLGEPLHSLIITG 255
Cdd:cd11647 223 LLKEDFGPPPHSLIIPG 239
|
|
| DPH5 |
COG1798 |
Diphthamide biosynthesis methyltransferase [Translation, ribosomal structure and biogenesis]; |
1-270 |
1.50e-108 |
|
Diphthamide biosynthesis methyltransferase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441403 Cd Length: 255 Bit Score: 314.82 E-value: 1.50e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117190324 1 MLYLIGLGLGDAKDITVKGLEVVRRCSRVYLEAYTSVLT-VGKEALEEFYGRKLVVADREEVEQEADNILKDADISDVAF 79
Cdd:COG1798 1 MLTFVGLGLSDERDITLKGLEALRSADKVYAEFYTSRLIgTDLEKLEELIGKEIVVLDREDVEDNPEEILEEAKEKDVVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117190324 80 LVVGDPFGATTHSDLVLRATKLGIPYRVIHNASIMNAV-GCCGLQLYKFGETVSIVFWTDTWRPESFFDKVKKNRQNGMH 158
Cdd:COG1798 81 LTAGDPMIATTHVDLRLRAKRRGIETRVIHGVSIVSAAiGLTGLQNYKFGKTVTIPFPYEGFVPTSPYDTIKENLERGLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117190324 159 TLCLLDIKVKEQslenlikgrkiyeppRYMSVNQAAQQLLEIvqnQRIRGEEPVTEETLCVGLARVGADDQKIAAGTLRQ 238
Cdd:COG1798 161 TLVLLDIKADKN---------------RYMTANEALELLLEI---EKKRREGVISDDTLAVVVARAGSPDPKIVAGKLSE 222
|
250 260 270
....*....|....*....|....*....|..
gi 117190324 239 MCTVDLGEPLHSLIITgGSIHPMEMEMLSLFS 270
Cdd:COG1798 223 LANYDFGEPPHSLIIP-GRLHFMEAEALKALA 253
|
|
| dph5 |
TIGR00522 |
diphthine synthase; Alternate name: diphthamide biosynthesis S-adenosylmethionine-dependent ... |
1-270 |
6.49e-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: 292.87 E-value: 6.49e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117190324 1 MLYLIGLGLGDAKDITVKGLEVVRRCSRVYLEAYTSVLTVGK-EALEEFYGRKLVVADREEVEQEADNILKDADISDVAF 79
Cdd:TIGR00522 1 MLYLIGLGLYDENDISVKGLEAIKKADEVYAEFYTSKLLGSSiEEIEEFFGKRVVVLERSDVEENSFRLIERAKSKDVAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117190324 80 LVVGDPFGATTHSDLVLRATKLGIPYRVIHNASIMNAV-GCCGLQLYKFGETVSIVFWTDTWRPESFFDKVKKNRQNGMH 158
Cdd:TIGR00522 81 LVAGDPMVATTHTDLKLEAKRKGIETRIIHGASISSAVcGLTGLQLYKFGKTATIVFFTDNYRPQTPYNVIKENRKIGLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117190324 159 TLCLLDIKVKEqslenlikgrkiyepPRYMSVNQAAQQLLEIvQNQriRGEEPVTEETLCVGLARVGADDQKIAAGTLRQ 238
Cdd:TIGR00522 161 TLVLLDIHPKE---------------NRAMTIGEGLENLLEE-EEK--RKTGAITPDTYAVVIARAGSGKPVVKCDKIEN 222
|
250 260 270
....*....|....*....|....*....|..
gi 117190324 239 MCTVDLGEPLHSLIITGGSIHPMEMEMLSLFS 270
Cdd:TIGR00522 223 LKNYDFGEPLHCLVVLAKTLHFMEFEYLREFA 254
|
|
| TP_methylase |
pfam00590 |
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ... |
1-239 |
1.08e-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: 100.88 E-value: 1.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117190324 1 MLYLIGLGLGDAKDITVKGLEVVRRCSRVYLE---AYTSVLTVGKEALeeFYGRKLVVADREEVEQEADNILKDA--DIS 75
Cdd:pfam00590 1 KLYLVGVGPGDPDLLTLRALRALKEADVVLGDdsrALEILLDLLPEDL--YFPMTEDKEPLEEAYEEIAEALAAAlrAGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117190324 76 DVAFLVVGDPFGATTHSDLVLRATKLGIPYRVIHNASIMNAVGCC-GLQLYKFGETVSIVFWTDT-WRPESFFDKVKKNR 153
Cdd:pfam00590 79 DVARLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARlGIPLTEGGEVLSVLFLPGLaRIELRLLEALLANG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117190324 154 qngmHTLCLLDIKVKeqslenlikgrkiyepprymsVNQAAQQLLEIvqnqrirgeepVTEETLCVGLARVGADDQKIAA 233
Cdd:pfam00590 159 ----DTVVLLYGPRR---------------------LAELAELLLEL-----------YPDTTPVAVVERAGTPDEKVVR 202
|
....*.
gi 117190324 234 GTLRQM 239
Cdd:pfam00590 203 GTLGEL 208
|
|
| TP_methylase |
cd09815 |
S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet ... |
5-253 |
6.30e-23 |
|
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: 93.61 E-value: 6.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117190324 5 IGLGLGDAKDITVKGLEVVRRCSRVYLEAYTSVLTVGKEALEEFYG-RKLVVADREEVEQEADNILKDADIS-DVAFLVV 82
Cdd:cd09815 1 VGVGPGDPDLLTLRALEILRAADVVVAEDKDSKLLSLVLRAILKDGkRIYDLHDPNVEEEMAELLLEEARQGkDVAFLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117190324 83 GDPFGATTHSDLVLRATKLGIPYRVIHNASIMNAVGC-CGLQLYKFGETVSIVFWTDTWRpesfFDKVKKNRQNGMHTLC 161
Cdd:cd09815 81 GDPGVAGTGAELVERAEREGVEVKVIPGVSAADAAAAaLGIDLGESFLFVTASDLLENPR----LLVLKALAKERRHLVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117190324 162 LLDIKVKEQSLENLIKgrkiyepprymsvnqaaqqlleivqnqrirgeEPVTEETLCVGLARVGADDQKIAAGTLRQMCT 241
Cdd:cd09815 157 FLDGHRFLKALERLLK--------------------------------ELGEDDTPVVLVANAGSEGEVIRTGTVKELRA 204
|
250
....*....|....
gi 117190324 242 V--DLGEPLHSLII 253
Cdd:cd09815 205 ErtERGKPLTTILV 218
|
|
| YabN_N_like |
cd11723 |
N-terminal S-AdoMet-dependent tetrapyrrole methylase domain of Bacillus subtilis YabN and ... |
2-124 |
6.04e-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: 52.11 E-value: 6.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117190324 2 LYLIGLGLGDAKDITVKGLEVVRRCSRVYL-----EAYTSVLTVGK--EALEEFYGRKlvvADREEVEQE-ADNILKDAD 73
Cdd:cd11723 1 ITIVGLGPGDPDLLTLGALEALKSADKVYLrtarhPVVEELKEEGIefESFDDLYEEA---EDFEEVYEAiAERLLEAAE 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 117190324 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 |
9.38e-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: 51.79 E-value: 9.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117190324 2 LYLIGLGLGDAKDITVKGLEVVRR-----CSRVYLEAYTSVLTvGKEALE------EFYGRKLVVADREEVEQEADNILK 70
Cdd:cd11724 2 LYLVGVGPGDPDLITLRALKAIKKadvvfAPPDLRKRFAEYLA-GKEVLDdphglfTYYGKKCSPLEEAEKECEELEKQR 80
|
90 100
....*....|....*....|....*....
gi 117190324 71 DADIS----------DVAFLVVGDP--FG 87
Cdd:cd11724 81 AEIVQkirealaqgkNVALLDSGDPtiYG 109
|
|
| PRK05576 |
PRK05576 |
cobalt-factor II C(20)-methyltransferase; |
1-108 |
3.05e-07 |
|
cobalt-factor II C(20)-methyltransferase;
Pssm-ID: 235512 [Multi-domain] Cd Length: 229 Bit Score: 50.30 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117190324 1 MLYLIGLGLGDAKDITVKGLEVVRRCSRVYleAYTSVLTVGKEAL---EEFYGRKLVV--------ADREEVEQE----A 65
Cdd:PRK05576 3 KLYGIGLGPGDPELLTVKAARILEEADVVY--APASRKGGGSLALnivRPYLKEETEIvelhfpmsKDEEEKEAVwkenA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 117190324 66 DNILKDA-DISDVAFLVVGDPFGATTHSDLVLRATKLGIPYRVI 108
Cdd:PRK05576 81 EEIAAEAeEGKNVAFITLGDPNLYSTFSHLLEYLKCHDIEVETV 124
|
|
| CobF |
COG2243 |
Precorrin-2 methylase [Coenzyme transport and metabolism]; Precorrin-2 methylase is part of ... |
2-108 |
5.02e-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: 49.33 E-value: 5.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117190324 2 LYLIGLGLGDAKDITVKGLEVVRRCSRV-------------------YLEAYTSV-----LTVGKEALEEFYgrklvvad 57
Cdd:COG2243 5 LYGVGVGPGDPELLTLKAVRALREADVIaypakgagkaslareivapYLPPARIVelvfpMTTDYEALVAAW-------- 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 117190324 58 reevEQEADNILKDADI-SDVAFLVVGDPF--GATTHsdLVLRATKLGIPYRVI 108
Cdd:COG2243 77 ----DEAAARIAEELEAgRDVAFLTEGDPSlySTFMY--LLERLRERGFEVEVI 124
|
|
| cobI_cbiL |
TIGR01467 |
precorrin-2 C(20)-methyltransferase; This model represents precorrin-2 C(20)-methyltransferase, ... |
1-117 |
1.25e-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: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117190324 1 MLYLIGLGLGDAKDITVKGLEVVRRCSRVYLEAytsvltvgKEALEEFYGRKLV------------------VADREEVE 62
Cdd:TIGR01467 2 KLYGVGVGPGDPELITVKALEALRSADVIAVPA--------SKKGRESLARKIVedylkpndtrilelvfpmTKDRDELE 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 117190324 63 Q---EADNILKDA--DISDVAFLVVGDPFGATTHSDLVLRATKLGIPYRVIHNASIMNAV 117
Cdd:TIGR01467 74 KawdEAAEAVAAEleEGRDVAFLTLGDPSLYSTFSYLLQRLQGMGIEVEVVPGITSFAAC 133
|
|
| cobM_cbiF |
TIGR01465 |
precorrin-4 C11-methyltransferase; This model represents precorrin-4 C11-methyltransferase, ... |
2-260 |
2.14e-05 |
|
precorrin-4 C11-methyltransferase; This model represents precorrin-4 C11-methyltransferase, one of two methyltransferases commonly referred to as precorrin-3 methylase (the other is precorrin-3B C17-methyltransferase, EC 2.1.1.131). This enzyme participates in the pathway toward the biosynthesis of cobalamin and related products. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
Pssm-ID: 200107 Cd Length: 247 Bit Score: 44.62 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117190324 2 LYLIGLGLGDAKDITVKGLEVVRRCSRVYleaYTSVLtVGKEALEEFYGRKLVVADREEVEQEADNILKDA--DISDVAF 79
Cdd:TIGR01465 1 VYFIGAGPGDPDLITVKGRKLIESADVIL---YAGSL-VPPELLAHCRPGAEVVNSAGMSLEEIVDIMSDAhrEGKDVAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117190324 80 LVVGDP--FGATTHSDLVLRAtkLGIPYRVIHN-ASIMNAVGCCGLQLYKFGETVSIVFWTDTWR---PEsfFDKVKKNR 153
Cdd:TIGR01465 77 LHSGDPsiYGAIAEQMRLLEA--LGIPYEVVPGvSSFFAAAAALGAELTVPEVSQTVILTRASGRtpmPE--GEKLADLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117190324 154 QNGMhTLCLldikvkeqslenlikgrkiyepprYMSVnqaaqQLLEIVQNQRIRGEEPvtEETLCVGLARVGADDQKIAA 233
Cdd:TIGR01465 153 KHGA-TMAI------------------------FLSA-----HILDKVVKELIEHGYS--EDTPVAVVYRATWPDEKIVR 200
|
250 260
....*....|....*....|....*....
gi 117190324 234 GTLRQMCTVDLGEPL--HSLIITGGSIHP 260
Cdd:TIGR01465 201 GTLADLADLVREEGIyrTTLILVGPALDP 229
|
|
| PRK05787 |
PRK05787 |
cobalt-precorrin-7 (C(5))-methyltransferase; |
1-85 |
9.74e-04 |
|
cobalt-precorrin-7 (C(5))-methyltransferase;
Pssm-ID: 235609 [Multi-domain] Cd Length: 210 Bit Score: 39.47 E-value: 9.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117190324 1 MLYLIGLGLGDAKDITVKGLEVVRRCSRVYleaytsvltVGKEALEEFygRKLVVADREEV----EQEADNILKDADISD 76
Cdd:PRK05787 1 MIYIVGIGPGDPEYLTLKALEAIRKADVVV---------GSKRVLELF--PELIDGEAFVLtaglRDLLEWLELAAKGKN 69
|
....*....
gi 117190324 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 |
1.10e-03 |
|
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: 39.41 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117190324 5 IGLGLGDAKDITVKGLEVVRRCSRVYL---EAYTSVLTVGKEALEEFYGRKLV------VADREEVEQE----ADNILKD 71
Cdd:cd11645 1 VGVGPGDPELLTLKAVRILKEADVIFVpvsKGGEGSAALIIAAALLIPDKEIIplefpmTKDREELEEAwdeaAEEIAEE 80
|
90
....*....|....*.
gi 117190324 72 ADIS-DVAFLVVGDPF 86
Cdd:cd11645 81 LKEGkDVAFLTLGDPS 96
|
|
| Precorrin-6Y-MT |
cd11644 |
Precorrin-6Y methyltransferase (also named CbiE); CbiE (precorrin-6Y methyltransferase, also ... |
5-86 |
6.04e-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: 37.09 E-value: 6.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117190324 5 IGLGLGDAKDITVKGLEVVRRCSRVYleAYTSVLtvgkEALEEFYGRKLVVAdREEVEQEADNILKDADisDVAFLVVGD 84
Cdd:cd11644 1 IGIGPGGPEYLTPEAREAIEEADVVI--GAKRLL----ELFPDLGAEKIPLP-SEDIAELLEEIAEAGK--RVVVLASGD 71
|
..
gi 117190324 85 PF 86
Cdd:cd11644 72 PG 73
|
|
| PLN02625 |
PLN02625 |
uroporphyrin-III C-methyltransferase |
3-137 |
6.73e-03 |
|
uroporphyrin-III C-methyltransferase
Pssm-ID: 178232 [Multi-domain] Cd Length: 263 Bit Score: 37.30 E-value: 6.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117190324 3 YLIGLGLGDAKDITVKGLEVVRRCSRVYLE--AYTSVLTVGKEALEEFYGRKLvvADREEVEQ-EADNILKD--ADISDV 77
Cdd:PLN02625 18 FLVGTGPGDPDLLTLKALRLLQTADVVLYDrlVSPDILDLVPPGAELLYVGKR--GGYHSRTQeEIHELLLSfaEAGKTV 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 117190324 78 AFLVVGDP--FGATTHSDLVLRatKLGIPYRVIhnASIMNAVGCC---GLQLYKFGETVSIVFWT 137
Cdd:PLN02625 96 VRLKGGDPlvFGRGGEEMDALR--KNGIPVTVV--PGITAAIGAPaelGIPLTHRGVATSVRFLT 156
|
|
| Precorrin-4_C11-MT |
cd11641 |
Precorrin-4 C11-methyltransferase (CbiF/CobM); Precorrin-4 C11-methyltransferase participates ... |
5-108 |
7.22e-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: 36.99 E-value: 7.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117190324 5 IGLGLGDAKDITVKGLEVVRRCSRVYleaYTSVLtVGKEALEEFYGRKLVVA----DREEVEQeadnILKDADIS--DVA 78
Cdd:cd11641 1 VGAGPGDPELITVKGARLLEEADVVI---YAGSL-VPPELLAYAKPGAEIVDsagmTLEEIIE----VMREAAREgkDVV 72
|
90 100 110
....*....|....*....|....*....|..
gi 117190324 79 FLVVGDP--FGATTHSDLVLRatKLGIPYRVI 108
Cdd:cd11641 73 RLHTGDPslYGAIREQIDALD--KLGIPYEVV 102
|
|
| |
