|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00175 |
PTZ00175 |
diphthine synthase; Provisional |
1-270 |
1.36e-154 |
|
diphthine synthase; Provisional
Pssm-ID: 185500 Cd Length: 270 Bit Score: 431.69 E-value: 1.36e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194746329 1 MFYLIGLGLGDLKDITVKGLEIVKQCSRVYLEMYTSILG-CSLEDMQEFYGRPLLLADRDLVEQGADEILSGAGESDVAL 79
Cdd:PTZ00175 2 MLYIIGLGLGDEKDITVKGLEAVKSADVVYLESYTSILInSNKEKLEEFYGKPVIEADREMVEEGCDEILEEAKEKNVAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194746329 80 LVVGDPFGATTHTDFILRAKEKNIPYKVIHNASIMNAVGCCGLQLYKFGETVSIPYWDETWKPDSFYDKIKLNRLHNMHT 159
Cdd:PTZ00175 82 LVVGDPFCATTHTDLYLRAKKKGIEVEVIHNASIMNAIGCTGLQLYRFGETVSIPFFTETWKPDSFYDKIKANRDNGLHT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194746329 160 LCLLDIKVKEPTPESLMRKRKEYMPPRFMSVAEAAHQLLAIVEKKdsleKNTVLNEQSLCVGLARVGQESQQIAVGTLLE 239
Cdd:PTZ00175 162 LCLLDIKVKERSVENLMKGRKIYEPPRYMTINQAIEQLLEVEEKK----GGGVIAEDTLVVGVARVGSDDQQIVSGTLED 237
|
250 260 270
....*....|....*....|....*....|.
gi 194746329 240 MRSTDMGGPLHSLIIPAKEMHPLEVEFLQQY 270
Cdd:PTZ00175 238 LLDVDFGPPLHSLVICAPTLHDIEEEFFELY 268
|
|
| DHP5_DphB |
cd11647 |
diphthine methyl ester synthase and diphthine synthase; Eukaryotic diphthine methyl ester ... |
1-257 |
3.17e-133 |
|
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: 376.76 E-value: 3.17e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194746329 1 MFYLIGLGLGDLKDITVKGLEIVKQCSRVYLEMYTSILGCS-LEDMQEFYGRPLLLADRDLVEQGADEILSGAGESDVAL 79
Cdd:cd11647 1 MLYLIGLGLGDEKDITLEGLEALKKADKVYLEAYTSILPGSkLEELEKLIGKKIILLDREDLEEESEEILEEAKKKDVAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194746329 80 LVVGDPFGATTHTDFILRAKEKNIPYKVIHNASIMNAVGCC-GLQLYKFGETVSIPYWDETWKPDSFYDKIKLNRLHNMH 158
Cdd:cd11647 81 LVPGDPLIATTHIDLRLEAKKRGIKVKVIHNASILSAAGSTsGLQLYKFGRTVTIPFPEENYKPESPYDVIKENLKRGLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194746329 159 TLCLLDIKVKeptpeslmrkrkeymPPRFMSVAEAAHQLLAIVEKKdsleKNTVLNEQSLCVGLARVGQESQQIAVGTLL 238
Cdd:cd11647 161 TLLLLDIKVE---------------EGRFMTINEAIEILLEIEEKR----KEGVITEDTLVVGLARLGSDDQKIVAGTLK 221
|
250
....*....|....*....
gi 194746329 239 EMRSTDMGGPLHSLIIPAK 257
Cdd:cd11647 222 ELLKEDFGPPPHSLIIPGK 240
|
|
| DPH5 |
COG1798 |
Diphthamide biosynthesis methyltransferase [Translation, ribosomal structure and biogenesis]; |
1-267 |
3.03e-103 |
|
Diphthamide biosynthesis methyltransferase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441403 Cd Length: 255 Bit Score: 301.34 E-value: 3.03e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194746329 1 MFYLIGLGLGDLKDITVKGLEIVKQCSRVYLEMYTSIL-GCSLEDMQEFYGRPLLLADRDLVEQGADEILSGAGESDVAL 79
Cdd:COG1798 1 MLTFVGLGLSDERDITLKGLEALRSADKVYAEFYTSRLiGTDLEKLEELIGKEIVVLDREDVEDNPEEILEEAKEKDVVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194746329 80 LVVGDPFGATTHTDFILRAKEKNIPYKVIHNASIMNAV-GCCGLQLYKFGETVSIPYWDETWKPDSFYDKIKLNRLHNMH 158
Cdd:COG1798 81 LTAGDPMIATTHVDLRLRAKRRGIETRVIHGVSIVSAAiGLTGLQNYKFGKTVTIPFPYEGFVPTSPYDTIKENLERGLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194746329 159 TLCLLDIKVKEptpeslmrkrkeympPRFMSVAEAAHQLLAIvEKKdslEKNTVLNEQSLCVGLARVGQESQQIAVGTLL 238
Cdd:COG1798 161 TLVLLDIKADK---------------NRYMTANEALELLLEI-EKK---RREGVISDDTLAVVVARAGSPDPKIVAGKLS 221
|
250 260
....*....|....*....|....*....
gi 194746329 239 EMRSTDMGGPLHSLIIPAKeMHPLEVEFL 267
Cdd:COG1798 222 ELANYDFGEPPHSLIIPGR-LHFMEAEAL 249
|
|
| dph5 |
TIGR00522 |
diphthine synthase; Alternate name: diphthamide biosynthesis S-adenosylmethionine-dependent ... |
1-274 |
8.01e-94 |
|
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: 277.47 E-value: 8.01e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194746329 1 MFYLIGLGLGDLKDITVKGLEIVKQCSRVYLEMYTSIL-GCSLEDMQEFYGRPLLLADRDLVEQGADEILSGAGESDVAL 79
Cdd:TIGR00522 1 MLYLIGLGLYDENDISVKGLEAIKKADEVYAEFYTSKLlGSSIEEIEEFFGKRVVVLERSDVEENSFRLIERAKSKDVAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194746329 80 LVVGDPFGATTHTDFILRAKEKNIPYKVIHNASIMNAV-GCCGLQLYKFGETVSIPYWDETWKPDSFYDKIKLNRLHNMH 158
Cdd:TIGR00522 81 LVAGDPMVATTHTDLKLEAKRKGIETRIIHGASISSAVcGLTGLQLYKFGKTATIVFFTDNYRPQTPYNVIKENRKIGLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194746329 159 TLCLLDIKVKEptpeslmrkrkeympPRFMSVAEAAHQLLAIVEKKdsleKNTVLNEQSLCVGLARVGQESQQIAVGTLL 238
Cdd:TIGR00522 161 TLVLLDIHPKE---------------NRAMTIGEGLENLLEEEEKR----KTGAITPDTYAVVIARAGSGKPVVKCDKIE 221
|
250 260 270
....*....|....*....|....*....|....*.
gi 194746329 239 EMRSTDMGGPLHSLIIPAKEMHPLEVEFLQQYAASI 274
Cdd:TIGR00522 222 NLKNYDFGEPLHCLVVLAKTLHFMEFEYLREFADAP 257
|
|
| TP_methylase |
pfam00590 |
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ... |
1-240 |
1.42e-20 |
|
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: 87.01 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194746329 1 MFYLIGLGLGDLKDITVKGLEIVKQCSRVYLEM--YTSILGCSLEDMQEF----YGRPLLLADRDLVEQGADEILSGAge 74
Cdd:pfam00590 1 KLYLVGVGPGDPDLLTLRALRALKEADVVLGDDsrALEILLDLLPEDLYFpmteDKEPLEEAYEEIAEALAAALRAGK-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194746329 75 sDVALLVVGDPFGATTHTDFILRAKEKNIPYKVIHNASIMNAVGCC-GLQLYKFGETVSIPYWDET-WKPDSFYDKIkln 152
Cdd:pfam00590 79 -DVARLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARlGIPLTEGGEVLSVLFLPGLaRIELRLLEAL--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194746329 153 rLHNMHTLCLLdikvkeptpeslmrkrkeYMPPRFmsvAEAAHQLLAIVekkdslekntvlNEQSLCVGLARVGQESQQI 232
Cdd:pfam00590 155 -LANGDTVVLL------------------YGPRRL---AELAELLLELY------------PDTTPVAVVERAGTPDEKV 200
|
....*...
gi 194746329 233 AVGTLLEM 240
Cdd:pfam00590 201 VRGTLGEL 208
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00175 |
PTZ00175 |
diphthine synthase; Provisional |
1-270 |
1.36e-154 |
|
diphthine synthase; Provisional
Pssm-ID: 185500 Cd Length: 270 Bit Score: 431.69 E-value: 1.36e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194746329 1 MFYLIGLGLGDLKDITVKGLEIVKQCSRVYLEMYTSILG-CSLEDMQEFYGRPLLLADRDLVEQGADEILSGAGESDVAL 79
Cdd:PTZ00175 2 MLYIIGLGLGDEKDITVKGLEAVKSADVVYLESYTSILInSNKEKLEEFYGKPVIEADREMVEEGCDEILEEAKEKNVAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194746329 80 LVVGDPFGATTHTDFILRAKEKNIPYKVIHNASIMNAVGCCGLQLYKFGETVSIPYWDETWKPDSFYDKIKLNRLHNMHT 159
Cdd:PTZ00175 82 LVVGDPFCATTHTDLYLRAKKKGIEVEVIHNASIMNAIGCTGLQLYRFGETVSIPFFTETWKPDSFYDKIKANRDNGLHT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194746329 160 LCLLDIKVKEPTPESLMRKRKEYMPPRFMSVAEAAHQLLAIVEKKdsleKNTVLNEQSLCVGLARVGQESQQIAVGTLLE 239
Cdd:PTZ00175 162 LCLLDIKVKERSVENLMKGRKIYEPPRYMTINQAIEQLLEVEEKK----GGGVIAEDTLVVGVARVGSDDQQIVSGTLED 237
|
250 260 270
....*....|....*....|....*....|.
gi 194746329 240 MRSTDMGGPLHSLIIPAKEMHPLEVEFLQQY 270
Cdd:PTZ00175 238 LLDVDFGPPLHSLVICAPTLHDIEEEFFELY 268
|
|
| DHP5_DphB |
cd11647 |
diphthine methyl ester synthase and diphthine synthase; Eukaryotic diphthine methyl ester ... |
1-257 |
3.17e-133 |
|
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: 376.76 E-value: 3.17e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194746329 1 MFYLIGLGLGDLKDITVKGLEIVKQCSRVYLEMYTSILGCS-LEDMQEFYGRPLLLADRDLVEQGADEILSGAGESDVAL 79
Cdd:cd11647 1 MLYLIGLGLGDEKDITLEGLEALKKADKVYLEAYTSILPGSkLEELEKLIGKKIILLDREDLEEESEEILEEAKKKDVAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194746329 80 LVVGDPFGATTHTDFILRAKEKNIPYKVIHNASIMNAVGCC-GLQLYKFGETVSIPYWDETWKPDSFYDKIKLNRLHNMH 158
Cdd:cd11647 81 LVPGDPLIATTHIDLRLEAKKRGIKVKVIHNASILSAAGSTsGLQLYKFGRTVTIPFPEENYKPESPYDVIKENLKRGLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194746329 159 TLCLLDIKVKeptpeslmrkrkeymPPRFMSVAEAAHQLLAIVEKKdsleKNTVLNEQSLCVGLARVGQESQQIAVGTLL 238
Cdd:cd11647 161 TLLLLDIKVE---------------EGRFMTINEAIEILLEIEEKR----KEGVITEDTLVVGLARLGSDDQKIVAGTLK 221
|
250
....*....|....*....
gi 194746329 239 EMRSTDMGGPLHSLIIPAK 257
Cdd:cd11647 222 ELLKEDFGPPPHSLIIPGK 240
|
|
| DPH5 |
COG1798 |
Diphthamide biosynthesis methyltransferase [Translation, ribosomal structure and biogenesis]; |
1-267 |
3.03e-103 |
|
Diphthamide biosynthesis methyltransferase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441403 Cd Length: 255 Bit Score: 301.34 E-value: 3.03e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194746329 1 MFYLIGLGLGDLKDITVKGLEIVKQCSRVYLEMYTSIL-GCSLEDMQEFYGRPLLLADRDLVEQGADEILSGAGESDVAL 79
Cdd:COG1798 1 MLTFVGLGLSDERDITLKGLEALRSADKVYAEFYTSRLiGTDLEKLEELIGKEIVVLDREDVEDNPEEILEEAKEKDVVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194746329 80 LVVGDPFGATTHTDFILRAKEKNIPYKVIHNASIMNAV-GCCGLQLYKFGETVSIPYWDETWKPDSFYDKIKLNRLHNMH 158
Cdd:COG1798 81 LTAGDPMIATTHVDLRLRAKRRGIETRVIHGVSIVSAAiGLTGLQNYKFGKTVTIPFPYEGFVPTSPYDTIKENLERGLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194746329 159 TLCLLDIKVKEptpeslmrkrkeympPRFMSVAEAAHQLLAIvEKKdslEKNTVLNEQSLCVGLARVGQESQQIAVGTLL 238
Cdd:COG1798 161 TLVLLDIKADK---------------NRYMTANEALELLLEI-EKK---RREGVISDDTLAVVVARAGSPDPKIVAGKLS 221
|
250 260
....*....|....*....|....*....
gi 194746329 239 EMRSTDMGGPLHSLIIPAKeMHPLEVEFL 267
Cdd:COG1798 222 ELANYDFGEPPHSLIIPGR-LHFMEAEAL 249
|
|
| dph5 |
TIGR00522 |
diphthine synthase; Alternate name: diphthamide biosynthesis S-adenosylmethionine-dependent ... |
1-274 |
8.01e-94 |
|
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: 277.47 E-value: 8.01e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194746329 1 MFYLIGLGLGDLKDITVKGLEIVKQCSRVYLEMYTSIL-GCSLEDMQEFYGRPLLLADRDLVEQGADEILSGAGESDVAL 79
Cdd:TIGR00522 1 MLYLIGLGLYDENDISVKGLEAIKKADEVYAEFYTSKLlGSSIEEIEEFFGKRVVVLERSDVEENSFRLIERAKSKDVAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194746329 80 LVVGDPFGATTHTDFILRAKEKNIPYKVIHNASIMNAV-GCCGLQLYKFGETVSIPYWDETWKPDSFYDKIKLNRLHNMH 158
Cdd:TIGR00522 81 LVAGDPMVATTHTDLKLEAKRKGIETRIIHGASISSAVcGLTGLQLYKFGKTATIVFFTDNYRPQTPYNVIKENRKIGLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194746329 159 TLCLLDIKVKEptpeslmrkrkeympPRFMSVAEAAHQLLAIVEKKdsleKNTVLNEQSLCVGLARVGQESQQIAVGTLL 238
Cdd:TIGR00522 161 TLVLLDIHPKE---------------NRAMTIGEGLENLLEEEEKR----KTGAITPDTYAVVIARAGSGKPVVKCDKIE 221
|
250 260 270
....*....|....*....|....*....|....*.
gi 194746329 239 EMRSTDMGGPLHSLIIPAKEMHPLEVEFLQQYAASI 274
Cdd:TIGR00522 222 NLKNYDFGEPLHCLVVLAKTLHFMEFEYLREFADAP 257
|
|
| TP_methylase |
cd09815 |
S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet ... |
5-255 |
1.27e-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: 90.14 E-value: 1.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194746329 5 IGLGLGDLKDITVKGLEIVKQCSRVYLEMYTSILGCSLEDMQEFYGRPLL-LADRDLVEQGADEILS-GAGESDVALLVV 82
Cdd:cd09815 1 VGVGPGDPDLLTLRALEILRAADVVVAEDKDSKLLSLVLRAILKDGKRIYdLHDPNVEEEMAELLLEeARQGKDVAFLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194746329 83 GDPFGATTHTDFILRAKEKNIPYKVIHNASIMNAVGC-CGLQLYKFGETVSIPYWDETWKPdsfyDKIKLNRLHNMHTLC 161
Cdd:cd09815 81 GDPGVAGTGAELVERAEREGVEVKVIPGVSAADAAAAaLGIDLGESFLFVTASDLLENPRL----LVLKALAKERRHLVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194746329 162 LLDIkvkeptpeslmrkrkeympprfmsvaeaaHQLLAIVEKkdsLEKNtVLNEQSLCVGLARVGQESQQIAVGTLLEMR 241
Cdd:cd09815 157 FLDG-----------------------------HRFLKALER---LLKE-LGEDDTPVVLVANAGSEGEVIRTGTVKELR 203
|
250
....*....|....*.
gi 194746329 242 S--TDMGGPLHSLIIP 255
Cdd:cd09815 204 AerTERGKPLTTILVG 219
|
|
| TP_methylase |
pfam00590 |
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ... |
1-240 |
1.42e-20 |
|
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: 87.01 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194746329 1 MFYLIGLGLGDLKDITVKGLEIVKQCSRVYLEM--YTSILGCSLEDMQEF----YGRPLLLADRDLVEQGADEILSGAge 74
Cdd:pfam00590 1 KLYLVGVGPGDPDLLTLRALRALKEADVVLGDDsrALEILLDLLPEDLYFpmteDKEPLEEAYEEIAEALAAALRAGK-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194746329 75 sDVALLVVGDPFGATTHTDFILRAKEKNIPYKVIHNASIMNAVGCC-GLQLYKFGETVSIPYWDET-WKPDSFYDKIkln 152
Cdd:pfam00590 79 -DVARLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARlGIPLTEGGEVLSVLFLPGLaRIELRLLEAL--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194746329 153 rLHNMHTLCLLdikvkeptpeslmrkrkeYMPPRFmsvAEAAHQLLAIVekkdslekntvlNEQSLCVGLARVGQESQQI 232
Cdd:pfam00590 155 -LANGDTVVLL------------------YGPRRL---AELAELLLELY------------PDTTPVAVVERAGTPDEKV 200
|
....*...
gi 194746329 233 AVGTLLEM 240
Cdd:pfam00590 201 VRGTLGEL 208
|
|
| YabN_N_like |
cd11723 |
N-terminal S-AdoMet-dependent tetrapyrrole methylase domain of Bacillus subtilis YabN and ... |
3-124 |
3.15e-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: 3.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194746329 3 YLIGLGLGDLKDITVKGLEIVKQCSRVYLEmyTSI---------LGCSLEDMQEFYGRplllADR--DLVEQGADEILSG 71
Cdd:cd11723 2 TIVGLGPGDPDLLTLGALEALKSADKVYLR--TARhpvveelkeEGIEFESFDDLYEE----AEDfeEVYEAIAERLLEA 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 194746329 72 AGESDVALLVVGDPFGATTHTDFILRAKEKNIPYKVIHNAS----IMNAVGCC---GLQL 124
Cdd:cd11723 76 AEHGDVVYAVPGHPLVAERTVQLLLERAEEGIEVEIIPGVSfldaALAALGIDpieGLQI 135
|
|
| cobI_cbiL |
TIGR01467 |
precorrin-2 C(20)-methyltransferase; This model represents precorrin-2 C(20)-methyltransferase, ... |
1-117 |
7.31e-04 |
|
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: 39.99 E-value: 7.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194746329 1 MFYLIGLGLGDLKDITVKGLEIVKQCSRVYLEMYTSILGCSLEDMQEFYGRPL----------LLADRDLVEQGADEILS 70
Cdd:TIGR01467 2 KLYGVGVGPGDPELITVKALEALRSADVIAVPASKKGRESLARKIVEDYLKPNdtrilelvfpMTKDRDELEKAWDEAAE 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 194746329 71 G-----AGESDVALLVVGDPFGATTHTDFILRAKEKNIPYKVIHNASIMNAV 117
Cdd:TIGR01467 82 AvaaelEEGRDVAFLTLGDPSLYSTFSYLLQRLQGMGIEVEVVPGITSFAAC 133
|
|
| TP_methylase |
cd11724 |
uncharacterized family of the tetrapyrrole methylase superfamily; Members of this superfamily ... |
2-87 |
3.47e-03 |
|
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: 37.92 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194746329 2 FYLIGLGLGDLKDITVKGLEIVKQ-----CSRVYLEMYTSILG-----CSLEDMQEFYGRPLLLADRDLVEQGA-----D 66
Cdd:cd11724 2 LYLVGVGPGDPDLITLRALKAIKKadvvfAPPDLRKRFAEYLAgkevlDDPHGLFTYYGKKCSPLEEAEKECEElekqrA 81
|
90 100
....*....|....*....|....*....
gi 194746329 67 EILS------GAGESdVALLVVGDP--FG 87
Cdd:cd11724 82 EIVQkirealAQGKN-VALLDSGDPtiYG 109
|
|
| PRK05576 |
PRK05576 |
cobalt-factor II C(20)-methyltransferase; |
1-30 |
6.40e-03 |
|
cobalt-factor II C(20)-methyltransferase;
Pssm-ID: 235512 [Multi-domain] Cd Length: 229 Bit Score: 37.20 E-value: 6.40e-03
10 20 30
....*....|....*....|....*....|
gi 194746329 1 MFYLIGLGLGDLKDITVKGLEIVKQCSRVY 30
Cdd:PRK05576 3 KLYGIGLGPGDPELLTVKAARILEEADVVY 32
|
|
| |
