|
Name |
Accession |
Description |
Interval |
E-value |
| DPH5 |
COG1798 |
Diphthamide biosynthesis methyltransferase [Translation, ribosomal structure and biogenesis]; |
1-252 |
2.94e-120 |
|
Diphthamide biosynthesis methyltransferase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441403 Cd Length: 255 Bit Score: 346.79 E-value: 2.94e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118193853 1 MLWFVGMGLAGAGSIPADAKNVIEQAEMVYLEGFTSIVTESDERALEEMAGGKIIPARRWMVED-GKEILDNARTKKVVL 79
Cdd:COG1798 1 MLTFVGLGLSDERDITLKGLEALRSADKVYAEFYTSRLIGTDLEKLEELIGKEIVVLDREDVEDnPEEILEEAKEKDVVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118193853 80 VSYGDPYTATTHIELRTRAAELNIPTGSIHAASILASAVGECGLHHYKMGRTATVTRDPR--AASTPYRIIYENLVSGSH 157
Cdd:COG1798 81 LTAGDPMIATTHVDLRLRAKRRGIETRVIHGVSIVSAAIGLTGLQNYKFGKTVTIPFPYEgfVPTSPYDTIKENLERGLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118193853 158 TVLLLEYDQDGGFFLDPGDALGLLIEYEKEQRRGVITDELFAVIASRIGMKGQSIVAGRISSLKGYDFGAPPHAVIIPGG 237
Cdd:COG1798 161 TLVLLDIKADKNRYMTANEALELLLEIEKKRREGVISDDTLAVVVARAGSPDPKIVAGKLSELANYDFGEPPHSLIIPGR 240
|
250
....*....|....*
gi 118193853 238 LHFTESEALSASAKC 252
Cdd:COG1798 241 LHFMEAEALKALAGA 255
|
|
| DHP5_DphB |
cd11647 |
diphthine methyl ester synthase and diphthine synthase; Eukaryotic diphthine methyl ester ... |
1-238 |
2.08e-99 |
|
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: 293.55 E-value: 2.08e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118193853 1 MLWFVGMGLAGAGSIPADAKNVIEQAEMVYLEGFTSIVTESDERALEEMAGGKIIPARRWMVED-GKEILDNARTKKVVL 79
Cdd:cd11647 1 MLYLIGLGLGDEKDITLEGLEALKKADKVYLEAYTSILPGSKLEELEKLIGKKIILLDREDLEEeSEEILEEAKKKDVAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118193853 80 VSYGDPYTATTHIELRTRAAELNIPTGSIHAASILASAVGECGLHHYKMGRTATVTRDPR--AASTPYRIIYENLVSGSH 157
Cdd:cd11647 81 LVPGDPLIATTHIDLRLEAKKRGIKVKVIHNASILSAAGSTSGLQLYKFGRTVTIPFPEEnyKPESPYDVIKENLKRGLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118193853 158 TVLLLEYDQDGGFFLDPGDALGLLIEYEKEQRRGVITDELFAVIASRIGMKGQSIVAGRISSLKGYDFGAPPHAVIIPGG 237
Cdd:cd11647 161 TLLLLDIKVEEGRFMTINEAIEILLEIEEKRKEGVITEDTLVVGLARLGSDDQKIVAGTLKELLKEDFGPPPHSLIIPGK 240
|
.
gi 118193853 238 L 238
Cdd:cd11647 241 L 241
|
|
| dph5 |
TIGR00522 |
diphthine synthase; Alternate name: diphthamide biosynthesis S-adenosylmethionine-dependent ... |
1-246 |
9.08e-59 |
|
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: 190.41 E-value: 9.08e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118193853 1 MLWFVGMGLAGAGSIPADAKNVIEQAEMVYLEGFTSIVTESDERALEEMAGGKIIPARRWMVE-DGKEILDNARTKKVVL 79
Cdd:TIGR00522 1 MLYLIGLGLYDENDISVKGLEAIKKADEVYAEFYTSKLLGSSIEEIEEFFGKRVVVLERSDVEeNSFRLIERAKSKDVAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118193853 80 VSYGDPYTATTHIELRTRAAELNIPTGSIHAASILASAVGECGLHHYKMGRTATV--TRDPRAASTPYRIIYENLVSGSH 157
Cdd:TIGR00522 81 LVAGDPMVATTHTDLKLEAKRKGIETRIIHGASISSAVCGLTGLQLYKFGKTATIvfFTDNYRPQTPYNVIKENRKIGLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118193853 158 TVLLLEYDQDGGFFLDPGDALGLLIEYEKEQRRGVITDELFAVIASRIGMKGQSIVAGRISSLKGYDFGAPPHAVIIPG- 236
Cdd:TIGR00522 161 TLVLLDIHPKENRAMTIGEGLENLLEEEEKRKTGAITPDTYAVVIARAGSGKPVVKCDKIENLKNYDFGEPLHCLVVLAk 240
|
250
....*....|
gi 118193853 237 GLHFTESEAL 246
Cdd:TIGR00522 241 TLHFMEFEYL 250
|
|
| PTZ00175 |
PTZ00175 |
diphthine synthase; Provisional |
1-244 |
5.27e-56 |
|
diphthine synthase; Provisional
Pssm-ID: 185500 Cd Length: 270 Bit Score: 183.62 E-value: 5.27e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118193853 1 MLWFVGMGLAGAGSIPADAKNVIEQAEMVYLEGFTSIVTESDERALEEMAGGKIIPARRWMVEDG-KEILDNARTKKVVL 79
Cdd:PTZ00175 2 MLYIIGLGLGDEKDITVKGLEAVKSADVVYLESYTSILINSNKEKLEEFYGKPVIEADREMVEEGcDEILEEAKEKNVAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118193853 80 VSYGDPYTATTHIELRTRAAELNIPTGSIHAASILaSAVGECGLHHYKMGRTATV-----TRDPraaSTPYRIIYENLVS 154
Cdd:PTZ00175 82 LVVGDPFCATTHTDLYLRAKKKGIEVEVIHNASIM-NAIGCTGLQLYRFGETVSIpffteTWKP---DSFYDKIKANRDN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118193853 155 GSHTVLLL-----EYDQDG----------GFFLDPGDALGLLIEYEKEQRRGVITDELFAVIASRIGMKGQSIVAGRISS 219
Cdd:PTZ00175 158 GLHTLCLLdikvkERSVENlmkgrkiyepPRYMTINQAIEQLLEVEEKKGGGVIAEDTLVVGVARVGSDDQQIVSGTLED 237
|
250 260
....*....|....*....|....*.
gi 118193853 220 LKGYDFGAPPHAVIIPG-GLHFTESE 244
Cdd:PTZ00175 238 LLDVDFGPPLHSLVICApTLHDIEEE 263
|
|
| COG1849 |
COG1849 |
Uncharacterized conserved protein [Function unknown]; |
263-342 |
6.33e-20 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 441454 Cd Length: 90 Bit Score: 83.03 E-value: 6.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118193853 263 MPSIPQQMVKKYVPMVRDAMKTIEALED----NPPEYGHVLENAGHYLRDAEEFMGKGEGELAVLSVGYADGLVDALRMA 338
Cdd:COG1849 2 MSADLEEKVEKYIRMLEEALEKVEPAPPegspLYKAAEDFLEMAESYLEDAKYFLEKGDLVTALACISYAEGWLDAGRRL 81
|
....
gi 118193853 339 RGID 342
Cdd:COG1849 82 GLFD 85
|
|
| TP_methylase |
pfam00590 |
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ... |
1-220 |
6.97e-13 |
|
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: 66.60 E-value: 6.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118193853 1 MLWFVGMGLAGAGSIPADAKNVIEQAEMVYLEGftSIVTESDERALEEMAGGKIIPARRWMVEDGKEI----LDNARTKK 76
Cdd:pfam00590 1 KLYLVGVGPGDPDLLTLRALRALKEADVVLGDD--SRALEILLDLLPEDLYFPMTEDKEPLEEAYEEIaealAAALRAGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118193853 77 -VVLVSYGDPYTATTHIELRTRAAELNIPTGSIHAASILASAVGECGLHHYKMGRTATVTRDPRAASTPYRiIYENLVSG 155
Cdd:pfam00590 79 dVARLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARLGIPLTEGGEVLSVLFLPGLARIELR-LLEALLAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 118193853 156 SHTVLLLEydqdGGFFLDpgDALGLLIEYEKEQRRgvitdelfAVIASRIGMKGQSIVAGRISSL 220
Cdd:pfam00590 158 GDTVVLLY----GPRRLA--ELAELLLELYPDTTP--------VAVVERAGTPDEKVVRGTLGEL 208
|
|
| DUF357 |
pfam04010 |
Protein of unknown function (DUF357); Members of this family are short (less than 100 amino ... |
273-338 |
1.27e-12 |
|
Protein of unknown function (DUF357); Members of this family are short (less than 100 amino acid) proteins found in archaebacteria. The function of these proteins is unknown.
Pssm-ID: 427649 Cd Length: 73 Bit Score: 62.23 E-value: 1.27e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118193853 273 KYVPMVRDAMKTIE-ALEDNPP---EYGHVLENAGHYLRDAEEFMGKGEGELAVLSVGYADGLVDALRMA 338
Cdd:pfam04010 1 RYIRLLEEALESVKiAPPEGSPlydAAEDVLEMAESYLEDAKYFLEKGDLVNALACFSYAHGWLDAGARL 70
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DPH5 |
COG1798 |
Diphthamide biosynthesis methyltransferase [Translation, ribosomal structure and biogenesis]; |
1-252 |
2.94e-120 |
|
Diphthamide biosynthesis methyltransferase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441403 Cd Length: 255 Bit Score: 346.79 E-value: 2.94e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118193853 1 MLWFVGMGLAGAGSIPADAKNVIEQAEMVYLEGFTSIVTESDERALEEMAGGKIIPARRWMVED-GKEILDNARTKKVVL 79
Cdd:COG1798 1 MLTFVGLGLSDERDITLKGLEALRSADKVYAEFYTSRLIGTDLEKLEELIGKEIVVLDREDVEDnPEEILEEAKEKDVVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118193853 80 VSYGDPYTATTHIELRTRAAELNIPTGSIHAASILASAVGECGLHHYKMGRTATVTRDPR--AASTPYRIIYENLVSGSH 157
Cdd:COG1798 81 LTAGDPMIATTHVDLRLRAKRRGIETRVIHGVSIVSAAIGLTGLQNYKFGKTVTIPFPYEgfVPTSPYDTIKENLERGLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118193853 158 TVLLLEYDQDGGFFLDPGDALGLLIEYEKEQRRGVITDELFAVIASRIGMKGQSIVAGRISSLKGYDFGAPPHAVIIPGG 237
Cdd:COG1798 161 TLVLLDIKADKNRYMTANEALELLLEIEKKRREGVISDDTLAVVVARAGSPDPKIVAGKLSELANYDFGEPPHSLIIPGR 240
|
250
....*....|....*
gi 118193853 238 LHFTESEALSASAKC 252
Cdd:COG1798 241 LHFMEAEALKALAGA 255
|
|
| DHP5_DphB |
cd11647 |
diphthine methyl ester synthase and diphthine synthase; Eukaryotic diphthine methyl ester ... |
1-238 |
2.08e-99 |
|
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: 293.55 E-value: 2.08e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118193853 1 MLWFVGMGLAGAGSIPADAKNVIEQAEMVYLEGFTSIVTESDERALEEMAGGKIIPARRWMVED-GKEILDNARTKKVVL 79
Cdd:cd11647 1 MLYLIGLGLGDEKDITLEGLEALKKADKVYLEAYTSILPGSKLEELEKLIGKKIILLDREDLEEeSEEILEEAKKKDVAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118193853 80 VSYGDPYTATTHIELRTRAAELNIPTGSIHAASILASAVGECGLHHYKMGRTATVTRDPR--AASTPYRIIYENLVSGSH 157
Cdd:cd11647 81 LVPGDPLIATTHIDLRLEAKKRGIKVKVIHNASILSAAGSTSGLQLYKFGRTVTIPFPEEnyKPESPYDVIKENLKRGLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118193853 158 TVLLLEYDQDGGFFLDPGDALGLLIEYEKEQRRGVITDELFAVIASRIGMKGQSIVAGRISSLKGYDFGAPPHAVIIPGG 237
Cdd:cd11647 161 TLLLLDIKVEEGRFMTINEAIEILLEIEEKRKEGVITEDTLVVGLARLGSDDQKIVAGTLKELLKEDFGPPPHSLIIPGK 240
|
.
gi 118193853 238 L 238
Cdd:cd11647 241 L 241
|
|
| dph5 |
TIGR00522 |
diphthine synthase; Alternate name: diphthamide biosynthesis S-adenosylmethionine-dependent ... |
1-246 |
9.08e-59 |
|
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: 190.41 E-value: 9.08e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118193853 1 MLWFVGMGLAGAGSIPADAKNVIEQAEMVYLEGFTSIVTESDERALEEMAGGKIIPARRWMVE-DGKEILDNARTKKVVL 79
Cdd:TIGR00522 1 MLYLIGLGLYDENDISVKGLEAIKKADEVYAEFYTSKLLGSSIEEIEEFFGKRVVVLERSDVEeNSFRLIERAKSKDVAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118193853 80 VSYGDPYTATTHIELRTRAAELNIPTGSIHAASILASAVGECGLHHYKMGRTATV--TRDPRAASTPYRIIYENLVSGSH 157
Cdd:TIGR00522 81 LVAGDPMVATTHTDLKLEAKRKGIETRIIHGASISSAVCGLTGLQLYKFGKTATIvfFTDNYRPQTPYNVIKENRKIGLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118193853 158 TVLLLEYDQDGGFFLDPGDALGLLIEYEKEQRRGVITDELFAVIASRIGMKGQSIVAGRISSLKGYDFGAPPHAVIIPG- 236
Cdd:TIGR00522 161 TLVLLDIHPKENRAMTIGEGLENLLEEEEKRKTGAITPDTYAVVIARAGSGKPVVKCDKIENLKNYDFGEPLHCLVVLAk 240
|
250
....*....|
gi 118193853 237 GLHFTESEAL 246
Cdd:TIGR00522 241 TLHFMEFEYL 250
|
|
| PTZ00175 |
PTZ00175 |
diphthine synthase; Provisional |
1-244 |
5.27e-56 |
|
diphthine synthase; Provisional
Pssm-ID: 185500 Cd Length: 270 Bit Score: 183.62 E-value: 5.27e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118193853 1 MLWFVGMGLAGAGSIPADAKNVIEQAEMVYLEGFTSIVTESDERALEEMAGGKIIPARRWMVEDG-KEILDNARTKKVVL 79
Cdd:PTZ00175 2 MLYIIGLGLGDEKDITVKGLEAVKSADVVYLESYTSILINSNKEKLEEFYGKPVIEADREMVEEGcDEILEEAKEKNVAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118193853 80 VSYGDPYTATTHIELRTRAAELNIPTGSIHAASILaSAVGECGLHHYKMGRTATV-----TRDPraaSTPYRIIYENLVS 154
Cdd:PTZ00175 82 LVVGDPFCATTHTDLYLRAKKKGIEVEVIHNASIM-NAIGCTGLQLYRFGETVSIpffteTWKP---DSFYDKIKANRDN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118193853 155 GSHTVLLL-----EYDQDG----------GFFLDPGDALGLLIEYEKEQRRGVITDELFAVIASRIGMKGQSIVAGRISS 219
Cdd:PTZ00175 158 GLHTLCLLdikvkERSVENlmkgrkiyepPRYMTINQAIEQLLEVEEKKGGGVIAEDTLVVGVARVGSDDQQIVSGTLED 237
|
250 260
....*....|....*....|....*.
gi 118193853 220 LKGYDFGAPPHAVIIPG-GLHFTESE 244
Cdd:PTZ00175 238 LLDVDFGPPLHSLVICApTLHDIEEE 263
|
|
| COG1849 |
COG1849 |
Uncharacterized conserved protein [Function unknown]; |
263-342 |
6.33e-20 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 441454 Cd Length: 90 Bit Score: 83.03 E-value: 6.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118193853 263 MPSIPQQMVKKYVPMVRDAMKTIEALED----NPPEYGHVLENAGHYLRDAEEFMGKGEGELAVLSVGYADGLVDALRMA 338
Cdd:COG1849 2 MSADLEEKVEKYIRMLEEALEKVEPAPPegspLYKAAEDFLEMAESYLEDAKYFLEKGDLVTALACISYAEGWLDAGRRL 81
|
....
gi 118193853 339 RGID 342
Cdd:COG1849 82 GLFD 85
|
|
| TP_methylase |
cd09815 |
S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet ... |
5-235 |
1.94e-16 |
|
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: 77.05 E-value: 1.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118193853 5 VGMGLAGAGSIPADAKNVIEQAEMVYLEgfTSIVTESDERALEEMAGGK-IIPARRWMV--EDGKEILDNART-KKVVLV 80
Cdd:cd09815 1 VGVGPGDPDLLTLRALEILRAADVVVAE--DKDSKLLSLVLRAILKDGKrIYDLHDPNVeeEMAELLLEEARQgKDVAFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118193853 81 SYGDPYTATTHIELRTRAAELNIPTGSIHAASILASAVGECGLHHYKmgRTATVTRDPRAASTPYRIIYENLVSGSHTVl 160
Cdd:cd09815 79 SPGDPGVAGTGAELVERAEREGVEVKVIPGVSAADAAAAALGIDLGE--SFLFVTASDLLENPRLLVLKALAKERRHLV- 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 118193853 161 lleydqdggFFLDPGDALGLLIEYEKEQRRgvitDELFAVIASRIGMKGQSIVAGRISSLKGY--DFGAPPHAVIIP 235
Cdd:cd09815 156 ---------LFLDGHRFLKALERLLKELGE----DDTPVVLVANAGSEGEVIRTGTVKELRAErtERGKPLTTILVG 219
|
|
| TP_methylase |
pfam00590 |
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ... |
1-220 |
6.97e-13 |
|
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: 66.60 E-value: 6.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118193853 1 MLWFVGMGLAGAGSIPADAKNVIEQAEMVYLEGftSIVTESDERALEEMAGGKIIPARRWMVEDGKEI----LDNARTKK 76
Cdd:pfam00590 1 KLYLVGVGPGDPDLLTLRALRALKEADVVLGDD--SRALEILLDLLPEDLYFPMTEDKEPLEEAYEEIaealAAALRAGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118193853 77 -VVLVSYGDPYTATTHIELRTRAAELNIPTGSIHAASILASAVGECGLHHYKMGRTATVTRDPRAASTPYRiIYENLVSG 155
Cdd:pfam00590 79 dVARLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARLGIPLTEGGEVLSVLFLPGLARIELR-LLEALLAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 118193853 156 SHTVLLLEydqdGGFFLDpgDALGLLIEYEKEQRRgvitdelfAVIASRIGMKGQSIVAGRISSL 220
Cdd:pfam00590 158 GDTVVLLY----GPRRLA--ELAELLLELYPDTTP--------VAVVERAGTPDEKVVRGTLGEL 208
|
|
| DUF357 |
pfam04010 |
Protein of unknown function (DUF357); Members of this family are short (less than 100 amino ... |
273-338 |
1.27e-12 |
|
Protein of unknown function (DUF357); Members of this family are short (less than 100 amino acid) proteins found in archaebacteria. The function of these proteins is unknown.
Pssm-ID: 427649 Cd Length: 73 Bit Score: 62.23 E-value: 1.27e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118193853 273 KYVPMVRDAMKTIE-ALEDNPP---EYGHVLENAGHYLRDAEEFMGKGEGELAVLSVGYADGLVDALRMA 338
Cdd:pfam04010 1 RYIRLLEEALESVKiAPPEGSPlydAAEDVLEMAESYLEDAKYFLEKGDLVNALACFSYAHGWLDAGARL 70
|
|
| Precorrin-6Y-MT |
cd11644 |
Precorrin-6Y methyltransferase (also named CbiE); CbiE (precorrin-6Y methyltransferase, also ... |
5-234 |
8.16e-06 |
|
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: 45.95 E-value: 8.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118193853 5 VGMGLAGAGSIPADAKNVIEQAEMVYleGFtsivtesdERALEEMAGgkiIPARRWMVEDG--KEILDNARTKK---VVL 79
Cdd:cd11644 1 IGIGPGGPEYLTPEAREAIEEADVVI--GA--------KRLLELFPD---LGAEKIPLPSEdiAELLEEIAEAGkrvVVL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118193853 80 VSyGDP--YTATTHIELRTRAAELN-IPtgSIHAASILASAVGECglhhykMGRTATVT---RDPRAastpyriIYENLV 153
Cdd:cd11644 68 AS-GDPgfYGIGKTLLRRLGGEEVEvIP--GISSVQLAAARLGLP------WEDARLVSlhgRDLEN-------LRRALR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118193853 154 SGSHTVLLLeydqDGGFflDPGDALGLLIEYEKEQRRgvitdelfAVIASRIGMKGQSIVAGRISSLKGYDFgAPPHAVI 233
Cdd:cd11644 132 RGRKVFVLT----DGKN--TPAEIARLLLERGLGDSR--------VTVGENLGYPDERITEGTAEELAEEEF-SDLNVVL 196
|
.
gi 118193853 234 I 234
Cdd:cd11644 197 I 197
|
|
| PRK05787 |
PRK05787 |
cobalt-precorrin-7 (C(5))-methyltransferase; |
1-85 |
1.49e-03 |
|
cobalt-precorrin-7 (C(5))-methyltransferase;
Pssm-ID: 235609 [Multi-domain] Cd Length: 210 Bit Score: 39.47 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118193853 1 MLWFVGMGLAGAGSIPADAKNVIEQAEMVYleGFtsivtesdERALEEMAggKIIPARRWMVEDGKEILDN-----ARTK 75
Cdd:PRK05787 1 MIYIVGIGPGDPEYLTLKALEAIRKADVVV--GS--------KRVLELFP--ELIDGEAFVLTAGLRDLLEwlelaAKGK 68
|
90
....*....|
gi 118193853 76 KVVLVSYGDP 85
Cdd:PRK05787 69 NVVVLSTGDP 78
|
|
| |
