|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00175 |
PTZ00175 |
diphthine synthase; Provisional |
1-272 |
2.77e-163 |
|
diphthine synthase; Provisional
Pssm-ID: 185500 Cd Length: 270 Bit Score: 453.65 E-value: 2.77e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357112131 1 MLYIVGLGLGDERDITVRGLDAVRRCSKVYMEAYTSLLSlgldPASLANLEKLYGKEITVADREMVEERSDQMLSEATDA 80
Cdd:PTZ00175 2 MLYIIGLGLGDEKDITVKGLEAVKSADVVYLESYTSILI----NSNKEKLEEFYGKPVIEADREMVEEGCDEILEEAKEK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357112131 81 DVAFLVVGDPFGATTHTDLVVRAKSIGVEVKVIHNASVMNAVGVCGLQLYRYGETISIPFFTETWRPDSFYEKIQNSRRL 160
Cdd:PTZ00175 78 NVAFLVVGDPFCATTHTDLYLRAKKKGIEVEVIHNASIMNAIGCTGLQLYRFGETVSIPFFTETWKPDSFYDKIKANRDN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357112131 161 GLHTLCLLDIRVKEPTLESLCRGKKVYEPPRFMTVNTAISQLLEVEELHGGSAYGPDSLCMGVARLGSDDQKIVAGPMKK 240
Cdd:PTZ00175 158 GLHTLCLLDIKVKERSVENLMKGRKIYEPPRYMTINQAIEQLLEVEEKKGGGVIAEDTLVVGVARVGSDDQQIVSGTLED 237
|
250 260 270
....*....|....*....|....*....|...
gi 357112131 241 LLDVDFGPPLHCLIIVGET-HPVEQEMLEFYMI 272
Cdd:PTZ00175 238 LLDVDFGPPLHSLVICAPTlHDIEEEFFELYRI 270
|
|
| DHP5_DphB |
cd11647 |
diphthine methyl ester synthase and diphthine synthase; Eukaryotic diphthine methyl ester ... |
1-259 |
1.96e-134 |
|
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: 379.45 E-value: 1.96e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357112131 1 MLYIVGLGLGDERDITVRGLDAVRRCSKVYMEAYTSLLSlgldPASLANLEKLYGKEITVADREMVEERSDQMLSEATDA 80
Cdd:cd11647 1 MLYLIGLGLGDEKDITLEGLEALKKADKVYLEAYTSILP----GSKLEELEKLIGKKIILLDREDLEEESEEILEEAKKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357112131 81 DVAFLVVGDPFGATTHTDLVVRAKSIGVEVKVIHNASVMNAVGVC-GLQLYRYGETISIPFFTETWRPDSFYEKIQNSRR 159
Cdd:cd11647 77 DVALLVPGDPLIATTHIDLRLEAKKRGIKVKVIHNASILSAAGSTsGLQLYKFGRTVTIPFPEENYKPESPYDVIKENLK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357112131 160 LGLHTLCLLDIRVkeptleslcrgkkvyEPPRFMTVNTAISQLLEVEELHGGSAYGPDSLCMGVARLGSDDQKIVAGPMK 239
Cdd:cd11647 157 RGLHTLLLLDIKV---------------EEGRFMTINEAIEILLEIEEKRKEGVITEDTLVVGLARLGSDDQKIVAGTLK 221
|
250 260
....*....|....*....|
gi 357112131 240 KLLDVDFGPPLHCLIIVGET 259
Cdd:cd11647 222 ELLKEDFGPPPHSLIIPGKL 241
|
|
| DPH5 |
COG1798 |
Diphthamide biosynthesis methyltransferase [Translation, ribosomal structure and biogenesis]; |
1-268 |
5.77e-111 |
|
Diphthamide biosynthesis methyltransferase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441403 Cd Length: 255 Bit Score: 320.60 E-value: 5.77e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357112131 1 MLYIVGLGLGDERDITVRGLDAVRRCSKVYMEAYTSLLSlgldPASLANLEKLYGKEITVADREMVEERSDQMLSEATDA 80
Cdd:COG1798 1 MLTFVGLGLSDERDITLKGLEALRSADKVYAEFYTSRLI----GTDLEKLEELIGKEIVVLDREDVEDNPEEILEEAKEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357112131 81 DVAFLVVGDPFGATTHTDLVVRAKSIGVEVKVIHNASVMNAV-GVCGLQLYRYGETISIPFFTETWRPDSFYEKIQNSRR 159
Cdd:COG1798 77 DVVFLTAGDPMIATTHVDLRLRAKRRGIETRVIHGVSIVSAAiGLTGLQNYKFGKTVTIPFPYEGFVPTSPYDTIKENLE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357112131 160 LGLHTLCLLDIRVkeptleslcrgkkvyEPPRFMTVNTAISQLLEVEELHGGSAYGPDSLCMGVARLGSDDQKIVAGPMK 239
Cdd:COG1798 157 RGLHTLVLLDIKA---------------DKNRYMTANEALELLLEIEKKRREGVISDDTLAVVVARAGSPDPKIVAGKLS 221
|
250 260
....*....|....*....|....*....
gi 357112131 240 KLLDVDFGPPLHCLIIVGETHPVEQEMLE 268
Cdd:COG1798 222 ELANYDFGEPPHSLIIPGRLHFMEAEALK 250
|
|
| dph5 |
TIGR00522 |
diphthine synthase; Alternate name: diphthamide biosynthesis S-adenosylmethionine-dependent ... |
1-267 |
5.87e-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: 292.49 E-value: 5.87e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357112131 1 MLYIVGLGLGDERDITVRGLDAVRRCSKVYMEAYTSLLSlgldPASLANLEKLYGKEITVADREMVEERSDQMLSEATDA 80
Cdd:TIGR00522 1 MLYLIGLGLYDENDISVKGLEAIKKADEVYAEFYTSKLL----GSSIEEIEEFFGKRVVVLERSDVEENSFRLIERAKSK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357112131 81 DVAFLVVGDPFGATTHTDLVVRAKSIGVEVKVIHNASVMNAV-GVCGLQLYRYGETISIPFFTETWRPDSFYEKIQNSRR 159
Cdd:TIGR00522 77 DVALLVAGDPMVATTHTDLKLEAKRKGIETRIIHGASISSAVcGLTGLQLYKFGKTATIVFFTDNYRPQTPYNVIKENRK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357112131 160 LGLHTLCLLDIRVKEptleslcrgkkvyepPRFMTVNTAISQLLEVEELHGGSAYGPDSLCMGVARLGSDDQKIVAGPMK 239
Cdd:TIGR00522 157 IGLHTLVLLDIHPKE---------------NRAMTIGEGLENLLEEEEKRKTGAITPDTYAVVIARAGSGKPVVKCDKIE 221
|
250 260
....*....|....*....|....*....
gi 357112131 240 KLLDVDFGPPLHCLIIVGET-HPVEQEML 267
Cdd:TIGR00522 222 NLKNYDFGEPLHCLVVLAKTlHFMEFEYL 250
|
|
| TP_methylase |
pfam00590 |
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ... |
1-241 |
3.52e-21 |
|
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: 88.55 E-value: 3.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357112131 1 MLYIVGLGLGDERDITVRGLDAVRRCSKVY---MEAYTSLLslgldpaSLANLEKLYGKEITVADREMVEERSDQMLSEA 77
Cdd:pfam00590 1 KLYLVGVGPGDPDLLTLRALRALKEADVVLgddSRALEILL-------DLLPEDLYFPMTEDKEPLEEAYEEIAEALAAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357112131 78 TDA--DVAFLVVGDPFGATTHTDLVVRAKSIGVEVKVIHNASVMNAVGVC-GLQLYRYGETISIPFFTET-WRPDSFYEK 153
Cdd:pfam00590 74 LRAgkDVARLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARlGIPLTEGGEVLSVLFLPGLaRIELRLLEA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357112131 154 IQNsrrlGLHTLCLLDIRVKeptleslcrgkkvyepprfmtVNTAISQLLEveelhggsAYGPDSLCMGVARLGSDDQKI 233
Cdd:pfam00590 154 LLA----NGDTVVLLYGPRR---------------------LAELAELLLE--------LYPDTTPVAVVERAGTPDEKV 200
|
....*...
gi 357112131 234 VAGPMKKL 241
Cdd:pfam00590 201 VRGTLGEL 208
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00175 |
PTZ00175 |
diphthine synthase; Provisional |
1-272 |
2.77e-163 |
|
diphthine synthase; Provisional
Pssm-ID: 185500 Cd Length: 270 Bit Score: 453.65 E-value: 2.77e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357112131 1 MLYIVGLGLGDERDITVRGLDAVRRCSKVYMEAYTSLLSlgldPASLANLEKLYGKEITVADREMVEERSDQMLSEATDA 80
Cdd:PTZ00175 2 MLYIIGLGLGDEKDITVKGLEAVKSADVVYLESYTSILI----NSNKEKLEEFYGKPVIEADREMVEEGCDEILEEAKEK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357112131 81 DVAFLVVGDPFGATTHTDLVVRAKSIGVEVKVIHNASVMNAVGVCGLQLYRYGETISIPFFTETWRPDSFYEKIQNSRRL 160
Cdd:PTZ00175 78 NVAFLVVGDPFCATTHTDLYLRAKKKGIEVEVIHNASIMNAIGCTGLQLYRFGETVSIPFFTETWKPDSFYDKIKANRDN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357112131 161 GLHTLCLLDIRVKEPTLESLCRGKKVYEPPRFMTVNTAISQLLEVEELHGGSAYGPDSLCMGVARLGSDDQKIVAGPMKK 240
Cdd:PTZ00175 158 GLHTLCLLDIKVKERSVENLMKGRKIYEPPRYMTINQAIEQLLEVEEKKGGGVIAEDTLVVGVARVGSDDQQIVSGTLED 237
|
250 260 270
....*....|....*....|....*....|...
gi 357112131 241 LLDVDFGPPLHCLIIVGET-HPVEQEMLEFYMI 272
Cdd:PTZ00175 238 LLDVDFGPPLHSLVICAPTlHDIEEEFFELYRI 270
|
|
| DHP5_DphB |
cd11647 |
diphthine methyl ester synthase and diphthine synthase; Eukaryotic diphthine methyl ester ... |
1-259 |
1.96e-134 |
|
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: 379.45 E-value: 1.96e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357112131 1 MLYIVGLGLGDERDITVRGLDAVRRCSKVYMEAYTSLLSlgldPASLANLEKLYGKEITVADREMVEERSDQMLSEATDA 80
Cdd:cd11647 1 MLYLIGLGLGDEKDITLEGLEALKKADKVYLEAYTSILP----GSKLEELEKLIGKKIILLDREDLEEESEEILEEAKKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357112131 81 DVAFLVVGDPFGATTHTDLVVRAKSIGVEVKVIHNASVMNAVGVC-GLQLYRYGETISIPFFTETWRPDSFYEKIQNSRR 159
Cdd:cd11647 77 DVALLVPGDPLIATTHIDLRLEAKKRGIKVKVIHNASILSAAGSTsGLQLYKFGRTVTIPFPEENYKPESPYDVIKENLK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357112131 160 LGLHTLCLLDIRVkeptleslcrgkkvyEPPRFMTVNTAISQLLEVEELHGGSAYGPDSLCMGVARLGSDDQKIVAGPMK 239
Cdd:cd11647 157 RGLHTLLLLDIKV---------------EEGRFMTINEAIEILLEIEEKRKEGVITEDTLVVGLARLGSDDQKIVAGTLK 221
|
250 260
....*....|....*....|
gi 357112131 240 KLLDVDFGPPLHCLIIVGET 259
Cdd:cd11647 222 ELLKEDFGPPPHSLIIPGKL 241
|
|
| DPH5 |
COG1798 |
Diphthamide biosynthesis methyltransferase [Translation, ribosomal structure and biogenesis]; |
1-268 |
5.77e-111 |
|
Diphthamide biosynthesis methyltransferase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441403 Cd Length: 255 Bit Score: 320.60 E-value: 5.77e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357112131 1 MLYIVGLGLGDERDITVRGLDAVRRCSKVYMEAYTSLLSlgldPASLANLEKLYGKEITVADREMVEERSDQMLSEATDA 80
Cdd:COG1798 1 MLTFVGLGLSDERDITLKGLEALRSADKVYAEFYTSRLI----GTDLEKLEELIGKEIVVLDREDVEDNPEEILEEAKEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357112131 81 DVAFLVVGDPFGATTHTDLVVRAKSIGVEVKVIHNASVMNAV-GVCGLQLYRYGETISIPFFTETWRPDSFYEKIQNSRR 159
Cdd:COG1798 77 DVVFLTAGDPMIATTHVDLRLRAKRRGIETRVIHGVSIVSAAiGLTGLQNYKFGKTVTIPFPYEGFVPTSPYDTIKENLE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357112131 160 LGLHTLCLLDIRVkeptleslcrgkkvyEPPRFMTVNTAISQLLEVEELHGGSAYGPDSLCMGVARLGSDDQKIVAGPMK 239
Cdd:COG1798 157 RGLHTLVLLDIKA---------------DKNRYMTANEALELLLEIEKKRREGVISDDTLAVVVARAGSPDPKIVAGKLS 221
|
250 260
....*....|....*....|....*....
gi 357112131 240 KLLDVDFGPPLHCLIIVGETHPVEQEMLE 268
Cdd:COG1798 222 ELANYDFGEPPHSLIIPGRLHFMEAEALK 250
|
|
| dph5 |
TIGR00522 |
diphthine synthase; Alternate name: diphthamide biosynthesis S-adenosylmethionine-dependent ... |
1-267 |
5.87e-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: 292.49 E-value: 5.87e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357112131 1 MLYIVGLGLGDERDITVRGLDAVRRCSKVYMEAYTSLLSlgldPASLANLEKLYGKEITVADREMVEERSDQMLSEATDA 80
Cdd:TIGR00522 1 MLYLIGLGLYDENDISVKGLEAIKKADEVYAEFYTSKLL----GSSIEEIEEFFGKRVVVLERSDVEENSFRLIERAKSK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357112131 81 DVAFLVVGDPFGATTHTDLVVRAKSIGVEVKVIHNASVMNAV-GVCGLQLYRYGETISIPFFTETWRPDSFYEKIQNSRR 159
Cdd:TIGR00522 77 DVALLVAGDPMVATTHTDLKLEAKRKGIETRIIHGASISSAVcGLTGLQLYKFGKTATIVFFTDNYRPQTPYNVIKENRK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357112131 160 LGLHTLCLLDIRVKEptleslcrgkkvyepPRFMTVNTAISQLLEVEELHGGSAYGPDSLCMGVARLGSDDQKIVAGPMK 239
Cdd:TIGR00522 157 IGLHTLVLLDIHPKE---------------NRAMTIGEGLENLLEEEEKRKTGAITPDTYAVVIARAGSGKPVVKCDKIE 221
|
250 260
....*....|....*....|....*....
gi 357112131 240 KLLDVDFGPPLHCLIIVGET-HPVEQEML 267
Cdd:TIGR00522 222 NLKNYDFGEPLHCLVVLAKTlHFMEFEYL 250
|
|
| TP_methylase |
cd09815 |
S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet ... |
5-255 |
2.38e-24 |
|
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: 97.46 E-value: 2.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357112131 5 VGLGLGDERDITVRGLDAVRRCSKVYMEAYTSLLSLGLDPAslanlEKLYGKEI-TVADREMVEERSDQMLSEATD-ADV 82
Cdd:cd09815 1 VGVGPGDPDLLTLRALEILRAADVVVAEDKDSKLLSLVLRA-----ILKDGKRIyDLHDPNVEEEMAELLLEEARQgKDV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357112131 83 AFLVVGDPFGATTHTDLVVRAKSIGVEVKVIHNASVMNAV-GVCGLQLYRYGETISIPFFTETWRPDsfyeKIQNSRRLG 161
Cdd:cd09815 76 AFLSPGDPGVAGTGAELVERAEREGVEVKVIPGVSAADAAaAALGIDLGESFLFVTASDLLENPRLL----VLKALAKER 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357112131 162 LHTLCLLDIRvkeptleslcrgkkvyepprfmTVNTAISQLLEVEElhggsayGPDSLCMGVARLGSDDQKIVAGPMKKL 241
Cdd:cd09815 152 RHLVLFLDGH----------------------RFLKALERLLKELG-------EDDTPVVLVANAGSEGEVIRTGTVKEL 202
|
250
....*....|....*.
gi 357112131 242 --LDVDFGPPLHCLII 255
Cdd:cd09815 203 raERTERGKPLTTILV 218
|
|
| TP_methylase |
pfam00590 |
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ... |
1-241 |
3.52e-21 |
|
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: 88.55 E-value: 3.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357112131 1 MLYIVGLGLGDERDITVRGLDAVRRCSKVY---MEAYTSLLslgldpaSLANLEKLYGKEITVADREMVEERSDQMLSEA 77
Cdd:pfam00590 1 KLYLVGVGPGDPDLLTLRALRALKEADVVLgddSRALEILL-------DLLPEDLYFPMTEDKEPLEEAYEEIAEALAAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357112131 78 TDA--DVAFLVVGDPFGATTHTDLVVRAKSIGVEVKVIHNASVMNAVGVC-GLQLYRYGETISIPFFTET-WRPDSFYEK 153
Cdd:pfam00590 74 LRAgkDVARLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARlGIPLTEGGEVLSVLFLPGLaRIELRLLEA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357112131 154 IQNsrrlGLHTLCLLDIRVKeptleslcrgkkvyepprfmtVNTAISQLLEveelhggsAYGPDSLCMGVARLGSDDQKI 233
Cdd:pfam00590 154 LLA----NGDTVVLLYGPRR---------------------LAELAELLLE--------LYPDTTPVAVVERAGTPDEKV 200
|
....*...
gi 357112131 234 VAGPMKKL 241
Cdd:pfam00590 201 VRGTLGEL 208
|
|
| YabN_N_like |
cd11723 |
N-terminal S-AdoMet-dependent tetrapyrrole methylase domain of Bacillus subtilis YabN and ... |
2-129 |
5.44e-10 |
|
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: 57.88 E-value: 5.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357112131 2 LYIVGLGLGDERDITVRGLDAVRRCSKVYM-----EAYTSLLSLGLDPASL-------ANLEKLYgKEITvadremveer 69
Cdd:cd11723 1 ITIVGLGPGDPDLLTLGALEALKSADKVYLrtarhPVVEELKEEGIEFESFddlyeeaEDFEEVY-EAIA---------- 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 357112131 70 sDQMLSEATDADVAFLVVGDPFGATTHTDLVVRAKSIGVEVKVIHNAS----VMNAVGVC---GLQL 129
Cdd:cd11723 70 -ERLLEAAEHGDVVYAVPGHPLVAERTVQLLLERAEEGIEVEIIPGVSfldaALAALGIDpieGLQI 135
|
|
| PRK05576 |
PRK05576 |
cobalt-factor II C(20)-methyltransferase; |
1-113 |
5.07e-07 |
|
cobalt-factor II C(20)-methyltransferase;
Pssm-ID: 235512 [Multi-domain] Cd Length: 229 Bit Score: 49.53 E-value: 5.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357112131 1 MLYIVGLGLGDERDITVRGLDAVRRCSKVYMEAYTSllslglDPASLA-NLEKLYGKEITV---------ADREMVE--- 67
Cdd:PRK05576 3 KLYGIGLGPGDPELLTVKAARILEEADVVYAPASRK------GGGSLAlNIVRPYLKEETEivelhfpmsKDEEEKEavw 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 357112131 68 -ERSDQMLSEATD-ADVAFLVVGDPFGATTHTDLVVRAKSIGVEVKVI 113
Cdd:PRK05576 77 kENAEEIAAEAEEgKNVAFITLGDPNLYSTFSHLLEYLKCHDIEVETV 124
|
|
| cobI_cbiL |
TIGR01467 |
precorrin-2 C(20)-methyltransferase; This model represents precorrin-2 C(20)-methyltransferase, ... |
1-122 |
1.34e-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: 48.08 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357112131 1 MLYIVGLGLGDERDITVRGLDAVRRCSKVYMEAYTSllslglDPASLA-NLEKLYGKEITVADREMV-------EERSDQ 72
Cdd:TIGR01467 2 KLYGVGVGPGDPELITVKALEALRSADVIAVPASKK------GRESLArKIVEDYLKPNDTRILELVfpmtkdrDELEKA 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 357112131 73 MLSEAT--------DADVAFLVVGDPFGATTHTDLVVRAKSIGVEVKVIHNASVMNAV 122
Cdd:TIGR01467 76 WDEAAEavaaeleeGRDVAFLTLGDPSLYSTFSYLLQRLQGMGIEVEVVPGITSFAAC 133
|
|
| TP_methylase |
cd11724 |
uncharacterized family of the tetrapyrrole methylase superfamily; Members of this superfamily ... |
2-92 |
4.87e-05 |
|
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: 43.70 E-value: 4.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357112131 2 LYIVGLGLGDERDITVRGLDAVRR-----CSKVYMEAYTSLLSlG---LDpASLANLEKLYGKEITVADREMVEERSDQM 73
Cdd:cd11724 2 LYLVGVGPGDPDLITLRALKAIKKadvvfAPPDLRKRFAEYLA-GkevLD-DPHGLFTYYGKKCSPLEEAEKECEELEKQ 79
|
90 100 110
....*....|....*....|....*....|
gi 357112131 74 LSEAT----DA-----DVAFLVVGDP--FG 92
Cdd:cd11724 80 RAEIVqkirEAlaqgkNVALLDSGDPtiYG 109
|
|
| PRK05787 |
PRK05787 |
cobalt-precorrin-7 (C(5))-methyltransferase; |
1-90 |
4.31e-04 |
|
cobalt-precorrin-7 (C(5))-methyltransferase;
Pssm-ID: 235609 [Multi-domain] Cd Length: 210 Bit Score: 40.62 E-value: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357112131 1 MLYIVGLGLGDERDITVRGLDAVRRCSKVYmeaytsllslgldpASLANLEKLygKEITVADREMV----EERSDQMLSE 76
Cdd:PRK05787 1 MIYIVGIGPGDPEYLTLKALEAIRKADVVV--------------GSKRVLELF--PELIDGEAFVLtaglRDLLEWLELA 64
|
90
....*....|....
gi 357112131 77 ATDADVAFLVVGDP 90
Cdd:PRK05787 65 AKGKNVVVLSTGDP 78
|
|
| cobJ_cbiH |
TIGR01466 |
precorrin-3B C17-methyltransferase; This model represents precorrin-3B C17-methyltransferase, ... |
2-123 |
4.59e-03 |
|
precorrin-3B C17-methyltransferase; This model represents precorrin-3B C17-methyltransferase, one of two methyltransferases commonly referred to as precorrin-3 methylase (the other is precorrin-4 C11-methyltransferase, EC 2.1.1.133). This enzyme participates in the pathway toward the biosynthesis of cobalamin and related products. Members of this family may appear as fusion proteins with other enzymes of cobalamin biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
Pssm-ID: 273641 [Multi-domain] Cd Length: 239 Bit Score: 37.67 E-value: 4.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357112131 2 LYIVGLGLGDERDITVRGLDAVRRCSKVYmeAYTSLLSLgldpasLANLekLYGKEITVADreMVEE--RSDQMLSEATD 79
Cdd:TIGR01466 1 LYVVGIGPGAEELMTPEAKEALAEADVIV--GYKTYLDL------IEDL--IPGKEVVTSG--MREEiaRAELAIELAAE 68
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 357112131 80 A-DVAFLVVGDP--FGATTHTDLVVRAKSIGVEVKVIHNASVMNAVG 123
Cdd:TIGR01466 69 GrTVALVSSGDPgiYGMAALVFEALEKKGAEVDIEVIPGITAASAAA 115
|
|
| CobL |
COG2241 |
Precorrin-6B methylase 1 [Coenzyme transport and metabolism]; Precorrin-6B methylase 1 is part ... |
1-255 |
4.69e-03 |
|
Precorrin-6B methylase 1 [Coenzyme transport and metabolism]; Precorrin-6B methylase 1 is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 441842 [Multi-domain] Cd Length: 207 Bit Score: 37.43 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357112131 1 MLYIVGLGLGDERDITVRGLDAVRRCSKVYmeAYTSLLSLgldpasLANLEKLyGKEITVADREMVEErsdqMLSEATDA 80
Cdd:COG2241 3 WLTVVGIGPGGPDGLTPAAREAIAEADVVV--GGKRHLEL------FPDLGAE-RIVWPSPLSELLEE----LLALLRGR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357112131 81 DVAFLVVGDPF----GATthtdlVVRAKSIGvEVKVI-----------------HNASVMNAVGvcglqlyrygetisip 139
Cdd:COG2241 70 RVVVLASGDPLfygiGAT-----LARHLPAE-EVRVIpgisslqlaaarlgwpwQDAAVVSLHG---------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357112131 140 fftetwRP-DSFYEKIQNSRRLglhtLCLLDirvkeptleslcrgkkvyepPRFMTvnTAISQLLEveelhggsAYGPDS 218
Cdd:COG2241 128 ------RPlERLLPALAPGRRV----LVLTD--------------------DGNTP--AAIARLLL--------ERGFGD 167
|
250 260 270
....*....|....*....|....*....|....*...
gi 357112131 219 LCMGVA-RLGSDDQKIVAGPMKKLLDVDFgPPLHCLII 255
Cdd:COG2241 168 SRLTVLeNLGGPDERITRGTAEELADADF-SDLNVVAI 204
|
|
| |
