|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00175 |
PTZ00175 |
diphthine synthase; Provisional |
1-273 |
1.06e-162 |
|
diphthine synthase; Provisional
Pssm-ID: 185500 Cd Length: 270 Bit Score: 452.11 E-value: 1.06e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573117 1 MLYIIGLGLGDEKDITLRGLEAVKKSQKVYMEAYTSLLsFGLSADglsNLEKFYGKPIILADREMVEEKAGDMIDEAIDN 80
Cdd:PTZ00175 2 MLYIIGLGLGDEKDITVKGLEAVKSADVVYLESYTSIL-INSNKE---KLEEFYGKPVIEADREMVEEGCDEILEEAKEK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573117 81 DVAFLVVGDPFGATTHSDLVVRAKTLGVKVEVVHNASVMNAVGICGLQLYHYGETVSIPFFTETWRPDSFYEKIKKNRSL 160
Cdd:PTZ00175 78 NVAFLVVGDPFCATTHTDLYLRAKKKGIEVEVIHNASIMNAIGCTGLQLYRFGETVSIPFFTETWKPDSFYDKIKANRDN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573117 161 GLHTLCLLDIRVKEPTFESLCRgGKKQYEPPRYMSVNTAIEQLLEVEQKHGDSVYGEDTQCVGFARLGSEDQTIVAGTMK 240
Cdd:PTZ00175 158 GLHTLCLLDIKVKERSVENLMK-GRKIYEPPRYMTINQAIEQLLEVEEKKGGGVIAEDTLVVGVARVGSDDQQIVSGTLE 236
|
250 260 270
....*....|....*....|....*....|....
gi 42573117 241 QLESVDFGAPLHCLVIVGET-HPVEEEMLEFYKY 273
Cdd:PTZ00175 237 DLLDVDFGPPLHSLVICAPTlHDIEEEFFELYRI 270
|
|
| DHP5_DphB |
cd11647 |
diphthine methyl ester synthase and diphthine synthase; Eukaryotic diphthine methyl ester ... |
1-260 |
1.54e-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: 392.55 E-value: 1.54e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573117 1 MLYIIGLGLGDEKDITLRGLEAVKKSQKVYMEAYTSLLSFGLsadgLSNLEKFYGKPIILADREMVEEKAGDMIDEAIDN 80
Cdd:cd11647 1 MLYLIGLGLGDEKDITLEGLEALKKADKVYLEAYTSILPGSK----LEELEKLIGKKIILLDREDLEEESEEILEEAKKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573117 81 DVAFLVVGDPFGATTHSDLVVRAKTLGVKVEVVHNASVMNAVGIC-GLQLYHYGETVSIPFFTETWRPDSFYEKIKKNRS 159
Cdd:cd11647 77 DVALLVPGDPLIATTHIDLRLEAKKRGIKVKVIHNASILSAAGSTsGLQLYKFGRTVTIPFPEENYKPESPYDVIKENLK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573117 160 LGLHTLCLLDIRVkeptfeslcrggkkqyEPPRYMSVNTAIEQLLEVEQKHGDSVYGEDTQCVGFARLGSEDQTIVAGTM 239
Cdd:cd11647 157 RGLHTLLLLDIKV----------------EEGRFMTINEAIEILLEIEEKRKEGVITEDTLVVGLARLGSDDQKIVAGTL 220
|
250 260
....*....|....*....|.
gi 42573117 240 KQLESVDFGAPLHCLVIVGET 260
Cdd:cd11647 221 KELLKEDFGPPPHSLIIPGKL 241
|
|
| DPH5 |
COG1798 |
Diphthamide biosynthesis methyltransferase [Translation, ribosomal structure and biogenesis]; |
1-269 |
5.18e-110 |
|
Diphthamide biosynthesis methyltransferase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441403 Cd Length: 255 Bit Score: 318.29 E-value: 5.18e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573117 1 MLYIIGLGLGDEKDITLRGLEAVKKSQKVYMEAYTSLLSfGLSadgLSNLEKFYGKPIILADREMVEEKAGDMIDEAIDN 80
Cdd:COG1798 1 MLTFVGLGLSDERDITLKGLEALRSADKVYAEFYTSRLI-GTD---LEKLEELIGKEIVVLDREDVEDNPEEILEEAKEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573117 81 DVAFLVVGDPFGATTHSDLVVRAKTLGVKVEVVHNASVMNAV-GICGLQLYHYGETVSIPFFTETWRPDSFYEKIKKNRS 159
Cdd:COG1798 77 DVVFLTAGDPMIATTHVDLRLRAKRRGIETRVIHGVSIVSAAiGLTGLQNYKFGKTVTIPFPYEGFVPTSPYDTIKENLE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573117 160 LGLHTLCLLDIRVkeptfeslcrggkkqyEPPRYMSVNTAIEQLLEVEQKHGDSVYGEDTQCVGFARLGSEDQTIVAGTM 239
Cdd:COG1798 157 RGLHTLVLLDIKA----------------DKNRYMTANEALELLLEIEKKRREGVISDDTLAVVVARAGSPDPKIVAGKL 220
|
250 260 270
....*....|....*....|....*....|
gi 42573117 240 KQLESVDFGAPLHCLVIVGETHPVEEEMLE 269
Cdd:COG1798 221 SELANYDFGEPPHSLIIPGRLHFMEAEALK 250
|
|
| dph5 |
TIGR00522 |
diphthine synthase; Alternate name: diphthamide biosynthesis S-adenosylmethionine-dependent ... |
1-268 |
2.30e-102 |
|
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: 299.04 E-value: 2.30e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573117 1 MLYIIGLGLGDEKDITLRGLEAVKKSQKVYMEAYTSLLSfglsADGLSNLEKFYGKPIILADREMVEEKAGDMIDEAIDN 80
Cdd:TIGR00522 1 MLYLIGLGLYDENDISVKGLEAIKKADEVYAEFYTSKLL----GSSIEEIEEFFGKRVVVLERSDVEENSFRLIERAKSK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573117 81 DVAFLVVGDPFGATTHSDLVVRAKTLGVKVEVVHNASVMNAV-GICGLQLYHYGETVSIPFFTETWRPDSFYEKIKKNRS 159
Cdd:TIGR00522 77 DVALLVAGDPMVATTHTDLKLEAKRKGIETRIIHGASISSAVcGLTGLQLYKFGKTATIVFFTDNYRPQTPYNVIKENRK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573117 160 LGLHTLCLLDIRVKEptfeslcrggkkqyepPRYMSVNTAIEQLLEVEQKHGDSVYGEDTQCVGFARLGSEDQTIVAGTM 239
Cdd:TIGR00522 157 IGLHTLVLLDIHPKE----------------NRAMTIGEGLENLLEEEEKRKTGAITPDTYAVVIARAGSGKPVVKCDKI 220
|
250 260 270
....*....|....*....|....*....|
gi 42573117 240 KQLESVDFGAPLHCLVIVGET-HPVEEEML 268
Cdd:TIGR00522 221 ENLKNYDFGEPLHCLVVLAKTlHFMEFEYL 250
|
|
| TP_methylase |
pfam00590 |
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ... |
1-243 |
3.29e-26 |
|
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: 102.04 E-value: 3.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573117 1 MLYIIGLGLGDEKDITLRGLEAVKKSQKVY---MEAYTSLLSfglsadgLSNLEKFYGKPIILADREMVEEKAGDMIDEA 77
Cdd:pfam00590 1 KLYLVGVGPGDPDLLTLRALRALKEADVVLgddSRALEILLD-------LLPEDLYFPMTEDKEPLEEAYEEIAEALAAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573117 78 IDN--DVAFLVVGDPFGATTHSDLVVRAKTLGVKVEVVHNASVMNAVGIC-GLQLYHYGETVSIPFFTET-WRPDSFYEK 153
Cdd:pfam00590 74 LRAgkDVARLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARlGIPLTEGGEVLSVLFLPGLaRIELRLLEA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573117 154 IKKNRslglHTLCLLDIRVKeptfeslcrggkkqyepprymsVNTAIEQLLEveqkhgdsVYGEDTQCVGFARLGSEDQT 233
Cdd:pfam00590 154 LLANG----DTVVLLYGPRR----------------------LAELAELLLE--------LYPDTTPVAVVERAGTPDEK 199
|
250
....*....|
gi 42573117 234 IVAGTMKQLE 243
Cdd:pfam00590 200 VVRGTLGELA 209
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00175 |
PTZ00175 |
diphthine synthase; Provisional |
1-273 |
1.06e-162 |
|
diphthine synthase; Provisional
Pssm-ID: 185500 Cd Length: 270 Bit Score: 452.11 E-value: 1.06e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573117 1 MLYIIGLGLGDEKDITLRGLEAVKKSQKVYMEAYTSLLsFGLSADglsNLEKFYGKPIILADREMVEEKAGDMIDEAIDN 80
Cdd:PTZ00175 2 MLYIIGLGLGDEKDITVKGLEAVKSADVVYLESYTSIL-INSNKE---KLEEFYGKPVIEADREMVEEGCDEILEEAKEK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573117 81 DVAFLVVGDPFGATTHSDLVVRAKTLGVKVEVVHNASVMNAVGICGLQLYHYGETVSIPFFTETWRPDSFYEKIKKNRSL 160
Cdd:PTZ00175 78 NVAFLVVGDPFCATTHTDLYLRAKKKGIEVEVIHNASIMNAIGCTGLQLYRFGETVSIPFFTETWKPDSFYDKIKANRDN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573117 161 GLHTLCLLDIRVKEPTFESLCRgGKKQYEPPRYMSVNTAIEQLLEVEQKHGDSVYGEDTQCVGFARLGSEDQTIVAGTMK 240
Cdd:PTZ00175 158 GLHTLCLLDIKVKERSVENLMK-GRKIYEPPRYMTINQAIEQLLEVEEKKGGGVIAEDTLVVGVARVGSDDQQIVSGTLE 236
|
250 260 270
....*....|....*....|....*....|....
gi 42573117 241 QLESVDFGAPLHCLVIVGET-HPVEEEMLEFYKY 273
Cdd:PTZ00175 237 DLLDVDFGPPLHSLVICAPTlHDIEEEFFELYRI 270
|
|
| DHP5_DphB |
cd11647 |
diphthine methyl ester synthase and diphthine synthase; Eukaryotic diphthine methyl ester ... |
1-260 |
1.54e-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: 392.55 E-value: 1.54e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573117 1 MLYIIGLGLGDEKDITLRGLEAVKKSQKVYMEAYTSLLSFGLsadgLSNLEKFYGKPIILADREMVEEKAGDMIDEAIDN 80
Cdd:cd11647 1 MLYLIGLGLGDEKDITLEGLEALKKADKVYLEAYTSILPGSK----LEELEKLIGKKIILLDREDLEEESEEILEEAKKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573117 81 DVAFLVVGDPFGATTHSDLVVRAKTLGVKVEVVHNASVMNAVGIC-GLQLYHYGETVSIPFFTETWRPDSFYEKIKKNRS 159
Cdd:cd11647 77 DVALLVPGDPLIATTHIDLRLEAKKRGIKVKVIHNASILSAAGSTsGLQLYKFGRTVTIPFPEENYKPESPYDVIKENLK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573117 160 LGLHTLCLLDIRVkeptfeslcrggkkqyEPPRYMSVNTAIEQLLEVEQKHGDSVYGEDTQCVGFARLGSEDQTIVAGTM 239
Cdd:cd11647 157 RGLHTLLLLDIKV----------------EEGRFMTINEAIEILLEIEEKRKEGVITEDTLVVGLARLGSDDQKIVAGTL 220
|
250 260
....*....|....*....|.
gi 42573117 240 KQLESVDFGAPLHCLVIVGET 260
Cdd:cd11647 221 KELLKEDFGPPPHSLIIPGKL 241
|
|
| DPH5 |
COG1798 |
Diphthamide biosynthesis methyltransferase [Translation, ribosomal structure and biogenesis]; |
1-269 |
5.18e-110 |
|
Diphthamide biosynthesis methyltransferase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441403 Cd Length: 255 Bit Score: 318.29 E-value: 5.18e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573117 1 MLYIIGLGLGDEKDITLRGLEAVKKSQKVYMEAYTSLLSfGLSadgLSNLEKFYGKPIILADREMVEEKAGDMIDEAIDN 80
Cdd:COG1798 1 MLTFVGLGLSDERDITLKGLEALRSADKVYAEFYTSRLI-GTD---LEKLEELIGKEIVVLDREDVEDNPEEILEEAKEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573117 81 DVAFLVVGDPFGATTHSDLVVRAKTLGVKVEVVHNASVMNAV-GICGLQLYHYGETVSIPFFTETWRPDSFYEKIKKNRS 159
Cdd:COG1798 77 DVVFLTAGDPMIATTHVDLRLRAKRRGIETRVIHGVSIVSAAiGLTGLQNYKFGKTVTIPFPYEGFVPTSPYDTIKENLE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573117 160 LGLHTLCLLDIRVkeptfeslcrggkkqyEPPRYMSVNTAIEQLLEVEQKHGDSVYGEDTQCVGFARLGSEDQTIVAGTM 239
Cdd:COG1798 157 RGLHTLVLLDIKA----------------DKNRYMTANEALELLLEIEKKRREGVISDDTLAVVVARAGSPDPKIVAGKL 220
|
250 260 270
....*....|....*....|....*....|
gi 42573117 240 KQLESVDFGAPLHCLVIVGETHPVEEEMLE 269
Cdd:COG1798 221 SELANYDFGEPPHSLIIPGRLHFMEAEALK 250
|
|
| dph5 |
TIGR00522 |
diphthine synthase; Alternate name: diphthamide biosynthesis S-adenosylmethionine-dependent ... |
1-268 |
2.30e-102 |
|
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: 299.04 E-value: 2.30e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573117 1 MLYIIGLGLGDEKDITLRGLEAVKKSQKVYMEAYTSLLSfglsADGLSNLEKFYGKPIILADREMVEEKAGDMIDEAIDN 80
Cdd:TIGR00522 1 MLYLIGLGLYDENDISVKGLEAIKKADEVYAEFYTSKLL----GSSIEEIEEFFGKRVVVLERSDVEENSFRLIERAKSK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573117 81 DVAFLVVGDPFGATTHSDLVVRAKTLGVKVEVVHNASVMNAV-GICGLQLYHYGETVSIPFFTETWRPDSFYEKIKKNRS 159
Cdd:TIGR00522 77 DVALLVAGDPMVATTHTDLKLEAKRKGIETRIIHGASISSAVcGLTGLQLYKFGKTATIVFFTDNYRPQTPYNVIKENRK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573117 160 LGLHTLCLLDIRVKEptfeslcrggkkqyepPRYMSVNTAIEQLLEVEQKHGDSVYGEDTQCVGFARLGSEDQTIVAGTM 239
Cdd:TIGR00522 157 IGLHTLVLLDIHPKE----------------NRAMTIGEGLENLLEEEEKRKTGAITPDTYAVVIARAGSGKPVVKCDKI 220
|
250 260 270
....*....|....*....|....*....|
gi 42573117 240 KQLESVDFGAPLHCLVIVGET-HPVEEEML 268
Cdd:TIGR00522 221 ENLKNYDFGEPLHCLVVLAKTlHFMEFEYL 250
|
|
| TP_methylase |
cd09815 |
S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet ... |
5-256 |
7.04e-31 |
|
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: 114.80 E-value: 7.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573117 5 IGLGLGDEKDITLRGLEAVKKSQKVYMEAYTSLLSFGLSADGLsnlekFYGKPII-LADREMVEEKAGDMIDEA-IDNDV 82
Cdd:cd09815 1 VGVGPGDPDLLTLRALEILRAADVVVAEDKDSKLLSLVLRAIL-----KDGKRIYdLHDPNVEEEMAELLLEEArQGKDV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573117 83 AFLVVGDPFGATTHSDLVVRAKTLGVKVEVVHNASVMNAVGI-CGLQLYHYGETVSIPFFTETWRPDsfyeKIKKNRSLG 161
Cdd:cd09815 76 AFLSPGDPGVAGTGAELVERAEREGVEVKVIPGVSAADAAAAaLGIDLGESFLFVTASDLLENPRLL----VLKALAKER 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573117 162 LHTLclldirvkepTFESLCRGGKkqyepprymsvntAIEQLLEVEQKhgdsvygEDTQCVGFARLGSEDQTIVAGTMKQ 241
Cdd:cd09815 152 RHLV----------LFLDGHRFLK-------------ALERLLKELGE-------DDTPVVLVANAGSEGEVIRTGTVKE 201
|
250
....*....|....*..
gi 42573117 242 L--ESVDFGAPLHCLVI 256
Cdd:cd09815 202 LraERTERGKPLTTILV 218
|
|
| TP_methylase |
pfam00590 |
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ... |
1-243 |
3.29e-26 |
|
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: 102.04 E-value: 3.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573117 1 MLYIIGLGLGDEKDITLRGLEAVKKSQKVY---MEAYTSLLSfglsadgLSNLEKFYGKPIILADREMVEEKAGDMIDEA 77
Cdd:pfam00590 1 KLYLVGVGPGDPDLLTLRALRALKEADVVLgddSRALEILLD-------LLPEDLYFPMTEDKEPLEEAYEEIAEALAAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573117 78 IDN--DVAFLVVGDPFGATTHSDLVVRAKTLGVKVEVVHNASVMNAVGIC-GLQLYHYGETVSIPFFTET-WRPDSFYEK 153
Cdd:pfam00590 74 LRAgkDVARLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARlGIPLTEGGEVLSVLFLPGLaRIELRLLEA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573117 154 IKKNRslglHTLCLLDIRVKeptfeslcrggkkqyepprymsVNTAIEQLLEveqkhgdsVYGEDTQCVGFARLGSEDQT 233
Cdd:pfam00590 154 LLANG----DTVVLLYGPRR----------------------LAELAELLLE--------LYPDTTPVAVVERAGTPDEK 199
|
250
....*....|
gi 42573117 234 IVAGTMKQLE 243
Cdd:pfam00590 200 VVRGTLGELA 209
|
|
| YabN_N_like |
cd11723 |
N-terminal S-AdoMet-dependent tetrapyrrole methylase domain of Bacillus subtilis YabN and ... |
2-129 |
1.06e-09 |
|
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: 57.11 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573117 2 LYIIGLGLGDEKDITLRGLEAVKKSQKVYM-----EAYTSLLSFGL---SADGL----SNLEKFYgkpiiladREMVEEk 69
Cdd:cd11723 1 ITIVGLGPGDPDLLTLGALEALKSADKVYLrtarhPVVEELKEEGIefeSFDDLyeeaEDFEEVY--------EAIAER- 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42573117 70 agdMIDEAIDNDVAFLVVGDPFGATTHSDLVVRAKTLGVKVEVVHNAS----VMNAVGIC---GLQL 129
Cdd:cd11723 72 ---LLEAAEHGDVVYAVPGHPLVAERTVQLLLERAEEGIEVEIIPGVSfldaALAALGIDpieGLQI 135
|
|
| PRK05576 |
PRK05576 |
cobalt-factor II C(20)-methyltransferase; |
1-113 |
1.64e-08 |
|
cobalt-factor II C(20)-methyltransferase;
Pssm-ID: 235512 [Multi-domain] Cd Length: 229 Bit Score: 53.77 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573117 1 MLYIIGLGLGDEKDITLRGLEAVKKSQKVYMEAYTSllsfglSADGLS-NLEKFYGKP----IIL-----ADREMVE--- 67
Cdd:PRK05576 3 KLYGIGLGPGDPELLTVKAARILEEADVVYAPASRK------GGGSLAlNIVRPYLKEeteiVELhfpmsKDEEEKEavw 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 42573117 68 EKAGDMIDEAI--DNDVAFLVVGDPFGATTHSDLVVRAKTLGVKVEVV 113
Cdd:PRK05576 77 KENAEEIAAEAeeGKNVAFITLGDPNLYSTFSHLLEYLKCHDIEVETV 124
|
|
| cobI_cbiL |
TIGR01467 |
precorrin-2 C(20)-methyltransferase; This model represents precorrin-2 C(20)-methyltransferase, ... |
1-122 |
1.28e-07 |
|
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: 51.16 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573117 1 MLYIIGLGLGDEKDITLRGLEAVKKSQKVYMEAYTSllsfGLSADGLSNLEKfYGKPIILADREMV---------EEKAG 71
Cdd:TIGR01467 2 KLYGVGVGPGDPELITVKALEALRSADVIAVPASKK----GRESLARKIVED-YLKPNDTRILELVfpmtkdrdeLEKAW 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 42573117 72 DMIDEAI------DNDVAFLVVGDPFGATTHSDLVVRAKTLGVKVEVVHNASVMNAV 122
Cdd:TIGR01467 77 DEAAEAVaaeleeGRDVAFLTLGDPSLYSTFSYLLQRLQGMGIEVEVVPGITSFAAC 133
|
|
| CobF |
COG2243 |
Precorrin-2 methylase [Coenzyme transport and metabolism]; Precorrin-2 methylase is part of ... |
2-113 |
1.54e-06 |
|
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: 47.79 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573117 2 LYIIGLGLGDEKDITLRGLEAVKKSQKVYMeaytsllsFGLSADGLSN----LEKFYGKPIILA--------DREMVE-- 67
Cdd:COG2243 5 LYGVGVGPGDPELLTLKAVRALREADVIAY--------PAKGAGKASLareiVAPYLPPARIVElvfpmttdYEALVAaw 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 42573117 68 EKAGDMIDEAIDN--DVAFLVVGDPF--GATTHsdLVVRAKTLGVKVEVV 113
Cdd:COG2243 77 DEAAARIAEELEAgrDVAFLTEGDPSlySTFMY--LLERLRERGFEVEVI 124
|
|
| TP_methylase |
cd11724 |
uncharacterized family of the tetrapyrrole methylase superfamily; Members of this superfamily ... |
2-92 |
1.70e-06 |
|
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: 47.94 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573117 2 LYIIGLGLGDEKDITLRGLEAVKKSQ-----KVYMEAYTSLLS-----------FGLSADGLSNLEKfyGKPIILADREM 65
Cdd:cd11724 2 LYLVGVGPGDPDLITLRALKAIKKADvvfapPDLRKRFAEYLAgkevlddphglFTYYGKKCSPLEE--AEKECEELEKQ 79
|
90 100 110
....*....|....*....|....*....|.
gi 42573117 66 VEEKAGdMIDEAIDN--DVAFLVVGDP--FG 92
Cdd:cd11724 80 RAEIVQ-KIREALAQgkNVALLDSGDPtiYG 109
|
|
| PRK05787 |
PRK05787 |
cobalt-precorrin-7 (C(5))-methyltransferase; |
1-113 |
1.32e-05 |
|
cobalt-precorrin-7 (C(5))-methyltransferase;
Pssm-ID: 235609 [Multi-domain] Cd Length: 210 Bit Score: 44.86 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573117 1 MLYIIGLGLGDEKDITLRGLEAVKKSQKVYmeaytsllsfGlsadGLSNLEKFygKPIILADREMVEEKAGDMID----E 76
Cdd:PRK05787 1 MIYIVGIGPGDPEYLTLKALEAIRKADVVV----------G----SKRVLELF--PELIDGEAFVLTAGLRDLLEwlelA 64
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 42573117 77 AIDNDVAFLVVGDPfgatTHSDL--VVRAKTL-GVKVEVV 113
Cdd:PRK05787 65 AKGKNVVVLSTGDP----LFSGLgkLLKVRRAvAEDVEVI 100
|
|
| Precorrin_2_C20_MT |
cd11645 |
Precorrin-2 C20-methyltransferase, also named CobI or CbiL; Precorrin-2 C20-methyltransferase ... |
5-113 |
1.71e-05 |
|
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: 44.81 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573117 5 IGLGLGDEKDITLRGLEAVKKSQKVY----MEAYTSLLSFGLSADGLSNlekfygKPIIL------ADREMVEE---KAG 71
Cdd:cd11645 1 VGVGPGDPELLTLKAVRILKEADVIFvpvsKGGEGSAALIIAAALLIPD------KEIIPlefpmtKDREELEEawdEAA 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 42573117 72 DMIDEAIDN--DVAFLVVGDPFGATTHSDLVVRAKTLGVKVEVV 113
Cdd:cd11645 75 EEIAEELKEgkDVAFLTLGDPSLYSTFSYLLERLRAPGVEVEII 118
|
|
| cobJ_cbiH |
TIGR01466 |
precorrin-3B C17-methyltransferase; This model represents precorrin-3B C17-methyltransferase, ... |
2-123 |
3.42e-05 |
|
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: 44.21 E-value: 3.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573117 2 LYIIGLGLGDEKDITLRGLEAVKKSQKVYmeAYTSLLSFglsadgLSNLekFYGKPIILADreMVEE--KAGDMIDEAID 79
Cdd:TIGR01466 1 LYVVGIGPGAEELMTPEAKEALAEADVIV--GYKTYLDL------IEDL--IPGKEVVTSG--MREEiaRAELAIELAAE 68
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 42573117 80 -NDVAFLVVGDP--FGATTHSDLVVRAKTLGVKVEVVHNASVMNAVG 123
Cdd:TIGR01466 69 gRTVALVSSGDPgiYGMAALVFEALEKKGAEVDIEVIPGITAASAAA 115
|
|
| PRK05765 |
PRK05765 |
precorrin-3B C17-methyltransferase; Provisional |
2-113 |
3.16e-04 |
|
precorrin-3B C17-methyltransferase; Provisional
Pssm-ID: 235597 Cd Length: 246 Bit Score: 41.31 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573117 2 LYIIGLGLGDEKDITLRGLEAVKKSQKVYmeAYTSLLsfGLSADGLSnlekfyGKPIILAdrEMVEE--KAGDMIDEAI- 78
Cdd:PRK05765 4 LYIVGIGPGSKEQRTIKAQEAIEKSNVII--GYNTYL--RLISDLLD------GKEVIGA--RMKEEifRANTAIEKALe 71
|
90 100 110
....*....|....*....|....*....|....*...
gi 42573117 79 DNDVAFLVVGDP--FG-ATTHSDLVVRAKtLGVKVEVV 113
Cdd:PRK05765 72 GNIVALVSSGDPqvYGmAGLVFELISRRK-LDVDVEVI 108
|
|
| CobL |
COG2241 |
Precorrin-6B methylase 1 [Coenzyme transport and metabolism]; Precorrin-6B methylase 1 is part ... |
1-256 |
1.87e-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: 38.59 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573117 1 MLYIIGLGLGDEKDITLRGLEAVKKSQKVymeaytsllsFGlsadGLSNLEKFygkPIILADREMVEEKAGDMIDE---- 76
Cdd:COG2241 3 WLTVVGIGPGGPDGLTPAAREAIAEADVV----------VG----GKRHLELF---PDLGAERIVWPSPLSELLEEllal 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573117 77 AIDNDVAFLVVGDPF----GATthsdlvVRAKTLGVKVEVVHNASVM----NAVGICglqlYHYGETVSIpffteTWRP- 147
Cdd:COG2241 66 LRGRRVVVLASGDPLfygiGAT------LARHLPAEEVRVIPGISSLqlaaARLGWP----WQDAAVVSL-----HGRPl 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573117 148 DSFYEKIKKNRSLGLhtlclldirvkeptfesLCRGGKkqyePPRymsvntAIEQLLEveqKHGdsvYGEDTQCVGfARL 227
Cdd:COG2241 131 ERLLPALAPGRRVLV-----------------LTDDGN----TPA------AIARLLL---ERG---FGDSRLTVL-ENL 176
|
250 260
....*....|....*....|....*....
gi 42573117 228 GSEDQTIVAGTMKQLESVDFgAPLHCLVI 256
Cdd:COG2241 177 GGPDERITRGTAEELADADF-SDLNVVAI 204
|
|
| Precorrin-6Y-MT |
cd11644 |
Precorrin-6Y methyltransferase (also named CbiE); CbiE (precorrin-6Y methyltransferase, also ... |
5-256 |
6.25e-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: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573117 5 IGLGLGDEKDITLRGLEAVKKSQKVYmeaytsllsfglsadG----LSNLEKFYGKPIILADREMVEekagdMIDE--AI 78
Cdd:cd11644 1 IGIGPGGPEYLTPEAREAIEEADVVI---------------GakrlLELFPDLGAEKIPLPSEDIAE-----LLEEiaEA 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573117 79 DNDVAFLVVGDP--FGATThsdlVVRAKTLGVKVEVV-----------------HNASVMNAVGicglqlyhygetvsip 139
Cdd:cd11644 61 GKRVVVLASGDPgfYGIGK----TLLRRLGGEEVEVIpgissvqlaaarlglpwEDARLVSLHG---------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573117 140 fftetwRPD-SFYEKIKKNRSLGLhtlclldirvkeptfesLCRGGKkqyepprymSVNTAIEQLLEveqkhgdsvYG-E 217
Cdd:cd11644 121 ------RDLeNLRRALRRGRKVFV-----------------LTDGKN---------TPAEIARLLLE---------RGlG 159
|
250 260 270
....*....|....*....|....*....|....*....
gi 42573117 218 DTQCVGFARLGSEDQTIVAGTMKQLESVDFgAPLHCLVI 256
Cdd:cd11644 160 DSRVTVGENLGYPDERITEGTAEELAEEEF-SDLNVVLI 197
|
|
| |
