|
Name |
Accession |
Description |
Interval |
E-value |
| DPH5 |
COG1798 |
Diphthamide biosynthesis methyltransferase [Translation, ribosomal structure and biogenesis]; |
3-256 |
5.39e-143 |
|
Diphthamide biosynthesis methyltransferase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441403 Cd Length: 255 Bit Score: 401.11 E-value: 5.39e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2P9D_A 3 LYFIGLGLYDERDITVKGLEIAKKCDYVFAEFYTSLMAGTTLGRIQKLIGKEIRVMSREDVELNFENIvLPLAKENDVAF 82
Cdd:COG1798 2 LTFVGLGLSDERDITLKGLEALRSADKVYAEFYTSRLIGTDLEKLEELIGKEIVVLDREDVEDNPEEI-LEEAKEKDVVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2P9D_A 83 LTPGDPLVATTHAELRIRAKRAGVESYVIHAPSIYSAV-GITGLHIYKFGKSATVAYPEGNWFPTSYYDVIKENAERGLH 161
Cdd:COG1798 81 LTAGDPMIATTHVDLRLRAKRRGIETRVIHGVSIVSAAiGLTGLQNYKFGKTVTIPFPYEGFVPTSPYDTIKENLERGLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2P9D_A 162 TLLFLDIKAEKRMYMTANEAMELLLKVEDMKKGGVFTDDTLVVVLARAGSLNPTIRAGYVKDLIREDFGDPPHILIVPGK 241
Cdd:COG1798 161 TLVLLDIKADKNRYMTANEALELLLEIEKKRREGVISDDTLAVVVARAGSPDPKIVAGKLSELANYDFGEPPHSLIIPGR 240
|
250
....*....|....*
2P9D_A 242 LHIVEAEYLVEIAGA 256
Cdd:COG1798 241 LHFMEAEALKALAGA 255
|
|
| DHP5_DphB |
cd11647 |
diphthine methyl ester synthase and diphthine synthase; Eukaryotic diphthine methyl ester ... |
3-242 |
1.32e-132 |
|
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: 374.45 E-value: 1.32e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2P9D_A 3 LYFIGLGLYDERDITVKGLEIAKKCDYVFAEFYTSLMAGTTLGRIQKLIGKEIRVMSREDVELNFENIvLPLAKENDVAF 82
Cdd:cd11647 2 LYLIGLGLGDEKDITLEGLEALKKADKVYLEAYTSILPGSKLEELEKLIGKKIILLDREDLEEESEEI-LEEAKKKDVAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2P9D_A 83 LTPGDPLVATTHAELRIRAKRAGVESYVIHAPSIYSAV-GITGLHIYKFGKSATVAYPEGNWFPTSYYDVIKENAERGLH 161
Cdd:cd11647 81 LVPGDPLIATTHIDLRLEAKKRGIKVKVIHNASILSAAgSTSGLQLYKFGRTVTIPFPEENYKPESPYDVIKENLKRGLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2P9D_A 162 TLLFLDIKAEKRMYMTANEAMELLLKVEDMKKGGVFTDDTLVVVLARAGSLNPTIRAGYVKDLIREDFGDPPHILIVPGK 241
Cdd:cd11647 161 TLLLLDIKVEEGRFMTINEAIEILLEIEEKRKEGVITEDTLVVGLARLGSDDQKIVAGTLKELLKEDFGPPPHSLIIPGK 240
|
.
2P9D_A 242 L 242
Cdd:cd11647 241 L 241
|
|
| dph5 |
TIGR00522 |
diphthine synthase; Alternate name: diphthamide biosynthesis S-adenosylmethionine-dependent ... |
2-257 |
7.24e-113 |
|
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: 325.23 E-value: 7.24e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2P9D_A 2 VLYFIGLGLYDERDITVKGLEIAKKCDYVFAEFYTSLMAGTTLGRIQKLIGKEIRVMSREDVELNfENIVLPLAKENDVA 81
Cdd:TIGR00522 1 MLYLIGLGLYDENDISVKGLEAIKKADEVYAEFYTSKLLGSSIEEIEEFFGKRVVVLERSDVEEN-SFRLIERAKSKDVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2P9D_A 82 FLTPGDPLVATTHAELRIRAKRAGVESYVIHAPSIYSAV-GITGLHIYKFGKSATVAYPEGNWFPTSYYDVIKENAERGL 160
Cdd:TIGR00522 80 LLVAGDPMVATTHTDLKLEAKRKGIETRIIHGASISSAVcGLTGLQLYKFGKTATIVFFTDNYRPQTPYNVIKENRKIGL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2P9D_A 161 HTLLFLDIKAEKRMYMTANEAMELLLKVEDMKKGGVFTDDTLVVVLARAGSLNPTIRAGYVKDLIREDFGDPPHILIVPG 240
Cdd:TIGR00522 160 HTLVLLDIHPKENRAMTIGEGLENLLEEEEKRKTGAITPDTYAVVIARAGSGKPVVKCDKIENLKNYDFGEPLHCLVVLA 239
|
250
....*....|....*...
2P9D_A 241 K-LHIVEAEYLVEIAGAP 257
Cdd:TIGR00522 240 KtLHFMEFEYLREFADAP 257
|
|
| PTZ00175 |
PTZ00175 |
diphthine synthase; Provisional |
1-250 |
4.38e-91 |
|
diphthine synthase; Provisional
Pssm-ID: 185500 Cd Length: 270 Bit Score: 270.29 E-value: 4.38e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2P9D_A 1 MVLYFIGLGLYDERDITVKGLEIAKKCDYVFAEFYTSLMAGTTLGRIQKLIGKEIRVMSREDVELNFENIVLPlAKENDV 80
Cdd:PTZ00175 1 MMLYIIGLGLGDEKDITVKGLEAVKSADVVYLESYTSILINSNKEKLEEFYGKPVIEADREMVEEGCDEILEE-AKEKNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2P9D_A 81 AFLTPGDPLVATTHAELRIRAKRAGVESYVIHAPSIYSAVGITGLHIYKFGKSATVAYPEGNWFPTSYYDVIKENAERGL 160
Cdd:PTZ00175 80 AFLVVGDPFCATTHTDLYLRAKKKGIEVEVIHNASIMNAIGCTGLQLYRFGETVSIPFFTETWKPDSFYDKIKANRDNGL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2P9D_A 161 HTLLFLDIKAEKR---------------MYMTANEAMELLLKVEDMKKGGVFTDDTLVVVLARAGSLNPTIRAGYVKDLI 225
Cdd:PTZ00175 160 HTLCLLDIKVKERsvenlmkgrkiyeppRYMTINQAIEQLLEVEEKKGGGVIAEDTLVVGVARVGSDDQQIVSGTLEDLL 239
|
250 260
....*....|....*....|....*.
2P9D_A 226 REDFGDPPHILIVPGK-LHIVEAEYL 250
Cdd:PTZ00175 240 DVDFGPPLHSLVICAPtLHDIEEEFF 265
|
|
| TP_methylase |
pfam00590 |
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ... |
2-224 |
1.08e-16 |
|
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: 76.23 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2P9D_A 2 VLYFIGLGLYDERDITVKGLEIAKKCDYVFAE---FYTSLMAgttLGRIQKLIGKEIRVMSREDVELNFENIVLPLAKE- 77
Cdd:pfam00590 1 KLYLVGVGPGDPDLLTLRALRALKEADVVLGDdsrALEILLD---LLPEDLYFPMTEDKEPLEEAYEEIAEALAAALRAg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2P9D_A 78 NDVAFLTPGDPLVATTHAELRIRAKRAGVESYVIHAPSIYSAVG-ITGLHIYKFGKSATVAYPEGnwfPTSYYDVIKENA 156
Cdd:pfam00590 78 KDVARLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAaRLGIPLTEGGEVLSVLFLPG---LARIELRLLEAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
2P9D_A 157 ERGLHTLLFLDIKAekrmymTANEAMELLLKVEDmkkggvftDDTLVVVLARAGSLNPTIRAGYVKDL 224
Cdd:pfam00590 155 LANGDTVVLLYGPR------RLAELAELLLELYP--------DTTPVAVVERAGTPDEKVVRGTLGEL 208
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DPH5 |
COG1798 |
Diphthamide biosynthesis methyltransferase [Translation, ribosomal structure and biogenesis]; |
3-256 |
5.39e-143 |
|
Diphthamide biosynthesis methyltransferase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441403 Cd Length: 255 Bit Score: 401.11 E-value: 5.39e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2P9D_A 3 LYFIGLGLYDERDITVKGLEIAKKCDYVFAEFYTSLMAGTTLGRIQKLIGKEIRVMSREDVELNFENIvLPLAKENDVAF 82
Cdd:COG1798 2 LTFVGLGLSDERDITLKGLEALRSADKVYAEFYTSRLIGTDLEKLEELIGKEIVVLDREDVEDNPEEI-LEEAKEKDVVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2P9D_A 83 LTPGDPLVATTHAELRIRAKRAGVESYVIHAPSIYSAV-GITGLHIYKFGKSATVAYPEGNWFPTSYYDVIKENAERGLH 161
Cdd:COG1798 81 LTAGDPMIATTHVDLRLRAKRRGIETRVIHGVSIVSAAiGLTGLQNYKFGKTVTIPFPYEGFVPTSPYDTIKENLERGLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2P9D_A 162 TLLFLDIKAEKRMYMTANEAMELLLKVEDMKKGGVFTDDTLVVVLARAGSLNPTIRAGYVKDLIREDFGDPPHILIVPGK 241
Cdd:COG1798 161 TLVLLDIKADKNRYMTANEALELLLEIEKKRREGVISDDTLAVVVARAGSPDPKIVAGKLSELANYDFGEPPHSLIIPGR 240
|
250
....*....|....*
2P9D_A 242 LHIVEAEYLVEIAGA 256
Cdd:COG1798 241 LHFMEAEALKALAGA 255
|
|
| DHP5_DphB |
cd11647 |
diphthine methyl ester synthase and diphthine synthase; Eukaryotic diphthine methyl ester ... |
3-242 |
1.32e-132 |
|
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: 374.45 E-value: 1.32e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2P9D_A 3 LYFIGLGLYDERDITVKGLEIAKKCDYVFAEFYTSLMAGTTLGRIQKLIGKEIRVMSREDVELNFENIvLPLAKENDVAF 82
Cdd:cd11647 2 LYLIGLGLGDEKDITLEGLEALKKADKVYLEAYTSILPGSKLEELEKLIGKKIILLDREDLEEESEEI-LEEAKKKDVAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2P9D_A 83 LTPGDPLVATTHAELRIRAKRAGVESYVIHAPSIYSAV-GITGLHIYKFGKSATVAYPEGNWFPTSYYDVIKENAERGLH 161
Cdd:cd11647 81 LVPGDPLIATTHIDLRLEAKKRGIKVKVIHNASILSAAgSTSGLQLYKFGRTVTIPFPEENYKPESPYDVIKENLKRGLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2P9D_A 162 TLLFLDIKAEKRMYMTANEAMELLLKVEDMKKGGVFTDDTLVVVLARAGSLNPTIRAGYVKDLIREDFGDPPHILIVPGK 241
Cdd:cd11647 161 TLLLLDIKVEEGRFMTINEAIEILLEIEEKRKEGVITEDTLVVGLARLGSDDQKIVAGTLKELLKEDFGPPPHSLIIPGK 240
|
.
2P9D_A 242 L 242
Cdd:cd11647 241 L 241
|
|
| dph5 |
TIGR00522 |
diphthine synthase; Alternate name: diphthamide biosynthesis S-adenosylmethionine-dependent ... |
2-257 |
7.24e-113 |
|
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: 325.23 E-value: 7.24e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2P9D_A 2 VLYFIGLGLYDERDITVKGLEIAKKCDYVFAEFYTSLMAGTTLGRIQKLIGKEIRVMSREDVELNfENIVLPLAKENDVA 81
Cdd:TIGR00522 1 MLYLIGLGLYDENDISVKGLEAIKKADEVYAEFYTSKLLGSSIEEIEEFFGKRVVVLERSDVEEN-SFRLIERAKSKDVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2P9D_A 82 FLTPGDPLVATTHAELRIRAKRAGVESYVIHAPSIYSAV-GITGLHIYKFGKSATVAYPEGNWFPTSYYDVIKENAERGL 160
Cdd:TIGR00522 80 LLVAGDPMVATTHTDLKLEAKRKGIETRIIHGASISSAVcGLTGLQLYKFGKTATIVFFTDNYRPQTPYNVIKENRKIGL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2P9D_A 161 HTLLFLDIKAEKRMYMTANEAMELLLKVEDMKKGGVFTDDTLVVVLARAGSLNPTIRAGYVKDLIREDFGDPPHILIVPG 240
Cdd:TIGR00522 160 HTLVLLDIHPKENRAMTIGEGLENLLEEEEKRKTGAITPDTYAVVIARAGSGKPVVKCDKIENLKNYDFGEPLHCLVVLA 239
|
250
....*....|....*...
2P9D_A 241 K-LHIVEAEYLVEIAGAP 257
Cdd:TIGR00522 240 KtLHFMEFEYLREFADAP 257
|
|
| PTZ00175 |
PTZ00175 |
diphthine synthase; Provisional |
1-250 |
4.38e-91 |
|
diphthine synthase; Provisional
Pssm-ID: 185500 Cd Length: 270 Bit Score: 270.29 E-value: 4.38e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2P9D_A 1 MVLYFIGLGLYDERDITVKGLEIAKKCDYVFAEFYTSLMAGTTLGRIQKLIGKEIRVMSREDVELNFENIVLPlAKENDV 80
Cdd:PTZ00175 1 MMLYIIGLGLGDEKDITVKGLEAVKSADVVYLESYTSILINSNKEKLEEFYGKPVIEADREMVEEGCDEILEE-AKEKNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2P9D_A 81 AFLTPGDPLVATTHAELRIRAKRAGVESYVIHAPSIYSAVGITGLHIYKFGKSATVAYPEGNWFPTSYYDVIKENAERGL 160
Cdd:PTZ00175 80 AFLVVGDPFCATTHTDLYLRAKKKGIEVEVIHNASIMNAIGCTGLQLYRFGETVSIPFFTETWKPDSFYDKIKANRDNGL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2P9D_A 161 HTLLFLDIKAEKR---------------MYMTANEAMELLLKVEDMKKGGVFTDDTLVVVLARAGSLNPTIRAGYVKDLI 225
Cdd:PTZ00175 160 HTLCLLDIKVKERsvenlmkgrkiyeppRYMTINQAIEQLLEVEEKKGGGVIAEDTLVVGVARVGSDDQQIVSGTLEDLL 239
|
250 260
....*....|....*....|....*.
2P9D_A 226 REDFGDPPHILIVPGK-LHIVEAEYL 250
Cdd:PTZ00175 240 DVDFGPPLHSLVICAPtLHDIEEEFF 265
|
|
| TP_methylase |
cd09815 |
S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet ... |
6-239 |
3.65e-59 |
|
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: 187.22 E-value: 3.65e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2P9D_A 6 IGLGLYDERDITVKGLEIAKKCDYVFAEFYTSLMAGTTLgRIQKLIGKEIRVMSREDVELNFENIVLPLAKE-NDVAFLT 84
Cdd:cd09815 1 VGVGPGDPDLLTLRALEILRAADVVVAEDKDSKLLSLVL-RAILKDGKRIYDLHDPNVEEEMAELLLEEARQgKDVAFLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2P9D_A 85 PGDPLVATTHAELRIRAKRAGVESYVIHAPSIYSAVGIT-GLHIYKFGKSATVAYPEGNWFPtsyyDVIKENAERGLHTL 163
Cdd:cd09815 80 PGDPGVAGTGAELVERAEREGVEVKVIPGVSAADAAAAAlGIDLGESFLFVTASDLLENPRL----LVLKALAKERRHLV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
2P9D_A 164 LFLDIKaekrmymTANEAMELLLKVEDMkkggvftDDTLVVVLARAGSLNPTIRAGYVKDLI--REDFGDPPHILIVP 239
Cdd:cd09815 156 LFLDGH-------RFLKALERLLKELGE-------DDTPVVLVANAGSEGEVIRTGTVKELRaeRTERGKPLTTILVG 219
|
|
| TP_methylase |
pfam00590 |
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ... |
2-224 |
1.08e-16 |
|
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: 76.23 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2P9D_A 2 VLYFIGLGLYDERDITVKGLEIAKKCDYVFAE---FYTSLMAgttLGRIQKLIGKEIRVMSREDVELNFENIVLPLAKE- 77
Cdd:pfam00590 1 KLYLVGVGPGDPDLLTLRALRALKEADVVLGDdsrALEILLD---LLPEDLYFPMTEDKEPLEEAYEEIAEALAAALRAg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2P9D_A 78 NDVAFLTPGDPLVATTHAELRIRAKRAGVESYVIHAPSIYSAVG-ITGLHIYKFGKSATVAYPEGnwfPTSYYDVIKENA 156
Cdd:pfam00590 78 KDVARLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAaRLGIPLTEGGEVLSVLFLPG---LARIELRLLEAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
2P9D_A 157 ERGLHTLLFLDIKAekrmymTANEAMELLLKVEDmkkggvftDDTLVVVLARAGSLNPTIRAGYVKDL 224
Cdd:pfam00590 155 LANGDTVVLLYGPR------RLAELAELLLELYP--------DTTPVAVVERAGTPDEKVVRGTLGEL 208
|
|
| PRK05576 |
PRK05576 |
cobalt-factor II C(20)-methyltransferase; |
1-107 |
2.01e-07 |
|
cobalt-factor II C(20)-methyltransferase;
Pssm-ID: 235512 [Multi-domain] Cd Length: 229 Bit Score: 50.30 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2P9D_A 1 MVLYFIGLGLYDERDITVKGLEIAKKCDYVFAEFYTSLMAGTTLGRIQKLIGKEIRV------MSREDVEL------NFE 68
Cdd:PRK05576 2 GKLYGIGLGPGDPELLTVKAARILEEADVVYAPASRKGGGSLALNIVRPYLKEETEIvelhfpMSKDEEEKeavwkeNAE 81
|
90 100 110
....*....|....*....|....*....|....*....
2P9D_A 69 NIVLPLAKENDVAFLTPGDPLVATTHAELRIRAKRAGVE 107
Cdd:PRK05576 82 EIAAEAEEGKNVAFITLGDPNLYSTFSHLLEYLKCHDIE 120
|
|
| Precorrin_2_C20_MT |
cd11645 |
Precorrin-2 C20-methyltransferase, also named CobI or CbiL; Precorrin-2 C20-methyltransferase ... |
6-111 |
5.79e-06 |
|
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: 45.96 E-value: 5.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2P9D_A 6 IGLGLYDERDITVKGLEIAKKCDYVFAeFYTSLMAGTTLGRIQK---LIGKEIRV----MSREDVEL------NFENIVL 72
Cdd:cd11645 1 VGVGPGDPELLTLKAVRILKEADVIFV-PVSKGGEGSAALIIAAallIPDKEIIPlefpMTKDREELeeawdeAAEEIAE 79
|
90 100 110
....*....|....*....|....*....|....*....
2P9D_A 73 PLAKENDVAFLTPGDPLVATTHAELRIRAKRAGVESYVI 111
Cdd:cd11645 80 ELKEGKDVAFLTLGDPSLYSTFSYLLERLRAPGVEVEII 118
|
|
| YabN_N_like |
cd11723 |
N-terminal S-AdoMet-dependent tetrapyrrole methylase domain of Bacillus subtilis YabN and ... |
6-122 |
7.00e-06 |
|
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: 45.94 E-value: 7.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2P9D_A 6 IGLGLYDERDITVKGLEIAKKCDYVFAefytslmagttlgR------IQKLIGKEIRVMSREDV---ELNFENI------ 70
Cdd:cd11723 4 VGLGPGDPDLLTLGALEALKSADKVYL-------------RtarhpvVEELKEEGIEFESFDDLyeeAEDFEEVyeaiae 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
2P9D_A 71 -VLPLAKENDVAFLTPGDPLVATTHAELRIRAKRAGVESYVIHAPS----IYSAVGI 122
Cdd:cd11723 71 rLLEAAEHGDVVYAVPGHPLVAERTVQLLLERAEEGIEVEIIPGVSfldaALAALGI 127
|
|
| RsmI_like |
cd19917 |
tetrapyrrole methylase family protein similar to ribosomal RNA small subunit methyltransferase ... |
4-225 |
2.47e-04 |
|
tetrapyrrole methylase family protein similar to ribosomal RNA small subunit methyltransferase I (RsmI); RsmI, also known as rRNA (cytidine-2'-O-)-methyltransferase, is an S-AdoMet (S-adenosyl-L-methionine or SAM)-dependent methyltransferase responsible for the 2'-O-methylation of cytidine 1402 (C1402) at the P site of bacterial 16S rRNA. Another S-AdoMet-dependent methyltransferase, RsmH (not included in this family), is responsible for N4-methylation at C1402. These methylation reactions may occur at a late step during 30S assembly in the cell. The dimethyl modification is believed to be conserved in bacteria, may play a role in fine-tuning the shape and functions of the P-site to increase the translation fidelity, and has been shown for Staphylococcus aureus, to contribute to virulence in host animals by conferring resistance to oxidative stress.
Pssm-ID: 381180 Cd Length: 217 Bit Score: 41.18 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2P9D_A 4 YFIGLGLYDERDITVKGLEIAKKCDYVFAEFYTSlmaGTTLGRIQKLIGKEIRVMSREDVELNFENIVLPLAKENDVAFL 83
Cdd:cd19917 1 YLVATPIGNTDDITLRALETLKAVDLIICEDTRN---ASRLLKHVGIIGKTLEVLNEHNTPEDIQELLDKLAGGKNVALV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2P9D_A 84 T-PGDPLVATTHAELRIRAKRAGVEsyVIHAP---SIYSAVGITGLHIYKFgksatvaYPEGnwfptsYYDVIKENAERG 159
Cdd:cd19917 78 SdAGTPAFADPGADLVKLCRDAGIP--VVPLPgasSLMTALSASGLKSDRF-------LFYG------FLPAEPGERKKA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
2P9D_A 160 LHTLlfldiKAEKRMYMTANEAMELLLKVEDMKKggVFTDDTLVVVLARAGSLNPTIRAGYVKDLI 225
Cdd:cd19917 143 LKAL-----EQEPRTLIFMETPYRLKKTLEDLAA--VFGPNRKVVLARNLTQEEETILTGTLGELL 201
|
|
| TP_methylase |
cd11724 |
uncharacterized family of the tetrapyrrole methylase superfamily; Members of this superfamily ... |
3-90 |
1.14e-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: 39.46 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2P9D_A 3 LYFIGLGLYDERDITVKGLEIAKKCDYVFA-----EFYTSLMAG-----------TTLGRIQKLIGKEIRVMSREDVELN 66
Cdd:cd11724 2 LYLVGVGPGDPDLITLRALKAIKKADVVFAppdlrKRFAEYLAGkevlddphglfTYYGKKCSPLEEAEKECEELEKQRA 81
|
90 100
....*....|....*....|....*.
2P9D_A 67 -FENIVL-PLAKENDVAFLTPGDPLV 90
Cdd:cd11724 82 eIVQKIReALAQGKNVALLDSGDPTI 107
|
|
| |
