|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00175 |
PTZ00175 |
diphthine synthase; Provisional |
1-266 |
1.45e-150 |
|
diphthine synthase; Provisional
Pssm-ID: 185500 Cd Length: 270 Bit Score: 421.68 E-value: 1.45e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075941 1 MFYLIGLGLFDEKDITLRGLETVKKCQRIYLEAYTSILL-VQKEKLEELYGKEVILADREMVESSSDEILKDADNCDVAM 79
Cdd:PTZ00175 2 MLYIIGLGLGDEKDITVKGLEAVKSADVVYLESYTSILInSNKEKLEEFYGKPVIEADREMVEEGCDEILEEAKEKNVAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075941 80 LVVGDPMGATTHADLVIRARELKIPVRMIHNASIMNAIGACGLQLYKFGQTVSLVFFENNYRPQSFYDHIKENVSLGLHT 159
Cdd:PTZ00175 82 LVVGDPFCATTHTDLYLRAKKKGIEVEVIHNASIMNAIGCTGLQLYRFGETVSIPFFTETWKPDSFYDKIKANRDNGLHT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075941 160 LVLLDIKVKEQSWENLARGRKVYEPPRYMSASLAAQQMLEVEEDRQENICTPDSLCVAVGRMGSDDQVIFAGTLQELAEH 239
Cdd:PTZ00175 162 LCLLDIKVKERSVENLMKGRKIYEPPRYMTINQAIEQLLEVEEKKGGGVIAEDTLVVGVARVGSDDQQIVSGTLEDLLDV 241
|
250 260
....*....|....*....|....*..
gi 19075941 240 DIGPPLHSVVLVGRDVHDLELEFLRAY 266
Cdd:PTZ00175 242 DFGPPLHSLVICAPTLHDIEEEFFELY 268
|
|
| DHP5_DphB |
cd11647 |
diphthine methyl ester synthase and diphthine synthase; Eukaryotic diphthine methyl ester ... |
1-253 |
9.21e-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: 377.91 E-value: 9.21e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075941 1 MFYLIGLGLFDEKDITLRGLETVKKCQRIYLEAYTSILLV-QKEKLEELYGKEVILADREMVESSSDEILKDADNCDVAM 79
Cdd:cd11647 1 MLYLIGLGLGDEKDITLEGLEALKKADKVYLEAYTSILPGsKLEELEKLIGKKIILLDREDLEEESEEILEEAKKKDVAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075941 80 LVVGDPMGATTHADLVIRARELKIPVRMIHNASIMNAIGAC-GLQLYKFGQTVSLVFFENNYRPQSFYDHIKENVSLGLH 158
Cdd:cd11647 81 LVPGDPLIATTHIDLRLEAKKRGIKVKVIHNASILSAAGSTsGLQLYKFGRTVTIPFPEENYKPESPYDVIKENLKRGLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075941 159 TLVLLDIKVkeqswenlargrkvyEPPRYMSASLAAQQMLEVEEDRQENICTPDSLCVAVGRMGSDDQVIFAGTLQELAE 238
Cdd:cd11647 161 TLLLLDIKV---------------EEGRFMTINEAIEILLEIEEKRKEGVITEDTLVVGLARLGSDDQKIVAGTLKELLK 225
|
250
....*....|....*
gi 19075941 239 HDIGPPLHSVVLVGR 253
Cdd:cd11647 226 EDFGPPPHSLIIPGK 240
|
|
| DPH5 |
COG1798 |
Diphthamide biosynthesis methyltransferase [Translation, ribosomal structure and biogenesis]; |
1-267 |
2.46e-114 |
|
Diphthamide biosynthesis methyltransferase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441403 Cd Length: 255 Bit Score: 329.46 E-value: 2.46e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075941 1 MFYLIGLGLFDEKDITLRGLETVKKCQRIYLEAYTSILL-VQKEKLEELYGKEVILADREMVESSSDEILKDADNCDVAM 79
Cdd:COG1798 1 MLTFVGLGLSDERDITLKGLEALRSADKVYAEFYTSRLIgTDLEKLEELIGKEIVVLDREDVEDNPEEILEEAKEKDVVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075941 80 LVVGDPMGATTHADLVIRARELKIPVRMIHNASIMNAI-GACGLQLYKFGQTVSLVFFENNYRPQSFYDHIKENVSLGLH 158
Cdd:COG1798 81 LTAGDPMIATTHVDLRLRAKRRGIETRVIHGVSIVSAAiGLTGLQNYKFGKTVTIPFPYEGFVPTSPYDTIKENLERGLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075941 159 TLVLLDIKVKEQswenlargrkvyeppRYMSASLAAQQMLEVEEDRQENICTPDSLCVAVGRMGSDDQVIFAGTLQELAE 238
Cdd:COG1798 161 TLVLLDIKADKN---------------RYMTANEALELLLEIEKKRREGVISDDTLAVVVARAGSPDPKIVAGKLSELAN 225
|
250 260
....*....|....*....|....*....
gi 19075941 239 HDIGPPLHSVVLVGRdVHDLELEFLRAYA 267
Cdd:COG1798 226 YDFGEPPHSLIIPGR-LHFMEAEALKALA 253
|
|
| dph5 |
TIGR00522 |
diphthine synthase; Alternate name: diphthamide biosynthesis S-adenosylmethionine-dependent ... |
1-267 |
1.41e-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: 299.81 E-value: 1.41e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075941 1 MFYLIGLGLFDEKDITLRGLETVKKCQRIYLEAYTSILLVQK-EKLEELYGKEVILADREMVESSSDEILKDADNCDVAM 79
Cdd:TIGR00522 1 MLYLIGLGLYDENDISVKGLEAIKKADEVYAEFYTSKLLGSSiEEIEEFFGKRVVVLERSDVEENSFRLIERAKSKDVAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075941 80 LVVGDPMGATTHADLVIRARELKIPVRMIHNASIMNAI-GACGLQLYKFGQTVSLVFFENNYRPQSFYDHIKENVSLGLH 158
Cdd:TIGR00522 81 LVAGDPMVATTHTDLKLEAKRKGIETRIIHGASISSAVcGLTGLQLYKFGKTATIVFFTDNYRPQTPYNVIKENRKIGLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075941 159 TLVLLDIKVKEqswenlargrkvyepPRYMSASLAAQQMLEVEEDRQENICTPDSLCVAVGRMGSDDQVIFAGTLQELAE 238
Cdd:TIGR00522 161 TLVLLDIHPKE---------------NRAMTIGEGLENLLEEEEKRKTGAITPDTYAVVIARAGSGKPVVKCDKIENLKN 225
|
250 260
....*....|....*....|....*....
gi 19075941 239 HDIGPPLHSVVLVGRDVHDLELEFLRAYA 267
Cdd:TIGR00522 226 YDFGEPLHCLVVLAKTLHFMEFEYLREFA 254
|
|
| TP_methylase |
pfam00590 |
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ... |
1-237 |
1.11e-20 |
|
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of diverse substrates. This family includes a related group of bacterial proteins of unknown function. This family includes the methylase Dipthine synthase.
Pssm-ID: 425769 [Multi-domain] Cd Length: 209 Bit Score: 87.40 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075941 1 MFYLIGLGLFDEKDITLRGLETVKKCQRIYLE---AYTSILLVQKEKLEELYGKEVILADREMVESSsdEILKDA--DNC 75
Cdd:pfam00590 1 KLYLVGVGPGDPDLLTLRALRALKEADVVLGDdsrALEILLDLLPEDLYFPMTEDKEPLEEAYEEIA--EALAAAlrAGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075941 76 DVAMLVVGDPMGATTHADLVIRARELKIPVRMIHNASIMNAIGAC-GLQLYKFGQTVSLVFFENNYRP-QSFYDHIKENv 153
Cdd:pfam00590 79 DVARLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARlGIPLTEGGEVLSVLFLPGLARIeLRLLEALLAN- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075941 154 slgLHTLVLLDikvkeqSWENLARgrkvyepprymsaslAAQQMLEVEEDRQEnictpdslCVAVGRMGSDDQVIFAGTL 233
Cdd:pfam00590 158 ---GDTVVLLY------GPRRLAE---------------LAELLLELYPDTTP--------VAVVERAGTPDEKVVRGTL 205
|
....
gi 19075941 234 QELA 237
Cdd:pfam00590 206 GELA 209
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00175 |
PTZ00175 |
diphthine synthase; Provisional |
1-266 |
1.45e-150 |
|
diphthine synthase; Provisional
Pssm-ID: 185500 Cd Length: 270 Bit Score: 421.68 E-value: 1.45e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075941 1 MFYLIGLGLFDEKDITLRGLETVKKCQRIYLEAYTSILL-VQKEKLEELYGKEVILADREMVESSSDEILKDADNCDVAM 79
Cdd:PTZ00175 2 MLYIIGLGLGDEKDITVKGLEAVKSADVVYLESYTSILInSNKEKLEEFYGKPVIEADREMVEEGCDEILEEAKEKNVAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075941 80 LVVGDPMGATTHADLVIRARELKIPVRMIHNASIMNAIGACGLQLYKFGQTVSLVFFENNYRPQSFYDHIKENVSLGLHT 159
Cdd:PTZ00175 82 LVVGDPFCATTHTDLYLRAKKKGIEVEVIHNASIMNAIGCTGLQLYRFGETVSIPFFTETWKPDSFYDKIKANRDNGLHT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075941 160 LVLLDIKVKEQSWENLARGRKVYEPPRYMSASLAAQQMLEVEEDRQENICTPDSLCVAVGRMGSDDQVIFAGTLQELAEH 239
Cdd:PTZ00175 162 LCLLDIKVKERSVENLMKGRKIYEPPRYMTINQAIEQLLEVEEKKGGGVIAEDTLVVGVARVGSDDQQIVSGTLEDLLDV 241
|
250 260
....*....|....*....|....*..
gi 19075941 240 DIGPPLHSVVLVGRDVHDLELEFLRAY 266
Cdd:PTZ00175 242 DFGPPLHSLVICAPTLHDIEEEFFELY 268
|
|
| DHP5_DphB |
cd11647 |
diphthine methyl ester synthase and diphthine synthase; Eukaryotic diphthine methyl ester ... |
1-253 |
9.21e-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: 377.91 E-value: 9.21e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075941 1 MFYLIGLGLFDEKDITLRGLETVKKCQRIYLEAYTSILLV-QKEKLEELYGKEVILADREMVESSSDEILKDADNCDVAM 79
Cdd:cd11647 1 MLYLIGLGLGDEKDITLEGLEALKKADKVYLEAYTSILPGsKLEELEKLIGKKIILLDREDLEEESEEILEEAKKKDVAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075941 80 LVVGDPMGATTHADLVIRARELKIPVRMIHNASIMNAIGAC-GLQLYKFGQTVSLVFFENNYRPQSFYDHIKENVSLGLH 158
Cdd:cd11647 81 LVPGDPLIATTHIDLRLEAKKRGIKVKVIHNASILSAAGSTsGLQLYKFGRTVTIPFPEENYKPESPYDVIKENLKRGLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075941 159 TLVLLDIKVkeqswenlargrkvyEPPRYMSASLAAQQMLEVEEDRQENICTPDSLCVAVGRMGSDDQVIFAGTLQELAE 238
Cdd:cd11647 161 TLLLLDIKV---------------EEGRFMTINEAIEILLEIEEKRKEGVITEDTLVVGLARLGSDDQKIVAGTLKELLK 225
|
250
....*....|....*
gi 19075941 239 HDIGPPLHSVVLVGR 253
Cdd:cd11647 226 EDFGPPPHSLIIPGK 240
|
|
| DPH5 |
COG1798 |
Diphthamide biosynthesis methyltransferase [Translation, ribosomal structure and biogenesis]; |
1-267 |
2.46e-114 |
|
Diphthamide biosynthesis methyltransferase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441403 Cd Length: 255 Bit Score: 329.46 E-value: 2.46e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075941 1 MFYLIGLGLFDEKDITLRGLETVKKCQRIYLEAYTSILL-VQKEKLEELYGKEVILADREMVESSSDEILKDADNCDVAM 79
Cdd:COG1798 1 MLTFVGLGLSDERDITLKGLEALRSADKVYAEFYTSRLIgTDLEKLEELIGKEIVVLDREDVEDNPEEILEEAKEKDVVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075941 80 LVVGDPMGATTHADLVIRARELKIPVRMIHNASIMNAI-GACGLQLYKFGQTVSLVFFENNYRPQSFYDHIKENVSLGLH 158
Cdd:COG1798 81 LTAGDPMIATTHVDLRLRAKRRGIETRVIHGVSIVSAAiGLTGLQNYKFGKTVTIPFPYEGFVPTSPYDTIKENLERGLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075941 159 TLVLLDIKVKEQswenlargrkvyeppRYMSASLAAQQMLEVEEDRQENICTPDSLCVAVGRMGSDDQVIFAGTLQELAE 238
Cdd:COG1798 161 TLVLLDIKADKN---------------RYMTANEALELLLEIEKKRREGVISDDTLAVVVARAGSPDPKIVAGKLSELAN 225
|
250 260
....*....|....*....|....*....
gi 19075941 239 HDIGPPLHSVVLVGRdVHDLELEFLRAYA 267
Cdd:COG1798 226 YDFGEPPHSLIIPGR-LHFMEAEALKALA 253
|
|
| dph5 |
TIGR00522 |
diphthine synthase; Alternate name: diphthamide biosynthesis S-adenosylmethionine-dependent ... |
1-267 |
1.41e-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: 299.81 E-value: 1.41e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075941 1 MFYLIGLGLFDEKDITLRGLETVKKCQRIYLEAYTSILLVQK-EKLEELYGKEVILADREMVESSSDEILKDADNCDVAM 79
Cdd:TIGR00522 1 MLYLIGLGLYDENDISVKGLEAIKKADEVYAEFYTSKLLGSSiEEIEEFFGKRVVVLERSDVEENSFRLIERAKSKDVAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075941 80 LVVGDPMGATTHADLVIRARELKIPVRMIHNASIMNAI-GACGLQLYKFGQTVSLVFFENNYRPQSFYDHIKENVSLGLH 158
Cdd:TIGR00522 81 LVAGDPMVATTHTDLKLEAKRKGIETRIIHGASISSAVcGLTGLQLYKFGKTATIVFFTDNYRPQTPYNVIKENRKIGLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075941 159 TLVLLDIKVKEqswenlargrkvyepPRYMSASLAAQQMLEVEEDRQENICTPDSLCVAVGRMGSDDQVIFAGTLQELAE 238
Cdd:TIGR00522 161 TLVLLDIHPKE---------------NRAMTIGEGLENLLEEEEKRKTGAITPDTYAVVIARAGSGKPVVKCDKIENLKN 225
|
250 260
....*....|....*....|....*....
gi 19075941 239 HDIGPPLHSVVLVGRDVHDLELEFLRAYA 267
Cdd:TIGR00522 226 YDFGEPLHCLVVLAKTLHFMEFEYLREFA 254
|
|
| TP_methylase |
cd09815 |
S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet ... |
5-250 |
1.21e-25 |
|
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: 100.93 E-value: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075941 5 IGLGLFDEKDITLRGLETVKKCQRIYLEAYTSILLVQKEKLEELYGKEVI-LADREMVESSSDEILKDADN-CDVAMLVV 82
Cdd:cd09815 1 VGVGPGDPDLLTLRALEILRAADVVVAEDKDSKLLSLVLRAILKDGKRIYdLHDPNVEEEMAELLLEEARQgKDVAFLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075941 83 GDPMGATTHADLVIRARELKIPVRMIHNASIMNA-IGACGLQLYKFGQTVSLVffenNYRPQSFYDHIKENVSLGLHTLV 161
Cdd:cd09815 81 GDPGVAGTGAELVERAEREGVEVKVIPGVSAADAaAAALGIDLGESFLFVTAS----DLLENPRLLVLKALAKERRHLVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075941 162 LLDIKVKEQSWENLArgrKVYEPprymsaslaaqqmleveedrqenictPDSLCVAVGRMGSDDQVIFAGTLQELAEHDI 241
Cdd:cd09815 157 FLDGHRFLKALERLL---KELGE--------------------------DDTPVVLVANAGSEGEVIRTGTVKELRAERT 207
|
250
....*....|.
gi 19075941 242 --GPPLHSVVL 250
Cdd:cd09815 208 erGKPLTTILV 218
|
|
| TP_methylase |
pfam00590 |
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ... |
1-237 |
1.11e-20 |
|
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of diverse substrates. This family includes a related group of bacterial proteins of unknown function. This family includes the methylase Dipthine synthase.
Pssm-ID: 425769 [Multi-domain] Cd Length: 209 Bit Score: 87.40 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075941 1 MFYLIGLGLFDEKDITLRGLETVKKCQRIYLE---AYTSILLVQKEKLEELYGKEVILADREMVESSsdEILKDA--DNC 75
Cdd:pfam00590 1 KLYLVGVGPGDPDLLTLRALRALKEADVVLGDdsrALEILLDLLPEDLYFPMTEDKEPLEEAYEEIA--EALAAAlrAGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075941 76 DVAMLVVGDPMGATTHADLVIRARELKIPVRMIHNASIMNAIGAC-GLQLYKFGQTVSLVFFENNYRP-QSFYDHIKENv 153
Cdd:pfam00590 79 DVARLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARlGIPLTEGGEVLSVLFLPGLARIeLRLLEALLAN- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075941 154 slgLHTLVLLDikvkeqSWENLARgrkvyepprymsaslAAQQMLEVEEDRQEnictpdslCVAVGRMGSDDQVIFAGTL 233
Cdd:pfam00590 158 ---GDTVVLLY------GPRRLAE---------------LAELLLELYPDTTP--------VAVVERAGTPDEKVVRGTL 205
|
....
gi 19075941 234 QELA 237
Cdd:pfam00590 206 GELA 209
|
|
| RsmI_like |
cd19917 |
tetrapyrrole methylase family protein similar to ribosomal RNA small subunit methyltransferase ... |
3-178 |
4.76e-05 |
|
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: 43.49 E-value: 4.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075941 3 YLIGLGLFDEKDITLRGLETVKKCQRIYLEAY--TSILLvqkeKLEELYGKEVILADREMVESSSDEILKD-ADNCDVAM 79
Cdd:cd19917 1 YLVATPIGNTDDITLRALETLKAVDLIICEDTrnASRLL----KHVGIIGKTLEVLNEHNTPEDIQELLDKlAGGKNVAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075941 80 LV-VGDPMGATTHADLVIRARELKIPVRMIHNAS-IMNAIGACGLQLYKF---------------------GQTVSLVFF 136
Cdd:cd19917 77 VSdAGTPAFADPGADLVKLCRDAGIPVVPLPGASsLMTALSASGLKSDRFlfygflpaepgerkkalkaleQEPRTLIFM 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 19075941 137 ENNYRPQSFYDHIKENvsLGLHTLVLLDIKVKeQSWENLARG 178
Cdd:cd19917 157 ETPYRLKKTLEDLAAV--FGPNRKVVLARNLT-QEEETILTG 195
|
|
| cobI_cbiL |
TIGR01467 |
precorrin-2 C(20)-methyltransferase; This model represents precorrin-2 C(20)-methyltransferase, ... |
1-119 |
1.58e-04 |
|
precorrin-2 C(20)-methyltransferase; This model represents precorrin-2 C(20)-methyltransferase, one of several closely related S-adenosylmethionine-dependent methyltransferases involved in cobalamin (vitamin B12) biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
Pssm-ID: 273642 [Multi-domain] Cd Length: 230 Bit Score: 41.91 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075941 1 MFYLIGLGLFDEKDITLRGLETVKKCQRIYLEAytsillvqKEKLEELYGKEVIL------------------ADREMVE 62
Cdd:TIGR01467 2 KLYGVGVGPGDPELITVKALEALRSADVIAVPA--------SKKGRESLARKIVEdylkpndtrilelvfpmtKDRDELE 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19075941 63 SSSDEILKDADNC-----DVAMLVVGDPMGATTHADLVIRARELKIPVRMIHNASIMNAIGA 119
Cdd:TIGR01467 74 KAWDEAAEAVAAEleegrDVAFLTLGDPSLYSTFSYLLQRLQGMGIEVEVVPGITSFAACAS 135
|
|
| Precorrin_2_C20_MT |
cd11645 |
Precorrin-2 C20-methyltransferase, also named CobI or CbiL; Precorrin-2 C20-methyltransferase ... |
5-108 |
3.23e-04 |
|
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: 40.95 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075941 5 IGLGLFDEKDITLRGLETVKKCQRIYL---EAYTSILLVQKEKLEELYGKEVIL------ADREMVESSSDE----ILKD 71
Cdd:cd11645 1 VGVGPGDPELLTLKAVRILKEADVIFVpvsKGGEGSAALIIAAALLIPDKEIIPlefpmtKDREELEEAWDEaaeeIAEE 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 19075941 72 -ADNCDVAMLVVGDPMGATTHADLVIRARELKIPVRMI 108
Cdd:cd11645 81 lKEGKDVAFLTLGDPSLYSTFSYLLERLRAPGVEVEII 118
|
|
| RsmI_like |
cd19918 |
uncharacterized subfamily of the tetrapyrrole methylase family similar to Ribosomal RNA small ... |
13-127 |
5.98e-04 |
|
uncharacterized subfamily of the tetrapyrrole methylase family 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: 381181 Cd Length: 217 Bit Score: 40.21 E-value: 5.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075941 13 KDITLRGLETVKKCQRIYLEAY--TSILLvqKEKLEElygKEVILADREMVESSSDEILKDADNCDVAMLV--VGDPMGA 88
Cdd:cd19918 11 DDITLRALEVLKEVDVIICEEFkeGSRLL--KKLIIE---KELLLLNEHNEKEDAAELLDLLAQGKSVALIsdCGTPVFA 85
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 19075941 89 TTHADLVIRARELKIPVRMIHNAS-IMNAIGACGLQLYKF 127
Cdd:cd19918 86 DPGALLVKLCIQKGIPVVPVPGASsLMAALSVSGFKIDRF 125
|
|
| YabN_N_like |
cd11723 |
N-terminal S-AdoMet-dependent tetrapyrrole methylase domain of Bacillus subtilis YabN and ... |
3-112 |
6.34e-04 |
|
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: 40.16 E-value: 6.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075941 3 YLIGLGLFDEKDITLRGLETVKKCQRIYL---------------EAYTSI--LLVQKEKLEELYgkeviladREMVEsss 65
Cdd:cd11723 2 TIVGLGPGDPDLLTLGALEALKSADKVYLrtarhpvveelkeegIEFESFddLYEEAEDFEEVY--------EAIAE--- 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 19075941 66 dEILKDADNCDVAMLVVGDPMGATTHADLVIRARELKIPVRMIHNAS 112
Cdd:cd11723 71 -RLLEAAEHGDVVYAVPGHPLVAERTVQLLLERAEEGIEVEIIPGVS 116
|
|
| PRK05576 |
PRK05576 |
cobalt-factor II C(20)-methyltransferase; |
1-86 |
1.80e-03 |
|
cobalt-factor II C(20)-methyltransferase;
Pssm-ID: 235512 [Multi-domain] Cd Length: 229 Bit Score: 38.74 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075941 1 MFYLIGLGLFDEKDITLRGLETVKKCQRIYLEAYT----SILL-VQKEKLEElyGKEVIL------ADREMVESS----S 65
Cdd:PRK05576 3 KLYGIGLGPGDPELLTVKAARILEEADVVYAPASRkgggSLALnIVRPYLKE--ETEIVElhfpmsKDEEEKEAVwkenA 80
|
90 100
....*....|....*....|..
gi 19075941 66 DEILKDADNC-DVAMLVVGDPM 86
Cdd:PRK05576 81 EEIAAEAEEGkNVAFITLGDPN 102
|
|
| |
