|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00175 |
PTZ00175 |
diphthine synthase; Provisional |
1-267 |
3.07e-153 |
|
diphthine synthase; Provisional
Pssm-ID: 185500 Cd Length: 270 Bit Score: 428.99 E-value: 3.07e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568764 1 MLYLIGLGLSYETDITVRGLQTVKKCKRVYLEAYTSILMAADQDSLSKFYGKDVILADRELVETGSDDILEGADKDDIAF 80
Cdd:PTZ00175 2 MLYIIGLGLGDEKDITVKGLEAVKSADVVYLESYTSILINSNKEKLEEFYGKPVIEADREMVEEGCDEILEEAKEKNVAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568764 81 LVVGDPFGATTHTDLVIRARELGIKVEAIHNASVMNAVGACGLQLYQFGQTISMVFFTDSWKPDSFYEKIMGNRKLGLHT 160
Cdd:PTZ00175 82 LVVGDPFCATTHTDLYLRAKKKGIEVEVIHNASIMNAIGCTGLQLYRFGETVSIPFFTETWKPDSFYDKIKANRDNGLHT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568764 161 LILLDIKVKEQSFENMMKGKLIYEPPRYMNIATAAQQLIEVEETKKEQAYTENTPCVAVSRLGAPTQKFKAGTLKELASY 240
Cdd:PTZ00175 162 LCLLDIKVKERSVENLMKGRKIYEPPRYMTINQAIEQLLEVEEKKGGGVIAEDTLVVGVARVGSDDQQIVSGTLEDLLDV 241
|
250 260
....*....|....*....|....*..
gi 254568764 241 DSGEPLHSLVMLGRQLHDLELEYLYEY 267
Cdd:PTZ00175 242 DFGPPLHSLVICAPTLHDIEEEFFELY 268
|
|
| DHP5_DphB |
cd11647 |
diphthine methyl ester synthase and diphthine synthase; Eukaryotic diphthine methyl ester ... |
1-254 |
2.92e-131 |
|
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: 372.52 E-value: 2.92e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568764 1 MLYLIGLGLSYETDITVRGLQTVKKCKRVYLEAYTSILMAADQDSLSKFYGKDVILADRELVETGSDDILEGADKDDIAF 80
Cdd:cd11647 1 MLYLIGLGLGDEKDITLEGLEALKKADKVYLEAYTSILPGSKLEELEKLIGKKIILLDREDLEEESEEILEEAKKKDVAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568764 81 LVVGDPFGATTHTDLVIRARELGIKVEAIHNASVMNAVGAC-GLQLYQFGQTISMVFFTDSWKPDSFYEKIMGNRKLGLH 159
Cdd:cd11647 81 LVPGDPLIATTHIDLRLEAKKRGIKVKVIHNASILSAAGSTsGLQLYKFGRTVTIPFPEENYKPESPYDVIKENLKRGLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568764 160 TLILLDIKVkeqsfenmmkgkliyEPPRYMNIATAAQQLIEVEETKKEQAYTENTPCVAVSRLGAPTQKFKAGTLKELAS 239
Cdd:cd11647 161 TLLLLDIKV---------------EEGRFMTINEAIEILLEIEEKRKEGVITEDTLVVGLARLGSDDQKIVAGTLKELLK 225
|
250
....*....|....*
gi 254568764 240 YDSGEPLHSLVMLGR 254
Cdd:cd11647 226 EDFGPPPHSLIIPGK 240
|
|
| dph5 |
TIGR00522 |
diphthine synthase; Alternate name: diphthamide biosynthesis S-adenosylmethionine-dependent ... |
1-271 |
3.78e-117 |
|
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: 337.17 E-value: 3.78e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568764 1 MLYLIGLGLSYETDITVRGLQTVKKCKRVYLEAYTSILMAADQDSLSKFYGKDVILADRELVETGSDDILEGADKDDIAF 80
Cdd:TIGR00522 1 MLYLIGLGLYDENDISVKGLEAIKKADEVYAEFYTSKLLGSSIEEIEEFFGKRVVVLERSDVEENSFRLIERAKSKDVAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568764 81 LVVGDPFGATTHTDLVIRARELGIKVEAIHNASVMNAV-GACGLQLYQFGQTISMVFFTDSWKPDSFYEKIMGNRKLGLH 159
Cdd:TIGR00522 81 LVAGDPMVATTHTDLKLEAKRKGIETRIIHGASISSAVcGLTGLQLYKFGKTATIVFFTDNYRPQTPYNVIKENRKIGLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568764 160 TLILLDIKVKEqsfenmmkgkliyepPRYMNIATAAQQLIEVEETKKEQAYTENTPCVAVSRLGAPTQKFKAGTLKELAS 239
Cdd:TIGR00522 161 TLVLLDIHPKE---------------NRAMTIGEGLENLLEEEEKRKTGAITPDTYAVVIARAGSGKPVVKCDKIENLKN 225
|
250 260 270
....*....|....*....|....*....|..
gi 254568764 240 YDSGEPLHSLVMLGRQLHDLELEYLYEYCDDK 271
Cdd:TIGR00522 226 YDFGEPLHCLVVLAKTLHFMEFEYLREFADAP 257
|
|
| DPH5 |
COG1798 |
Diphthamide biosynthesis methyltransferase [Translation, ribosomal structure and biogenesis]; |
1-269 |
7.46e-109 |
|
Diphthamide biosynthesis methyltransferase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441403 Cd Length: 255 Bit Score: 315.98 E-value: 7.46e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568764 1 MLYLIGLGLSYETDITVRGLQTVKKCKRVYLEAYTSILMAADQDSLSKFYGKDVILADRELVETGSDDILEGADKDDIAF 80
Cdd:COG1798 1 MLTFVGLGLSDERDITLKGLEALRSADKVYAEFYTSRLIGTDLEKLEELIGKEIVVLDREDVEDNPEEILEEAKEKDVVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568764 81 LVVGDPFGATTHTDLVIRARELGIKVEAIHNASVMNAV-GACGLQLYQFGQTISMVFFTDSWKPDSFYEKIMGNRKLGLH 159
Cdd:COG1798 81 LTAGDPMIATTHVDLRLRAKRRGIETRVIHGVSIVSAAiGLTGLQNYKFGKTVTIPFPYEGFVPTSPYDTIKENLERGLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568764 160 TLILLDIKVKEQsfenmmkgkliyeppRYMNIATAAQQLIEVEETKKEQAYTENTPCVAVSRLGAPTQKFKAGTLKELAS 239
Cdd:COG1798 161 TLVLLDIKADKN---------------RYMTANEALELLLEIEKKRREGVISDDTLAVVVARAGSPDPKIVAGKLSELAN 225
|
250 260 270
....*....|....*....|....*....|
gi 254568764 240 YDSGEPLHSLVMLGRqLHDLELEYLYEYCD 269
Cdd:COG1798 226 YDFGEPPHSLIIPGR-LHFMEAEALKALAG 254
|
|
| TP_methylase |
pfam00590 |
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ... |
1-238 |
2.22e-27 |
|
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: 105.50 E-value: 2.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568764 1 MLYLIGLGLSYETDITVRGLQTVKKCKRVYLE---AYTSILMAADQDSLSKFYGKDVIL--ADRELVETGSDDILEGadk 75
Cdd:pfam00590 1 KLYLVGVGPGDPDLLTLRALRALKEADVVLGDdsrALEILLDLLPEDLYFPMTEDKEPLeeAYEEIAEALAAALRAG--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568764 76 DDIAFLVVGDPFGATTHTDLVIRARELGIKVEAIHNASVMNAVGACGLQLYQFGQTISMVFFTDSW--KPDSFYEKIMGN 153
Cdd:pfam00590 78 KDVARLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARLGIPLTEGGEVLSVLFLPGLarIELRLLEALLAN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568764 154 RklglHTLIlldikvkeqsfenmmkgklIYEPPRymNIATAAQQLIEveetkkeqAYTENTPCVAVSRLGAPTQKFKAGT 233
Cdd:pfam00590 158 G----DTVV-------------------LLYGPR--RLAELAELLLE--------LYPDTTPVAVVERAGTPDEKVVRGT 204
|
....*
gi 254568764 234 LKELA 238
Cdd:pfam00590 205 LGELA 209
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00175 |
PTZ00175 |
diphthine synthase; Provisional |
1-267 |
3.07e-153 |
|
diphthine synthase; Provisional
Pssm-ID: 185500 Cd Length: 270 Bit Score: 428.99 E-value: 3.07e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568764 1 MLYLIGLGLSYETDITVRGLQTVKKCKRVYLEAYTSILMAADQDSLSKFYGKDVILADRELVETGSDDILEGADKDDIAF 80
Cdd:PTZ00175 2 MLYIIGLGLGDEKDITVKGLEAVKSADVVYLESYTSILINSNKEKLEEFYGKPVIEADREMVEEGCDEILEEAKEKNVAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568764 81 LVVGDPFGATTHTDLVIRARELGIKVEAIHNASVMNAVGACGLQLYQFGQTISMVFFTDSWKPDSFYEKIMGNRKLGLHT 160
Cdd:PTZ00175 82 LVVGDPFCATTHTDLYLRAKKKGIEVEVIHNASIMNAIGCTGLQLYRFGETVSIPFFTETWKPDSFYDKIKANRDNGLHT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568764 161 LILLDIKVKEQSFENMMKGKLIYEPPRYMNIATAAQQLIEVEETKKEQAYTENTPCVAVSRLGAPTQKFKAGTLKELASY 240
Cdd:PTZ00175 162 LCLLDIKVKERSVENLMKGRKIYEPPRYMTINQAIEQLLEVEEKKGGGVIAEDTLVVGVARVGSDDQQIVSGTLEDLLDV 241
|
250 260
....*....|....*....|....*..
gi 254568764 241 DSGEPLHSLVMLGRQLHDLELEYLYEY 267
Cdd:PTZ00175 242 DFGPPLHSLVICAPTLHDIEEEFFELY 268
|
|
| DHP5_DphB |
cd11647 |
diphthine methyl ester synthase and diphthine synthase; Eukaryotic diphthine methyl ester ... |
1-254 |
2.92e-131 |
|
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: 372.52 E-value: 2.92e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568764 1 MLYLIGLGLSYETDITVRGLQTVKKCKRVYLEAYTSILMAADQDSLSKFYGKDVILADRELVETGSDDILEGADKDDIAF 80
Cdd:cd11647 1 MLYLIGLGLGDEKDITLEGLEALKKADKVYLEAYTSILPGSKLEELEKLIGKKIILLDREDLEEESEEILEEAKKKDVAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568764 81 LVVGDPFGATTHTDLVIRARELGIKVEAIHNASVMNAVGAC-GLQLYQFGQTISMVFFTDSWKPDSFYEKIMGNRKLGLH 159
Cdd:cd11647 81 LVPGDPLIATTHIDLRLEAKKRGIKVKVIHNASILSAAGSTsGLQLYKFGRTVTIPFPEENYKPESPYDVIKENLKRGLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568764 160 TLILLDIKVkeqsfenmmkgkliyEPPRYMNIATAAQQLIEVEETKKEQAYTENTPCVAVSRLGAPTQKFKAGTLKELAS 239
Cdd:cd11647 161 TLLLLDIKV---------------EEGRFMTINEAIEILLEIEEKRKEGVITEDTLVVGLARLGSDDQKIVAGTLKELLK 225
|
250
....*....|....*
gi 254568764 240 YDSGEPLHSLVMLGR 254
Cdd:cd11647 226 EDFGPPPHSLIIPGK 240
|
|
| dph5 |
TIGR00522 |
diphthine synthase; Alternate name: diphthamide biosynthesis S-adenosylmethionine-dependent ... |
1-271 |
3.78e-117 |
|
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: 337.17 E-value: 3.78e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568764 1 MLYLIGLGLSYETDITVRGLQTVKKCKRVYLEAYTSILMAADQDSLSKFYGKDVILADRELVETGSDDILEGADKDDIAF 80
Cdd:TIGR00522 1 MLYLIGLGLYDENDISVKGLEAIKKADEVYAEFYTSKLLGSSIEEIEEFFGKRVVVLERSDVEENSFRLIERAKSKDVAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568764 81 LVVGDPFGATTHTDLVIRARELGIKVEAIHNASVMNAV-GACGLQLYQFGQTISMVFFTDSWKPDSFYEKIMGNRKLGLH 159
Cdd:TIGR00522 81 LVAGDPMVATTHTDLKLEAKRKGIETRIIHGASISSAVcGLTGLQLYKFGKTATIVFFTDNYRPQTPYNVIKENRKIGLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568764 160 TLILLDIKVKEqsfenmmkgkliyepPRYMNIATAAQQLIEVEETKKEQAYTENTPCVAVSRLGAPTQKFKAGTLKELAS 239
Cdd:TIGR00522 161 TLVLLDIHPKE---------------NRAMTIGEGLENLLEEEEKRKTGAITPDTYAVVIARAGSGKPVVKCDKIENLKN 225
|
250 260 270
....*....|....*....|....*....|..
gi 254568764 240 YDSGEPLHSLVMLGRQLHDLELEYLYEYCDDK 271
Cdd:TIGR00522 226 YDFGEPLHCLVVLAKTLHFMEFEYLREFADAP 257
|
|
| DPH5 |
COG1798 |
Diphthamide biosynthesis methyltransferase [Translation, ribosomal structure and biogenesis]; |
1-269 |
7.46e-109 |
|
Diphthamide biosynthesis methyltransferase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441403 Cd Length: 255 Bit Score: 315.98 E-value: 7.46e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568764 1 MLYLIGLGLSYETDITVRGLQTVKKCKRVYLEAYTSILMAADQDSLSKFYGKDVILADRELVETGSDDILEGADKDDIAF 80
Cdd:COG1798 1 MLTFVGLGLSDERDITLKGLEALRSADKVYAEFYTSRLIGTDLEKLEELIGKEIVVLDREDVEDNPEEILEEAKEKDVVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568764 81 LVVGDPFGATTHTDLVIRARELGIKVEAIHNASVMNAV-GACGLQLYQFGQTISMVFFTDSWKPDSFYEKIMGNRKLGLH 159
Cdd:COG1798 81 LTAGDPMIATTHVDLRLRAKRRGIETRVIHGVSIVSAAiGLTGLQNYKFGKTVTIPFPYEGFVPTSPYDTIKENLERGLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568764 160 TLILLDIKVKEQsfenmmkgkliyeppRYMNIATAAQQLIEVEETKKEQAYTENTPCVAVSRLGAPTQKFKAGTLKELAS 239
Cdd:COG1798 161 TLVLLDIKADKN---------------RYMTANEALELLLEIEKKRREGVISDDTLAVVVARAGSPDPKIVAGKLSELAN 225
|
250 260 270
....*....|....*....|....*....|
gi 254568764 240 YDSGEPLHSLVMLGRqLHDLELEYLYEYCD 269
Cdd:COG1798 226 YDFGEPPHSLIIPGR-LHFMEAEALKALAG 254
|
|
| TP_methylase |
pfam00590 |
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ... |
1-238 |
2.22e-27 |
|
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: 105.50 E-value: 2.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568764 1 MLYLIGLGLSYETDITVRGLQTVKKCKRVYLE---AYTSILMAADQDSLSKFYGKDVIL--ADRELVETGSDDILEGadk 75
Cdd:pfam00590 1 KLYLVGVGPGDPDLLTLRALRALKEADVVLGDdsrALEILLDLLPEDLYFPMTEDKEPLeeAYEEIAEALAAALRAG--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568764 76 DDIAFLVVGDPFGATTHTDLVIRARELGIKVEAIHNASVMNAVGACGLQLYQFGQTISMVFFTDSW--KPDSFYEKIMGN 153
Cdd:pfam00590 78 KDVARLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARLGIPLTEGGEVLSVLFLPGLarIELRLLEALLAN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568764 154 RklglHTLIlldikvkeqsfenmmkgklIYEPPRymNIATAAQQLIEveetkkeqAYTENTPCVAVSRLGAPTQKFKAGT 233
Cdd:pfam00590 158 G----DTVV-------------------LLYGPR--RLAELAELLLE--------LYPDTTPVAVVERAGTPDEKVVRGT 204
|
....*
gi 254568764 234 LKELA 238
Cdd:pfam00590 205 LGELA 209
|
|
| TP_methylase |
cd09815 |
S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet ... |
5-217 |
1.17e-20 |
|
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: 87.83 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568764 5 IGLGLSYETDITVRGLQTVKKCKRVYLEAYTSILMAADQDSLSKFyGKDVI-LADRELVETGSDDILEGADKD-DIAFLV 82
Cdd:cd09815 1 VGVGPGDPDLLTLRALEILRAADVVVAEDKDSKLLSLVLRAILKD-GKRIYdLHDPNVEEEMAELLLEEARQGkDVAFLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568764 83 VGDPFGATTHTDLVIRARELGIKVEAIHNASVMNAVGA-CGLQLYQFGQTISMVFFtdswKPDSFYEKIMGNRKLGLHTL 161
Cdd:cd09815 80 PGDPGVAGTGAELVERAEREGVEVKVIPGVSAADAAAAaLGIDLGESFLFVTASDL----LENPRLLVLKALAKERRHLV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254568764 162 ILLDIKVKEQSFENMMKGKLiyEPPRYMNIATAA---QQLIE---VEETKKEQAYTENTPCV 217
Cdd:cd09815 156 LFLDGHRFLKALERLLKELG--EDDTPVVLVANAgseGEVIRtgtVKELRAERTERGKPLTT 215
|
|
| YabN_N_like |
cd11723 |
N-terminal S-AdoMet-dependent tetrapyrrole methylase domain of Bacillus subtilis YabN and ... |
2-125 |
4.76e-05 |
|
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: 43.63 E-value: 4.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568764 2 LYLIGLGLSYETDITVRGLQTVKKCKRVYLEayTSILMAADQ--------DSLSKFYGKdvilADR--ELVETGSDDILE 71
Cdd:cd11723 1 ITIVGLGPGDPDLLTLGALEALKSADKVYLR--TARHPVVEElkeegiefESFDDLYEE----AEDfeEVYEAIAERLLE 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254568764 72 GADKDDIAFLVVGDPFGATTHTDLVIRARELGIKVEAIHNAS----VMNAVGAC---GLQL 125
Cdd:cd11723 75 AAEHGDVVYAVPGHPLVAERTVQLLLERAEEGIEVEIIPGVSfldaALAALGIDpieGLQI 135
|
|
| cobI_cbiL |
TIGR01467 |
precorrin-2 C(20)-methyltransferase; This model represents precorrin-2 C(20)-methyltransferase, ... |
1-120 |
4.39e-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: 40.76 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568764 1 MLYLIGLGLSYETDITVRGLQTVK-------------------KCKRVYLEAYTSIL------MAADQDSLSKFYgkdvi 55
Cdd:TIGR01467 2 KLYGVGVGPGDPELITVKALEALRsadviavpaskkgreslarKIVEDYLKPNDTRIlelvfpMTKDRDELEKAW----- 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254568764 56 ladRELVETGSDDILEGADkddIAFLVVGDPFGATTHTDLVIRARELGIKVEAIHNASVMNAVGA 120
Cdd:TIGR01467 77 ---DEAAEAVAAELEEGRD---VAFLTLGDPSLYSTFSYLLQRLQGMGIEVEVVPGITSFAACAS 135
|
|
| SUMT |
cd11642 |
Uroporphyrin-III C-methyltransferase (also known as S-Adenosyl-L-methionine:uroporphyrinogen ... |
188-254 |
4.42e-03 |
|
Uroporphyrin-III C-methyltransferase (also known as S-Adenosyl-L-methionine:uroporphyrinogen III methyltransferase, SUMT); SUMT is an enzyme of the cobalamin and siroheme biosynthetic pathway. It catalyzes the first of three steps leading to the formation of siroheme from uroporphyrinogen III; it transfers two methyl groups from S-adenosyl-L-methionine to the C-2 and C-7 atoms of uroporphyrinogen III to yield precorrin-2 via the intermediate formation of precorrin-1. Precorrin-2 is also a precursor for the biosynthesis of vitamin B12, coenzyme F430, siroheme and heme d1. This family includes proteins in which the SUMT domain is fused to other functional domains, such as to a uroporphyrinogen-III synthase domain to form bifunctional uroporphyrinogen-III methylase/uroporphyrinogen-III synthase, or to a dual function dehydrogenase-chelatase domain, as in the case of the multifunctional S-adenosyl-L-methionine (SAM)-dependent bismethyltransferase/dehydrogenase/ferrochelatase CysG, which catalyzes all three steps that transform uroporphyrinogen III into siroheme.
Pssm-ID: 381169 Cd Length: 228 Bit Score: 37.80 E-value: 4.42e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254568764 188 YM---NIATAAQQLIEveetkkeQAYTENTPCVAVSRLGAPTQKFKAGTLKELASYDSGEPLHS--LVMLGR 254
Cdd:cd11642 162 YMgvsNLEEIAERLIA-------AGLPPDTPVAIVENATTPDQRVVVGTLAELAEKAAEAGIRSpaLIVVGE 226
|
|
| CobF |
COG2243 |
Precorrin-2 methylase [Coenzyme transport and metabolism]; Precorrin-2 methylase is part of ... |
2-109 |
7.43e-03 |
|
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: 37.00 E-value: 7.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254568764 2 LYLIGLG-----LsyetdITVRGLQTVKKCKRVY---------------LEAYTS---IL-----MAADQDSLSKFYgKD 53
Cdd:COG2243 5 LYGVGVGpgdpeL-----LTLKAVRALREADVIAypakgagkaslareiVAPYLPparIVelvfpMTTDYEALVAAW-DE 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 254568764 54 VILADRELVETGSDdilegadkddIAFLVVGDPF--GATTHtdLVIRARELGIKVEAI 109
Cdd:COG2243 79 AAARIAEELEAGRD----------VAFLTEGDPSlySTFMY--LLERLRERGFEVEVI 124
|
|
| |
