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Conserved domains on  [gi|383413479|gb|AFH29953|]
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diphthine synthase isoform a [Macaca mulatta]

Protein Classification

diphthine methyl ester synthase( domain architecture ID 10794325)

diphthine methyl ester synthase is a S-adenosyl-L-methionine-dependent methyltransferase that catalyzes four methylations of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine methyl ester

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PTZ00175 PTZ00175
diphthine synthase; Provisional
1-272 1.45e-164

diphthine synthase; Provisional


:

Pssm-ID: 185500  Cd Length: 270  Bit Score: 457.11  E-value: 1.45e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383413479   1 MLYLIGLGLGDAKDITVKGLEAVRRCSRVYLEAYTSVL-TVGKEALEEFYGRKLILADREEVEQEADNILKDADISDVAF 79
Cdd:PTZ00175   2 MLYIIGLGLGDEKDITVKGLEAVKSADVVYLESYTSILiNSNKEKLEEFYGKPVIEADREMVEEGCDEILEEAKEKNVAF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383413479  80 LVVGDPFGATTHSDLVLRATKLGIPYRVIHNASIMNAVGCCGLQLYKFGETVSIVFWTDTWRPESFFDKVKKNRQNGMHT 159
Cdd:PTZ00175  82 LVVGDPFCATTHTDLYLRAKKKGIEVEVIHNASIMNAIGCTGLQLYRFGETVSIPFFTETWKPDSFYDKIKANRDNGLHT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383413479 160 LCLLDIKVKEQSLENLIKGRKIYEPPRYMSVNQAAQQLLEIIQNQRirgeEPAITEETLCVGLARVGADDQKIAAGTLQQ 239
Cdd:PTZ00175 162 LCLLDIKVKERSVENLMKGRKIYEPPRYMTINQAIEQLLEVEEKKG----GGVIAEDTLVVGVARVGSDDQQIVSGTLED 237
                        250       260       270
                 ....*....|....*....|....*....|...
gi 383413479 240 MCTVDLGEPLHSLIITGGSIHPIEMEMLNLFSI 272
Cdd:PTZ00175 238 LLDVDFGPPLHSLVICAPTLHDIEEEFFELYRI 270
 
Name Accession Description Interval E-value
PTZ00175 PTZ00175
diphthine synthase; Provisional
1-272 1.45e-164

diphthine synthase; Provisional


Pssm-ID: 185500  Cd Length: 270  Bit Score: 457.11  E-value: 1.45e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383413479   1 MLYLIGLGLGDAKDITVKGLEAVRRCSRVYLEAYTSVL-TVGKEALEEFYGRKLILADREEVEQEADNILKDADISDVAF 79
Cdd:PTZ00175   2 MLYIIGLGLGDEKDITVKGLEAVKSADVVYLESYTSILiNSNKEKLEEFYGKPVIEADREMVEEGCDEILEEAKEKNVAF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383413479  80 LVVGDPFGATTHSDLVLRATKLGIPYRVIHNASIMNAVGCCGLQLYKFGETVSIVFWTDTWRPESFFDKVKKNRQNGMHT 159
Cdd:PTZ00175  82 LVVGDPFCATTHTDLYLRAKKKGIEVEVIHNASIMNAIGCTGLQLYRFGETVSIPFFTETWKPDSFYDKIKANRDNGLHT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383413479 160 LCLLDIKVKEQSLENLIKGRKIYEPPRYMSVNQAAQQLLEIIQNQRirgeEPAITEETLCVGLARVGADDQKIAAGTLQQ 239
Cdd:PTZ00175 162 LCLLDIKVKERSVENLMKGRKIYEPPRYMTINQAIEQLLEVEEKKG----GGVIAEDTLVVGVARVGSDDQQIVSGTLED 237
                        250       260       270
                 ....*....|....*....|....*....|...
gi 383413479 240 MCTVDLGEPLHSLIITGGSIHPIEMEMLNLFSI 272
Cdd:PTZ00175 238 LLDVDFGPPLHSLVICAPTLHDIEEEFFELYRI 270
DHP5_DphB cd11647
diphthine methyl ester synthase and diphthine synthase; Eukaryotic diphthine methyl ester ...
1-256 2.01e-138

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: 389.85  E-value: 2.01e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383413479   1 MLYLIGLGLGDAKDITVKGLEAVRRCSRVYLEAYTSVLTVGK-EALEEFYGRKLILADREEVEQEADNILKDADISDVAF 79
Cdd:cd11647    1 MLYLIGLGLGDEKDITLEGLEALKKADKVYLEAYTSILPGSKlEELEKLIGKKIILLDREDLEEESEEILEEAKKKDVAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383413479  80 LVVGDPFGATTHSDLVLRATKLGIPYRVIHNASIMNAVGCC-GLQLYKFGETVSIVFWTDTWRPESFFDKVKKNRQNGMH 158
Cdd:cd11647   81 LVPGDPLIATTHIDLRLEAKKRGIKVKVIHNASILSAAGSTsGLQLYKFGRTVTIPFPEENYKPESPYDVIKENLKRGLH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383413479 159 TLCLLDIKVkeqslenlikgrkiyEPPRYMSVNQAAQQLLEIIQNQRirgeEPAITEETLCVGLARVGADDQKIAAGTLQ 238
Cdd:cd11647  161 TLLLLDIKV---------------EEGRFMTINEAIEILLEIEEKRK----EGVITEDTLVVGLARLGSDDQKIVAGTLK 221
                        250
                 ....*....|....*...
gi 383413479 239 QMCTVDLGEPLHSLIITG 256
Cdd:cd11647  222 ELLKEDFGPPPHSLIIPG 239
DPH5 COG1798
Diphthamide biosynthesis methyltransferase [Translation, ribosomal structure and biogenesis];
1-267 8.79e-107

Diphthamide biosynthesis methyltransferase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441403  Cd Length: 255  Bit Score: 310.20  E-value: 8.79e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383413479   1 MLYLIGLGLGDAKDITVKGLEAVRRCSRVYLEAYTSVLT-VGKEALEEFYGRKLILADREEVEQEADNILKDADISDVAF 79
Cdd:COG1798    1 MLTFVGLGLSDERDITLKGLEALRSADKVYAEFYTSRLIgTDLEKLEELIGKEIVVLDREDVEDNPEEILEEAKEKDVVF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383413479  80 LVVGDPFGATTHSDLVLRATKLGIPYRVIHNASIMNAV-GCCGLQLYKFGETVSIVFWTDTWRPESFFDKVKKNRQNGMH 158
Cdd:COG1798   81 LTAGDPMIATTHVDLRLRAKRRGIETRVIHGVSIVSAAiGLTGLQNYKFGKTVTIPFPYEGFVPTSPYDTIKENLERGLH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383413479 159 TLCLLDIKVKEQslenlikgrkiyeppRYMSVNQAAQQLLEIIQNQRirgeEPAITEETLCVGLARVGADDQKIAAGTLQ 238
Cdd:COG1798  161 TLVLLDIKADKN---------------RYMTANEALELLLEIEKKRR----EGVISDDTLAVVVARAGSPDPKIVAGKLS 221
                        250       260
                 ....*....|....*....|....*....
gi 383413479 239 QMCTVDLGEPLHSLIITgGSIHPIEMEML 267
Cdd:COG1798  222 ELANYDFGEPPHSLIIP-GRLHFMEAEAL 249
dph5 TIGR00522
diphthine synthase; Alternate name: diphthamide biosynthesis S-adenosylmethionine-dependent ...
1-271 2.81e-100

diphthine synthase; Alternate name: diphthamide biosynthesis S-adenosylmethionine-dependent methyltransferase. This protein participates in the modification of a specific His of elongation factor 2 of eukarotes and Archaea to diphthamide. The protein was characterized in Saccharomyces cerevisiae and designated DPH5. [Protein fate, Protein modification and repair]


Pssm-ID: 273117  Cd Length: 257  Bit Score: 294.03  E-value: 2.81e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383413479    1 MLYLIGLGLGDAKDITVKGLEAVRRCSRVYLEAYTSVLTVGK-EALEEFYGRKLILADREEVEQEADNILKDADISDVAF 79
Cdd:TIGR00522   1 MLYLIGLGLYDENDISVKGLEAIKKADEVYAEFYTSKLLGSSiEEIEEFFGKRVVVLERSDVEENSFRLIERAKSKDVAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383413479   80 LVVGDPFGATTHSDLVLRATKLGIPYRVIHNASIMNAV-GCCGLQLYKFGETVSIVFWTDTWRPESFFDKVKKNRQNGMH 158
Cdd:TIGR00522  81 LVAGDPMVATTHTDLKLEAKRKGIETRIIHGASISSAVcGLTGLQLYKFGKTATIVFFTDNYRPQTPYNVIKENRKIGLH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383413479  159 TLCLLDIKVKEqslenlikgrkiyepPRYMSVNQAAQQLLEiIQNQRirgEEPAITEETLCVGLARVGADDQKIAAGTLQ 238
Cdd:TIGR00522 161 TLVLLDIHPKE---------------NRAMTIGEGLENLLE-EEEKR---KTGAITPDTYAVVIARAGSGKPVVKCDKIE 221
                         250       260       270
                  ....*....|....*....|....*....|...
gi 383413479  239 QMCTVDLGEPLHSLIITGGSIHPIEMEMLNLFS 271
Cdd:TIGR00522 222 NLKNYDFGEPLHCLVVLAKTLHFMEFEYLREFA 254
TP_methylase pfam00590
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ...
1-240 1.31e-25

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: 100.49  E-value: 1.31e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383413479    1 MLYLIGLGLGDAKDITVKGLEAVRRCSRVYLE---AYTSVLTVGKEALeeFYGRKLILADREEVEQEADNILKDA--DIS 75
Cdd:pfam00590   1 KLYLVGVGPGDPDLLTLRALRALKEADVVLGDdsrALEILLDLLPEDL--YFPMTEDKEPLEEAYEEIAEALAAAlrAGK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383413479   76 DVAFLVVGDPFGATTHSDLVLRATKLGIPYRVIHNASIMNAVGCC-GLQLYKFGETVSIVFWTDT-WRPESFFDKVKKNR 153
Cdd:pfam00590  79 DVARLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARlGIPLTEGGEVLSVLFLPGLaRIELRLLEALLANG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383413479  154 qngmHTLCLLDIKVKeqslenlikgrkiyepprymsVNQAAQQLLEiiqnqrirgeepAITEETLCVGLARVGADDQKIA 233
Cdd:pfam00590 159 ----DTVVLLYGPRR---------------------LAELAELLLE------------LYPDTTPVAVVERAGTPDEKVV 201

                  ....*..
gi 383413479  234 AGTLQQM 240
Cdd:pfam00590 202 RGTLGEL 208
 
Name Accession Description Interval E-value
PTZ00175 PTZ00175
diphthine synthase; Provisional
1-272 1.45e-164

diphthine synthase; Provisional


Pssm-ID: 185500  Cd Length: 270  Bit Score: 457.11  E-value: 1.45e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383413479   1 MLYLIGLGLGDAKDITVKGLEAVRRCSRVYLEAYTSVL-TVGKEALEEFYGRKLILADREEVEQEADNILKDADISDVAF 79
Cdd:PTZ00175   2 MLYIIGLGLGDEKDITVKGLEAVKSADVVYLESYTSILiNSNKEKLEEFYGKPVIEADREMVEEGCDEILEEAKEKNVAF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383413479  80 LVVGDPFGATTHSDLVLRATKLGIPYRVIHNASIMNAVGCCGLQLYKFGETVSIVFWTDTWRPESFFDKVKKNRQNGMHT 159
Cdd:PTZ00175  82 LVVGDPFCATTHTDLYLRAKKKGIEVEVIHNASIMNAIGCTGLQLYRFGETVSIPFFTETWKPDSFYDKIKANRDNGLHT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383413479 160 LCLLDIKVKEQSLENLIKGRKIYEPPRYMSVNQAAQQLLEIIQNQRirgeEPAITEETLCVGLARVGADDQKIAAGTLQQ 239
Cdd:PTZ00175 162 LCLLDIKVKERSVENLMKGRKIYEPPRYMTINQAIEQLLEVEEKKG----GGVIAEDTLVVGVARVGSDDQQIVSGTLED 237
                        250       260       270
                 ....*....|....*....|....*....|...
gi 383413479 240 MCTVDLGEPLHSLIITGGSIHPIEMEMLNLFSI 272
Cdd:PTZ00175 238 LLDVDFGPPLHSLVICAPTLHDIEEEFFELYRI 270
DHP5_DphB cd11647
diphthine methyl ester synthase and diphthine synthase; Eukaryotic diphthine methyl ester ...
1-256 2.01e-138

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: 389.85  E-value: 2.01e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383413479   1 MLYLIGLGLGDAKDITVKGLEAVRRCSRVYLEAYTSVLTVGK-EALEEFYGRKLILADREEVEQEADNILKDADISDVAF 79
Cdd:cd11647    1 MLYLIGLGLGDEKDITLEGLEALKKADKVYLEAYTSILPGSKlEELEKLIGKKIILLDREDLEEESEEILEEAKKKDVAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383413479  80 LVVGDPFGATTHSDLVLRATKLGIPYRVIHNASIMNAVGCC-GLQLYKFGETVSIVFWTDTWRPESFFDKVKKNRQNGMH 158
Cdd:cd11647   81 LVPGDPLIATTHIDLRLEAKKRGIKVKVIHNASILSAAGSTsGLQLYKFGRTVTIPFPEENYKPESPYDVIKENLKRGLH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383413479 159 TLCLLDIKVkeqslenlikgrkiyEPPRYMSVNQAAQQLLEIIQNQRirgeEPAITEETLCVGLARVGADDQKIAAGTLQ 238
Cdd:cd11647  161 TLLLLDIKV---------------EEGRFMTINEAIEILLEIEEKRK----EGVITEDTLVVGLARLGSDDQKIVAGTLK 221
                        250
                 ....*....|....*...
gi 383413479 239 QMCTVDLGEPLHSLIITG 256
Cdd:cd11647  222 ELLKEDFGPPPHSLIIPG 239
DPH5 COG1798
Diphthamide biosynthesis methyltransferase [Translation, ribosomal structure and biogenesis];
1-267 8.79e-107

Diphthamide biosynthesis methyltransferase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441403  Cd Length: 255  Bit Score: 310.20  E-value: 8.79e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383413479   1 MLYLIGLGLGDAKDITVKGLEAVRRCSRVYLEAYTSVLT-VGKEALEEFYGRKLILADREEVEQEADNILKDADISDVAF 79
Cdd:COG1798    1 MLTFVGLGLSDERDITLKGLEALRSADKVYAEFYTSRLIgTDLEKLEELIGKEIVVLDREDVEDNPEEILEEAKEKDVVF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383413479  80 LVVGDPFGATTHSDLVLRATKLGIPYRVIHNASIMNAV-GCCGLQLYKFGETVSIVFWTDTWRPESFFDKVKKNRQNGMH 158
Cdd:COG1798   81 LTAGDPMIATTHVDLRLRAKRRGIETRVIHGVSIVSAAiGLTGLQNYKFGKTVTIPFPYEGFVPTSPYDTIKENLERGLH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383413479 159 TLCLLDIKVKEQslenlikgrkiyeppRYMSVNQAAQQLLEIIQNQRirgeEPAITEETLCVGLARVGADDQKIAAGTLQ 238
Cdd:COG1798  161 TLVLLDIKADKN---------------RYMTANEALELLLEIEKKRR----EGVISDDTLAVVVARAGSPDPKIVAGKLS 221
                        250       260
                 ....*....|....*....|....*....
gi 383413479 239 QMCTVDLGEPLHSLIITgGSIHPIEMEML 267
Cdd:COG1798  222 ELANYDFGEPPHSLIIP-GRLHFMEAEAL 249
dph5 TIGR00522
diphthine synthase; Alternate name: diphthamide biosynthesis S-adenosylmethionine-dependent ...
1-271 2.81e-100

diphthine synthase; Alternate name: diphthamide biosynthesis S-adenosylmethionine-dependent methyltransferase. This protein participates in the modification of a specific His of elongation factor 2 of eukarotes and Archaea to diphthamide. The protein was characterized in Saccharomyces cerevisiae and designated DPH5. [Protein fate, Protein modification and repair]


Pssm-ID: 273117  Cd Length: 257  Bit Score: 294.03  E-value: 2.81e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383413479    1 MLYLIGLGLGDAKDITVKGLEAVRRCSRVYLEAYTSVLTVGK-EALEEFYGRKLILADREEVEQEADNILKDADISDVAF 79
Cdd:TIGR00522   1 MLYLIGLGLYDENDISVKGLEAIKKADEVYAEFYTSKLLGSSiEEIEEFFGKRVVVLERSDVEENSFRLIERAKSKDVAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383413479   80 LVVGDPFGATTHSDLVLRATKLGIPYRVIHNASIMNAV-GCCGLQLYKFGETVSIVFWTDTWRPESFFDKVKKNRQNGMH 158
Cdd:TIGR00522  81 LVAGDPMVATTHTDLKLEAKRKGIETRIIHGASISSAVcGLTGLQLYKFGKTATIVFFTDNYRPQTPYNVIKENRKIGLH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383413479  159 TLCLLDIKVKEqslenlikgrkiyepPRYMSVNQAAQQLLEiIQNQRirgEEPAITEETLCVGLARVGADDQKIAAGTLQ 238
Cdd:TIGR00522 161 TLVLLDIHPKE---------------NRAMTIGEGLENLLE-EEEKR---KTGAITPDTYAVVIARAGSGKPVVKCDKIE 221
                         250       260       270
                  ....*....|....*....|....*....|...
gi 383413479  239 QMCTVDLGEPLHSLIITGGSIHPIEMEMLNLFS 271
Cdd:TIGR00522 222 NLKNYDFGEPLHCLVVLAKTLHFMEFEYLREFA 254
TP_methylase pfam00590
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ...
1-240 1.31e-25

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: 100.49  E-value: 1.31e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383413479    1 MLYLIGLGLGDAKDITVKGLEAVRRCSRVYLE---AYTSVLTVGKEALeeFYGRKLILADREEVEQEADNILKDA--DIS 75
Cdd:pfam00590   1 KLYLVGVGPGDPDLLTLRALRALKEADVVLGDdsrALEILLDLLPEDL--YFPMTEDKEPLEEAYEEIAEALAAAlrAGK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383413479   76 DVAFLVVGDPFGATTHSDLVLRATKLGIPYRVIHNASIMNAVGCC-GLQLYKFGETVSIVFWTDT-WRPESFFDKVKKNR 153
Cdd:pfam00590  79 DVARLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARlGIPLTEGGEVLSVLFLPGLaRIELRLLEALLANG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383413479  154 qngmHTLCLLDIKVKeqslenlikgrkiyepprymsVNQAAQQLLEiiqnqrirgeepAITEETLCVGLARVGADDQKIA 233
Cdd:pfam00590 159 ----DTVVLLYGPRR---------------------LAELAELLLE------------LYPDTTPVAVVERAGTPDEKVV 201

                  ....*..
gi 383413479  234 AGTLQQM 240
Cdd:pfam00590 202 RGTLGEL 208
TP_methylase cd09815
S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet ...
5-254 1.08e-22

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: 93.23  E-value: 1.08e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383413479   5 IGLGLGDAKDITVKGLEAVRRCSRVYLEAYTSVLTVGKEALEEFYG-RKLILADREEVEQEADNILKDADIS-DVAFLVV 82
Cdd:cd09815    1 VGVGPGDPDLLTLRALEILRAADVVVAEDKDSKLLSLVLRAILKDGkRIYDLHDPNVEEEMAELLLEEARQGkDVAFLSP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383413479  83 GDPFGATTHSDLVLRATKLGIPYRVIHNASIMNAVGC-CGLQLYKFGETVSIVFWTDTWRpesfFDKVKKNRQNGMHTLC 161
Cdd:cd09815   81 GDPGVAGTGAELVERAEREGVEVKVIPGVSAADAAAAaLGIDLGESFLFVTASDLLENPR----LLVLKALAKERRHLVL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383413479 162 LLDIKVKEQSLENLIkgrKIYEPPrymsvnqaaqqlleiiqnqrirgeepaiteETLCVGLARVGADDQKIAAGTLQQMC 241
Cdd:cd09815  157 FLDGHRFLKALERLL---KELGED------------------------------DTPVVLVANAGSEGEVIRTGTVKELR 203
                        250
                 ....*....|....*
gi 383413479 242 TV--DLGEPLHSLII 254
Cdd:cd09815  204 AErtERGKPLTTILV 218
YabN_N_like cd11723
N-terminal S-AdoMet-dependent tetrapyrrole methylase domain of Bacillus subtilis YabN and ...
2-124 2.90e-08

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: 52.88  E-value: 2.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383413479   2 LYLIGLGLGDAKDITVKGLEAVRRCSRVYL-----EAYTSVLTVGK--EALEEFYGRKlilADREEVEQE-ADNILKDAD 73
Cdd:cd11723    1 ITIVGLGPGDPDLLTLGALEALKSADKVYLrtarhPVVEELKEEGIefESFDDLYEEA---EDFEEVYEAiAERLLEAAE 77
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 383413479  74 ISDVAFLVVGDPFGATTHSDLVLRATKLGIPYRVIHNAS----IMNAVGCC---GLQL 124
Cdd:cd11723   78 HGDVVYAVPGHPLVAERTVQLLLERAEEGIEVEIIPGVSfldaALAALGIDpieGLQI 135
TP_methylase cd11724
uncharacterized family of the tetrapyrrole methylase superfamily; Members of this superfamily ...
2-87 1.37e-07

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: 51.40  E-value: 1.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383413479   2 LYLIGLGLGDAKDITVKGLEAVRR-----CSRVYLEAYTSVLTvGKEALE------EFYGRKLILADREEVEQEADNILK 70
Cdd:cd11724    2 LYLVGVGPGDPDLITLRALKAIKKadvvfAPPDLRKRFAEYLA-GKEVLDdphglfTYYGKKCSPLEEAEKECEELEKQR 80
                         90       100
                 ....*....|....*....|....*....
gi 383413479  71 DADIS----------DVAFLVVGDP--FG 87
Cdd:cd11724   81 AEIVQkirealaqgkNVALLDSGDPtiYG 109
CobF COG2243
Precorrin-2 methylase [Coenzyme transport and metabolism]; Precorrin-2 methylase is part of ...
2-108 3.11e-07

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: 50.10  E-value: 3.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383413479   2 LYLIGLGLGDAKDITVKGLEAVRRCSRV-------------------YLEAYTSV-----LTVGKEALEEFYgrklilad 57
Cdd:COG2243    5 LYGVGVGPGDPELLTLKAVRALREADVIaypakgagkaslareivapYLPPARIVelvfpMTTDYEALVAAW-------- 76
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 383413479  58 reevEQEADNILKDADI-SDVAFLVVGDPF--GATTHsdLVLRATKLGIPYRVI 108
Cdd:COG2243   77 ----DEAAARIAEELEAgRDVAFLTEGDPSlySTFMY--LLERLRERGFEVEVI 124
PRK05576 PRK05576
cobalt-factor II C(20)-methyltransferase;
1-108 7.70e-07

cobalt-factor II C(20)-methyltransferase;


Pssm-ID: 235512 [Multi-domain]  Cd Length: 229  Bit Score: 48.76  E-value: 7.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383413479   1 MLYLIGLGLGDAKDITVKGLEAVRRCSRVYleAYTSVLTVGKEAL---EEFYGRKLIL--------ADREEVEQE----A 65
Cdd:PRK05576   3 KLYGIGLGPGDPELLTVKAARILEEADVVY--APASRKGGGSLALnivRPYLKEETEIvelhfpmsKDEEEKEAVwkenA 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 383413479  66 DNILKDA-DISDVAFLVVGDPFGATTHSDLVLRATKLGIPYRVI 108
Cdd:PRK05576  81 EEIAAEAeEGKNVAFITLGDPNLYSTFSHLLEYLKCHDIEVETV 124
cobI_cbiL TIGR01467
precorrin-2 C(20)-methyltransferase; This model represents precorrin-2 C(20)-methyltransferase, ...
1-117 9.82e-06

precorrin-2 C(20)-methyltransferase; This model represents precorrin-2 C(20)-methyltransferase, one of several closely related S-adenosylmethionine-dependent methyltransferases involved in cobalamin (vitamin B12) biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 273642 [Multi-domain]  Cd Length: 230  Bit Score: 45.76  E-value: 9.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383413479    1 MLYLIGLGLGDAKDITVKGLEAVRRCSRVYLEAytsvltvgKEALEEFYGRKLIL------------------ADREEVE 62
Cdd:TIGR01467   2 KLYGVGVGPGDPELITVKALEALRSADVIAVPA--------SKKGRESLARKIVEdylkpndtrilelvfpmtKDRDELE 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 383413479   63 Q---EADNILKDA--DISDVAFLVVGDPFGATTHSDLVLRATKLGIPYRVIHNASIMNAV 117
Cdd:TIGR01467  74 KawdEAAEAVAAEleEGRDVAFLTLGDPSLYSTFSYLLQRLQGMGIEVEVVPGITSFAAC 133
PRK05787 PRK05787
cobalt-precorrin-7 (C(5))-methyltransferase;
1-85 6.98e-05

cobalt-precorrin-7 (C(5))-methyltransferase;


Pssm-ID: 235609 [Multi-domain]  Cd Length: 210  Bit Score: 42.93  E-value: 6.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383413479   1 MLYLIGLGLGDAKDITVKGLEAVRRCSRVYleaytsvltVGKEALEEFygRKLILADREEV----EQEADNILKDADISD 76
Cdd:PRK05787   1 MIYIVGIGPGDPEYLTLKALEAIRKADVVV---------GSKRVLELF--PELIDGEAFVLtaglRDLLEWLELAAKGKN 69

                 ....*....
gi 383413479  77 VAFLVVGDP 85
Cdd:PRK05787  70 VVVLSTGDP 78
Precorrin_2_C20_MT cd11645
Precorrin-2 C20-methyltransferase, also named CobI or CbiL; Precorrin-2 C20-methyltransferase ...
5-86 7.28e-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: 39.80  E-value: 7.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383413479   5 IGLGLGDAKDITVKGLEAVRRCSRVyleaYTSVLTVGKEALEEFYGRKLILADREEVE-----------------QEADN 67
Cdd:cd11645    1 VGVGPGDPELLTLKAVRILKEADVI----FVPVSKGGEGSAALIIAAALLIPDKEIIPlefpmtkdreeleeawdEAAEE 76
                         90       100
                 ....*....|....*....|
gi 383413479  68 ILKDADIS-DVAFLVVGDPF 86
Cdd:cd11645   77 IAEELKEGkDVAFLTLGDPS 96
Precorrin-6Y-MT cd11644
Precorrin-6Y methyltransferase (also named CbiE); CbiE (precorrin-6Y methyltransferase, also ...
5-86 3.55e-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: 37.86  E-value: 3.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383413479   5 IGLGLGDAKDITVKGLEAVRRCSRVYleAYTSVLtvgkEALEEFYGRKLILAdREEVEQEADNILKDADisDVAFLVVGD 84
Cdd:cd11644    1 IGIGPGGPEYLTPEAREAIEEADVVI--GAKRLL----ELFPDLGAEKIPLP-SEDIAELLEEIAEAGK--RVVVLASGD 71

                 ..
gi 383413479  85 PF 86
Cdd:cd11644   72 PG 73
PLN02625 PLN02625
uroporphyrin-III C-methyltransferase
3-137 7.02e-03

uroporphyrin-III C-methyltransferase


Pssm-ID: 178232 [Multi-domain]  Cd Length: 263  Bit Score: 37.30  E-value: 7.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383413479   3 YLIGLGLGDAKDITVKGLEAVRRCSRVYLE--AYTSVLTVGKEALEEFYGRKliLADREEVEQ-EADNILKD--ADISDV 77
Cdd:PLN02625  18 FLVGTGPGDPDLLTLKALRLLQTADVVLYDrlVSPDILDLVPPGAELLYVGK--RGGYHSRTQeEIHELLLSfaEAGKTV 95
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 383413479  78 AFLVVGDP--FGATTHSDLVLRatKLGIPYRVIhnASIMNAVGCC---GLQLYKFGETVSIVFWT 137
Cdd:PLN02625  96 VRLKGGDPlvFGRGGEEMDALR--KNGIPVTVV--PGITAAIGAPaelGIPLTHRGVATSVRFLT 156
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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