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Conserved domains on  [gi|146095033|ref|XP_001467458|]
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diphthine synthase-like protein [Leishmania infantum JPCM5]

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

CATH:  3.30.950.10|3.40.1010.10
EC:  2.1.1.314
Gene Ontology:  GO:0004164|GO:0017183|GO:0141133|GO:0032259|GO:0017183|GO:1904047
SCOP:  4000056

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTZ00175 PTZ00175
diphthine synthase; Provisional
 1-268 8.67e-169

diphthine synthase; Provisional


:

Pssm-ID: 185500  Cd Length: 270  Bit Score: 467.13  E-value: 8.67e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146095033   1 MFTLVGVGLGDASDVTVKGMNAVKEADVVFLEAYTSFLINSNAEELAGIYGKPVILADREMVESGA--VLDDAKVKKVVL 78
Cdd:PTZ00175   2 MLYIIGLGLGDEKDITVKGLEAVKSADVVYLESYTSILINSNKEKLEEFYGKPVIEADREMVEEGCdeILEEAKEKNVAF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146095033  79 LVVGDVFGATTHSDLIVRCNRQGIESKVVHNASIINAVGCCGLQLYRFGQVISLCFWTETWRPDSWYERLRSNRAAGIHT 158
Cdd:PTZ00175  82 LVVGDPFCATTHTDLYLRAKKKGIEVEVIHNASIMNAIGCTGLQLYRFGETVSIPFFTETWKPDSFYDKIKANRDNGLHT 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146095033 159 LVLLDIKVKEISDENLARGRKIYEPPRYMTIRQAVEQILEVEGYKQGGAVAADgsTFAVGLARVGSESQQVVAGTMKDLL 238
Cdd:PTZ00175 162 LCLLDIKVKERSVENLMKGRKIYEPPRYMTINQAIEQLLEVEEKKGGGVIAED--TLVVGVARVGSDDQQIVSGTLEDLL 239

                        250       260       270
                 ....*....|....*....|....*....|.
gi 146095033 239 SVDFGAPLHSLVIAGD-VHDCEQEHVDLFRM 268
Cdd:PTZ00175 240 DVDFGPPLHSLVICAPtLHDIEEEFFELYRI 270
 
Name Accession Description Interval E-value
PTZ00175 PTZ00175
diphthine synthase; Provisional
 1-268 8.67e-169

diphthine synthase; Provisional


Pssm-ID: 185500  Cd Length: 270  Bit Score: 467.13  E-value: 8.67e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146095033   1 MFTLVGVGLGDASDVTVKGMNAVKEADVVFLEAYTSFLINSNAEELAGIYGKPVILADREMVESGA--VLDDAKVKKVVL 78
Cdd:PTZ00175   2 MLYIIGLGLGDEKDITVKGLEAVKSADVVYLESYTSILINSNKEKLEEFYGKPVIEADREMVEEGCdeILEEAKEKNVAF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146095033  79 LVVGDVFGATTHSDLIVRCNRQGIESKVVHNASIINAVGCCGLQLYRFGQVISLCFWTETWRPDSWYERLRSNRAAGIHT 158
Cdd:PTZ00175  82 LVVGDPFCATTHTDLYLRAKKKGIEVEVIHNASIMNAIGCTGLQLYRFGETVSIPFFTETWKPDSFYDKIKANRDNGLHT 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146095033 159 LVLLDIKVKEISDENLARGRKIYEPPRYMTIRQAVEQILEVEGYKQGGAVAADgsTFAVGLARVGSESQQVVAGTMKDLL 238
Cdd:PTZ00175 162 LCLLDIKVKERSVENLMKGRKIYEPPRYMTINQAIEQLLEVEEKKGGGVIAED--TLVVGVARVGSDDQQIVSGTLEDLL 239

                        250       260       270
                 ....*....|....*....|....*....|.
gi 146095033 239 SVDFGAPLHSLVIAGD-VHDCEQEHVDLFRM 268
Cdd:PTZ00175 240 DVDFGPPLHSLVICAPtLHDIEEEFFELYRI 270
DHP5_DphB cd11647
diphthine methyl ester synthase and diphthine synthase; Eukaryotic diphthine methyl ester ...
 1-254 4.47e-112

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: 322.44  E-value: 4.47e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146095033   1 MFTLVGVGLGDASDVTVKGMNAVKEADVVFLEAYTSFLINSNAEELAGIYGKPVILADREMVE--SGAVLDDAKVKKVVL 78
Cdd:cd11647    1 MLYLIGLGLGDEKDITLEGLEALKKADKVYLEAYTSILPGSKLEELEKLIGKKIILLDREDLEeeSEEILEEAKKKDVAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146095033  79 LVVGDVFGATTHSDLIVRCNRQGIESKVVHNASIINAVGCC-GLQLYRFGQVISLCFWTETWRPDSWYERLRSNRAAGIH 157
Cdd:cd11647   81 LVPGDPLIATTHIDLRLEAKKRGIKVKVIHNASILSAAGSTsGLQLYKFGRTVTIPFPEENYKPESPYDVIKENLKRGLH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146095033 158 TLVLLDIKVkeisdenlargrkiyEPPRYMTIRQAVEQILEVEGYKQGGAVAADgsTFAVGLARVGSESQQVVAGTMKDL 237
Cdd:cd11647  161 TLLLLDIKV---------------EEGRFMTINEAIEILLEIEEKRKEGVITED--TLVVGLARLGSDDQKIVAGTLKEL 223

                        250
                 ....*....|....*..
gi 146095033 238 LSVDFGAPLHSLVIAGD 254
Cdd:cd11647  224 LKEDFGPPPHSLIIPGK 240
DPH5 COG1798
Diphthamide biosynthesis methyltransferase [Translation, ribosomal structure and biogenesis];
1-261 1.26e-91

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


Pssm-ID: 441403  Cd Length: 255  Bit Score: 271.29  E-value: 1.26e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146095033   1 MFTLVGVGLGDASDVTVKGMNAVKEADVVFLEAYTSFLINSNAEELAGIYGKPVILADREMVESGA--VLDDAKVKKVVL 78
Cdd:COG1798    1 MLTFVGLGLSDERDITLKGLEALRSADKVYAEFYTSRLIGTDLEKLEELIGKEIVVLDREDVEDNPeeILEEAKEKDVVF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146095033  79 LVVGDVFGATTHSDLIVRCNRQGIESKVVHNASIINAV-GCCGLQLYRFGQVISLCFWTETWRPDSWYERLRSNRAAGIH 157
Cdd:COG1798   81 LTAGDPMIATTHVDLRLRAKRRGIETRVIHGVSIVSAAiGLTGLQNYKFGKTVTIPFPYEGFVPTSPYDTIKENLERGLH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146095033 158 TLVLLDIKVkeisDENlargrkiyeppRYMTIRQAVEQILEVEGYKQGGAVAADgsTFAVGLARVGSESQQVVAGTMKDL 237
Cdd:COG1798  161 TLVLLDIKA----DKN-----------RYMTANEALELLLEIEKKRREGVISDD--TLAVVVARAGSPDPKIVAGKLSEL 223

                        250       260
                 ....*....|....*....|....
gi 146095033 238 LSVDFGAPLHSLVIAGDVHDCEQE 261
Cdd:COG1798  224 ANYDFGEPPHSLIIPGRLHFMEAE 247
dph5 TIGR00522
diphthine synthase; Alternate name: diphthamide biosynthesis S-adenosylmethionine-dependent ...
 1-261 5.92e-84

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: 252.04  E-value: 5.92e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146095033    1 MFTLVGVGLGDASDVTVKGMNAVKEADVVFLEAYTSFLINSNAEELAGIYGKPVILADREMVESGA--VLDDAKVKKVVL 78
Cdd:TIGR00522   1 MLYLIGLGLYDENDISVKGLEAIKKADEVYAEFYTSKLLGSSIEEIEEFFGKRVVVLERSDVEENSfrLIERAKSKDVAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146095033   79 LVVGDVFGATTHSDLIVRCNRQGIESKVVHNASIINAV-GCCGLQLYRFGQVISLCFWTETWRPDSWYERLRSNRAAGIH 157
Cdd:TIGR00522  81 LVAGDPMVATTHTDLKLEAKRKGIETRIIHGASISSAVcGLTGLQLYKFGKTATIVFFTDNYRPQTPYNVIKENRKIGLH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146095033  158 TLVLLDIKVKEisdenlargrkiyepPRYMTIRQAVEQILEVEGYKQGGAVAADgsTFAVGLARVGSESQQVVAGTMKDL 237
Cdd:TIGR00522 161 TLVLLDIHPKE---------------NRAMTIGEGLENLLEEEEKRKTGAITPD--TYAVVIARAGSGKPVVKCDKIENL 223

                         250       260
                  ....*....|....*....|....*
gi 146095033  238 LSVDFGAPLHSLVIAG-DVHDCEQE 261
Cdd:TIGR00522 224 KNYDFGEPLHCLVVLAkTLHFMEFE 248
TP_methylase pfam00590
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ...
 1-237 4.19e-14

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: 69.29  E-value: 4.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146095033    1 MFTLVGVGLGDASDVTVKGMNAVKEADVVFLEA--YTSFLINSNAEELAGIYGKPVILADREMVESGAVLDDAKVKKVV- 77
Cdd:pfam00590   1 KLYLVGVGPGDPDLLTLRALRALKEADVVLGDDsrALEILLDLLPEDLYFPMTEDKEPLEEAYEEIAEALAAALRAGKDv 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146095033   78 -LLVVGDVFGATTHSDLIVRCNRQGIESKVVHNASIINAVGCC-GLQLYRFGQVISLCFWTET-WRPDSWYERLRSNRaa 154
Cdd:pfam00590  81 aRLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARlGIPLTEGGEVLSVLFLPGLaRIELRLLEALLANG-- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146095033  155 giHTLVLLDIKVKeisdenlargrkiyepprymtIRQAVEQILEvegykqggavaADGSTFAVGL-ARVGSESQQVVAGT 233
Cdd:pfam00590 159 --DTVVLLYGPRR---------------------LAELAELLLE-----------LYPDTTPVAVvERAGTPDEKVVRGT 204


                  ....
gi 146095033  234 MKDL 237
Cdd:pfam00590 205 LGEL 208
 
Name Accession Description Interval E-value
PTZ00175 PTZ00175
diphthine synthase; Provisional
 1-268 8.67e-169

diphthine synthase; Provisional


Pssm-ID: 185500  Cd Length: 270  Bit Score: 467.13  E-value: 8.67e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146095033   1 MFTLVGVGLGDASDVTVKGMNAVKEADVVFLEAYTSFLINSNAEELAGIYGKPVILADREMVESGA--VLDDAKVKKVVL 78
Cdd:PTZ00175   2 MLYIIGLGLGDEKDITVKGLEAVKSADVVYLESYTSILINSNKEKLEEFYGKPVIEADREMVEEGCdeILEEAKEKNVAF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146095033  79 LVVGDVFGATTHSDLIVRCNRQGIESKVVHNASIINAVGCCGLQLYRFGQVISLCFWTETWRPDSWYERLRSNRAAGIHT 158
Cdd:PTZ00175  82 LVVGDPFCATTHTDLYLRAKKKGIEVEVIHNASIMNAIGCTGLQLYRFGETVSIPFFTETWKPDSFYDKIKANRDNGLHT 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146095033 159 LVLLDIKVKEISDENLARGRKIYEPPRYMTIRQAVEQILEVEGYKQGGAVAADgsTFAVGLARVGSESQQVVAGTMKDLL 238
Cdd:PTZ00175 162 LCLLDIKVKERSVENLMKGRKIYEPPRYMTINQAIEQLLEVEEKKGGGVIAED--TLVVGVARVGSDDQQIVSGTLEDLL 239

                        250       260       270
                 ....*....|....*....|....*....|.
gi 146095033 239 SVDFGAPLHSLVIAGD-VHDCEQEHVDLFRM 268
Cdd:PTZ00175 240 DVDFGPPLHSLVICAPtLHDIEEEFFELYRI 270
DHP5_DphB cd11647
diphthine methyl ester synthase and diphthine synthase; Eukaryotic diphthine methyl ester ...
 1-254 4.47e-112

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: 322.44  E-value: 4.47e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146095033   1 MFTLVGVGLGDASDVTVKGMNAVKEADVVFLEAYTSFLINSNAEELAGIYGKPVILADREMVE--SGAVLDDAKVKKVVL 78
Cdd:cd11647    1 MLYLIGLGLGDEKDITLEGLEALKKADKVYLEAYTSILPGSKLEELEKLIGKKIILLDREDLEeeSEEILEEAKKKDVAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146095033  79 LVVGDVFGATTHSDLIVRCNRQGIESKVVHNASIINAVGCC-GLQLYRFGQVISLCFWTETWRPDSWYERLRSNRAAGIH 157
Cdd:cd11647   81 LVPGDPLIATTHIDLRLEAKKRGIKVKVIHNASILSAAGSTsGLQLYKFGRTVTIPFPEENYKPESPYDVIKENLKRGLH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146095033 158 TLVLLDIKVkeisdenlargrkiyEPPRYMTIRQAVEQILEVEGYKQGGAVAADgsTFAVGLARVGSESQQVVAGTMKDL 237
Cdd:cd11647  161 TLLLLDIKV---------------EEGRFMTINEAIEILLEIEEKRKEGVITED--TLVVGLARLGSDDQKIVAGTLKEL 223

                        250
                 ....*....|....*..
gi 146095033 238 LSVDFGAPLHSLVIAGD 254
Cdd:cd11647  224 LKEDFGPPPHSLIIPGK 240
DPH5 COG1798
Diphthamide biosynthesis methyltransferase [Translation, ribosomal structure and biogenesis];
1-261 1.26e-91

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


Pssm-ID: 441403  Cd Length: 255  Bit Score: 271.29  E-value: 1.26e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146095033   1 MFTLVGVGLGDASDVTVKGMNAVKEADVVFLEAYTSFLINSNAEELAGIYGKPVILADREMVESGA--VLDDAKVKKVVL 78
Cdd:COG1798    1 MLTFVGLGLSDERDITLKGLEALRSADKVYAEFYTSRLIGTDLEKLEELIGKEIVVLDREDVEDNPeeILEEAKEKDVVF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146095033  79 LVVGDVFGATTHSDLIVRCNRQGIESKVVHNASIINAV-GCCGLQLYRFGQVISLCFWTETWRPDSWYERLRSNRAAGIH 157
Cdd:COG1798   81 LTAGDPMIATTHVDLRLRAKRRGIETRVIHGVSIVSAAiGLTGLQNYKFGKTVTIPFPYEGFVPTSPYDTIKENLERGLH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146095033 158 TLVLLDIKVkeisDENlargrkiyeppRYMTIRQAVEQILEVEGYKQGGAVAADgsTFAVGLARVGSESQQVVAGTMKDL 237
Cdd:COG1798  161 TLVLLDIKA----DKN-----------RYMTANEALELLLEIEKKRREGVISDD--TLAVVVARAGSPDPKIVAGKLSEL 223

                        250       260
                 ....*....|....*....|....
gi 146095033 238 LSVDFGAPLHSLVIAGDVHDCEQE 261
Cdd:COG1798  224 ANYDFGEPPHSLIIPGRLHFMEAE 247
dph5 TIGR00522
diphthine synthase; Alternate name: diphthamide biosynthesis S-adenosylmethionine-dependent ...
 1-261 5.92e-84

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: 252.04  E-value: 5.92e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146095033    1 MFTLVGVGLGDASDVTVKGMNAVKEADVVFLEAYTSFLINSNAEELAGIYGKPVILADREMVESGA--VLDDAKVKKVVL 78
Cdd:TIGR00522   1 MLYLIGLGLYDENDISVKGLEAIKKADEVYAEFYTSKLLGSSIEEIEEFFGKRVVVLERSDVEENSfrLIERAKSKDVAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146095033   79 LVVGDVFGATTHSDLIVRCNRQGIESKVVHNASIINAV-GCCGLQLYRFGQVISLCFWTETWRPDSWYERLRSNRAAGIH 157
Cdd:TIGR00522  81 LVAGDPMVATTHTDLKLEAKRKGIETRIIHGASISSAVcGLTGLQLYKFGKTATIVFFTDNYRPQTPYNVIKENRKIGLH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146095033  158 TLVLLDIKVKEisdenlargrkiyepPRYMTIRQAVEQILEVEGYKQGGAVAADgsTFAVGLARVGSESQQVVAGTMKDL 237
Cdd:TIGR00522 161 TLVLLDIHPKE---------------NRAMTIGEGLENLLEEEEKRKTGAITPD--TYAVVIARAGSGKPVVKCDKIENL 223

                         250       260
                  ....*....|....*....|....*
gi 146095033  238 LSVDFGAPLHSLVIAG-DVHDCEQE 261
Cdd:TIGR00522 224 KNYDFGEPLHCLVVLAkTLHFMEFE 248
TP_methylase cd09815
S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet ...
 5-251 2.94e-17

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: 78.20  E-value: 2.94e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146095033   5 VGVGLGDASDVTVKGMNAVKEADVVFLEAYTSFLINSNAEELAGIyGKPVI-LADREMVESGA--VLDDAKVKKV-VLLV 80
Cdd:cd09815    1 VGVGPGDPDLLTLRALEILRAADVVVAEDKDSKLLSLVLRAILKD-GKRIYdLHDPNVEEEMAelLLEEARQGKDvAFLS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146095033  81 VGDVFGATTHSDLIVRCNRQGIESKVVHNASIINAVGC-CGLQLYRFGQVISLCFWTETWRPDSWyERLRSNRAagiHTL 159
Cdd:cd09815   80 PGDPGVAGTGAELVERAEREGVEVKVIPGVSAADAAAAaLGIDLGESFLFVTASDLLENPRLLVL-KALAKERR---HLV 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146095033 160 VLLDIKvkeisdenlargrkiyepprymTIRQAVEQILEVEGYKQggavaadgsTFAVGLARVGSESQQVVAGTMKDLLS 239
Cdd:cd09815  156 LFLDGH----------------------RFLKALERLLKELGEDD---------TPVVLVANAGSEGEVIRTGTVKELRA 204

                        250
                 ....*....|....
gi 146095033 240 V--DFGAPLHSLVI 251
Cdd:cd09815  205 ErtERGKPLTTILV 218
TP_methylase pfam00590
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ...
 1-237 4.19e-14

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: 69.29  E-value: 4.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146095033    1 MFTLVGVGLGDASDVTVKGMNAVKEADVVFLEA--YTSFLINSNAEELAGIYGKPVILADREMVESGAVLDDAKVKKVV- 77
Cdd:pfam00590   1 KLYLVGVGPGDPDLLTLRALRALKEADVVLGDDsrALEILLDLLPEDLYFPMTEDKEPLEEAYEEIAEALAAALRAGKDv 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146095033   78 -LLVVGDVFGATTHSDLIVRCNRQGIESKVVHNASIINAVGCC-GLQLYRFGQVISLCFWTET-WRPDSWYERLRSNRaa 154
Cdd:pfam00590  81 aRLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARlGIPLTEGGEVLSVLFLPGLaRIELRLLEALLANG-- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146095033  155 giHTLVLLDIKVKeisdenlargrkiyepprymtIRQAVEQILEvegykqggavaADGSTFAVGL-ARVGSESQQVVAGT 233
Cdd:pfam00590 159 --DTVVLLYGPRR---------------------LAELAELLLE-----------LYPDTTPVAVvERAGTPDEKVVRGT 204


                  ....
gi 146095033  234 MKDL 237
Cdd:pfam00590 205 LGEL 208
TP_methylase cd11724
uncharacterized family of the tetrapyrrole methylase superfamily; Members of this superfamily ...
 2-57 1.96e-04

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: 41.77  E-value: 1.96e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 146095033   2 FTLVGVGLGDASDVTVKGMNAVKEADVVFleaYTSFLINSNAEELAgiyGKPVILA 57
Cdd:cd11724    2 LYLVGVGPGDPDLITLRALKAIKKADVVF---APPDLRKRFAEYLA---GKEVLDD 51
Precorrin_2_C20_MT cd11645
Precorrin-2 C20-methyltransferase, also named CobI or CbiL; Precorrin-2 C20-methyltransferase ...
 5-30 1.32e-03

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: 39.03  E-value: 1.32e-03
                         10        20
                 ....*....|....*....|....*.
gi 146095033   5 VGVGLGDASDVTVKGMNAVKEADVVF 30
Cdd:cd11645    1 VGVGPGDPELLTLKAVRILKEADVIF 26
PRK05576 PRK05576
cobalt-factor II C(20)-methyltransferase;
1-30 1.54e-03

cobalt-factor II C(20)-methyltransferase;


Pssm-ID: 235512 [Multi-domain]  Cd Length: 229  Bit Score: 39.13  E-value: 1.54e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 146095033   1 MFTLVGVGLG--DASDVTVKGMNAVKEADVVF 30
Cdd:PRK05576   1 MGKLYGIGLGpgDPELLTVKAARILEEADVVY 32
Precorrin-4_C11-MT cd11641
Precorrin-4 C11-methyltransferase (CbiF/CobM); Precorrin-4 C11-methyltransferase participates ...
 5-40 2.24e-03

Precorrin-4 C11-methyltransferase (CbiF/CobM); Precorrin-4 C11-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. In the aerobic pathway, CobM catalyzes the methylation of precorrin-4 at C-11 to yield precorrin-5. In the anaerobic pathway, CibF catalyzes the methylation of cobalt-precorrin-4 to cobalt-precorrin-5. Both CibF and CobM, which are homologous, are included in this model. There are about 30 enzymes involved in vitamin B12 synthetic pathway. The enzymes involved in the aerobic pathway are prefixed Cob and those of the anaerobic pathway Cbi. Most of the enzymes are shared in both pathways and several of these enzymes are pathway-specific.


Pssm-ID: 381168 [Multi-domain]  Cd Length: 225  Bit Score: 38.53  E-value: 2.24e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 146095033   5 VGVGLGDASDVTVKGMNAVKEADVVFleaYTSFLIN 40
Cdd:cd11641    1 VGAGPGDPELITVKGARLLEEADVVI---YAGSLVP 33
CobF COG2243
Precorrin-2 methylase [Coenzyme transport and metabolism]; Precorrin-2 methylase is part of ...
 2-30 6.82e-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: 6.82e-03
                         10        20
                 ....*....|....*....|....*....
gi 146095033   2 FTLVGVGLGDASDVTVKGMNAVKEADVVF 30
Cdd:COG2243    5 LYGVGVGPGDPELLTLKAVRALREADVIA 33
CysG COG0007
Uroporphyrinogen-III methylase (siroheme synthase) [Coenzyme transport and metabolism]; ...
 3-30 9.21e-03

Uroporphyrinogen-III methylase (siroheme synthase) [Coenzyme transport and metabolism]; Uroporphyrinogen-III methylase (siroheme synthase) is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 439778 [Multi-domain]  Cd Length: 245  Bit Score: 36.59  E-value: 9.21e-03
                         10        20
                 ....*....|....*....|....*...
gi 146095033   3 TLVGVGLGDASDVTVKGMNAVKEADVVF 30
Cdd:COG0007    5 YLVGAGPGDPDLLTLKALRALQQADVVL 32
 
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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