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Conserved domains on  [gi|389631497|ref|XP_003713401|]
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diphthine synthase [Pyricularia oryzae 70-15]

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
 1-274 4.47e-143

diphthine synthase; Provisional


:

Pssm-ID: 185500  Cd Length: 270  Bit Score: 403.19  E-value: 4.47e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631497   1 MLYLIGLGLSDETDITVKGLEIVKTAARVYLEAYTSILL-VDQKVLESYYGRSIEVADREMVESNSDEILRNAATEDVAF 79
Cdd:PTZ00175   2 MLYIIGLGLGDEKDITVKGLEAVKSADVVYLESYTSILInSNKEKLEEFYGKPVIEADREMVEEGCDEILEEAKEKNVAF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631497  80 LVVGDPFGATTHTDLVIRARQLQIPIRTIPNASIMSAIGACGLQLYNFGQTVSMVFFTENWRPSSFYDRVAENRALGLHT 159
Cdd:PTZ00175  82 LVVGDPFCATTHTDLYLRAKKKGIEVEVIHNASIMNAIGCTGLQLYRFGETVSIPFFTETWKPDSFYDKIKANRDNGLHT 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631497 160 LVLLDIKVKEPNFESLARGKLVYEPPRFMTVGTCARQMLEVEEEKvkdgaEGGVCGGEALAIGAARVGGKTEKFVAGTLR 239
Cdd:PTZ00175 162 LCLLDIKVKERSVENLMKGRKIYEPPRYMTINQAIEQLLEVEEKK-----GGGVIAEDTLVVGVARVGSDDQQIVSGTLE 236

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 389631497 240 ELadgADELLGAPLHSLVLLGKKTHELEHDFVREF 274
Cdd:PTZ00175 237 DL---LDVDFGPPLHSLVICAPTLHDIEEEFFELY 268
 
Name Accession Description Interval E-value
PTZ00175 PTZ00175
diphthine synthase; Provisional
 1-274 4.47e-143

diphthine synthase; Provisional


Pssm-ID: 185500  Cd Length: 270  Bit Score: 403.19  E-value: 4.47e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631497   1 MLYLIGLGLSDETDITVKGLEIVKTAARVYLEAYTSILL-VDQKVLESYYGRSIEVADREMVESNSDEILRNAATEDVAF 79
Cdd:PTZ00175   2 MLYIIGLGLGDEKDITVKGLEAVKSADVVYLESYTSILInSNKEKLEEFYGKPVIEADREMVEEGCDEILEEAKEKNVAF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631497  80 LVVGDPFGATTHTDLVIRARQLQIPIRTIPNASIMSAIGACGLQLYNFGQTVSMVFFTENWRPSSFYDRVAENRALGLHT 159
Cdd:PTZ00175  82 LVVGDPFCATTHTDLYLRAKKKGIEVEVIHNASIMNAIGCTGLQLYRFGETVSIPFFTETWKPDSFYDKIKANRDNGLHT 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631497 160 LVLLDIKVKEPNFESLARGKLVYEPPRFMTVGTCARQMLEVEEEKvkdgaEGGVCGGEALAIGAARVGGKTEKFVAGTLR 239
Cdd:PTZ00175 162 LCLLDIKVKERSVENLMKGRKIYEPPRYMTINQAIEQLLEVEEKK-----GGGVIAEDTLVVGVARVGSDDQQIVSGTLE 236

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 389631497 240 ELadgADELLGAPLHSLVLLGKKTHELEHDFVREF 274
Cdd:PTZ00175 237 DL---LDVDFGPPLHSLVICAPTLHDIEEEFFELY 268
DHP5_DphB cd11647
diphthine methyl ester synthase and diphthine synthase; Eukaryotic diphthine methyl ester ...
 1-261 2.51e-121

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: 347.10  E-value: 2.51e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631497   1 MLYLIGLGLSDETDITVKGLEIVKTAARVYLEAYTSILLVDQ-KVLESYYGRSIEVADREMVESNSDEILRNAATEDVAF 79
Cdd:cd11647    1 MLYLIGLGLGDEKDITLEGLEALKKADKVYLEAYTSILPGSKlEELEKLIGKKIILLDREDLEEESEEILEEAKKKDVAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631497  80 LVVGDPFGATTHTDLVIRARQLQIPIRTIPNASIMSAIGAC-GLQLYNFGQTVSMVFFTENWRPSSFYDRVAENRALGLH 158
Cdd:cd11647   81 LVPGDPLIATTHIDLRLEAKKRGIKVKVIHNASILSAAGSTsGLQLYKFGRTVTIPFPEENYKPESPYDVIKENLKRGLH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631497 159 TLVLLDIKVkepnfeslargklvyEPPRFMTVGTCARQMLEVEEEKvkdgaEGGVCGGEALAIGAARVGGKTEKFVAGTL 238
Cdd:cd11647  161 TLLLLDIKV---------------EEGRFMTINEAIEILLEIEEKR-----KEGVITEDTLVVGLARLGSDDQKIVAGTL 220

                        250       260
                 ....*....|....*....|...
gi 389631497 239 RELadgADELLGAPLHSLVLLGK 261
Cdd:cd11647  221 KEL---LKEDFGPPPHSLIIPGK 240
dph5 TIGR00522
diphthine synthase; Alternate name: diphthamide biosynthesis S-adenosylmethionine-dependent ...
 1-275 1.65e-98

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: 289.79  E-value: 1.65e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631497    1 MLYLIGLGLSDETDITVKGLEIVKTAARVYLEAYTSILL-VDQKVLESYYGRSIEVADREMVESNSDEILRNAATEDVAF 79
Cdd:TIGR00522   1 MLYLIGLGLYDENDISVKGLEAIKKADEVYAEFYTSKLLgSSIEEIEEFFGKRVVVLERSDVEENSFRLIERAKSKDVAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631497   80 LVVGDPFGATTHTDLVIRARQLQIPIRTIPNASIMSAI-GACGLQLYNFGQTVSMVFFTENWRPSSFYDRVAENRALGLH 158
Cdd:TIGR00522  81 LVAGDPMVATTHTDLKLEAKRKGIETRIIHGASISSAVcGLTGLQLYKFGKTATIVFFTDNYRPQTPYNVIKENRKIGLH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631497  159 TLVLLDIKVKEpnfeslargklvyepPRFMTVGTCARQMLEvEEEKVKDGAeggvCGGEALAIGAARVGGKTEKFVAGTL 238
Cdd:TIGR00522 161 TLVLLDIHPKE---------------NRAMTIGEGLENLLE-EEEKRKTGA----ITPDTYAVVIARAGSGKPVVKCDKI 220

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 389631497  239 RELadgADELLGAPLHSLVLLGKKTHELEHDFVREFA 275
Cdd:TIGR00522 221 ENL---KNYDFGEPLHCLVVLAKTLHFMEFEYLREFA 254
DPH5 COG1798
Diphthamide biosynthesis methyltransferase [Translation, ribosomal structure and biogenesis];
1-275 2.51e-98

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


Pssm-ID: 441403  Cd Length: 255  Bit Score: 289.01  E-value: 2.51e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631497   1 MLYLIGLGLSDETDITVKGLEIVKTAARVYLEAYTSILL-VDQKVLESYYGRSIEVADREMVESNSDEILRNAATEDVAF 79
Cdd:COG1798    1 MLTFVGLGLSDERDITLKGLEALRSADKVYAEFYTSRLIgTDLEKLEELIGKEIVVLDREDVEDNPEEILEEAKEKDVVF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631497  80 LVVGDPFGATTHTDLVIRARQLQIPIRTIPNASIMSAI-GACGLQLYNFGQTVSMVFFTENWRPSSFYDRVAENRALGLH 158
Cdd:COG1798   81 LTAGDPMIATTHVDLRLRAKRRGIETRVIHGVSIVSAAiGLTGLQNYKFGKTVTIPFPYEGFVPTSPYDTIKENLERGLH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631497 159 TLVLLDIKVkepnfeslargklvyEPPRFMTVGTCARQMLEVEEEKVKdgaegGVCGGEALAIGAARVGGKTEKFVAGTL 238
Cdd:COG1798  161 TLVLLDIKA---------------DKNRYMTANEALELLLEIEKKRRE-----GVISDDTLAVVVARAGSPDPKIVAGKL 220

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 389631497 239 RELADgADelLGAPLHSLVLLGkKTHELEHDFVREFA 275
Cdd:COG1798  221 SELAN-YD--FGEPPHSLIIPG-RLHFMEAEALKALA 253
TP_methylase pfam00590
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ...
 1-177 1.97e-19

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: 84.32  E-value: 1.97e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631497    1 MLYLIGLGLSDETDITVKGLEIVKTAARVYLE---AYTSILLVDQKVLESYYGRSIEVADREMVESNSDEILRNAATEDV 77
Cdd:pfam00590   1 KLYLVGVGPGDPDLLTLRALRALKEADVVLGDdsrALEILLDLLPEDLYFPMTEDKEPLEEAYEEIAEALAAALRAGKDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631497   78 AFLVVGDPFGATTHTDLVIRARQLQIPIRTIPNASIMSAIGACGLQLYNFGQTVSMVFFTENWRPSSfyDRVAENRALGL 157
Cdd:pfam00590  81 ARLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARLGIPLTEGGEVLSVLFLPGLARIE--LRLLEALLANG 158

                         170       180
                  ....*....|....*....|
gi 389631497  158 HTLVLLDIKvkePNFESLAR 177
Cdd:pfam00590 159 DTVVLLYGP---RRLAELAE 175
 
Name Accession Description Interval E-value
PTZ00175 PTZ00175
diphthine synthase; Provisional
 1-274 4.47e-143

diphthine synthase; Provisional


Pssm-ID: 185500  Cd Length: 270  Bit Score: 403.19  E-value: 4.47e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631497   1 MLYLIGLGLSDETDITVKGLEIVKTAARVYLEAYTSILL-VDQKVLESYYGRSIEVADREMVESNSDEILRNAATEDVAF 79
Cdd:PTZ00175   2 MLYIIGLGLGDEKDITVKGLEAVKSADVVYLESYTSILInSNKEKLEEFYGKPVIEADREMVEEGCDEILEEAKEKNVAF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631497  80 LVVGDPFGATTHTDLVIRARQLQIPIRTIPNASIMSAIGACGLQLYNFGQTVSMVFFTENWRPSSFYDRVAENRALGLHT 159
Cdd:PTZ00175  82 LVVGDPFCATTHTDLYLRAKKKGIEVEVIHNASIMNAIGCTGLQLYRFGETVSIPFFTETWKPDSFYDKIKANRDNGLHT 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631497 160 LVLLDIKVKEPNFESLARGKLVYEPPRFMTVGTCARQMLEVEEEKvkdgaEGGVCGGEALAIGAARVGGKTEKFVAGTLR 239
Cdd:PTZ00175 162 LCLLDIKVKERSVENLMKGRKIYEPPRYMTINQAIEQLLEVEEKK-----GGGVIAEDTLVVGVARVGSDDQQIVSGTLE 236

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 389631497 240 ELadgADELLGAPLHSLVLLGKKTHELEHDFVREF 274
Cdd:PTZ00175 237 DL---LDVDFGPPLHSLVICAPTLHDIEEEFFELY 268
DHP5_DphB cd11647
diphthine methyl ester synthase and diphthine synthase; Eukaryotic diphthine methyl ester ...
 1-261 2.51e-121

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: 347.10  E-value: 2.51e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631497   1 MLYLIGLGLSDETDITVKGLEIVKTAARVYLEAYTSILLVDQ-KVLESYYGRSIEVADREMVESNSDEILRNAATEDVAF 79
Cdd:cd11647    1 MLYLIGLGLGDEKDITLEGLEALKKADKVYLEAYTSILPGSKlEELEKLIGKKIILLDREDLEEESEEILEEAKKKDVAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631497  80 LVVGDPFGATTHTDLVIRARQLQIPIRTIPNASIMSAIGAC-GLQLYNFGQTVSMVFFTENWRPSSFYDRVAENRALGLH 158
Cdd:cd11647   81 LVPGDPLIATTHIDLRLEAKKRGIKVKVIHNASILSAAGSTsGLQLYKFGRTVTIPFPEENYKPESPYDVIKENLKRGLH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631497 159 TLVLLDIKVkepnfeslargklvyEPPRFMTVGTCARQMLEVEEEKvkdgaEGGVCGGEALAIGAARVGGKTEKFVAGTL 238
Cdd:cd11647  161 TLLLLDIKV---------------EEGRFMTINEAIEILLEIEEKR-----KEGVITEDTLVVGLARLGSDDQKIVAGTL 220

                        250       260
                 ....*....|....*....|...
gi 389631497 239 RELadgADELLGAPLHSLVLLGK 261
Cdd:cd11647  221 KEL---LKEDFGPPPHSLIIPGK 240
dph5 TIGR00522
diphthine synthase; Alternate name: diphthamide biosynthesis S-adenosylmethionine-dependent ...
 1-275 1.65e-98

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: 289.79  E-value: 1.65e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631497    1 MLYLIGLGLSDETDITVKGLEIVKTAARVYLEAYTSILL-VDQKVLESYYGRSIEVADREMVESNSDEILRNAATEDVAF 79
Cdd:TIGR00522   1 MLYLIGLGLYDENDISVKGLEAIKKADEVYAEFYTSKLLgSSIEEIEEFFGKRVVVLERSDVEENSFRLIERAKSKDVAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631497   80 LVVGDPFGATTHTDLVIRARQLQIPIRTIPNASIMSAI-GACGLQLYNFGQTVSMVFFTENWRPSSFYDRVAENRALGLH 158
Cdd:TIGR00522  81 LVAGDPMVATTHTDLKLEAKRKGIETRIIHGASISSAVcGLTGLQLYKFGKTATIVFFTDNYRPQTPYNVIKENRKIGLH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631497  159 TLVLLDIKVKEpnfeslargklvyepPRFMTVGTCARQMLEvEEEKVKDGAeggvCGGEALAIGAARVGGKTEKFVAGTL 238
Cdd:TIGR00522 161 TLVLLDIHPKE---------------NRAMTIGEGLENLLE-EEEKRKTGA----ITPDTYAVVIARAGSGKPVVKCDKI 220

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 389631497  239 RELadgADELLGAPLHSLVLLGKKTHELEHDFVREFA 275
Cdd:TIGR00522 221 ENL---KNYDFGEPLHCLVVLAKTLHFMEFEYLREFA 254
DPH5 COG1798
Diphthamide biosynthesis methyltransferase [Translation, ribosomal structure and biogenesis];
1-275 2.51e-98

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


Pssm-ID: 441403  Cd Length: 255  Bit Score: 289.01  E-value: 2.51e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631497   1 MLYLIGLGLSDETDITVKGLEIVKTAARVYLEAYTSILL-VDQKVLESYYGRSIEVADREMVESNSDEILRNAATEDVAF 79
Cdd:COG1798    1 MLTFVGLGLSDERDITLKGLEALRSADKVYAEFYTSRLIgTDLEKLEELIGKEIVVLDREDVEDNPEEILEEAKEKDVVF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631497  80 LVVGDPFGATTHTDLVIRARQLQIPIRTIPNASIMSAI-GACGLQLYNFGQTVSMVFFTENWRPSSFYDRVAENRALGLH 158
Cdd:COG1798   81 LTAGDPMIATTHVDLRLRAKRRGIETRVIHGVSIVSAAiGLTGLQNYKFGKTVTIPFPYEGFVPTSPYDTIKENLERGLH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631497 159 TLVLLDIKVkepnfeslargklvyEPPRFMTVGTCARQMLEVEEEKVKdgaegGVCGGEALAIGAARVGGKTEKFVAGTL 238
Cdd:COG1798  161 TLVLLDIKA---------------DKNRYMTANEALELLLEIEKKRRE-----GVISDDTLAVVVARAGSPDPKIVAGKL 220

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 389631497 239 RELADgADelLGAPLHSLVLLGkKTHELEHDFVREFA 275
Cdd:COG1798  221 SELAN-YD--FGEPPHSLIIPG-RLHFMEAEALKALA 253
TP_methylase pfam00590
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ...
 1-177 1.97e-19

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: 84.32  E-value: 1.97e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631497    1 MLYLIGLGLSDETDITVKGLEIVKTAARVYLE---AYTSILLVDQKVLESYYGRSIEVADREMVESNSDEILRNAATEDV 77
Cdd:pfam00590   1 KLYLVGVGPGDPDLLTLRALRALKEADVVLGDdsrALEILLDLLPEDLYFPMTEDKEPLEEAYEEIAEALAAALRAGKDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631497   78 AFLVVGDPFGATTHTDLVIRARQLQIPIRTIPNASIMSAIGACGLQLYNFGQTVSMVFFTENWRPSSfyDRVAENRALGL 157
Cdd:pfam00590  81 ARLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARLGIPLTEGGEVLSVLFLPGLARIE--LRLLEALLANG 158

                         170       180
                  ....*....|....*....|
gi 389631497  158 HTLVLLDIKvkePNFESLAR 177
Cdd:pfam00590 159 DTVVLLYGP---RRLAELAE 175
TP_methylase cd09815
S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet ...
 5-176 7.41e-19

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: 82.83  E-value: 7.41e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631497   5 IGLGLSDETDITVKGLEIVKTAARVYLEAYTSILLVDQKVLESYYG-RSIEVADREMVESNSDEILRNAATE-DVAFLVV 82
Cdd:cd09815    1 VGVGPGDPDLLTLRALEILRAADVVVAEDKDSKLLSLVLRAILKDGkRIYDLHDPNVEEEMAELLLEEARQGkDVAFLSP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631497  83 GDPFGATTHTDLVIRARQLQIPIRTIPNASIMSA-IGACGLQLYNFGQTVSMVFFTENWRPssfyDRVAENRALGLHTLV 161
Cdd:cd09815   81 GDPGVAGTGAELVERAEREGVEVKVIPGVSAADAaAAALGIDLGESFLFVTASDLLENPRL----LVLKALAKERRHLVL 156

                        170
                 ....*....|....*
gi 389631497 162 LLDIKVKEPNFESLA 176
Cdd:cd09815  157 FLDGHRFLKALERLL 171
cobI_cbiL TIGR01467
precorrin-2 C(20)-methyltransferase; This model represents precorrin-2 C(20)-methyltransferase, ...
 1-119 7.95e-08

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: 51.93  E-value: 7.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631497    1 MLYLIGLGLSDETDITVKGLEIVKTAARVYLEAYTS-ILLVDQKVLESYYGRSIEV---------ADREMVESNSDEILR 70
Cdd:TIGR01467   2 KLYGVGVGPGDPELITVKALEALRSADVIAVPASKKgRESLARKIVEDYLKPNDTRilelvfpmtKDRDELEKAWDEAAE 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 389631497   71 NAATE-----DVAFLVVGDPFGATTHTDLVIRARQLQIPIRTIPNASIMSAIGA 119
Cdd:TIGR01467  82 AVAAEleegrDVAFLTLGDPSLYSTFSYLLQRLQGMGIEVEVVPGITSFAACAS 135
PRK05576 PRK05576
cobalt-factor II C(20)-methyltransferase;
1-119 1.64e-07

cobalt-factor II C(20)-methyltransferase;


Pssm-ID: 235512 [Multi-domain]  Cd Length: 229  Bit Score: 51.07  E-value: 1.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631497   1 MLYLIGLGLSDETDITVKGLEIVKTAARVYLEAYT----SILLvdqKVLESYYGRSIEV--------ADREMVESNSDEI 68
Cdd:PRK05576   3 KLYGIGLGPGDPELLTVKAARILEEADVVYAPASRkgggSLAL---NIVRPYLKEETEIvelhfpmsKDEEEKEAVWKEN 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 389631497  69 LRNAATE-----DVAFLVVGDPFGATTHTDLVIRARQLQIPIRTIPNASIMSAIGA 119
Cdd:PRK05576  80 AEEIAAEaeegkNVAFITLGDPNLYSTFSHLLEYLKCHDIEVETVPGISSFTAIAS 135
YabN_N_like cd11723
N-terminal S-AdoMet-dependent tetrapyrrole methylase domain of Bacillus subtilis YabN and ...
 2-117 3.40e-06

N-terminal S-AdoMet-dependent tetrapyrrole methylase domain of Bacillus subtilis YabN and similar domains; This family includes the S-AdoMet (S-adenosyl-L-methionine or SAM)-dependent tetrapyrrole methylase (TP-methylase) domain of Bacillus subtilis YabN, and similar domains. YabN is a fusion of an N-terminal TP-methylase and a C-terminal MazG-type nucleotide pyrophosphohydrolase domain. MazG-like NTP-PPases have been implicated in house-cleaning functions such as degrading abnormal (d)NTPs. TP-methylases use S-AdoMet in the methylation of diverse substrates. Most TP-methylase family members catalyze various methylation steps in cobalamin (vitamin B12) biosynthesis, other members like diphthine synthase and ribosomal RNA small subunit methyltransferase I (RsmI) act on other substrates. The specific function of YabN's TP-methylase domain is not known.


Pssm-ID: 381177  Cd Length: 218  Bit Score: 47.10  E-value: 3.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631497   2 LYLIGLGLSDETDITVKGLEIVKTAARVYLEayTSI------LLVDQKVLES---YY--GRSIEVADREMVEsnsdEILR 70
Cdd:cd11723    1 ITIVGLGPGDPDLLTLGALEALKSADKVYLR--TARhpvveeLKEEGIEFESfddLYeeAEDFEEVYEAIAE----RLLE 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 389631497  71 NAATEDVAFLVVGDPFGATTHTDLVIRARQLQIPIRTIPNASIMSAI 117
Cdd:cd11723   75 AAEHGDVVYAVPGHPLVAERTVQLLLERAEEGIEVEIIPGVSFLDAA 121
CobF COG2243
Precorrin-2 methylase [Coenzyme transport and metabolism]; Precorrin-2 methylase is part of ...
 2-119 1.20e-05

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: 45.47  E-value: 1.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631497   2 LYLIGLGLSDETDITVKGLEIVKTAARVY---------------LEAYtsilLVDQKVLESYYGRSIEVADREMV-ESNS 65
Cdd:COG2243    5 LYGVGVGPGDPELLTLKAVRALREADVIAypakgagkaslareiVAPY----LPPARIVELVFPMTTDYEALVAAwDEAA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 389631497  66 DEILRN-AATEDVAFLVVGDPF--GATTHtdLVIRARQLQIPIRTIPNASIMSAIGA 119
Cdd:COG2243   81 ARIAEElEAGRDVAFLTEGDPSlySTFMY--LLERLRERGFEVEVIPGITSFSAAAA 135
PRK05787 PRK05787
cobalt-precorrin-7 (C(5))-methyltransferase;
1-85 1.41e-04

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


Pssm-ID: 235609 [Multi-domain]  Cd Length: 210  Bit Score: 42.16  E-value: 1.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631497   1 MLYLIGLGLSDETDITVKGLEIVKTAARVY-----LEAYTSILLVDQKVLESYYgrsievadREMVEsnsdEILRNAATE 75
Cdd:PRK05787   1 MIYIVGIGPGDPEYLTLKALEAIRKADVVVgskrvLELFPELIDGEAFVLTAGL--------RDLLE----WLELAAKGK 68

                         90
                 ....*....|
gi 389631497  76 DVAFLVVGDP 85
Cdd:PRK05787  69 NVVVLSTGDP 78
RsmI_like cd19917
tetrapyrrole methylase family protein similar to ribosomal RNA small subunit methyltransferase ...
 3-127 1.77e-03

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: 38.87  E-value: 1.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631497   3 YLIGLGLSDETDITVKGLEIVKTAARVYLEAY--TSILLvdQKVLESyyGRSIEVADREMVESNSDEILRNAATEDVAFL 80
Cdd:cd19917    1 YLVATPIGNTDDITLRALETLKAVDLIICEDTrnASRLL--KHVGII--GKTLEVLNEHNTPEDIQELLDKLAGGKNVAL 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 389631497  81 V--VGDPFGATTHTDLVIRARQLQIPIRTIPNAS-IMSAIGACGLQLYNF 127
Cdd:cd19917   77 VsdAGTPAFADPGADLVKLCRDAGIPVVPLPGASsLMTALSASGLKSDRF 126
Precorrin_2_C20_MT cd11645
Precorrin-2 C20-methyltransferase, also named CobI or CbiL; Precorrin-2 C20-methyltransferase ...
 5-119 2.36e-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: 38.64  E-value: 2.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631497   5 IGLGLSDETDITVKGLEIVKTAARVY------------LEAYTSILLVDQKVLESYY--GRSIEVADREmVESNSDEILR 70
Cdd:cd11645    1 VGVGPGDPELLTLKAVRILKEADVIFvpvskggegsaaLIIAAALLIPDKEIIPLEFpmTKDREELEEA-WDEAAEEIAE 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 389631497  71 NAAT-EDVAFLVVGDPFGATTHTDLVIRARQLQIPIRTIPNASIMSAIGA 119
Cdd:cd11645   80 ELKEgKDVAFLTLGDPSLYSTFSYLLERLRAPGVEVEIIPGITSFSAAAA 129
 
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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