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Conserved domains on  [gi|50540308|ref|NP_001002620|]
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ubiquinone biosynthesis O-methyltransferase, mitochondrial [Danio rerio]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 106779)

class I SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AdoMet_MTases super family cl17173
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 73-303 1.97e-103

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


The actual alignment was detected with superfamily member TIGR01983:

Pssm-ID: 473071  Cd Length: 224  Bit Score: 301.91  E-value: 1.97e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540308    73 EVRKFQAMASKWWDLQGELSALHSMNDLRVPFIRDNLLnmhgvRQLGKPLSGLRILDVGCGGGLLSEPLGRLGADVLGID 152
Cdd:TIGR01983   1 EIAKFSALAHEWWDPNGKFKPLHKMNPLRLDYIRDRIR-----KNFKNPLDGLRVLDVGCGGGLLSEPLARLGANVTGID 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540308   153 PVEDSVRTAELHCSYDPdfrERVRYQACTLEELAEDEAESFHAIVASEVVEHLADLDAFANCCHQVLKPGGSLFITTINK 232
Cdd:TIGR01983  76 ASEENIEVAKLHAKKDP---LQIDYRCTTVEDLAEKKAGSFDVVTCMEVLEHVPDPQAFIRACAQLLKPGGILFFSTINR 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50540308   233 TNLSYVFGIVAAEQLLRIVPSGTHDWEKFISPEDLERLLESFGFYVEAIRGMMYNPLTGAWSWQQSTAINY 303
Cdd:TIGR01983 153 TPKSYLLAIVGAEYILRIVPKGTHDWEKFIKPSELLSWLESAGLRVKDIKGLVYNPIKNTWKLSKDTDVNY 223
 
Name Accession Description Interval E-value
UbiG TIGR01983
ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase ...
 73-303 1.97e-103

ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase believed to act at two points in the ubiquinone biosynthetic pathway in bacteria (UbiG) and fungi (COQ3). A separate methylase (MenG/UbiE) catalyzes the single C-methylation step. The most commonly used names for genes in this family do not indicate whether this gene is an O-methyl, or C-methyl transferase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273910  Cd Length: 224  Bit Score: 301.91  E-value: 1.97e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540308    73 EVRKFQAMASKWWDLQGELSALHSMNDLRVPFIRDNLLnmhgvRQLGKPLSGLRILDVGCGGGLLSEPLGRLGADVLGID 152
Cdd:TIGR01983   1 EIAKFSALAHEWWDPNGKFKPLHKMNPLRLDYIRDRIR-----KNFKNPLDGLRVLDVGCGGGLLSEPLARLGANVTGID 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540308   153 PVEDSVRTAELHCSYDPdfrERVRYQACTLEELAEDEAESFHAIVASEVVEHLADLDAFANCCHQVLKPGGSLFITTINK 232
Cdd:TIGR01983  76 ASEENIEVAKLHAKKDP---LQIDYRCTTVEDLAEKKAGSFDVVTCMEVLEHVPDPQAFIRACAQLLKPGGILFFSTINR 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50540308   233 TNLSYVFGIVAAEQLLRIVPSGTHDWEKFISPEDLERLLESFGFYVEAIRGMMYNPLTGAWSWQQSTAINY 303
Cdd:TIGR01983 153 TPKSYLLAIVGAEYILRIVPKGTHDWEKFIKPSELLSWLESAGLRVKDIKGLVYNPIKNTWKLSKDTDVNY 223
PLN02396 PLN02396
hexaprenyldihydroxybenzoate methyltransferase
 46-312 9.84e-68

hexaprenyldihydroxybenzoate methyltransferase


Pssm-ID: 178018 [Multi-domain]  Cd Length: 322  Bit Score: 214.60  E-value: 9.84e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540308   46 HRQKSQLSNGLTRLNVRSISQSTLDPAEVRKFQAMASKWWDLQGELSALHSMNDLRVPFIRDNLLNmHGVR--QLGKPLS 123
Cdd:PLN02396  53 HPKMQTLEGKASNKSRSTSTTTSLNEDELAKFSAIADTWWHSEGPFKPLHQMNPTRLAFIRSTLCR-HFSKdpSSAKPFE 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540308  124 GLRILDVGCGGGLLSEPLGRLGADVLGIDPVEDSVRTAELHCSYDPDfRERVRYqACTLEELAEDEAESFHAIVASEVVE 203
Cdd:PLN02396 132 GLKFIDIGCGGGLLSEPLARMGATVTGVDAVDKNVKIARLHADMDPV-TSTIEY-LCTTAEKLADEGRKFDAVLSLEVIE 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540308  204 HLADLDAFANCCHQVLKPGGSLFITTINKTNLSYVFGIVAAEQLLRIVPSGTHDWEKFISPEDLERLLESFGFYVEAIRG 283
Cdd:PLN02396 210 HVANPAEFCKSLSALTIPNGATVLSTINRTMRAYASTIVGAEYILRWLPKGTHQWSSFVTPEELSMILQRASVDVKEMAG 289

                        250       260
                 ....*....|....*....|....*....
gi 50540308  284 MMYNPLTGAWSWQQSTAINYALHAVKRKE 312
Cdd:PLN02396 290 FVYNPITGRWLLSDDISVNYIAYGTKRKD 318
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 122-231 2.28e-28

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 106.26  E-value: 2.28e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540308 122 LSGLRILDVGCGGGLLSEPLGRLGADVLGIDPVEDSVRTAELHCSydpdfRERVRYQaCTLEELAEDEAESFHAIVASEV 201
Cdd:COG2227  23 PAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAA-----ELNVDFV-QGDLEDLPLEDGSFDLVICSEV 96

                        90       100       110
                ....*....|....*....|....*....|
gi 50540308 202 VEHLADLDAFANCCHQVLKPGGSLFITTIN 231
Cdd:COG2227  97 LEHLPDPAALLRELARLLKPGGLLLLSTPN 126
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 116-280 5.90e-19

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 82.09  E-value: 5.90e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540308   116 RQLGKPLSGLRILDVGCGGGLLSEPLGRLGADVLGIDPVEDSVRTAELHCSYDPDFRERVRYQActleelaedeaESFHA 195
Cdd:pfam13489  15 RLLPKLPSPGRVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERALLNVRFDQFDEQEAAVPA-----------GKFDV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540308   196 IVASEVVEHLADLDAFANCCHQVLKPGGSLFITTINKTNLSyvfgIVAAEQLLRIVPSGTHDWekFISPEDLERLLESFG 275
Cdd:pfam13489  84 IVAREVLEHVPDPPALLRQIAALLKPGGLLLLSTPLASDEA----DRLLLEWPYLRPRNGHIS--LFSARSLKRLLEEAG 157


                  ....*
gi 50540308   276 FYVEA 280
Cdd:pfam13489 158 FEVVS 162
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 126-228 1.94e-12

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 62.83  E-value: 1.94e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540308 126 RILDVGCGGGLLSEPLGRL-GADVLGIDPVEDSVRTAELHCSYDpdFRERVRYQACTLEELAEDEAESFHAIVASEVVEH 204
Cdd:cd02440   1 RVLDLGCGTGALALALASGpGARVTGVDISPVALELARKAAAAL--LADNVEVLKGDAEELPPEADESFDVIISDPPLHH 78

                        90       100
                ....*....|....*....|....*
gi 50540308 205 L-ADLDAFANCCHQVLKPGGSLFIT 228
Cdd:cd02440  79 LvEDLARFLEEARRLLKPGGVLVLT 103
 
Name Accession Description Interval E-value
UbiG TIGR01983
ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase ...
 73-303 1.97e-103

ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase believed to act at two points in the ubiquinone biosynthetic pathway in bacteria (UbiG) and fungi (COQ3). A separate methylase (MenG/UbiE) catalyzes the single C-methylation step. The most commonly used names for genes in this family do not indicate whether this gene is an O-methyl, or C-methyl transferase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273910  Cd Length: 224  Bit Score: 301.91  E-value: 1.97e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540308    73 EVRKFQAMASKWWDLQGELSALHSMNDLRVPFIRDNLLnmhgvRQLGKPLSGLRILDVGCGGGLLSEPLGRLGADVLGID 152
Cdd:TIGR01983   1 EIAKFSALAHEWWDPNGKFKPLHKMNPLRLDYIRDRIR-----KNFKNPLDGLRVLDVGCGGGLLSEPLARLGANVTGID 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540308   153 PVEDSVRTAELHCSYDPdfrERVRYQACTLEELAEDEAESFHAIVASEVVEHLADLDAFANCCHQVLKPGGSLFITTINK 232
Cdd:TIGR01983  76 ASEENIEVAKLHAKKDP---LQIDYRCTTVEDLAEKKAGSFDVVTCMEVLEHVPDPQAFIRACAQLLKPGGILFFSTINR 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50540308   233 TNLSYVFGIVAAEQLLRIVPSGTHDWEKFISPEDLERLLESFGFYVEAIRGMMYNPLTGAWSWQQSTAINY 303
Cdd:TIGR01983 153 TPKSYLLAIVGAEYILRIVPKGTHDWEKFIKPSELLSWLESAGLRVKDIKGLVYNPIKNTWKLSKDTDVNY 223
PLN02396 PLN02396
hexaprenyldihydroxybenzoate methyltransferase
 46-312 9.84e-68

hexaprenyldihydroxybenzoate methyltransferase


Pssm-ID: 178018 [Multi-domain]  Cd Length: 322  Bit Score: 214.60  E-value: 9.84e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540308   46 HRQKSQLSNGLTRLNVRSISQSTLDPAEVRKFQAMASKWWDLQGELSALHSMNDLRVPFIRDNLLNmHGVR--QLGKPLS 123
Cdd:PLN02396  53 HPKMQTLEGKASNKSRSTSTTTSLNEDELAKFSAIADTWWHSEGPFKPLHQMNPTRLAFIRSTLCR-HFSKdpSSAKPFE 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540308  124 GLRILDVGCGGGLLSEPLGRLGADVLGIDPVEDSVRTAELHCSYDPDfRERVRYqACTLEELAEDEAESFHAIVASEVVE 203
Cdd:PLN02396 132 GLKFIDIGCGGGLLSEPLARMGATVTGVDAVDKNVKIARLHADMDPV-TSTIEY-LCTTAEKLADEGRKFDAVLSLEVIE 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540308  204 HLADLDAFANCCHQVLKPGGSLFITTINKTNLSYVFGIVAAEQLLRIVPSGTHDWEKFISPEDLERLLESFGFYVEAIRG 283
Cdd:PLN02396 210 HVANPAEFCKSLSALTIPNGATVLSTINRTMRAYASTIVGAEYILRWLPKGTHQWSSFVTPEELSMILQRASVDVKEMAG 289

                        250       260
                 ....*....|....*....|....*....
gi 50540308  284 MMYNPLTGAWSWQQSTAINYALHAVKRKE 312
Cdd:PLN02396 290 FVYNPITGRWLLSDDISVNYIAYGTKRKD 318
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 122-231 2.28e-28

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 106.26  E-value: 2.28e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540308 122 LSGLRILDVGCGGGLLSEPLGRLGADVLGIDPVEDSVRTAELHCSydpdfRERVRYQaCTLEELAEDEAESFHAIVASEV 201
Cdd:COG2227  23 PAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAA-----ELNVDFV-QGDLEDLPLEDGSFDLVICSEV 96

                        90       100       110
                ....*....|....*....|....*....|
gi 50540308 202 VEHLADLDAFANCCHQVLKPGGSLFITTIN 231
Cdd:COG2227  97 LEHLPDPAALLRELARLLKPGGLLLLSTPN 126
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 116-280 5.90e-19

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 82.09  E-value: 5.90e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540308   116 RQLGKPLSGLRILDVGCGGGLLSEPLGRLGADVLGIDPVEDSVRTAELHCSYDPDFRERVRYQActleelaedeaESFHA 195
Cdd:pfam13489  15 RLLPKLPSPGRVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERALLNVRFDQFDEQEAAVPA-----------GKFDV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540308   196 IVASEVVEHLADLDAFANCCHQVLKPGGSLFITTINKTNLSyvfgIVAAEQLLRIVPSGTHDWekFISPEDLERLLESFG 275
Cdd:pfam13489  84 IVAREVLEHVPDPPALLRQIAALLKPGGLLLLSTPLASDEA----DRLLLEWPYLRPRNGHIS--LFSARSLKRLLEEAG 157


                  ....*
gi 50540308   276 FYVEA 280
Cdd:pfam13489 158 FEVVS 162
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 124-244 2.71e-18

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 80.04  E-value: 2.71e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540308 124 GLRILDVGCGGGLLSEPLGRLGADVLGIDPVEDSVRTAELHCsydPDFRERVRYQACTlEELAEDEAESFHAIVASEVVE 203
Cdd:COG2226  23 GARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERA---AEAGLNVEFVVGD-AEDLPFPDGSFDLVISSFVLH 98

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 50540308 204 HLADLDAFANCCHQVLKPGGSLFITTINKTNLSYVFGIVAA 244
Cdd:COG2226  99 HLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELEELLAE 139
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
68-249 6.44e-18

Predicted methyltransferase, contains TPR repeat [General function prediction only];


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 80.04  E-value: 6.44e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540308  68 TLDPAEVRKFQAMAsKWWDlqgelSALHSMNDLRVPF-IRDNLLNMHGvrqlgkPLSGLRILDVGCGGGLLSEPLGRLGA 146
Cdd:COG4976   2 ALDAYVEALFDQYA-DSYD-----AALVEDLGYEAPAlLAEELLARLP------PGPFGRVLDLGCGTGLLGEALRPRGY 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540308 147 DVLGIDPVEDSVRTAELHCSYDP----DFRErvryqactleelAEDEAESFHAIVASEVVEHLADLDAFANCCHQVLKPG 222
Cdd:COG4976  70 RLTGVDLSEEMLAKAREKGVYDRllvaDLAD------------LAEPDGRFDLIVAADVLTYLGDLAAVFAGVARALKPG 137

                       170       180
                ....*....|....*....|....*....
gi 50540308 223 GsLFITTINKTNLS--YVFGIVAAEQLLR 249
Cdd:COG4976 138 G-LFIFSVEDADGSgrYAHSLDYVRDLLA 165
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 128-227 9.64e-16

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 71.54  E-value: 9.64e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540308   128 LDVGCGGGLLSEPLGRLGADVLGIDPVEDSVRTAELHcsydpdFRERVRYQACTLEELAEDEAESFHAIVASEVVEHLAD 207
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREK------APREGLTFVVGDAEDLPFPDNSFDLVLSSEVLHHVED 74

                          90       100
                  ....*....|....*....|
gi 50540308   208 LDAFANCCHQVLKPGGSLFI 227
Cdd:pfam08241  75 PERALREIARVLKPGGILII 94
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 127-223 1.96e-15

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 70.67  E-value: 1.96e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540308   127 ILDVGCGGGLLSEPL-GRLGADVLGIDPVEDSVRTAELHCSYDPdfrERVRYQACTlEELAEDEAESFHAIVASEVVEHL 205
Cdd:pfam13649   1 VLDLGCGTGRLTLALaRRGGARVTGVDLSPEMLERARERAAEAG---LNVEFVQGD-AEDLPFPDGSFDLVVSSGVLHHL 76

                          90       100
                  ....*....|....*....|
gi 50540308   206 --ADLDAFANCCHQVLKPGG 223
Cdd:pfam13649  77 pdPDLEAALREIARVLKPGG 96
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 128-225 3.22e-14

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 67.39  E-value: 3.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540308   128 LDVGCGGGLLSEPLGRL--GADVLGIDPVEDSV-RTAELHCSYDPDFRERVRYQACtleELAEDEAESFHAIVASEVVEH 204
Cdd:pfam08242   1 LEIGCGTGTLLRALLEAlpGLEYTGLDISPAALeAARERLAALGLLNAVRVELFQL---DLGELDPGSFDVVVASNVLHH 77

                          90       100
                  ....*....|....*....|.
gi 50540308   205 LADLDAFANCCHQVLKPGGSL 225
Cdd:pfam08242  78 LADPRAVLRNIRRLLKPGGVL 98
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 126-228 1.94e-12

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 62.83  E-value: 1.94e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540308 126 RILDVGCGGGLLSEPLGRL-GADVLGIDPVEDSVRTAELHCSYDpdFRERVRYQACTLEELAEDEAESFHAIVASEVVEH 204
Cdd:cd02440   1 RVLDLGCGTGALALALASGpGARVTGVDISPVALELARKAAAAL--LADNVEVLKGDAEELPPEADESFDVIISDPPLHH 78

                        90       100
                ....*....|....*....|....*
gi 50540308 205 L-ADLDAFANCCHQVLKPGGSLFIT 228
Cdd:cd02440  79 LvEDLARFLEEARRLLKPGGVLVLT 103
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
124-229 2.67e-12

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 62.15  E-value: 2.67e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540308 124 GLRILDVGCGGGLLSEPLGRL--GADVLGIDPVEDSVRTA-------ELHCSydpDFRErvryqactleelaEDEAESFH 194
Cdd:COG4106   2 PRRVLDLGCGTGRLTALLAERfpGARVTGVDLSPEMLARArarlpnvRFVVA---DLRD-------------LDPPEPFD 65

                        90       100       110
                ....*....|....*....|....*....|....*
gi 50540308 195 AIVASEVVEHLADLDAFANCCHQVLKPGGSLFITT 229
Cdd:COG4106  66 LVVSNAALHWLPDHAALLARLAAALAPGGVLAVQV 100
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 124-288 9.74e-12

SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 63.01  E-value: 9.74e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540308 124 GLRILDVGCGGGLLSEPL-GRLGADVLGIDPVEDSVRTAElhCSYDPDFRERVRYQACTLEELAEDEAESFHAIVASEVV 202
Cdd:COG0500  27 GGRVLDLGCGTGRNLLALaARFGGRVIGIDLSPEAIALAR--ARAAKAGLGNVEFLVADLAELDPLPAESFDLVVAFGVL 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540308 203 EHL--ADLDAFANCCHQVLKPGGSLFITTINKTNLSYvfgIVAAEQLLRIVPSGTHDWEKFISPEDLERLLESFGFYVEA 280
Cdd:COG0500 105 HHLppEEREALLRELARALKPGGVLLLSASDAAAALS---LARLLLLATASLLELLLLLRLLALELYLRALLAAAATEDL 181


                ....*...
gi 50540308 281 IRGMMYNP 288
Cdd:COG0500 182 RSDALLES 189
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 124-229 1.43e-11

Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 61.48  E-value: 1.43e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540308 124 GLRILDVGCGGGLLSEPL-GRLGADVLGIDPVEDSVRTAE-------LHCSYDP---DFRErvryqactleelaEDEAES 192
Cdd:COG2230  52 GMRVLDIGCGWGGLALYLaRRYGVRVTGVTLSPEQLEYAReraaeagLADRVEVrlaDYRD-------------LPADGQ 118

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 50540308 193 FHAIVASEVVEHL--ADLDAFANCCHQVLKPGGSLFITT 229
Cdd:COG2230 119 FDAIVSIGMFEHVgpENYPAYFAKVARLLKPGGRLLLHT 157
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 122-152 9.53e-08

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 51.76  E-value: 9.53e-08
                         10        20        30
                 ....*....|....*....|....*....|.
gi 50540308  122 LSGLRILDVGCGGGLLSEPLGRLGADVLGID 152
Cdd:PRK07580  62 LTGLRILDAGCGVGSLSIPLARRGAKVVASD 92
PRK08317 PRK08317
hypothetical protein; Provisional
 124-227 1.83e-07

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 51.09  E-value: 1.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540308  124 GLRILDVGCGGGLLSEPL-GRLGAD--VLGIDPVEDSVRTAELHCSYDPDFRERVRYQActleELAEDEAESFHAIVASE 200
Cdd:PRK08317  20 GDRVLDVGCGPGNDARELaRRVGPEgrVVGIDRSEAMLALAKERAAGLGPNVEFVRGDA----DGLPFPDGSFDAVRSDR 95

                         90       100
                 ....*....|....*....|....*..
gi 50540308  201 VVEHLADLDAFANCCHQVLKPGGSLFI 227
Cdd:PRK08317  96 VLQHLEDPARALAEIARVLRPGGRVVV 122
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 123-275 1.28e-06

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 47.41  E-value: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540308   123 SGLRILDVGCGGGLLSEPLGRL---GADVLGIDPVEDSVRTAELHCsyDPDFRERVRYQAC-TLEELAEDEAESFHAIVA 198
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEElgpNAEVVGIDISEEAIEKARENA--QKLGFDNVEFEQGdIEELPELLEDDKFDVVIS 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50540308   199 SEVVEHLADLDAFANCCHQVLKPGGSLFITTINktNLSYVFGIVAAEQllrivPSGTHDWEKFISPEDLERLLESFG 275
Cdd:pfam13847  81 NCVLNHIPDPDKVLQEILRVLKPGGRLIISDPD--SLAELPAHVKEDS-----TYYAGCVGGAILKKKLYELLEEAG 150
COG4627 COG4627
Predicted SAM-depedendent methyltransferase [General function prediction only];
192-229 5.25e-06

Predicted SAM-depedendent methyltransferase [General function prediction only];


Pssm-ID: 443666 [Multi-domain]  Cd Length: 161  Bit Score: 45.63  E-value: 5.25e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 50540308 192 SFHAIVASEVVEHL--ADLDAFANCCHQVLKPGGSLFITT 229
Cdd:COG4627  46 SVDAIYSSHVLEHLdyEEAPLALKECYRVLKPGGILRIVV 85
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 77-291 1.14e-04

ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of methyltransferases involved in the biosynthesis of menaquinone and ubiqinone. Some members such as the UbiE enzyme from E. coli are believed to act in both pathways, while others may act in only the menaquinone pathway. These methyltransferases are members of the UbiE/CoQ family of methyltransferases (pfam01209) which also contains ubiquinone methyltransferases and other methyltransferases. Members of this clade include a wide distribution of bacteria and eukaryotes, but no archaea. An outgroup for this clade is provided by the phosphatidylethanolamine methyltransferase (EC 2.1.1.17) from Rhodobacter sphaeroides. Note that a number of non-orthologous genes which are members of pfam03737 have been erroneously annotated as MenG methyltransferases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273884 [Multi-domain]  Cd Length: 223  Bit Score: 42.63  E-value: 1.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540308    77 FQAMASKWwDLqgelsalhsMNDLrVPFIRDNLLNMHGVRQLGKPlSGLRILDVGCGGGLLSEPLGRLGAD---VLGIDP 153
Cdd:TIGR01934   5 FDRIAPKY-DL---------LNDL-LSFGLHRLWRRRAVKLIGVF-KGQKVLDVACGTGDLAIELAKSAPDrgkVTGVDF 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540308   154 VEDSVRTAELHCSYDpdfrERVRYQaCTLEELAEDEAESFHAIVASEVVEHLADLDAFANCCHQVLKPGGSLFITTINKT 233
Cdd:TIGR01934  73 SSEMLEVAKKKSELP----LNIEFI-QADAEALPFEDNSFDAVTIAFGLRNVTDIQKALREMYRVLKPGGRLVILEFSKP 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50540308   234 NLSyVFGIVAAEQLLRIVPS---------GTHDW-----EKFISPEDLERLLESFGFyvEAIRgmmYNPLTG 291
Cdd:TIGR01934 148 ANA-LLKKFYKFYLKNVLPSigglisknaEAYTYlpesiRAFPSQEELAAMLKEAGF--EEVR---YRSLTF 213
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 124-230 1.57e-04

Mycolic acid cyclopropane synthetase; This family consist of Cyclopropane-fatty-acyl-phospholipid synthase or CFA synthase EC:2.1.1.79 this enzyme catalyze the reaction: S-adenosyl-L-methionine + phospholipid olefinic fatty acid <=> S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid.


Pssm-ID: 396777 [Multi-domain]  Cd Length: 272  Bit Score: 42.70  E-value: 1.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540308   124 GLRILDVGCG-GGLLSEPLGRLGADVLGID-------------PVEDSVRTAELHCSYDPDFRERvryqactleelaede 189
Cdd:pfam02353  62 GMTLLDIGCGwGGLMRRAAERYDVNVVGLTlsknqyklarkrvAAEGLARKVEVLLQDYRDFDEP--------------- 126

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 50540308   190 aesFHAIVASEVVEHL--ADLDAFANCCHQVLKPGGSLFITTI 230
Cdd:pfam02353 127 ---FDRIVSVGMFEHVghENYDTFFKKLYNLLPPGGLMLLHTI 166
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 104-235 6.52e-04

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 40.35  E-value: 6.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540308   104 FIRDNLLNMhgVRQLGKPLSGlRILDVGCGGGLLSEPLGRLG--ADVLGIDPVEDSVRTAELHCSydpdfrERVRYQaCT 181
Cdd:TIGR02072  18 EMAKRLLAL--LKEKGIFIPA-SVLDIGCGTGYLTRALLKRFpqAEFIALDISAGMLAQAKTKLS------ENVQFI-CG 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 50540308   182 LEELAEDEAESFHAIVASEVVEHLADLDAFANCCHQVLKPGGSLFITTINKTNL 235
Cdd:TIGR02072  88 DAEKLPLEDSSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFGPGTL 141
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
121-225 1.35e-03

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 39.75  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540308  121 PLSGLRILDVGCGGGLLSEPLGRLGA-DVLG--IDPVedSVRTAelhcsydpdfRERVRYQACTLEELAEDEAESFHAIV 197
Cdd:PRK00517 117 VLPGKTVLDVGCGSGILAIAAAKLGAkKVLAvdIDPQ--AVEAA----------RENAELNGVELNVYLPQGDLKADVIV 184

                         90       100       110
                 ....*....|....*....|....*....|.
gi 50540308  198 A---SEVVEHLADLdaFANCchqvLKPGGSL 225
Cdd:PRK00517 185 AnilANPLLELAPD--LARL----LKPGGRL 209
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
 112-169 2.46e-03

2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family has members identified as 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide A dehydrogenase and alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176217 [Multi-domain]  Cd Length: 277  Bit Score: 38.79  E-value: 2.46e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50540308 112 MHGVRQLGkPLSGLRILDVGCG--GGLLSEPLGRLGA-DVLGIDPVEDSVRTAELHCSYDP 169
Cdd:cd08255  87 LNGVRDAE-PRLGERVAVVGLGlvGLLAAQLAKAAGArEVVGVDPDAARRELAEALGPADP 146
PRK14968 PRK14968
putative methyltransferase; Provisional
 124-162 4.18e-03

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 37.57  E-value: 4.18e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 50540308  124 GLRILDVGCGGGLLSEPLGRLGADVLGIDPVEDSVRTAE 162
Cdd:PRK14968  24 GDRVLEVGTGSGIVAIVAAKNGKKVVGVDINPYAVECAK 62
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 115-161 7.13e-03

tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure and biogenesis]; tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441866 [Multi-domain]  Cd Length: 377  Bit Score: 37.85  E-value: 7.13e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 50540308 115 VRQLGKPLSGLRILDVGCGGGLLSEPLGRLGADVLGIDPVEDSVRTA 161
Cdd:COG2265 225 ALEWLDLTGGERVLDLYCGVGTFALPLARRAKKVIGVEIVPEAVEDA 271
 
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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