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Conserved domains on  [gi|1907155456|ref|XP_036019878|]
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ubiquinone biosynthesis O-methyltransferase, mitochondrial isoform X1 [Mus musculus]

Protein Classification

bifunctional 2-polyprenyl-6-hydroxyphenol methylase/3-demethylubiquinol 3-O-methyltransferase UbiG( domain architecture ID 11493423)

bifunctional 2-polyprenyl-6-hydroxyphenol methylase/3-demethylubiquinol 3-O-methyltransferase UbiG is a class I SAM-dependent methyltransferase that catalyzes both methylation steps in ubiquinone biosynthesis

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UbiG TIGR01983
ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase ...
38-268 9.30e-121

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: 345.82  E-value: 9.30e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456  38 EVKNFQALAHTWWDEYGKFAPLHSMNDLRVPFIRDNLLKtsashHPGKPLSGMKILDVGCGGGLLTEPLGRLGASVVGID 117
Cdd:TIGR01983   1 EIAKFSALAHEWWDPNGKFKPLHKMNPLRLDYIRDRIRK-----NFKNPLDGLRVLDVGCGGGLLSEPLARLGANVTGID 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456 118 PVAENIKIAQHHKSFDPVLdkrIQYKVCSLEEAVDESAECFDAVVASEVVEHVSHLEMFIQCCYQVLKPGGSLFITTVNK 197
Cdd:TIGR01983  76 ASEENIEVAKLHAKKDPLQ---IDYRCTTVEDLAEKKAGSFDVVTCMEVLEHVPDPQAFIRACAQLLKPGGILFFSTINR 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907155456 198 TQLSYALGIVFAEQIAGIVPKGTHTWEKFVSPEKLESILEPNGLSVETVAGLVYNPFSGYWHWSENTSLNY 268
Cdd:TIGR01983 153 TPKSYLLAIVGAEYILRIVPKGTHDWEKFIKPSELLSWLESAGLRVKDIKGLVYNPIKNTWKLSKDTDVNY 223
 
Name Accession Description Interval E-value
UbiG TIGR01983
ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase ...
38-268 9.30e-121

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: 345.82  E-value: 9.30e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456  38 EVKNFQALAHTWWDEYGKFAPLHSMNDLRVPFIRDNLLKtsashHPGKPLSGMKILDVGCGGGLLTEPLGRLGASVVGID 117
Cdd:TIGR01983   1 EIAKFSALAHEWWDPNGKFKPLHKMNPLRLDYIRDRIRK-----NFKNPLDGLRVLDVGCGGGLLSEPLARLGANVTGID 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456 118 PVAENIKIAQHHKSFDPVLdkrIQYKVCSLEEAVDESAECFDAVVASEVVEHVSHLEMFIQCCYQVLKPGGSLFITTVNK 197
Cdd:TIGR01983  76 ASEENIEVAKLHAKKDPLQ---IDYRCTTVEDLAEKKAGSFDVVTCMEVLEHVPDPQAFIRACAQLLKPGGILFFSTINR 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907155456 198 TQLSYALGIVFAEQIAGIVPKGTHTWEKFVSPEKLESILEPNGLSVETVAGLVYNPFSGYWHWSENTSLNY 268
Cdd:TIGR01983 153 TPKSYLLAIVGAEYILRIVPKGTHDWEKFIKPSELLSWLESAGLRVKDIKGLVYNPIKNTWKLSKDTDVNY 223
PLN02396 PLN02396
hexaprenyldihydroxybenzoate methyltransferase
28-274 2.25e-76

hexaprenyldihydroxybenzoate methyltransferase


Pssm-ID: 178018 [Multi-domain]  Cd Length: 322  Bit Score: 236.55  E-value: 2.25e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456  28 STSQTTVDSREVKNFQALAHTWWDEYGKFAPLHSMNDLRVPFIRDNLLKT-SASHHPGKPLSGMKILDVGCGGGLLTEPL 106
Cdd:PLN02396   70 TSTTTSLNEDELAKFSAIADTWWHSEGPFKPLHQMNPTRLAFIRSTLCRHfSKDPSSAKPFEGLKFIDIGCGGGLLSEPL 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456 107 GRLGASVVGIDPVAENIKIAQHHKSFDPVLDKrIQYkVCSLEEAVDESAECFDAVVASEVVEHVSHLEMFIQCCYQVLKP 186
Cdd:PLN02396  150 ARMGATVTGVDAVDKNVKIARLHADMDPVTST-IEY-LCTTAEKLADEGRKFDAVLSLEVIEHVANPAEFCKSLSALTIP 227
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456 187 GGSLFITTVNKTQLSYALGIVFAEQIAGIVPKGTHTWEKFVSPEKLESILEPNGLSVETVAGLVYNPFSGYWHWSENTSL 266
Cdd:PLN02396  228 NGATVLSTINRTMRAYASTIVGAEYILRWLPKGTHQWSSFVTPEELSMILQRASVDVKEMAGFVYNPITGRWLLSDDISV 307

                  ....*...
gi 1907155456 267 NYAAHAVR 274
Cdd:PLN02396  308 NYIAYGTK 315
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
87-196 1.34e-32

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: 117.04  E-value: 1.34e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456  87 LSGMKILDVGCGGGLLTEPLGRLGASVVGIDPVAENIKIAQHHksfdpVLDKRIQYKVCSLEEaVDESAECFDAVVASEV 166
Cdd:COG2227    23 PAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARER-----AAELNVDFVQGDLED-LPLEDGSFDLVICSEV 96
                          90       100       110
                  ....*....|....*....|....*....|
gi 1907155456 167 VEHVSHLEMFIQCCYQVLKPGGSLFITTVN 196
Cdd:COG2227    97 LEHLPDPAALLRELARLLKPGGLLLLSTPN 126
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
93-192 7.23e-24

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 93.11  E-value: 7.23e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456  93 LDVGCGGGLLTEPLGRLGASVVGIDPVAENIKIAQHHKSFDPVldkriQYKVCSLEEaVDESAECFDAVVASEVVEHVSH 172
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREGL-----TFVVGDAED-LPFPDNSFDLVLSSEVLHHVED 74
                          90       100
                  ....*....|....*....|
gi 1907155456 173 LEMFIQCCYQVLKPGGSLFI 192
Cdd:pfam08241  75 PERALREIARVLKPGGILII 94
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
91-195 6.56e-16

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: 72.08  E-value: 6.56e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456  91 KILDVGCGGGLLTEPLGRL-GASVVGIDPVAENIKIAQhhKSFDPVLDKRIQYKVCSLEEAVDESAECFDAVVASEVVEH 169
Cdd:cd02440     1 RVLDLGCGTGALALALASGpGARVTGVDISPVALELAR--KAAAALLADNVEVLKGDAEELPPEADESFDVIISDPPLHH 78
                          90       100
                  ....*....|....*....|....*..
gi 1907155456 170 VSHLEM-FIQCCYQVLKPGGSLFITTV 195
Cdd:cd02440    79 LVEDLArFLEEARRLLKPGGVLVLTLV 105
 
Name Accession Description Interval E-value
UbiG TIGR01983
ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase ...
38-268 9.30e-121

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: 345.82  E-value: 9.30e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456  38 EVKNFQALAHTWWDEYGKFAPLHSMNDLRVPFIRDNLLKtsashHPGKPLSGMKILDVGCGGGLLTEPLGRLGASVVGID 117
Cdd:TIGR01983   1 EIAKFSALAHEWWDPNGKFKPLHKMNPLRLDYIRDRIRK-----NFKNPLDGLRVLDVGCGGGLLSEPLARLGANVTGID 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456 118 PVAENIKIAQHHKSFDPVLdkrIQYKVCSLEEAVDESAECFDAVVASEVVEHVSHLEMFIQCCYQVLKPGGSLFITTVNK 197
Cdd:TIGR01983  76 ASEENIEVAKLHAKKDPLQ---IDYRCTTVEDLAEKKAGSFDVVTCMEVLEHVPDPQAFIRACAQLLKPGGILFFSTINR 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907155456 198 TQLSYALGIVFAEQIAGIVPKGTHTWEKFVSPEKLESILEPNGLSVETVAGLVYNPFSGYWHWSENTSLNY 268
Cdd:TIGR01983 153 TPKSYLLAIVGAEYILRIVPKGTHDWEKFIKPSELLSWLESAGLRVKDIKGLVYNPIKNTWKLSKDTDVNY 223
PLN02396 PLN02396
hexaprenyldihydroxybenzoate methyltransferase
28-274 2.25e-76

hexaprenyldihydroxybenzoate methyltransferase


Pssm-ID: 178018 [Multi-domain]  Cd Length: 322  Bit Score: 236.55  E-value: 2.25e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456  28 STSQTTVDSREVKNFQALAHTWWDEYGKFAPLHSMNDLRVPFIRDNLLKT-SASHHPGKPLSGMKILDVGCGGGLLTEPL 106
Cdd:PLN02396   70 TSTTTSLNEDELAKFSAIADTWWHSEGPFKPLHQMNPTRLAFIRSTLCRHfSKDPSSAKPFEGLKFIDIGCGGGLLSEPL 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456 107 GRLGASVVGIDPVAENIKIAQHHKSFDPVLDKrIQYkVCSLEEAVDESAECFDAVVASEVVEHVSHLEMFIQCCYQVLKP 186
Cdd:PLN02396  150 ARMGATVTGVDAVDKNVKIARLHADMDPVTST-IEY-LCTTAEKLADEGRKFDAVLSLEVIEHVANPAEFCKSLSALTIP 227
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456 187 GGSLFITTVNKTQLSYALGIVFAEQIAGIVPKGTHTWEKFVSPEKLESILEPNGLSVETVAGLVYNPFSGYWHWSENTSL 266
Cdd:PLN02396  228 NGATVLSTINRTMRAYASTIVGAEYILRWLPKGTHQWSSFVTPEELSMILQRASVDVKEMAGFVYNPITGRWLLSDDISV 307

                  ....*...
gi 1907155456 267 NYAAHAVR 274
Cdd:PLN02396  308 NYIAYGTK 315
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
87-196 1.34e-32

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: 117.04  E-value: 1.34e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456  87 LSGMKILDVGCGGGLLTEPLGRLGASVVGIDPVAENIKIAQHHksfdpVLDKRIQYKVCSLEEaVDESAECFDAVVASEV 166
Cdd:COG2227    23 PAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARER-----AAELNVDFVQGDLED-LPLEDGSFDLVICSEV 96
                          90       100       110
                  ....*....|....*....|....*....|
gi 1907155456 167 VEHVSHLEMFIQCCYQVLKPGGSLFITTVN 196
Cdd:COG2227    97 LEHLPDPAALLRELARLLKPGGLLLLSTPN 126
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
89-200 4.87e-24

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: 95.06  E-value: 4.87e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456  89 GMKILDVGCGGGLLTEPLGRLGASVVGIDPVAENIKIAQHHKsfdPVLDKRIQYKVCSLeEAVDESAECFDAVVASEVVE 168
Cdd:COG2226    23 GARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERA---AEAGLNVEFVVGDA-EDLPFPDGSFDLVISSFVLH 98
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1907155456 169 HVSHLEMFIQCCYQVLKPGGSLFITTVNKTQL 200
Cdd:COG2226    99 HLPDPERALAEIARVLKPGGRLVVVDFSPPDL 130
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
93-192 7.23e-24

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 93.11  E-value: 7.23e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456  93 LDVGCGGGLLTEPLGRLGASVVGIDPVAENIKIAQHHKSFDPVldkriQYKVCSLEEaVDESAECFDAVVASEVVEHVSH 172
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREGL-----TFVVGDAED-LPFPDNSFDLVLSSEVLHHVED 74
                          90       100
                  ....*....|....*....|
gi 1907155456 173 LEMFIQCCYQVLKPGGSLFI 192
Cdd:pfam08241  75 PERALREIARVLKPGGILII 94
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
92-188 2.00e-22

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 89.16  E-value: 2.00e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456  92 ILDVGCGGGLLTEPL-GRLGASVVGIDPVAENIKIAQHHKSFDPVldkRIQYKVCSLEEaVDESAECFDAVVASEVVEHV 170
Cdd:pfam13649   1 VLDLGCGTGRLTLALaRRGGARVTGVDLSPEMLERARERAAEAGL---NVEFVQGDAED-LPFPDGSFDLVVSSGVLHHL 76
                          90       100
                  ....*....|....*....|
gi 1907155456 171 SH--LEMFIQCCYQVLKPGG 188
Cdd:pfam13649  77 PDpdLEAALREIARVLKPGG 96
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
69-245 4.05e-22

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 90.57  E-value: 4.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456  69 FIRDNLLKTSAshhpgKPLSGMKILDVGCGGGLLTEPLGRLGASVVGIDPVAENIKIA---QHHKSFDPVLDkriqykvc 145
Cdd:pfam13489   8 LLADLLLRLLP-----KLPSPGRVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERAllnVRFDQFDEQEA-------- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456 146 sleeavDESAECFDAVVASEVVEHVSHLEMFIQCCYQVLKPGGSLFITTVNKTQLSYALgivfAEQIAGIVPKGTHTWek 225
Cdd:pfam13489  75 ------AVPAGKFDVIVAREVLEHVPDPPALLRQIAALLKPGGLLLLSTPLASDEADRL----LLEWPYLRPRNGHIS-- 142
                         170       180
                  ....*....|....*....|
gi 1907155456 226 FVSPEKLESILEPNGLSVET 245
Cdd:pfam13489 143 LFSARSLKRLLEEAGFEVVS 162
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
91-193 1.51e-17

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 79.19  E-value: 1.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456  91 KILDVGCGGGLLTEPL-GRLGASVVGIDPVAENIKIAQhhKSFDPVLDKRIQYKVCSLEEAVDESAECFDAVVASEVVEH 169
Cdd:COG0500    29 RVLDLGCGTGRNLLALaARFGGRVIGIDLSPEAIALAR--ARAAKAGLGNVEFLVADLAELDPLPAESFDLVVAFGVLHH 106
                          90       100
                  ....*....|....*....|....*.
gi 1907155456 170 VSHLEM--FIQCCYQVLKPGGSLFIT 193
Cdd:COG0500   107 LPPEEReaLLRELARALKPGGVLLLS 132
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
53-196 3.41e-17

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 77.73  E-value: 3.41e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456  53 YGKFAPL---HSMNDLRVPFIRDNLLKTSASHHPGKPLSgmkILDVGCGGGLLTEPLGRLGASVVGIDPVAENIKIAQHH 129
Cdd:COG4976    11 FDQYADSydaALVEDLGYEAPALLAEELLARLPPGPFGR---VLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAREK 87
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907155456 130 KSFDPVLdkriqykVCSLEEaVDESAECFDAVVASEVVEHVSHLEMFIQCCYQVLKPGGsLFITTVN 196
Cdd:COG4976    88 GVYDRLL-------VADLAD-LAEPDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGG-LFIFSVE 145
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
89-194 3.77e-17

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 76.89  E-value: 3.77e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456  89 GMKILDVGCGGGLLTEPL-GRLGASVVGIDPVAENIKIAQhHKSFDPVLDKRIQYKVCSLEEAVDEsaECFDAVVASEVV 167
Cdd:COG2230    52 GMRVLDIGCGWGGLALYLaRRYGVRVTGVTLSPEQLEYAR-ERAAEAGLADRVEVRLADYRDLPAD--GQFDAIVSIGMF 128
                          90       100
                  ....*....|....*....|....*....
gi 1907155456 168 EHVS--HLEMFIQCCYQVLKPGGSLFITT 194
Cdd:COG2230   129 EHVGpeNYPAYFAKVARLLKPGGRLLLHT 157
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
91-195 6.56e-16

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: 72.08  E-value: 6.56e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456  91 KILDVGCGGGLLTEPLGRL-GASVVGIDPVAENIKIAQhhKSFDPVLDKRIQYKVCSLEEAVDESAECFDAVVASEVVEH 169
Cdd:cd02440     1 RVLDLGCGTGALALALASGpGARVTGVDISPVALELAR--KAAAALLADNVEVLKGDAEELPPEADESFDVIISDPPLHH 78
                          90       100
                  ....*....|....*....|....*..
gi 1907155456 170 VSHLEM-FIQCCYQVLKPGGSLFITTV 195
Cdd:cd02440    79 LVEDLArFLEEARRLLKPGGVLVLTLV 105
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
93-190 1.04e-15

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 71.24  E-value: 1.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456  93 LDVGCGGGLLTEPLGRL--GASVVGIDPVAENIKIA-QHHKSFDPVLDKRIQYKVCSLEEAVDESaecFDAVVASEVVEH 169
Cdd:pfam08242   1 LEIGCGTGTLLRALLEAlpGLEYTGLDISPAALEAArERLAALGLLNAVRVELFQLDLGELDPGS---FDVVVASNVLHH 77
                          90       100
                  ....*....|....*....|.
gi 1907155456 170 VSHLEMFIQCCYQVLKPGGSL 190
Cdd:pfam08242  78 LADPRAVLRNIRRLLKPGGVL 98
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
89-194 1.73e-15

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 70.62  E-value: 1.73e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456  89 GMKILDVGCGGGLLTEPLGRL--GASVVGIDPVAENIKIAQHHKSfdpvldkRIQYKVCSLEEAvdESAECFDAVVASEV 166
Cdd:COG4106     2 PRRVLDLGCGTGRLTALLAERfpGARVTGVDLSPEMLARARARLP-------NVRFVVADLRDL--DPPEPFDLVVSNAA 72
                          90       100
                  ....*....|....*....|....*...
gi 1907155456 167 VEHVSHLEMFIQCCYQVLKPGGSLFITT 194
Cdd:COG4106    73 LHWLPDHAALLARLAAALAPGGVLAVQV 100
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
87-169 9.92e-11

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 60.62  E-value: 9.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456  87 LSGMKILDVGCGGGLLTEPLGRLGASVVGIDPVAENIKIAQHHKSFDPVlDKRIQYKVCSLEEAvdesAECFDAVVASEV 166
Cdd:PRK07580   62 LTGLRILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEARERAPEAGL-AGNITFEVGDLESL----LGRFDTVVCLDV 136

                  ...
gi 1907155456 167 VEH 169
Cdd:PRK07580  137 LIH 139
PRK08317 PRK08317
hypothetical protein; Provisional
89-192 1.52e-10

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 60.34  E-value: 1.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456  89 GMKILDVGCGGGLLTEPLGRL---GASVVGIDPVAENIKIAQHHKSFDPVldkRIQYkVCSLEEAVDESAECFDAVVASE 165
Cdd:PRK08317   20 GDRVLDVGCGPGNDARELARRvgpEGRVVGIDRSEAMLALAKERAAGLGP---NVEF-VRGDADGLPFPDGSFDAVRSDR 95
                          90       100
                  ....*....|....*....|....*..
gi 1907155456 166 VVEHVSHLEMFIQCCYQVLKPGGSLFI 192
Cdd:PRK08317   96 VLQHLEDPARALAEIARVLRPGGRVVV 122
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
89-195 1.65e-10

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: 60.42  E-value: 1.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456  89 GMKILDVGCG-GGLLTEPLGRLGASVVGIDPVAENIKIAQhhKSFDPV-LDKRIQYKVCSLEEaVDESaecFDAVVASEV 166
Cdd:pfam02353  62 GMTLLDIGCGwGGLMRRAAERYDVNVVGLTLSKNQYKLAR--KRVAAEgLARKVEVLLQDYRD-FDEP---FDRIVSVGM 135
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1907155456 167 VEHVSH--LEMFIQCCYQVLKPGGSLFITTV 195
Cdd:pfam02353 136 FEHVGHenYDTFFKKLYNLLPPGGLMLLHTI 166
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
88-196 5.49e-10

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 57.04  E-value: 5.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456  88 SGMKILDVGCGGGLLTEPLGRL---GASVVGIDPVAENIKIAQHHKSFDPVldKRIQYKVCSLEEA-VDESAECFDAVVA 163
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEElgpNAEVVGIDISEEAIEKARENAQKLGF--DNVEFEQGDIEELpELLEDDKFDVVIS 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1907155456 164 SEVVEHVSHLEMFIQCCYQVLKPGGSLFITTVN 196
Cdd:pfam13847  81 NCVLNHIPDPDKVLQEILRVLKPGGRLIISDPD 113
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
86-256 6.61e-07

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: 49.18  E-value: 6.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456  86 PLSGMKILDVGCGGGLLTEPLGRLG---ASVVGIDPVAENIKIAQHHKSfdpvLDKRIQYKVCSLEEAVDESAEcFDAVV 162
Cdd:TIGR01934  37 VFKGQKVLDVACGTGDLAIELAKSApdrGKVTGVDFSSEMLEVAKKKSE----LPLNIEFIQADAEALPFEDNS-FDAVT 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456 163 ASEVVEHVSHLEMFIQCCYQVLKPGGSLFI---TTVNKTQLS-----YALGIVfaEQIAGIVPKGTH--TW-----EKFV 227
Cdd:TIGR01934 112 IAFGLRNVTDIQKALREMYRVLKPGGRLVIlefSKPANALLKkfykfYLKNVL--PSIGGLISKNAEayTYlpesiRAFP 189
                         170       180
                  ....*....|....*....|....*....
gi 1907155456 228 SPEKLESILEPNGLsvetvAGLVYNPFSG 256
Cdd:TIGR01934 190 SQEELAAMLKEAGF-----EEVRYRSLTF 213
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
88-201 7.44e-07

tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 N-methylase Trm61 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442009 [Multi-domain]  Cd Length: 249  Bit Score: 49.39  E-value: 7.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456  88 SGMKILDVGCGGGLLTEPLGR-LGAS--VVGIDPVAENIKIAQHH-KSFDpvLDKRIQYKVCSLEEAVDESAecFDAVVA 163
Cdd:COG2519    91 PGARVLEAGTGSGALTLALARaVGPEgkVYSYERREDFAEIARKNlERFG--LPDNVELKLGDIREGIDEGD--VDAVFL 166
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1907155456 164 S-----EVVEHVshlemfiqccYQVLKPGGSL--FITTVNktQLS 201
Cdd:COG2519   167 DmpdpwEALEAV----------AKALKPGGVLvaYVPTVN--QVS 199
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
86-256 1.15e-06

bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 48.61  E-value: 1.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456  86 PLSGMKILDVGCGGGLLTEPLGRLG---ASVVGIDPVAENIKIAQhHKSFDPVLDKRIQYKVCSLEE---AvDESaecFD 159
Cdd:PRK00216   49 VRPGDKVLDLACGTGDLAIALAKAVgktGEVVGLDFSEGMLAVGR-EKLRDLGLSGNVEFVQGDAEAlpfP-DNS---FD 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456 160 AVVAS----EVVEHVSHL-EMfiqccYQVLKPGGSLFI---TTVNKTQLS-----YALGIV--FAEQIAG-------IVP 217
Cdd:PRK00216  124 AVTIAfglrNVPDIDKALrEM-----YRVLKPGGRLVIlefSKPTNPPLKkaydfYLFKVLplIGKLISKnaeaysyLAE 198
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1907155456 218 kgthTWEKFVSPEKLESILEPNGLSVETvaglvYNPFSG 256
Cdd:PRK00216  199 ----SIRAFPDQEELAAMLEEAGFERVR-----YRNLTG 228
COG4627 COG4627
Predicted SAM-depedendent methyltransferase [General function prediction only];
157-194 1.66e-06

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


Pssm-ID: 443666 [Multi-domain]  Cd Length: 161  Bit Score: 47.17  E-value: 1.66e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1907155456 157 CFDAVVASEVVEHVSHLEM--FIQCCYQVLKPGGSLFITT 194
Cdd:COG4627    46 SVDAIYSSHVLEHLDYEEAplALKECYRVLKPGGILRIVV 85
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
87-193 4.57e-06

Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal protein L11 methyltransferase (EC:2.1.1.-) sequences.


Pssm-ID: 428888 [Multi-domain]  Cd Length: 294  Bit Score: 47.26  E-value: 4.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456  87 LSGMKILDVGCGGGLLTEPLGRLGA-SVVG--IDPVAenIKIAQHHKSFDPVlDKRIQYKVcsLEEAVDESaecFDAVVA 163
Cdd:pfam06325 160 KPGESVLDVGCGSGILAIAALKLGAkKVVGvdIDPVA--VRAAKENAELNGV-EARLEVYL--PGDLPKEK---ADVVVA 231
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1907155456 164 ---SEVvehvshLEMFIQCCYQVLKPGGsLFIT 193
Cdd:pfam06325 232 nilADP------LIELAPDIYALVKPGG-YLIL 257
PRK14968 PRK14968
putative methyltransferase; Provisional
89-199 1.32e-05

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 44.89  E-value: 1.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456  89 GMKILDVGCGGGLLTEPLGRLGASVVGID--PVAenIKIAQHHKSFDPVLDKRIQYKVCSLEEAVDesAECFDAVV---- 162
Cdd:PRK14968   24 GDRVLEVGTGSGIVAIVAAKNGKKVVGVDinPYA--VECAKCNAKLNNIRNNGVEVIRSDLFEPFR--GDKFDVILfnpp 99
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907155456 163 ---ASEVVEHVSHLEM--------------FIQCCYQVLKPGGSLFI-----TTVNKTQ 199
Cdd:PRK14968  100 ylpTEEEEEWDDWLNYalsggkdgrevidrFLDEVGRYLKPGGRILLlqsslTGEDEVL 158
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
91-194 1.71e-05

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: 45.36  E-value: 1.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456  91 KILDVGCGGGLLTEPLGRLG--ASVVGIDPVAENIKIAQHHKSfdpvldKRIQYkVCSLEEAVDESAECFDAVVASEVVE 168
Cdd:TIGR02072  37 SVLDIGCGTGYLTRALLKRFpqAEFIALDISAGMLAQAKTKLS------ENVQF-ICGDAEKLPLEDSSFDLIVSNLALQ 109
                          90       100
                  ....*....|....*....|....*.
gi 1907155456 169 HVSHLEMFIQCCYQVLKPGGSLFITT 194
Cdd:TIGR02072 110 WCDDLSQALSELARVLKPGGLLAFST 135
PRK11036 PRK11036
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
75-214 2.70e-05

tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;


Pssm-ID: 182918  Cd Length: 255  Bit Score: 44.57  E-value: 2.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456  75 LKTSASHHPGKPLSgmkILDVGCGGGLLTEPLGRLGASVVGIDPVAENIKIAQHHKSFDPVLDKrIQYKVCSLEEAVDES 154
Cdd:PRK11036   34 LDRLLAELPPRPLR---VLDAGGGEGQTAIKLAELGHQVILCDLSAEMIQRAKQAAEAKGVSDN-MQFIHCAAQDIAQHL 109
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456 155 AECFDAVVASEVVEHVSHLEMFIQCCYQVLKPGGSLFITTVNktqlsyALGIVFAEQIAG 214
Cdd:PRK11036  110 ETPVDLILFHAVLEWVADPKSVLQTLWSVLRPGGALSLMFYN------ANGLLMHNMVAG 163
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
81-247 6.49e-05

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 43.60  E-value: 6.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456  81 HHP----------GKPLSGMKILDVGCGGGLLTEPLGRLGA-SVVG--IDPVAenIKIAQHHksfdpvldkrIQYKVCSL 147
Cdd:PRK00517  102 THPttrlclealeKLVLPGKTVLDVGCGSGILAIAAAKLGAkKVLAvdIDPQA--VEAAREN----------AELNGVEL 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456 148 EEAVDESAECFDAVVA---SEVvehvshLEMFIQCCYQVLKPGGSLFittvnktqLSyalGIVfAEQIagivpkgthtwe 224
Cdd:PRK00517  170 NVYLPQGDLKADVIVAnilANP------LLELAPDLARLLKPGGRLI--------LS---GIL-EEQA------------ 219
                         170       180
                  ....*....|....*....|...
gi 1907155456 225 kfvspEKLESILEPNGLSVETVA 247
Cdd:PRK00517  220 -----DEVLEAYEEAGFTLDEVL 237
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
86-247 7.72e-05

Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 43.62  E-value: 7.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456  86 PLSGMKILDVGCGGGLLTepLG--RLGAS-VVG--IDPVA-----ENIKIAQhhksfdpvLDKRIQykvcsLEEAVDESA 155
Cdd:COG2264   146 LKPGKTVLDVGCGSGILA--IAaaKLGAKrVLAvdIDPVAveaarENAELNG--------VEDRIE-----VVLGDLLED 210
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456 156 ECFDAVVA---SEVvehvshLEMFIQCCYQVLKPGGSLFittvnktqLSyalGIVfAEQIagivpkgthtwekfvspEKL 232
Cdd:COG2264   211 GPYDLVVAnilANP------LIELAPDLAALLKPGGYLI--------LS---GIL-EEQA-----------------DEV 255
                         170
                  ....*....|....*
gi 1907155456 233 ESILEPNGLSVETVA 247
Cdd:COG2264   256 LAAYEAAGFELVERR 270
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
85-193 1.49e-04

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 43.20  E-value: 1.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456  85 KPlsGMKILDVGCG-GG---LLTEplgRLGASVVGIDPVAENIKIAqhhksfdpvLDKRIQYKvCSLEEAVdesAEC--- 157
Cdd:PLN02336  265 KP--GQKVLDVGCGiGGgdfYMAE---NFDVHVVGIDLSVNMISFA---------LERAIGRK-CSVEFEV---ADCtkk 326
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1907155456 158 ------FDAVVASEVVEHVSHLEMFIQCCYQVLKPGGSLFIT 193
Cdd:PLN02336  327 typdnsFDVIYSRDTILHIQDKPALFRSFFKWLKPGGKVLIS 368
PRK15068 PRK15068
tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB;
86-194 1.55e-04

tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB;


Pssm-ID: 237898  Cd Length: 322  Bit Score: 42.92  E-value: 1.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456  86 PLSGMKILDVGCGGGL-LTEPLGRLGASVVGIDPVaenikiAQHHKSFDPV-----LDKRIQYKVCSLEEAvdESAECFD 159
Cdd:PRK15068  120 PLKGRTVLDVGCGNGYhMWRMLGAGAKLVVGIDPS------QLFLCQFEAVrkllgNDQRAHLLPLGIEQL--PALKAFD 191
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907155456 160 AVVASEVVEH-VSHLEMFIQcCYQVLKPGGSLFITT 194
Cdd:PRK15068  192 TVFSMGVLYHrRSPLDHLKQ-LKDQLVPGGELVLET 226
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
91-193 2.86e-04

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 41.88  E-value: 2.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456  91 KILDVGCG-GGLLTEPLGRLGASVVGIDPVAENIKIAQhhksfdpvldKRIQYKVCSLEEAVD----ESAEC-FDAVVAS 164
Cdd:PTZ00098   55 KVLDIGSGlGGGCKYINEKYGAHVHGVDICEKMVNIAK----------LRNSDKNKIEFEANDilkkDFPENtFDMIYSR 124
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1907155456 165 EVVEHVSHLE--MFIQCCYQVLKPGGSLFIT 193
Cdd:PTZ00098  125 DAILHLSYADkkKLFEKCYKWLKPNGILLIT 155
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
86-190 4.43e-04

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 40.89  E-value: 4.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456  86 PLSGMKILDVGCGGGLLTEPLGRL-GAS--VVGIDPVAENIKIAQhhKSFDPVLDKRIQYkVCSLEEAVDESAECFDAVV 162
Cdd:pfam01209  40 VKRGNKFLDVAGGTGDWTFGLSDSaGSSgkVVGLDINENMLKEGE--KKAKEEGKYNIEF-LQGNAEELPFEDDSFDIVT 116
                          90       100
                  ....*....|....*....|....*...
gi 1907155456 163 ASEVVEHVSHLEMFIQCCYQVLKPGGSL 190
Cdd:pfam01209 117 ISFGLRNFPDYLKVLKEAFRVLKPGGRV 144
PRK06202 PRK06202
hypothetical protein; Provisional
83-171 6.42e-04

hypothetical protein; Provisional


Pssm-ID: 180466 [Multi-domain]  Cd Length: 232  Bit Score: 40.37  E-value: 6.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456  83 PGKPLSgmkILDVGCGGGLLTEPLGRLGA------SVVGIDPVAENIKIAQHHksfdpVLDKRIQYKVCSLEEAVDESaE 156
Cdd:PRK06202   58 ADRPLT---LLDIGCGGGDLAIDLARWARrdglrlEVTAIDPDPRAVAFARAN-----PRRPGVTFRQAVSDELVAEG-E 128
                          90
                  ....*....|....*
gi 1907155456 157 CFDAVVASEVVEHVS 171
Cdd:PRK06202  129 RFDVVTSNHFLHHLD 143
Methyltransf_15 pfam09445
RNA cap guanine-N2 methyltransferase; RNA cap guanine-N2 methyltransferases such as ...
91-164 6.89e-04

RNA cap guanine-N2 methyltransferase; RNA cap guanine-N2 methyltransferases such as Schizosaccharomyces pombe Tgs1 and Giardia lamblia Tgs2 catalyze methylation of the exocyclic N2 amine of 7-methylguanosine.


Pssm-ID: 370496  Cd Length: 165  Bit Score: 39.62  E-value: 6.89e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907155456  91 KILDVGCGGGLLTEPLGRLGASVVGIDPVAENIKIAQHHKSFDPVLDkRIQYKVCSLEEAVD---ESAECFDAVVAS 164
Cdd:pfam09445   3 RILDVFCGGGGNTIQFANVFDSVISIDINLEHLACAQHNAEVYGVSD-RIWLIHGDWFELLAklkFEKIKYDCVFAS 78
PRK11705 PRK11705
cyclopropane fatty acyl phospholipid synthase;
89-201 8.65e-04

cyclopropane fatty acyl phospholipid synthase;


Pssm-ID: 183282  Cd Length: 383  Bit Score: 40.60  E-value: 8.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456  89 GMKILDVGCG-GGLLTEPLGRLGASVVGIDPVAENIKIAQHHKSFDPVlDKRIQ-YKvcsleeAVDESaecFDAVVASEV 166
Cdd:PRK11705  168 GMRVLDIGCGwGGLARYAAEHYGVSVVGVTISAEQQKLAQERCAGLPV-EIRLQdYR------DLNGQ---FDRIVSVGM 237
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1907155456 167 VEHVSH--LEMFIQCCYQVLKPGGSLFITTV--NKTQLS 201
Cdd:PRK11705  238 FEHVGPknYRTYFEVVRRCLKPDGLFLLHTIgsNKTDTN 276
Methyltransf_9 pfam08003
Protein of unknown function (DUF1698); This family contains many hypothetical proteins. It ...
86-194 9.28e-04

Protein of unknown function (DUF1698); This family contains many hypothetical proteins. It also includes two putative methyltransferase proteins, Swiss:Q8EEE6 and Swiss:Q88MX8.


Pssm-ID: 429781 [Multi-domain]  Cd Length: 315  Bit Score: 40.47  E-value: 9.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456  86 PLSGMKILDVGCGGGL-LTEPLGRLGASVVGIDPVaenikiAQHHKSFDPV-----LDKRIQYKVCSLEEAvdESAECFD 159
Cdd:pfam08003 113 PLKGRTILDVGCGNGYhMWRMLGEGAAMVVGIDPS------ELFLCQFEAVrkllgNDQRAHLLPLGIEQL--PALAAFD 184
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907155456 160 AVVASEVVEH-VSHLEMFIQCCYQvLKPGGSLFITT 194
Cdd:pfam08003 185 TVFSMGVLYHrRSPLDHLLQLKDQ-LVKGGELVLET 219
PLN02244 PLN02244
tocopherol O-methyltransferase
50-194 1.28e-03

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 40.11  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456  50 WDEY---GKFAPLHSMNDLRVPFIR--DNLLKTSAShhPGKPLSGMK-ILDVGCGGGLLTEPLGR-LGASVVGI--DPV- 119
Cdd:PLN02244   76 WGEHmhhGYYDPGASRGDHRQAQIRmiEESLAWAGV--PDDDEKRPKrIVDVGCGIGGSSRYLARkYGANVKGItlSPVq 153
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907155456 120 ---AENIKIAQHhksfdpvLDKRIQYKVC-SLEEAVDESaeCFDAVVASEVVEHVSHLEMFIQCCYQVLKPGGSLFITT 194
Cdd:PLN02244  154 aarANALAAAQG-------LSDKVSFQVAdALNQPFEDG--QFDLVWSMESGEHMPDKRKFVQELARVAAPGGRIIIVT 223
PRK06922 PRK06922
class I SAM-dependent methyltransferase;
87-192 2.28e-03

class I SAM-dependent methyltransferase;


Pssm-ID: 180751 [Multi-domain]  Cd Length: 677  Bit Score: 39.47  E-value: 2.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907155456  87 LSGMKILDVGCGGG----LLTEPLGRlgASVVGIDpVAENI------KIAQHHKSFDPvldkrIQYKVCSLEEAVDEsaE 156
Cdd:PRK06922  417 IKGDTIVDVGAGGGvmldMIEEETED--KRIYGID-ISENVidtlkkKKQNEGRSWNV-----IKGDAINLSSSFEK--E 486
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1907155456 157 CFDAVVASEVV-EHVSHLEM------------FIQCCYQVLKPGGSLFI 192
Cdd:PRK06922  487 SVDTIVYSSILhELFSYIEYegkkfnhevikkGLQSAYEVLKPGGRIII 535
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
86-137 7.88e-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: 37.25  E-value: 7.88e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907155456  86 PLSGMKILDVGCG--GGLLTEPLGRLGAS-VVGIDPVAENIKIAQHHKSFDPVLD 137
Cdd:cd08255    95 PRLGERVAVVGLGlvGLLAAQLAKAAGAReVVGVDPDAARRELAEALGPADPVAA 149
 
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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