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Conserved domains on  [gi|189037623|sp|A9M0C4|]
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RecName: Full=Ubiquinone biosynthesis O-methyltransferase; AltName: Full=2-polyprenyl-6-hydroxyphenol methylase; AltName: Full=3-demethylubiquinone 3-O-methyltransferase

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

CATH:  3.40.50.150
EC:  2.1.1.222|2.1.1.64
Gene Ontology:  GO:0102208|GO:0008425|GO:0032259|GO:0006744
PubMed:  10419476|11583838

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 ...
 12-231 6.45e-133

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: 373.17  E-value: 6.45e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623   12 EIAKFSRIADKWWDKSGEFKTLHDINPLRLDYIDGHA------DLRGKRVLDVGCGGGILAESMARRGAAfVKGIDMAEQ 85
Cdd:TIGR01983   1 EIAKFSALAHEWWDPNGKFKPLHKMNPLRLDYIRDRIrknfknPLDGLRVLDVGCGGGLLSEPLARLGAN-VTGIDASEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623   86 SLETARLHAALNNVAdIEYECIRVEDLAEAEPHSFDVVTCMEMMEHVPDPAAIVRACANLVKPDGMVFFSTINKNPKSYL 165
Cdd:TIGR01983  80 NIEVAKLHAKKDPLQ-IDYRCTTVEDLAEKKAGSFDVVTCMEVLEHVPDPQAFIRACAQLLKPGGILFFSTINRTPKSYL 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 189037623  166 HLIVAAEYLLKFVPKGTHDWKKFIAPAELARMCRQAGLDVADTKGMTYHVLSQTYALCDSTDVNYM 231
Cdd:TIGR01983 159 LAIVGAEYILRIVPKGTHDWEKFIKPSELLSWLESAGLRVKDIKGLVYNPIKNTWKLSKDTDVNYM 224
 
Name Accession Description Interval E-value
UbiG TIGR01983
ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase ...
 12-231 6.45e-133

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: 373.17  E-value: 6.45e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623   12 EIAKFSRIADKWWDKSGEFKTLHDINPLRLDYIDGHA------DLRGKRVLDVGCGGGILAESMARRGAAfVKGIDMAEQ 85
Cdd:TIGR01983   1 EIAKFSALAHEWWDPNGKFKPLHKMNPLRLDYIRDRIrknfknPLDGLRVLDVGCGGGLLSEPLARLGAN-VTGIDASEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623   86 SLETARLHAALNNVAdIEYECIRVEDLAEAEPHSFDVVTCMEMMEHVPDPAAIVRACANLVKPDGMVFFSTINKNPKSYL 165
Cdd:TIGR01983  80 NIEVAKLHAKKDPLQ-IDYRCTTVEDLAEKKAGSFDVVTCMEVLEHVPDPQAFIRACAQLLKPGGILFFSTINRTPKSYL 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 189037623  166 HLIVAAEYLLKFVPKGTHDWKKFIAPAELARMCRQAGLDVADTKGMTYHVLSQTYALCDSTDVNYM 231
Cdd:TIGR01983 159 LAIVGAEYILRIVPKGTHDWEKFIKPSELLSWLESAGLRVKDIKGLVYNPIKNTWKLSKDTDVNYM 224
PLN02396 PLN02396
hexaprenyldihydroxybenzoate methyltransferase
 7-231 3.18e-67

hexaprenyldihydroxybenzoate methyltransferase


Pssm-ID: 178018 [Multi-domain]  Cd Length: 322  Bit Score: 210.36  E-value: 3.18e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623   7 NVDEGEIAKFSRIADKWWDKSGEFKTLHDINPLRLDYI------------DGHADLRGKRVLDVGCGGGILAESMARRGA 74
Cdd:PLN02396  75 SLNEDELAKFSAIADTWWHSEGPFKPLHQMNPTRLAFIrstlcrhfskdpSSAKPFEGLKFIDIGCGGGLLSEPLARMGA 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623  75 AfVKGIDMAEQSLETARLHAALNNV-ADIEYECIRVEDLAEaEPHSFDVVTCMEMMEHVPDPAAIVRACANLVKPDGMVF 153
Cdd:PLN02396 155 T-VTGVDAVDKNVKIARLHADMDPVtSTIEYLCTTAEKLAD-EGRKFDAVLSLEVIEHVANPAEFCKSLSALTIPNGATV 232

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189037623 154 FSTINKNPKSYLHLIVAAEYLLKFVPKGTHDWKKFIAPAELARMCRQAGLDVADTKGMTYHVLSQTYALCDSTDVNYM 231
Cdd:PLN02396 233 LSTINRTMRAYASTIVGAEYILRWLPKGTHQWSSFVTPEELSMILQRASVDVKEMAGFVYNPITGRWLLSDDISVNYI 310
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 17-158 1.85e-39

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: 132.45  E-value: 1.85e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623  17 SRIADKWWDKsgefktlhdinplRLDYIDGHADLRGKRVLDVGCGGGILAESMARRGAAfVKGIDMAEQSLETARLHAAL 96
Cdd:COG2227    3 DPDARDFWDR-------------RLAALLARLLPAGGRVLDVGCGTGRLALALARRGAD-VTGVDISPEALEIARERAAE 68

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 189037623  97 NNvadIEYECIRVEDLAeAEPHSFDVVTCMEMMEHVPDPAAIVRACANLVKPDGMVFFSTIN 158
Cdd:COG2227   69 LN---VDFVQGDLEDLP-LEDGSFDLVICSEVLEHLPDPAALLRELARLLKPGGLLLLSTPN 126
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 55-150 1.35e-23

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 90.70  E-value: 1.35e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623   55 VLDVGCGGGILAESMARRGAAFVKGIDMAEQSLETARLHAALNNVaDIEYECIRVEDLaEAEPHSFDVVTCMEMMEHVPD 134
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGL-NVEFVQGDAEDL-PFPDGSFDLVVSSGVLHHLPD 78

                          90
                  ....*....|....*...
gi 189037623  135 P--AAIVRACANLVKPDG 150
Cdd:pfam13649  79 PdlEAALREIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 54-155 9.38e-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: 70.54  E-value: 9.38e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623  54 RVLDVGCGGGILAESMARRGAAFVKGIDMAEQSLETARLHAALNNVADIEYECIRVEDLAEAEPHSFDVVTC-MEMMEHV 132
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPEADESFDVIISdPPLHHLV 80

                         90       100
                 ....*....|....*....|...
gi 189037623 133 PDPAAIVRACANLVKPDGMVFFS 155
Cdd:cd02440   81 EDLARFLEEARRLLKPGGVLVLT 103
 
Name Accession Description Interval E-value
UbiG TIGR01983
ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase ...
 12-231 6.45e-133

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: 373.17  E-value: 6.45e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623   12 EIAKFSRIADKWWDKSGEFKTLHDINPLRLDYIDGHA------DLRGKRVLDVGCGGGILAESMARRGAAfVKGIDMAEQ 85
Cdd:TIGR01983   1 EIAKFSALAHEWWDPNGKFKPLHKMNPLRLDYIRDRIrknfknPLDGLRVLDVGCGGGLLSEPLARLGAN-VTGIDASEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623   86 SLETARLHAALNNVAdIEYECIRVEDLAEAEPHSFDVVTCMEMMEHVPDPAAIVRACANLVKPDGMVFFSTINKNPKSYL 165
Cdd:TIGR01983  80 NIEVAKLHAKKDPLQ-IDYRCTTVEDLAEKKAGSFDVVTCMEVLEHVPDPQAFIRACAQLLKPGGILFFSTINRTPKSYL 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 189037623  166 HLIVAAEYLLKFVPKGTHDWKKFIAPAELARMCRQAGLDVADTKGMTYHVLSQTYALCDSTDVNYM 231
Cdd:TIGR01983 159 LAIVGAEYILRIVPKGTHDWEKFIKPSELLSWLESAGLRVKDIKGLVYNPIKNTWKLSKDTDVNYM 224
PLN02396 PLN02396
hexaprenyldihydroxybenzoate methyltransferase
 7-231 3.18e-67

hexaprenyldihydroxybenzoate methyltransferase


Pssm-ID: 178018 [Multi-domain]  Cd Length: 322  Bit Score: 210.36  E-value: 3.18e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623   7 NVDEGEIAKFSRIADKWWDKSGEFKTLHDINPLRLDYI------------DGHADLRGKRVLDVGCGGGILAESMARRGA 74
Cdd:PLN02396  75 SLNEDELAKFSAIADTWWHSEGPFKPLHQMNPTRLAFIrstlcrhfskdpSSAKPFEGLKFIDIGCGGGLLSEPLARMGA 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623  75 AfVKGIDMAEQSLETARLHAALNNV-ADIEYECIRVEDLAEaEPHSFDVVTCMEMMEHVPDPAAIVRACANLVKPDGMVF 153
Cdd:PLN02396 155 T-VTGVDAVDKNVKIARLHADMDPVtSTIEYLCTTAEKLAD-EGRKFDAVLSLEVIEHVANPAEFCKSLSALTIPNGATV 232

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189037623 154 FSTINKNPKSYLHLIVAAEYLLKFVPKGTHDWKKFIAPAELARMCRQAGLDVADTKGMTYHVLSQTYALCDSTDVNYM 231
Cdd:PLN02396 233 LSTINRTMRAYASTIVGAEYILRWLPKGTHQWSSFVTPEELSMILQRASVDVKEMAGFVYNPITGRWLLSDDISVNYI 310
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 17-158 1.85e-39

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: 132.45  E-value: 1.85e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623  17 SRIADKWWDKsgefktlhdinplRLDYIDGHADLRGKRVLDVGCGGGILAESMARRGAAfVKGIDMAEQSLETARLHAAL 96
Cdd:COG2227    3 DPDARDFWDR-------------RLAALLARLLPAGGRVLDVGCGTGRLALALARRGAD-VTGVDISPEALEIARERAAE 68

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 189037623  97 NNvadIEYECIRVEDLAeAEPHSFDVVTCMEMMEHVPDPAAIVRACANLVKPDGMVFFSTIN 158
Cdd:COG2227   69 LN---VDFVQGDLEDLP-LEDGSFDLVICSEVLEHLPDPAALLRELARLLKPGGLLLLSTPN 126
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 44-171 1.20e-23

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: 92.36  E-value: 1.20e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623  44 IDGHADLRGKRVLDVGCGGGILAESMARRGAAFVkGIDMAEQSLETARLHAALNNVaDIEYECIRVEDLaEAEPHSFDVV 123
Cdd:COG2226   15 LAALGLRPGARVLDLGCGTGRLALALAERGARVT-GVDISPEMLELARERAAEAGL-NVEFVVGDAEDL-PFPDGSFDLV 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 189037623 124 TCMEMMEHVPDPAAIVRACANLVKPDGMVFFSTINKNPKSYLHLIVAA 171
Cdd:COG2226   92 ISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELEELLAE 139
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 55-150 1.35e-23

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 90.70  E-value: 1.35e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623   55 VLDVGCGGGILAESMARRGAAFVKGIDMAEQSLETARLHAALNNVaDIEYECIRVEDLaEAEPHSFDVVTCMEMMEHVPD 134
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGL-NVEFVQGDAEDL-PFPDGSFDLVVSSGVLHHLPD 78

                          90
                  ....*....|....*...
gi 189037623  135 P--AAIVRACANLVKPDG 150
Cdd:pfam13649  79 PdlEAALREIARVLKPGG 96
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 23-156 2.94e-22

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 89.22  E-value: 2.94e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623  23 WWDK-----SGEFK----TLHDINPLRLDYIDGHADLR-GKRVLDVGCGGGILAESMARRGAAFVKGIDMAEQSLETARL 92
Cdd:COG2230   13 FLDPtmtysCAYFEdpddTLEEAQEAKLDLILRKLGLKpGMRVLDIGCGWGGLALYLARRYGVRVTGVTLSPEQLEYARE 92

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189037623  93 HAALNNVAD-IEYECIRVEDLAEAEPhsFDVVTCMEMMEHVPDP--AAIVRACANLVKPDGMVFFST 156
Cdd:COG2230   93 RAAEAGLADrVEVRLADYRDLPADGQ--FDAIVSIGMFEHVGPEnyPAYFAKVARLLKPGGRLLLHT 157
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 51-205 4.03e-22

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 89.02  E-value: 4.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623   51 RGKRVLDVGCGGGILAESMARRGAAFVkGIDmaeqSLETARLHAALNNVADIEYEcirveDLAEAEPHSFDVVTCMEMME 130
Cdd:pfam13489  22 SPGRVLDFGCGTGIFLRLLRAQGFSVT-GVD----PSPIAIERALLNVRFDQFDE-----QEAAVPAGKFDVIVAREVLE 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189037623  131 HVPDPAAIVRACANLVKPDGMVFFSTINknpkSYLHLIVAAEYLLKFVPKGTHDWkkFIAPAELARMCRQAGLDV 205
Cdd:pfam13489  92 HVPDPPALLRQIAALLKPGGLLLLSTPL----ASDEADRLLLEWPYLRPRNGHIS--LFSARSLKRLLEEAGFEV 160
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 56-154 1.16e-20

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 83.10  E-value: 1.16e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623   56 LDVGCGGGILAESMARRGAAFVkGIDMAEQSLETARLHAalnNVADIEYECIRVEDLAEAEpHSFDVVTCMEMMEHVPDP 135
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVT-GVDISPEMLELAREKA---PREGLTFVVGDAEDLPFPD-NSFDLVLSSEVLHHVEDP 75

                          90
                  ....*....|....*....
gi 189037623  136 AAIVRACANLVKPDGMVFF 154
Cdd:pfam08241  76 ERALREIARVLKPGGILII 94
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 23-155 3.89e-19

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 82.27  E-value: 3.89e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623  23 WWDKSGEFKTlhdiNPLRLDYIDGHADL-RGKRVLDVGCGGGILAESMARRGAAFVKGIDMAEQSLETARLHAALNNVAD 101
Cdd:COG0500    1 PWDSYYSDEL----LPGLAALLALLERLpKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAGLGN 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 189037623 102 IEYECIRVEDLAEAEPHSFDVVTCMEMMEHVP--DPAAIVRACANLVKPDGMVFFS 155
Cdd:COG0500   77 VEFLVADLAELDPLPAESFDLVVAFGVLHHLPpeEREALLRELARALKPGGVLLLS 132
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
51-156 4.92e-18

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 76.40  E-value: 4.92e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623  51 RGKRVLDVGCGGGILAESMARR--GAAFVkGIDMAEQSLETARlhaalNNVADIEYECIRVEDLAEAEPhsFDVVTCMEM 128
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALLAERfpGARVT-GVDLSPEMLARAR-----ARLPNVRFVVADLRDLDPPEP--FDLVVSNAA 72

                         90       100
                 ....*....|....*....|....*...
gi 189037623 129 MEHVPDPAAIVRACANLVKPDGMVFFST 156
Cdd:COG4106   73 LHWLPDHAALLARLAAALAPGGVLAVQV 100
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
6-205 2.77e-17

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 76.58  E-value: 2.77e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623   6 YNVDEGEIAKFSRIADKWWDKSGEfkTLHDINPLRL--DYIDGHADLRGKRVLDVGCGGGILAESMARRGAAFVkGIDMA 83
Cdd:COG4976    1 MALDAYVEALFDQYADSYDAALVE--DLGYEAPALLaeELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLT-GVDLS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623  84 EQSLETARLHAAlnnvaDIEYECIRVEDLAEaEPHSFDVVTCMEMMEHVPDPAAIVRACANLVKPDGMVFFSTINKNPKS 163
Cdd:COG4976   78 EEMLAKAREKGV-----YDRLLVADLADLAE-PDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGGLFIFSVEDADGSG 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 189037623 164 -YLHlivaaeyllkfvpkgthdwkkfiAPAELARMCRQAGLDV 205
Cdd:COG4976  152 rYAH-----------------------SLDYVRDLLAAAGFEV 171
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
41-155 1.36e-16

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 76.75  E-value: 1.36e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623  41 LDYIDGHaDLRGKRVLDVGCGGGILAESMARRGAAFVKGIDMAEQSLETARLHAALNNVADIeyecIRVE--DLAEAEPh 118
Cdd:COG2264  139 LEALEKL-LKPGKTVLDVGCGSGILAIAAAKLGAKRVLAVDIDPVAVEAARENAELNGVEDR----IEVVlgDLLEDGP- 212

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 189037623 119 sFDVVTC-------MEMMEHVpdpaaivracANLVKPDGMVFFS 155
Cdd:COG2264  213 -YDLVVAnilanplIELAPDL----------AALLKPGGYLILS 245
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 54-155 9.38e-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: 70.54  E-value: 9.38e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623  54 RVLDVGCGGGILAESMARRGAAFVKGIDMAEQSLETARLHAALNNVADIEYECIRVEDLAEAEPHSFDVVTC-MEMMEHV 132
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPEADESFDVIISdPPLHHLV 80

                         90       100
                 ....*....|....*....|...
gi 189037623 133 PDPAAIVRACANLVKPDGMVFFS 155
Cdd:cd02440   81 EDLARFLEEARRLLKPGGVLVLT 103
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
41-157 1.52e-15

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 73.26  E-value: 1.52e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623  41 LDYIDGHaDLRGKRVLDVGCGGGILAESMARRGAAFVKGIDMAEQSLETARLHAALNNVADIEYecirvedLAEAEPhSF 120
Cdd:PRK00517 110 LEALEKL-VLPGKTVLDVGCGSGILAIAAAKLGAKKVLAVDIDPQAVEAARENAELNGVELNVY-------LPQGDL-KA 180

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 189037623 121 DVVTC-------MEMMEHVpdpaaivracANLVKPDGMVFFSTI 157
Cdd:PRK00517 181 DVIVAnilanplLELAPDL----------ARLLKPGGRLILSGI 214
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 41-145 3.00e-15

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 72.18  E-value: 3.00e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623  41 LDYIDGHADLRGKRVLDVGCGGGILAESMARRGAAfVKGIDMAEQSLETA--RLHAALNNvADIEYeciRVEDLaeaEPH 118
Cdd:PRK07580  53 LSWLPADGDLTGLRILDAGCGVGSLSIPLARRGAK-VVASDISPQMVEEAreRAPEAGLA-GNITF---EVGDL---ESL 124

                         90       100
                 ....*....|....*....|....*....
gi 189037623 119 S--FDVVTCMEMMEHVPDPAAiVRACANL 145
Cdd:PRK07580 125 LgrFDTVVCLDVLIHYPQEDA-ARMLAHL 152
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 56-152 1.85e-14

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 67.01  E-value: 1.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623   56 LDVGCGGGILAESMAR--RGAAFVkGIDMAEQSLETARLHAALNNVADIEYECIRVEDLAEAEPHSFDVVTCMEMMEHVP 133
Cdd:pfam08242   1 LEIGCGTGTLLRALLEalPGLEYT-GLDISPAALEAARERLAALGLLNAVRVELFQLDLGELDPGSFDVVVASNVLHHLA 79

                          90
                  ....*....|....*....
gi 189037623  134 DPAAIVRACANLVKPDGMV 152
Cdd:pfam08242  80 DPRAVLRNIRRLLKPGGVL 98
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 42-125 3.12e-14

Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443104 [Multi-domain]  Cd Length: 216  Bit Score: 69.14  E-value: 3.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623  42 DYIDGHADLRGKRVLDVGCGGGILAESMARRGAAFVKGIDMAEQSLETARLHAALNNVAdIEYECIRVEDLAEAEphSFD 121
Cdd:COG3897   61 RYLLDHPEVAGKRVLELGCGLGLVGIAAAKAGAADVTATDYDPEALAALRLNAALNGVA-ITTRLGDWRDPPAAG--GFD 137


                 ....
gi 189037623 122 VVTC 125
Cdd:COG3897  138 LILG 141
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 52-188 5.76e-14

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 67.06  E-value: 5.76e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623   52 GKRVLDVGCGGGILAESMARRGA--AFVKGIDMAEQSLETARLHAALNNVADIEYECIRVEDLAEA-EPHSFDVVTCMEM 128
Cdd:pfam13847   4 GMRVLDLGCGTGHLSFELAEELGpnAEVVGIDISEEAIEKARENAQKLGFDNVEFEQGDIEELPELlEDDKFDVVISNCV 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623  129 MEHVPDPAAIVRACANLVKPDGMVFFSTINkNPKSYLHLIVAAEYLLKFVPKGTHDWKKF 188
Cdd:pfam13847  84 LNHIPDPDKVLQEILRVLKPGGRLIISDPD-SLAELPAHVKEDSTYYAGCVGGAILKKKL 142
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 49-157 7.72e-14

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: 69.22  E-value: 7.72e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623   49 DLRGKRVLDVGCGGGILAESMARRGAAFVKGIDMAEQSLETARLHAALNNVADIeyecIRVEDLAEAEPHSFDVVTC--- 125
Cdd:pfam06325 159 VKPGESVLDVGCGSGILAIAALKLGAKKVVGVDIDPVAVRAAKENAELNGVEAR----LEVYLPGDLPKEKADVVVAnil 234

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 189037623  126 ----MEMMEHVpdpaaivracANLVKPDGMVFFSTI 157
Cdd:pfam06325 235 adplIELAPDI----------YALVKPGGYLILSGI 260
RlmK COG1092
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ...
 51-156 1.08e-12

23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure and biogenesis]; 23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 440709 [Multi-domain]  Cd Length: 392  Bit Score: 66.36  E-value: 1.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623  51 RGKRVLDVGC--GG-GILAesmARRGAAFVKGIDMAEQSLETARLHAALNNVADiEYECIR--VEDL---AEAEPHSFDV 122
Cdd:COG1092  216 KGKRVLNLFSytGGfSVHA---AAGGAKSVTSVDLSATALEWAKENAALNGLDD-RHEFVQadAFDWlreLAREGERFDL 291

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 189037623 123 VTCmemmehvpDPAA-----------------IVRACANLVKPDGMVFFST 156
Cdd:COG1092  292 IIL--------DPPAfakskkdlfdaqrdykdLNRLALKLLAPGGILVTSS 334
PRK08317 PRK08317
hypothetical protein; Provisional
 51-150 3.51e-12

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 63.80  E-value: 3.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623  51 RGKRVLDVGCGGGILAESMARR--GAAFVKGIDMAEQSLETARLHAAlNNVADIEYECIRVEDLaEAEPHSFDVVTCMEM 128
Cdd:PRK08317  19 PGDRVLDVGCGPGNDARELARRvgPEGRVVGIDRSEAMLALAKERAA-GLGPNVEFVRGDADGL-PFPDGSFDAVRSDRV 96

                         90       100
                 ....*....|....*....|..
gi 189037623 129 MEHVPDPAAIVRACANLVKPDG 150
Cdd:PRK08317  97 LQHLEDPARALAEIARVLRPGG 118
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
 34-157 4.35e-12

ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an S-adenosyl-L-methionine-dependent methyltransferase required for the modification of ribosomal protein L11. This protein is found in bacteria and (with a probable transit peptide) in Arabidopsis. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273061  Cd Length: 288  Bit Score: 64.08  E-value: 4.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623   34 HDINPLRLDYIDGhADLRGKRVLDVGCGGGILAESMARRGAAFVKGIDMAEQSLETARLHAALNNVADI-EYECIRVEDL 112
Cdd:TIGR00406 143 HPTTSLCLEWLED-LDLKDKNVIDVGCGSGILSIAALKLGAAKVVGIDIDPLAVESARKNAELNQVSDRlQVKLIYLEQP 221

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 189037623  113 AEAEphsFDVVTCMEMMEHVPDPAAIVracANLVKPDGMVFFSTI 157
Cdd:TIGR00406 222 IEGK---ADVIVANILAEVIKELYPQF---SRLVKPGGWLILSGI 260
PRK15068 PRK15068
tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB;
48-208 8.17e-11

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


Pssm-ID: 237898  Cd Length: 322  Bit Score: 60.64  E-value: 8.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623  48 ADLRGKRVLDVGCGGGILAESMARRGAAFVKGIDMAEQSLetARLHAA---LNNVADIEYECIRVEDLaeAEPHSFDVVT 124
Cdd:PRK15068 119 SPLKGRTVLDVGCGNGYHMWRMLGAGAKLVVGIDPSQLFL--CQFEAVrklLGNDQRAHLLPLGIEQL--PALKAFDTVF 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623 125 CMEMMEHVPDPAAIVRACANLVKPDGMVFFSTinknpksylhLIVAAEYLLKFVPKGTHD-----WkkFI--APAeLARM 197
Cdd:PRK15068 195 SMGVLYHRRSPLDHLKQLKDQLVPGGELVLET----------LVIDGDENTVLVPGDRYAkmrnvY--FIpsVPA-LKNW 261

                        170
                 ....*....|....*..
gi 189037623 198 CRQAG------LDVADT 208
Cdd:PRK15068 262 LERAGfkdvriVDVSVT 278
PLN02244 PLN02244
tocopherol O-methyltransferase
 44-216 2.13e-10

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 59.76  E-value: 2.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623  44 IDGHADLRGKRVLDVGCGGGILAESMARRGAAFVKGIDMAEQSLETARLHAALNNVADieyeciRVE-DLAEA-----EP 117
Cdd:PLN02244 111 VPDDDEKRPKRIVDVGCGIGGSSRYLARKYGANVKGITLSPVQAARANALAAAQGLSD------KVSfQVADAlnqpfED 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623 118 HSFDVVTCMEMMEHVPDPAAIVRACANLVKPDGMVFFST------------INKNPKSYLHLIVAAEYLlkfvPkgthDW 185
Cdd:PLN02244 185 GQFDLVWSMESGEHMPDKRKFVQELARVAAPGGRIIIVTwchrdlepgetsLKPDEQKLLDKICAAYYL----P----AW 256

                        170       180       190
                 ....*....|....*....|....*....|.
gi 189037623 186 kkfIAPAELARMCRQAGLDVADTKGMTYHVL 216
Cdd:PLN02244 257 ---CSTSDYVKLAESLGLQDIKTEDWSEHVA 284
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 51-154 2.30e-10

tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 58.62  E-value: 2.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623  51 RGKRVLDVGCGGGILAESMARR-GAAFVKGIDMAEQSLETARLHAALNNVAD-IEYECIRVEDLAEA-EPHSFDVVTC-- 125
Cdd:COG4123   37 KGGRVLDLGTGTGVIALMLAQRsPGARITGVEIQPEAAELARRNVALNGLEDrITVIHGDLKEFAAElPPGSFDLVVSnp 116

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 189037623 126 --MEMMEHV--PDPA-------------AIVRACANLVKPDGMVFF 154
Cdd:COG4123  117 pyFKAGSGRksPDEAraiarhedaltleDLIRAAARLLKPGGRFAL 162
PRK06202 PRK06202
hypothetical protein; Provisional
 51-143 7.31e-10

hypothetical protein; Provisional


Pssm-ID: 180466 [Multi-domain]  Cd Length: 232  Bit Score: 57.32  E-value: 7.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623  51 RGKRVLDVGCGGGILAESMARRGA-----AFVKGIDMAEQSLETARLHAAlnnVADIEYECIRVEDLAeAEPHSFDVVTC 125
Cdd:PRK06202  60 RPLTLLDIGCGGGDLAIDLARWARrdglrLEVTAIDPDPRAVAFARANPR---RPGVTFRQAVSDELV-AEGERFDVVTS 135

                         90
                 ....*....|....*...
gi 189037623 126 MEMMEHVpDPAAIVRACA 143
Cdd:PRK06202 136 NHFLHHL-DDAEVVRLLA 152
PRK14967 PRK14967
putative methyltransferase; Provisional
 52-125 2.41e-09

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 55.44  E-value: 2.41e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189037623  52 GKRVLDVGCGGGILAESMARRGAAFVKGIDMAEQSLETARLHAALNNVaDIEyecIRVEDLAEAEP-HSFDVVTC 125
Cdd:PRK14967  37 GRRVLDLCTGSGALAVAAAAAGAGSVTAVDISRRAVRSARLNALLAGV-DVD---VRRGDWARAVEfRPFDVVVS 107
RsmG COG0357
16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ...
 47-154 2.53e-09

16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ribosomal structure and biogenesis]; 16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 440126  Cd Length: 211  Bit Score: 55.16  E-value: 2.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623  47 HADLRGKRVLDVGCGGG---------------ILAESMARRgAAFvkgidmaeqsLETARLHAALNNVadiEYECIRVED 111
Cdd:COG0357   63 LLPKEGARVLDVGSGAGfpgiplaiarpdlqvTLVDSLGKK-IAF----------LREVVRELGLKNV---TVVHGRAEE 128

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 189037623 112 LAEAEPhsFDVVTC---MEMmehvpdpAAIVRACANLVKPDGMVFF 154
Cdd:COG0357  129 LAPREK--FDVVTAravAPL-------PDLLELALPLLKPGGRLLA 165
PLN02585 PLN02585
magnesium protoporphyrin IX methyltransferase
 35-180 2.77e-09

magnesium protoporphyrin IX methyltransferase


Pssm-ID: 215319 [Multi-domain]  Cd Length: 315  Bit Score: 56.40  E-value: 2.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623  35 DINPLRLDYIDGHA--------------DLRGKRVLDVGCGGGILAESMARRGAAfVKGIDM-------AEQSLETARLH 93
Cdd:PLN02585 114 EVNKVQLDIRLGHAqtvekvllwlaedgSLAGVTVCDAGCGTGSLAIPLALEGAI-VSASDIsaamvaeAERRAKEALAA 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623  94 AALNNVADIEyecirVEDLAEAEpHSFDVVTCMEMMEHVPDPaaivracanlvKPDGMVffstinknpksyLHLIVAAE- 172
Cdd:PLN02585 193 LPPEVLPKFE-----ANDLESLS-GKYDTVTCLDVLIHYPQD-----------KADGMI------------AHLASLAEk 243


                 ....*....
gi 189037623 173 -YLLKFVPK 180
Cdd:PLN02585 244 rLIISFAPK 252
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 41-157 3.35e-09

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: 55.37  E-value: 3.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623   41 LDYIDGHADLRGKRVLDVGCGGGILAESMARRG-AAFVKGIDMAEQSLETARLHaalnNVADIEYECIRVEDLAeAEPHS 119
Cdd:TIGR02072  24 LALLKEKGIFIPASVLDIGCGTGYLTRALLKRFpQAEFIALDISAGMLAQAKTK----LSENVQFICGDAEKLP-LEDSS 98

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 189037623  120 FDVVTCMEMMEHVPDPAAIVRACANLVKPDGMVFFSTI 157
Cdd:TIGR02072  99 FDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTF 136
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
43-123 3.41e-09

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 54.91  E-value: 3.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623  43 YIDGhaDLRGKRVLDVGCGGGILAESMARRGAAFVKGIDMAEQSLETARlHAALNNVADIEYECIRVEDLAEAEphSFDV 122
Cdd:COG2263   39 YLRG--DIEGKTVLDLGCGTGMLAIGAALLGAKKVVGVDIDPEALEIAR-ENAERLGVRVDFIRADVTRIPLGG--SVDT 113


                 .
gi 189037623 123 V 123
Cdd:COG2263  114 V 114
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 51-212 4.44e-09

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 55.16  E-value: 4.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623  51 RGKRVLDVGCGGGILAESMARRG--AAFVKGIDMAEQSLETAR-LHAALNNVADIEYecirVEDLAEAEP---HSFDVVT 124
Cdd:PRK00216  51 PGDKVLDLACGTGDLAIALAKAVgkTGEVVGLDFSEGMLAVGReKLRDLGLSGNVEF----VQGDAEALPfpdNSFDAVT 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623 125 cmemM----EHVPDPAAIVRACANLVKPDGMVF---FSTINKNPKSYLHlivaAEYLLKFVP---------KGTHDW--- 185
Cdd:PRK00216 127 ----IafglRNVPDIDKALREMYRVLKPGGRLVileFSKPTNPPLKKAY----DFYLFKVLPligklisknAEAYSYlae 198

                        170       180
                 ....*....|....*....|....*....
gi 189037623 186 --KKFIAPAELARMCRQAGLDVADTKGMT 212
Cdd:PRK00216 199 siRAFPDQEELAAMLEEAGFERVRYRNLT 227
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 52-125 1.49e-08

16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA G1207 methylase RsmC is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 442062 [Multi-domain]  Cd Length: 191  Bit Score: 52.88  E-value: 1.49e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189037623  52 GKRVLDVGCGGGILAESMARRGA-AFVKGIDMAEQSLETARLHAALNNVADIeyECIRVEDLAEAEPHSFDVVTC 125
Cdd:COG2813   50 GGRVLDLGCGYGVIGLALAKRNPeARVTLVDVNARAVELARANAAANGLENV--EVLWSDGLSGVPDGSFDLILS 122
PRK14968 PRK14968
putative methyltransferase; Provisional
 52-124 2.11e-08

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 52.59  E-value: 2.11e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189037623  52 GKRVLDVGCGGGILAESMARRGaAFVKGIDMAEQSLETARLHAALNNVADIEYECIRvEDLAEA-EPHSFDVVT 124
Cdd:PRK14968  24 GDRVLEVGTGSGIVAIVAAKNG-KKVVGVDINPYAVECAKCNAKLNNIRNNGVEVIR-SDLFEPfRGDKFDVIL 95
Methyltransf_9 pfam08003
Protein of unknown function (DUF1698); This family contains many hypothetical proteins. It ...
 48-157 2.14e-08

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: 53.56  E-value: 2.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623   48 ADLRGKRVLDVGCGGGILAESMARRGAAFVKGIDMAEQSL---ETARLHAALNNVA-DIEyecIRVEDLAEAEphSFDVV 123
Cdd:pfam08003 112 SPLKGRTILDVGCGNGYHMWRMLGEGAAMVVGIDPSELFLcqfEAVRKLLGNDQRAhLLP---LGIEQLPALA--AFDTV 186

                          90       100       110
                  ....*....|....*....|....*....|....
gi 189037623  124 TCMEMMEHVPDPAAIVRACANLVKPDGMVFFSTI 157
Cdd:pfam08003 187 FSMGVLYHRRSPLDHLLQLKDQLVKGGELVLETL 220
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 51-125 5.29e-08

Methyltransferase small domain; This domain is found in ribosomal RNA small subunit methyltransferase C as well as other methyltransferases.


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 51.05  E-value: 5.29e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189037623   51 RGKRVLDVGCGGGILAESMARRGA-AFVKGIDMAEQSLETARLHAALNNVADIEyecIRVED-LAEAEPHSFDVVTC 125
Cdd:pfam05175  31 LSGKVLDLGCGAGVLGAALAKESPdAELTMVDINARALESARENLAANGLENGE---VVASDvYSGVEDGKFDLIIS 104
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 44-154 1.07e-06

Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 48.22  E-value: 1.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623  44 IDGHADLRGKRVLDVGCGGGILAESMAR-RGAAFVKGIDMAEQSLETARLHAALNNVADieyeciRVE----DLAEAEPH 118
Cdd:COG2890  105 LALLPAGAPPRVLDLGTGSGAIALALAKeRPDARVTAVDISPDALAVARRNAERLGLED------RVRflqgDLFEPLPG 178

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189037623 119 --SFDVVTC----------MEMMEHV------------PDP----AAIVRACANLVKPDGMVFF 154
Cdd:COG2890  179 dgRFDLIVSnppyipedeiALLPPEVrdheprlaldggEDGldfyRRIIAQAPRLLKPGGWLLL 242
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 32-157 1.48e-06

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: 48.09  E-value: 1.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623   32 TLHDINPLRLDYIDGHADLR-GKRVLDVGCGGGILAESMARRGAAFVKGIDMAEQSLETAR-LHAALNNVADIEYECIRV 109
Cdd:pfam02353  41 TLEEAQQAKLDLILDKLGLKpGMTLLDIGCGWGGLMRRAAERYDVNVVGLTLSKNQYKLARkRVAAEGLARKVEVLLQDY 120

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 189037623  110 EDLAEaephSFDVVTCMEMMEHV--PDPAAIVRACANLVKPDGMVFFSTI 157
Cdd:pfam02353 121 RDFDE----PFDRIVSVGMFEHVghENYDTFFKKLYNLLPPGGLMLLHTI 166
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
44-152 1.93e-06

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 47.43  E-value: 1.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623   44 IDGHADLRGKRVLDVGCGGGILAESMARR-GAAF-VKGIDMAEQSLETARLHAALNNVADIEYECIRVEDLAEaEPHSFD 121
Cdd:pfam01209  35 MKCMGVKRGNKFLDVAGGTGDWTFGLSDSaGSSGkVVGLDINENMLKEGEKKAKEEGKYNIEFLQGNAEELPF-EDDSFD 113

                          90       100       110
                  ....*....|....*....|....*....|.
gi 189037623  122 VVTCMEMMEHVPDPAAIVRACANLVKPDGMV 152
Cdd:pfam01209 114 IVTISFGLRNFPDYLKVLKEAFRVLKPGGRV 144
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 49-204 5.01e-06

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 46.67  E-value: 5.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623  49 DLR-GKRVLDVGCGGGILAESMARRGAAFVKGIDMAEQSLETArLHAALNNVADIEYEcirVEDLAEAE--PHSFDVVTC 125
Cdd:PLN02336 263 DLKpGQKVLDVGCGIGGGDFYMAENFDVHVVGIDLSVNMISFA-LERAIGRKCSVEFE---VADCTKKTypDNSFDVIYS 338

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623 126 MEMMEHVPDPAAIVRACANLVKPDGMVFFSTINKNPKSylhliVAAEYLLKFVPKG--THDWKKFiapaelARMCRQAGL 203
Cdd:PLN02336 339 RDTILHIQDKPALFRSFFKWLKPGGKVLISDYCRSPGT-----PSPEFAEYIKQRGydLHDVQAY------GQMLKDAGF 407


                 .
gi 189037623 204 D 204
Cdd:PLN02336 408 D 408
PRK11705 PRK11705
cyclopropane fatty acyl phospholipid synthase;
51-160 8.55e-06

cyclopropane fatty acyl phospholipid synthase;


Pssm-ID: 183282  Cd Length: 383  Bit Score: 45.99  E-value: 8.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623  51 RGKRVLDVGCGGGILAESMARRGAAFVKGIDMaeqSLETARLHAALNNVADIEyecIRVEDLAEAEPHsFDVVTCMEMME 130
Cdd:PRK11705 167 PGMRVLDIGCGWGGLARYAAEHYGVSVVGVTI---SAEQQKLAQERCAGLPVE---IRLQDYRDLNGQ-FDRIVSVGMFE 239

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 189037623 131 HV-PDPAA----IVRACanlVKPDGMVFFSTINKN 160
Cdd:PRK11705 240 HVgPKNYRtyfeVVRRC---LKPDGLFLLHTIGSN 271
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
52-153 1.38e-05

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 44.64  E-value: 1.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623  52 GKRVLDVGCGGGILAESMARRGAAFVKGIDMAEQSLETARLHAALNNVADieyeciRVEDLAEAE-----PHSFDVVTCm 126
Cdd:COG4076   36 GDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNPDIAAVARRIIAANGLSD------RITVINADAtdldlPEKADVIIS- 108

                         90       100       110
                 ....*....|....*....|....*....|.
gi 189037623 127 EMMEHV-PDP---AAIVRACANLVKPDGMVF 153
Cdd:COG4076  109 EMLDTAlLDEgqvPILNHARKRLLKPGGRII 139
TPMT pfam05724
Thiopurine S-methyltransferase (TPMT); This family consists of thiopurine S-methyltransferase ...
 20-157 3.79e-05

Thiopurine S-methyltransferase (TPMT); This family consists of thiopurine S-methyltransferase proteins from both eukaryotes and prokaryotes. Thiopurine S-methyltransferase (TPMT) is a cytosolic enzyme that catalyzes S-methylation of aromatic and heterocyclic sulfhydryl compounds, including anticancer and immunosuppressive thiopurines.


Pssm-ID: 399030  Cd Length: 218  Bit Score: 43.18  E-value: 3.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623   20 ADKWWDKSGEFKT---LHDINPLRLDYIDGHADLRGKRVLDVGCGGGILAESMARRGaAFVKGIDMAEQSLETARLHAAL 96
Cdd:pfam05724   3 PDFWLKRWVEGQTpfhQEGVNPLLVRHWDALKLPPGLRVLVPLCGKALDMVWLAEQG-HFVVGVEISELAVEKFFAEAGL 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189037623   97 N------------NVADIEYECIRVEDLAEAEPHSFD-----VVTCMEMMEHVPDPAAIVRAcanLVKPDGMVFFSTI 157
Cdd:pfam05724  82 SppitelsgfkeySSGNISLYCGDFFTLPREELGKFDliydrAALCALPPEMRPRYAKQMYE---LLPPGGRGLLITL 156
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 43-158 8.71e-05

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: 42.45  E-value: 8.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623  43 YIDGHADLR-GKRVLDVGCGGGILAESMARrgaaFVKG-------------IDMAEQSLETARLHaalNNVAdieyecIR 108
Cdd:COG2519   82 YIIARLDIFpGARVLEAGTGSGALTLALAR----AVGPegkvysyerredfAEIARKNLERFGLP---DNVE------LK 148

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 189037623 109 VEDLAEA-EPHSFDVVTcMEMmehvPDPAAIVRACANLVKPDGM--VFFSTIN 158
Cdd:COG2519  149 LGDIREGiDEGDVDAVF-LDM----PDPWEALEAVAKALKPGGVlvAYVPTVN 196
PRK11036 PRK11036
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
54-152 1.01e-04

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


Pssm-ID: 182918  Cd Length: 255  Bit Score: 42.26  E-value: 1.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623  54 RVLDVGCGGGILAESMARRGAAfVKGIDMAEQSLETARLHAALNNVADiEYECIR--VEDLAEAEPHSFDVVTCMEMMEH 131
Cdd:PRK11036  47 RVLDAGGGEGQTAIKLAELGHQ-VILCDLSAEMIQRAKQAAEAKGVSD-NMQFIHcaAQDIAQHLETPVDLILFHAVLEW 124

                         90       100
                 ....*....|....*....|.
gi 189037623 132 VPDPAAIVRACANLVKPDGMV 152
Cdd:PRK11036 125 VADPKSVLQTLWSVLRPGGAL 145
rsmG_gidB TIGR00138
16S rRNA (guanine(527)-N(7))-methyltransferase RsmG; RsmG was previously called GidB ...
 27-154 1.13e-04

16S rRNA (guanine(527)-N(7))-methyltransferase RsmG; RsmG was previously called GidB (glucose-inhibited division protein B). It is present and a single copy in nearly all complete eubacterial genomes. It is missing only from some obligate intracellular species of various lineages (Chlamydiae, Ehrlichia, Wolbachia, Anaplasma, Buchnera, etc.). RsmG shows a methytransferase fold in its the crystal structure, and acts as a 7-methylguanosine (m(7)G) methyltransferase, apparently specific to 16S rRNA. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 272928  Cd Length: 181  Bit Score: 41.47  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623   27 SGEFKTLHDINPLR-LDYIDGhadlrgKRVLDVGCGGGI---------------LAESMARRgAAFvkgidmaeqsLETA 90
Cdd:TIGR00138  23 PEEIWQRHILDSLAlLPYLDG------KRVIDIGSGAGFpgiplaiarpelkltLLESNHKK-VAF----------LREV 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189037623   91 RLHAALNNVADIEYeciRVEDLAEAEPhsFDVVTCMEMMEhVPDPAAIvraCANLVKPDGMVFF 154
Cdd:TIGR00138  86 KAELGLNNVEIVNG---RAEDYQHEEQ--FDIITSRALAS-LNVLLEL---TLNLLKVGGYFLA 140
arsM PRK11873
arsenite methyltransferase;
47-157 1.73e-04

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 41.86  E-value: 1.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623  47 HADLR-GKRVLDVGCGGGI---LAesmARR-GA-AFVKGIDMAEQSLETARLHAA---LNNVA----DIEYecIRVEDla 113
Cdd:PRK11873  72 LAELKpGETVLDLGSGGGFdcfLA---ARRvGPtGKVIGVDMTPEMLAKARANARkagYTNVEfrlgEIEA--LPVAD-- 144

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 189037623 114 eaepHSFDVVTCMEMMEHVPDPAAIVRACANLVKPDGMVFFSTI 157
Cdd:PRK11873 145 ----NSVDVIISNCVINLSPDKERVFKEAFRVLKPGGRFAISDV 184
idonate-5-DH cd08232
L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of ...
 47-152 4.80e-04

L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of L-lodonate to 5-ketogluconate in the metabolism of L-Idonate to 6-P-gluconate. In E. coli, this GntII pathway is a subsidiary pathway to the canonical GntI system, which also phosphorylates and transports gluconate. L-ido 5-DH is found in an operon with a regulator indR, transporter idnT, 5-keto-D-gluconate 5-reductase, and Gnt kinase. L-ido 5-DH is a zinc-dependent alcohol dehydrogenase-like protein. The alcohol dehydrogenase ADH-like family of proteins is a diverse group of proteins related to the first identified member, class I mammalian ADH. This group is also called the medium chain dehydrogenases/reductase family (MDR) which displays 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 GroES-like catalytic domain. 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. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176194 [Multi-domain]  Cd Length: 339  Bit Score: 40.68  E-value: 4.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623  47 HA-----DLRGKRVLDVGCG--GGILAESMARRGAAFVKGIDMAEQSLETARlhaALNnvADiEYECIRVEDLA--EAEP 117
Cdd:cd08232  156 HAvnragDLAGKRVLVTGAGpiGALVVAAARRAGAAEIVATDLADAPLAVAR---AMG--AD-ETVNLARDPLAayAADK 229

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 189037623 118 HSFDVVtcmemMEHVPDPAAIvRACANLVKPDGMV 152
Cdd:cd08232  230 GDFDVV-----FEASGAPAAL-ASALRVVRPGGTV 258
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 41-154 5.33e-04

N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 40.15  E-value: 5.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623  41 LDYIDGHAdlrGKRVLDVGCGGGILAESMAR-RGAAFVKGIDMAEQSLETARLHAALNNVADIEyecIRVEDLAEAEPH- 118
Cdd:PRK09328 101 LEALLLKE---PLRVLDLGTGSGAIALALAKeRPDAEVTAVDISPEALAVARRNAKHGLGARVE---FLQGDWFEPLPGg 174

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 189037623 119 SFDVVTC----------MEMMEHV----P------------DPAAIVRACANLVKPDGMVFF 154
Cdd:PRK09328 175 RFDLIVSnppyipeadiHLLQPEVrdhePhlalfggedgldFYRRIIEQAPRYLKPGGWLLL 236
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 51-125 1.01e-03

FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal sources FtsJ is a methyltransferase, but actually has no effect on cell division. FtsJ's substrate is the 23S rRNA. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. This family also includes the N terminus of flaviviral NS5 protein. It has been hypothesized that the N-terminal domain of NS5 is a methyltransferase involved in viral RNA capping.


Pssm-ID: 426399  Cd Length: 179  Bit Score: 38.72  E-value: 1.01e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 189037623   51 RGKRVLDVGCGGGILAESMARRGAAFVKGIDMAEQSLETARLHAALNNV-ADIEYECIrVEDLAEAEPHSFDVVTC 125
Cdd:pfam01728  21 PGKTVLDLGAAPGGWSQVALQRGAGKVVGVDLGPMQLWKPRNDPGVTFIqGDIRDPET-LDLLEELLGRKVDLVLS 95
PRK14103 PRK14103
trans-aconitate 2-methyltransferase; Provisional
 49-101 1.68e-03

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 184509  Cd Length: 255  Bit Score: 38.52  E-value: 1.68e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 189037623  49 DLRGKRVLDVGCGGGILAESMARR-GAAFVKGIDMAEQSLETAR---LHAALNNVAD 101
Cdd:PRK14103  27 AERARRVVDLGCGPGNLTRYLARRwPGAVIEALDSSPEMVAAARergVDARTGDVRD 83
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
 54-155 2.00e-03

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 38.41  E-value: 2.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623  54 RVLDVGCGGGILAESMARRGAAFVKGIDMAEQSLETARLHAALNNVADIEYECIRVEDLAEAephSFDVVTCMEMMEHVP 133
Cdd:PTZ00098  55 KVLDIGSGLGGGCKYINEKYGAHVHGVDICEKMVNIAKLRNSDKNKIEFEANDILKKDFPEN---TFDMIYSRDAILHLS 131

                         90       100
                 ....*....|....*....|....
gi 189037623 134 --DPAAIVRACANLVKPDGMVFFS 155
Cdd:PTZ00098 132 yaDKKKLFEKCYKWLKPNGILLIT 155
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 55-157 2.15e-03

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 38.20  E-value: 2.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189037623  55 VLDVGCGGGILAESMARRGAAfVKGIDMAEQSLETARLHAALNN--VADIEyecirVEDLAEAephSFDVVTCMEMMEHV 132
Cdd:PRK10258  46 VLDAGCGPGWMSRYWRERGSQ-VTALDLSPPMLAQARQKDAADHylAGDIE-----SLPLATA---TFDLAWSNLAVQWC 116

                         90       100
                 ....*....|....*....|....*
gi 189037623 133 PDPAAIVRACANLVKPDGMVFFSTI 157
Cdd:PRK10258 117 GNLSTALRELYRVVRPGGVVAFTTL 141
PRK14966 PRK14966
unknown domain/N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase fusion protein; ...
 54-95 7.71e-03

unknown domain/N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase fusion protein; Provisional


Pssm-ID: 184930 [Multi-domain]  Cd Length: 423  Bit Score: 36.98  E-value: 7.71e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 189037623  54 RVLDVGCGGGILAESMA-RRGAAFVKGIDMAEQSLETARLHAA 95
Cdd:PRK14966 254 RVWDLGTGSGAVAVTVAlERPDAFVRASDISPPALETARKNAA 296
 
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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