NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|493864634|ref|WP_006811346|]
View 

MULTISPECIES: bifunctional 2-polyprenyl-6-hydroxyphenol methylase/3-demethylubiquinol 3-O-methyltransferase UbiG [Enterobacter]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
UbiG TIGR01983
ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase ...
 16-234 7.74e-135

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: 378.56  E-value: 7.74e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634   16 EIAKFEAVASRWWDLEGEFKPLHRINPLRLGYIAERSGG-----LFGKKVLDVGCGGGILAESMAREGATVTGLDMGFEP 90
Cdd:TIGR01983   1 EIAKFSALAHEWWDPNGKFKPLHKMNPLRLDYIRDRIRKnfknpLDGLRVLDVGCGGGLLSEPLARLGANVTGIDASEEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634   91 LQVARLHALESGVQVEYVQETVEEHAAKHAHQYDVVTCMEMLEHVPDPQSVVSACAKLVKPGGQVFFSTINRNGKAWLMA 170
Cdd:TIGR01983  81 IEVAKLHAKKDPLQIDYRCTTVEDLAEKKAGSFDVVTCMEVLEHVPDPQAFIRACAQLLKPGGILFFSTINRTPKSYLLA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493864634  171 VVGAEYVLRMVPKGTHDVKKFIKPAELLGWVDQTWLKEQHMTGLHYNPLTDKFKLAPGVDVNYM 234
Cdd:TIGR01983 161 IVGAEYILRIVPKGTHDWEKFIKPSELLSWLESAGLRVKDIKGLVYNPIKNTWKLSKDTDVNYM 224
 
Name Accession Description Interval E-value
UbiG TIGR01983
ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase ...
 16-234 7.74e-135

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: 378.56  E-value: 7.74e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634   16 EIAKFEAVASRWWDLEGEFKPLHRINPLRLGYIAERSGG-----LFGKKVLDVGCGGGILAESMAREGATVTGLDMGFEP 90
Cdd:TIGR01983   1 EIAKFSALAHEWWDPNGKFKPLHKMNPLRLDYIRDRIRKnfknpLDGLRVLDVGCGGGLLSEPLARLGANVTGIDASEEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634   91 LQVARLHALESGVQVEYVQETVEEHAAKHAHQYDVVTCMEMLEHVPDPQSVVSACAKLVKPGGQVFFSTINRNGKAWLMA 170
Cdd:TIGR01983  81 IEVAKLHAKKDPLQIDYRCTTVEDLAEKKAGSFDVVTCMEVLEHVPDPQAFIRACAQLLKPGGILFFSTINRTPKSYLLA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493864634  171 VVGAEYVLRMVPKGTHDVKKFIKPAELLGWVDQTWLKEQHMTGLHYNPLTDKFKLAPGVDVNYM 234
Cdd:TIGR01983 161 IVGAEYILRIVPKGTHDWEKFIKPSELLSWLESAGLRVKDIKGLVYNPIKNTWKLSKDTDVNYM 224
PLN02396 PLN02396
hexaprenyldihydroxybenzoate methyltransferase
 11-242 2.79e-63

hexaprenyldihydroxybenzoate methyltransferase


Pssm-ID: 178018 [Multi-domain]  Cd Length: 322  Bit Score: 200.34  E-value: 2.79e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634  11 NVDHEEIAKFEAVASRWWDLEGEFKPLHRINPLRLGYIAERSGGLFGK-----------KVLDVGCGGGILAESMAREGA 79
Cdd:PLN02396  75 SLNEDELAKFSAIADTWWHSEGPFKPLHQMNPTRLAFIRSTLCRHFSKdpssakpfeglKFIDIGCGGGLLSEPLARMGA 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634  80 TVTGLDMGFEPLQVARLHALESGVQ--VEYVQETVEEhAAKHAHQYDVVTCMEMLEHVPDPQSVVSACAKLVKPGGQVFF 157
Cdd:PLN02396 155 TVTGVDAVDKNVKIARLHADMDPVTstIEYLCTTAEK-LADEGRKFDAVLSLEVIEHVANPAEFCKSLSALTIPNGATVL 233

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634 158 STINRNGKAWLMAVVGAEYVLRMVPKGTHDVKKFIKPAELLGWVDQTWLKEQHMTGLHYNPLTDKFKLAPGVDVNYMLHT 237
Cdd:PLN02396 234 STINRTMRAYASTIVGAEYILRWLPKGTHQWSSFVTPEELSMILQRASVDVKEMAGFVYNPITGRWLLSDDISVNYIAYG 313


                 ....*
gi 493864634 238 TAKND 242
Cdd:PLN02396 314 TKRKD 318
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 57-161 1.32e-38

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: 130.52  E-value: 1.32e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634  57 GKKVLDVGCGGGILAESMAREGATVTGLDMGFEPLQVARLHALEsgVQVEYVQETVEEHAAKHAhQYDVVTCMEMLEHVP 136
Cdd:COG2227   25 GGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAE--LNVDFVQGDLEDLPLEDG-SFDLVICSEVLEHLP 101

                         90       100
                 ....*....|....*....|....*
gi 493864634 137 DPQSVVSACAKLVKPGGQVFFSTIN 161
Cdd:COG2227  102 DPAALLRELARLLKPGGLLLLSTPN 126
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 61-157 9.91e-23

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 88.49  E-value: 9.91e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634   61 LDVGCGGGILAESMAREGATVTGLDMGFEPLQVARLHAleSGVQVEYVQETVEEHAAKhAHQYDVVTCMEMLEHVPDPQS 140
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKA--PREGLTFVVGDAEDLPFP-DNSFDLVLSSEVLHHVEDPER 77

                          90
                  ....*....|....*..
gi 493864634  141 VVSACAKLVKPGGQVFF 157
Cdd:pfam08241  78 ALREIARVLKPGGILII 94
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 59-158 2.05e-12

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


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 61.68  E-value: 2.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634  59 KVLDVGCGGGILAESMAR-EGATVTGLDMGFEPLQVAR-LHALESGVQVEYVQETVEEHAAKHAHQYDVVTCMEMLEH-V 135
Cdd:cd02440    1 RVLDLGCGTGALALALASgPGARVTGVDISPVALELARkAAAALLADNVEVLKGDAEELPPEADESFDVIISDPPLHHlV 80

                         90       100
                 ....*....|....*....|...
gi 493864634 136 PDPQSVVSACAKLVKPGGQVFFS 158
Cdd:cd02440   81 EDLARFLEEARRLLKPGGVLVLT 103
 
Name Accession Description Interval E-value
UbiG TIGR01983
ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase ...
 16-234 7.74e-135

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: 378.56  E-value: 7.74e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634   16 EIAKFEAVASRWWDLEGEFKPLHRINPLRLGYIAERSGG-----LFGKKVLDVGCGGGILAESMAREGATVTGLDMGFEP 90
Cdd:TIGR01983   1 EIAKFSALAHEWWDPNGKFKPLHKMNPLRLDYIRDRIRKnfknpLDGLRVLDVGCGGGLLSEPLARLGANVTGIDASEEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634   91 LQVARLHALESGVQVEYVQETVEEHAAKHAHQYDVVTCMEMLEHVPDPQSVVSACAKLVKPGGQVFFSTINRNGKAWLMA 170
Cdd:TIGR01983  81 IEVAKLHAKKDPLQIDYRCTTVEDLAEKKAGSFDVVTCMEVLEHVPDPQAFIRACAQLLKPGGILFFSTINRTPKSYLLA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493864634  171 VVGAEYVLRMVPKGTHDVKKFIKPAELLGWVDQTWLKEQHMTGLHYNPLTDKFKLAPGVDVNYM 234
Cdd:TIGR01983 161 IVGAEYILRIVPKGTHDWEKFIKPSELLSWLESAGLRVKDIKGLVYNPIKNTWKLSKDTDVNYM 224
PLN02396 PLN02396
hexaprenyldihydroxybenzoate methyltransferase
 11-242 2.79e-63

hexaprenyldihydroxybenzoate methyltransferase


Pssm-ID: 178018 [Multi-domain]  Cd Length: 322  Bit Score: 200.34  E-value: 2.79e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634  11 NVDHEEIAKFEAVASRWWDLEGEFKPLHRINPLRLGYIAERSGGLFGK-----------KVLDVGCGGGILAESMAREGA 79
Cdd:PLN02396  75 SLNEDELAKFSAIADTWWHSEGPFKPLHQMNPTRLAFIRSTLCRHFSKdpssakpfeglKFIDIGCGGGLLSEPLARMGA 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634  80 TVTGLDMGFEPLQVARLHALESGVQ--VEYVQETVEEhAAKHAHQYDVVTCMEMLEHVPDPQSVVSACAKLVKPGGQVFF 157
Cdd:PLN02396 155 TVTGVDAVDKNVKIARLHADMDPVTstIEYLCTTAEK-LADEGRKFDAVLSLEVIEHVANPAEFCKSLSALTIPNGATVL 233

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634 158 STINRNGKAWLMAVVGAEYVLRMVPKGTHDVKKFIKPAELLGWVDQTWLKEQHMTGLHYNPLTDKFKLAPGVDVNYMLHT 237
Cdd:PLN02396 234 STINRTMRAYASTIVGAEYILRWLPKGTHQWSSFVTPEELSMILQRASVDVKEMAGFVYNPITGRWLLSDDISVNYIAYG 313


                 ....*
gi 493864634 238 TAKND 242
Cdd:PLN02396 314 TKRKD 318
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 57-161 1.32e-38

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: 130.52  E-value: 1.32e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634  57 GKKVLDVGCGGGILAESMAREGATVTGLDMGFEPLQVARLHALEsgVQVEYVQETVEEHAAKHAhQYDVVTCMEMLEHVP 136
Cdd:COG2227   25 GGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAE--LNVDFVQGDLEDLPLEDG-SFDLVICSEVLEHLP 101

                         90       100
                 ....*....|....*....|....*
gi 493864634 137 DPQSVVSACAKLVKPGGQVFFSTIN 161
Cdd:COG2227  102 DPAALLRELARLLKPGGLLLLSTPN 126
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 57-170 1.69e-25

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: 97.37  E-value: 1.69e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634  57 GKKVLDVGCGGGILAESMAREGATVTGLDMGFEPLQVARLHALESGVQVEYVQETVEEHAAKhAHQYDVVTCMEMLEHVP 136
Cdd:COG2226   23 GARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGLNVEFVVGDAEDLPFP-DGSFDLVISSFVLHHLP 101

                         90       100       110
                 ....*....|....*....|....*....|....
gi 493864634 137 DPQSVVSACAKLVKPGGQVFFSTINRNGKAWLMA 170
Cdd:COG2226  102 DPERALAEIARVLKPGGRLVVVDFSPPDLAELEE 135
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 61-157 9.91e-23

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 88.49  E-value: 9.91e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634   61 LDVGCGGGILAESMAREGATVTGLDMGFEPLQVARLHAleSGVQVEYVQETVEEHAAKhAHQYDVVTCMEMLEHVPDPQS 140
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKA--PREGLTFVVGDAEDLPFP-DNSFDLVLSSEVLHHVEDPER 77

                          90
                  ....*....|....*..
gi 493864634  141 VVSACAKLVKPGGQVFF 157
Cdd:pfam08241  78 ALREIARVLKPGGILII 94
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 60-153 4.62e-22

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 86.85  E-value: 4.62e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634   60 VLDVGCGGGILAESMARE-GATVTGLDMGFEPLQVARLHALESGVQVEYVQETVEEHAAKHAhQYDVVTCMEMLEHVPDP 138
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRgGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFPDG-SFDLVVSSGVLHHLPDP 79

                          90
                  ....*....|....*..
gi 493864634  139 Q--SVVSACAKLVKPGG 153
Cdd:pfam13649  80 DleAALREIARVLKPGG 96
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 57-186 2.44e-21

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 87.10  E-value: 2.44e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634   57 GKKVLDVGCGGGILAESMAREGATVTGLDMGFEPLQVARLHALEsgvqveyvQETVEEHAAKHAHQYDVVTCMEMLEHVP 136
Cdd:pfam13489  23 PGRVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERALLNVRF--------DQFDEQEAAVPAGKFDVIVAREVLEHVP 94

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 493864634  137 DPQSVVSACAKLVKPGGQVFFSTINRNGKAWLMavvgAEYVLRMVPKGTH 186
Cdd:pfam13489  95 DPPALLRQIAALLKPGGLLLLSTPLASDEADRL----LLEWPYLRPRNGH 140
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 57-159 1.46e-18

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 79.59  E-value: 1.46e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634  57 GKKVLDVGCGGGILAESMARE-GATVTGLDMGFEPLQVARLHALESGV--QVEYVQETVEEHAAKhaHQYDVVTCMEMLE 133
Cdd:COG2230   52 GMRVLDIGCGWGGLALYLARRyGVRVTGVTLSPEQLEYARERAAEAGLadRVEVRLADYRDLPAD--GQFDAIVSIGMFE 129

                         90       100
                 ....*....|....*....|....*...
gi 493864634 134 HVPDPQ--SVVSACAKLVKPGGQVFFST 159
Cdd:COG2230  130 HVGPENypAYFAKVARLLKPGGRLLLHT 157
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
48-159 4.49e-16

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 73.49  E-value: 4.49e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634  48 IAERSGGLFGKKVLDVGCGGGILAESMAREGATVTGLDMGFEPLQVARlhalESGVQVEYVQETVEEhAAKHAHQYDVVT 127
Cdd:COG4976   38 LLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAR----EKGVYDRLLVADLAD-LAEPDGRFDLIV 112

                         90       100       110
                 ....*....|....*....|....*....|..
gi 493864634 128 CMEMLEHVPDPQSVVSACAKLVKPGGQVFFST 159
Cdd:COG4976  113 AADVLTYLGDLAAVFAGVARALKPGGLFIFSV 144
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
57-159 4.74e-15

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 68.70  E-value: 4.74e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634  57 GKKVLDVGCGGGILAESMARE--GATVTGLDMGFEPLQVARlhalESGVQVEYVQETVEEHAAkhAHQYDVVTCMEMLEH 134
Cdd:COG4106    2 PRRVLDLGCGTGRLTALLAERfpGARVTGVDLSPEMLARAR----ARLPNVRFVVADLRDLDP--PEPFDLVVSNAALHW 75

                         90       100
                 ....*....|....*....|....*
gi 493864634 135 VPDPQSVVSACAKLVKPGGQVFFST 159
Cdd:COG4106   76 LPDHAALLARLAAALAPGGVLAVQV 100
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 57-158 1.83e-14

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 69.56  E-value: 1.83e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634  57 GKKVLDVGCGGGILAESMA-REGATVTGLDMGFEPLQVARLHALESGV-QVEYVQETVEEHAAKHAHQYDVVTCMEMLEH 134
Cdd:COG0500   27 GGRVLDLGCGTGRNLLALAaRFGGRVIGIDLSPEAIALARARAAKAGLgNVEFLVADLAELDPLPAESFDLVVAFGVLHH 106

                         90       100
                 ....*....|....*....|....*.
gi 493864634 135 VP--DPQSVVSACAKLVKPGGQVFFS 158
Cdd:COG0500  107 LPpeEREALLRELARALKPGGVLLLS 132
PRK08317 PRK08317
hypothetical protein; Provisional
 57-155 2.29e-13

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 67.27  E-value: 2.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634  57 GKKVLDVGCGGGILAESMARE---GATVTGLDMGFEPLQVARLHALESGVQVEYVQeTVEEHAAKHAHQYDVVTCMEMLE 133
Cdd:PRK08317  20 GDRVLDVGCGPGNDARELARRvgpEGRVVGIDRSEAMLALAKERAAGLGPNVEFVR-GDADGLPFPDGSFDAVRSDRVLQ 98

                         90       100
                 ....*....|....*....|..
gi 493864634 134 HVPDPQSVVSACAKLVKPGGQV 155
Cdd:PRK08317  99 HLEDPARALAEIARVLRPGGRV 120
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 57-161 3.44e-13

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 65.13  E-value: 3.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634   57 GKKVLDVGCGGGILAESMARE---GATVTGLDMGFEPLQVARLHALESGVQ-VEYVQETVEE-HAAKHAHQYDVVTCMEM 131
Cdd:pfam13847   4 GMRVLDLGCGTGHLSFELAEElgpNAEVVGIDISEEAIEKARENAQKLGFDnVEFEQGDIEElPELLEDDKFDVVISNCV 83

                          90       100       110
                  ....*....|....*....|....*....|
gi 493864634  132 LEHVPDPQSVVSACAKLVKPGGQVFFSTIN 161
Cdd:pfam13847  84 LNHIPDPDKVLQEILRVLKPGGRLIISDPD 113
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 61-153 8.03e-13

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 62.39  E-value: 8.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634   61 LDVGCGGGILAESMARE--GATVTGLDMGFEPLQVARLHALE-SGVQVEYVQETVEEHAAKHAHQYDVVTCMEMLEHVPD 137
Cdd:pfam08242   1 LEIGCGTGTLLRALLEAlpGLEYTGLDISPAALEAARERLAAlGLLNAVRVELFQLDLGELDPGSFDVVVASNVLHHLAD 80

                          90
                  ....*....|....*.
gi 493864634  138 PQSVVSACAKLVKPGG 153
Cdd:pfam08242  81 PRAVLRNIRRLLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 59-158 2.05e-12

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


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 61.68  E-value: 2.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634  59 KVLDVGCGGGILAESMAR-EGATVTGLDMGFEPLQVAR-LHALESGVQVEYVQETVEEHAAKHAHQYDVVTCMEMLEH-V 135
Cdd:cd02440    1 RVLDLGCGTGALALALASgPGARVTGVDISPVALELARkAAAALLADNVEVLKGDAEELPPEADESFDVIISDPPLHHlV 80

                         90       100
                 ....*....|....*....|...
gi 493864634 136 PDPQSVVSACAKLVKPGGQVFFS 158
Cdd:cd02440   81 EDLARFLEEARRLLKPGGVLVLT 103
PRK11036 PRK11036
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
60-203 1.14e-11

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


Pssm-ID: 182918  Cd Length: 255  Bit Score: 62.67  E-value: 1.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634  60 VLDVGCGGGILAESMAREGATVTGLDMGFEPLQVARLHALESGV--QVEYVQETVEEHAAKHAHQYDVVTCMEMLEHVPD 137
Cdd:PRK11036  48 VLDAGGGEGQTAIKLAELGHQVILCDLSAEMIQRAKQAAEAKGVsdNMQFIHCAAQDIAQHLETPVDLILFHAVLEWVAD 127

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493864634 138 PQSVVSACAKLVKPGGQVFFSTINRNGKAWLMAVVGA-EYVLRMVPKGthdvKKF-------IKPAELLGWVDQ 203
Cdd:PRK11036 128 PKSVLQTLWSVLRPGGALSLMFYNANGLLMHNMVAGNfDYVQAGMPKR----KKRtlspdypLDPEQVYQWLEE 197
PLN02244 PLN02244
tocopherol O-methyltransferase
 58-159 6.10e-11

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 61.30  E-value: 6.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634  58 KKVLDVGCGGGILAESMARE-GATVTGLDMgfEPLQVARLHAL--ESGVqVEYVQETVEE--HAAKHAHQYDVVTCMEML 132
Cdd:PLN02244 120 KRIVDVGCGIGGSSRYLARKyGANVKGITL--SPVQAARANALaaAQGL-SDKVSFQVADalNQPFEDGQFDLVWSMESG 196

                         90       100
                 ....*....|....*....|....*..
gi 493864634 133 EHVPDPQSVVSACAKLVKPGGQVFFST 159
Cdd:PLN02244 197 EHMPDKRKFVQELARVAAPGGRIIIVT 223
PRK06202 PRK06202
hypothetical protein; Provisional
 60-205 1.33e-09

hypothetical protein; Provisional


Pssm-ID: 180466 [Multi-domain]  Cd Length: 232  Bit Score: 56.55  E-value: 1.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634  60 VLDVGCGGGILAESMAREGA------TVTGLDMGFEPLQVARLHALESGVQVEYV--QETVEEHAakhahQYDVVTCMEM 131
Cdd:PRK06202  64 LLDIGCGGGDLAIDLARWARrdglrlEVTAIDPDPRAVAFARANPRRPGVTFRQAvsDELVAEGE-----RFDVVTSNHF 138

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493864634 132 LEHVPDPQ--SVVSACAKLVKpgGQVFFSTINRNGKAWLMAVVGAEYVLR---MVPKGTHDVKKFIKPAELLGWVDQTW 205
Cdd:PRK06202 139 LHHLDDAEvvRLLADSAALAR--RLVLHNDLIRSRLAYALFWAGTRLLSRssfVHTDGLLSVRRSYTPAELAALAPQGW 215
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 47-189 1.75e-08

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: 52.96  E-value: 1.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634  47 YIAERSGgLFGKKVLDVGCGGGILAESMAREGA-TVTGLDMGFEPLQVARLHALESGVQVEYVQETVEEHAAkhAHQYDV 125
Cdd:COG3897   62 YLLDHPE-VAGKRVLELGCGLGLVGIAAAKAGAaDVTATDYDPEALAALRLNAALNGVAITTRLGDWRDPPA--AGGFDL 138

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493864634 126 VTC------MEMLEHvpdpqsVVSACAKLVKPGGQVFFSTINR----NGKAWLMAVVGAEYVLRMVPKGTHDVK 189
Cdd:COG3897  139 ILGgdvlyeRDLAEP------LLPFLDRLAAPGGEVLIGDPGRgylpAFRERLEALAGYEVVTRELEDTEKVKR 206
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
20-155 4.04e-08

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 52.06  E-value: 4.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634   20 FEAVASRWwDLEGEFKPLhRINPLRLGYIAERSGGLFGKKVLDVGCGGGILAESM---AREGATVTGLDMGFEPLQVARL 96
Cdd:pfam01209   8 FSSVASKY-DLMNDVISF-GIHRLWKDFTMKCMGVKRGNKFLDVAGGTGDWTFGLsdsAGSSGKVVGLDINENMLKEGEK 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634   97 HALESGV-QVEYVQETVEEHAAKHAhQYDVVTCMEMLEHVPDPQSVVSACAKLVKPGGQV 155
Cdd:pfam01209  86 KAKEEGKyNIEFLQGNAEELPFEDD-SFDIVTISFGLRNFPDYLKVLKEAFRVLKPGGRV 144
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 52-148 7.68e-08

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 51.38  E-value: 7.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634  52 SGGLFGKKVLDVGCGGGILAESMAREGATVTGLDMGFEPLQVARLHALESGV--QVEYVQETVEEHAAkhahQYDVVTCM 129
Cdd:PRK07580  59 DGDLTGLRILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEARERAPEAGLagNITFEVGDLESLLG----RFDTVVCL 134

                         90
                 ....*....|....*....
gi 493864634 130 EMLEHVPDPQsVVSACAKL 148
Cdd:PRK07580 135 DVLIHYPQED-AARMLAHL 152
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 58-160 1.82e-07

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: 50.36  E-value: 1.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634   58 KKVLDVGCGGGILAESMAREG--ATVTGLDMGFEPLQVARLHaleSGVQVEYVQETVEeHAAKHAHQYDVVTCMEMLEHV 135
Cdd:TIGR02072  36 ASVLDIGCGTGYLTRALLKRFpqAEFIALDISAGMLAQAKTK---LSENVQFICGDAE-KLPLEDSSFDLIVSNLALQWC 111

                          90       100
                  ....*....|....*....|....*
gi 493864634  136 PDPQSVVSACAKLVKPGGQVFFSTI 160
Cdd:TIGR02072 112 DDLSQALSELARVLKPGGLLAFSTF 136
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
47-126 2.51e-07

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 49.52  E-value: 2.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634  47 YIAERSGGLFGKKVLDVGCGGGILAESMAREGAT-VTGLDMGFEPLQVARLHALESGVQVEYVQETVEEHAAkhAHQYDV 125
Cdd:COG2263   36 HLAYLRGDIEGKTVLDLGCGTGMLAIGAALLGAKkVVGVDIDPEALEIARENAERLGVRVDFIRADVTRIPL--GGSVDT 113


                 .
gi 493864634 126 V 126
Cdd:COG2263  114 V 114
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 50-172 4.25e-07

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 49.38  E-value: 4.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634  50 ERSGGLFGKKVLDVGCGGGILAESMAREG---ATVTGLDMGFEPLQVA--RLHALESGVQVEYVQETVEEHAAKHAHqYD 124
Cdd:PRK00216  45 KWLGVRPGDKVLDLACGTGDLAIALAKAVgktGEVVGLDFSEGMLAVGreKLRDLGLSGNVEFVQGDAEALPFPDNS-FD 123

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 493864634 125 VVTcmeM---LEHVPDPQSVVSACAKLVKPGGQVF---FSTINRNG-----KAWLMAVV 172
Cdd:PRK00216 124 AVT---IafgLRNVPDIDKALREMYRVLKPGGRLVileFSKPTNPPlkkayDFYLFKVL 179
PLN02585 PLN02585
magnesium protoporphyrin IX methyltransferase
 45-137 5.78e-07

magnesium protoporphyrin IX methyltransferase


Pssm-ID: 215319 [Multi-domain]  Cd Length: 315  Bit Score: 49.47  E-value: 5.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634  45 LGYIAErSGGLFGKKVLDVGCGGGILAESMAREGATVTGLD----MGFEPLQVAR--LHALESGVQVEYVQETVEEHAAK 118
Cdd:PLN02585 134 LLWLAE-DGSLAGVTVCDAGCGTGSLAIPLALEGAIVSASDisaaMVAEAERRAKeaLAALPPEVLPKFEANDLESLSGK 212

                         90
                 ....*....|....*....
gi 493864634 119 hahqYDVVTCMEMLEHVPD 137
Cdd:PLN02585 213 ----YDTVTCLDVLIHYPQ 227
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
57-158 2.10e-06

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 47.48  E-value: 2.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634  57 GKKVLDVGCGGGILAESMAREGAT-VTGLDmgFEP--LQVARLHALESGV--QVEYVQETVEEHAakhahQYDVVTC--- 128
Cdd:COG2264  149 GKTVLDVGCGSGILAIAAAKLGAKrVLAVD--IDPvaVEAARENAELNGVedRIEVVLGDLLEDG-----PYDLVVAnil 221

                         90       100       110
                 ....*....|....*....|....*....|....
gi 493864634 129 ----MEMLEHVpdpqsvvsacAKLVKPGGQVFFS 158
Cdd:COG2264  222 anplIELAPDL----------AALLKPGGYLILS 245
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
57-160 2.62e-06

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 47.07  E-value: 2.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634  57 GKKVLDVGCGGGILAESMAREGAT-VTGLDMgfEPL--QVARLHALESGVQveyvqetVEEHAAKHAHQYDVVTC----- 128
Cdd:PRK00517 120 GKTVLDVGCGSGILAIAAAKLGAKkVLAVDI--DPQavEAARENAELNGVE-------LNVYLPQGDLKADVIVAnilan 190

                         90       100       110
                 ....*....|....*....|....*....|....
gi 493864634 129 --MEMLEHVpdpqsvvsacAKLVKPGGQVFFSTI 160
Cdd:PRK00517 191 plLELAPDL----------ARLLKPGGRLILSGI 214
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 57-160 3.87e-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: 46.88  E-value: 3.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634   57 GKKVLDVGCGGGILAESMAREGAT-VTGLDMGFEPLQVARLHALESGV----QVEYVQETVEEhaakhahQYDVVTC--- 128
Cdd:pfam06325 162 GESVLDVGCGSGILAIAALKLGAKkVVGVDIDPVAVRAAKENAELNGVearlEVYLPGDLPKE-------KADVVVAnil 234

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 493864634  129 ----MEMLEHVpdpqsvvsacAKLVKPGGQVFFSTI 160
Cdd:pfam06325 235 adplIELAPDI----------YALVKPGGYLILSGI 260
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 57-157 5.55e-06

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: 45.91  E-value: 5.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634  57 GKKVLDVGCGGGILAESMAR--EGATVTGLDMGFEPLQVARLHALESGV--QVEYVQETVEEHAAK-HAHQYDVVTC--- 128
Cdd:COG4123   38 GGRVLDLGTGTGVIALMLAQrsPGARITGVEIQPEAAELARRNVALNGLedRITVIHGDLKEFAAElPPGSFDLVVSnpp 117

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 493864634 129 -MEMLEHV--PDPQ-------------SVVSACAKLVKPGGQVFF 157
Cdd:COG4123  118 yFKAGSGRksPDEAraiarhedaltleDLIRAAARLLKPGGRFAL 162
PRK14967 PRK14967
putative methyltransferase; Provisional
 48-128 6.51e-06

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 45.81  E-value: 6.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634  48 IAERSGGLFGKKVLDVGCGGGILAESMAREGA-TVTGLDMGFEPLQVARLHALESGVQVEYVQETVEEhaAKHAHQYDVV 126
Cdd:PRK14967  28 ALAAEGLGPGRRVLDLCTGSGALAVAAAAAGAgSVTAVDISRRAVRSARLNALLAGVDVDVRRGDWAR--AVEFRPFDVV 105


                 ..
gi 493864634 127 TC 128
Cdd:PRK14967 106 VS 107
PRK15068 PRK15068
tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB;
55-159 1.23e-05

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


Pssm-ID: 237898  Cd Length: 322  Bit Score: 45.23  E-value: 1.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634  55 LFGKKVLDVGCGGGILAESMAREGA-TVTGLD------MGFEPLQvarlHALESGVQVEYVQETVEEHAAKHAhqYDVVT 127
Cdd:PRK15068 121 LKGRTVLDVGCGNGYHMWRMLGAGAkLVVGIDpsqlflCQFEAVR----KLLGNDQRAHLLPLGIEQLPALKA--FDTVF 194

                         90       100       110
                 ....*....|....*....|....*....|..
gi 493864634 128 CMEMLEHVPDPQSVVSACAKLVKPGGQVFFST 159
Cdd:PRK15068 195 SMGVLYHRRSPLDHLKQLKDQLVPGGELVLET 226
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
 57-160 2.06e-05

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: 44.44  E-value: 2.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634   57 GKKVLDVGCGGGILAESMAREGA-TVTGLDMGFEPLQVARLHALESGVQvEYVQETVEEHAAKHAHQYDVVTCMEMLEHV 135
Cdd:TIGR00406 160 DKNVIDVGCGSGILSIAALKLGAaKVVGIDIDPLAVESARKNAELNQVS-DRLQVKLIYLEQPIEGKADVIVANILAEVI 238

                          90       100
                  ....*....|....*....|....*
gi 493864634  136 PDPQSVVSacaKLVKPGGQVFFSTI 160
Cdd:TIGR00406 239 KELYPQFS---RLVKPGGWLILSGI 260
PRK14968 PRK14968
putative methyltransferase; Provisional
 57-85 4.45e-05

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 42.96  E-value: 4.45e-05
                         10        20
                 ....*....|....*....|....*....
gi 493864634  57 GKKVLDVGCGGGILAESMAREGATVTGLD 85
Cdd:PRK14968  24 GDRVLEVGTGSGIVAIVAAKNGKKVVGVD 52
arsM PRK11873
arsenite methyltransferase;
41-177 4.50e-05

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 43.40  E-value: 4.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634  41 NPLRLGYIAErsgglfGKKVLDVGCGGGI---LAesmARE-GAT--VTGLDMGFEPLQVARLHALESGVQ-VEYVQETVe 113
Cdd:PRK11873  68 NPTALAELKP------GETVLDLGSGGGFdcfLA---ARRvGPTgkVIGVDMTPEMLAKARANARKAGYTnVEFRLGEI- 137

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493864634 114 EHAAKHAHQYDVV--TCMEMLehVPDPQSVVSACAKLVKPGGQVFFS----------TINRNGKAWLMAVVGAEYV 177
Cdd:PRK11873 138 EALPVADNSVDVIisNCVINL--SPDKERVFKEAFRVLKPGGRFAISdvvlrgelpeEIRNDAELYAGCVAGALQE 211
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 57-191 4.56e-05

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 43.97  E-value: 4.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634  57 GKKVLDVGCGGGILAESMARE-GATVTGLDMGFEPLQVARLHALESGVQVEYvqeTVEEHAAKH--AHQYDVVTCMEMLE 133
Cdd:PLN02336 267 GQKVLDVGCGIGGGDFYMAENfDVHVVGIDLSVNMISFALERAIGRKCSVEF---EVADCTKKTypDNSFDVIYSRDTIL 343

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634 134 HVPDPQSVVSACAKLVKPGGQVFFSTINRNGKAwlmavVGAEYVLRMVPKG--THDVKKF 191
Cdd:PLN02336 344 HIQDKPALFRSFFKWLKPGGKVLISDYCRSPGT-----PSPEFAEYIKQRGydLHDVQAY 398
RsmG COG0357
16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ...
 57-157 6.46e-05

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: 42.45  E-value: 6.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634  57 GKKVLDVGCGGG----ILAesMAREGATVTGLDmgfePL--------QVARLHALEsGVQVeyVQETVEEHAAKhaHQYD 124
Cdd:COG0357   68 GARVLDVGSGAGfpgiPLA--IARPDLQVTLVD----SLgkkiaflrEVVRELGLK-NVTV--VHGRAEELAPR--EKFD 136

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 493864634 125 VVTC-----MEMLehvpdpqsvVSACAKLVKPGGQVFF 157
Cdd:COG0357  137 VVTAravapLPDL---------LELALPLLKPGGRLLA 165
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 56-128 1.47e-04

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: 41.04  E-value: 1.47e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493864634   56 FGKKVLDVGCGGGILAESMAREG--ATVTGLDMGFEPLQVARLHALESGVQ-VEYVQETVeeHAAKHAHQYDVVTC 128
Cdd:pfam05175  31 LSGKVLDLGCGAGVLGAALAKESpdAELTMVDINARALESARENLAANGLEnGEVVASDV--YSGVEDGKFDLIIS 104
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 57-105 3.25e-04

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 40.90  E-value: 3.25e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 493864634  57 GKKVLDVGCGGGILAESMARE--GATVTGLDMGFEPLQVAR----LHALESGVQV 105
Cdd:COG2890  113 PPRVLDLGTGSGAIALALAKErpDARVTAVDISPDALAVARrnaeRLGLEDRVRF 167
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 57-160 5.03e-04

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


Pssm-ID: 396777 [Multi-domain]  Cd Length: 272  Bit Score: 40.39  E-value: 5.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634   57 GKKVLDVGCG-GGILAESMAREGATVTGLDMgfeplqvarlhaleSGVQVEYVQETVEEHAAKHAH------------QY 123
Cdd:pfam02353  62 GMTLLDIGCGwGGLMRRAAERYDVNVVGLTL--------------SKNQYKLARKRVAAEGLARKVevllqdyrdfdePF 127

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 493864634  124 DVVTCMEMLEHV-----PDpqsVVSACAKLVKPGGQVFFSTI 160
Cdd:pfam02353 128 DRIVSVGMFEHVghenyDT---FFKKLYNLLPPGGLMLLHTI 166
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 60-160 3.85e-03

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 37.43  E-value: 3.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634  60 VLDVGCGGGILAESMAREGATVTGLDMGFEPLQVARlhalesgvqveyvqetvEEHAAKHAHQYDVvtcmemlEHVPDPQ 139
Cdd:PRK10258  46 VLDAGCGPGWMSRYWRERGSQVTALDLSPPMLAQAR-----------------QKDAADHYLAGDI-------ESLPLAT 101

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 493864634 140 SV---------VSACAKL----------VKPGGQVFFSTI 160
Cdd:PRK10258 102 ATfdlawsnlaVQWCGNLstalrelyrvVRPGGVVAFTTL 141
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
57-156 5.11e-03

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 36.94  E-value: 5.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634  57 GKKVLDVGCGGGILAESMAREGAT-VTGLDMGFEPLQVARLHALESGV--QVEYVQetveehaaKHAHQY------DVVT 127
Cdd:COG4076   36 GDVVLDIGTGSGLLSMLAARAGAKkVYAVEVNPDIAAVARRIIAANGLsdRITVIN--------ADATDLdlpekaDVII 107

                         90       100       110
                 ....*....|....*....|....*....|...
gi 493864634 128 CmEMLEHV-PDPQSV---VSACAKLVKPGGQVF 156
Cdd:COG4076  108 S-EMLDTAlLDEGQVpilNHARKRLLKPGGRII 139
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 57-105 5.88e-03

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 37.06  E-value: 5.88e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 493864634  57 GKKVLDVGCGGGILAESMARE--GATVTGLDMGFEPLQVAR---LHALESGVQV 105
Cdd:PRK09328 109 PLRVLDLGTGSGAIALALAKErpDAEVTAVDISPEALAVARrnaKHGLGARVEF 162
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 57-128 6.26e-03

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: 36.71  E-value: 6.26e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493864634  57 GKKVLDVGCGGGILAESMARE--GATVTGLDMGFEPLQVARLHALESGVQ-VEYVQETVEEHAAkhAHQYDVVTC 128
Cdd:COG2813   50 GGRVLDLGCGYGVIGLALAKRnpEARVTLVDVNARAVELARANAAANGLEnVEVLWSDGLSGVP--DGSFDLILS 122
MDR1 cd08267
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 57-183 9.33e-03

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent 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. 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: 176228 [Multi-domain]  Cd Length: 319  Bit Score: 36.81  E-value: 9.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493864634  57 GKKVLDVGCGGGI--LAESMAR-EGATVTG------LDMgfeplqVARLHALEsgVqVEYVQETVEEHAAKHaHQYDVVt 127
Cdd:cd08267  144 GQRVLINGASGGVgtFAVQIAKaLGAHVTGvcstrnAEL------VRSLGADE--V-IDYTTEDFVALTAGG-EKYDVI- 212

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 493864634 128 cmemLEHVPDPQSVVSACAKLVKPGGQvfFSTINRNGKAWLMAVVGAEYVLRMVPK 183
Cdd:cd08267  213 ----FDAVGNSPFSLYRASLALKPGGR--YVSVGGGPSGLLLVLLLLPLTLGGGGR 262
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH