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Conserved domains on  [gi|491994992|ref|WP_005711610|]
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bifunctional 2-polyprenyl-6-hydroxyphenol methylase/3-demethylubiquinol 3-O-methyltransferase UbiG [Glaesserella parasuis]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AdoMet_MTases super family cl17173
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 8-230 1.49e-112

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


The actual alignment was detected with superfamily member TIGR01983:

Pssm-ID: 473071  Cd Length: 224  Bit Score: 321.55  E-value: 1.49e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992    8 EVEKFEKMAKTWWDPQGDFKPIHLLNPLRLAYINDK-----TNGLFGKKVLDIGCGGGILSESMAGLGAIVTGIDMAADA 82
Cdd:TIGR01983   1 EIAKFSALAHEWWDPNGKFKPLHKMNPLRLDYIRDRirknfKNPLDGLRVLDVGCGGGLLSEPLARLGANVTGIDASEEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992   83 LLVARQHAESNHLNICYQQITVEDFLKQHcitdTEKFDIITCMEVLEHVPNPHSIIQSCKNLLKEDGLLFISTINRTAKA 162
Cdd:TIGR01983  81 IEVAKLHAKKDPLQIDYRCTTVEDLAEKK----AGSFDVVTCMEVLEHVPDPQAFIRACAQLLKPGGILFFSTINRTPKS 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491994992  163 YMLIIIGAEYVLKMLPKGTHNFEKFIKPSELLRWCSQEDFECKEIVGYHFNPLTKNFWINKDINCNYI 230
Cdd:TIGR01983 157 YLLAIVGAEYILRIVPKGTHDWEKFIKPSELLSWLESAGLRVKDIKGLVYNPIKNTWKLSKDTDVNYM 224
 
Name Accession Description Interval E-value
UbiG TIGR01983
ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase ...
 8-230 1.49e-112

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: 321.55  E-value: 1.49e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992    8 EVEKFEKMAKTWWDPQGDFKPIHLLNPLRLAYINDK-----TNGLFGKKVLDIGCGGGILSESMAGLGAIVTGIDMAADA 82
Cdd:TIGR01983   1 EIAKFSALAHEWWDPNGKFKPLHKMNPLRLDYIRDRirknfKNPLDGLRVLDVGCGGGLLSEPLARLGANVTGIDASEEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992   83 LLVARQHAESNHLNICYQQITVEDFLKQHcitdTEKFDIITCMEVLEHVPNPHSIIQSCKNLLKEDGLLFISTINRTAKA 162
Cdd:TIGR01983  81 IEVAKLHAKKDPLQIDYRCTTVEDLAEKK----AGSFDVVTCMEVLEHVPDPQAFIRACAQLLKPGGILFFSTINRTPKS 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491994992  163 YMLIIIGAEYVLKMLPKGTHNFEKFIKPSELLRWCSQEDFECKEIVGYHFNPLTKNFWINKDINCNYI 230
Cdd:TIGR01983 157 YLLAIVGAEYILRIVPKGTHDWEKFIKPSELLSWLESAGLRVKDIKGLVYNPIKNTWKLSKDTDVNYM 224
PLN02396 PLN02396
hexaprenyldihydroxybenzoate methyltransferase
 2-231 2.69e-62

hexaprenyldihydroxybenzoate methyltransferase


Pssm-ID: 178018 [Multi-domain]  Cd Length: 322  Bit Score: 197.65  E-value: 2.69e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992   2 NNIDQQEVEKFEKMAKTWWDPQGDFKPIHLLNPLRLAYINDKTNGLFGK-----------KVLDIGCGGGILSESMAGLG 70
Cdd:PLN02396  74 TSLNEDELAKFSAIADTWWHSEGPFKPLHQMNPTRLAFIRSTLCRHFSKdpssakpfeglKFIDIGCGGGLLSEPLARMG 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992  71 AIVTGIDMAADALLVARQHAESNHLN--ICYQQITVEDFLKQHcitdtEKFDIITCMEVLEHVPNPHSIIQSCKNLLKED 148
Cdd:PLN02396 154 ATVTGVDAVDKNVKIARLHADMDPVTstIEYLCTTAEKLADEG-----RKFDAVLSLEVIEHVANPAEFCKSLSALTIPN 228

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992 149 GLLFISTINRTAKAYMLIIIGAEYVLKMLPKGTHNFEKFIKPSELLRWCSQEDFECKEIVGYHFNPLTKNFWINKDINCN 228
Cdd:PLN02396 229 GATVLSTINRTMRAYASTIVGAEYILRWLPKGTHQWSSFVTPEELSMILQRASVDVKEMAGFVYNPITGRWLLSDDISVN 308


                 ...
gi 491994992 229 YIA 231
Cdd:PLN02396 309 YIA 311
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 49-157 1.69e-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: 132.83  E-value: 1.69e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992  49 GKKVLDIGCGGGILSESMAGLGAIVTGIDMAADALLVARQHAEsnHLNICYQQITVEDFLKQHcitdtEKFDIITCMEVL 128
Cdd:COG2227   25 GGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAA--ELNVDFVQGDLEDLPLED-----GSFDLVICSEVL 97

                         90       100
                 ....*....|....*....|....*....
gi 491994992 129 EHVPNPHSIIQSCKNLLKEDGLLFISTIN 157
Cdd:COG2227   98 EHLPDPAALLRELARLLKPGGLLLLSTPN 126
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 49-203 1.18e-21

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 87.87  E-value: 1.18e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992   49 GKKVLDIGCGGGILSESMAGLGAIVTGIDMAADALLVARQhaesnhlnicyqQITVEDFLKQHCITDTEKFDIITCMEVL 128
Cdd:pfam13489  23 PGRVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERALL------------NVRFDQFDEQEAAVPAGKFDVIVAREVL 90

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491994992  129 EHVPNPHSIIQSCKNLLKEDGLLFISTINRTAKAYMLiiigAEYVLKMLPKGTHNfeKFIKPSELLRWCSQEDFE 203
Cdd:pfam13489  91 EHVPDPPALLRQIAALLKPGGLLLLSTPLASDEADRL----LLEWPYLRPRNGHI--SLFSARSLKRLLEEAGFE 159
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 51-154 1.28e-14

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: 67.46  E-value: 1.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992  51 KVLDIGCGGGILSESMA-GLGAIVTGIDMAADALlvarQHAESNHLNICYQQITV--EDFLKQHCITDtEKFDIITCMEV 127
Cdd:cd02440    1 RVLDLGCGTGALALALAsGPGARVTGVDISPVAL----ELARKAAAALLADNVEVlkGDAEELPPEAD-ESFDVIISDPP 75

                         90       100
                 ....*....|....*....|....*...
gi 491994992 128 LEH-VPNPHSIIQSCKNLLKEDGLLFIS 154
Cdd:cd02440   76 LHHlVEDLARFLEEARRLLKPGGVLVLT 103
 
Name Accession Description Interval E-value
UbiG TIGR01983
ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase ...
 8-230 1.49e-112

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: 321.55  E-value: 1.49e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992    8 EVEKFEKMAKTWWDPQGDFKPIHLLNPLRLAYINDK-----TNGLFGKKVLDIGCGGGILSESMAGLGAIVTGIDMAADA 82
Cdd:TIGR01983   1 EIAKFSALAHEWWDPNGKFKPLHKMNPLRLDYIRDRirknfKNPLDGLRVLDVGCGGGLLSEPLARLGANVTGIDASEEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992   83 LLVARQHAESNHLNICYQQITVEDFLKQHcitdTEKFDIITCMEVLEHVPNPHSIIQSCKNLLKEDGLLFISTINRTAKA 162
Cdd:TIGR01983  81 IEVAKLHAKKDPLQIDYRCTTVEDLAEKK----AGSFDVVTCMEVLEHVPDPQAFIRACAQLLKPGGILFFSTINRTPKS 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491994992  163 YMLIIIGAEYVLKMLPKGTHNFEKFIKPSELLRWCSQEDFECKEIVGYHFNPLTKNFWINKDINCNYI 230
Cdd:TIGR01983 157 YLLAIVGAEYILRIVPKGTHDWEKFIKPSELLSWLESAGLRVKDIKGLVYNPIKNTWKLSKDTDVNYM 224
PLN02396 PLN02396
hexaprenyldihydroxybenzoate methyltransferase
 2-231 2.69e-62

hexaprenyldihydroxybenzoate methyltransferase


Pssm-ID: 178018 [Multi-domain]  Cd Length: 322  Bit Score: 197.65  E-value: 2.69e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992   2 NNIDQQEVEKFEKMAKTWWDPQGDFKPIHLLNPLRLAYINDKTNGLFGK-----------KVLDIGCGGGILSESMAGLG 70
Cdd:PLN02396  74 TSLNEDELAKFSAIADTWWHSEGPFKPLHQMNPTRLAFIRSTLCRHFSKdpssakpfeglKFIDIGCGGGLLSEPLARMG 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992  71 AIVTGIDMAADALLVARQHAESNHLN--ICYQQITVEDFLKQHcitdtEKFDIITCMEVLEHVPNPHSIIQSCKNLLKED 148
Cdd:PLN02396 154 ATVTGVDAVDKNVKIARLHADMDPVTstIEYLCTTAEKLADEG-----RKFDAVLSLEVIEHVANPAEFCKSLSALTIPN 228

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992 149 GLLFISTINRTAKAYMLIIIGAEYVLKMLPKGTHNFEKFIKPSELLRWCSQEDFECKEIVGYHFNPLTKNFWINKDINCN 228
Cdd:PLN02396 229 GATVLSTINRTMRAYASTIVGAEYILRWLPKGTHQWSSFVTPEELSMILQRASVDVKEMAGFVYNPITGRWLLSDDISVN 308


                 ...
gi 491994992 229 YIA 231
Cdd:PLN02396 309 YIA 311
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 49-157 1.69e-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: 132.83  E-value: 1.69e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992  49 GKKVLDIGCGGGILSESMAGLGAIVTGIDMAADALLVARQHAEsnHLNICYQQITVEDFLKQHcitdtEKFDIITCMEVL 128
Cdd:COG2227   25 GGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAA--ELNVDFVQGDLEDLPLED-----GSFDLVICSEVL 97

                         90       100
                 ....*....|....*....|....*....
gi 491994992 129 EHVPNPHSIIQSCKNLLKEDGLLFISTIN 157
Cdd:COG2227   98 EHLPDPAALLRELARLLKPGGLLLLSTPN 126
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 49-158 6.90e-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: 95.45  E-value: 6.90e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992  49 GKKVLDIGCGGGILSESMAGLGAIVTGIDMAADALLVARQHAESNHLNICYQQITVED--FlkqhcitDTEKFDIITCME 126
Cdd:COG2226   23 GARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGLNVEFVVGDAEDlpF-------PDGSFDLVISSF 95

                         90       100       110
                 ....*....|....*....|....*....|..
gi 491994992 127 VLEHVPNPHSIIQSCKNLLKEDGLLFISTINR 158
Cdd:COG2226   96 VLHHLPDPERALAEIARVLKPGGRLVVVDFSP 127
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 49-203 1.18e-21

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 87.87  E-value: 1.18e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992   49 GKKVLDIGCGGGILSESMAGLGAIVTGIDMAADALLVARQhaesnhlnicyqQITVEDFLKQHCITDTEKFDIITCMEVL 128
Cdd:pfam13489  23 PGRVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERALL------------NVRFDQFDEQEAAVPAGKFDVIVAREVL 90

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491994992  129 EHVPNPHSIIQSCKNLLKEDGLLFISTINRTAKAYMLiiigAEYVLKMLPKGTHNfeKFIKPSELLRWCSQEDFE 203
Cdd:pfam13489  91 EHVPDPPALLRQIAALLKPGGLLLLSTPLASDEADRL----LLEWPYLRPRNGHI--SLFSARSLKRLLEEAGFE 159
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 52-149 1.43e-21

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 85.31  E-value: 1.43e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992   52 VLDIGCGGGILSESMAG-LGAIVTGIDMAADALLVARQHAESNHLNICYQQITVEDFLkqhciTDTEKFDIITCMEVLEH 130
Cdd:pfam13649   1 VLDLGCGTGRLTLALARrGGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLP-----FPDGSFDLVVSSGVLHH 75

                          90       100
                  ....*....|....*....|.
gi 491994992  131 VPNP--HSIIQSCKNLLKEDG 149
Cdd:pfam13649  76 LPDPdlEAALREIARVLKPGG 96
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 53-153 3.51e-21

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 84.25  E-value: 3.51e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992   53 LDIGCGGGILSESMAGLGAIVTGIDMAADALLVARQHAESNHLNicYQQITVED--FlkqhcitDTEKFDIITCMEVLEH 130
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREGLT--FVVGDAEDlpF-------PDNSFDLVLSSEVLHH 71

                          90       100
                  ....*....|....*....|...
gi 491994992  131 VPNPHSIIQSCKNLLKEDGLLFI 153
Cdd:pfam08241  72 VEDPERALREIARVLKPGGILII 94
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 49-155 9.91e-19

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 79.97  E-value: 9.91e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992  49 GKKVLDIGCGGGILSESMAG-LGAIVTGIDMAADALLVARQHAESNHLNicyQQITVE--DFLKqhcITDTEKFDIITCM 125
Cdd:COG2230   52 GMRVLDIGCGWGGLALYLARrYGVRVTGVTLSPEQLEYARERAAEAGLA---DRVEVRlaDYRD---LPADGQFDAIVSI 125

                         90       100       110
                 ....*....|....*....|....*....|..
gi 491994992 126 EVLEHVPNPH--SIIQSCKNLLKEDGLLFIST 155
Cdd:COG2230  126 GMFEHVGPENypAYFAKVARLLKPGGRLLLHT 157
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 49-154 1.26e-18

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 80.73  E-value: 1.26e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992  49 GKKVLDIGCGGGILSESMAGL-GAIVTGIDMAADALLVARQHAESNHL-NICYQQITVEDFLKqhciTDTEKFDIITCME 126
Cdd:COG0500   27 GGRVLDLGCGTGRNLLALAARfGGRVIGIDLSPEAIALARARAAKAGLgNVEFLVADLAELDP----LPAESFDLVVAFG 102

                         90       100       110
                 ....*....|....*....|....*....|
gi 491994992 127 VLEHVP--NPHSIIQSCKNLLKEDGLLFIS 154
Cdd:COG0500  103 VLHHLPpeEREALLRELARALKPGGVLLLS 132
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
12-155 1.64e-18

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 80.04  E-value: 1.64e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992  12 FEKMAKTW----WDPQGDFKPIHLLNPLRLAYINDKtnglfGKKVLDIGCGGGILSESMAGLGAIVTGIDMAADALLVAR 87
Cdd:COG4976   11 FDQYADSYdaalVEDLGYEAPALLAEELLARLPPGP-----FGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAR 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491994992  88 QHAesnhlniCYQQITVEDFLKQHciTDTEKFDIITCMEVLEHVPNPHSIIQSCKNLLKEDGLLFIST 155
Cdd:COG4976   86 EKG-------VYDRLLVADLADLA--EPDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGGLFIFSV 144
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 49-157 9.54e-17

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 74.38  E-value: 9.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992   49 GKKVLDIGCGGGILSESMAGL---GAIVTGIDMAADALLVARQHAESNHL-NICYQQitvEDFLKQHCITDTEKFDIITC 124
Cdd:pfam13847   4 GMRVLDLGCGTGHLSFELAEElgpNAEVVGIDISEEAIEKARENAQKLGFdNVEFEQ---GDIEELPELLEDDKFDVVIS 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 491994992  125 MEVLEHVPNPHSIIQSCKNLLKEDGLLFISTIN 157
Cdd:pfam13847  81 NCVLNHIPDPDKVLQEILRVLKPGGRLIISDPD 113
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 53-151 4.54e-16

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 71.24  E-value: 4.54e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992   53 LDIGCGGGILSESMAGL--GAIVTGIDMAADALLVARQHAESNHLNICYQ-QITVEDFLKQhcitDTEKFDIITCMEVLE 129
Cdd:pfam08242   1 LEIGCGTGTLLRALLEAlpGLEYTGLDISPAALEAARERLAALGLLNAVRvELFQLDLGEL----DPGSFDVVVASNVLH 76

                          90       100
                  ....*....|....*....|..
gi 491994992  130 HVPNPHSIIQSCKNLLKEDGLL 151
Cdd:pfam08242  77 HLADPRAVLRNIRRLLKPGGVL 98
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
49-155 1.22e-15

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 69.85  E-value: 1.22e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992  49 GKKVLDIGCGGGILSESMAGL--GAIVTGIDMAADALLVARQHAEsnhlNICYQQITVEDFlkqhciTDTEKFDIITCME 126
Cdd:COG4106    2 PRRVLDLGCGTGRLTALLAERfpGARVTGVDLSPEMLARARARLP----NVRFVVADLRDL------DPPEPFDLVVSNA 71

                         90       100
                 ....*....|....*....|....*....
gi 491994992 127 VLEHVPNPHSIIQSCKNLLKEDGLLFIST 155
Cdd:COG4106   72 ALHWLPDHAALLARLAAALAPGGVLAVQV 100
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 51-154 1.28e-14

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: 67.46  E-value: 1.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992  51 KVLDIGCGGGILSESMA-GLGAIVTGIDMAADALlvarQHAESNHLNICYQQITV--EDFLKQHCITDtEKFDIITCMEV 127
Cdd:cd02440    1 RVLDLGCGTGALALALAsGPGARVTGVDISPVAL----ELARKAAAALLADNVEVlkGDAEELPPEAD-ESFDVIISDPP 75

                         90       100
                 ....*....|....*....|....*...
gi 491994992 128 LEH-VPNPHSIIQSCKNLLKEDGLLFIS 154
Cdd:cd02440   76 LHHlVEDLARFLEEARRLLKPGGVLVLT 103
PRK08317 PRK08317
hypothetical protein; Provisional
 49-149 3.17e-12

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 63.80  E-value: 3.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992  49 GKKVLDIGCGGGILSESMAGL---GAIVTGIDMAADALLVARQHAESNHLNICYQQiTVEDFLKqhciTDTEKFDIITCM 125
Cdd:PRK08317  20 GDRVLDVGCGPGNDARELARRvgpEGRVVGIDRSEAMLALAKERAAGLGPNVEFVR-GDADGLP----FPDGSFDAVRSD 94

                         90       100
                 ....*....|....*....|....
gi 491994992 126 EVLEHVPNPHSIIQSCKNLLKEDG 149
Cdd:PRK08317  95 RVLQHLEDPARALAEIARVLRPGG 118
PRK15068 PRK15068
tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB;
36-204 2.17e-11

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


Pssm-ID: 237898  Cd Length: 322  Bit Score: 62.18  E-value: 2.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992  36 RLA-YINDktngLFGKKVLDIGCGGGILSESMAGLGA-IVTGID------MAADALlvarQHAESNHLNICYQQITVEDf 107
Cdd:PRK15068 113 RVLpHLSP----LKGRTVLDVGCGNGYHMWRMLGAGAkLVVGIDpsqlflCQFEAV----RKLLGNDQRAHLLPLGIEQ- 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992 108 lkqhcITDTEKFDIITCMEVLEHVPNPHSIIQSCKNLLKEDGLLFISTinrtakaymLIIIG-AEYVLkmLPKGT----H 182
Cdd:PRK15068 184 -----LPALKAFDTVFSMGVLYHRRSPLDHLKQLKDQLVPGGELVLET---------LVIDGdENTVL--VPGDRyakmR 247

                        170       180
                 ....*....|....*....|....*..
gi 491994992 183 NFeKFIkPS--ELLRWCSQ---EDFEC 204
Cdd:PRK15068 248 NV-YFI-PSvpALKNWLERagfKDVRI 272
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 49-153 3.34e-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: 58.23  E-value: 3.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992  49 GKKVLDIGCGGGILSESMA--GLGAIVTGIDMAADALLVARQHAESNHLNicyQQITVE--DFLKQHCITDTEKFDIITC 124
Cdd:COG4123   38 GGRVLDLGTGTGVIALMLAqrSPGARITGVEIQPEAAELARRNVALNGLE---DRITVIhgDLKEFAAELPPGSFDLVVS 114

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 491994992 125 ----MEVLEHVPNPHS---------------IIQSCKNLLKEDGLLFI 153
Cdd:COG4123  115 nppyFKAGSGRKSPDEaraiarhedaltledLIRAAARLLKPGGRFAL 162
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
49-154 4.74e-10

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 58.26  E-value: 4.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992  49 GKKVLDIGCGGGILseSMAG--LGAI-VTGIDMAADALLVARQHAESNHLNicyQQITVE--DFLKQhcitdtEKFDIIT 123
Cdd:COG2264  149 GKTVLDVGCGSGIL--AIAAakLGAKrVLAVDIDPVAVEAARENAELNGVE---DRIEVVlgDLLED------GPYDLVV 217

                         90       100       110
                 ....*....|....*....|....*....|....
gi 491994992 124 C---MEVLEhvpnphSIIQSCKNLLKEDGLLFIS 154
Cdd:COG2264  218 AnilANPLI------ELAPDLAALLKPGGYLILS 245
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
49-156 1.27e-09

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 56.70  E-value: 1.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992  49 GKKVLDIGCGGGILSESMAGLGAI-VTGIDMAADALLVARQHAESNHlnicyqqITVEDFLKQhcitDTEKFDIITC--- 124
Cdd:PRK00517 120 GKTVLDVGCGSGILAIAAAKLGAKkVLAVDIDPQAVEAARENAELNG-------VELNVYLPQ----GDLKADVIVAnil 188

                         90       100       110
                 ....*....|....*....|....*....|..
gi 491994992 125 MEVLEHvpnphsIIQSCKNLLKEDGLLFISTI 156
Cdd:PRK00517 189 ANPLLE------LAPDLARLLKPGGRLILSGI 214
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 49-128 1.45e-09

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: 56.05  E-value: 1.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992  49 GKKVLDIGCGGGILSESMAGLGAI-VTGIDMAADALLVARQHAESNHLNIcyqQITVEDFLKQhciTDTEKFDIITCMEV 127
Cdd:COG3897   71 GKRVLELGCGLGLVGIAAAKAGAAdVTATDYDPEALAALRLNAALNGVAI---TTRLGDWRDP---PAAGGFDLILGGDV 144


                 .
gi 491994992 128 L 128
Cdd:COG3897  145 L 145
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 49-156 2.56e-09

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: 56.12  E-value: 2.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992   49 GKKVLDIGCGGGILSESMAGLGAI-VTGIDMAADALLVARQHAESNHLNICYQQITVEDFLKqhcitdtEKFDIITC--- 124
Cdd:pfam06325 162 GESVLDVGCGSGILAIAALKLGAKkVVGVDIDPVAVRAAKENAELNGVEARLEVYLPGDLPK-------EKADVVVAnil 234

                          90       100       110
                  ....*....|....*....|....*....|..
gi 491994992  125 MEVLEHvpnphsIIQSCKNLLKEDGLLFISTI 156
Cdd:pfam06325 235 ADPLIE------LAPDIYALVKPGGYLILSGI 260
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
37-122 5.82e-09

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 54.14  E-value: 5.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992  37 LAYINdktNGLFGKKVLDIGCGGGILSESMAGLGA-IVTGIDMAADALLVARQHAESNHLNIcyqQITVEDFLKqhcITD 115
Cdd:COG2263   37 LAYLR---GDIEGKTVLDLGCGTGMLAIGAALLGAkKVVGVDIDPEALEIARENAERLGVRV---DFIRADVTR---IPL 107


                 ....*..
gi 491994992 116 TEKFDII 122
Cdd:COG2263  108 GGSVDTV 114
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 49-153 5.41e-08

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 52.07  E-value: 5.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992  49 GKKVLDIGCGGGILSESMAGL--GAIVTGIDMAADALLVARQHAESNHLNicyQQITVE--DFLKQhcITDTEKFDIITC 124
Cdd:COG2890  113 PPRVLDLGTGSGAIALALAKErpDARVTAVDISPDALAVARRNAERLGLE---DRVRFLqgDLFEP--LPGDGRFDLIVS 187

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 491994992 125 ------------M--EVLEHvpNPHS--------------IIQSCKNLLKEDGLLFI 153
Cdd:COG2890  188 nppyipedeialLppEVRDH--EPRLaldggedgldfyrrIIAQAPRLLKPGGWLLL 242
PRK14968 PRK14968
putative methyltransferase; Provisional
 49-123 6.72e-08

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 51.05  E-value: 6.72e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491994992  49 GKKVLDIGCGGGILSESMAGLGAIVTGIDMAADALLVARQHAESNHLNICYQQITVEDFLKqhCITDtEKFDIIT 123
Cdd:PRK14968  24 GDRVLEVGTGSGIVAIVAAKNGKKVVGVDINPYAVECAKCNAKLNNIRNNGVEVIRSDLFE--PFRG-DKFDVIL 95
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 48-158 7.02e-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: 50.67  E-value: 7.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992   48 FGKKVLDIGCGGGILSESMAGLG--AIVTGIDMAADALLVARQHAESNHLNICyqQITVEDFLKQhciTDTEKFDIITCm 125
Cdd:pfam05175  31 LSGKVLDLGCGAGVLGAALAKESpdAELTMVDINARALESARENLAANGLENG--EVVASDVYSG---VEDGKFDLIIS- 104

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 491994992  126 evlehvpNP-------------HSIIQSCKNLLKEDGLLFIsTINR 158
Cdd:pfam05175 105 -------NPpfhaglattynvaQRFIADAKRHLRPGGELWI-VANR 142
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 49-152 8.20e-08

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 51.38  E-value: 8.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992  49 GKKVLDIGCGGGILSESMAGLGAIVTGIDMAADALLVARQHAESNHLNicyQQItveDFLKQHCITDTEKFDIITCMEVL 128
Cdd:PRK07580  64 GLRILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEARERAPEAGLA---GNI---TFEVGDLESLLGRFDTVVCLDVL 137

                         90       100
                 ....*....|....*....|....*.
gi 491994992 129 EHVPNPhSIIQSCKNL--LKEDGLLF 152
Cdd:PRK07580 138 IHYPQE-DAARMLAHLasLTRGSLIF 162
PRK11705 PRK11705
cyclopropane fatty acyl phospholipid synthase;
49-159 1.36e-07

cyclopropane fatty acyl phospholipid synthase;


Pssm-ID: 183282  Cd Length: 383  Bit Score: 51.39  E-value: 1.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992  49 GKKVLDIGCGGGILSESMA-GLGAIVTGIDMAADALLVARQHAEsnHLNIcyqQITVEDFLKQHcitdtEKFDIITCMEV 127
Cdd:PRK11705 168 GMRVLDIGCGWGGLARYAAeHYGVSVVGVTISAEQQKLAQERCA--GLPV---EIRLQDYRDLN-----GQFDRIVSVGM 237

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 491994992 128 LEHV--PNPHSIIQSCKNLLKEDGLLFISTI--NRT 159
Cdd:PRK11705 238 FEHVgpKNYRTYFEVVRRCLKPDGLFLLHTIgsNKT 273
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 49-153 1.57e-07

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: 49.80  E-value: 1.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992  49 GKKVLDIGCGGGILSESMAGL--GAIVTGIDMAADALLVARQHAESNHLNICyqQITVEDFLKQhciTDTEKFDIITCme 126
Cdd:COG2813   50 GGRVLDLGCGYGVIGLALAKRnpEARVTLVDVNARAVELARANAAANGLENV--EVLWSDGLSG---VPDGSFDLILS-- 122

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 491994992 127 vlehvpNP-------------HSIIQSCKNLLKEDGLLFI 153
Cdd:COG2813  123 ------NPpfhagravdkevaHALIADAARHLRPGGELWL 156
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
 49-156 2.64e-07

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: 50.22  E-value: 2.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992   49 GKKVLDIGCGGGILSESMAGLGAI-VTGIDMAADALLVARQHAESNhlnicyqQITVEDFLKQHCITD--TEKFDIITCM 125
Cdd:TIGR00406 160 DKNVIDVGCGSGILSIAALKLGAAkVVGIDIDPLAVESARKNAELN-------QVSDRLQVKLIYLEQpiEGKADVIVAN 232

                          90       100       110
                  ....*....|....*....|....*....|.
gi 491994992  126 EVLEHVPNPHSIIQScknLLKEDGLLFISTI 156
Cdd:TIGR00406 233 ILAEVIKELYPQFSR---LVKPGGWLILSGI 260
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 49-153 7.76e-07

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 48.62  E-value: 7.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992  49 GKKVLDIGCGGGILSESMAGL--GAIVTGIDMAADALLVARQHAESNHLNicyqQITvedFLKQHCIT--DTEKFDIITC 124
Cdd:PRK09328 109 PLRVLDLGTGSGAIALALAKErpDAEVTAVDISPEALAVARRNAKHGLGA----RVE---FLQGDWFEplPGGRFDLIVS 181

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 491994992 125 ------------M--EVLEHvpNPHS--------------IIQSCKNLLKEDGLLFI 153
Cdd:PRK09328 182 nppyipeadihlLqpEVRDH--EPHLalfggedgldfyrrIIEQAPRYLKPGGWLLL 236
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 29-156 8.66e-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: 48.44  E-value: 8.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992   29 IHLLNPLrlayinDKTNGLFGKKVLDIGCGGGILSESMA--GLGAIVTGIDMAADALLVARQHaesNHLNICYQQITVEd 106
Cdd:TIGR02072  21 KRLLALL------KEKGIFIPASVLDIGCGTGYLTRALLkrFPQAEFIALDISAGMLAQAKTK---LSENVQFICGDAE- 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 491994992  107 flkqHCITDTEKFDIITCMEVLEHVPNPHSIIQSCKNLLKEDGLLFISTI 156
Cdd:TIGR02072  91 ----KLPLEDSSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTF 136
NodS pfam05401
Nodulation protein S (NodS); This family consists of nodulation S (NodS) proteins. The ...
 52-176 4.21e-06

Nodulation protein S (NodS); This family consists of nodulation S (NodS) proteins. The products of the rhizobial nodulation genes are involved in the biosynthesis of lipochitin oligosaccharides (LCOs), which are host-specific signal molecules required for nodule formation. NodS is an S-adenosyl-L-methionine (SAM)-dependent methyltransferase involved in N methylation of LCOs. NodS uses N-deacetylated chitooligosaccharides, the products of the NodBC proteins, as its methyl acceptors.


Pssm-ID: 428457  Cd Length: 201  Bit Score: 46.15  E-value: 4.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992   52 VLDIGCGGGILSESMAGLGAIVTGIDMAADALLVARQHAeSNHLNICYQQITVEDFlkqhciTDTEKFDIITCMEVLEHV 131
Cdd:pfam05401  47 ALEIGCAAGAFTEMLAILCERLTVVDLMPEAIAKAQERT-GKWSDIIWHECDICQF------DLNAKFDLIICAEVLYYI 119

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 491994992  132 PNP---HSIIQSCKNLLKEDG-LLFISTINRTAKAYMLiIIGAEYVLKM 176
Cdd:pfam05401 120 HDKeelHAAIENIVQLLAPDEqFIFGSARDAICQRWGH-AAGAEAVIAL 167
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
49-152 4.22e-06

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 46.18  E-value: 4.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992  49 GKKVLDIGCGGGILSESMAGLGAI-VTGIDMAADALLVARQHAESNHLNicyQQITVEDFLKQHcITDTEKFDIITC--- 124
Cdd:COG4076   36 GDVVLDIGTGSGLLSMLAARAGAKkVYAVEVNPDIAAVARRIIAANGLS---DRITVINADATD-LDLPEKADVIISeml 111

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 491994992 125 ---------MEVLEHVPnphsiiqscKNLLKEDGLLF 152
Cdd:COG4076  112 dtalldegqVPILNHAR---------KRLLKPGGRII 139
PRK11036 PRK11036
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
52-203 7.34e-06

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


Pssm-ID: 182918  Cd Length: 255  Bit Score: 45.72  E-value: 7.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992  52 VLDIGCGGGILSESMAGLGAIVTGIDMAADALLVARQHAESNHLNICYQ--QITVEDfLKQHCitdTEKFDIITCMEVLE 129
Cdd:PRK11036  48 VLDAGGGEGQTAIKLAELGHQVILCDLSAEMIQRAKQAAEAKGVSDNMQfiHCAAQD-IAQHL---ETPVDLILFHAVLE 123

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491994992 130 HVPNPHSIIQSCKNLLKEDGLLFISTINRTAKAYMLIIIGA-EYVLKMLPKG---THNFEKFIKPSELLRWCSQEDFE 203
Cdd:PRK11036 124 WVADPKSVLQTLWSVLRPGGALSLMFYNANGLLMHNMVAGNfDYVQAGMPKRkkrTLSPDYPLDPEQVYQWLEEAGWQ 201
PRK06202 PRK06202
hypothetical protein; Provisional
 52-165 1.34e-05

hypothetical protein; Provisional


Pssm-ID: 180466 [Multi-domain]  Cd Length: 232  Bit Score: 44.61  E-value: 1.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992  52 VLDIGCGGGILSESMA------GLGAIVTGIDMAADALLVARQHAESnhlnicyQQITVEDFLKQHCITDTEKFDIITCM 125
Cdd:PRK06202  64 LLDIGCGGGDLAIDLArwarrdGLRLEVTAIDPDPRAVAFARANPRR-------PGVTFRQAVSDELVAEGERFDVVTSN 136

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 491994992 126 EVLEHVPNPH--SIIQSCKNLLKedGLLFISTINRTAKAYML 165
Cdd:PRK06202 137 HFLHHLDDAEvvRLLADSAALAR--RLVLHNDLIRSRLAYAL 176
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 49-156 2.50e-05

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: 44.24  E-value: 2.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992   49 GKKVLDIGCG-GGILSESMAGLGAIVTGIDMAAdallvarqhaesNHLNICYQQITVEDF------LKQHCITDTEKFDI 121
Cdd:pfam02353  62 GMTLLDIGCGwGGLMRRAAERYDVNVVGLTLSK------------NQYKLARKRVAAEGLarkvevLLQDYRDFDEPFDR 129

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 491994992  122 ITCMEVLEHV--PNPHSIIQSCKNLLKEDGLLFISTI 156
Cdd:pfam02353 130 IVSVGMFEHVghENYDTFFKKLYNLLPPGGLMLLHTI 166
PLN02585 PLN02585
magnesium protoporphyrin IX methyltransferase
 49-132 5.26e-05

magnesium protoporphyrin IX methyltransferase


Pssm-ID: 215319 [Multi-domain]  Cd Length: 315  Bit Score: 43.31  E-value: 5.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992  49 GKKVLDIGCGGGILSESMAGLGAIVTGIDMAADalLVARQHAESNHLNICYQQITVEDFLKQHCITDTEKFDIITCMEVL 128
Cdd:PLN02585 145 GVTVCDAGCGTGSLAIPLALEGAIVSASDISAA--MVAEAERRAKEALAALPPEVLPKFEANDLESLSGKYDTVTCLDVL 222


                 ....
gi 491994992 129 EHVP 132
Cdd:PLN02585 223 IHYP 226
PLN02244 PLN02244
tocopherol O-methyltransferase
 50-203 1.01e-04

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 42.42  E-value: 1.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992  50 KKVLDIGCGGGILSESMA-GLGAIVTGIDM----AADALLVARQHAESNHLNicYQqitVEDFLKQHciTDTEKFDIITC 124
Cdd:PLN02244 120 KRIVDVGCGIGGSSRYLArKYGANVKGITLspvqAARANALAAAQGLSDKVS--FQ---VADALNQP--FEDGQFDLVWS 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992 125 MEVLEHVPnphsiiqscknllkeDGLLFISTINRTAKAYMLIIIgAEYVLKMLPKGthnfEKFIKPSE------------ 192
Cdd:PLN02244 193 MESGEHMP---------------DKRKFVQELARVAAPGGRIII-VTWCHRDLEPG----ETSLKPDEqklldkicaayy 252

                        170
                 ....*....|.
gi 491994992 193 LLRWCSQEDFE 203
Cdd:PLN02244 253 LPAWCSTSDYV 263
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 49-122 1.25e-04

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


Pssm-ID: 441866 [Multi-domain]  Cd Length: 377  Bit Score: 42.47  E-value: 1.25e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491994992  49 GKKVLDIGCGGGILSESMAGLGAIVTGIDMAADALLVARQHAESNHL-NICYQQITVEDFLKQhcITDTEKFDII 122
Cdd:COG2265  234 GERVLDLYCGVGTFALPLARRAKKVIGVEIVPEAVEDARENARLNGLkNVEFVAGDLEEVLPE--LLWGGRPDVV 306
Bmt2 pfam11968
25S rRNA (adenine(2142)-N(1))-methyltransferase, Bmt2; This entry represents Bmt2 and its ...
 31-156 1.78e-03

25S rRNA (adenine(2142)-N(1))-methyltransferase, Bmt2; This entry represents Bmt2 and its homogues. In Saccharomyces cerevisiae, Bmt2 is a nucleolar S-adenosylmethionine-dependent rRNA methyltransferase that is responsible for the N-1-methyl-adenosine base modification of 25S rRNA.It specifically methylates the N1 position of adenine 2142 in 25S rRNA.


Pssm-ID: 371825  Cd Length: 221  Bit Score: 38.38  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992   31 LLNPLRLAYINDKTnGLFGKKVLDIGCgggiLSE----SMAGLGAIVTGIDMaadallvarqhaESNHLNICYQqitveD 106
Cdd:pfam11968  36 LVEWLKPLLVRLKL-GEGKLRALEVGA----LSTknaiSKCGLFDEVTRIDL------------NSQEPGILQQ-----D 93

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 491994992  107 FLKQHCITDT-EKFDIITCMEVLEHVPNPHS---IIQSCKNLLKEDGLLFISTI 156
Cdd:pfam11968  94 FMERPLPRDEsEKFDLISLSLVLNFVPDPADrgeMLKRCTKFLRPPGPASPPSL 147
PRK12335 PRK12335
tellurite resistance protein TehB; Provisional
 51-122 2.57e-03

tellurite resistance protein TehB; Provisional


Pssm-ID: 183450 [Multi-domain]  Cd Length: 287  Bit Score: 38.00  E-value: 2.57e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491994992  51 KVLDIGCGGGILSESMAGLGAIVTGIDMAADALLVARQHAESNHLNIcyqQITVEDfLKQHCItdTEKFDII 122
Cdd:PRK12335 123 KALDLGCGQGRNSLYLALLGFDVTAVDINQQSLENLQEIAEKENLNI---RTGLYD-INSASI--QEEYDFI 188
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 49-161 3.03e-03

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 38.19  E-value: 3.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992  49 GKKVLDIGCGGGILSESMA-GLGAIVTGIDMAADALLVARQHAESNHlniCYQQITVEDFLKQHCITDTekFDIITCMEV 127
Cdd:PLN02336 267 GQKVLDVGCGIGGGDFYMAeNFDVHVVGIDLSVNMISFALERAIGRK---CSVEFEVADCTKKTYPDNS--FDVIYSRDT 341

                         90       100       110
                 ....*....|....*....|....*....|....
gi 491994992 128 LEHVPNPHSIIQSCKNLLKEDGLLFISTINRTAK 161
Cdd:PLN02336 342 ILHIQDKPALFRSFFKWLKPGGKVLISDYCRSPG 375
YtxK COG0827
Adenine-specific DNA N6-methylase [Replication, recombination and repair];
28-152 4.47e-03

Adenine-specific DNA N6-methylase [Replication, recombination and repair];


Pssm-ID: 440589 [Multi-domain]  Cd Length: 327  Bit Score: 37.62  E-value: 4.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491994992  28 PIHLLNP----LRLAYINDKTNGLFGKKVLDIGCGGGILSES-MAGLGAIVT--GIDMAADALLVARQHAESNHLNIcyq 100
Cdd:COG0827   91 PNHQMTPdaigLLIGYLVEKFTKKEGLRILDPAVGTGNLLTTvLNQLKKKVNayGVEVDDLLIRLAAVLANLQGHPV--- 167

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491994992 101 QITVEDFLKQHCItdtEKFDIITC---------------MEVLEhvPNPHS------IIQSCkNLLKEDGLLF 152
Cdd:COG0827  168 ELFHQDALQPLLI---DPVDVVISdlpvgyypnderakrFKLKA--DEGHSyahhlfIEQSL-NYLKPGGYLF 234
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 52-105 7.04e-03

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 36.66  E-value: 7.04e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 491994992  52 VLDIGCGGGILSESMAGLGAIVTGIDMAADALLVARQHAESNHlnicYQQITVE 105
Cdd:PRK10258  46 VLDAGCGPGWMSRYWRERGSQVTALDLSPPMLAQARQKDAADH----YLAGDIE 95
arsM PRK11873
arsenite methyltransferase;
33-91 8.38e-03

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 36.46  E-value: 8.38e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491994992  33 NPLRLAYINDktnglfGKKVLDIGCGGGI---LSESMAGLGAIVTGIDMAADALLVARQHAE 91
Cdd:PRK11873  68 NPTALAELKP------GETVLDLGSGGGFdcfLAARRVGPTGKVIGVDMTPEMLAKARANAR 123
 
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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