NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|614093331|sp|P9WPB0|]
View 

RecName: Full=Mycolic acid methyltransferase MmaA1; AltName: Full=S-adenosylmethionine-dependent methyltransferase; Short=AdoMet-MT; Short=SAM-MT

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 12034117)

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; similar to Mycobacterium tuberculosis mycolic acid cyclopropane synthases (such as PcaA, CmaA, and MmaA) that are responsible for site-specific modifications of mycolic acids

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
CMAS super family cl47167
Mycolic acid cyclopropane synthetase; This family consist of ...
 4-286 0e+00

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.


The actual alignment was detected with superfamily member NF040660:

Pssm-ID: 481507  Cd Length: 283  Bit Score: 527.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614093331   4 LRPYYEESQSAYDISDDFFALFLDPTWVYTCAYFERDDMTLEEAQLAKVDLALDKLNLEPGMTLLDVGCGWGGALVRAVE 83
Cdd:NF040660   1 LRPHFEDVQAHYDLSDDFFALFLDPTQTYSCAYFERDDMTLEEAQIAKIDLALGKLNLEPGMTLLDIGCGWGATMRRAVE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614093331  84 KYDVNVIGLTLSRNHYERSKDRLAAIGTQRRAEARLQGWEEFEENVDRIVSFEAFDAFKKERYLTFFERSYDILPDDGRM 163
Cdd:NF040660  81 KYDVNVVGLTLSKNQAAHVQQVLDEIDTPRSRRVLLQGWEEFDEPVDRIVSIGAFEHFGHERYDDFFKRAYNILPADGRM 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614093331 164 LLHSLFTYDRRWLHEQGIALTMSDLRFLKFLRESIFPGGELPSEPDIVDNAQAAGFTIEHVQLLQQHYARTLDAWAANLQ 243
Cdd:NF040660 161 LLHTITGLHRKEMHERGLPLTMELARFIKFIVTEIFPGGRLPSIEMVVEHAEKAGFTVTRVQSLQPHYARTLDLWADALQ 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 614093331 244 AARERAIAVQSEEVYNNFMHYLTGCAERFRRGLINVAQFTMTK 286
Cdd:NF040660 241 AHKDEAIAIQSEEVYERYMKYLTGCAKLFRDGYIDVNQFTLAK 283
 
Name Accession Description Interval E-value
mycolic_MTase NF040660
cyclopropane mycolic acid synthase family methyltransferase; Members of this family include ...
 4-286 0e+00

cyclopropane mycolic acid synthase family methyltransferase; Members of this family include tailoring enzymes that make site-specific modifications to mycolic acid precursor molecules. These include Mycobacterium tuberculosis enzymes MmaA1-MmaA4, CmaA1-CmaA2, and PcaA. The family also includes UmaA, reported to be the lone member of this family not involved in mycolic acid biosynthesis. No members of this family are found in species that lack mycolic acids. This model excludes two more distantly related paralogs, Rv0447c (UfaA1 ) and Rv3720, that are also encoded in the Mycobacterium tuberculosis H37Rv genome.


Pssm-ID: 468626  Cd Length: 283  Bit Score: 527.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614093331   4 LRPYYEESQSAYDISDDFFALFLDPTWVYTCAYFERDDMTLEEAQLAKVDLALDKLNLEPGMTLLDVGCGWGGALVRAVE 83
Cdd:NF040660   1 LRPHFEDVQAHYDLSDDFFALFLDPTQTYSCAYFERDDMTLEEAQIAKIDLALGKLNLEPGMTLLDIGCGWGATMRRAVE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614093331  84 KYDVNVIGLTLSRNHYERSKDRLAAIGTQRRAEARLQGWEEFEENVDRIVSFEAFDAFKKERYLTFFERSYDILPDDGRM 163
Cdd:NF040660  81 KYDVNVVGLTLSKNQAAHVQQVLDEIDTPRSRRVLLQGWEEFDEPVDRIVSIGAFEHFGHERYDDFFKRAYNILPADGRM 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614093331 164 LLHSLFTYDRRWLHEQGIALTMSDLRFLKFLRESIFPGGELPSEPDIVDNAQAAGFTIEHVQLLQQHYARTLDAWAANLQ 243
Cdd:NF040660 161 LLHTITGLHRKEMHERGLPLTMELARFIKFIVTEIFPGGRLPSIEMVVEHAEKAGFTVTRVQSLQPHYARTLDLWADALQ 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 614093331 244 AARERAIAVQSEEVYNNFMHYLTGCAERFRRGLINVAQFTMTK 286
Cdd:NF040660 241 AHKDEAIAIQSEEVYERYMKYLTGCAKLFRDGYIDVNQFTLAK 283
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 3-282 8.07e-159

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: 442.92  E-value: 8.07e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614093331    3 KLRPYYEESQSAYDISDDFFALFLDPTWVYTCAYFERDDMTLEEAQLAKVDLALDKLNLEPGMTLLDVGCGWGGALVRAV 82
Cdd:pfam02353   1 SKTRDAENIQAHYDLSNDFFALFLDPTMTYSCAYFERPDMTLEEAQQAKLDLILDKLGLKPGMTLLDIGCGWGGLMRRAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614093331   83 EKYDVNVIGLTLSRNHYERSKDRLAAIGTQRRAEARLQGWEEFEENVDRIVSFEAFDAFKKERYLTFFERSYDILPDDGR 162
Cdd:pfam02353  81 ERYDVNVVGLTLSKNQYKLARKRVAAEGLARKVEVLLQDYRDFDEPFDRIVSVGMFEHVGHENYDTFFKKLYNLLPPGGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614093331  163 MLLHSLFTYDRRWLHEQGIAltmsdlrfLKFLRESIFPGGELPSEPDIVDNAQAAGFTIEHVQLLQQHYARTLDAWAANL 242
Cdd:pfam02353 161 MLLHTITGLHPDETSERGLP--------LKFIDKYIFPGGELPSISMIVESSSEAGFTVEDVESLRPHYAKTLDLWAENL 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 614093331  243 QAARERAIAVQSEEVYNNFMHYLTGCAERFRRGLINVAQF 282
Cdd:pfam02353 233 QANKDEAIALQSEEFYRMWMLYLTGCAVAFRIGYIDVHQF 272
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 15-167 5.19e-60

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 187.83  E-value: 5.19e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614093331  15 YDISDDFFALFLDPTWVYTCAYFERDDMTLEEAQLAKVDLALDKLNLEPGMTLLDVGCGWGGALVRAVEKYDVNVIGLTL 94
Cdd:COG2230    3 YDLGNDFYRLFLDPTMTYSCAYFEDPDDTLEEAQEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGVTL 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 614093331  95 SRNHYERSKDRLAAIGTQRRAEARLQGWEEF--EENVDRIVSFEAFDAFKKERYLTFFERSYDILPDDGRMLLHS 167
Cdd:COG2230   83 SPEQLEYARERAAEAGLADRVEVRLADYRDLpaDGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLLHT 157
PRK11705 PRK11705
cyclopropane fatty acyl phospholipid synthase;
15-273 1.71e-49

cyclopropane fatty acyl phospholipid synthase;


Pssm-ID: 183282  Cd Length: 383  Bit Score: 168.10  E-value: 1.71e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614093331  15 YDISDDFFALFLDPTWVYTCAYFERDDmTLEEAQLAKVDLALDKLNLEPGMTLLDVGCGWGGALVRAVEKYDVNVIGLTL 94
Cdd:PRK11705 120 YDLGNDLFEAMLDPRMQYSCGYWKDAD-TLEEAQEAKLDLICRKLQLKPGMRVLDIGCGWGGLARYAAEHYGVSVVGVTI 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614093331  95 SRNHyerskdrlAAIGTQRRA----EARLQGWEEFEENVDRIVSFEAFDAFKKERYLTFFERSYDILPDDGRMLLHSlft 170
Cdd:PRK11705 199 SAEQ--------QKLAQERCAglpvEIRLQDYRDLNGQFDRIVSVGMFEHVGPKNYRTYFEVVRRCLKPDGLFLLHT--- 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614093331 171 ydrrwlheqgIALTMSDLRFLKFLRESIFPGGELPSEPDIvdnAQAAG--FTIEHVQLLQQHYARTLDAWAANLQAARER 248
Cdd:PRK11705 268 ----------IGSNKTDTNVDPWINKYIFPNGCLPSVRQI---AQASEglFVMEDWHNFGADYDRTLMAWHENFEAAWPE 334

                        250       260
                 ....*....|....*....|....*
gi 614093331 249 AIAVQSEEVYNNFMHYLTGCAERFR 273
Cdd:PRK11705 335 LADNYSERFYRMWRYYLLSCAGAFR 359
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 66-166 5.89e-08

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: 50.12  E-value: 5.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614093331  66 TLLDVGCGWGGALVRAVEKYDVNVIGLTLSRNHYERSKDRLAAIGTQrRAEARLQGWEEF----EENVDRIVSFEAFDAF 141
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLAD-NVEVLKGDAEELppeaDESFDVIISDPPLHHL 79

                         90       100
                 ....*....|....*....|....*
gi 614093331 142 kKERYLTFFERSYDILPDDGRMLLH 166
Cdd:cd02440   80 -VEDLARFLEEARRLLKPGGVLVLT 103
 
Name Accession Description Interval E-value
mycolic_MTase NF040660
cyclopropane mycolic acid synthase family methyltransferase; Members of this family include ...
 4-286 0e+00

cyclopropane mycolic acid synthase family methyltransferase; Members of this family include tailoring enzymes that make site-specific modifications to mycolic acid precursor molecules. These include Mycobacterium tuberculosis enzymes MmaA1-MmaA4, CmaA1-CmaA2, and PcaA. The family also includes UmaA, reported to be the lone member of this family not involved in mycolic acid biosynthesis. No members of this family are found in species that lack mycolic acids. This model excludes two more distantly related paralogs, Rv0447c (UfaA1 ) and Rv3720, that are also encoded in the Mycobacterium tuberculosis H37Rv genome.


Pssm-ID: 468626  Cd Length: 283  Bit Score: 527.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614093331   4 LRPYYEESQSAYDISDDFFALFLDPTWVYTCAYFERDDMTLEEAQLAKVDLALDKLNLEPGMTLLDVGCGWGGALVRAVE 83
Cdd:NF040660   1 LRPHFEDVQAHYDLSDDFFALFLDPTQTYSCAYFERDDMTLEEAQIAKIDLALGKLNLEPGMTLLDIGCGWGATMRRAVE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614093331  84 KYDVNVIGLTLSRNHYERSKDRLAAIGTQRRAEARLQGWEEFEENVDRIVSFEAFDAFKKERYLTFFERSYDILPDDGRM 163
Cdd:NF040660  81 KYDVNVVGLTLSKNQAAHVQQVLDEIDTPRSRRVLLQGWEEFDEPVDRIVSIGAFEHFGHERYDDFFKRAYNILPADGRM 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614093331 164 LLHSLFTYDRRWLHEQGIALTMSDLRFLKFLRESIFPGGELPSEPDIVDNAQAAGFTIEHVQLLQQHYARTLDAWAANLQ 243
Cdd:NF040660 161 LLHTITGLHRKEMHERGLPLTMELARFIKFIVTEIFPGGRLPSIEMVVEHAEKAGFTVTRVQSLQPHYARTLDLWADALQ 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 614093331 244 AARERAIAVQSEEVYNNFMHYLTGCAERFRRGLINVAQFTMTK 286
Cdd:NF040660 241 AHKDEAIAIQSEEVYERYMKYLTGCAKLFRDGYIDVNQFTLAK 283
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 3-282 8.07e-159

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: 442.92  E-value: 8.07e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614093331    3 KLRPYYEESQSAYDISDDFFALFLDPTWVYTCAYFERDDMTLEEAQLAKVDLALDKLNLEPGMTLLDVGCGWGGALVRAV 82
Cdd:pfam02353   1 SKTRDAENIQAHYDLSNDFFALFLDPTMTYSCAYFERPDMTLEEAQQAKLDLILDKLGLKPGMTLLDIGCGWGGLMRRAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614093331   83 EKYDVNVIGLTLSRNHYERSKDRLAAIGTQRRAEARLQGWEEFEENVDRIVSFEAFDAFKKERYLTFFERSYDILPDDGR 162
Cdd:pfam02353  81 ERYDVNVVGLTLSKNQYKLARKRVAAEGLARKVEVLLQDYRDFDEPFDRIVSVGMFEHVGHENYDTFFKKLYNLLPPGGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614093331  163 MLLHSLFTYDRRWLHEQGIAltmsdlrfLKFLRESIFPGGELPSEPDIVDNAQAAGFTIEHVQLLQQHYARTLDAWAANL 242
Cdd:pfam02353 161 MLLHTITGLHPDETSERGLP--------LKFIDKYIFPGGELPSISMIVESSSEAGFTVEDVESLRPHYAKTLDLWAENL 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 614093331  243 QAARERAIAVQSEEVYNNFMHYLTGCAERFRRGLINVAQF 282
Cdd:pfam02353 233 QANKDEAIALQSEEFYRMWMLYLTGCAVAFRIGYIDVHQF 272
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 15-167 5.19e-60

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 187.83  E-value: 5.19e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614093331  15 YDISDDFFALFLDPTWVYTCAYFERDDMTLEEAQLAKVDLALDKLNLEPGMTLLDVGCGWGGALVRAVEKYDVNVIGLTL 94
Cdd:COG2230    3 YDLGNDFYRLFLDPTMTYSCAYFEDPDDTLEEAQEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGVTL 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 614093331  95 SRNHYERSKDRLAAIGTQRRAEARLQGWEEF--EENVDRIVSFEAFDAFKKERYLTFFERSYDILPDDGRMLLHS 167
Cdd:COG2230   83 SPEQLEYARERAAEAGLADRVEVRLADYRDLpaDGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLLHT 157
PRK11705 PRK11705
cyclopropane fatty acyl phospholipid synthase;
15-273 1.71e-49

cyclopropane fatty acyl phospholipid synthase;


Pssm-ID: 183282  Cd Length: 383  Bit Score: 168.10  E-value: 1.71e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614093331  15 YDISDDFFALFLDPTWVYTCAYFERDDmTLEEAQLAKVDLALDKLNLEPGMTLLDVGCGWGGALVRAVEKYDVNVIGLTL 94
Cdd:PRK11705 120 YDLGNDLFEAMLDPRMQYSCGYWKDAD-TLEEAQEAKLDLICRKLQLKPGMRVLDIGCGWGGLARYAAEHYGVSVVGVTI 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614093331  95 SRNHyerskdrlAAIGTQRRA----EARLQGWEEFEENVDRIVSFEAFDAFKKERYLTFFERSYDILPDDGRMLLHSlft 170
Cdd:PRK11705 199 SAEQ--------QKLAQERCAglpvEIRLQDYRDLNGQFDRIVSVGMFEHVGPKNYRTYFEVVRRCLKPDGLFLLHT--- 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614093331 171 ydrrwlheqgIALTMSDLRFLKFLRESIFPGGELPSEPDIvdnAQAAG--FTIEHVQLLQQHYARTLDAWAANLQAARER 248
Cdd:PRK11705 268 ----------IGSNKTDTNVDPWINKYIFPNGCLPSVRQI---AQASEglFVMEDWHNFGADYDRTLMAWHENFEAAWPE 334

                        250       260
                 ....*....|....*....|....*
gi 614093331 249 AIAVQSEEVYNNFMHYLTGCAERFR 273
Cdd:PRK11705 335 LADNYSERFYRMWRYYLLSCAGAFR 359
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 68-161 8.62e-09

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 51.80  E-value: 8.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614093331   68 LDVGCGWGGALVRAVEKYDVNVIGLTLSRNHYERSKDRLAAIGTQ-RRAEARLQGWEEFEENVDRIVSFEAFDAFKKERY 146
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLNvEFVQGDAEDLPFPDGSFDLVVSSGVLHHLPDPDL 81

                          90
                  ....*....|....*
gi 614093331  147 LTFFERSYDILPDDG 161
Cdd:pfam13649  82 EAALREIARVLKPGG 96
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 53-178 2.41e-08

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: 51.92  E-value: 2.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614093331  53 DLALDKLNLEPGMTLLDVGCGwGGALVRAVEKYDVNVIGLTLSRNHYERSKDRLAAIGtqRRAEARLQGWEE--FEEN-V 129
Cdd:COG2226   12 EALLAALGLRPGARVLDLGCG-TGRLALALAERGARVTGVDISPEMLELARERAAEAG--LNVEFVVGDAEDlpFPDGsF 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 614093331 130 DRIVSFEAFDAFkkERYLTFFERSYDILPDDGRMLLHSLFTYDRRWLHE 178
Cdd:COG2226   89 DLVISSFVLHHL--PDPERALAEIARVLKPGGRLVVVDFSPPDLAELEE 135
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 66-166 5.89e-08

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: 50.12  E-value: 5.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614093331  66 TLLDVGCGWGGALVRAVEKYDVNVIGLTLSRNHYERSKDRLAAIGTQrRAEARLQGWEEF----EENVDRIVSFEAFDAF 141
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLAD-NVEVLKGDAEELppeaDESFDVIISDPPLHHL 79

                         90       100
                 ....*....|....*....|....*
gi 614093331 142 kKERYLTFFERSYDILPDDGRMLLH 166
Cdd:cd02440   80 -VEDLARFLEEARRLLKPGGVLVLT 103
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 56-116 7.43e-08

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 53.22  E-value: 7.43e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 614093331  56 LDKLNLEPGMTLLDVGCGWGGALVRAVEKYDVNVIGLTLSRNHYERSKDRlaAIGTQRRAE 116
Cdd:PLN02336 259 VDKLDLKPGQKVLDVGCGIGGGDFYMAENFDVHVVGIDLSVNMISFALER--AIGRKCSVE 317
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 45-170 7.42e-06

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 45.68  E-value: 7.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614093331  45 EEAQLAKVDLALDKLNLEPGMTLLDVGCGWGGALVRAVEKYDVNVIGLTLSRNHYERSKDRLAAIGTQ--RRAEARLQGW 122
Cdd:COG0500    8 DELLPGLAALLALLERLPKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAGLGnvEFLVADLAEL 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 614093331 123 EEFEEN-VDRIVSFEAFDAFKKERYLTFFERSYDILPDDGRMLLHSLFT 170
Cdd:COG0500   88 DPLPAEsFDLVVAFGVLHHLPPEEREALLRELARALKPGGVLLLSASDA 136
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 61-165 1.72e-04

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: 40.39  E-value: 1.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614093331  61 LEPGMTLLDVGCGwGGALVRAVEKYDVNVIGLTLSRNHYERSKDRLAAIGTQRRAeARLQGWEEFEENVDRIVSFEAFDA 140
Cdd:COG2227   22 LPAGGRVLDVGCG-TGRLALALARRGADVTGVDISPEALEIARERAAELNVDFVQ-GDLEDLPLEDGSFDLVICSEVLEH 99

                         90       100
                 ....*....|....*....|....*
gi 614093331 141 FKKERylTFFERSYDILPDDGRMLL 165
Cdd:COG2227  100 LPDPA--ALLRELARLLKPGGLLLL 122
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
63-165 1.76e-04

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 39.81  E-value: 1.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614093331  63 PGMTLLDVGCGWGGALVRAVEKY-DVNVIGLTLSRNHYERSKDRLAAIgtqRRAEARLQGWeEFEENVDRIVSFEAFDAF 141
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALLAERFpGARVTGVDLSPEMLARARARLPNV---RFVVADLRDL-DPPEPFDLVVSNAALHWL 76

                         90       100
                 ....*....|....*....|....
gi 614093331 142 kkERYLTFFERSYDILPDDGRMLL 165
Cdd:COG4106   77 --PDHAALLARLAAALAPGGVLAV 98
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
 37-116 4.83e-04

cobalt-precorrin-6Y C(15)-methyltransferase; Provisional


Pssm-ID: 234740  Cd Length: 198  Bit Score: 40.17  E-value: 4.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614093331  37 FERDD---MTLEEAQLakvdLALDKLNLEPGMTLLDVGCGWGGALVRAV----EKYDVnvigltlsrnhYERSKDRLAAI 109
Cdd:PRK00377  15 FERDEeipMTKEEIRA----LALSKLRLRKGDMILDIGCGTGSVTVEASllvgETGKV-----------YAVDKDEKAIN 79


                 ....*..
gi 614093331 110 GTQRRAE 116
Cdd:PRK00377  80 LTRRNAE 86
PLN02244 PLN02244
tocopherol O-methyltransferase
 66-110 1.80e-03

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 39.34  E-value: 1.80e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 614093331  66 TLLDVGCGWGGALVRAVEKYDVNVIGLTLSRNHYERSKDRLAAIG 110
Cdd:PLN02244 121 RIVDVGCGIGGSSRYLARKYGANVKGITLSPVQAARANALAAAQG 165
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
 56-183 2.03e-03

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 38.80  E-value: 2.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614093331  56 LDKLNLEPGMTLLDVGCGWGGALVRAVEKYDVNVIGLTLSRNhyerskdrLAAIgtqrrAEARLQGWEEFEenvdrivsF 135
Cdd:PTZ00098  45 LSDIELNENSKVLDIGSGLGGGCKYINEKYGAHVHGVDICEK--------MVNI-----AKLRNSDKNKIE--------F 103

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 614093331 136 EAFDAFKKEryltFFERSYDILPDDGRMLLHS------LFTYDRRWLHEQGIAL 183
Cdd:PTZ00098 104 EANDILKKD----FPENTFDMIYSRDAILHLSyadkkkLFEKCYKWLKPNGILL 153
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
51-182 5.96e-03

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 36.90  E-value: 5.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614093331  51 KVDLALDKLNLEPGMTLLDVGCGwGGALVRAVEKYDVNVIGLTLSRNHYERSKDRlaaiGTQRR-AEARLQGWEEFEENV 129
Cdd:COG4976   34 LAEELLARLPPGPFGRVLDLGCG-TGLLGEALRPRGYRLTGVDLSEEMLAKAREK----GVYDRlLVADLADLAEPDGRF 108

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 614093331 130 DRIVSFEAFDAFkkERYLTFFERSYDILPDDGRMLL-------HSLFTYDRRWLHEQGIA 182
Cdd:COG4976  109 DLIVAADVLTYL--GDLAAVFAGVARALKPGGLFIFsvedadgSGRYAHSLDYVRDLLAA 166
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 59-223 6.44e-03

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 36.64  E-value: 6.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614093331   59 LNLEPGMTLLDVGCGwGGALVRAVEKYDVNVIGLTLSRNHYERskdrlaAIGTQRRAEARLQGWEEFEENVDRIVSFEAF 138
Cdd:pfam13489  18 PKLPSPGRVLDFGCG-TGIFLRLLRAQGFSVTGVDPSPIAIER------ALLNVRFDQFDEQEAAVPAGKFDVIVAREVL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614093331  139 DAFK-KERYLTFFersYDILPDDGRMLLHslfTYDRRWLHEQgialtmsDLRFLKFLREsIFPGGELPSEPDIVDNAQAA 217
Cdd:pfam13489  91 EHVPdPPALLRQI---AALLKPGGLLLLS---TPLASDEADR-------LLLEWPYLRP-RNGHISLFSARSLKRLLEEA 156


                  ....*.
gi 614093331  218 GFTIEH 223
Cdd:pfam13489 157 GFEVVS 162
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 68-162 8.27e-03

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 35.04  E-value: 8.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614093331   68 LDVGCGWGGALVRAVEKY-DVNVIGLTLSRNHYERSKDRLAAIGTQRRAEARLQGWEEFEEN---VDRIVSFEAFDAFKK 143
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALpGLEYTGLDISPAALEAARERLAALGLLNAVRVELFQLDLGELDpgsFDVVVASNVLHHLAD 80

                          90
                  ....*....|....*....
gi 614093331  144 ERylTFFERSYDILPDDGR 162
Cdd:pfam08242  81 PR--AVLRNIRRLLKPGGV 97
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 68-165 8.89e-03

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 34.95  E-value: 8.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614093331   68 LDVGCGwGGALVRAVEKYDVNVIGLTLSRNHYERSKDRLAAIG-TQRRAEARLQGWEefEENVDRIVSFEAFDAFkkERY 146
Cdd:pfam08241   1 LDVGCG-TGLLTELLARLGARVTGVDISPEMLELAREKAPREGlTFVVGDAEDLPFP--DNSFDLVLSSEVLHHV--EDP 75

                          90
                  ....*....|....*....
gi 614093331  147 LTFFERSYDILPDDGRMLL 165
Cdd:pfam08241  76 ERALREIARVLKPGGILII 94
 
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