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Conserved domains on  [gi|523436459|gb|AGQ34167|]
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SAM-dependent methyltransferase [Mycobacterium tuberculosis EAI5]

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

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List of domain hits

 Name Accession Description Interval E-value
CMAS super family cl47167
Mycolic acid cyclopropane synthetase; This family consist of ...
 11-293 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: 571.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523436459  11 SRSNVDDVQAHYDLSDAFFALFQDPTRTYSCAYFERDDMTLHEAQVAKLDLTLGKLGLEPGMTLLDVGCGWGSVMKRAVE 90
Cdd:NF040660   1 LRPHFEDVQAHYDLSDDFFALFLDPTQTYSCAYFERDDMTLEEAQIAKIDLALGKLNLEPGMTLLDIGCGWGATMRRAVE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523436459  91 RYDVNVVGLTLSKNQHAYCQQVLDKVDTNRSHRVLLSDWANFSEPVDRIVTIEAIEHFGFERYDDFFKFAYNAMPADGVM 170
Cdd:NF040660  81 KYDVNVVGLTLSKNQAAHVQQVLDEIDTPRSRRVLLQGWEEFDEPVDRIVSIGAFEHFGHERYDDFFKRAYNILPADGRM 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523436459 171 LLHSITGLHVKQVIERGIPLTMEMAKFIRFIVTDIFPGGRLPTIETIEEHVTKAGFTITDIQSLQPHFARTLDLWAEALQ 250
Cdd:NF040660 161 LLHTITGLHRKEMHERGLPLTMELARFIKFIVTEIFPGGRLPSIEMVVEHAEKAGFTVTRVQSLQPHYARTLDLWADALQ 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 523436459 251 AHKDEAIEIQSAEVYERYMKYLTGCAKAFRMGYIDCNQFTLAK 293
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 ...
 11-293 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: 571.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523436459  11 SRSNVDDVQAHYDLSDAFFALFQDPTRTYSCAYFERDDMTLHEAQVAKLDLTLGKLGLEPGMTLLDVGCGWGSVMKRAVE 90
Cdd:NF040660   1 LRPHFEDVQAHYDLSDDFFALFLDPTQTYSCAYFERDDMTLEEAQIAKIDLALGKLNLEPGMTLLDIGCGWGATMRRAVE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523436459  91 RYDVNVVGLTLSKNQHAYCQQVLDKVDTNRSHRVLLSDWANFSEPVDRIVTIEAIEHFGFERYDDFFKFAYNAMPADGVM 170
Cdd:NF040660  81 KYDVNVVGLTLSKNQAAHVQQVLDEIDTPRSRRVLLQGWEEFDEPVDRIVSIGAFEHFGHERYDDFFKRAYNILPADGRM 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523436459 171 LLHSITGLHVKQVIERGIPLTMEMAKFIRFIVTDIFPGGRLPTIETIEEHVTKAGFTITDIQSLQPHFARTLDLWAEALQ 250
Cdd:NF040660 161 LLHTITGLHRKEMHERGLPLTMELARFIKFIVTEIFPGGRLPSIEMVVEHAEKAGFTVTRVQSLQPHYARTLDLWADALQ 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 523436459 251 AHKDEAIEIQSAEVYERYMKYLTGCAKAFRMGYIDCNQFTLAK 293
Cdd:NF040660 241 AHKDEAIAIQSEEVYERYMKYLTGCAKLFRDGYIDVNQFTLAK 283
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 10-289 3.31e-175

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: 484.52  E-value: 3.31e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523436459   10 KSRSNVDDVQAHYDLSDAFFALFQDPTRTYSCAYFERDDMTLHEAQVAKLDLTLGKLGLEPGMTLLDVGCGWGSVMKRAV 89
Cdd:pfam02353   1 SKTRDAENIQAHYDLSNDFFALFLDPTMTYSCAYFERPDMTLEEAQQAKLDLILDKLGLKPGMTLLDIGCGWGGLMRRAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523436459   90 ERYDVNVVGLTLSKNQHAYCQQVLDKVDTNRSHRVLLSDWANFSEPVDRIVTIEAIEHFGFERYDDFFKFAYNAMPADGV 169
Cdd:pfam02353  81 ERYDVNVVGLTLSKNQYKLARKRVAAEGLARKVEVLLQDYRDFDEPFDRIVSVGMFEHVGHENYDTFFKKLYNLLPPGGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523436459  170 MLLHSITGLHVKQVIERGIPLtmemakfiRFIVTDIFPGGRLPTIETIEEHVTKAGFTITDIQSLQPHFARTLDLWAEAL 249
Cdd:pfam02353 161 MLLHTITGLHPDETSERGLPL--------KFIDKYIFPGGELPSISMIVESSSEAGFTVEDVESLRPHYAKTLDLWAENL 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 523436459  250 QAHKDEAIEIQSAEVYERYMKYLTGCAKAFRMGYIDCNQF 289
Cdd:pfam02353 233 QANKDEAIALQSEEFYRMWMLYLTGCAVAFRIGYIDVHQF 272
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 20-174 5.76e-63

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 195.53  E-value: 5.76e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523436459  20 AHYDLSDAFFALFQDPTRTYSCAYFERDDMTLHEAQVAKLDLTLGKLGLEPGMTLLDVGCGWGSVMKRAVERYDVNVVGL 99
Cdd:COG2230    1 HHYDLGNDFYRLFLDPTMTYSCAYFEDPDDTLEEAQEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGV 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 523436459 100 TLSKNQHAYCQQVLDKVDTNRSHRVLLSDWANF--SEPVDRIVTIEAIEHFGFERYDDFFKFAYNAMPADGVMLLHS 174
Cdd:COG2230   81 TLSPEQLEYARERAAEAGLADRVEVRLADYRDLpaDGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLLHT 157
cyclopro_CfaB NF040703
C17 cyclopropane fatty acid synthase CfaB;
16-288 2.91e-61

C17 cyclopropane fatty acid synthase CfaB;


Pssm-ID: 468667 [Multi-domain]  Cd Length: 393  Bit Score: 199.07  E-value: 2.91e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523436459  16 DDVQAHYDLSDAFFALFQDPTRTYSCAYFERDDMTLHEAQVAKLDLTLGKLGLEPGMTLLDVGCGWGSVMKRAVERYDVN 95
Cdd:NF040703 105 AAISYHYDLSNDFYALWLDPDMVYSCAYFETGTEDLAQAQQAKLRHLCRKLRLQPGERLLDVGCGWGGLARFAAREFGVE 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523436459  96 VVGLTLSKNQHAYCQQ------VLDKVDTN-RSHRVLLSDwANFsepvDRIVTIEAIEHFGFERYDDFFKFAYNAMPADG 168
Cdd:NF040703 185 VFGITLSKEQLKLARErvaaegLQDRVQLElLDYRDLPQD-GRF----DKVVSVGMFEHVGHANLPLYCQRLFGAVRPGG 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523436459 169 VMLLHSITGLHVKqvierGIPLTMEMAKFI-RFivtdIFPGGRLPTIETIEEHVTKAGFTITDIQSLQPHFARTLDLWAE 247
Cdd:NF040703 260 LVMNHGITARHTD-----GRPVGRGAGEFIgRY----VFPHGELPHLATITASISEAGLEVVDVESLRLHYARTLEHWSA 330

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 523436459 248 ALQAHKDEAieiqSAEVYERYMK----YLTGCAKAFRMGYIDCNQ 288
Cdd:NF040703 331 RLEARLDEA----ARLVPERALRiwrlYLAGCAYGFARGWINLHQ 371
PRK11705 PRK11705
cyclopropane fatty acyl phospholipid synthase;
19-280 3.78e-57

cyclopropane fatty acyl phospholipid synthase;


Pssm-ID: 183282  Cd Length: 383  Bit Score: 188.13  E-value: 3.78e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523436459  19 QAHYDLSDAFFALFQDPTRTYSCAYFERDDmTLHEAQVAKLDLTLGKLGLEPGMTLLDVGCGWGSVMKRAVERYDVNVVG 98
Cdd:PRK11705 117 KEHYDLGNDLFEAMLDPRMQYSCGYWKDAD-TLEEAQEAKLDLICRKLQLKPGMRVLDIGCGWGGLARYAAEHYGVSVVG 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523436459  99 LTLSKNQHAYCQQVLDKVDTNrshrVLLSDWANFSEPVDRIVTIEAIEHFGFERYDDFFKFAYNAMPADGVMLLHSI--- 175
Cdd:PRK11705 196 VTISAEQQKLAQERCAGLPVE----IRLQDYRDLNGQFDRIVSVGMFEHVGPKNYRTYFEVVRRCLKPDGLFLLHTIgsn 271

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523436459 176 -TGLHVKQVIERGipltmemakfirfivtdIFPGGRLPTIetieEHVTKAG---FTITDIQSLQPHFARTLDLWAEALQA 251
Cdd:PRK11705 272 kTDTNVDPWINKY-----------------IFPNGCLPSV----RQIAQASeglFVMEDWHNFGADYDRTLMAWHENFEA 330

                        250       260       270
                 ....*....|....*....|....*....|
gi 523436459 252 HKDEaIEIQSAEVYERYMK-YLTGCAKAFR 280
Cdd:PRK11705 331 AWPE-LADNYSERFYRMWRyYLLSCAGAFR 359
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 73-173 2.10e-06

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: 45.50  E-value: 2.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523436459  73 TLLDVGCGWGSVMKRAVERYDVNVVGLTLSKNQHAYCQQVLDKVDTNRShRVLLSDWANFS----EPVDRIVTIEAIEHF 148
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNV-EVLKGDAEELPpeadESFDVIISDPPLHHL 79

                         90       100
                 ....*....|....*....|....*
gi 523436459 149 gFERYDDFFKFAYNAMPADGVMLLH 173
Cdd:cd02440   80 -VEDLARFLEEARRLLKPGGVLVLT 103
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
 49-84 2.97e-04

precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes the CbiT methylase which is responsible, in part (along with CbiE), for methylating precorrin-6y (or cobalt-precorrin-6y) at both the 5 and 15 positions as well as the concomitant decarbozylation at C-12. In many organisms, this protein is fused to the CbiE subunit. The fused protein, when found in organisms catalyzing the oxidative version of the cobalamin biosynthesis pathway, is called CobL. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 274148 [Multi-domain]  Cd Length: 124  Bit Score: 40.01  E-value: 2.97e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 523436459   49 MTLHEAQVakldLTLGKLGLEPGMTLLDVGCGWGSV 84
Cdd:TIGR02469   2 MTKREVRA----LTLAKLRLRPGDVLWDIGAGTGSV 33
 
Name Accession Description Interval E-value
mycolic_MTase NF040660
cyclopropane mycolic acid synthase family methyltransferase; Members of this family include ...
 11-293 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: 571.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523436459  11 SRSNVDDVQAHYDLSDAFFALFQDPTRTYSCAYFERDDMTLHEAQVAKLDLTLGKLGLEPGMTLLDVGCGWGSVMKRAVE 90
Cdd:NF040660   1 LRPHFEDVQAHYDLSDDFFALFLDPTQTYSCAYFERDDMTLEEAQIAKIDLALGKLNLEPGMTLLDIGCGWGATMRRAVE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523436459  91 RYDVNVVGLTLSKNQHAYCQQVLDKVDTNRSHRVLLSDWANFSEPVDRIVTIEAIEHFGFERYDDFFKFAYNAMPADGVM 170
Cdd:NF040660  81 KYDVNVVGLTLSKNQAAHVQQVLDEIDTPRSRRVLLQGWEEFDEPVDRIVSIGAFEHFGHERYDDFFKRAYNILPADGRM 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523436459 171 LLHSITGLHVKQVIERGIPLTMEMAKFIRFIVTDIFPGGRLPTIETIEEHVTKAGFTITDIQSLQPHFARTLDLWAEALQ 250
Cdd:NF040660 161 LLHTITGLHRKEMHERGLPLTMELARFIKFIVTEIFPGGRLPSIEMVVEHAEKAGFTVTRVQSLQPHYARTLDLWADALQ 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 523436459 251 AHKDEAIEIQSAEVYERYMKYLTGCAKAFRMGYIDCNQFTLAK 293
Cdd:NF040660 241 AHKDEAIAIQSEEVYERYMKYLTGCAKLFRDGYIDVNQFTLAK 283
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 10-289 3.31e-175

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: 484.52  E-value: 3.31e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523436459   10 KSRSNVDDVQAHYDLSDAFFALFQDPTRTYSCAYFERDDMTLHEAQVAKLDLTLGKLGLEPGMTLLDVGCGWGSVMKRAV 89
Cdd:pfam02353   1 SKTRDAENIQAHYDLSNDFFALFLDPTMTYSCAYFERPDMTLEEAQQAKLDLILDKLGLKPGMTLLDIGCGWGGLMRRAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523436459   90 ERYDVNVVGLTLSKNQHAYCQQVLDKVDTNRSHRVLLSDWANFSEPVDRIVTIEAIEHFGFERYDDFFKFAYNAMPADGV 169
Cdd:pfam02353  81 ERYDVNVVGLTLSKNQYKLARKRVAAEGLARKVEVLLQDYRDFDEPFDRIVSVGMFEHVGHENYDTFFKKLYNLLPPGGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523436459  170 MLLHSITGLHVKQVIERGIPLtmemakfiRFIVTDIFPGGRLPTIETIEEHVTKAGFTITDIQSLQPHFARTLDLWAEAL 249
Cdd:pfam02353 161 MLLHTITGLHPDETSERGLPL--------KFIDKYIFPGGELPSISMIVESSSEAGFTVEDVESLRPHYAKTLDLWAENL 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 523436459  250 QAHKDEAIEIQSAEVYERYMKYLTGCAKAFRMGYIDCNQF 289
Cdd:pfam02353 233 QANKDEAIALQSEEFYRMWMLYLTGCAVAFRIGYIDVHQF 272
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 20-174 5.76e-63

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 195.53  E-value: 5.76e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523436459  20 AHYDLSDAFFALFQDPTRTYSCAYFERDDMTLHEAQVAKLDLTLGKLGLEPGMTLLDVGCGWGSVMKRAVERYDVNVVGL 99
Cdd:COG2230    1 HHYDLGNDFYRLFLDPTMTYSCAYFEDPDDTLEEAQEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGV 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 523436459 100 TLSKNQHAYCQQVLDKVDTNRSHRVLLSDWANF--SEPVDRIVTIEAIEHFGFERYDDFFKFAYNAMPADGVMLLHS 174
Cdd:COG2230   81 TLSPEQLEYARERAAEAGLADRVEVRLADYRDLpaDGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLLHT 157
cyclopro_CfaB NF040703
C17 cyclopropane fatty acid synthase CfaB;
16-288 2.91e-61

C17 cyclopropane fatty acid synthase CfaB;


Pssm-ID: 468667 [Multi-domain]  Cd Length: 393  Bit Score: 199.07  E-value: 2.91e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523436459  16 DDVQAHYDLSDAFFALFQDPTRTYSCAYFERDDMTLHEAQVAKLDLTLGKLGLEPGMTLLDVGCGWGSVMKRAVERYDVN 95
Cdd:NF040703 105 AAISYHYDLSNDFYALWLDPDMVYSCAYFETGTEDLAQAQQAKLRHLCRKLRLQPGERLLDVGCGWGGLARFAAREFGVE 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523436459  96 VVGLTLSKNQHAYCQQ------VLDKVDTN-RSHRVLLSDwANFsepvDRIVTIEAIEHFGFERYDDFFKFAYNAMPADG 168
Cdd:NF040703 185 VFGITLSKEQLKLARErvaaegLQDRVQLElLDYRDLPQD-GRF----DKVVSVGMFEHVGHANLPLYCQRLFGAVRPGG 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523436459 169 VMLLHSITGLHVKqvierGIPLTMEMAKFI-RFivtdIFPGGRLPTIETIEEHVTKAGFTITDIQSLQPHFARTLDLWAE 247
Cdd:NF040703 260 LVMNHGITARHTD-----GRPVGRGAGEFIgRY----VFPHGELPHLATITASISEAGLEVVDVESLRLHYARTLEHWSA 330

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 523436459 248 ALQAHKDEAieiqSAEVYERYMK----YLTGCAKAFRMGYIDCNQ 288
Cdd:NF040703 331 RLEARLDEA----ARLVPERALRiwrlYLAGCAYGFARGWINLHQ 371
PRK11705 PRK11705
cyclopropane fatty acyl phospholipid synthase;
19-280 3.78e-57

cyclopropane fatty acyl phospholipid synthase;


Pssm-ID: 183282  Cd Length: 383  Bit Score: 188.13  E-value: 3.78e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523436459  19 QAHYDLSDAFFALFQDPTRTYSCAYFERDDmTLHEAQVAKLDLTLGKLGLEPGMTLLDVGCGWGSVMKRAVERYDVNVVG 98
Cdd:PRK11705 117 KEHYDLGNDLFEAMLDPRMQYSCGYWKDAD-TLEEAQEAKLDLICRKLQLKPGMRVLDIGCGWGGLARYAAEHYGVSVVG 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523436459  99 LTLSKNQHAYCQQVLDKVDTNrshrVLLSDWANFSEPVDRIVTIEAIEHFGFERYDDFFKFAYNAMPADGVMLLHSI--- 175
Cdd:PRK11705 196 VTISAEQQKLAQERCAGLPVE----IRLQDYRDLNGQFDRIVSVGMFEHVGPKNYRTYFEVVRRCLKPDGLFLLHTIgsn 271

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523436459 176 -TGLHVKQVIERGipltmemakfirfivtdIFPGGRLPTIetieEHVTKAG---FTITDIQSLQPHFARTLDLWAEALQA 251
Cdd:PRK11705 272 kTDTNVDPWINKY-----------------IFPNGCLPSV----RQIAQASeglFVMEDWHNFGADYDRTLMAWHENFEA 330

                        250       260       270
                 ....*....|....*....|....*....|
gi 523436459 252 HKDEaIEIQSAEVYERYMK-YLTGCAKAFR 280
Cdd:PRK11705 331 AWPE-LADNYSERFYRMWRyYLLSCAGAFR 359
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 75-158 1.45e-09

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 54.11  E-value: 1.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523436459   75 LDVGCGWGSVMKRAVERYDVNVVGLTLSKNQHAYCQQVLDKVDTNrsHRVLLSDWANFSEP---VDRIVTIEAIEHFGFE 151
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLN--VEFVQGDAEDLPFPdgsFDLVVSSGVLHHLPDP 79


                  ....*..
gi 523436459  152 RYDDFFK 158
Cdd:pfam13649  80 DLEAALR 86
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 63-227 2.62e-07

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: 48.84  E-value: 2.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523436459  63 LGKLGLEPGMTLLDVGCGWGSVMKRAVERyDVNVVGLTLSKNQHAYCQQVLDKVDTNRshRVLLSDWANF---SEPVDRI 139
Cdd:COG2226   15 LAALGLRPGARVLDLGCGTGRLALALAER-GARVTGVDISPEMLELARERAAEAGLNV--EFVVGDAEDLpfpDGSFDLV 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523436459 140 VTIEAIEHfgFERYDDFFKFAYNAMPADGvmllhsitglhvkqviergipltmemakfiRFIVTDIFPggrlPTIETIEE 219
Cdd:COG2226   92 ISSFVLHH--LPDPERALAEIARVLKPGG------------------------------RLVVVDFSP----PDLAELEE 135


                 ....*...
gi 523436459 220 HVTKAGFT 227
Cdd:COG2226  136 LLAEAGFE 143
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 68-172 7.04e-07

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: 47.32  E-value: 7.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523436459  68 LEPGMTLLDVGCGWGSVMKRAVERyDVNVVGLTLSKNQHAYCQQVLDKVDTnrshRVLLSDWANFS---EPVDRIVTIEA 144
Cdd:COG2227   22 LPAGGRVLDVGCGTGRLALALARR-GADVTGVDISPEALEIARERAAELNV----DFVQGDLEDLPledGSFDLVICSEV 96

                         90       100
                 ....*....|....*....|....*...
gi 523436459 145 IEHfgFERYDDFFKFAYNAMPADGVMLL 172
Cdd:COG2227   97 LEH--LPDPAALLRELARLLKPGGLLLL 122
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 73-173 2.10e-06

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: 45.50  E-value: 2.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523436459  73 TLLDVGCGWGSVMKRAVERYDVNVVGLTLSKNQHAYCQQVLDKVDTNRShRVLLSDWANFS----EPVDRIVTIEAIEHF 148
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNV-EVLKGDAEELPpeadESFDVIISDPPLHHL 79

                         90       100
                 ....*....|....*....|....*
gi 523436459 149 gFERYDDFFKFAYNAMPADGVMLLH 173
Cdd:cd02440   80 -VEDLARFLEEARRLLKPGGVLVLT 103
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
70-172 1.35e-05

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 42.89  E-value: 1.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523436459  70 PGMTLLDVGCGWGSVMKRAVERY-DVNVVGLTLSKNQHAYCQQVLDKVdtnrshRVLLSDWANFS--EPVDRIVTIEAIE 146
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALLAERFpGARVTGVDLSPEMLARARARLPNV------RFVVADLRDLDppEPFDLVVSNAALH 74

                         90       100
                 ....*....|....*....|....*.
gi 523436459 147 HfgFERYDDFFKFAYNAMPADGVMLL 172
Cdd:COG4106   75 W--LPDHAALLARLAAALAPGGVLAV 98
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 44-90 1.68e-05

Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441843 [Multi-domain]  Cd Length: 403  Bit Score: 45.93  E-value: 1.68e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 523436459  44 FERDD--MTLHEAQVakldLTLGKLGLEPGMTLLDVGCGWGSVmkrAVE 90
Cdd:COG2242  223 FERDKgpITKREVRA----LTLAKLALRPGDVLWDIGAGSGSV---SIE 264
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 63-104 2.63e-05

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 45.13  E-value: 2.63e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 523436459  63 LGKLGLEPGMTLLDVGCGWGSVMKRAVERYDVNVVGLTLSKN 104
Cdd:PLN02336 259 VDKLDLKPGQKVLDVGCGIGGGDFYMAENFDVHVVGIDLSVN 300
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
 49-84 2.97e-04

precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes the CbiT methylase which is responsible, in part (along with CbiE), for methylating precorrin-6y (or cobalt-precorrin-6y) at both the 5 and 15 positions as well as the concomitant decarbozylation at C-12. In many organisms, this protein is fused to the CbiE subunit. The fused protein, when found in organisms catalyzing the oxidative version of the cobalamin biosynthesis pathway, is called CobL. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 274148 [Multi-domain]  Cd Length: 124  Bit Score: 40.01  E-value: 2.97e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 523436459   49 MTLHEAQVakldLTLGKLGLEPGMTLLDVGCGWGSV 84
Cdd:TIGR02469   2 MTKREVRA----LTLAKLRLRPGDVLWDIGAGTGSV 33
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 53-172 3.53e-04

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 40.67  E-value: 3.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523436459  53 EAQVAKLDLTLGKLGLEPGMTLLDVGCGWGSVMKRAVERYDVNVVGLTLSKNQHAYCQQVLDKVDTNRSHrVLLSDWANF 132
Cdd:COG0500    9 ELLPGLAALLALLERLPKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAGLGNVE-FLVADLAEL 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 523436459 133 ----SEPVDRIVTIEAIEHFGFERYDDFFKFAYNAMPADGVMLL 172
Cdd:COG0500   88 dplpAESFDLVVAFGVLHHLPPEEREALLRELARALKPGGVLLL 131
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 66-229 1.72e-03

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 38.18  E-value: 1.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523436459   66 LGLEPGMTLLDVGCGWGSVMkRAVERYDVNVVGLTLSknqhayCQQVLDKVDTNRSHRVLLSDWANFSEPVDRIVTIEAI 145
Cdd:pfam13489  18 PKLPSPGRVLDFGCGTGIFL-RLLRAQGFSVTGVDPS------PIAIERALLNVRFDQFDEQEAAVPAGKFDVIVAREVL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523436459  146 EHFGFerYDDFFKFAYNAMPADGVMLLHSITGLHVKQVIERGIPLTMEMAKFIRFIvtdifpggrlpTIETIEEHVTKAG 225
Cdd:pfam13489  91 EHVPD--PPALLRQIAALLKPGGLLLLSTPLASDEADRLLLEWPYLRPRNGHISLF-----------SARSLKRLLEEAG 157


                  ....
gi 523436459  226 FTIT 229
Cdd:pfam13489 158 FEVV 161
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
 44-84 3.36e-03

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


Pssm-ID: 234740  Cd Length: 198  Bit Score: 37.85  E-value: 3.36e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 523436459  44 FERDD---MTLHEAQVakldLTLGKLGLEPGMTLLDVGCGWGSV 84
Cdd:PRK00377  15 FERDEeipMTKEEIRA----LALSKLRLRKGDMILDIGCGTGSV 54
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 75-148 6.69e-03

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 35.33  E-value: 6.69e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 523436459   75 LDVGCGWGSVMkRAVERYDVNVVGLTLSKNQHAYCQQVLdkvdTNRSHRVLLSDWANF---SEPVDRIVTIEAIEHF 148
Cdd:pfam08241   1 LDVGCGTGLLT-ELLARLGARVTGVDISPEMLELAREKA----PREGLTFVVGDAEDLpfpDNSFDLVLSSEVLHHV 72
 
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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