NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|18655943|pdb|1KPH|B]
View 

Chain B, CYCLOPROPANE-FATTY-ACYL-PHOSPHOLIPID SYNTHASE 1

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
mycolic_MTase NF040660
cyclopropane mycolic acid synthase family methyltransferase; Members of this family include ...
5-287 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: 587.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KPH_B         5 LKPHFANVQAHYDLSDDFFRLFLDPTQTYSCAYFERDDMTLQEAQIAKIDLALGKLGLQPGMTLLDVGCGWGATMMRAVE 84
Cdd:NF040660   1 LRPHFEDVQAHYDLSDDFFALFLDPTQTYSCAYFERDDMTLEEAQIAKIDLALGKLNLEPGMTLLDIGCGWGATMRRAVE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KPH_B        85 KYDVNVVGLTLSKNQANHVQQLVANSENLRSKRVLLAGWEQFDEPVDRIVSIGAFEHFGHERYDAFFSLAHRLLPADGVM 164
Cdd:NF040660  81 KYDVNVVGLTLSKNQAAHVQQVLDEIDTPRSRRVLLQGWEEFDEPVDRIVSIGAFEHFGHERYDDFFKRAYNILPADGRM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KPH_B       165 LLHTITGLHPKEIHERGLPMSFTFARFLKFIVTEIFPGGRLPSIPMVQECASANGFTVTRVQSLQPHYAKTLDLWSAALQ 244
Cdd:NF040660 161 LLHTITGLHRKEMHERGLPLTMELARFIKFIVTEIFPGGRLPSIEMVVEHAEKAGFTVTRVQSLQPHYARTLDLWADALQ 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
1KPH_B       245 ANKGQAIALQSEEVYERYMKYLTGCAEMFRIGYIDVNQFTCQK 287
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 ...
5-287 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: 587.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KPH_B         5 LKPHFANVQAHYDLSDDFFRLFLDPTQTYSCAYFERDDMTLQEAQIAKIDLALGKLGLQPGMTLLDVGCGWGATMMRAVE 84
Cdd:NF040660   1 LRPHFEDVQAHYDLSDDFFALFLDPTQTYSCAYFERDDMTLEEAQIAKIDLALGKLNLEPGMTLLDIGCGWGATMRRAVE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KPH_B        85 KYDVNVVGLTLSKNQANHVQQLVANSENLRSKRVLLAGWEQFDEPVDRIVSIGAFEHFGHERYDAFFSLAHRLLPADGVM 164
Cdd:NF040660  81 KYDVNVVGLTLSKNQAAHVQQVLDEIDTPRSRRVLLQGWEEFDEPVDRIVSIGAFEHFGHERYDDFFKRAYNILPADGRM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KPH_B       165 LLHTITGLHPKEIHERGLPMSFTFARFLKFIVTEIFPGGRLPSIPMVQECASANGFTVTRVQSLQPHYAKTLDLWSAALQ 244
Cdd:NF040660 161 LLHTITGLHRKEMHERGLPLTMELARFIKFIVTEIFPGGRLPSIEMVVEHAEKAGFTVTRVQSLQPHYARTLDLWADALQ 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
1KPH_B       245 ANKGQAIALQSEEVYERYMKYLTGCAEMFRIGYIDVNQFTCQK 287
Cdd:NF040660 241 AHKDEAIAIQSEEVYERYMKYLTGCAKLFRDGYIDVNQFTLAK 283
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
5-283 5.55e-179

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: 493.77  E-value: 5.55e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KPH_B          5 LKPHFANVQAHYDLSDDFFRLFLDPTQTYSCAYFERDDMTLQEAQIAKIDLALGKLGLQPGMTLLDVGCGWGATMMRAVE 84
Cdd:pfam02353   2 KTRDAENIQAHYDLSNDFFALFLDPTMTYSCAYFERPDMTLEEAQQAKLDLILDKLGLKPGMTLLDIGCGWGGLMRRAAE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KPH_B         85 KYDVNVVGLTLSKNQANHVQQLVANSENLRSKRVLLAGWEQFDEPVDRIVSIGAFEHFGHERYDAFFSLAHRLLPADGVM 164
Cdd:pfam02353  82 RYDVNVVGLTLSKNQYKLARKRVAAEGLARKVEVLLQDYRDFDEPFDRIVSVGMFEHVGHENYDTFFKKLYNLLPPGGLM 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KPH_B        165 LLHTITGLHPKEIHERGLPmsftfarfLKFIVTEIFPGGRLPSIPMVQECASANGFTVTRVQSLQPHYAKTLDLWSAALQ 244
Cdd:pfam02353 162 LLHTITGLHPDETSERGLP--------LKFIDKYIFPGGELPSISMIVESSSEAGFTVEDVESLRPHYAKTLDLWAENLQ 233
                         250       260       270
                  ....*....|....*....|....*....|....*....
1KPH_B        245 ANKGQAIALQSEEVYERYMKYLTGCAEMFRIGYIDVNQF 283
Cdd:pfam02353 234 ANKDEAIALQSEEFYRMWMLYLTGCAVAFRIGYIDVHQF 272
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
14-168 2.73e-69

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 211.71  E-value: 2.73e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KPH_B       14 AHYDLSDDFFRLFLDPTQTYSCAYFERDDMTLQEAQIAKIDLALGKLGLQPGMTLLDVGCGWGATMMRAVEKYDVNVVGL 93
Cdd:COG2230   1 HHYDLGNDFYRLFLDPTMTYSCAYFEDPDDTLEEAQEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGV 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1KPH_B       94 TLSKNQANHVQQLVANsENLRSK-RVLLAGWEQF--DEPVDRIVSIGAFEHFGHERYDAFFSLAHRLLPADGVMLLHT 168
Cdd:COG2230  81 TLSPEQLEYARERAAE-AGLADRvEVRLADYRDLpaDGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLLHT 157
cyclopro_CfaB NF040703
C17 cyclopropane fatty acid synthase CfaB;
15-282 1.24e-64

C17 cyclopropane fatty acid synthase CfaB;


Pssm-ID: 468667 [Multi-domain]  Cd Length: 393  Bit Score: 207.54  E-value: 1.24e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KPH_B        15 HYDLSDDFFRLFLDPTQTYSCAYFERDDMTLQEAQIAKIDLALGKLGLQPGMTLLDVGCGWGATMMRAVEKYDVNVVGLT 94
Cdd:NF040703 110 HYDLSNDFYALWLDPDMVYSCAYFETGTEDLAQAQQAKLRHLCRKLRLQPGERLLDVGCGWGGLARFAAREFGVEVFGIT 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KPH_B        95 LSKNQANHVQQLVAnSENLrSKRVLLAGWEQFDEP----VDRIVSIGAFEHFGHERYDAFFSLAHRLLPADGVMLLHTIT 170
Cdd:NF040703 190 LSKEQLKLARERVA-AEGL-QDRVQLELLDYRDLPqdgrFDKVVSVGMFEHVGHANLPLYCQRLFGAVRPGGLVMNHGIT 267
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KPH_B       171 GLHPKeiherGLPMSFTFArflKFIVTEIFPGGRLPSIPMVQECASANGFTVTRVQSLQPHYAKTLDLWSAALQANKGQA 250
Cdd:NF040703 268 ARHTD-----GRPVGRGAG---EFIGRYVFPHGELPHLATITASISEAGLEVVDVESLRLHYARTLEHWSARLEARLDEA 339
                        250       260       270
                 ....*....|....*....|....*....|..
1KPH_B       251 IALQSEEVYERYMKYLTGCAEMFRIGYIDVNQ 282
Cdd:NF040703 340 ARLVPERALRIWRLYLAGCAYGFARGWINLHQ 371
PRK11705 PRK11705
cyclopropane fatty acyl phospholipid synthase;
13-274 2.35e-64

cyclopropane fatty acyl phospholipid synthase;


Pssm-ID: 183282  Cd Length: 383  Bit Score: 206.62  E-value: 2.35e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KPH_B        13 QAHYDLSDDFFRLFLDPTQTYSCAYFERDDmTLQEAQIAKIDLALGKLGLQPGMTLLDVGCGWGATMMRAVEKYDVNVVG 92
Cdd:PRK11705 117 KEHYDLGNDLFEAMLDPRMQYSCGYWKDAD-TLEEAQEAKLDLICRKLQLKPGMRVLDIGCGWGGLARYAAEHYGVSVVG 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KPH_B        93 LTLSKNQANHVQQLVANSenlrSKRVLLAGWEQFDEPVDRIVSIGAFEHFGHERYDAFFSLAHRLLPADGVMLLHTI--- 169
Cdd:PRK11705 196 VTISAEQQKLAQERCAGL----PVEIRLQDYRDLNGQFDRIVSVGMFEHVGPKNYRTYFEVVRRCLKPDGLFLLHTIgsn 271
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KPH_B       170 -TGLHPKeiherglpmsftfarflKFIVTEIFPGGRLPSIPMVQEcASANGFTVTRVQSLQPHYAKTLDLWSAALQANKG 248
Cdd:PRK11705 272 kTDTNVD-----------------PWINKYIFPNGCLPSVRQIAQ-ASEGLFVMEDWHNFGADYDRTLMAWHENFEAAWP 333
                        250       260
                 ....*....|....*....|....*...
1KPH_B       249 QAIALQSEEVYE--RYmkYLTGCAEMFR 274
Cdd:PRK11705 334 ELADNYSERFYRmwRY--YLLSCAGAFR 359
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
67-171 1.27e-13

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: 65.53  E-value: 1.27e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KPH_B       67 TLLDVGCGWGATMMRAVEKYDVNVVGLTLSKNQANHVQQLVANSENLRsKRVLLAGWEQF----DEPVDRIVSIGAFEHF 142
Cdd:cd02440   1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADN-VEVLKGDAEELppeaDESFDVIISDPPLHHL 79
                        90       100
                ....*....|....*....|....*....
1KPH_B      143 gHERYDAFFSLAHRLLPADGVMLLHTITG 171
Cdd:cd02440  80 -VEDLARFLEEARRLLKPGGVLVLTLVLA 107
 
Name Accession Description Interval E-value
mycolic_MTase NF040660
cyclopropane mycolic acid synthase family methyltransferase; Members of this family include ...
5-287 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: 587.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KPH_B         5 LKPHFANVQAHYDLSDDFFRLFLDPTQTYSCAYFERDDMTLQEAQIAKIDLALGKLGLQPGMTLLDVGCGWGATMMRAVE 84
Cdd:NF040660   1 LRPHFEDVQAHYDLSDDFFALFLDPTQTYSCAYFERDDMTLEEAQIAKIDLALGKLNLEPGMTLLDIGCGWGATMRRAVE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KPH_B        85 KYDVNVVGLTLSKNQANHVQQLVANSENLRSKRVLLAGWEQFDEPVDRIVSIGAFEHFGHERYDAFFSLAHRLLPADGVM 164
Cdd:NF040660  81 KYDVNVVGLTLSKNQAAHVQQVLDEIDTPRSRRVLLQGWEEFDEPVDRIVSIGAFEHFGHERYDDFFKRAYNILPADGRM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KPH_B       165 LLHTITGLHPKEIHERGLPMSFTFARFLKFIVTEIFPGGRLPSIPMVQECASANGFTVTRVQSLQPHYAKTLDLWSAALQ 244
Cdd:NF040660 161 LLHTITGLHRKEMHERGLPLTMELARFIKFIVTEIFPGGRLPSIEMVVEHAEKAGFTVTRVQSLQPHYARTLDLWADALQ 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
1KPH_B       245 ANKGQAIALQSEEVYERYMKYLTGCAEMFRIGYIDVNQFTCQK 287
Cdd:NF040660 241 AHKDEAIAIQSEEVYERYMKYLTGCAKLFRDGYIDVNQFTLAK 283
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
5-283 5.55e-179

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: 493.77  E-value: 5.55e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KPH_B          5 LKPHFANVQAHYDLSDDFFRLFLDPTQTYSCAYFERDDMTLQEAQIAKIDLALGKLGLQPGMTLLDVGCGWGATMMRAVE 84
Cdd:pfam02353   2 KTRDAENIQAHYDLSNDFFALFLDPTMTYSCAYFERPDMTLEEAQQAKLDLILDKLGLKPGMTLLDIGCGWGGLMRRAAE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KPH_B         85 KYDVNVVGLTLSKNQANHVQQLVANSENLRSKRVLLAGWEQFDEPVDRIVSIGAFEHFGHERYDAFFSLAHRLLPADGVM 164
Cdd:pfam02353  82 RYDVNVVGLTLSKNQYKLARKRVAAEGLARKVEVLLQDYRDFDEPFDRIVSVGMFEHVGHENYDTFFKKLYNLLPPGGLM 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KPH_B        165 LLHTITGLHPKEIHERGLPmsftfarfLKFIVTEIFPGGRLPSIPMVQECASANGFTVTRVQSLQPHYAKTLDLWSAALQ 244
Cdd:pfam02353 162 LLHTITGLHPDETSERGLP--------LKFIDKYIFPGGELPSISMIVESSSEAGFTVEDVESLRPHYAKTLDLWAENLQ 233
                         250       260       270
                  ....*....|....*....|....*....|....*....
1KPH_B        245 ANKGQAIALQSEEVYERYMKYLTGCAEMFRIGYIDVNQF 283
Cdd:pfam02353 234 ANKDEAIALQSEEFYRMWMLYLTGCAVAFRIGYIDVHQF 272
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
14-168 2.73e-69

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 211.71  E-value: 2.73e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KPH_B       14 AHYDLSDDFFRLFLDPTQTYSCAYFERDDMTLQEAQIAKIDLALGKLGLQPGMTLLDVGCGWGATMMRAVEKYDVNVVGL 93
Cdd:COG2230   1 HHYDLGNDFYRLFLDPTMTYSCAYFEDPDDTLEEAQEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGV 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1KPH_B       94 TLSKNQANHVQQLVANsENLRSK-RVLLAGWEQF--DEPVDRIVSIGAFEHFGHERYDAFFSLAHRLLPADGVMLLHT 168
Cdd:COG2230  81 TLSPEQLEYARERAAE-AGLADRvEVRLADYRDLpaDGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLLHT 157
cyclopro_CfaB NF040703
C17 cyclopropane fatty acid synthase CfaB;
15-282 1.24e-64

C17 cyclopropane fatty acid synthase CfaB;


Pssm-ID: 468667 [Multi-domain]  Cd Length: 393  Bit Score: 207.54  E-value: 1.24e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KPH_B        15 HYDLSDDFFRLFLDPTQTYSCAYFERDDMTLQEAQIAKIDLALGKLGLQPGMTLLDVGCGWGATMMRAVEKYDVNVVGLT 94
Cdd:NF040703 110 HYDLSNDFYALWLDPDMVYSCAYFETGTEDLAQAQQAKLRHLCRKLRLQPGERLLDVGCGWGGLARFAAREFGVEVFGIT 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KPH_B        95 LSKNQANHVQQLVAnSENLrSKRVLLAGWEQFDEP----VDRIVSIGAFEHFGHERYDAFFSLAHRLLPADGVMLLHTIT 170
Cdd:NF040703 190 LSKEQLKLARERVA-AEGL-QDRVQLELLDYRDLPqdgrFDKVVSVGMFEHVGHANLPLYCQRLFGAVRPGGLVMNHGIT 267
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KPH_B       171 GLHPKeiherGLPMSFTFArflKFIVTEIFPGGRLPSIPMVQECASANGFTVTRVQSLQPHYAKTLDLWSAALQANKGQA 250
Cdd:NF040703 268 ARHTD-----GRPVGRGAG---EFIGRYVFPHGELPHLATITASISEAGLEVVDVESLRLHYARTLEHWSARLEARLDEA 339
                        250       260       270
                 ....*....|....*....|....*....|..
1KPH_B       251 IALQSEEVYERYMKYLTGCAEMFRIGYIDVNQ 282
Cdd:NF040703 340 ARLVPERALRIWRLYLAGCAYGFARGWINLHQ 371
PRK11705 PRK11705
cyclopropane fatty acyl phospholipid synthase;
13-274 2.35e-64

cyclopropane fatty acyl phospholipid synthase;


Pssm-ID: 183282  Cd Length: 383  Bit Score: 206.62  E-value: 2.35e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KPH_B        13 QAHYDLSDDFFRLFLDPTQTYSCAYFERDDmTLQEAQIAKIDLALGKLGLQPGMTLLDVGCGWGATMMRAVEKYDVNVVG 92
Cdd:PRK11705 117 KEHYDLGNDLFEAMLDPRMQYSCGYWKDAD-TLEEAQEAKLDLICRKLQLKPGMRVLDIGCGWGGLARYAAEHYGVSVVG 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KPH_B        93 LTLSKNQANHVQQLVANSenlrSKRVLLAGWEQFDEPVDRIVSIGAFEHFGHERYDAFFSLAHRLLPADGVMLLHTI--- 169
Cdd:PRK11705 196 VTISAEQQKLAQERCAGL----PVEIRLQDYRDLNGQFDRIVSVGMFEHVGPKNYRTYFEVVRRCLKPDGLFLLHTIgsn 271
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KPH_B       170 -TGLHPKeiherglpmsftfarflKFIVTEIFPGGRLPSIPMVQEcASANGFTVTRVQSLQPHYAKTLDLWSAALQANKG 248
Cdd:PRK11705 272 kTDTNVD-----------------PWINKYIFPNGCLPSVRQIAQ-ASEGLFVMEDWHNFGADYDRTLMAWHENFEAAWP 333
                        250       260
                 ....*....|....*....|....*...
1KPH_B       249 QAIALQSEEVYE--RYmkYLTGCAEMFR 274
Cdd:PRK11705 334 ELADNYSERFYRmwRY--YLLSCAGAFR 359
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
67-171 1.27e-13

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: 65.53  E-value: 1.27e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KPH_B       67 TLLDVGCGWGATMMRAVEKYDVNVVGLTLSKNQANHVQQLVANSENLRsKRVLLAGWEQF----DEPVDRIVSIGAFEHF 142
Cdd:cd02440   1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADN-VEVLKGDAEELppeaDESFDVIISDPPLHHL 79
                        90       100
                ....*....|....*....|....*....
1KPH_B      143 gHERYDAFFSLAHRLLPADGVMLLHTITG 171
Cdd:cd02440  80 -VEDLARFLEEARRLLKPGGVLVLTLVLA 107
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
69-158 1.56e-12

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 62.20  E-value: 1.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KPH_B         69 LDVGCGWGATMMRAVEKYDVNVVGLTLSKNQANHVQQLVANSE-NLRSKRVLLAGWEQFDEPVDRIVSIGAFEHFGHERY 147
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGlNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLPDPDL 81
                          90
                  ....*....|.
1KPH_B        148 DAFFSLAHRLL 158
Cdd:pfam13649  82 EAALREIARVL 92
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
54-180 6.66e-11

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: 59.24  E-value: 6.66e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KPH_B       54 DLALGKLGLQPGMTLLDVGCGWGATmMRAVEKYDVNVVGLTLSKNQANHVQQLVAnSENLRSkRVLLAGWEQF---DEPV 130
Cdd:COG2226  12 EALLAALGLRPGARVLDLGCGTGRL-ALALAERGARVTGVDISPEMLELARERAA-EAGLNV-EFVVGDAEDLpfpDGSF 88
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
1KPH_B      131 DRIVSIGAFEHFghERYDAFFSLAHRLLPADGVMLLHTITGLHPKEIHER 180
Cdd:COG2226  89 DLVISSFVLHHL--PDPERALAEIARVLKPGGRLVVVDFSPPDLAELEEL 136
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
62-169 3.71e-08

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: 51.17  E-value: 3.71e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KPH_B       62 LQPGMTLLDVGCGWGAtMMRAVEKYDVNVVGLTLSKNQANHVQQLvANSENLrskRVLLAGWEQF---DEPVDRIVSIGA 138
Cdd:COG2227  22 LPAGGRVLDVGCGTGR-LALALARRGADVTGVDISPEALEIARER-AAELNV---DFVQGDLEDLpleDGSFDLVICSEV 96
                        90       100       110
                ....*....|....*....|....*....|.
1KPH_B      139 FEHFGHEryDAFFSLAHRLLPADGVMLLHTI 169
Cdd:COG2227  97 LEHLPDP--AALLRELARLLKPGGLLLLSTP 125
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
53-166 1.43e-07

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 50.69  E-value: 1.43e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KPH_B       53 IDLALGKLGLQPGMTLLDVGCGWGATMMRAVEKYDVNVVGLTLSKNQANHVQQLvANSENLRSKRVLLAGWEQF----DE 128
Cdd:COG0500  15 AALLALLERLPKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARAR-AAKAGLGNVEFLVADLAELdplpAE 93
                        90       100       110
                ....*....|....*....|....*....|....*...
1KPH_B      129 PVDRIVSIGAFEHFGHERYDAFFSLAHRLLPADGVMLL 166
Cdd:COG0500  94 SFDLVVAFGVLHHLPPEEREALLRELARALKPGGVLLL 131
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
20-98 8.77e-07

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 49.75  E-value: 8.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KPH_B        20 DDFFRLFLDPTQtYSCAYFERDDMTLQEAQIAKIDLA-----LGKLGLQPGMTLLDVGCGWGATMMRAVEKYDVNVVGLT 94
Cdd:PLN02336 218 DKGFQRFLDNVQ-YKSSGILRYERVFGEGFVSTGGLEttkefVDKLDLKPGQKVLDVGCGIGGGDFYMAENFDVHVVGID 296

                 ....
1KPH_B        95 LSKN 98
Cdd:PLN02336 297 LSVN 300
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
69-166 4.02e-06

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 44.58  E-value: 4.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KPH_B         69 LDVGCGWGAtMMRAVEKYDVNVVGLTLS---------KNQANHVQQLVANSENLrskrvllagweQF-DEPVDRIVSIGA 138
Cdd:pfam08241   1 LDVGCGTGL-LTELLARLGARVTGVDISpemlelareKAPREGLTFVVGDAEDL-----------PFpDNSFDLVLSSEV 68
                          90       100
                  ....*....|....*....|....*...
1KPH_B        139 FEHFghERYDAFFSLAHRLLPADGVMLL 166
Cdd:pfam08241  69 LHHV--EDPERALREIARVLKPGGILII 94
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
64-166 7.44e-06

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 43.66  E-value: 7.44e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KPH_B       64 PGMTLLDVGCGWGATMMRAVEKY-DVNVVGLTLSknqANHVQQLVANSENLRSKRVLLAGWeQFDEPVDRIVSIGAFEHF 142
Cdd:COG4106   1 PPRRVLDLGCGTGRLTALLAERFpGARVTGVDLS---PEMLARARARLPNVRFVVADLRDL-DPPEPFDLVVSNAALHWL 76
                        90       100
                ....*....|....*....|....
1KPH_B      143 ghERYDAFFSLAHRLLPADGVMLL 166
Cdd:COG4106  77 --PDHAALLARLAAALAPGGVLAV 98
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
69-163 2.89e-05

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 41.97  E-value: 2.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KPH_B         69 LDVGCGWGATMMRAVEKY-DVNVVGLTLSKNQANHVQQLVANSENLRSKRVLLAGW---EQFDEPVDRIVSIGAFEHFGH 144
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALpGLEYTGLDISPAALEAARERLAALGLLNAVRVELFQLdlgELDPGSFDVVVASNVLHHLAD 80
                          90
                  ....*....|....*....
1KPH_B        145 ERydAFFSLAHRLLPADGV 163
Cdd:pfam08242  81 PR--AVLRNIRRLLKPGGV 97
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
64-170 1.49e-04

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 41.26  E-value: 1.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KPH_B         64 PGMTLLDVGCGWGaTMMRAVEKYDVNVVGLTLSKNQANHVqqlvanSENLRSKRVLLAGWEQFDEPVDRIVSIGAFEHFG 143
Cdd:pfam13489  22 SPGRVLDFGCGTG-IFLRLLRAQGFSVTGVDPSPIAIERA------LLNVRFDQFDEQEAAVPAGKFDVIVAREVLEHVP 94
                          90       100
                  ....*....|....*....|....*..
1KPH_B        144 HerYDAFFSLAHRLLPADGVMLLHTIT 170
Cdd:pfam13489  95 D--PPALLRQIAALLKPGGLLLLSTPL 119
PLN02244 PLN02244
tocopherol O-methyltransferase
37-108 3.05e-04

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 41.65  E-value: 3.05e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1KPH_B        37 YFERDDMT--LQEAQIAKIDLALGKLGLQPGM-----TLLDVGCGWGATMMRAVEKYDVNVVGLTLSKNQANHVQQLVA 108
Cdd:PLN02244  84 YYDPGASRgdHRQAQIRMIEESLAWAGVPDDDekrpkRIVDVGCGIGGSSRYLARKYGANVKGITLSPVQAARANALAA 162
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
52-226 4.99e-04

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: 40.17  E-value: 4.99e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KPH_B       52 KIDLA----LGKLGLQPGMTLLDVGCGWG---ATMMRA-----VEKYDVNVVGLTLSK-----NQANHVQQLVANsenlr 114
Cdd:COG2813  33 RLDIGtrllLEHLPEPLGGRVLDLGCGYGvigLALAKRnpearVTLVDVNARAVELARanaaaNGLENVEVLWSD----- 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KPH_B      115 skrvLLAGWEqfDEPVDRIVS---IgafeHFGHERYD----AFFSLAHRLLPADGVMLLhtitglhpkeIHERGLPMsft 187
Cdd:COG2813 108 ----GLSGVP--DGSFDLILSnppF----HAGRAVDKevahALIADAARHLRPGGELWL----------VANRHLPY--- 164
                       170       180       190
                ....*....|....*....|....*....|....*....
1KPH_B      188 fARFLKfivtEIFPGgrlpsipmVQECASANGFTVTRVQ 226
Cdd:COG2813 165 -ERKLE----ELFGN--------VEVLARNKGFKVLRAV 190
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
38-85 5.07e-04

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: 41.31  E-value: 5.07e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
1KPH_B       38 FERDD--MTLQEAQIakidLALGKLGLQPGMTLLDVGCGWGA---TMMR--------AVEK 85
Cdd:COG2242 223 FERDKgpITKREVRA----LTLAKLALRPGDVLWDIGAGSGSvsiEAARlapggrvyAIER 279
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
52-163 5.33e-04

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 39.98  E-value: 5.33e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KPH_B       52 KIDLALGKLGLQPGMTLLDVGCGWGaTMMRAVEKYDVNVVGLTLSKN-----QANHVQQLVANSEnlrskrvlLAGWEQF 126
Cdd:COG4976  34 LAEELLARLPPGPFGRVLDLGCGTG-LLGEALRPRGYRLTGVDLSEEmlakaREKGVYDRLLVAD--------LADLAEP 104
                        90       100       110
                ....*....|....*....|....*....|....*..
1KPH_B      127 DEPVDRIVSIGAFEHFGheRYDAFFSLAHRLLPADGV 163
Cdd:COG4976 105 DGRFDLIVAADVLTYLG--DLAAVFAGVARALKPGGL 139
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
55-138 1.96e-03

Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 38.50  E-value: 1.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KPH_B         55 LALGKLGLQPGMTLLDVGCGWG---ATMMRAVeKYDVNVVGLtlsknqaNHVQQLV----ANSENLRSKRVLLA------ 121
Cdd:pfam01135  64 MMLELLELKPGMRVLEIGSGSGyltACFARMV-GEVGRVVSI-------EHIPELVeiarRNLEKLGLENVIVVvgdgrq 135
                          90
                  ....*....|....*...
1KPH_B        122 GWEQFdEPVDRI-VSIGA 138
Cdd:pfam01135 136 GWPEF-APYDAIhVGAAA 152
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
38-82 5.67e-03

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


Pssm-ID: 234740  Cd Length: 198  Bit Score: 37.08  E-value: 5.67e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
1KPH_B        38 FERDD---MTLQEAQIakidLALGKLGLQPGMTLLDVGCGWGATMMRA 82
Cdd:PRK00377  15 FERDEeipMTKEEIRA----LALSKLRLRKGDMILDIGCGTGSVTVEA 58
 
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