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Conserved domains on  [gi|1718143695|gb|QDX30550|]
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cyclopropane fatty acyl phospholipid synthase [Dickeya poaceiphila]

Protein Classification

cyclopropane-fatty-acyl-phospholipid synthase( domain architecture ID 11485462)

cyclopropane-fatty-acyl-phospholipid synthase is a class I SAM-dependent methyltransferase catalyzing the transfer of a methylene group from S-adenosyl-L-methionine (SAM or AdoMet) to the cis double bond of an unsaturated fatty acid chain resulting in the replacement of the double bond with a methylene bridge

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK11705 PRK11705
cyclopropane fatty acyl phospholipid synthase;
1-382 0e+00

cyclopropane fatty acyl phospholipid synthase;


:

Pssm-ID: 183282  Cd Length: 383  Bit Score: 786.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695   1 MSNVCIVDDISEKNEWRRITQELLHQASITINGTEPWDIQINDSRFFKRVLQQGSLGLGESYMEGWWDCPRLDMFFHRIL 80
Cdd:PRK11705    1 MSSSCIEEVSVPDDNWYRIANELLARAGITINGSRPWDIQVHNPRFFKRVLQEGSLGLGESYMDGWWDCDRLDEFFSRVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695  81 AARLDEQRPSRWRDLMRIALARLVNLQSRKRAWQVGKVHYDLGNDLFSHMLDPYMQYSCGYWKQADTLEEAQQHKLALIC 160
Cdd:PRK11705   81 RAGLDEKLPHHLKDTLRILRARLFNLQSKKRAWIVGKEHYDLGNDLFEAMLDPRMQYSCGYWKDADTLEEAQEAKLDLIC 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 161 EKLQLKPGMTLLDIGCGWGGLAVYAAQHYGVTVHGITISAEQKAFIEERCGELDIHILLQDYRDLHQQYDRIVSVGMFEH 240
Cdd:PRK11705  161 RKLQLKPGMRVLDIGCGWGGLARYAAEHYGVSVVGVTISAEQQKLAQERCAGLPVEIRLQDYRDLNGQFDRIVSVGMFEH 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 241 VGPKNYADYFEMADRCLKPDGLFLLHTIGSNTTAHNVDPWINKYIFPNGCLPSIKQIASTSEPYFVMEDWHNFGADYDKT 320
Cdd:PRK11705  241 VGPKNYRTYFEVVRRCLKPDGLFLLHTIGSNKTDTNVDPWINKYIFPNGCLPSVRQIAQASEGLFVMEDWHNFGADYDRT 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1718143695 321 LMAWLARFNTAWPQLAADYSPAFRRMFSYYLTACAGAFRARNIQLWQVLFS-RGVTHGLCVPR 382
Cdd:PRK11705  321 LMAWHENFEAAWPELADNYSERFYRMWRYYLLSCAGAFRARDIQLWQVVFSpRGVEGGYRVPR 383
 
Name Accession Description Interval E-value
PRK11705 PRK11705
cyclopropane fatty acyl phospholipid synthase;
1-382 0e+00

cyclopropane fatty acyl phospholipid synthase;


Pssm-ID: 183282  Cd Length: 383  Bit Score: 786.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695   1 MSNVCIVDDISEKNEWRRITQELLHQASITINGTEPWDIQINDSRFFKRVLQQGSLGLGESYMEGWWDCPRLDMFFHRIL 80
Cdd:PRK11705    1 MSSSCIEEVSVPDDNWYRIANELLARAGITINGSRPWDIQVHNPRFFKRVLQEGSLGLGESYMDGWWDCDRLDEFFSRVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695  81 AARLDEQRPSRWRDLMRIALARLVNLQSRKRAWQVGKVHYDLGNDLFSHMLDPYMQYSCGYWKQADTLEEAQQHKLALIC 160
Cdd:PRK11705   81 RAGLDEKLPHHLKDTLRILRARLFNLQSKKRAWIVGKEHYDLGNDLFEAMLDPRMQYSCGYWKDADTLEEAQEAKLDLIC 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 161 EKLQLKPGMTLLDIGCGWGGLAVYAAQHYGVTVHGITISAEQKAFIEERCGELDIHILLQDYRDLHQQYDRIVSVGMFEH 240
Cdd:PRK11705  161 RKLQLKPGMRVLDIGCGWGGLARYAAEHYGVSVVGVTISAEQQKLAQERCAGLPVEIRLQDYRDLNGQFDRIVSVGMFEH 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 241 VGPKNYADYFEMADRCLKPDGLFLLHTIGSNTTAHNVDPWINKYIFPNGCLPSIKQIASTSEPYFVMEDWHNFGADYDKT 320
Cdd:PRK11705  241 VGPKNYRTYFEVVRRCLKPDGLFLLHTIGSNKTDTNVDPWINKYIFPNGCLPSVRQIAQASEGLFVMEDWHNFGADYDRT 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1718143695 321 LMAWLARFNTAWPQLAADYSPAFRRMFSYYLTACAGAFRARNIQLWQVLFS-RGVTHGLCVPR 382
Cdd:PRK11705  321 LMAWHENFEAAWPELADNYSERFYRMWRYYLLSCAGAFRARDIQLWQVVFSpRGVEGGYRVPR 383
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
108-368 6.54e-126

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: 363.57  E-value: 6.54e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 108 SRKRAWQVGKVHYDLGNDLFSHMLDPYMQYSCGYWKQAD-TLEEAQQHKLALICEKLQLKPGMTLLDIGCGWGGLAVYAA 186
Cdd:pfam02353   1 SKTRDAENIQAHYDLSNDFFALFLDPTMTYSCAYFERPDmTLEEAQQAKLDLILDKLGLKPGMTLLDIGCGWGGLMRRAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 187 QHYGVTVHGITISAEQKAFIEERCGELD----IHILLQDYRDLHQQYDRIVSVGMFEHVGPKNYADYFEMADRCLKPDGL 262
Cdd:pfam02353  81 ERYDVNVVGLTLSKNQYKLARKRVAAEGlarkVEVLLQDYRDFDEPFDRIVSVGMFEHVGHENYDTFFKKLYNLLPPGGL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 263 FLLHTIGS-----NTTAHNVDPWINKYIFPNGCLPSIKQIAST-SEPYFVMEDWHNFGADYDKTLMAWLARFNTAWPQLA 336
Cdd:pfam02353 161 MLLHTITGlhpdeTSERGLPLKFIDKYIFPGGELPSISMIVESsSEAGFTVEDVESLRPHYAKTLDLWAENLQANKDEAI 240
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1718143695 337 ADYSPAFRRMFSYYLTACAGAFRARNIQLWQV 368
Cdd:pfam02353 241 ALQSEEFYRMWMLYLTGCAVAFRIGYIDVHQF 272
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
119-267 4.00e-80

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 242.53  E-value: 4.00e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 119 HYDLGNDLFSHMLDPYMQYSCGYWKQAD-TLEEAQQHKLALICEKLQLKPGMTLLDIGCGWGGLAVYAAQHYGVTVHGIT 197
Cdd:COG2230     2 HYDLGNDFYRLFLDPTMTYSCAYFEDPDdTLEEAQEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGVT 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1718143695 198 ISAEQKAFIEERCGELD----IHILLQDYRDL--HQQYDRIVSVGMFEHVGPKNYADYFEMADRCLKPDGLFLLHT 267
Cdd:COG2230    82 LSPEQLEYARERAAEAGladrVEVRLADYRDLpaDGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLLHT 157
cyclopro_CfaB NF040703
C17 cyclopropane fatty acid synthase CfaB;
119-369 1.58e-66

C17 cyclopropane fatty acid synthase CfaB;


Pssm-ID: 468667 [Multi-domain]  Cd Length: 393  Bit Score: 215.63  E-value: 1.58e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 119 HYDLGNDLFSHMLDPYMQYSCGYWKQA-DTLEEAQQHKLALICEKLQLKPGMTLLDIGCGWGGLAVYAAQHYGVTVHGIT 197
Cdd:NF040703  110 HYDLSNDFYALWLDPDMVYSCAYFETGtEDLAQAQQAKLRHLCRKLRLQPGERLLDVGCGWGGLARFAAREFGVEVFGIT 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 198 ISAEQKAFIEERCGE--LD--IHILLQDYRDLHQ--QYDRIVSVGMFEHVGPKNYADYFEMADRCLKPDGLFLLHTIgsn 271
Cdd:NF040703  190 LSKEQLKLARERVAAegLQdrVQLELLDYRDLPQdgRFDKVVSVGMFEHVGHANLPLYCQRLFGAVRPGGLVMNHGI--- 266
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 272 tTAHNVD---------PWINKYIFPNGCLPSIKQI-ASTSEPYFVMEDWHNFGADYDKTLMAWLARFNTAWPQLAADYSP 341
Cdd:NF040703  267 -TARHTDgrpvgrgagEFIGRYVFPHGELPHLATItASISEAGLEVVDVESLRLHYARTLEHWSARLEARLDEAARLVPE 345
                         250       260
                  ....*....|....*....|....*...
gi 1718143695 342 AFRRMFSYYLTACAGAFRARNIQLWQVL 369
Cdd:NF040703  346 RALRIWRLYLAGCAYGFARGWINLHQIL 373
mycolic_MTase NF040660
cyclopropane mycolic acid synthase family methyltransferase; Members of this family include ...
119-368 1.73e-57

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: 188.82  E-value: 1.73e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 119 HYDLGNDLFSHMLDPYMQYSCGYWKQAD-TLEEAQQHKLALICEKLQLKPGMTLLDIGCGWGGLAVYAAQHYGVTVHGIT 197
Cdd:NF040660   11 HYDLSDDFFALFLDPTQTYSCAYFERDDmTLEEAQIAKIDLALGKLNLEPGMTLLDIGCGWGATMRRAVEKYDVNVVGLT 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 198 ISAEQKAFIEERCGELDI----HILLQDYRDLHQQYDRIVSVGMFEHVGPKNYADYFEMADRCLKPDGLFLLHTIGSNTT 273
Cdd:NF040660   91 LSKNQAAHVQQVLDEIDTprsrRVLLQGWEEFDEPVDRIVSIGAFEHFGHERYDDFFKRAYNILPADGRMLLHTITGLHR 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 274 AHNVD-------------PWINKYIFPNGCLPSIKQIASTSEPY-FVMEDWHNFGADYDKTLMAWLARFNTAWPQLAADY 339
Cdd:NF040660  171 KEMHErglpltmelarfiKFIVTEIFPGGRLPSIEMVVEHAEKAgFTVTRVQSLQPHYARTLDLWADALQAHKDEAIAIQ 250
                         250       260
                  ....*....|....*....|....*....
gi 1718143695 340 SPAFRRMFSYYLTACAGAFRARNIQLWQV 368
Cdd:NF040660  251 SEEVYERYMKYLTGCAKLFRDGYIDVNQF 279
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
170-266 2.61e-12

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


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 62.83  E-value: 2.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 170 TLLDIGCGWGGLAVYAAQHYGVTVHGITISAEQKAFIEE---RCGELDIHILLQDYRDLH----QQYDRIVSVGMFEHVg 242
Cdd:cd02440     1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKaaaALLADNVEVLKGDAEELPpeadESFDVIISDPPLHHL- 79
                          90       100
                  ....*....|....*....|....
gi 1718143695 243 PKNYADYFEMADRCLKPDGLFLLH 266
Cdd:cd02440    80 VEDLARFLEEARRLLKPGGVLVLT 103
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
172-272 4.35e-07

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 50.49  E-value: 4.35e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695  172 LDIGCGWG-GLAVYAAQHYGVTVHGITISAEQKAFIEERCGELdihiLLQD-----YRDLHQQ-----YDRIVSVGMFEH 240
Cdd:smart00828   4 LDFGCGYGsDLIDLAERHPHLQLHGYTISPEQAEVGRERIRAL----GLQGririfYRDSAKDpfpdtYDLVFGFEVIHH 79
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1718143695  241 VgpKNYADYFEMADRCLKPDGLFLLHTIGSNT 272
Cdd:smart00828  80 I--KDKMDLFSNISRHLKDGGHLVLADFIANL 109
 
Name Accession Description Interval E-value
PRK11705 PRK11705
cyclopropane fatty acyl phospholipid synthase;
1-382 0e+00

cyclopropane fatty acyl phospholipid synthase;


Pssm-ID: 183282  Cd Length: 383  Bit Score: 786.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695   1 MSNVCIVDDISEKNEWRRITQELLHQASITINGTEPWDIQINDSRFFKRVLQQGSLGLGESYMEGWWDCPRLDMFFHRIL 80
Cdd:PRK11705    1 MSSSCIEEVSVPDDNWYRIANELLARAGITINGSRPWDIQVHNPRFFKRVLQEGSLGLGESYMDGWWDCDRLDEFFSRVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695  81 AARLDEQRPSRWRDLMRIALARLVNLQSRKRAWQVGKVHYDLGNDLFSHMLDPYMQYSCGYWKQADTLEEAQQHKLALIC 160
Cdd:PRK11705   81 RAGLDEKLPHHLKDTLRILRARLFNLQSKKRAWIVGKEHYDLGNDLFEAMLDPRMQYSCGYWKDADTLEEAQEAKLDLIC 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 161 EKLQLKPGMTLLDIGCGWGGLAVYAAQHYGVTVHGITISAEQKAFIEERCGELDIHILLQDYRDLHQQYDRIVSVGMFEH 240
Cdd:PRK11705  161 RKLQLKPGMRVLDIGCGWGGLARYAAEHYGVSVVGVTISAEQQKLAQERCAGLPVEIRLQDYRDLNGQFDRIVSVGMFEH 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 241 VGPKNYADYFEMADRCLKPDGLFLLHTIGSNTTAHNVDPWINKYIFPNGCLPSIKQIASTSEPYFVMEDWHNFGADYDKT 320
Cdd:PRK11705  241 VGPKNYRTYFEVVRRCLKPDGLFLLHTIGSNKTDTNVDPWINKYIFPNGCLPSVRQIAQASEGLFVMEDWHNFGADYDRT 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1718143695 321 LMAWLARFNTAWPQLAADYSPAFRRMFSYYLTACAGAFRARNIQLWQVLFS-RGVTHGLCVPR 382
Cdd:PRK11705  321 LMAWHENFEAAWPELADNYSERFYRMWRYYLLSCAGAFRARDIQLWQVVFSpRGVEGGYRVPR 383
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
108-368 6.54e-126

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: 363.57  E-value: 6.54e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 108 SRKRAWQVGKVHYDLGNDLFSHMLDPYMQYSCGYWKQAD-TLEEAQQHKLALICEKLQLKPGMTLLDIGCGWGGLAVYAA 186
Cdd:pfam02353   1 SKTRDAENIQAHYDLSNDFFALFLDPTMTYSCAYFERPDmTLEEAQQAKLDLILDKLGLKPGMTLLDIGCGWGGLMRRAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 187 QHYGVTVHGITISAEQKAFIEERCGELD----IHILLQDYRDLHQQYDRIVSVGMFEHVGPKNYADYFEMADRCLKPDGL 262
Cdd:pfam02353  81 ERYDVNVVGLTLSKNQYKLARKRVAAEGlarkVEVLLQDYRDFDEPFDRIVSVGMFEHVGHENYDTFFKKLYNLLPPGGL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 263 FLLHTIGS-----NTTAHNVDPWINKYIFPNGCLPSIKQIAST-SEPYFVMEDWHNFGADYDKTLMAWLARFNTAWPQLA 336
Cdd:pfam02353 161 MLLHTITGlhpdeTSERGLPLKFIDKYIFPGGELPSISMIVESsSEAGFTVEDVESLRPHYAKTLDLWAENLQANKDEAI 240
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1718143695 337 ADYSPAFRRMFSYYLTACAGAFRARNIQLWQV 368
Cdd:pfam02353 241 ALQSEEFYRMWMLYLTGCAVAFRIGYIDVHQF 272
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
119-267 4.00e-80

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 242.53  E-value: 4.00e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 119 HYDLGNDLFSHMLDPYMQYSCGYWKQAD-TLEEAQQHKLALICEKLQLKPGMTLLDIGCGWGGLAVYAAQHYGVTVHGIT 197
Cdd:COG2230     2 HYDLGNDFYRLFLDPTMTYSCAYFEDPDdTLEEAQEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGVT 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1718143695 198 ISAEQKAFIEERCGELD----IHILLQDYRDL--HQQYDRIVSVGMFEHVGPKNYADYFEMADRCLKPDGLFLLHT 267
Cdd:COG2230    82 LSPEQLEYARERAAEAGladrVEVRLADYRDLpaDGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLLHT 157
cyclopro_CfaB NF040703
C17 cyclopropane fatty acid synthase CfaB;
119-369 1.58e-66

C17 cyclopropane fatty acid synthase CfaB;


Pssm-ID: 468667 [Multi-domain]  Cd Length: 393  Bit Score: 215.63  E-value: 1.58e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 119 HYDLGNDLFSHMLDPYMQYSCGYWKQA-DTLEEAQQHKLALICEKLQLKPGMTLLDIGCGWGGLAVYAAQHYGVTVHGIT 197
Cdd:NF040703  110 HYDLSNDFYALWLDPDMVYSCAYFETGtEDLAQAQQAKLRHLCRKLRLQPGERLLDVGCGWGGLARFAAREFGVEVFGIT 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 198 ISAEQKAFIEERCGE--LD--IHILLQDYRDLHQ--QYDRIVSVGMFEHVGPKNYADYFEMADRCLKPDGLFLLHTIgsn 271
Cdd:NF040703  190 LSKEQLKLARERVAAegLQdrVQLELLDYRDLPQdgRFDKVVSVGMFEHVGHANLPLYCQRLFGAVRPGGLVMNHGI--- 266
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 272 tTAHNVD---------PWINKYIFPNGCLPSIKQI-ASTSEPYFVMEDWHNFGADYDKTLMAWLARFNTAWPQLAADYSP 341
Cdd:NF040703  267 -TARHTDgrpvgrgagEFIGRYVFPHGELPHLATItASISEAGLEVVDVESLRLHYARTLEHWSARLEARLDEAARLVPE 345
                         250       260
                  ....*....|....*....|....*...
gi 1718143695 342 AFRRMFSYYLTACAGAFRARNIQLWQVL 369
Cdd:NF040703  346 RALRIWRLYLAGCAYGFARGWINLHQIL 373
mycolic_MTase NF040660
cyclopropane mycolic acid synthase family methyltransferase; Members of this family include ...
119-368 1.73e-57

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: 188.82  E-value: 1.73e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 119 HYDLGNDLFSHMLDPYMQYSCGYWKQAD-TLEEAQQHKLALICEKLQLKPGMTLLDIGCGWGGLAVYAAQHYGVTVHGIT 197
Cdd:NF040660   11 HYDLSDDFFALFLDPTQTYSCAYFERDDmTLEEAQIAKIDLALGKLNLEPGMTLLDIGCGWGATMRRAVEKYDVNVVGLT 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 198 ISAEQKAFIEERCGELDI----HILLQDYRDLHQQYDRIVSVGMFEHVGPKNYADYFEMADRCLKPDGLFLLHTIGSNTT 273
Cdd:NF040660   91 LSKNQAAHVQQVLDEIDTprsrRVLLQGWEEFDEPVDRIVSIGAFEHFGHERYDDFFKRAYNILPADGRMLLHTITGLHR 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 274 AHNVD-------------PWINKYIFPNGCLPSIKQIASTSEPY-FVMEDWHNFGADYDKTLMAWLARFNTAWPQLAADY 339
Cdd:NF040660  171 KEMHErglpltmelarfiKFIVTEIFPGGRLPSIEMVVEHAEKAgFTVTRVQSLQPHYARTLDLWADALQAHKDEAIAIQ 250
                         250       260
                  ....*....|....*....|....*....
gi 1718143695 340 SPAFRRMFSYYLTACAGAFRARNIQLWQV 368
Cdd:NF040660  251 SEEVYERYMKYLTGCAKLFRDGYIDVNQF 279
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
172-261 1.07e-20

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 85.69  E-value: 1.07e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 172 LDIGCGWGGLAVYAAQHYGVTVHGITISAEQKAFIEERCGE--LDIHILLQDYRDLH---QQYDRIVSVGMFEHVGPKNY 246
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEagLNVEFVQGDAEDLPfpdGSFDLVVSSGVLHHLPDPDL 81
                          90
                  ....*....|....*
gi 1718143695 247 ADYFEMADRCLKPDG 261
Cdd:pfam13649  82 EAALREIARVLKPGG 96
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
165-268 6.73e-20

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: 84.68  E-value: 6.73e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 165 LKPGMTLLDIGCGWGGLAVYAAQHyGVTVHGITISAEQKAFIEERCGELDIHILLQDYRDL---HQQYDRIVSVGMFEHV 241
Cdd:COG2227    22 LPAGGRVLDVGCGTGRLALALARR-GADVTGVDISPEALEIARERAAELNVDFVQGDLEDLpleDGSFDLVICSEVLEHL 100
                          90       100
                  ....*....|....*....|....*..
gi 1718143695 242 gpKNYADYFEMADRCLKPDGLFLLHTI 268
Cdd:COG2227   101 --PDPAALLRELARLLKPGGLLLLSTP 125
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
149-265 1.03e-17

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 80.73  E-value: 1.03e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 149 EEAQQHKLALICEKLQLKPGMTLLDIGCGWGGLAVYAAQHYGVTVHGITISAEQKAFIEERCGELD---IHILLQDYRDL 225
Cdd:COG0500     8 DELLPGLAALLALLERLPKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAGlgnVEFLVADLAEL 87
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1718143695 226 H----QQYDRIVSVGMFEHVGPKNYADYFEMADRCLKPDGLFLL 265
Cdd:COG0500    88 DplpaESFDLVVAFGVLHHLPPEEREALLRELARALKPGGVLLL 131
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
159-269 3.82e-15

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: 71.95  E-value: 3.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 159 ICEKLQLKPGMTLLDIGCGWGGLAVYAAQHyGVTVHGITISAEQKAFIEERCGE--LDIHILLQDYRDLH---QQYDRIV 233
Cdd:COG2226    14 LLAALGLRPGARVLDLGCGTGRLALALAER-GARVTGVDISPEMLELARERAAEagLNVEFVVGDAEDLPfpdGSFDLVI 92
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1718143695 234 SVGMFEHVgpKNYADYFEMADRCLKPDGLFLLHTIG 269
Cdd:COG2226    93 SSFVLHHL--PDPERALAEIARVLKPGGRLVVVDFS 126
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
172-265 4.31e-15

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 70.00  E-value: 4.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 172 LDIGCGWGGLAVYAAQhYGVTVHGITISAEQKAFIEERCGELDIHILLQDYRDL---HQQYDRIVSVGMFEHVgpKNYAD 248
Cdd:pfam08241   1 LDVGCGTGLLTELLAR-LGARVTGVDISPEMLELAREKAPREGLTFVVGDAEDLpfpDNSFDLVLSSEVLHHV--EDPER 77
                          90
                  ....*....|....*..
gi 1718143695 249 YFEMADRCLKPDGLFLL 265
Cdd:pfam08241  78 ALREIARVLKPGGILII 94
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
170-266 2.61e-12

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


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 62.83  E-value: 2.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 170 TLLDIGCGWGGLAVYAAQHYGVTVHGITISAEQKAFIEE---RCGELDIHILLQDYRDLH----QQYDRIVSVGMFEHVg 242
Cdd:cd02440     1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKaaaALLADNVEVLKGDAEELPpeadESFDVIISDPPLHHL- 79
                          90       100
                  ....*....|....*....|....
gi 1718143695 243 PKNYADYFEMADRCLKPDGLFLLH 266
Cdd:cd02440    80 VEDLARFLEEARRLLKPGGVLVLT 103
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
150-265 3.06e-12

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 64.63  E-value: 3.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 150 EAQQHKLALICEKLQLKPGMTLLDIGCGWGGLAVYAAQHyGVTVHGITISAEQKAFIEERCgeLDIHILLQDYRDLHQ-- 227
Cdd:COG4976    29 EAPALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPR-GYRLTGVDLSEEMLAKAREKG--VYDRLLVADLADLAEpd 105
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1718143695 228 -QYDRIVSVGMFEHVGpkNYADYFEMADRCLKPDGLFLL 265
Cdd:COG4976   106 gRFDLIVAADVLTYLG--DLAAVFAGVARALKPGGLFIF 142
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
165-298 2.82e-10

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 58.59  E-value: 2.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 165 LKPGMTLLDIGCGWGGLAVYAAQHyGVTVHGITISAEQkafiEERCGELDIHIL--LQDYRDLHQQYDRIVSVGMFEHVg 242
Cdd:pfam13489  20 LPSPGRVLDFGCGTGIFLRLLRAQ-GFSVTGVDPSPIA----IERALLNVRFDQfdEQEAAVPAGKFDVIVAREVLEHV- 93
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1718143695 243 pKNYADYFEMADRCLKPDGLFLLHTIGSNTTAHNVDPWiNKYIFPNG---CLPSIKQIA 298
Cdd:pfam13489  94 -PDPPALLRQIAALLKPGGLLLLSTPLASDEADRLLLE-WPYLRPRNghiSLFSARSLK 150
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
167-265 1.25e-09

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 54.83  E-value: 1.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 167 PGMTLLDIGCGWGGLAVYAAQHY-GVTVHGITISAEQKAFIEERCGelDIHILLQDYRDL--HQQYDRIVSVGMFEHVgp 243
Cdd:COG4106     1 PPRRVLDLGCGTGRLTALLAERFpGARVTGVDLSPEMLARARARLP--NVRFVVADLRDLdpPEPFDLVVSNAALHWL-- 76
                          90       100
                  ....*....|....*....|..
gi 1718143695 244 KNYADYFEMADRCLKPDGLFLL 265
Cdd:COG4106    77 PDHAALLARLAAALAPGGVLAV 98
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
172-263 1.22e-08

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 51.98  E-value: 1.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 172 LDIGCGWGGLAVYAAQHY-GVTVHGITISAEQKAFIEERCGELDIHILLQ---DYRDLHQQ----YDRIVSVGMFEHVGP 243
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALpGLEYTGLDISPAALEAARERLAALGLLNAVRvelFQLDLGELdpgsFDVVVASNVLHHLAD 80
                          90       100
                  ....*....|....*....|
gi 1718143695 244 KnyADYFEMADRCLKPDGLF 263
Cdd:pfam08242  81 P--RAVLRNIRRLLKPGGVL 98
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
172-272 4.35e-07

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 50.49  E-value: 4.35e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695  172 LDIGCGWG-GLAVYAAQHYGVTVHGITISAEQKAFIEERCGELdihiLLQD-----YRDLHQQ-----YDRIVSVGMFEH 240
Cdd:smart00828   4 LDFGCGYGsDLIDLAERHPHLQLHGYTISPEQAEVGRERIRAL----GLQGririfYRDSAKDpfpdtYDLVFGFEVIHH 79
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1718143695  241 VgpKNYADYFEMADRCLKPDGLFLLHTIGSNT 272
Cdd:smart00828  80 I--KDKMDLFSNISRHLKDGGHLVLADFIANL 109
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
161-209 1.34e-06

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 50.13  E-value: 1.34e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1718143695 161 EKLQLKPGMTLLDIGCGWGGLAVYAAQHYGVTVHGITISAEQKAFIEER 209
Cdd:PLN02336  260 DKLDLKPGQKVLDVGCGIGGGDFYMAENFDVHVVGIDLSVNMISFALER 308
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
165-265 3.65e-06

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 46.26  E-value: 3.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 165 LKPGMTLLDIGCGWGGLAVYAAQHYG--VTVHGITISAEQKAFIEERCGEL----------DIHILLQDYRDlhQQYDRI 232
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELAEELGpnAEVVGIDISEEAIEKARENAQKLgfdnvefeqgDIEELPELLED--DKFDVV 78
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1718143695 233 VSVGMFEHVGpkNYADYFEMADRCLKPDGLFLL 265
Cdd:pfam13847  79 ISNCVLNHIP--DPDKVLQEILRVLKPGGRLII 109
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
159-265 4.45e-06

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 47.66  E-value: 4.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 159 ICEKLQLKPGMTLLDIGCGWGGLAVYAAQHYGVTVHGITISAEQKAFIEERCGELD------IHILLQDYRDlhQQYDRI 232
Cdd:PTZ00098   44 ILSDIELNENSKVLDIGSGLGGGCKYINEKYGAHVHGVDICEKMVNIAKLRNSDKNkiefeaNDILKKDFPE--NTFDMI 121
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1718143695 233 VSVGMFEHVGPKNYADYFEMADRCLKPDGLFLL 265
Cdd:PTZ00098  122 YSRDAILHLSYADKKKLFEKCYKWLKPNGILLI 154
PRK08317 PRK08317
hypothetical protein; Provisional
161-279 2.24e-05

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 45.31  E-value: 2.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 161 EKLQLKPGMTLLDIGCGWGGLAVYAAQHYGVT--VHGITISAEQKAFIEER-CGELDIHILLQD------YRDlhQQYDR 231
Cdd:PRK08317   13 ELLAVQPGDRVLDVGCGPGNDARELARRVGPEgrVVGIDRSEAMLALAKERaAGLGPNVEFVRGdadglpFPD--GSFDA 90
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1718143695 232 IVSVGMFEHV-GPKNYADyfEMAdRCLKPDG-LFLLHTIGSNTTAHNVDP 279
Cdd:PRK08317   91 VRSDRVLQHLeDPARALA--EIA-RVLRPGGrVVVLDTDWDTLVWHSGDR 137
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
161-265 4.66e-05

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: 43.64  E-value: 4.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 161 EKLQLKPGMTLLDIGCGWGGLAVYAAQHYGV-TVHGITI------SAEQKAfieERCGELDIHILLQDYRD--LHQQYDR 231
Cdd:COG2813    43 EHLPEPLGGRVLDLGCGYGVIGLALAKRNPEaRVTLVDVnaraveLARANA---AANGLENVEVLWSDGLSgvPDGSFDL 119
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1718143695 232 IVSVGMFeHVGPKNYAD----YFEMADRCLKPDGLFLL 265
Cdd:COG2813   120 ILSNPPF-HAGRAVDKEvahaLIADAARHLRPGGELWL 156
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
154-265 6.74e-05

FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal sources FtsJ is a methyltransferase, but actually has no effect on cell division. FtsJ's substrate is the 23S rRNA. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. This family also includes the N terminus of flaviviral NS5 protein. It has been hypothesized that the N-terminal domain of NS5 is a methyltransferase involved in viral RNA capping.


Pssm-ID: 426399  Cd Length: 179  Bit Score: 42.96  E-value: 6.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 154 HKLALICEKLQ-LKPGMTLLDIGCGWGGLAVYAAQHYGVTVHGITI----------------------SAEQKAFIEERC 210
Cdd:pfam01728   7 YKLLEIDEKFGlLKPGKTVLDLGAAPGGWSQVALQRGAGKVVGVDLgpmqlwkprndpgvtfiqgdirDPETLDLLEELL 86
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1718143695 211 GELdIHILLQD---YRDLHQQYDRIVSVGMFEHVgpknyadyFEMADRCLKPDGLFLL 265
Cdd:pfam01728  87 GRK-VDLVLSDgspFISGNKVLDHLRSLDLVKAA--------LEVALELLRKGGNFVC 135
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
157-208 6.90e-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: 44.39  E-value: 6.90e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1718143695 157 ALICEKLQLKPGMTLLDIGCGWGGLAVYAA-QHYGVTVHGITISAEQKAFIEE 208
Cdd:COG2242   237 ALTLAKLALRPGDVLWDIGAGSGSVSIEAArLAPGGRVYAIERDPERAALIRA 289
PLN02244 PLN02244
tocopherol O-methyltransferase
144-204 7.08e-05

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 44.35  E-value: 7.08e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1718143695 144 QADTLEEAQqhKLALICEKLQLKPgMTLLDIGCGWGGLAVYAAQHYGVTVHGITISAEQKA 204
Cdd:PLN02244   98 QIRMIEESL--AWAGVPDDDEKRP-KRIVDVGCGIGGSSRYLARKYGANVKGITLSPVQAA 155
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
119-264 8.61e-05

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 43.60  E-value: 8.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 119 HYDLGNDLFSHMLDPYmqyscgyWKQAdtleeaqqhklalICEKLQLKPGMTLLDIGCGWGGLAVYAAQHYGVTVH--GI 196
Cdd:PRK00216   23 KYDLMNDLLSFGLHRV-------WRRK-------------TIKWLGVRPGDKVLDLACGTGDLAIALAKAVGKTGEvvGL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 197 TIS------AEQKAfiEERCGELDIHILLQDYRDL---HQQYDrIVSVGmFehvGPKNYADYF----EMAdRCLKPDGLF 263
Cdd:PRK00216   83 DFSegmlavGREKL--RDLGLSGNVEFVQGDAEALpfpDNSFD-AVTIA-F---GLRNVPDIDkalrEMY-RVLKPGGRL 154

                  .
gi 1718143695 264 L 264
Cdd:PRK00216  155 V 155
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
165-263 2.24e-04

tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 42.44  E-value: 2.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 165 LKPGMTLLDIGCGWGGLAVYAAQHY-GVTVHGITISAE-----QKAF----IEERcgeldIHILLQDYRDL-----HQQY 229
Cdd:COG4123    35 VKKGGRVLDLGTGTGVIALMLAQRSpGARITGVEIQPEaaelaRRNValngLEDR-----ITVIHGDLKEFaaelpPGSF 109
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1718143695 230 DRIVS------VGMFE-----------HVGPKNYADYFEMADRCLKPDGLF 263
Cdd:COG4123   110 DLVVSnppyfkAGSGRkspdearaiarHEDALTLEDLIRAAARLLKPGGRF 160
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
152-190 4.15e-04

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


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 41.20  E-value: 4.15e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1718143695 152 QQHKLALICEKLQLKPGMTLLDIGCGWGGLAVYAAQHYG 190
Cdd:pfam01135  58 APHMHAMMLELLELKPGMRVLEIGSGSGYLTACFARMVG 96
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
161-265 1.05e-03

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 40.53  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 161 EKLQLKPGMTLLDIGCGWGGLAVYAAQHY-GVTVHGITIS------AEQKAfieERCGELDIHILLQDYRD--LHQQYDR 231
Cdd:PRK09328  102 EALLLKEPLRVLDLGTGSGAIALALAKERpDAEVTAVDISpealavARRNA---KHGLGARVEFLQGDWFEplPGGRFDL 178
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1718143695 232 IVS----------------VGMFE-HV----GPKNYADY---FEMADRCLKPDGLFLL 265
Cdd:PRK09328  179 IVSnppyipeadihllqpeVRDHEpHLalfgGEDGLDFYrriIEQAPRYLKPGGWLLL 236
PRK13942 PRK13942
protein-L-isoaspartate O-methyltransferase; Provisional
154-213 2.64e-03

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 184409  Cd Length: 212  Bit Score: 38.84  E-value: 2.64e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 154 HKLALICEKLQLKPGMTLLDIGCGWGGLAVYAAQHYGVTVHGITIsaeqkafieERCGEL 213
Cdd:PRK13942   63 HMVAIMCELLDLKEGMKVLEIGTGSGYHAAVVAEIVGKSGKVVTI---------ERIPEL 113
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
161-269 4.23e-03

NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and conversion, General function prediction only];


Pssm-ID: 440369 [Multi-domain]  Cd Length: 322  Bit Score: 38.59  E-value: 4.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 161 EKLQLKPGMTLLDIGCGwGGLAVYAAQ---HYGVTVHGITISAEQKAFIEERCGEldiHILlqDYR--DLHQQ------- 228
Cdd:COG0604   133 DRGRLKPGETVLVHGAA-GGVGSAAVQlakALGARVIATASSPEKAELLRALGAD---HVI--DYReeDFAERvraltgg 206
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1718143695 229 --YDRIvsvgmFEHVGpknyADYFEMADRCLKPDGLFLlhTIG 269
Cdd:COG0604   207 rgVDVV-----LDTVG----GDTLARSLRALAPGGRLV--SIG 238
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
174-270 6.19e-03

Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 37.50  E-value: 6.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 174 IGCGWGGLAVYAAQHYGVT-VHGITISAEQ----KAFIEERCGELD---IHILLQD---Y-RDLHQQYDrIVSVGMFEHV 241
Cdd:COG0421    44 IGGGDGGLARELLKHPPVErVDVVEIDPEVvelaREYFPLLAPAFDdprLRVVIGDgraFlREAEESYD-VIIVDLTDPV 122
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1718143695 242 GPKNY---ADYFEMADRCLKPDGLFLLHTIGS 270
Cdd:COG0421   123 GPAEGlftREFYEDCRRALKPGGVLVVNLGSP 154
 
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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