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Conserved domains on  [gi|489942924|ref|WP_003846231|]
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MULTISPECIES: cyclopropane fatty acyl phospholipid synthase [Enterobacteriaceae]

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;
1-384 0e+00

cyclopropane fatty acyl phospholipid synthase;


:

Pssm-ID: 183282  Cd Length: 383  Bit Score: 783.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924   1 MNSLCSDAVIVNEtnDNWTRMGKELLSQADIRINGSRAWDIQLHHTGFFKRVLQQGSLGLGESYMEGWWDCERLDILFCK 80
Cdd:PRK11705   1 MSSSCIEEVSVPD--DNWYRIANELLARAGITINGSRPWDIQVHNPRFFKRVLQEGSLGLGESYMDGWWDCDRLDEFFSR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924  81 ILKAKLDQQMPGNLKDILRIASARLFNLQSRSRAWIVGKEHYDIGNDLFALMLDPHMQYSCGYWKDATTLNDAQNAKLKM 160
Cdd:PRK11705  79 VLRAGLDEKLPHHLKDTLRILRARLFNLQSKKRAWIVGKEHYDLGNDLFEAMLDPRMQYSCGYWKDADTLEEAQEAKLDL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924 161 ICEKLQLKPGMRLLDIGCGWGGLAEYAARHYGVAVEGVTISKEQQKMAQQRCEGLDVNILLQDYRDLNKHYDRIVSVGMF 240
Cdd:PRK11705 159 ICRKLQLKPGMRVLDIGCGWGGLARYAAEHYGVSVVGVTISAEQQKLAQERCAGLPVEIRLQDYRDLNGQFDRIVSVGMF 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924 241 EHVGPKNYDTYFSIADRCLKPDGLFLLHTIGSNKKGMSVDPWINKYIFPNGCLPAISHIAEASESRFVMEDWHNFGSDYD 320
Cdd:PRK11705 239 EHVGPKNYRTYFEVVRRCLKPDGLFLLHTIGSNKTDTNVDPWINKYIFPNGCLPSVRQIAQASEGLFVMEDWHNFGADYD 318
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489942924 321 KTLMAWHERFNQAWPELSSRYSATFRRMFNYYLCACAGAFRARDIELWQVLFS-RGVEGGIRVYR 384
Cdd:PRK11705 319 RTLMAWHENFEAAWPELADNYSERFYRMWRYYLLSCAGAFRARDIQLWQVVFSpRGVEGGYRVPR 383
 
Name Accession Description Interval E-value
PRK11705 PRK11705
cyclopropane fatty acyl phospholipid synthase;
1-384 0e+00

cyclopropane fatty acyl phospholipid synthase;


Pssm-ID: 183282  Cd Length: 383  Bit Score: 783.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924   1 MNSLCSDAVIVNEtnDNWTRMGKELLSQADIRINGSRAWDIQLHHTGFFKRVLQQGSLGLGESYMEGWWDCERLDILFCK 80
Cdd:PRK11705   1 MSSSCIEEVSVPD--DNWYRIANELLARAGITINGSRPWDIQVHNPRFFKRVLQEGSLGLGESYMDGWWDCDRLDEFFSR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924  81 ILKAKLDQQMPGNLKDILRIASARLFNLQSRSRAWIVGKEHYDIGNDLFALMLDPHMQYSCGYWKDATTLNDAQNAKLKM 160
Cdd:PRK11705  79 VLRAGLDEKLPHHLKDTLRILRARLFNLQSKKRAWIVGKEHYDLGNDLFEAMLDPRMQYSCGYWKDADTLEEAQEAKLDL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924 161 ICEKLQLKPGMRLLDIGCGWGGLAEYAARHYGVAVEGVTISKEQQKMAQQRCEGLDVNILLQDYRDLNKHYDRIVSVGMF 240
Cdd:PRK11705 159 ICRKLQLKPGMRVLDIGCGWGGLARYAAEHYGVSVVGVTISAEQQKLAQERCAGLPVEIRLQDYRDLNGQFDRIVSVGMF 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924 241 EHVGPKNYDTYFSIADRCLKPDGLFLLHTIGSNKKGMSVDPWINKYIFPNGCLPAISHIAEASESRFVMEDWHNFGSDYD 320
Cdd:PRK11705 239 EHVGPKNYRTYFEVVRRCLKPDGLFLLHTIGSNKTDTNVDPWINKYIFPNGCLPSVRQIAQASEGLFVMEDWHNFGADYD 318
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489942924 321 KTLMAWHERFNQAWPELSSRYSATFRRMFNYYLCACAGAFRARDIELWQVLFS-RGVEGGIRVYR 384
Cdd:PRK11705 319 RTLMAWHENFEAAWPELADNYSERFYRMWRYYLLSCAGAFRARDIQLWQVVFSpRGVEGGYRVPR 383
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
110-370 9.21e-128

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: 368.19  E-value: 9.21e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924  110 SRSRAWIVGKEHYDIGNDLFALMLDPHMQYSCGYWKDA-TTLNDAQNAKLKMICEKLQLKPGMRLLDIGCGWGGLAEYAA 188
Cdd:pfam02353   1 SKTRDAENIQAHYDLSNDFFALFLDPTMTYSCAYFERPdMTLEEAQQAKLDLILDKLGLKPGMTLLDIGCGWGGLMRRAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924  189 RHYGVAVEGVTISKEQQKMAQQRCEGLD----VNILLQDYRDLNKHYDRIVSVGMFEHVGPKNYDTYFSIADRCLKPDGL 264
Cdd:pfam02353  81 ERYDVNVVGLTLSKNQYKLARKRVAAEGlarkVEVLLQDYRDFDEPFDRIVSVGMFEHVGHENYDTFFKKLYNLLPPGGL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924  265 FLLHTIGSNKKGMSVD-----PWINKYIFPNGCLPAISHIAE-ASESRFVMEDWHNFGSDYDKTLMAWHERFNQAWPELS 338
Cdd:pfam02353 161 MLLHTITGLHPDETSErglplKFIDKYIFPGGELPSISMIVEsSSEAGFTVEDVESLRPHYAKTLDLWAENLQANKDEAI 240
                         250       260       270
                  ....*....|....*....|....*....|..
gi 489942924  339 SRYSATFRRMFNYYLCACAGAFRARDIELWQV 370
Cdd:pfam02353 241 ALQSEEFYRMWMLYLTGCAVAFRIGYIDVHQF 272
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
120-269 1.42e-78

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 238.68  E-value: 1.42e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924 120 EHYDIGNDLFALMLDPHMQYSCGYWKD-ATTLNDAQNAKLKMICEKLQLKPGMRLLDIGCGWGGLAEYAARHYGVAVEGV 198
Cdd:COG2230    1 HHYDLGNDFYRLFLDPTMTYSCAYFEDpDDTLEEAQEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGV 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489942924 199 TISKEQQKMAQQRCE--GLD--VNILLQDYRDLNK--HYDRIVSVGMFEHVGPKNYDTYFSIADRCLKPDGLFLLHT 269
Cdd:COG2230   81 TLSPEQLEYARERAAeaGLAdrVEVRLADYRDLPAdgQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLLHT 157
cyclopro_CfaB NF040703
C17 cyclopropane fatty acid synthase CfaB;
53-379 3.53e-74

C17 cyclopropane fatty acid synthase CfaB;


Pssm-ID: 468667 [Multi-domain]  Cd Length: 393  Bit Score: 235.66  E-value: 3.53e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924  53 LQQGSLG-LGESYMEGwwdceRLDILfckilkakldqqmpGNLKDILRIASARlfnlqsrSRAwIVGKE----------- 120
Cdd:NF040703  47 LTHPSLDlLGSAYVEG-----RLDLE--------------GPIMEVIRVGDEL-------SQA-LLGDDdeappertahd 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924 121 ----------HYDIGNDLFALMLDPHMQYSCGYWKDAT-TLNDAQNAKLKMICEKLQLKPGMRLLDIGCGWGGLAEYAAR 189
Cdd:NF040703 100 katdaaaisyHYDLSNDFYALWLDPDMVYSCAYFETGTeDLAQAQQAKLRHLCRKLRLQPGERLLDVGCGWGGLARFAAR 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924 190 HYGVAVEGVTISKEQQKMAQQRC--EGLD--VNILLQDYRDL--NKHYDRIVSVGMFEHVGPKNYDTYFSIADRCLKPDG 263
Cdd:NF040703 180 EFGVEVFGITLSKEQLKLARERVaaEGLQdrVQLELLDYRDLpqDGRFDKVVSVGMFEHVGHANLPLYCQRLFGAVRPGG 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924 264 LFLLHTIGSNKK-----GMSVDPWINKYIFPNGCLPAISHI-AEASESRFVMEDWHNFGSDYDKTLMAWHERFNQAWPEL 337
Cdd:NF040703 260 LVMNHGITARHTdgrpvGRGAGEFIGRYVFPHGELPHLATItASISEAGLEVVDVESLRLHYARTLEHWSARLEARLDEA 339
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 489942924 338 SSRYSATFRRMFNYYLCACAGAFRARDIELWQVLFSRGVEGG 379
Cdd:NF040703 340 ARLVPERALRIWRLYLAGCAYGFARGWINLHQILAVKPLADG 381
mycolic_MTase NF040660
cyclopropane mycolic acid synthase family methyltransferase; Members of this family include ...
121-370 2.93e-59

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: 193.45  E-value: 2.93e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924 121 HYDIGNDLFALMLDPHMQYSCGYW-KDATTLNDAQNAKLKMICEKLQLKPGMRLLDIGCGWGGLAEYAARHYGVAVEGVT 199
Cdd:NF040660  11 HYDLSDDFFALFLDPTQTYSCAYFeRDDMTLEEAQIAKIDLALGKLNLEPGMTLLDIGCGWGATMRRAVEKYDVNVVGLT 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924 200 ISKEQQKMAQQRCEGLDVN----ILLQDYRDLNKHYDRIVSVGMFEHVGPKNYDTYFSIADRCLKPDGLFLLHTIGS--- 272
Cdd:NF040660  91 LSKNQAAHVQQVLDEIDTPrsrrVLLQGWEEFDEPVDRIVSIGAFEHFGHERYDDFFKRAYNILPADGRMLLHTITGlhr 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924 273 ---NKKGMSVDPWINKY-------IFPNGCLPAISHIAE-ASESRFVMEDWHNFGSDYDKTLMAWHERFNQAWPELSSRY 341
Cdd:NF040660 171 kemHERGLPLTMELARFikfivteIFPGGRLPSIEMVVEhAEKAGFTVTRVQSLQPHYARTLDLWADALQAHKDEAIAIQ 250
                        250       260
                 ....*....|....*....|....*....
gi 489942924 342 SATFRRMFNYYLCACAGAFRARDIELWQV 370
Cdd:NF040660 251 SEEVYERYMKYLTGCAKLFRDGYIDVNQF 279
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
172-268 1.64e-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: 63.22  E-value: 1.64e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924 172 RLLDIGCGWGGLAEYAARHYGVAVEGVTISKEQQKMAQQRCEGL---DVNILLQDYRDL----NKHYDRIVSVGMFEHVg 244
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALladNVEVLKGDAEELppeaDESFDVIISDPPLHHL- 79
                         90       100
                 ....*....|....*....|....
gi 489942924 245 PKNYDTYFSIADRCLKPDGLFLLH 268
Cdd:cd02440   80 VEDLARFLEEARRLLKPGGVLVLT 103
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
172-273 1.06e-07

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 52.03  E-value: 1.06e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924   172 RLLDIGCGWG-GLAEYAARHYGVAVEGVTISKEQQKMAQQRCE--GLDVNILLQdYRDLNK-----HYDRIVSVGMFEHV 243
Cdd:smart00828   2 RVLDFGCGYGsDLIDLAERHPHLQLHGYTISPEQAEVGRERIRalGLQGRIRIF-YRDSAKdpfpdTYDLVFGFEVIHHI 80
                           90       100       110
                   ....*....|....*....|....*....|
gi 489942924   244 gpKNYDTYFSIADRCLKPDGLFLLHTIGSN 273
Cdd:smart00828  81 --KDKMDLFSNISRHLKDGGHLVLADFIAN 108
 
Name Accession Description Interval E-value
PRK11705 PRK11705
cyclopropane fatty acyl phospholipid synthase;
1-384 0e+00

cyclopropane fatty acyl phospholipid synthase;


Pssm-ID: 183282  Cd Length: 383  Bit Score: 783.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924   1 MNSLCSDAVIVNEtnDNWTRMGKELLSQADIRINGSRAWDIQLHHTGFFKRVLQQGSLGLGESYMEGWWDCERLDILFCK 80
Cdd:PRK11705   1 MSSSCIEEVSVPD--DNWYRIANELLARAGITINGSRPWDIQVHNPRFFKRVLQEGSLGLGESYMDGWWDCDRLDEFFSR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924  81 ILKAKLDQQMPGNLKDILRIASARLFNLQSRSRAWIVGKEHYDIGNDLFALMLDPHMQYSCGYWKDATTLNDAQNAKLKM 160
Cdd:PRK11705  79 VLRAGLDEKLPHHLKDTLRILRARLFNLQSKKRAWIVGKEHYDLGNDLFEAMLDPRMQYSCGYWKDADTLEEAQEAKLDL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924 161 ICEKLQLKPGMRLLDIGCGWGGLAEYAARHYGVAVEGVTISKEQQKMAQQRCEGLDVNILLQDYRDLNKHYDRIVSVGMF 240
Cdd:PRK11705 159 ICRKLQLKPGMRVLDIGCGWGGLARYAAEHYGVSVVGVTISAEQQKLAQERCAGLPVEIRLQDYRDLNGQFDRIVSVGMF 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924 241 EHVGPKNYDTYFSIADRCLKPDGLFLLHTIGSNKKGMSVDPWINKYIFPNGCLPAISHIAEASESRFVMEDWHNFGSDYD 320
Cdd:PRK11705 239 EHVGPKNYRTYFEVVRRCLKPDGLFLLHTIGSNKTDTNVDPWINKYIFPNGCLPSVRQIAQASEGLFVMEDWHNFGADYD 318
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489942924 321 KTLMAWHERFNQAWPELSSRYSATFRRMFNYYLCACAGAFRARDIELWQVLFS-RGVEGGIRVYR 384
Cdd:PRK11705 319 RTLMAWHENFEAAWPELADNYSERFYRMWRYYLLSCAGAFRARDIQLWQVVFSpRGVEGGYRVPR 383
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
110-370 9.21e-128

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: 368.19  E-value: 9.21e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924  110 SRSRAWIVGKEHYDIGNDLFALMLDPHMQYSCGYWKDA-TTLNDAQNAKLKMICEKLQLKPGMRLLDIGCGWGGLAEYAA 188
Cdd:pfam02353   1 SKTRDAENIQAHYDLSNDFFALFLDPTMTYSCAYFERPdMTLEEAQQAKLDLILDKLGLKPGMTLLDIGCGWGGLMRRAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924  189 RHYGVAVEGVTISKEQQKMAQQRCEGLD----VNILLQDYRDLNKHYDRIVSVGMFEHVGPKNYDTYFSIADRCLKPDGL 264
Cdd:pfam02353  81 ERYDVNVVGLTLSKNQYKLARKRVAAEGlarkVEVLLQDYRDFDEPFDRIVSVGMFEHVGHENYDTFFKKLYNLLPPGGL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924  265 FLLHTIGSNKKGMSVD-----PWINKYIFPNGCLPAISHIAE-ASESRFVMEDWHNFGSDYDKTLMAWHERFNQAWPELS 338
Cdd:pfam02353 161 MLLHTITGLHPDETSErglplKFIDKYIFPGGELPSISMIVEsSSEAGFTVEDVESLRPHYAKTLDLWAENLQANKDEAI 240
                         250       260       270
                  ....*....|....*....|....*....|..
gi 489942924  339 SRYSATFRRMFNYYLCACAGAFRARDIELWQV 370
Cdd:pfam02353 241 ALQSEEFYRMWMLYLTGCAVAFRIGYIDVHQF 272
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
120-269 1.42e-78

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 238.68  E-value: 1.42e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924 120 EHYDIGNDLFALMLDPHMQYSCGYWKD-ATTLNDAQNAKLKMICEKLQLKPGMRLLDIGCGWGGLAEYAARHYGVAVEGV 198
Cdd:COG2230    1 HHYDLGNDFYRLFLDPTMTYSCAYFEDpDDTLEEAQEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGV 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489942924 199 TISKEQQKMAQQRCE--GLD--VNILLQDYRDLNK--HYDRIVSVGMFEHVGPKNYDTYFSIADRCLKPDGLFLLHT 269
Cdd:COG2230   81 TLSPEQLEYARERAAeaGLAdrVEVRLADYRDLPAdgQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLLHT 157
cyclopro_CfaB NF040703
C17 cyclopropane fatty acid synthase CfaB;
53-379 3.53e-74

C17 cyclopropane fatty acid synthase CfaB;


Pssm-ID: 468667 [Multi-domain]  Cd Length: 393  Bit Score: 235.66  E-value: 3.53e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924  53 LQQGSLG-LGESYMEGwwdceRLDILfckilkakldqqmpGNLKDILRIASARlfnlqsrSRAwIVGKE----------- 120
Cdd:NF040703  47 LTHPSLDlLGSAYVEG-----RLDLE--------------GPIMEVIRVGDEL-------SQA-LLGDDdeappertahd 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924 121 ----------HYDIGNDLFALMLDPHMQYSCGYWKDAT-TLNDAQNAKLKMICEKLQLKPGMRLLDIGCGWGGLAEYAAR 189
Cdd:NF040703 100 katdaaaisyHYDLSNDFYALWLDPDMVYSCAYFETGTeDLAQAQQAKLRHLCRKLRLQPGERLLDVGCGWGGLARFAAR 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924 190 HYGVAVEGVTISKEQQKMAQQRC--EGLD--VNILLQDYRDL--NKHYDRIVSVGMFEHVGPKNYDTYFSIADRCLKPDG 263
Cdd:NF040703 180 EFGVEVFGITLSKEQLKLARERVaaEGLQdrVQLELLDYRDLpqDGRFDKVVSVGMFEHVGHANLPLYCQRLFGAVRPGG 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924 264 LFLLHTIGSNKK-----GMSVDPWINKYIFPNGCLPAISHI-AEASESRFVMEDWHNFGSDYDKTLMAWHERFNQAWPEL 337
Cdd:NF040703 260 LVMNHGITARHTdgrpvGRGAGEFIGRYVFPHGELPHLATItASISEAGLEVVDVESLRLHYARTLEHWSARLEARLDEA 339
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 489942924 338 SSRYSATFRRMFNYYLCACAGAFRARDIELWQVLFSRGVEGG 379
Cdd:NF040703 340 ARLVPERALRIWRLYLAGCAYGFARGWINLHQILAVKPLADG 381
mycolic_MTase NF040660
cyclopropane mycolic acid synthase family methyltransferase; Members of this family include ...
121-370 2.93e-59

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: 193.45  E-value: 2.93e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924 121 HYDIGNDLFALMLDPHMQYSCGYW-KDATTLNDAQNAKLKMICEKLQLKPGMRLLDIGCGWGGLAEYAARHYGVAVEGVT 199
Cdd:NF040660  11 HYDLSDDFFALFLDPTQTYSCAYFeRDDMTLEEAQIAKIDLALGKLNLEPGMTLLDIGCGWGATMRRAVEKYDVNVVGLT 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924 200 ISKEQQKMAQQRCEGLDVN----ILLQDYRDLNKHYDRIVSVGMFEHVGPKNYDTYFSIADRCLKPDGLFLLHTIGS--- 272
Cdd:NF040660  91 LSKNQAAHVQQVLDEIDTPrsrrVLLQGWEEFDEPVDRIVSIGAFEHFGHERYDDFFKRAYNILPADGRMLLHTITGlhr 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924 273 ---NKKGMSVDPWINKY-------IFPNGCLPAISHIAE-ASESRFVMEDWHNFGSDYDKTLMAWHERFNQAWPELSSRY 341
Cdd:NF040660 171 kemHERGLPLTMELARFikfivteIFPGGRLPSIEMVVEhAEKAGFTVTRVQSLQPHYARTLDLWADALQAHKDEAIAIQ 250
                        250       260
                 ....*....|....*....|....*....
gi 489942924 342 SATFRRMFNYYLCACAGAFRARDIELWQV 370
Cdd:NF040660 251 SEEVYERYMKYLTGCAKLFRDGYIDVNQF 279
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
174-263 1.76e-21

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 88.00  E-value: 1.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924  174 LDIGCGWGGLAEYAARHYGVAVEGVTISKEQQKMAQQRCE--GLDVNILLQDYRDL---NKHYDRIVSVGMFEHVGPKNY 248
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAeaGLNVEFVQGDAEDLpfpDGSFDLVVSSGVLHHLPDPDL 81
                          90
                  ....*....|....*
gi 489942924  249 DTYFSIADRCLKPDG 263
Cdd:pfam13649  82 EAALREIARVLKPGG 96
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
167-270 3.64e-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: 85.45  E-value: 3.64e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924 167 LKPGMRLLDIGCGWGGLAEYAARHyGVAVEGVTISKEQQKMAQQRCEGLDVNILLQDYRDL---NKHYDRIVSVGMFEHV 243
Cdd:COG2227   22 LPAGGRVLDVGCGTGRLALALARR-GADVTGVDISPEALEIARERAAELNVDFVQGDLEDLpleDGSFDLVICSEVLEHL 100
                         90       100
                 ....*....|....*....|....*..
gi 489942924 244 gpKNYDTYFSIADRCLKPDGLFLLHTI 270
Cdd:COG2227  101 --PDPAALLRELARLLKPGGLLLLSTP 125
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
161-267 3.04e-17

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 79.19  E-value: 3.04e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924 161 ICEKLQLKPGMRLLDIGCGWGGLAEYAARHYGVAVEGVTISKEQQKMAQQRCEGLD---VNILLQDYRDLNK----HYDR 233
Cdd:COG0500   18 LALLERLPKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAGlgnVEFLVADLAELDPlpaeSFDL 97
                         90       100       110
                 ....*....|....*....|....*....|....
gi 489942924 234 IVSVGMFEHVGPKNYDTYFSIADRCLKPDGLFLL 267
Cdd:COG0500   98 VVAFGVLHHLPPEEREALLRELARALKPGGVLLL 131
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
161-271 3.36e-17

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: 77.73  E-value: 3.36e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924 161 ICEKLQLKPGMRLLDIGCGWGGLAEYAARHyGVAVEGVTISKEQQKMAQQRCE--GLDVNILLQDYRDL---NKHYDRIV 235
Cdd:COG2226   14 LLAALGLRPGARVLDLGCGTGRLALALAER-GARVTGVDISPEMLELARERAAeaGLNVEFVVGDAEDLpfpDGSFDLVI 92
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489942924 236 SVGMFEHVgpKNYDTYFSIADRCLKPDGLFLLHTIG 271
Cdd:COG2226   93 SSFVLHHL--PDPERALAEIARVLKPGGRLVVVDFS 126
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
174-267 1.95e-15

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 71.16  E-value: 1.95e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924  174 LDIGCGWGGLAEYAARhYGVAVEGVTISKEQQKMAQQRCEGLDVNILLQDYRDL---NKHYDRIVSVGMFEHVgpKNYDT 250
Cdd:pfam08241   1 LDVGCGTGLLTELLAR-LGARVTGVDISPEMLELAREKAPREGLTFVVGDAEDLpfpDNSFDLVLSSEVLHHV--EDPER 77
                          90
                  ....*....|....*..
gi 489942924  251 YFSIADRCLKPDGLFLL 267
Cdd:pfam08241  78 ALREIARVLKPGGILII 94
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
172-268 1.64e-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: 63.22  E-value: 1.64e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924 172 RLLDIGCGWGGLAEYAARHYGVAVEGVTISKEQQKMAQQRCEGL---DVNILLQDYRDL----NKHYDRIVSVGMFEHVg 244
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALladNVEVLKGDAEELppeaDESFDVIISDPPLHHL- 79
                         90       100
                 ....*....|....*....|....
gi 489942924 245 PKNYDTYFSIADRCLKPDGLFLLH 268
Cdd:cd02440   80 VEDLARFLEEARRLLKPGGVLVLT 103
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
127-267 2.10e-12

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 65.02  E-value: 2.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924 127 DLFALMLDPHMQYSCGYwkdattlnDAQNAKLKMICEKLQLKPGMRLLDIGCGWGGLAEyAARHYGVAVEGVTISKEQQK 206
Cdd:COG4976   12 DQYADSYDAALVEDLGY--------EAPALLAEELLARLPPGPFGRVLDLGCGTGLLGE-ALRPRGYRLTGVDLSEEMLA 82
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489942924 207 MAQQRceGLDVNILLQDYRDL---NKHYDRIVSVGMFEHVGpkNYDTYFSIADRCLKPDGLFLL 267
Cdd:COG4976   83 KAREK--GVYDRLLVADLADLaepDGRFDLIVAADVLTYLG--DLAAVFAGVARALKPGGLFIF 142
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
169-267 4.12e-11

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 59.07  E-value: 4.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924 169 PGMRLLDIGCGWGGLAEY-AARHYGVAVEGVTISKEQQKMAQQRCEGLDVniLLQDYRDL--NKHYDRIVSVGMFEHVgp 245
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALlAERFPGARVTGVDLSPEMLARARARLPNVRF--VVADLRDLdpPEPFDLVVSNAALHWL-- 76
                         90       100
                 ....*....|....*....|..
gi 489942924 246 KNYDTYFSIADRCLKPDGLFLL 267
Cdd:COG4106   77 PDHAALLARLAAALAPGGVLAV 98
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
167-273 3.58e-10

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 58.21  E-value: 3.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924  167 LKPGMRLLDIGCGWGGLAEYaARHYGVAVEGVTISKEQQKMA--QQRCEGLDVnillQDYRDLNKHYDRIVSVGMFEHVg 244
Cdd:pfam13489  20 LPSPGRVLDFGCGTGIFLRL-LRAQGFSVTGVDPSPIAIERAllNVRFDQFDE----QEAAVPAGKFDVIVAREVLEHV- 93
                          90       100
                  ....*....|....*....|....*....
gi 489942924  245 pKNYDTYFSIADRCLKPDGLFLLHTIGSN 273
Cdd:pfam13489  94 -PDPPALLRQIAALLKPGGLLLLSTPLAS 121
PLN02244 PLN02244
tocopherol O-methyltransferase
122-209 8.73e-08

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 53.59  E-value: 8.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924 122 YDIGNDLFALMLDPHMQYscGYWKDATTLNDAQNAKLKMICEKL---------QLKPgMRLLDIGCGWGGLAEYAARHYG 192
Cdd:PLN02244  65 YDESSGVWEDVWGEHMHH--GYYDPGASRGDHRQAQIRMIEESLawagvpdddEKRP-KRIVDVGCGIGGSSRYLARKYG 141
                         90
                 ....*....|....*..
gi 489942924 193 VAVEGVTISKEQQKMAQ 209
Cdd:PLN02244 142 ANVKGITLSPVQAARAN 158
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
172-273 1.06e-07

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 52.03  E-value: 1.06e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924   172 RLLDIGCGWG-GLAEYAARHYGVAVEGVTISKEQQKMAQQRCE--GLDVNILLQdYRDLNK-----HYDRIVSVGMFEHV 243
Cdd:smart00828   2 RVLDFGCGYGsDLIDLAERHPHLQLHGYTISPEQAEVGRERIRalGLQGRIRIF-YRDSAKdpfpdTYDLVFGFEVIHHI 80
                           90       100       110
                   ....*....|....*....|....*....|
gi 489942924   244 gpKNYDTYFSIADRCLKPDGLFLLHTIGSN 273
Cdd:smart00828  81 --KDKMDLFSNISRHLKDGGHLVLADFIAN 108
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
159-275 7.24e-07

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 49.97  E-value: 7.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924 159 KMICEKLQLKPGMRLLDIGCGWGGLAEYAARHYGVAVEGVTISKEQQKMAQQRCEGLD------VNILLQDYRDLNkhYD 232
Cdd:PTZ00098  42 TKILSDIELNENSKVLDIGSGLGGGCKYINEKYGAHVHGVDICEKMVNIAKLRNSDKNkiefeaNDILKKDFPENT--FD 119
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 489942924 233 RIVSVGMFEHVGPKNYDTYFSIADRCLKPDGLFLLHTIGSNKK 275
Cdd:PTZ00098 120 MIYSRDAILHLSYADKKKLFEKCYKWLKPNGILLITDYCADKI 162
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
121-219 1.95e-06

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 48.61  E-value: 1.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924 121 HYDIGNDLFALMLDPhmqyscgYWKDATtlndaqnaklkmiCEKLQLKPGMRLLDIGCGWGGLAEYAARHYGVA--VEGV 198
Cdd:PRK00216  23 KYDLMNDLLSFGLHR-------VWRRKT-------------IKWLGVRPGDKVLDLACGTGDLAIALAKAVGKTgeVVGL 82
                         90       100
                 ....*....|....*....|...
gi 489942924 199 TISKEQQKMAQQRC--EGLDVNI 219
Cdd:PRK00216  83 DFSEGMLAVGREKLrdLGLSGNV 105
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
174-265 4.12e-06

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 45.05  E-value: 4.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924  174 LDIGCGWGGLAEYAARHY-GVAVEGVTISKEQQKMAQQR-CEGLDVNILLQDYRDLN------KHYDRIVSVGMFEHVGP 245
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALpGLEYTGLDISPAALEAARERlAALGLLNAVRVELFQLDlgeldpGSFDVVVASNVLHHLAD 80
                          90       100
                  ....*....|....*....|
gi 489942924  246 KnyDTYFSIADRCLKPDGLF 265
Cdd:pfam08242  81 P--RAVLRNIRRLLKPGGVL 98
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
159-215 1.19e-05

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 47.05  E-value: 1.19e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489942924 159 KMICEKLQLKPGMRLLDIGCGWGGLAEYAARHYGVAVEGVTISKEQQKMAQQRCEGL 215
Cdd:PLN02336 256 KEFVDKLDLKPGQKVLDVGCGIGGGDFYMAENFDVHVVGIDLSVNMISFALERAIGR 312
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
167-265 7.09e-05

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: 43.59  E-value: 7.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924 167 LKPGMRLLDIGCGWGGLAEY-AARHYGVAVEGVTISKEQQKMAQQRCE--GLD--VNILLQDYRDLNKH-----YDRIVS 236
Cdd:COG4123   35 VKKGGRVLDLGTGTGVIALMlAQRSPGARITGVEIQPEAAELARRNVAlnGLEdrITVIHGDLKEFAAElppgsFDLVVS 114
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 489942924 237 ------VGMFE-----------HVGPKNYDTYFSIADRCLKPDGLF 265
Cdd:COG4123  115 nppyfkAGSGRkspdearaiarHEDALTLEDLIRAAARLLKPGGRF 160
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
167-267 1.01e-04

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: 42.58  E-value: 1.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924  167 LKPGMRLLDIGCGWGGLAEYAARHYGVAVEGVTISKEQ--QKMAQQRCEGLDVNIL-LQDYRDLNKHYDRIVSV----GM 239
Cdd:pfam01728  19 LKPGKTVLDLGAAPGGWSQVALQRGAGKVVGVDLGPMQlwKPRNDPGVTFIQGDIRdPETLDLLEELLGRKVDLvlsdGS 98
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 489942924  240 FEHVGPKNYDTY---------FSIADRCLKPDGLFLL 267
Cdd:pfam01728  99 PFISGNKVLDHLrsldlvkaaLEVALELLRKGGNFVC 135
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
160-216 1.44e-04

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


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 42.36  E-value: 1.44e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924  160 MICEKLQLKPGMRLLDIGCGWGGLAEYAAR---HYGVAVeGVTISKEQQKMAQQRCEGLD 216
Cdd:pfam01135  64 MMLELLELKPGMRVLEIGSGSGYLTACFARmvgEVGRVV-SIEHIPELVEIARRNLEKLG 122
PRK08317 PRK08317
hypothetical protein; Provisional
163-263 2.38e-04

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 42.23  E-value: 2.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924 163 EKLQLKPGMRLLDIGCGWGGLAEYAARHYGVA--VEGVTISKEQQKMAQQRCEGLDVNILLQ-------DYRDLNkhYDR 233
Cdd:PRK08317  13 ELLAVQPGDRVLDVGCGPGNDARELARRVGPEgrVVGIDRSEAMLALAKERAAGLGPNVEFVrgdadglPFPDGS--FDA 90
                         90       100       110
                 ....*....|....*....|....*....|
gi 489942924 234 IVSVGMFEHVgpKNYDTYFSIADRCLKPDG 263
Cdd:PRK08317  91 VRSDRVLQHL--EDPARALAEIARVLRPGG 118
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
176-272 5.83e-04

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


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 40.58  E-value: 5.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924 176 IGCGWGGLAEYAARHYGVA-VEGVTISKEQQKMAQQ----RCEGLD---VNILLQD---Y-RDLNKHYDrIVSVGMFEHV 243
Cdd:COG0421   44 IGGGDGGLARELLKHPPVErVDVVEIDPEVVELAREyfplLAPAFDdprLRVVIGDgraFlREAEESYD-VIIVDLTDPV 122
                         90       100       110
                 ....*....|....*....|....*....|..
gi 489942924 244 GP-KNYDT--YFSIADRCLKPDGLFLLHTIGS 272
Cdd:COG0421  123 GPaEGLFTreFYEDCRRALKPGGVLVVNLGSP 154
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
163-267 9.60e-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: 39.79  E-value: 9.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924 163 EKLQLKPGMRLLDIGCGWGGLAEYAARHYGVA-VEGVTISKEQQKMAQQRCE--GLD-VNILLQDYRD--LNKHYDRIVS 236
Cdd:COG2813   43 EHLPEPLGGRVLDLGCGYGVIGLALAKRNPEArVTLVDVNARAVELARANAAanGLEnVEVLWSDGLSgvPDGSFDLILS 122
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489942924 237 VGMFeHVGPK-NYDTYFSI---ADRCLKPDGLFLL 267
Cdd:COG2813  123 NPPF-HAGRAvDKEVAHALiadAARHLRPGGELWL 156
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
167-267 9.62e-04

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 39.32  E-value: 9.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924  167 LKPGMRLLDIGCGWGGLAEYAARHYGVAVE--GVTISKEQQKMAQQRCE--GLD-VNILLQDYRDLNKHY-----DRIVS 236
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELAEELGPNAEvvGIDISEEAIEKARENAQklGFDnVEFEQGDIEELPELLeddkfDVVIS 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 489942924  237 VGMFEHVGpkNYDTYFSIADRCLKPDGLFLL 267
Cdd:pfam13847  81 NCVLNHIP--DPDKVLQEILRVLKPGGRLII 109
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
160-243 2.22e-03

Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 38.92  E-value: 2.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924 160 MICEKLQLKPGMRLLDIGCGwGG-----LAEYAARHYgvAVEgvtISKEQQKMAQQRCEGLDV-NILLqDYRDLNK---- 229
Cdd:COG2518   57 RMLEALDLKPGDRVLEIGTG-SGyqaavLARLAGRVY--SVE---RDPELAERARERLAALGYdNVTV-RVGDGALgwpe 129
                         90
                 ....*....|....*.
gi 489942924 230 --HYDRIVSVGMFEHV 243
Cdd:COG2518  130 haPFDRIIVTAAAPEV 145
RlmE COG0293
23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and ...
157-200 4.21e-03

23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and biogenesis]; 23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 440062 [Multi-domain]  Cd Length: 208  Bit Score: 38.13  E-value: 4.21e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489942924 157 KLKMICEKLQL-KPGMRLLDIGCGWGGLAEYAARHYG-----VAV--------EGVTI 200
Cdd:COG0293   37 KLLEIDEKDKLiKPGMRVVDLGAAPGGWSQVAAKRVGgkgrvIALdllpmepiPGVEF 94
pcm PRK00312
protein-L-isoaspartate(D-aspartate) O-methyltransferase;
159-235 6.71e-03

protein-L-isoaspartate(D-aspartate) O-methyltransferase;


Pssm-ID: 178974 [Multi-domain]  Cd Length: 212  Bit Score: 37.49  E-value: 6.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489942924 159 KMIcEKLQLKPGMRLLDIGCGWGG----LAEYAARHYgvavegvTIS--KEQQKMAQQRCEGLDV-NILLqdyrdlnKH- 230
Cdd:PRK00312  69 RMT-ELLELKPGDRVLEIGTGSGYqaavLAHLVRRVF-------SVEriKTLQWEAKRRLKQLGLhNVSV-------RHg 133
                         90
                 ....*....|....*.
gi 489942924 231 -----------YDRIV 235
Cdd:PRK00312 134 dgwkgwpayapFDRIL 149
 
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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