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Conserved domains on  [gi|1374243879|ref|WP_107217904|]
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cyclopropane fatty acyl phospholipid synthase [Photobacterium leiognathi]

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;
5-372 0e+00

cyclopropane fatty acyl phospholipid synthase;


:

Pssm-ID: 183282  Cd Length: 383  Bit Score: 624.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374243879   5 QIFQNILDFADVKINGDRPWDIQIHNEAVFDRVLKDGSLGFGESYMDGLWDCDAIDEMISRVLHAGIEDKLATTTKiqLG 84
Cdd:PRK11705   18 RIANELLARAGITINGSRPWDIQVHNPRFFKRVLQEGSLGLGESYMDGWWDCDRLDEFFSRVLRAGLDEKLPHHLK--DT 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374243879  85 LKAGASKLKHLFNPQSVERVTKDvpfHYDLGNDLFEAMLDPRMTYTCAYWKDSDDLKSAQEAKLDLVCRKMGLQPGMRLL 164
Cdd:PRK11705   96 LRILRARLFNLQSKKRAWIVGKE---HYDLGNDLFEAMLDPRMQYSCGYWKDADTLEEAQEAKLDLICRKLQLKPGMRVL 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374243879 165 DIGCGWGSFMMFAAEKYGVICDGLTLSKEQAALGQARAdeKGLPVNFILQDYRLYHpeQPYDRVVSIGMMEHVGPENYED 244
Cdd:PRK11705  173 DIGCGWGGLARYAAEHYGVSVVGVTISAEQQKLAQERC--AGLPVEIRLQDYRDLN--GQFDRIVSVGMFEHVGPKNYRT 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374243879 245 YFKAAYSFLADDGIFLLHTIGSPKSKSATDPWIDKYIFPNGVIPSMAQIGASAEDYFNIEDVQNIGPDYDKTLVAWNENF 324
Cdd:PRK11705  249 YFEVVRRCLKPDGLFLLHTIGSNKTDTNVDPWINKYIFPNGCLPSVRQIAQASEGLFVMEDWHNFGADYDRTLMAWHENF 328
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1374243879 325 EAAWPQLADKYGERFYRMWRYYLLSCAGAFRCRDLNVWQFGLTKKGAE 372
Cdd:PRK11705  329 EAAWPELADNYSERFYRMWRYYLLSCAGAFRARDIQLWQVVFSPRGVE 376
 
Name Accession Description Interval E-value
PRK11705 PRK11705
cyclopropane fatty acyl phospholipid synthase;
5-372 0e+00

cyclopropane fatty acyl phospholipid synthase;


Pssm-ID: 183282  Cd Length: 383  Bit Score: 624.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374243879   5 QIFQNILDFADVKINGDRPWDIQIHNEAVFDRVLKDGSLGFGESYMDGLWDCDAIDEMISRVLHAGIEDKLATTTKiqLG 84
Cdd:PRK11705   18 RIANELLARAGITINGSRPWDIQVHNPRFFKRVLQEGSLGLGESYMDGWWDCDRLDEFFSRVLRAGLDEKLPHHLK--DT 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374243879  85 LKAGASKLKHLFNPQSVERVTKDvpfHYDLGNDLFEAMLDPRMTYTCAYWKDSDDLKSAQEAKLDLVCRKMGLQPGMRLL 164
Cdd:PRK11705   96 LRILRARLFNLQSKKRAWIVGKE---HYDLGNDLFEAMLDPRMQYSCGYWKDADTLEEAQEAKLDLICRKLQLKPGMRVL 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374243879 165 DIGCGWGSFMMFAAEKYGVICDGLTLSKEQAALGQARAdeKGLPVNFILQDYRLYHpeQPYDRVVSIGMMEHVGPENYED 244
Cdd:PRK11705  173 DIGCGWGGLARYAAEHYGVSVVGVTISAEQQKLAQERC--AGLPVEIRLQDYRDLN--GQFDRIVSVGMFEHVGPKNYRT 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374243879 245 YFKAAYSFLADDGIFLLHTIGSPKSKSATDPWIDKYIFPNGVIPSMAQIGASAEDYFNIEDVQNIGPDYDKTLVAWNENF 324
Cdd:PRK11705  249 YFEVVRRCLKPDGLFLLHTIGSNKTDTNVDPWINKYIFPNGCLPSVRQIAQASEGLFVMEDWHNFGADYDRTLMAWHENF 328
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1374243879 325 EAAWPQLADKYGERFYRMWRYYLLSCAGAFRCRDLNVWQFGLTKKGAE 372
Cdd:PRK11705  329 EAAWPELADNYSERFYRMWRYYLLSCAGAFRARDIQLWQVVFSPRGVE 376
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
106-364 2.75e-118

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: 343.93  E-value: 2.75e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374243879 106 KDVPFHYDLGNDLFEAMLDPRMTYTCAYWKDSDD-LKSAQEAKLDLVCRKMGLQPGMRLLDIGCGWGSFMMFAAEKYGVI 184
Cdd:pfam02353   7 ENIQAHYDLSNDFFALFLDPTMTYSCAYFERPDMtLEEAQQAKLDLILDKLGLKPGMTLLDIGCGWGGLMRRAAERYDVN 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374243879 185 CDGLTLSKEQAALGQARADEKGLP--VNFILQDYRLYhpEQPYDRVVSIGMMEHVGPENYEDYFKAAYSFLADDGIFLLH 262
Cdd:pfam02353  87 VVGLTLSKNQYKLARKRVAAEGLArkVEVLLQDYRDF--DEPFDRIVSVGMFEHVGHENYDTFFKKLYNLLPPGGLMLLH 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374243879 263 TIGSPKSKSA-----TDPWIDKYIFPNGVIPSMAQIGASAEDY-FNIEDVQNIGPDYDKTLVAWNENFEAAWPQLADKYG 336
Cdd:pfam02353 165 TITGLHPDETserglPLKFIDKYIFPGGELPSISMIVESSSEAgFTVEDVESLRPHYAKTLDLWAENLQANKDEAIALQS 244
                         250       260
                  ....*....|....*....|....*...
gi 1374243879 337 ERFYRMWRYYLLSCAGAFRCRDLNVWQF 364
Cdd:pfam02353 245 EEFYRMWMLYLTGCAVAFRIGYIDVHQF 272
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
110-263 1.55e-76

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 233.28  E-value: 1.55e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374243879 110 FHYDLGNDLFEAMLDPRMTYTCAYWKDSDD-LKSAQEAKLDLVCRKMGLQPGMRLLDIGCGWGSFMMFAAEKYGVICDGL 188
Cdd:COG2230     1 HHYDLGNDFYRLFLDPTMTYSCAYFEDPDDtLEEAQEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGV 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1374243879 189 TLSKEQAALGQARADEKGLP--VNFILQDYRLYHPEQPYDRVVSIGMMEHVGPENYEDYFKAAYSFLADDGIFLLHT 263
Cdd:COG2230    81 TLSPEQLEYARERAAEAGLAdrVEVRLADYRDLPADGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLLHT 157
mycolic_MTase NF040660
cyclopropane mycolic acid synthase family methyltransferase; Members of this family include ...
107-368 1.83e-70

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: 222.34  E-value: 1.83e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374243879 107 DVPFHYDLGNDLFEAMLDPRMTYTCAYWKDSD-DLKSAQEAKLDLVCRKMGLQPGMRLLDIGCGWGSFMMFAAEKYGVIC 185
Cdd:NF040660    7 DVQAHYDLSDDFFALFLDPTQTYSCAYFERDDmTLEEAQIAKIDLALGKLNLEPGMTLLDIGCGWGATMRRAVEKYDVNV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374243879 186 DGLTLSKEQAALGQARADEKGLPVN--FILQDYRLYhpEQPYDRVVSIGMMEHVGPENYEDYFKAAYSFLADDGIFLLHT 263
Cdd:NF040660   87 VGLTLSKNQAAHVQQVLDEIDTPRSrrVLLQGWEEF--DEPVDRIVSIGAFEHFGHERYDDFFKRAYNILPADGRMLLHT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374243879 264 IGSPKSKSATD-------------PWIDKYIFPNGVIPSMAQIGASAEDY-FNIEDVQNIGPDYDKTLVAWNENFEAAWP 329
Cdd:NF040660  165 ITGLHRKEMHErglpltmelarfiKFIVTEIFPGGRLPSIEMVVEHAEKAgFTVTRVQSLQPHYARTLDLWADALQAHKD 244
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1374243879 330 QLADKYGERFYRMWRYYLLSCAGAFRCRDLNVWQFGLTK 368
Cdd:NF040660  245 EAIAIQSEEVYERYMKYLTGCAKLFRDGYIDVNQFTLAK 283
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
162-262 1.70e-09

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: 54.74  E-value: 1.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374243879 162 RLLDIGCGWGSFMMFAAEKYGVICDGLTLSKEQAALGQARADEKGLP-VNFILQDYR--LYHPEQPYDRVVSIGMMEHVg 238
Cdd:cd02440     1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADnVEVLKGDAEelPPEADESFDVIISDPPLHHL- 79
                          90       100
                  ....*....|....*....|....
gi 1374243879 239 PENYEDYFKAAYSFLADDGIFLLH 262
Cdd:cd02440    80 VEDLARFLEEARRLLKPGGVLVLT 103
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
162-261 7.49e-05

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 43.56  E-value: 7.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374243879  162 RLLDIGCGWGSFMMFAAEKYGVI-CDGLTLSKEQAALGQARADEKGLP--VNFILQDYRLYHPEQPYDRVVSIGMMEHVg 238
Cdd:smart00828   2 RVLDFGCGYGSDLIDLAERHPHLqLHGYTISPEQAEVGRERIRALGLQgrIRIFYRDSAKDPFPDTYDLVFGFEVIHHI- 80
                           90       100
                   ....*....|....*....|...
gi 1374243879  239 pENYEDYFKAAYSFLADDGIFLL 261
Cdd:smart00828  81 -KDKMDLFSNISRHLKDGGHLVL 102
 
Name Accession Description Interval E-value
PRK11705 PRK11705
cyclopropane fatty acyl phospholipid synthase;
5-372 0e+00

cyclopropane fatty acyl phospholipid synthase;


Pssm-ID: 183282  Cd Length: 383  Bit Score: 624.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374243879   5 QIFQNILDFADVKINGDRPWDIQIHNEAVFDRVLKDGSLGFGESYMDGLWDCDAIDEMISRVLHAGIEDKLATTTKiqLG 84
Cdd:PRK11705   18 RIANELLARAGITINGSRPWDIQVHNPRFFKRVLQEGSLGLGESYMDGWWDCDRLDEFFSRVLRAGLDEKLPHHLK--DT 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374243879  85 LKAGASKLKHLFNPQSVERVTKDvpfHYDLGNDLFEAMLDPRMTYTCAYWKDSDDLKSAQEAKLDLVCRKMGLQPGMRLL 164
Cdd:PRK11705   96 LRILRARLFNLQSKKRAWIVGKE---HYDLGNDLFEAMLDPRMQYSCGYWKDADTLEEAQEAKLDLICRKLQLKPGMRVL 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374243879 165 DIGCGWGSFMMFAAEKYGVICDGLTLSKEQAALGQARAdeKGLPVNFILQDYRLYHpeQPYDRVVSIGMMEHVGPENYED 244
Cdd:PRK11705  173 DIGCGWGGLARYAAEHYGVSVVGVTISAEQQKLAQERC--AGLPVEIRLQDYRDLN--GQFDRIVSVGMFEHVGPKNYRT 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374243879 245 YFKAAYSFLADDGIFLLHTIGSPKSKSATDPWIDKYIFPNGVIPSMAQIGASAEDYFNIEDVQNIGPDYDKTLVAWNENF 324
Cdd:PRK11705  249 YFEVVRRCLKPDGLFLLHTIGSNKTDTNVDPWINKYIFPNGCLPSVRQIAQASEGLFVMEDWHNFGADYDRTLMAWHENF 328
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1374243879 325 EAAWPQLADKYGERFYRMWRYYLLSCAGAFRCRDLNVWQFGLTKKGAE 372
Cdd:PRK11705  329 EAAWPELADNYSERFYRMWRYYLLSCAGAFRARDIQLWQVVFSPRGVE 376
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
106-364 2.75e-118

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: 343.93  E-value: 2.75e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374243879 106 KDVPFHYDLGNDLFEAMLDPRMTYTCAYWKDSDD-LKSAQEAKLDLVCRKMGLQPGMRLLDIGCGWGSFMMFAAEKYGVI 184
Cdd:pfam02353   7 ENIQAHYDLSNDFFALFLDPTMTYSCAYFERPDMtLEEAQQAKLDLILDKLGLKPGMTLLDIGCGWGGLMRRAAERYDVN 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374243879 185 CDGLTLSKEQAALGQARADEKGLP--VNFILQDYRLYhpEQPYDRVVSIGMMEHVGPENYEDYFKAAYSFLADDGIFLLH 262
Cdd:pfam02353  87 VVGLTLSKNQYKLARKRVAAEGLArkVEVLLQDYRDF--DEPFDRIVSVGMFEHVGHENYDTFFKKLYNLLPPGGLMLLH 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374243879 263 TIGSPKSKSA-----TDPWIDKYIFPNGVIPSMAQIGASAEDY-FNIEDVQNIGPDYDKTLVAWNENFEAAWPQLADKYG 336
Cdd:pfam02353 165 TITGLHPDETserglPLKFIDKYIFPGGELPSISMIVESSSEAgFTVEDVESLRPHYAKTLDLWAENLQANKDEAIALQS 244
                         250       260
                  ....*....|....*....|....*...
gi 1374243879 337 ERFYRMWRYYLLSCAGAFRCRDLNVWQF 364
Cdd:pfam02353 245 EEFYRMWMLYLTGCAVAFRIGYIDVHQF 272
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
110-263 1.55e-76

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 233.28  E-value: 1.55e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374243879 110 FHYDLGNDLFEAMLDPRMTYTCAYWKDSDD-LKSAQEAKLDLVCRKMGLQPGMRLLDIGCGWGSFMMFAAEKYGVICDGL 188
Cdd:COG2230     1 HHYDLGNDFYRLFLDPTMTYSCAYFEDPDDtLEEAQEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGV 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1374243879 189 TLSKEQAALGQARADEKGLP--VNFILQDYRLYHPEQPYDRVVSIGMMEHVGPENYEDYFKAAYSFLADDGIFLLHT 263
Cdd:COG2230    81 TLSPEQLEYARERAAEAGLAdrVEVRLADYRDLPADGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLLHT 157
mycolic_MTase NF040660
cyclopropane mycolic acid synthase family methyltransferase; Members of this family include ...
107-368 1.83e-70

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: 222.34  E-value: 1.83e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374243879 107 DVPFHYDLGNDLFEAMLDPRMTYTCAYWKDSD-DLKSAQEAKLDLVCRKMGLQPGMRLLDIGCGWGSFMMFAAEKYGVIC 185
Cdd:NF040660    7 DVQAHYDLSDDFFALFLDPTQTYSCAYFERDDmTLEEAQIAKIDLALGKLNLEPGMTLLDIGCGWGATMRRAVEKYDVNV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374243879 186 DGLTLSKEQAALGQARADEKGLPVN--FILQDYRLYhpEQPYDRVVSIGMMEHVGPENYEDYFKAAYSFLADDGIFLLHT 263
Cdd:NF040660   87 VGLTLSKNQAAHVQQVLDEIDTPRSrrVLLQGWEEF--DEPVDRIVSIGAFEHFGHERYDDFFKRAYNILPADGRMLLHT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374243879 264 IGSPKSKSATD-------------PWIDKYIFPNGVIPSMAQIGASAEDY-FNIEDVQNIGPDYDKTLVAWNENFEAAWP 329
Cdd:NF040660  165 ITGLHRKEMHErglpltmelarfiKFIVTEIFPGGRLPSIEMVVEHAEKAgFTVTRVQSLQPHYARTLDLWADALQAHKD 244
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1374243879 330 QLADKYGERFYRMWRYYLLSCAGAFRCRDLNVWQFGLTK 368
Cdd:NF040660  245 EAIAIQSEEVYERYMKYLTGCAKLFRDGYIDVNQFTLAK 283
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
164-257 1.60e-19

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 82.61  E-value: 1.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374243879 164 LDIGCGWGSFMMFAAEKYGVICDGLTLSKEQAALGQARADEKGLPVNFILQDYR-LYHPEQPYDRVVSIGMMEHVGPENY 242
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEdLPFPDGSFDLVVSSGVLHHLPDPDL 81
                          90
                  ....*....|....*
gi 1374243879 243 EDYFKAAYSFLADDG 257
Cdd:pfam13649  82 EAALREIARVLKPGG 96
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
143-261 6.92e-17

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 78.42  E-value: 6.92e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374243879 143 AQEAKLDLVCRKMGLQPGMRLLDIGCGWGSFMMFAAEKYGVICDGLTLSKEQAALGQARADEKGLP-VNFILQDYRLYH- 220
Cdd:COG0500    10 LLPGLAALLALLERLPKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAGLGnVEFLVADLAELDp 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1374243879 221 -PEQPYDRVVSIGMMEHVGPENYEDYFKAAYSFLADDGIFLL 261
Cdd:COG0500    90 lPAESFDLVVAFGVLHHLPPEEREALLRELARALKPGGVLLL 131
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
157-264 1.25e-15

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: 72.74  E-value: 1.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374243879 157 LQPGMRLLDIGCGWGSFMMFAAEKyGVICDGLTLSKEQAALGQARADEkgLPVNFILQDYR-LYHPEQPYDRVVSIGMME 235
Cdd:COG2227    22 LPAGGRVLDVGCGTGRLALALARR-GADVTGVDISPEALEIARERAAE--LNVDFVQGDLEdLPLEDGSFDLVICSEVLE 98
                          90       100
                  ....*....|....*....|....*....
gi 1374243879 236 HVgpENYEDYFKAAYSFLADDGIFLLHTI 264
Cdd:COG2227    99 HL--PDPAALLRELARLLKPGGLLLLSTP 125
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
149-267 3.53e-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: 3.53e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374243879 149 DLVCRKMGLQPGMRLLDIGCGWGSFMMFAAEKyGVICDGLTLSKEQAALGQARADEKGLPVNFILQD-YRLYHPEQPYDR 227
Cdd:COG2226    12 EALLAALGLRPGARVLDLGCGTGRLALALAER-GARVTGVDISPEMLELARERAAEAGLNVEFVVGDaEDLPFPDGSFDL 90
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1374243879 228 VVSIGMMEHVgpENYEDYFKAAYSFLADDGIFLLHTIGSP 267
Cdd:COG2226    91 VISSFVLHHL--PDPERALAEIARVLKPGGRLVVVDFSPP 128
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
159-261 4.63e-10

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 55.99  E-value: 4.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374243879 159 PGMRLLDIGCGWGSFMMFAAEKY-GVICDGLTLSKEQAALGQARADEkglpVNFILQDYRLYHPEQPYDRVVSIGMMEHV 237
Cdd:COG4106     1 PPRRVLDLGCGTGRLTALLAERFpGARVTGVDLSPEMLARARARLPN----VRFVVADLRDLDPPEPFDLVVSNAALHWL 76
                          90       100
                  ....*....|....*....|....
gi 1374243879 238 gpENYEDYFKAAYSFLADDGIFLL 261
Cdd:COG4106    77 --PDHAALLARLAAALAPGGVLAV 98
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
143-261 1.49e-09

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 56.93  E-value: 1.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374243879 143 AQEAKLDLVCRKMGLQPGMRLLDIGCGWGsfmMFAAE--KYGVICDGLTLSkeQAALgqARADEKGLPVNFILQDYR-LY 219
Cdd:COG4976    30 APALLAEELLARLPPGPFGRVLDLGCGTG---LLGEAlrPRGYRLTGVDLS--EEML--AKAREKGVYDRLLVADLAdLA 102
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1374243879 220 HPEQPYDRVVSIGMMEHVGpeNYEDYFKAAYSFLADDGIFLL 261
Cdd:COG4976   103 EPDGRFDLIVAADVLTYLG--DLAAVFAGVARALKPGGLFIF 142
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
162-262 1.70e-09

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: 54.74  E-value: 1.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374243879 162 RLLDIGCGWGSFMMFAAEKYGVICDGLTLSKEQAALGQARADEKGLP-VNFILQDYR--LYHPEQPYDRVVSIGMMEHVg 238
Cdd:cd02440     1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADnVEVLKGDAEelPPEADESFDVIISDPPLHHL- 79
                          90       100
                  ....*....|....*....|....
gi 1374243879 239 PENYEDYFKAAYSFLADDGIFLLH 262
Cdd:cd02440    80 VEDLARFLEEARRLLKPGGVLVLT 103
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
159-267 1.02e-07

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 51.27  E-value: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374243879 159 PGMRLLDIGCGWGSFMMFAAEK----YGVicdgltlskEQAALGQARADEKGLPVNFILQDyrLYHPEQPYDRVVSIGMM 234
Cdd:pfam13489  22 SPGRVLDFGCGTGIFLRLLRAQgfsvTGV---------DPSPIAIERALLNVRFDQFDEQE--AAVPAGKFDVIVAREVL 90
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1374243879 235 EHVgpENYEDYFKAAYSFLADDGIFLLHTIGSP 267
Cdd:pfam13489  91 EHV--PDPPALLRQIAALLKPGGLLLLSTPLAS 121
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
164-261 3.58e-07

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 47.66  E-value: 3.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374243879 164 LDIGCGWGSFMMFAAeKYGVICDGLTLSKEQAALgqARADEKGLPVNFILQD-YRLYHPEQPYDRVVSIGMMEHVgpENY 242
Cdd:pfam08241   1 LDVGCGTGLLTELLA-RLGARVTGVDISPEMLEL--AREKAPREGLTFVVGDaEDLPFPDNSFDLVLSSEVLHHV--EDP 75
                          90
                  ....*....|....*....
gi 1374243879 243 EDYFKAAYSFLADDGIFLL 261
Cdd:pfam08241  76 ERALREIARVLKPGGILII 94
PLN02244 PLN02244
tocopherol O-methyltransferase
162-237 5.85e-06

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 47.82  E-value: 5.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374243879 162 RLLDIGCGWGSFMMFAAEKYGVICDGLTLSKEQAALGQARADEKGL--PVNFILQDYRlyhpEQP-----YDRVVSIGMM 234
Cdd:PLN02244  121 RIVDVGCGIGGSSRYLARKYGANVKGITLSPVQAARANALAAAQGLsdKVSFQVADAL----NQPfedgqFDLVWSMESG 196

                  ...
gi 1374243879 235 EHV 237
Cdd:PLN02244  197 EHM 199
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
164-259 1.08e-05

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 43.90  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374243879 164 LDIGCGWGSFMMFAAEKY-GVICDGLTLSKEQAALGQARADEKGLPVNFILQDYRL---YHPEQPYDRVVSIGMMEHVgp 239
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALpGLEYTGLDISPAALEAARERLAALGLLNAVRVELFQLdlgELDPGSFDVVVASNVLHHL-- 78
                          90       100
                  ....*....|....*....|
gi 1374243879 240 ENYEDYFKAAYSFLADDGIF 259
Cdd:pfam08242  79 ADPRAVLRNIRRLLKPGGVL 98
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
157-261 6.24e-05

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 44.19  E-value: 6.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374243879 157 LQPGMRLLDIGCGWGSFMMFAAEKYGVICDGLTLSKEQAALGQARADEKGlPVNFILQD-YRLYHPEQPYDRVVSIGMME 235
Cdd:PTZ00098   50 LNENSKVLDIGSGLGGGCKYINEKYGAHVHGVDICEKMVNIAKLRNSDKN-KIEFEANDiLKKDFPENTFDMIYSRDAIL 128
                          90       100
                  ....*....|....*....|....*.
gi 1374243879 236 HVGPENYEDYFKAAYSFLADDGIFLL 261
Cdd:PTZ00098  129 HLSYADKKKLFEKCYKWLKPNGILLI 154
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
162-261 7.49e-05

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 43.56  E-value: 7.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374243879  162 RLLDIGCGWGSFMMFAAEKYGVI-CDGLTLSKEQAALGQARADEKGLP--VNFILQDYRLYHPEQPYDRVVSIGMMEHVg 238
Cdd:smart00828   2 RVLDFGCGYGSDLIDLAERHPHLqLHGYTISPEQAEVGRERIRALGLQgrIRIFYRDSAKDPFPDTYDLVFGFEVIHHI- 80
                           90       100
                   ....*....|....*....|...
gi 1374243879  239 pENYEDYFKAAYSFLADDGIFLL 261
Cdd:smart00828  81 -KDKMDLFSNISRHLKDGGHLVL 102
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
111-215 7.87e-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: 7.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374243879 111 HYDLGNDLFEAMLDpRmtytcaYWKDSddlksaqeakldlVCRKMGLQPGMRLLDIGCGWGSFMMFAAEKYGVI--CDGL 188
Cdd:PRK00216   23 KYDLMNDLLSFGLH-R------VWRRK-------------TIKWLGVRPGDKVLDLACGTGDLAIALAKAVGKTgeVVGL 82
                          90       100
                  ....*....|....*....|....*....
gi 1374243879 189 TLSKEQAALGQARADEKGL--PVNFILQD 215
Cdd:PRK00216   83 DFSEGMLAVGREKLRDLGLsgNVEFVQGD 111
PRK08317 PRK08317
hypothetical protein; Provisional
153-237 3.13e-04

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 41.85  E-value: 3.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374243879 153 RKMGLQPGMRLLDIGCGWGSFMMFAAEKYG----VIcdGLTLSKEQAALGQARADEKGLPVNFILQD-YRLYHPEQPYDR 227
Cdd:PRK08317   13 ELLAVQPGDRVLDVGCGPGNDARELARRVGpegrVV--GIDRSEAMLALAKERAAGLGPNVEFVRGDaDGLPFPDGSFDA 90
                          90
                  ....*....|
gi 1374243879 228 VVSIGMMEHV 237
Cdd:PRK08317   91 VRSDRVLQHL 100
PRK14103 PRK14103
trans-aconitate 2-methyltransferase; Provisional
149-230 1.31e-03

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 184509  Cd Length: 255  Bit Score: 40.06  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374243879 149 DLVCRkMGLQPGMRLLDIGCGWGSFMMFAAEKY-GVICDGLTLSKEQAAlgqaRADEKGlpVNFILQDYRLYHPEQPYDR 227
Cdd:PRK14103   20 DLLAR-VGAERARRVVDLGCGPGNLTRYLARRWpGAVIEALDSSPEMVA----AARERG--VDARTGDVRDWKPKPDTDV 92

                  ...
gi 1374243879 228 VVS 230
Cdd:PRK14103   93 VVS 95
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
159-261 1.92e-03

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 38.55  E-value: 1.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374243879 159 PGMRLLDIGCGWGSFMMFAAEKYGVICD--GLTLSKEQAALGQARADEKGLP-VNFILQDY----RLYHpEQPYDRVVSI 231
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEELGPNAEvvGIDISEEAIEKARENAQKLGFDnVEFEQGDIeelpELLE-DDKFDVVISN 81
                          90       100       110
                  ....*....|....*....|....*....|
gi 1374243879 232 GMMEHVGpeNYEDYFKAAYSFLADDGIFLL 261
Cdd:pfam13847  82 CVLNHIP--DPDKVLQEILRVLKPGGRLII 109
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
154-247 2.32e-03

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 39.73  E-value: 2.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374243879 154 KMGLQPGMRLLDIGCGWGSFMMFAAEKYGVICDGLTLSKEQAALGQARADEKGLPVNFILQD-YRLYHPEQPYDRVVSIG 232
Cdd:PLN02336  261 KLDLKPGQKVLDVGCGIGGGDFYMAENFDVHVVGIDLSVNMISFALERAIGRKCSVEFEVADcTKKTYPDNSFDVIYSRD 340
                          90
                  ....*....|....*..
gi 1374243879 233 MMEHV--GPENYEDYFK 247
Cdd:PLN02336  341 TILHIqdKPALFRSFFK 357
MetW pfam07021
Methionine biosynthesis protein MetW; This family consists of several bacterial and one ...
157-229 3.22e-03

Methionine biosynthesis protein MetW; This family consists of several bacterial and one archaeal methionine biosynthesis MetW proteins. Biosynthesis of methionine from homoserine in Pseudomonas putida takes place in three steps. The first step is the acylation of homoserine to yield an acyl-L-homoserine. This reaction is catalyzed by the products of the metXW genes and is equivalent to the first step in enterobacteria, gram-positive bacteria and fungi, except that in these microorganizms the reaction is catalyzed by a single polypeptide (the product of the metA gene in Escherichia coli and the met5 gene product in Neurospora crassa). In Pseudomonas putida, as in gram-positive bacteria and certain fungi, the second and third steps are a direct sulfhydrylation that converts the O-acyl-L-homoserine into homocysteine and further methylation to yield methionine. The latter reaction can be mediated by either of the two methionine synthetases present in the cells.


Pssm-ID: 399779  Cd Length: 193  Bit Score: 38.21  E-value: 3.22e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1374243879 157 LQPGMRLLDIGCGWGSFMMFAAEKYGVICDGLTLSKEqaalGQARADEKGLPVnfILQDYRL---YHPEQPYDRVV 229
Cdd:pfam07021  11 IPPGSRVLDLGCGDGTLLYLLKEEKGVDGYGIELDAA----GVAECVAKGLYV--IQGDLDEgleHFPDKSFDYVI 80
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
157-259 3.83e-03

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: 38.59  E-value: 3.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374243879 157 LQPGMRLLDIGCGWG--SFMMfAAEKYGVICDGLTLSKEQAALGQARADEKGLP--VNFI---LQDYRLYHPEQPYDRVV 229
Cdd:COG4123    35 VKKGGRVLDLGTGTGviALML-AQRSPGARITGVEIQPEAAELARRNVALNGLEdrITVIhgdLKEFAAELPPGSFDLVV 113
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1374243879 230 S-------------------IGMMEHVGPenYEDYFKAAYSFLADDGIF 259
Cdd:COG4123   114 SnppyfkagsgrkspdearaIARHEDALT--LEDLIRAAARLLKPGGRF 160
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
158-261 9.86e-03

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: 36.71  E-value: 9.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374243879 158 QPGMRLLDIGCGWGSFMMFAAEKYGVIcdGLTLS-KEQAALGQAR--ADEKGLP-VNFILQDYRLYHPEQPYDRVVS--- 230
Cdd:COG2813    48 PLGGRVLDLGCGYGVIGLALAKRNPEA--RVTLVdVNARAVELARanAAANGLEnVEVLWSDGLSGVPDGSFDLILSnpp 125
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1374243879 231 --IGMmeHVGPENYEDYFKAAYSFLADDGIFLL 261
Cdd:COG2813   126 fhAGR--AVDKEVAHALIADAARHLRPGGELWL 156
 
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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