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Conserved domains on  [gi|502861956|ref|WP_013096932|]
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MULTISPECIES: cyclopropane fatty acyl phospholipid synthase [Enterobacter]

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: 836.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956   1 MSSSCIEEVSVPDDNWSRIVSELLGRAGITINGSSPSDPQVKHPDFFKRVLREGSLGLGESYMDGWWDCERLDIFFASVL 80
Cdd:PRK11705   1 MSSSCIEEVSVPDDNWYRIANELLARAGITINGSRPWDIQVHNPRFFKRVLQEGSLGLGESYMDGWWDCDRLDEFFSRVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956  81 RAGLENQLPRNIKDTLRVASARLFNLQSKKRAWIVGKEHYDLGNDLFSRMLDPFMQYSCAYWKKATTLEEAQQDKLRLIS 160
Cdd:PRK11705  81 RAGLDEKLPHHLKDTLRILRARLFNLQSKKRAWIVGKEHYDLGNDLFEAMLDPRMQYSCGYWKDADTLEEAQEAKLDLIC 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956 161 EKLQLQPGMRVLDIGCGWGGLAYFMAKHYGVSVVGVTISAEQQKMARERCQGLDVDIRLQDYRDLNEQFDRIVSVGMFEH 240
Cdd:PRK11705 161 RKLQLKPGMRVLDIGCGWGGLARYAAEHYGVSVVGVTISAEQQKLAQERCAGLPVEIRLQDYRDLNGQFDRIVSVGMFEH 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956 241 VGPKNYDTYFEVVDRNLKPDGIFLLHTIGSKRTDNNVDPWINKYIFPNGCLPSVRQIANASESHFIMEDWHNFGADYDTT 320
Cdd:PRK11705 241 VGPKNYRTYFEVVRRCLKPDGLFLLHTIGSNKTDTNVDPWINKYIFPNGCLPSVRQIAQASEGLFVMEDWHNFGADYDRT 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502861956 321 LMAWHERFQQAWPEIADNYSERFKRMFSYYLNACAGAFRARDIQLWQVVFS-RGIEHGLRVPR 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: 836.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956   1 MSSSCIEEVSVPDDNWSRIVSELLGRAGITINGSSPSDPQVKHPDFFKRVLREGSLGLGESYMDGWWDCERLDIFFASVL 80
Cdd:PRK11705   1 MSSSCIEEVSVPDDNWYRIANELLARAGITINGSRPWDIQVHNPRFFKRVLQEGSLGLGESYMDGWWDCDRLDEFFSRVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956  81 RAGLENQLPRNIKDTLRVASARLFNLQSKKRAWIVGKEHYDLGNDLFSRMLDPFMQYSCAYWKKATTLEEAQQDKLRLIS 160
Cdd:PRK11705  81 RAGLDEKLPHHLKDTLRILRARLFNLQSKKRAWIVGKEHYDLGNDLFEAMLDPRMQYSCGYWKDADTLEEAQEAKLDLIC 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956 161 EKLQLQPGMRVLDIGCGWGGLAYFMAKHYGVSVVGVTISAEQQKMARERCQGLDVDIRLQDYRDLNEQFDRIVSVGMFEH 240
Cdd:PRK11705 161 RKLQLKPGMRVLDIGCGWGGLARYAAEHYGVSVVGVTISAEQQKLAQERCAGLPVEIRLQDYRDLNGQFDRIVSVGMFEH 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956 241 VGPKNYDTYFEVVDRNLKPDGIFLLHTIGSKRTDNNVDPWINKYIFPNGCLPSVRQIANASESHFIMEDWHNFGADYDTT 320
Cdd:PRK11705 241 VGPKNYRTYFEVVRRCLKPDGLFLLHTIGSNKTDTNVDPWINKYIFPNGCLPSVRQIAQASEGLFVMEDWHNFGADYDRT 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502861956 321 LMAWHERFQQAWPEIADNYSERFKRMFSYYLNACAGAFRARDIQLWQVVFS-RGIEHGLRVPR 382
Cdd:PRK11705 321 LMAWHENFEAAWPELADNYSERFYRMWRYYLLSCAGAFRARDIQLWQVVFSpRGVEGGYRVPR 383
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 108-368 3.32e-143

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: 407.48  E-value: 3.32e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956  108 SKKRAWIVGKEHYDLGNDLFSRMLDPFMQYSCAYWKKA-TTLEEAQQDKLRLISEKLQLQPGMRVLDIGCGWGGLAYFMA 186
Cdd:pfam02353   1 SKTRDAENIQAHYDLSNDFFALFLDPTMTYSCAYFERPdMTLEEAQQAKLDLILDKLGLKPGMTLLDIGCGWGGLMRRAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956  187 KHYGVSVVGVTISAEQQKMARERCQGLD----VDIRLQDYRDLNEQFDRIVSVGMFEHVGPKNYDTYFEVVDRNLKPDGI 262
Cdd:pfam02353  81 ERYDVNVVGLTLSKNQYKLARKRVAAEGlarkVEVLLQDYRDFDEPFDRIVSVGMFEHVGHENYDTFFKKLYNLLPPGGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956  263 FLLHTIGSKRTDNNVD-----PWINKYIFPNGCLPSVRQIA-NASESHFIMEDWHNFGADYDTTLMAWHERFQQAWPEIA 336
Cdd:pfam02353 161 MLLHTITGLHPDETSErglplKFIDKYIFPGGELPSISMIVeSSSEAGFTVEDVESLRPHYAKTLDLWAENLQANKDEAI 240

                         250       260       270
                  ....*....|....*....|....*....|..
gi 502861956  337 DNYSERFKRMFSYYLNACAGAFRARDIQLWQV 368
Cdd:pfam02353 241 ALQSEEFYRMWMLYLTGCAVAFRIGYIDVHQF 272
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 118-267 7.43e-82

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 247.15  E-value: 7.43e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956 118 EHYDLGNDLFSRMLDPFMQYSCAYWKK-ATTLEEAQQDKLRLISEKLQLQPGMRVLDIGCGWGGLAYFMAKHYGVSVVGV 196
Cdd:COG2230    1 HHYDLGNDFYRLFLDPTMTYSCAYFEDpDDTLEEAQEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGV 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502861956 197 TISAEQQKMARERCQ--GLD--VDIRLQDYRDL--NEQFDRIVSVGMFEHVGPKNYDTYFEVVDRNLKPDGIFLLHT 267
Cdd:COG2230   81 TLSPEQLEYARERAAeaGLAdrVEVRLADYRDLpaDGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLLHT 157
cyclopro_CfaB NF040703
C17 cyclopropane fatty acid synthase CfaB;
119-377 2.23e-74

C17 cyclopropane fatty acid synthase CfaB;


Pssm-ID: 468667 [Multi-domain]  Cd Length: 393  Bit Score: 236.05  E-value: 2.23e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956 119 HYDLGNDLFSRMLDPFMQYSCAYWKKAT-TLEEAQQDKLRLISEKLQLQPGMRVLDIGCGWGGLAYFMAKHYGVSVVGVT 197
Cdd:NF040703 110 HYDLSNDFYALWLDPDMVYSCAYFETGTeDLAQAQQAKLRHLCRKLRLQPGERLLDVGCGWGGLARFAAREFGVEVFGIT 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956 198 ISAEQQKMARERC--QGLD--VDIRLQDYRDL--NEQFDRIVSVGMFEHVGPKNYDTYFEVVDRNLKPDGIFLLHTIGSK 271
Cdd:NF040703 190 LSKEQLKLARERVaaEGLQdrVQLELLDYRDLpqDGRFDKVVSVGMFEHVGHANLPLYCQRLFGAVRPGGLVMNHGITAR 269

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956 272 RTD-----NNVDPWINKYIFPNGCLPSVRQI-ANASESHFIMEDWHNFGADYDTTLMAWHERFQQAWPEIADNYSERFKR 345
Cdd:NF040703 270 HTDgrpvgRGAGEFIGRYVFPHGELPHLATItASISEAGLEVVDVESLRLHYARTLEHWSARLEARLDEAARLVPERALR 349

                        250       260       270
                 ....*....|....*....|....*....|..
gi 502861956 346 MFSYYLNACAGAFRARDIQLWQVVFSRGIEHG 377
Cdd:NF040703 350 IWRLYLAGCAYGFARGWINLHQILAVKPLADG 381
mycolic_MTase NF040660
cyclopropane mycolic acid synthase family methyltransferase; Members of this family include ...
 119-359 1.72e-54

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: 181.12  E-value: 1.72e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956 119 HYDLGNDLFSRMLDPFMQYSCAYWKKA-TTLEEAQQDKLRLISEKLQLQPGMRVLDIGCGWGGLAYFMAKHYGVSVVGVT 197
Cdd:NF040660  11 HYDLSDDFFALFLDPTQTYSCAYFERDdMTLEEAQIAKIDLALGKLNLEPGMTLLDIGCGWGATMRRAVEKYDVNVVGLT 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956 198 ISAEQQKMARERCQGLDV----DIRLQDYRDLNEQFDRIVSVGMFEHVGPKNYDTYFEVVDRNLKPDGIFLLHTIGSKRT 273
Cdd:NF040660  91 LSKNQAAHVQQVLDEIDTprsrRVLLQGWEEFDEPVDRIVSIGAFEHFGHERYDDFFKRAYNILPADGRMLLHTITGLHR 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956 274 DNNVD-------------PWINKYIFPNGCLPSVRQIA-NASESHFIMEDWHNFGADYDTTLMAWHERFQQAWPEIADNY 339
Cdd:NF040660 171 KEMHErglpltmelarfiKFIVTEIFPGGRLPSIEMVVeHAEKAGFTVTRVQSLQPHYARTLDLWADALQAHKDEAIAIQ 250

                        250       260
                 ....*....|....*....|
gi 502861956 340 SERFKRMFSYYLNACAGAFR 359
Cdd:NF040660 251 SEEVYERYMKYLTGCAKLFR 270
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 170-266 6.30e-16

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: 72.85  E-value: 6.30e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956 170 RVLDIGCGWGGLAYFMAKHYGVSVVGVTISAEQQKMARERCQGL---DVDIRLQDYRDL----NEQFDRIVSVGMFEHVg 242
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALladNVEVLKGDAEELppeaDESFDVIISDPPLHHL- 79

                         90       100
                 ....*....|....*....|....
gi 502861956 243 PKNYDTYFEVVDRNLKPDGIFLLH 266
Cdd:cd02440   80 VEDLARFLEEARRLLKPGGVLVLT 103
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
170-265 2.09e-08

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 54.34  E-value: 2.09e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956   170 RVLDIGCGWG-GLAYFMAKHYGVSVVGVTISAEQQKMARERCQGLDVDIRLQ-DYRDLNEQ-----FDRIVSVGMFEHVg 242
Cdd:smart00828   2 RVLDFGCGYGsDLIDLAERHPHLQLHGYTISPEQAEVGRERIRALGLQGRIRiFYRDSAKDpfpdtYDLVFGFEVIHHI- 80

                           90       100
                   ....*....|....*....|...
gi 502861956   243 pKNYDTYFEVVDRNLKPDGIFLL 265
Cdd:smart00828  81 -KDKMDLFSNISRHLKDGGHLVL 102
metW TIGR02081
methionine biosynthesis protein MetW; This protein is found alongside MetX, of the enzyme that ...
 167-233 1.42e-03

methionine biosynthesis protein MetW; This protein is found alongside MetX, of the enzyme that acylates homoserine as a first step toward methionine biosynthesis, in many species. It appears to act in methionine biosynthesis but is not fully characterized. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 273958  Cd Length: 194  Bit Score: 39.27  E-value: 1.42e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502861956  167 PGMRVLDIGCGWGGLAYFMAKHYGVSVVGVTISAEQQKMARERcqGLDV-----DIRLQDYRDlnEQFDRIV 233
Cdd:TIGR02081  13 PGSRVLDLGCGDGELLALLRDEKQVRGYGIEIDQDGVLACVAR--GVNViqgdlDEGLEAFPD--KSFDYVI 80
 
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: 836.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956   1 MSSSCIEEVSVPDDNWSRIVSELLGRAGITINGSSPSDPQVKHPDFFKRVLREGSLGLGESYMDGWWDCERLDIFFASVL 80
Cdd:PRK11705   1 MSSSCIEEVSVPDDNWYRIANELLARAGITINGSRPWDIQVHNPRFFKRVLQEGSLGLGESYMDGWWDCDRLDEFFSRVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956  81 RAGLENQLPRNIKDTLRVASARLFNLQSKKRAWIVGKEHYDLGNDLFSRMLDPFMQYSCAYWKKATTLEEAQQDKLRLIS 160
Cdd:PRK11705  81 RAGLDEKLPHHLKDTLRILRARLFNLQSKKRAWIVGKEHYDLGNDLFEAMLDPRMQYSCGYWKDADTLEEAQEAKLDLIC 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956 161 EKLQLQPGMRVLDIGCGWGGLAYFMAKHYGVSVVGVTISAEQQKMARERCQGLDVDIRLQDYRDLNEQFDRIVSVGMFEH 240
Cdd:PRK11705 161 RKLQLKPGMRVLDIGCGWGGLARYAAEHYGVSVVGVTISAEQQKLAQERCAGLPVEIRLQDYRDLNGQFDRIVSVGMFEH 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956 241 VGPKNYDTYFEVVDRNLKPDGIFLLHTIGSKRTDNNVDPWINKYIFPNGCLPSVRQIANASESHFIMEDWHNFGADYDTT 320
Cdd:PRK11705 241 VGPKNYRTYFEVVRRCLKPDGLFLLHTIGSNKTDTNVDPWINKYIFPNGCLPSVRQIAQASEGLFVMEDWHNFGADYDRT 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502861956 321 LMAWHERFQQAWPEIADNYSERFKRMFSYYLNACAGAFRARDIQLWQVVFS-RGIEHGLRVPR 382
Cdd:PRK11705 321 LMAWHENFEAAWPELADNYSERFYRMWRYYLLSCAGAFRARDIQLWQVVFSpRGVEGGYRVPR 383
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 108-368 3.32e-143

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: 407.48  E-value: 3.32e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956  108 SKKRAWIVGKEHYDLGNDLFSRMLDPFMQYSCAYWKKA-TTLEEAQQDKLRLISEKLQLQPGMRVLDIGCGWGGLAYFMA 186
Cdd:pfam02353   1 SKTRDAENIQAHYDLSNDFFALFLDPTMTYSCAYFERPdMTLEEAQQAKLDLILDKLGLKPGMTLLDIGCGWGGLMRRAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956  187 KHYGVSVVGVTISAEQQKMARERCQGLD----VDIRLQDYRDLNEQFDRIVSVGMFEHVGPKNYDTYFEVVDRNLKPDGI 262
Cdd:pfam02353  81 ERYDVNVVGLTLSKNQYKLARKRVAAEGlarkVEVLLQDYRDFDEPFDRIVSVGMFEHVGHENYDTFFKKLYNLLPPGGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956  263 FLLHTIGSKRTDNNVD-----PWINKYIFPNGCLPSVRQIA-NASESHFIMEDWHNFGADYDTTLMAWHERFQQAWPEIA 336
Cdd:pfam02353 161 MLLHTITGLHPDETSErglplKFIDKYIFPGGELPSISMIVeSSSEAGFTVEDVESLRPHYAKTLDLWAENLQANKDEAI 240

                         250       260       270
                  ....*....|....*....|....*....|..
gi 502861956  337 DNYSERFKRMFSYYLNACAGAFRARDIQLWQV 368
Cdd:pfam02353 241 ALQSEEFYRMWMLYLTGCAVAFRIGYIDVHQF 272
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 118-267 7.43e-82

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 247.15  E-value: 7.43e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956 118 EHYDLGNDLFSRMLDPFMQYSCAYWKK-ATTLEEAQQDKLRLISEKLQLQPGMRVLDIGCGWGGLAYFMAKHYGVSVVGV 196
Cdd:COG2230    1 HHYDLGNDFYRLFLDPTMTYSCAYFEDpDDTLEEAQEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGV 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502861956 197 TISAEQQKMARERCQ--GLD--VDIRLQDYRDL--NEQFDRIVSVGMFEHVGPKNYDTYFEVVDRNLKPDGIFLLHT 267
Cdd:COG2230   81 TLSPEQLEYARERAAeaGLAdrVEVRLADYRDLpaDGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLLHT 157
cyclopro_CfaB NF040703
C17 cyclopropane fatty acid synthase CfaB;
119-377 2.23e-74

C17 cyclopropane fatty acid synthase CfaB;


Pssm-ID: 468667 [Multi-domain]  Cd Length: 393  Bit Score: 236.05  E-value: 2.23e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956 119 HYDLGNDLFSRMLDPFMQYSCAYWKKAT-TLEEAQQDKLRLISEKLQLQPGMRVLDIGCGWGGLAYFMAKHYGVSVVGVT 197
Cdd:NF040703 110 HYDLSNDFYALWLDPDMVYSCAYFETGTeDLAQAQQAKLRHLCRKLRLQPGERLLDVGCGWGGLARFAAREFGVEVFGIT 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956 198 ISAEQQKMARERC--QGLD--VDIRLQDYRDL--NEQFDRIVSVGMFEHVGPKNYDTYFEVVDRNLKPDGIFLLHTIGSK 271
Cdd:NF040703 190 LSKEQLKLARERVaaEGLQdrVQLELLDYRDLpqDGRFDKVVSVGMFEHVGHANLPLYCQRLFGAVRPGGLVMNHGITAR 269

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956 272 RTD-----NNVDPWINKYIFPNGCLPSVRQI-ANASESHFIMEDWHNFGADYDTTLMAWHERFQQAWPEIADNYSERFKR 345
Cdd:NF040703 270 HTDgrpvgRGAGEFIGRYVFPHGELPHLATItASISEAGLEVVDVESLRLHYARTLEHWSARLEARLDEAARLVPERALR 349

                        250       260       270
                 ....*....|....*....|....*....|..
gi 502861956 346 MFSYYLNACAGAFRARDIQLWQVVFSRGIEHG 377
Cdd:NF040703 350 IWRLYLAGCAYGFARGWINLHQILAVKPLADG 381
mycolic_MTase NF040660
cyclopropane mycolic acid synthase family methyltransferase; Members of this family include ...
 119-359 1.72e-54

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: 181.12  E-value: 1.72e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956 119 HYDLGNDLFSRMLDPFMQYSCAYWKKA-TTLEEAQQDKLRLISEKLQLQPGMRVLDIGCGWGGLAYFMAKHYGVSVVGVT 197
Cdd:NF040660  11 HYDLSDDFFALFLDPTQTYSCAYFERDdMTLEEAQIAKIDLALGKLNLEPGMTLLDIGCGWGATMRRAVEKYDVNVVGLT 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956 198 ISAEQQKMARERCQGLDV----DIRLQDYRDLNEQFDRIVSVGMFEHVGPKNYDTYFEVVDRNLKPDGIFLLHTIGSKRT 273
Cdd:NF040660  91 LSKNQAAHVQQVLDEIDTprsrRVLLQGWEEFDEPVDRIVSIGAFEHFGHERYDDFFKRAYNILPADGRMLLHTITGLHR 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956 274 DNNVD-------------PWINKYIFPNGCLPSVRQIA-NASESHFIMEDWHNFGADYDTTLMAWHERFQQAWPEIADNY 339
Cdd:NF040660 171 KEMHErglpltmelarfiKFIVTEIFPGGRLPSIEMVVeHAEKAGFTVTRVQSLQPHYARTLDLWADALQAHKDEAIAIQ 250

                        250       260
                 ....*....|....*....|
gi 502861956 340 SERFKRMFSYYLNACAGAFR 359
Cdd:NF040660 251 SEEVYERYMKYLTGCAKLFR 270
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 171-261 1.35e-25

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 99.18  E-value: 1.35e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956  171 VLDIGCGWGGLAYFMAKHYGVSVVGVTISAEQQKMARERC--QGLDVDIRLQDYRDL---NEQFDRIVSVGMFEHVGPKN 245
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAaeAGLNVEFVQGDAEDLpfpDGSFDLVVSSGVLHHLPDPD 80

                          90
                  ....*....|....*.
gi 502861956  246 YDTYFEVVDRNLKPDG 261
Cdd:pfam13649  81 LEAALREIARVLKPGG 96
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 165-268 1.33e-23

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: 94.70  E-value: 1.33e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956 165 LQPGMRVLDIGCGWGGLAYFMAKHyGVSVVGVTISAEQQKMARERCQGLDVDIRLQDYRDL---NEQFDRIVSVGMFEHV 241
Cdd:COG2227   22 LPAGGRVLDVGCGTGRLALALARR-GADVTGVDISPEALEIARERAAELNVDFVQGDLEDLpleDGSFDLVICSEVLEHL 100

                         90       100
                 ....*....|....*....|....*..
gi 502861956 242 gpKNYDTYFEVVDRNLKPDGIFLLHTI 268
Cdd:COG2227  101 --PDPAALLRELARLLKPGGLLLLSTP 125
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 154-269 1.14e-20

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: 87.36  E-value: 1.14e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956 154 DKLRLISEKLQLQPGMRVLDIGCGWGGLAYFMAKHyGVSVVGVTISAEQQKMARERCQ--GLDVDIRLQDYRDL---NEQ 228
Cdd:COG2226    9 DGREALLAALGLRPGARVLDLGCGTGRLALALAER-GARVTGVDISPEMLELARERAAeaGLNVEFVVGDAEDLpfpDGS 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 502861956 229 FDRIVSVGMFEHVgpKNYDTYFEVVDRNLKPDGIFLLHTIG 269
Cdd:COG2226   88 FDLVISSFVLHHL--PDPERALAEIARVLKPGGRLVVVDFS 126
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 156-265 1.20e-19

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 86.12  E-value: 1.20e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956 156 LRLISEKLQLQPGMRVLDIGCGWGGLAYFMAKHYGVSVVGVTISAEQQKMARERCQGLD---VDIRLQDYRDLN----EQ 228
Cdd:COG0500   15 AALLALLERLPKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAGlgnVEFLVADLAELDplpaES 94

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 502861956 229 FDRIVSVGMFEHVGPKNYDTYFEVVDRNLKPDGIFLL 265
Cdd:COG0500   95 FDLVVAFGVLHHLPPEEREALLRELARALKPGGVLLL 131
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 172-265 1.82e-16

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 73.85  E-value: 1.82e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956  172 LDIGCGWGGLAYFMAKhYGVSVVGVTISAEQQKMARERCQGLDVDIRLQDYRDL---NEQFDRIVSVGMFEHVgpKNYDT 248
Cdd:pfam08241   1 LDVGCGTGLLTELLAR-LGARVTGVDISPEMLELAREKAPREGLTFVVGDAEDLpfpDNSFDLVLSSEVLHHV--EDPER 77

                          90
                  ....*....|....*..
gi 502861956  249 YFEVVDRNLKPDGIFLL 265
Cdd:pfam08241  78 ALREIARVLKPGGILII 94
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 170-266 6.30e-16

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: 72.85  E-value: 6.30e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956 170 RVLDIGCGWGGLAYFMAKHYGVSVVGVTISAEQQKMARERCQGL---DVDIRLQDYRDL----NEQFDRIVSVGMFEHVg 242
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALladNVEVLKGDAEELppeaDESFDVIISDPPLHHL- 79

                         90       100
                 ....*....|....*....|....
gi 502861956 243 PKNYDTYFEVVDRNLKPDGIFLLH 266
Cdd:cd02440   80 VEDLARFLEEARRLLKPGGVLVLT 103
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
150-265 3.82e-15

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 72.72  E-value: 3.82e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956 150 EAQQDKLRLISEKLQLQPGMRVLDIGCGWGGLAYFMAKHyGVSVVGVTISAEQQKMARERcqGLDVDIRLQDYRDL---N 226
Cdd:COG4976   29 EAPALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPR-GYRLTGVDLSEEMLAKAREK--GVYDRLLVADLADLaepD 105

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 502861956 227 EQFDRIVSVGMFEHVGpkNYDTYFEVVDRNLKPDGIFLL 265
Cdd:COG4976  106 GRFDLIVAADVLTYLG--DLAAVFAGVARALKPGGLFIF 142
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
167-265 2.75e-14

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 67.93  E-value: 2.75e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956 167 PGMRVLDIGCGWGGLAYFMAKHY-GVSVVGVTISAEQQKMARERCQglDVDIRLQDYRDL--NEQFDRIVSVGMFEHVgp 243
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALLAERFpGARVTGVDLSPEMLARARARLP--NVRFVVADLRDLdpPEPFDLVVSNAALHWL-- 76

                         90       100
                 ....*....|....*....|..
gi 502861956 244 KNYDTYFEVVDRNLKPDGIFLL 265
Cdd:COG4106   77 PDHAALLARLAAALAPGGVLAV 98
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 119-264 3.34e-10

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 59.78  E-value: 3.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956 119 HYDLGNDLFSRMLDpfmqyscAYWKKATtleeaqqdklrliSEKLQLQPGMRVLDIGCGWGGLAYFMAKHYGV--SVVGV 196
Cdd:PRK00216  23 KYDLMNDLLSFGLH-------RVWRRKT-------------IKWLGVRPGDKVLDLACGTGDLAIALAKAVGKtgEVVGL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956 197 TISAEQQKMARERCQGLDVDIRLQ----DYRDL---NEQFDrIVSVGmFehvGPKNydtyfeVVDRN---------LKPD 260
Cdd:PRK00216  83 DFSEGMLAVGREKLRDLGLSGNVEfvqgDAEALpfpDNSFD-AVTIA-F---GLRN------VPDIDkalremyrvLKPG 151


                 ....
gi 502861956 261 GIFL 264
Cdd:PRK00216 152 GRLV 155
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 167-300 1.45e-09

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 56.28  E-value: 1.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956  167 PGMRVLDIGCGWGGLAYFMAKHyGVSVVGVTISAEQQKMARERCQGLDVDIrlQDYRDLNEQFDRIVSVGMFEHVgpKNY 246
Cdd:pfam13489  22 SPGRVLDFGCGTGIFLRLLRAQ-GFSVTGVDPSPIAIERALLNVRFDQFDE--QEAAVPAGKFDVIVAREVLEHV--PDP 96

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 502861956  247 DTYFEVVDRNLKPDGIFLLHTIGSKRTDNNVDPWiNKYIFPNG---CLPSVRQIANA 300
Cdd:pfam13489  97 PALLRQIAALLKPGGLLLLSTPLASDEADRLLLE-WPYLRPRNghiSLFSARSLKRL 152
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 161-265 1.68e-09

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 58.99  E-value: 1.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956 161 EKLQLQPGMRVLDIGCGWGGLAYFMAKHYGVSVVGVTISAEQQKMARERCQGLD-------VDIRLQDYRDlnEQFDRIV 233
Cdd:PLN02336 260 DKLDLKPGQKVLDVGCGIGGGDFYMAENFDVHVVGIDLSVNMISFALERAIGRKcsvefevADCTKKTYPD--NSFDVIY 337

                         90       100       110
                 ....*....|....*....|....*....|....
gi 502861956 234 SVGMFEHV--GPKNYDTYFevvdRNLKPDGIFLL 265
Cdd:PLN02336 338 SRDTILHIqdKPALFRSFF----KWLKPGGKVLI 367
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 167-272 2.38e-09

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 55.50  E-value: 2.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956  167 PGMRVLDIGCGWGGLAYFMAKHYG--VSVVGVTISAEQQKMARERCQ--GLD-VDIRLQDYRDL-----NEQFDRIVSVG 236
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEELGpnAEVVGIDISEEAIEKARENAQklGFDnVEFEQGDIEELpelleDDKFDVVISNC 82

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 502861956  237 MFEHVGpkNYDTYFEVVDRNLKPDGIFLLHTIGSKR 272
Cdd:pfam13847  83 VLNHIP--DPDKVLQEILRVLKPGGRLIISDPDSLA 116
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
 159-265 5.91e-09

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 56.52  E-value: 5.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956 159 ISEKLQLQPGMRVLDIGCGWGGLAYFMAKHYGVSVVGVTISAEQQKMARERCQGLD------VDIRLQDYRDLNeqFDRI 232
Cdd:PTZ00098  44 ILSDIELNENSKVLDIGSGLGGGCKYINEKYGAHVHGVDICEKMVNIAKLRNSDKNkiefeaNDILKKDFPENT--FDMI 121

                         90       100       110
                 ....*....|....*....|....*....|...
gi 502861956 233 VSVGMFEHVGPKNYDTYFEVVDRNLKPDGIFLL 265
Cdd:PTZ00098 122 YSRDAILHLSYADKKKLFEKCYKWLKPNGILLI 154
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 172-263 1.03e-08

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 52.37  E-value: 1.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956  172 LDIGCGWGGLAYFMAKHY-GVSVVGVTISAEQQKMARER----CQGLDVDIRLQDYRDLNE---QFDRIVSVGMFEHVGP 243
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALpGLEYTGLDISPAALEAARERlaalGLLNAVRVELFQLDLGELdpgSFDVVVASNVLHHLAD 80

                          90       100
                  ....*....|....*....|
gi 502861956  244 KnyDTYFEVVDRNLKPDGIF 263
Cdd:pfam08242  81 P--RAVLRNIRRLLKPGGVL 98
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
170-265 2.09e-08

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 54.34  E-value: 2.09e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956   170 RVLDIGCGWG-GLAYFMAKHYGVSVVGVTISAEQQKMARERCQGLDVDIRLQ-DYRDLNEQ-----FDRIVSVGMFEHVg 242
Cdd:smart00828   2 RVLDFGCGYGsDLIDLAERHPHLQLHGYTISPEQAEVGRERIRALGLQGRIRiFYRDSAKDpfpdtYDLVFGFEVIHHI- 80

                           90       100
                   ....*....|....*....|...
gi 502861956   243 pKNYDTYFEVVDRNLKPDGIFLL 265
Cdd:smart00828  81 -KDKMDLFSNISRHLKDGGHLVL 102
PRK08317 PRK08317
hypothetical protein; Provisional
 161-241 4.39e-08

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 53.40  E-value: 4.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956 161 EKLQLQPGMRVLDIGCGWGGLAYFMAKHYGVS--VVGVTISAEQQKMARERC--QGLDVDIRLQDYRDL---NEQFDRIV 233
Cdd:PRK08317  13 ELLAVQPGDRVLDVGCGPGNDARELARRVGPEgrVVGIDRSEAMLALAKERAagLGPNVEFVRGDADGLpfpDGSFDAVR 92


                 ....*...
gi 502861956 234 SVGMFEHV 241
Cdd:PRK08317  93 SDRVLQHL 100
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 155-265 3.23e-07

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: 49.89  E-value: 3.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956  155 KLRLISEKLQ-LQPGMRVLDIGCGWGGLAYFMAKHYGVSVVGVTI--SAEQQKMARERCQGLDVDIR-LQDYRDLNEQFD 230
Cdd:pfam01728   8 KLLEIDEKFGlLKPGKTVLDLGAAPGGWSQVALQRGAGKVVGVDLgpMQLWKPRNDPGVTFIQGDIRdPETLDLLEELLG 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 502861956  231 RIVSV----GMFEHVGPKNYDTY---------FEVVDRNLKPDGIFLL 265
Cdd:pfam01728  88 RKVDLvlsdGSPFISGNKVLDHLrsldlvkaaLEVALELLRKGGNFVC 135
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
166-264 7.29e-07

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 49.65  E-value: 7.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956 166 QPGMRVLDIGCGWGGLAYFMAKHYGVSVVGVTISAEQQKMARE--RCQGLDVDIRL-----QDYrDLNEQFDRIVS---- 234
Cdd:COG4076   34 KPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNPDIAAVARRiiAANGLSDRITVinadaTDL-DLPEKADVIISemld 112

                         90       100       110
                 ....*....|....*....|....*....|.
gi 502861956 235 VGMF-EHVGPknydTYFEVVDRNLKPDGIFL 264
Cdd:COG4076  113 TALLdEGQVP----ILNHARKRLLKPGGRII 139
PLN02244 PLN02244
tocopherol O-methyltransferase
 152-244 1.97e-06

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 49.36  E-value: 1.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956 152 QQDKLRLISEKL---------QLQPgMRVLDIGCGWGGLAYFMAKHYGVSVVGVTISAEQQKMARE--RCQGLDVDIRLQ 220
Cdd:PLN02244  95 RQAQIRMIEESLawagvpdddEKRP-KRIVDVGCGIGGSSRYLARKYGANVKGITLSPVQAARANAlaAAQGLSDKVSFQ 173

                         90       100
                 ....*....|....*....|....*....
gi 502861956 221 DYRDLNE-----QFDRIVSVGMFEHVGPK 244
Cdd:PLN02244 174 VADALNQpfedgQFDLVWSMESGEHMPDK 202
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 158-241 2.91e-06

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


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 47.39  E-value: 2.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956 158 LISEKLQLQPGMRVLDIGCGwGG-----LAYfMAKHygvsVVGVTISAEQQKMARERCQGLDVD-IRLqDYRDLNE---- 227
Cdd:COG2518   57 RMLEALDLKPGDRVLEIGTG-SGyqaavLAR-LAGR----VYSVERDPELAERARERLAALGYDnVTV-RVGDGALgwpe 129

                         90
                 ....*....|....*.
gi 502861956 228 --QFDRIVSVGMFEHV 241
Cdd:COG2518  130 haPFDRIIVTAAAPEV 145
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 157-234 5.45e-06

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: 46.72  E-value: 5.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956 157 RLISEKLQLQPGMRVLDIGCGWGGLAYFMAKHYGV-SVVGVTISAeqqkMARERCQ------GLD-VDIRLQDYRD--LN 226
Cdd:COG2813   39 RLLLEHLPEPLGGRVLDLGCGYGVIGLALAKRNPEaRVTLVDVNA----RAVELARanaaanGLEnVEVLWSDGLSgvPD 114


                 ....*...
gi 502861956 227 EQFDRIVS 234
Cdd:COG2813  115 GSFDLILS 122
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
161-216 6.21e-06

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


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 46.59  E-value: 6.21e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 502861956  161 EKLQLQPGMRVLDIGCGWGGLAYFMAKHYGVS--VVGVTISAEQQKMARERCQGLDVD 216
Cdd:pfam01135  67 ELLELKPGMRVLEIGSGSGYLTACFARMVGEVgrVVSIEHIPELVEIARRNLEKLGLE 124
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 165-263 1.60e-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: 45.91  E-value: 1.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956 165 LQPGMRVLDIGCGWGGLAYFMAKHY-GVSVVGVTISAEQQKMARERCQ--GLD--VDIRLQDYRDL-----NEQFDRIVS 234
Cdd:COG4123   35 VKKGGRVLDLGTGTGVIALMLAQRSpGARITGVEIQPEAAELARRNVAlnGLEdrITVIHGDLKEFaaelpPGSFDLVVS 114

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 502861956 235 ------VGMFE-----------HVGPKNYDTYFEVVDRNLKPDGIF 263
Cdd:COG4123  115 nppyfkAGSGRkspdearaiarHEDALTLEDLIRAAARLLKPGGRF 160
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
170-270 1.70e-05

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


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 45.20  E-value: 1.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956 170 RVLDIGCGWGGLAYFMAKHYGVS-VVGVTISAEQQKMARE----RCQGLD---VDIRLQD---Y-RDLNEQFDrIVSVGM 237
Cdd:COG0421   40 RVLIIGGGDGGLARELLKHPPVErVDVVEIDPEVVELAREyfplLAPAFDdprLRVVIGDgraFlREAEESYD-VIIVDL 118

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 502861956 238 FEHVGP-KNYDT--YFEVVDRNLKPDGIFLLHTIGS 270
Cdd:COG0421  119 TDPVGPaEGLFTreFYEDCRRALKPGGVLVVNLGSP 154
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 157-265 2.11e-05

Methyltransferase small domain; This domain is found in ribosomal RNA small subunit methyltransferase C as well as other methyltransferases.


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 44.50  E-value: 2.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956  157 RLISEKLQLQPGMRVLDIGCGWGGLAYFMAKHYG-VSVVGVTISAEQQKMARE--RCQGLD-VDIRLQD-YRDL-NEQFD 230
Cdd:pfam05175  21 RLLLEHLPKDLSGKVLDLGCGAGVLGAALAKESPdAELTMVDINARALESAREnlAANGLEnGEVVASDvYSGVeDGKFD 100

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 502861956  231 RIVSVGMFeHVGPK-NYDT---YFEVVDRNLKPDGIFLL 265
Cdd:pfam05175 101 LIISNPPF-HAGLAtTYNVaqrFIADAKRHLRPGGELWI 138
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 162-264 3.84e-05

tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 N-methylase Trm61 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442009 [Multi-domain]  Cd Length: 249  Bit Score: 44.77  E-value: 3.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956 162 KLQLQPGMRVLDIGCGWGGLAYFMAKHYGVS--VVGVTISAEQQKMARERCQ--GLD--VDIRLQDYRDLNEQ--FDRIV 233
Cdd:COG2519   86 RLDIFPGARVLEAGTGSGALTLALARAVGPEgkVYSYERREDFAEIARKNLErfGLPdnVELKLGDIREGIDEgdVDAVF 165

                         90       100       110
                 ....*....|....*....|....*....|.
gi 502861956 234 sVGMFEHVgpknydTYFEVVDRNLKPDGIFL 264
Cdd:COG2519  166 -LDMPDPW------EALEAVAKALKPGGVLV 189
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 167-265 7.34e-05

Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443104 [Multi-domain]  Cd Length: 216  Bit Score: 43.33  E-value: 7.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956 167 PGMRVLDIGCGWGGLAYFMAKHYGVSVVGVTISAEQQKMARERCQ--GLDVDIRLQDYRD--LNEQFDRIVsVG------ 236
Cdd:COG3897   70 AGKRVLELGCGLGLVGIAAAKAGAADVTATDYDPEALAALRLNAAlnGVAITTRLGDWRDppAAGGFDLIL-GGdvlyer 148

                         90       100       110
                 ....*....|....*....|....*....|
gi 502861956 237 -MFEHVGPknydtyfeVVDRNLKPDGIFLL 265
Cdd:COG3897  149 dLAEPLLP--------FLDRLAAPGGEVLI 170
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
 156-269 2.08e-04

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: 42.83  E-value: 2.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956 156 LRLISEKLQLQPGMRVLDIGCGwGGLAYF---MAKHYGVSVVGVTISAEQQKMARErcQGLDVDIrlqDYRDLN------ 226
Cdd:COG0604  128 WQALFDRGRLKPGETVLVHGAA-GGVGSAavqLAKALGARVIATASSPEKAELLRA--LGADHVI---DYREEDfaervr 201

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 502861956 227 -----EQFDRIvsvgmFEHVGPKNYDTYFEVvdrnLKPDGIFLlhTIG 269
Cdd:COG0604  202 altggRGVDVV-----LDTVGGDTLARSLRA----LAPGGRLV--SIG 238
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 167-233 2.88e-04

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 41.75  E-value: 2.88e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502861956 167 PGMRVLDIGCGWGGLAYFMAKHyGVSVVGVTISAEQQKMARERCQ--GLD--VDIRLQDYRDLNEQFDRIV 233
Cdd:PRK07580  63 TGLRILDAGCGVGSLSIPLARR-GAKVVASDISPQMVEEARERAPeaGLAgnITFEVGDLESLLGRFDTVV 132
HsdM COG0286
Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];
157-268 4.20e-04

Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];


Pssm-ID: 440055 [Multi-domain]  Cd Length: 243  Bit Score: 41.33  E-value: 4.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956 157 RLISEKLQLQPGMRVLDIGCGWGGL---AY-FMAKHYG-----VSVVGVTISAEQQKMARERC--QGL-DVDIRLQDY-- 222
Cdd:COG0286   33 RLMVELLDPKPGETVYDPACGSGGFlveAAeYLKEHGGderkkLSLYGQEINPTTYRLAKMNLllHGIgDPNIELGDTls 112

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 502861956 223 --RDLNEQFDRIVS----VGMFEHVGPKN--YDTYFEVVDRNLKPDGIFLLHTI 268
Cdd:COG0286  113 ndGDELEKFDVVLAnppfGGKWKKEELKDdlLGRFGYGLPPKSNADLLFLQHIL 166
pcm PRK00312
protein-L-isoaspartate(D-aspartate) O-methyltransferase;
158-262 8.78e-04

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


Pssm-ID: 178974 [Multi-domain]  Cd Length: 212  Bit Score: 40.19  E-value: 8.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956 158 LISEKLQLQPGMRVLDIGCGWGGLAYFMAKhygvsVVGVTISAEQ----QKMARERCQGLD---VDIRLQD-YRDLNEQ- 228
Cdd:PRK00312  69 RMTELLELKPGDRVLEIGTGSGYQAAVLAH-----LVRRVFSVERiktlQWEAKRRLKQLGlhnVSVRHGDgWKGWPAYa 143

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 502861956 229 -FDRIVSVGMFEHVgPKNydtYFEvvdrNLKPDGI 262
Cdd:PRK00312 144 pFDRILVTAAAPEI-PRA---LLE----QLKEGGI 170
RsmB COG0144
16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and ...
 158-232 9.26e-04

16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and biogenesis]; 16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 439914 [Multi-domain]  Cd Length: 441  Bit Score: 41.15  E-value: 9.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956 158 LISEKLQLQPGMRVLDIGCGWGG----LAYFMAKhyGVSVVGVTISAEQQKMARERCQ--GLD-VDIRLQDYRD----LN 226
Cdd:COG0144  240 LVALLLDPKPGERVLDLCAAPGGktlhLAELMGN--KGRVVAVDISEHRLKRLRENLArlGLSnVEVVVADAREllewLP 317


                 ....*.
gi 502861956 227 EQFDRI 232
Cdd:COG0144  318 GKFDRV 323
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 170-266 9.95e-04

tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; tRNA 5-hydroxyU34 O-methylase TrmR/YrrM is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443298  Cd Length: 173  Bit Score: 39.78  E-value: 9.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956 170 RVLDIGCGWGGLAYFMAKHY--GVSVVGVTISAEQQKMARERCQ--GLD--VDIRLQDYRD-----LNEQFDRIVSVGmf 238
Cdd:COG4122   19 RILEIGTGTGYSTLWLARALpdDGRLTTIEIDPERAAIARENFAraGLAdrIRLILGDALEvlprlADGPFDLVFIDA-- 96

                         90       100
                 ....*....|....*....|....*...
gi 502861956 239 ehvGPKNYDTYFEVVDRNLKPDGIFLLH 266
Cdd:COG4122   97 ---DKSNYPDYLELALPLLRPGGLIVAD 121
MDR1 cd08267
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 156-264 1.07e-03

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176228 [Multi-domain]  Cd Length: 319  Bit Score: 40.66  E-value: 1.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956 156 LRLISEKLQLQPGMRVLDIGCGwGGLAYF---MAKHYGVSVVGVTiSAEQQKMARErcQGLDVDIrlqDYRDLN------ 226
Cdd:cd08267  132 LQALRDAGKVKPGQRVLINGAS-GGVGTFavqIAKALGAHVTGVC-STRNAELVRS--LGADEVI---DYTTEDfvalta 204

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 502861956 227 --EQFDRIvsvgmFEHVGPKNYDTYFEVvdRNLKPDGIFL 264
Cdd:cd08267  205 ggEKYDVI-----FDAVGNSPFSLYRAS--LALKPGGRYV 237
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
 162-208 1.08e-03

D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport and metabolism];


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 40.48  E-value: 1.08e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 502861956 162 KLQLQPGMRVLDIGCgwGGLAYF---MAKHYGVSVVGVTISAEQQKMARE 208
Cdd:COG1064  157 RAGVGPGDRVAVIGA--GGLGHLavqIAKALGAEVIAVDRSPEKLELARE 204
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 161-265 1.24e-03

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 40.15  E-value: 1.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956 161 EKLQLQPGMRVLDIGCGWG--GLAyfMAKHY-GVSVVGVTISAEQQKMARE---RCQGLDVDIRLQDYRD--LNEQFDRI 232
Cdd:PRK09328 102 EALLLKEPLRVLDLGTGSGaiALA--LAKERpDAEVTAVDISPEALAVARRnakHGLGARVEFLQGDWFEplPGGRFDLI 179

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 502861956 233 VS----------------VGMFE-HV----GPKNYDTYFEVVD---RNLKPDGIFLL 265
Cdd:PRK09328 180 VSnppyipeadihllqpeVRDHEpHLalfgGEDGLDFYRRIIEqapRYLKPGGWLLL 236
metW TIGR02081
methionine biosynthesis protein MetW; This protein is found alongside MetX, of the enzyme that ...
 167-233 1.42e-03

methionine biosynthesis protein MetW; This protein is found alongside MetX, of the enzyme that acylates homoserine as a first step toward methionine biosynthesis, in many species. It appears to act in methionine biosynthesis but is not fully characterized. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 273958  Cd Length: 194  Bit Score: 39.27  E-value: 1.42e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502861956  167 PGMRVLDIGCGWGGLAYFMAKHYGVSVVGVTISAEQQKMARERcqGLDV-----DIRLQDYRDlnEQFDRIV 233
Cdd:TIGR02081  13 PGSRVLDLGCGDGELLALLRDEKQVRGYGIEIDQDGVLACVAR--GVNViqgdlDEGLEAFPD--KSFDYVI 80
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
167-234 2.48e-03

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 38.73  E-value: 2.48e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502861956 167 PGMRVLDIGCGWGGLAYFmAKHYGVS-VVGVTISAEQQKMARE--RCQGLDVDIRLQDYRD--LNEQFDRIVS 234
Cdd:COG2263   45 EGKTVLDLGCGTGMLAIG-AALLGAKkVVGVDIDPEALEIAREnaERLGVRVDFIRADVTRipLGGSVDTVVM 116
Trm5 COG2520
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 ...
 157-285 2.62e-03

tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 N-methylase Trm5 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442010 [Multi-domain]  Cd Length: 333  Bit Score: 39.46  E-value: 2.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956 157 RLISEKL----QLQPGMRVLDIGCGWGGLAYFMAKHYGVSVVGVTISAEQQKMARE-----RCQGlDVDIRLQDYRD--- 224
Cdd:COG2520  166 RLATERLriaeLVKPGERVLDMFAGVGPFSIPIAKRSGAKVVAIDINPDAVEYLKEnirlnKVED-RVTPILGDAREvap 244

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502861956 225 -LNEQFDRIVsvgmfehVG-PKNYDTYFEVVDRNLKPDGIFLLHTIGSKrtDNNVDPWINKYI 285
Cdd:COG2520  245 eLEGKADRII-------MNlPHSADEFLDAALRALKPGGVIHYYEIVPE--EDPFERAEERIE 298
PRK14968 PRK14968
putative methyltransferase; Provisional
 158-199 2.83e-03

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 38.34  E-value: 2.83e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 502861956 158 LISEKLQLQPGMRVLDIGCGWGGLAYFMAKHyGVSVVGVTIS 199
Cdd:PRK14968  14 LLAENAVDKKGDRVLEVGTGSGIVAIVAAKN-GKKVVGVDIN 54
TPMT pfam05724
Thiopurine S-methyltransferase (TPMT); This family consists of thiopurine S-methyltransferase ...
 148-268 3.25e-03

Thiopurine S-methyltransferase (TPMT); This family consists of thiopurine S-methyltransferase proteins from both eukaryotes and prokaryotes. Thiopurine S-methyltransferase (TPMT) is a cytosolic enzyme that catalyzes S-methylation of aromatic and heterocyclic sulfhydryl compounds, including anticancer and immunosuppressive thiopurines.


Pssm-ID: 399030  Cd Length: 218  Bit Score: 38.56  E-value: 3.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956  148 LEEAQQDKLRLISeKLQLQPGMRVLDIGCGWGGLAYFMAKHyGVSVVGVTIS--------AEQQKM-------ARERCQG 212
Cdd:pfam05724  19 QEGVNPLLVRHWD-ALKLPPGLRVLVPLCGKALDMVWLAEQ-GHFVVGVEISelavekffAEAGLSppitelsGFKEYSS 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956  213 LDVDIRLQDYRDLNEQ----FDRIVSVGMFEHVGPKNYDTYFEVVDRNLKPDGIFLLHTI 268
Cdd:pfam05724  97 GNISLYCGDFFTLPREelgkFDLIYDRAALCALPPEMRPRYAKQMYELLPPGGRGLLITL 156
MetW pfam07021
Methionine biosynthesis protein MetW; This family consists of several bacterial and one ...
 156-233 3.34e-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: 3.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956  156 LRLISEklQLQPGMRVLDIGCGWGGLAYFMAKHYGVSVVGVTISAEqqKMARERCQGL-----DVDIRLQDYRDlnEQFD 230
Cdd:pfam07021   4 FRYILE--WIPPGSRVLDLGCGDGTLLYLLKEEKGVDGYGIELDAA--GVAECVAKGLyviqgDLDEGLEHFPD--KSFD 77


                  ...
gi 502861956  231 RIV 233
Cdd:pfam07021  78 YVI 80
PRK14967 PRK14967
putative methyltransferase; Provisional
 152-234 3.95e-03

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 38.50  E-value: 3.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956 152 QQDKLRLIS--EKLQLQPGMRVLDIGCGWGGLAYFMAKHYGVSVVGVTISAEQQKMARERC--QGLDVDIRLQDY-RDLN 226
Cdd:PRK14967  19 QEDTQLLADalAAEGLGPGRRVLDLCTGSGALAVAAAAAGAGSVTAVDISRRAVRSARLNAllAGVDVDVRRGDWaRAVE 98


                 ....*....
gi 502861956 227 EQ-FDRIVS 234
Cdd:PRK14967  99 FRpFDVVVS 107
threonine_DH_like cd08234
L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 161-208 7.02e-03

L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent formation of 2-amino-3-ketobutyrate from L-threonine, via NAD(H)-dependent oxidation. THD is a member of the zinc-requiring, medium chain NAD(H)-dependent alcohol dehydrogenase family (MDR). MDRs have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose.


Pssm-ID: 176196 [Multi-domain]  Cd Length: 334  Bit Score: 38.28  E-value: 7.02e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 502861956 161 EKLQLQPGMRVLDIGCGWGGLayFMA---KHYGVS-VVGVTISAEQQKMARE 208
Cdd:cd08234  153 DLLGIKPGDSVLVFGAGPIGL--LLAqllKLNGASrVTVAEPNEEKLELAKK 202
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 156-280 9.09e-03

Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 37.69  E-value: 9.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502861956 156 LRLISEKLQLQPGMRVLDIGCGwG-GL-AYFMAKHYGVSVVGVTISAEQQKMARErcqgLDVDIRLQDYRDLNEQFDRIV 233
Cdd:cd05188  123 YHALRRAGVLKPGDTVLVLGAG-GvGLlAAQLAKAAGARVIVTDRSDEKLELAKE----LGADHVIDYKEEDLEEELRLT 197

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 502861956 234 SVGM----FEHVGpkNYDTyFEVVDRNLKPDGIFLLhtIGSKRTDNNVDPW 280
Cdd:cd05188  198 GGGGadvvIDAVG--GPET-LAQALRLLRPGGRIVV--VGGTSGGPPLDDL 243
 
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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