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Conserved domains on  [gi|1100983887|ref|WP_071490865|]
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MULTISPECIES: C17 cyclopropane fatty acid synthase CfaB [Pseudomonas]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 12034117)

class I SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor; similar to Mycobacterium tuberculosis mycolic acid cyclopropane synthases (such as PcaA, CmaA, and MmaA) that are responsible for site-specific modifications of mycolic acids

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cyclopro_CfaB NF040703
C17 cyclopropane fatty acid synthase CfaB;
1-393 0e+00

C17 cyclopropane fatty acid synthase CfaB;


:

Pssm-ID: 468667 [Multi-domain]  Cd Length: 393  Bit Score: 860.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887   1 MLAQLPPALQNLQLPLRLRLWDGHEFNLGPEPSVTIVVKDPTVVNKLTHPTLDSLGEAFVEGKLELEGSISEVIRVCDEL 80
Cdd:NF040703    1 MLAQLPPALRNLQLPLRLRLWDGKQLDLGPSPRVTLVVKDPSLLSQLTHPSLDLLGSAYVEGRLDLEGPIMEVIRVGDEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887  81 SHALIEDDEGSRPVRSIHDKATDAAAISYHYDLSNEFYQLWLDQDMAYSCGYFETGSESIDQAQQDKFRHLCRKLRLQPG 160
Cdd:NF040703   81 SQALLGDDDEAPPERTAHDKATDAAAISYHYDLSNDFYALWLDPDMVYSCAYFETGTEDLAQAQQAKLRHLCRKLRLQPG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 161 EYLLDVGCGWGGLARFAAREFGVKVFGITLSKEQLALARERVKAEGLEDQVDLQLLDYRDLPQDGRFDKVVSVGMFEHVG 240
Cdd:NF040703  161 ERLLDVGCGWGGLARFAAREFGVEVFGITLSKEQLKLARERVAAEGLQDRVQLELLDYRDLPQDGRFDKVVSVGMFEHVG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 241 HANLAQYCKTLFGAVREGGLVMNHGITAKHTDGRPVGRGAGEFIERYVFPNGELPHLAMMTAEISEVGLEVVDVESLRLH 320
Cdd:NF040703  241 HANLPLYCQRLFGAVRPGGLVMNHGITARHTDGRPVGRGAGEFIGRYVFPHGELPHLATITASISEAGLEVVDVESLRLH 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1100983887 321 YARTLDHWSERLEDNLEAAAKMVPEQALRIWRLYLAGCAYAFARGWINLHQILAVKPHADGSHDLPWTREDIY 393
Cdd:NF040703  321 YARTLEHWSARLEARLDEAARLVPERALRIWRLYLAGCAYGFARGWINLHQILAVKPLADGSHELPWTRADLY 393
 
Name Accession Description Interval E-value
cyclopro_CfaB NF040703
C17 cyclopropane fatty acid synthase CfaB;
1-393 0e+00

C17 cyclopropane fatty acid synthase CfaB;


Pssm-ID: 468667 [Multi-domain]  Cd Length: 393  Bit Score: 860.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887   1 MLAQLPPALQNLQLPLRLRLWDGHEFNLGPEPSVTIVVKDPTVVNKLTHPTLDSLGEAFVEGKLELEGSISEVIRVCDEL 80
Cdd:NF040703    1 MLAQLPPALRNLQLPLRLRLWDGKQLDLGPSPRVTLVVKDPSLLSQLTHPSLDLLGSAYVEGRLDLEGPIMEVIRVGDEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887  81 SHALIEDDEGSRPVRSIHDKATDAAAISYHYDLSNEFYQLWLDQDMAYSCGYFETGSESIDQAQQDKFRHLCRKLRLQPG 160
Cdd:NF040703   81 SQALLGDDDEAPPERTAHDKATDAAAISYHYDLSNDFYALWLDPDMVYSCAYFETGTEDLAQAQQAKLRHLCRKLRLQPG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 161 EYLLDVGCGWGGLARFAAREFGVKVFGITLSKEQLALARERVKAEGLEDQVDLQLLDYRDLPQDGRFDKVVSVGMFEHVG 240
Cdd:NF040703  161 ERLLDVGCGWGGLARFAAREFGVEVFGITLSKEQLKLARERVAAEGLQDRVQLELLDYRDLPQDGRFDKVVSVGMFEHVG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 241 HANLAQYCKTLFGAVREGGLVMNHGITAKHTDGRPVGRGAGEFIERYVFPNGELPHLAMMTAEISEVGLEVVDVESLRLH 320
Cdd:NF040703  241 HANLPLYCQRLFGAVRPGGLVMNHGITARHTDGRPVGRGAGEFIGRYVFPHGELPHLATITASISEAGLEVVDVESLRLH 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1100983887 321 YARTLDHWSERLEDNLEAAAKMVPEQALRIWRLYLAGCAYAFARGWINLHQILAVKPHADGSHDLPWTREDIY 393
Cdd:NF040703  321 YARTLEHWSARLEARLDEAARLVPERALRIWRLYLAGCAYGFARGWINLHQILAVKPLADGSHELPWTRADLY 393
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 99-372 1.11e-142

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: 406.33  E-value: 1.11e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887  99 DKATDAAAISYHYDLSNEFYQLWLDQDMAYSCGYFETGSESIDQAQQDKFRHLCRKLRLQPGEYLLDVGCGWGGLARFAA 178
Cdd:pfam02353   1 SKTRDAENIQAHYDLSNDFFALFLDPTMTYSCAYFERPDMTLEEAQQAKLDLILDKLGLKPGMTLLDIGCGWGGLMRRAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 179 REFGVKVFGITLSKEQLALARERVKAEGLEDQVDLQLLDYRDLpqDGRFDKVVSVGMFEHVGHANLAQYCKTLFGAVREG 258
Cdd:pfam02353  81 ERYDVNVVGLTLSKNQYKLARKRVAAEGLARKVEVLLQDYRDF--DEPFDRIVSVGMFEHVGHENYDTFFKKLYNLLPPG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 259 GLVMNHGITAKHTDGRPVGRGAGEFIERYVFPNGELPHLAMMTAEISEVGLEVVDVESLRLHYARTLDHWSERLEDNLEA 338
Cdd:pfam02353 159 GLMLLHTITGLHPDETSERGLPLKFIDKYIFPGGELPSISMIVESSSEAGFTVEDVESLRPHYAKTLDLWAENLQANKDE 238

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1100983887 339 AAKMVPEQALRIWRLYLAGCAYAFARGWINLHQI 372
Cdd:pfam02353 239 AIALQSEEFYRMWMLYLTGCAVAFRIGYIDVHQF 272
PRK11705 PRK11705
cyclopropane fatty acyl phospholipid synthase;
110-373 9.53e-82

cyclopropane fatty acyl phospholipid synthase;


Pssm-ID: 183282  Cd Length: 383  Bit Score: 255.16  E-value: 9.53e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 110 HYDLSNEFYQLWLDQDMAYSCGYFEtGSESIDQAQQDKFRHLCRKLRLQPGEYLLDVGCGWGGLARFAAREFGVKVFGIT 189
Cdd:PRK11705  119 HYDLGNDLFEAMLDPRMQYSCGYWK-DADTLEEAQEAKLDLICRKLQLKPGMRVLDIGCGWGGLARYAAEHYGVSVVGVT 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 190 LSKEQLALARERvkAEGLEdqVDLQLLDYRDLpqDGRFDKVVSVGMFEHVGHANLAQYCKTLFGAVREGGLVMNHGITAK 269
Cdd:PRK11705  198 ISAEQQKLAQER--CAGLP--VEIRLQDYRDL--NGQFDRIVSVGMFEHVGPKNYRTYFEVVRRCLKPDGLFLLHTIGSN 271

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 270 HTDgrpvgRGAGEFIERYVFPNGELPHLAMMtAEISEvGLEVV-DVESLRLHYARTLDHWSERLEDNLEAAAKMVPEQAL 348
Cdd:PRK11705  272 KTD-----TNVDPWINKYIFPNGCLPSVRQI-AQASE-GLFVMeDWHNFGADYDRTLMAWHENFEAAWPELADNYSERFY 344

                         250       260
                  ....*....|....*....|....*.
gi 1100983887 349 RIWRLYLAGCAYAF-ARGwINLHQIL 373
Cdd:PRK11705  345 RMWRYYLLSCAGAFrARD-IQLWQVV 369
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 109-265 2.36e-79

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 240.99  E-value: 2.36e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 109 YHYDLSNEFYQLWLDQDMAYSCGYFETGSESIDQAQQDKFRHLCRKLRLQPGEYLLDVGCGWGGLARFAAREFGVKVFGI 188
Cdd:COG2230     1 HHYDLGNDFYRLFLDPTMTYSCAYFEDPDDTLEEAQEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGV 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1100983887 189 TLSKEQLALARERVKAEGLEDQVDLQLLDYRDLPQDGRFDKVVSVGMFEHVGHANLAQYCKTLFGAVREGGLVMNHG 265
Cdd:COG2230    81 TLSPEQLEYARERAAEAGLADRVEVRLADYRDLPADGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLLHT 157
mycolic_MTase NF040660
cyclopropane mycolic acid synthase family methyltransferase; Members of this family include ...
 105-376 2.87e-55

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: 183.43  E-value: 2.87e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 105 AAISYHYDLSNEFYQLWLDQDMAYSCGYFETGSESIDQAQQDKFRHLCRKLRLQPGEYLLDVGCGWGGLARFAAREFGVK 184
Cdd:NF040660    6 EDVQAHYDLSDDFFALFLDPTQTYSCAYFERDDMTLEEAQIAKIDLALGKLNLEPGMTLLDIGCGWGATMRRAVEKYDVN 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 185 VFGITLSKEQLALARERVKAEGLEDQVDLQLLDYRDLpqDGRFDKVVSVGMFEHVGHANLAQYCKTLFGAVREGGLVMNH 264
Cdd:NF040660   86 VVGLTLSKNQAAHVQQVLDEIDTPRSRRVLLQGWEEF--DEPVDRIVSIGAFEHFGHERYDDFFKRAYNILPADGRMLLH 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 265 GITAKHTD-----GRPVGRGAGEFIERYV---FPNGELPHLAMMTAEISEVGLEVVDVESLRLHYARTLDHWSERLEDNL 336
Cdd:NF040660  164 TITGLHRKemherGLPLTMELARFIKFIVteiFPGGRLPSIEMVVEHAEKAGFTVTRVQSLQPHYARTLDLWADALQAHK 243

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1100983887 337 EAAAKMVPEQALRIWRLYLAGCAYAFARGWINLHQILAVK 376
Cdd:NF040660  244 DEAIAIQSEEVYERYMKYLTGCAKLFRDGYIDVNQFTLAK 283
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 163-262 1.09e-10

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: 58.21  E-value: 1.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 163 LLDVGCGWGGLARFAAREFGVKVFGITLSKEQLALAReRVKAEGLEDQVDLQLLDYRDLPQ--DGRFDKVVSVGMFEHVg 240
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVDISPVALELAR-KAAAALLADNVEVLKGDAEELPPeaDESFDVIISDPPLHHL- 79

                          90       100
                  ....*....|....*....|..
gi 1100983887 241 HANLAQYCKTLFGAVREGGLVM 262
Cdd:cd02440    80 VEDLARFLEEARRLLKPGGVLV 101
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
164-261 4.01e-07

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 50.49  E-value: 4.01e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887  164 LDVGCGWG-GLARFAAREFGVKVFGITLSKEQLALARERVKAEGLEDQVdlqLLDYRDLPQDGRFDKVVSVGMFEHVGH- 241
Cdd:smart00828   4 LDFGCGYGsDLIDLAERHPHLQLHGYTISPEQAEVGRERIRALGLQGRI---RIFYRDSAKDPFPDTYDLVFGFEVIHHi 80

                           90       100
                   ....*....|....*....|....*..
gi 1100983887  242 -------ANLAQYcktlfgaVREGGLV 261
Cdd:smart00828  81 kdkmdlfSNISRH-------LKDGGHL 100
 
Name Accession Description Interval E-value
cyclopro_CfaB NF040703
C17 cyclopropane fatty acid synthase CfaB;
1-393 0e+00

C17 cyclopropane fatty acid synthase CfaB;


Pssm-ID: 468667 [Multi-domain]  Cd Length: 393  Bit Score: 860.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887   1 MLAQLPPALQNLQLPLRLRLWDGHEFNLGPEPSVTIVVKDPTVVNKLTHPTLDSLGEAFVEGKLELEGSISEVIRVCDEL 80
Cdd:NF040703    1 MLAQLPPALRNLQLPLRLRLWDGKQLDLGPSPRVTLVVKDPSLLSQLTHPSLDLLGSAYVEGRLDLEGPIMEVIRVGDEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887  81 SHALIEDDEGSRPVRSIHDKATDAAAISYHYDLSNEFYQLWLDQDMAYSCGYFETGSESIDQAQQDKFRHLCRKLRLQPG 160
Cdd:NF040703   81 SQALLGDDDEAPPERTAHDKATDAAAISYHYDLSNDFYALWLDPDMVYSCAYFETGTEDLAQAQQAKLRHLCRKLRLQPG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 161 EYLLDVGCGWGGLARFAAREFGVKVFGITLSKEQLALARERVKAEGLEDQVDLQLLDYRDLPQDGRFDKVVSVGMFEHVG 240
Cdd:NF040703  161 ERLLDVGCGWGGLARFAAREFGVEVFGITLSKEQLKLARERVAAEGLQDRVQLELLDYRDLPQDGRFDKVVSVGMFEHVG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 241 HANLAQYCKTLFGAVREGGLVMNHGITAKHTDGRPVGRGAGEFIERYVFPNGELPHLAMMTAEISEVGLEVVDVESLRLH 320
Cdd:NF040703  241 HANLPLYCQRLFGAVRPGGLVMNHGITARHTDGRPVGRGAGEFIGRYVFPHGELPHLATITASISEAGLEVVDVESLRLH 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1100983887 321 YARTLDHWSERLEDNLEAAAKMVPEQALRIWRLYLAGCAYAFARGWINLHQILAVKPHADGSHDLPWTREDIY 393
Cdd:NF040703  321 YARTLEHWSARLEARLDEAARLVPERALRIWRLYLAGCAYGFARGWINLHQILAVKPLADGSHELPWTRADLY 393
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 99-372 1.11e-142

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: 406.33  E-value: 1.11e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887  99 DKATDAAAISYHYDLSNEFYQLWLDQDMAYSCGYFETGSESIDQAQQDKFRHLCRKLRLQPGEYLLDVGCGWGGLARFAA 178
Cdd:pfam02353   1 SKTRDAENIQAHYDLSNDFFALFLDPTMTYSCAYFERPDMTLEEAQQAKLDLILDKLGLKPGMTLLDIGCGWGGLMRRAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 179 REFGVKVFGITLSKEQLALARERVKAEGLEDQVDLQLLDYRDLpqDGRFDKVVSVGMFEHVGHANLAQYCKTLFGAVREG 258
Cdd:pfam02353  81 ERYDVNVVGLTLSKNQYKLARKRVAAEGLARKVEVLLQDYRDF--DEPFDRIVSVGMFEHVGHENYDTFFKKLYNLLPPG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 259 GLVMNHGITAKHTDGRPVGRGAGEFIERYVFPNGELPHLAMMTAEISEVGLEVVDVESLRLHYARTLDHWSERLEDNLEA 338
Cdd:pfam02353 159 GLMLLHTITGLHPDETSERGLPLKFIDKYIFPGGELPSISMIVESSSEAGFTVEDVESLRPHYAKTLDLWAENLQANKDE 238

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1100983887 339 AAKMVPEQALRIWRLYLAGCAYAFARGWINLHQI 372
Cdd:pfam02353 239 AIALQSEEFYRMWMLYLTGCAVAFRIGYIDVHQF 272
PRK11705 PRK11705
cyclopropane fatty acyl phospholipid synthase;
110-373 9.53e-82

cyclopropane fatty acyl phospholipid synthase;


Pssm-ID: 183282  Cd Length: 383  Bit Score: 255.16  E-value: 9.53e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 110 HYDLSNEFYQLWLDQDMAYSCGYFEtGSESIDQAQQDKFRHLCRKLRLQPGEYLLDVGCGWGGLARFAAREFGVKVFGIT 189
Cdd:PRK11705  119 HYDLGNDLFEAMLDPRMQYSCGYWK-DADTLEEAQEAKLDLICRKLQLKPGMRVLDIGCGWGGLARYAAEHYGVSVVGVT 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 190 LSKEQLALARERvkAEGLEdqVDLQLLDYRDLpqDGRFDKVVSVGMFEHVGHANLAQYCKTLFGAVREGGLVMNHGITAK 269
Cdd:PRK11705  198 ISAEQQKLAQER--CAGLP--VEIRLQDYRDL--NGQFDRIVSVGMFEHVGPKNYRTYFEVVRRCLKPDGLFLLHTIGSN 271

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 270 HTDgrpvgRGAGEFIERYVFPNGELPHLAMMtAEISEvGLEVV-DVESLRLHYARTLDHWSERLEDNLEAAAKMVPEQAL 348
Cdd:PRK11705  272 KTD-----TNVDPWINKYIFPNGCLPSVRQI-AQASE-GLFVMeDWHNFGADYDRTLMAWHENFEAAWPELADNYSERFY 344

                         250       260
                  ....*....|....*....|....*.
gi 1100983887 349 RIWRLYLAGCAYAF-ARGwINLHQIL 373
Cdd:PRK11705  345 RMWRYYLLSCAGAFrARD-IQLWQVV 369
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 109-265 2.36e-79

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 240.99  E-value: 2.36e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 109 YHYDLSNEFYQLWLDQDMAYSCGYFETGSESIDQAQQDKFRHLCRKLRLQPGEYLLDVGCGWGGLARFAAREFGVKVFGI 188
Cdd:COG2230     1 HHYDLGNDFYRLFLDPTMTYSCAYFEDPDDTLEEAQEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGV 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1100983887 189 TLSKEQLALARERVKAEGLEDQVDLQLLDYRDLPQDGRFDKVVSVGMFEHVGHANLAQYCKTLFGAVREGGLVMNHG 265
Cdd:COG2230    81 TLSPEQLEYARERAAEAGLADRVEVRLADYRDLPADGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLLHT 157
mycolic_MTase NF040660
cyclopropane mycolic acid synthase family methyltransferase; Members of this family include ...
 105-376 2.87e-55

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: 183.43  E-value: 2.87e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 105 AAISYHYDLSNEFYQLWLDQDMAYSCGYFETGSESIDQAQQDKFRHLCRKLRLQPGEYLLDVGCGWGGLARFAAREFGVK 184
Cdd:NF040660    6 EDVQAHYDLSDDFFALFLDPTQTYSCAYFERDDMTLEEAQIAKIDLALGKLNLEPGMTLLDIGCGWGATMRRAVEKYDVN 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 185 VFGITLSKEQLALARERVKAEGLEDQVDLQLLDYRDLpqDGRFDKVVSVGMFEHVGHANLAQYCKTLFGAVREGGLVMNH 264
Cdd:NF040660   86 VVGLTLSKNQAAHVQQVLDEIDTPRSRRVLLQGWEEF--DEPVDRIVSIGAFEHFGHERYDDFFKRAYNILPADGRMLLH 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 265 GITAKHTD-----GRPVGRGAGEFIERYV---FPNGELPHLAMMTAEISEVGLEVVDVESLRLHYARTLDHWSERLEDNL 336
Cdd:NF040660  164 TITGLHRKemherGLPLTMELARFIKFIVteiFPGGRLPSIEMVVEHAEKAGFTVTRVQSLQPHYARTLDLWADALQAHK 243

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1100983887 337 EAAAKMVPEQALRIWRLYLAGCAYAFARGWINLHQILAVK 376
Cdd:NF040660  244 DEAIAIQSEEVYERYMKYLTGCAKLFRDGYIDVNQFTLAK 283
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 164-259 4.48e-24

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 94.94  E-value: 4.48e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 164 LDVGCGWGGLARFAAREFGVKVFGITLSKEQLALARERVKAEGLedQVDLQLLDYRDLPQ-DGRFDKVVSVGMFEHVGHA 242
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAEDLPFpDGSFDLVVSSGVLHHLPDP 79

                          90
                  ....*....|....*..
gi 1100983887 243 NLAQYCKTLFGAVREGG 259
Cdd:pfam13649  80 DLEAALREIARVLKPGG 96
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 146-262 1.82e-19

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: 83.89  E-value: 1.82e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 146 DKFRHLCRKLRLQPGEYLLDVGCGWGGLARFAAREfGVKVFGITLSKEQLALARERVKAEGLedQVDLQLLDYRDLP-QD 224
Cdd:COG2226     9 DGREALLAALGLRPGARVLDLGCGTGRLALALAER-GARVTGVDISPEMLELARERAAEAGL--NVEFVVGDAEDLPfPD 85

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1100983887 225 GRFDKVVSVGMFEHVghANLAQYCKTLFGAVREGGLVM 262
Cdd:COG2226    86 GSFDLVISSFVLHHL--PDPERALAEIARVLKPGGRLV 121
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 127-262 2.69e-18

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 82.27  E-value: 2.69e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 127 AYSCGYFETGSESIDQAqqdkfrhLCRKLRLQPGEYLLDVGCGWGGLARFAAREFGVKVFGITLSKEQLALARERVKAEG 206
Cdd:COG0500     1 PWDSYYSDELLPGLAAL-------LALLERLPKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAG 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1100983887 207 LeDQVDLQLLDYRDLPQ--DGRFDKVVSVGMFEHVGHANLAQYCKTLFGAVREGGLVM 262
Cdd:COG0500    74 L-GNVEFLVADLAELDPlpAESFDLVVAFGVLHHLPPEEREALLRELARALKPGGVLL 130
PLN02244 PLN02244
tocopherol O-methyltransferase
 69-239 3.45e-17

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 81.71  E-value: 3.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887  69 SISEVIRVCDELSHALIEDDEGSRPVRSIHDKATDAAA----ISYHYDLSNEFYQ-LWLDQdMAYscGYFETGSESID-- 141
Cdd:PLN02244   19 SGSRSTRLSRPSSSASGVRRTLARLEDAASPAPAATADlkegIAEFYDESSGVWEdVWGEH-MHH--GYYDPGASRGDhr 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 142 QAQQD------KFRHLCRKLRLQPgEYLLDVGCGWGGLARFAAREFGVKVFGITLSKEQLALARERVKAEGLEDQVDLQL 215
Cdd:PLN02244   96 QAQIRmieeslAWAGVPDDDEKRP-KRIVDVGCGIGGSSRYLARKYGANVKGITLSPVQAARANALAAAQGLSDKVSFQV 174

                         170       180
                  ....*....|....*....|....*
gi 1100983887 216 LDYRDLP-QDGRFDKVVSVGMFEHV 239
Cdd:PLN02244  175 ADALNQPfEDGQFDLVWSMESGEHM 199
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 156-261 5.80e-17

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: 76.59  E-value: 5.80e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 156 RLQPGEYLLDVGCGWGGLARFAAREfGVKVFGITLSKEQLALARERVKAEGledqVDLQLLDYRDLP-QDGRFDKVVSVG 234
Cdd:COG2227    21 LLPAGGRVLDVGCGTGRLALALARR-GADVTGVDISPEALEIARERAAELN----VDFVQGDLEDLPlEDGSFDLVICSE 95

                          90       100
                  ....*....|....*....|....*..
gi 1100983887 235 MFEHVghANLAQYCKTLFGAVREGGLV 261
Cdd:COG2227    96 VLEHL--PDPAALLRELARLLKPGGLL 120
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 164-261 1.78e-13

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 65.76  E-value: 1.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 164 LDVGCGWGGLARFAAReFGVKVFGITLSKEQLALARERVKAEGLEdqvdLQLLDYRDLP-QDGRFDKVVSVGMFEHVghA 242
Cdd:pfam08241   1 LDVGCGTGLLTELLAR-LGARVTGVDISPEMLELAREKAPREGLT----FVVGDAEDLPfPDNSFDLVLSSEVLHHV--E 73

                          90
                  ....*....|....*....
gi 1100983887 243 NLAQYCKTLFGAVREGGLV 261
Cdd:pfam08241  74 DPERALREIARVLKPGGIL 92
PRK08317 PRK08317
hypothetical protein; Provisional
 153-259 3.68e-13

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 68.42  E-value: 3.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 153 RKLRLQPGEYLLDVGCGWGGLARFAAREFGV--KVFGITLSKEQLALARERvkAEGLEDQVDLQLLDYRDLP-QDGRFDK 229
Cdd:PRK08317   13 ELLAVQPGDRVLDVGCGPGNDARELARRVGPegRVVGIDRSEAMLALAKER--AAGLGPNVEFVRGDADGLPfPDGSFDA 90

                          90       100       110
                  ....*....|....*....|....*....|
gi 1100983887 230 VVSVGMFEHVghANLAQYCKTLFGAVREGG 259
Cdd:PRK08317   91 VRSDRVLQHL--EDPARALAEIARVLRPGG 118
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
123-286 5.76e-13

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 66.56  E-value: 5.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 123 DQDMAYSCGYfetgsesidQAQQDKFRHLCRKLRLQPGEYLLDVGCGwGGLARFAAREFGVKVFGITLSKEQLALARERv 202
Cdd:COG4976    19 DAALVEDLGY---------EAPALLAEELLARLPPGPFGRVLDLGCG-TGLLGEALRPRGYRLTGVDLSEEMLAKAREK- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 203 kaeglEDQVDLQLLDYRDLPQ-DGRFDKVVSVGMFEHVGhaNLAQYCKTLFGAVREGGLVMnhgITAKHTDGRPVGRGAG 281
Cdd:COG4976    88 -----GVYDRLLVADLADLAEpDGRFDLIVAADVLTYLG--DLAAVFAGVARALKPGGLFI---FSVEDADGSGRYAHSL 157


                  ....*
gi 1100983887 282 EFIER 286
Cdd:COG4976   158 DYVRD 162
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
159-262 4.87e-12

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 61.76  E-value: 4.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 159 PGEYLLDVGCGWGGLAR-FAAREFGVKVFGITLSKEQLALARERVkaegleDQVDLQLLDYRDLPQDGRFDKVVSVGMFE 237
Cdd:COG4106     1 PPRRVLDLGCGTGRLTAlLAERFPGARVTGVDLSPEMLARARARL------PNVRFVVADLRDLDPPEPFDLVVSNAALH 74

                          90       100
                  ....*....|....*....|....*
gi 1100983887 238 HVghANLAQYCKTLFGAVREGGLVM 262
Cdd:COG4106    75 WL--PDHAALLARLAAALAPGGVLA 97
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 145-234 1.07e-10

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 61.32  E-value: 1.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 145 QDKF--RHLCRKLRLQPGEYLLDVGCGWGGLARFAAREFGV--KVFGITLSKEQLALARERVKAEGLEDQVDLQLLDYRD 220
Cdd:PRK00216   35 LHRVwrRKTIKWLGVRPGDKVLDLACGTGDLAIALAKAVGKtgEVVGLDFSEGMLAVGREKLRDLGLSGNVEFVQGDAEA 114

                          90
                  ....*....|....*
gi 1100983887 221 LP-QDGRFDkVVSVG 234
Cdd:PRK00216  115 LPfPDNSFD-AVTIA 128
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 163-262 1.09e-10

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: 58.21  E-value: 1.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 163 LLDVGCGWGGLARFAAREFGVKVFGITLSKEQLALAReRVKAEGLEDQVDLQLLDYRDLPQ--DGRFDKVVSVGMFEHVg 240
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVDISPVALELAR-KAAAALLADNVEVLKGDAEELPPeaDESFDVIISDPPLHHL- 79

                          90       100
                  ....*....|....*....|..
gi 1100983887 241 HANLAQYCKTLFGAVREGGLVM 262
Cdd:cd02440    80 VEDLARFLEEARRLLKPGGVLV 101
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 164-261 5.29e-10

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 55.84  E-value: 5.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 164 LDVGCGWGGLARFAAREF-GVKVFGITLSKEQLALARERVKAEGLEDQVDLQLLDYRDLPQDGR-FDKVVSVGMFEHVgh 241
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALpGLEYTGLDISPAALEAARERLAALGLLNAVRVELFQLDLGELDPGsFDVVVASNVLHHL-- 78

                          90       100
                  ....*....|....*....|
gi 1100983887 242 ANLAQYCKTLFGAVREGGLV 261
Cdd:pfam08242  79 ADPRAVLRNIRRLLKPGGVL 98
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 159-262 1.43e-08

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 53.19  E-value: 1.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 159 PGEYLLDVGCGWGGLARFAAREFG--VKVFGITLSKEQLALARERVKAEGLEDqVDLQLLDYRDLPQ---DGRFDKVVSV 233
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEELGpnAEVVGIDISEEAIEKARENAQKLGFDN-VEFEQGDIEELPElleDDKFDVVISN 81

                          90       100
                  ....*....|....*....|....*....
gi 1100983887 234 GMFEHVghANLAQYCKTLFGAVREGGLVM 262
Cdd:pfam13847  82 CVLNHI--PDPDKVLQEILRVLKPGGRLI 108
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 129-232 1.43e-07

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 53.22  E-value: 1.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 129 SCGYFETGSESIDqaqqdkfrhlcrKLRLQPGEYLLDVGCGWGGLARFAAREFGVKVFGITLSKEQLALARERvkAEGLE 208
Cdd:PLN02336  248 STGGLETTKEFVD------------KLDLKPGQKVLDVGCGIGGGDFYMAENFDVHVVGIDLSVNMISFALER--AIGRK 313

                          90       100
                  ....*....|....*....|....*.
gi 1100983887 209 DQVDLQLLD--YRDLPqDGRFDKVVS 232
Cdd:PLN02336  314 CSVEFEVADctKKTYP-DNSFDVIYS 338
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 159-231 2.63e-07

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 50.99  E-value: 2.63e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1100983887 159 PGEYLLDVGCGWGGLARFAAREfGVKVFGITLSKEQLALARERVKAEGLEDQVDLQLLDYRDLpqDGRFDKVV 231
Cdd:PRK07580   63 TGLRILDAGCGVGSLSIPLARR-GAKVVASDISPQMVEEARERAPEAGLAGNITFEVGDLESL--LGRFDTVV 132
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
164-261 4.01e-07

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 50.49  E-value: 4.01e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887  164 LDVGCGWG-GLARFAAREFGVKVFGITLSKEQLALARERVKAEGLEDQVdlqLLDYRDLPQDGRFDKVVSVGMFEHVGH- 241
Cdd:smart00828   4 LDFGCGYGsDLIDLAERHPHLQLHGYTISPEQAEVGRERIRALGLQGRI---RIFYRDSAKDPFPDTYDLVFGFEVIHHi 80

                           90       100
                   ....*....|....*....|....*..
gi 1100983887  242 -------ANLAQYcktlfgaVREGGLV 261
Cdd:smart00828  81 kdkmdlfSNISRH-------LKDGGHL 100
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 156-232 7.90e-07

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: 49.76  E-value: 7.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 156 RLQPGEYLLDVGCGWGGLARF-AAREFGVKVFGITLSKEQLALARERVKAEGLEDQVDLQLLDYRDLP---QDGRFDKVV 231
Cdd:COG4123    34 PVKKGGRVLDLGTGTGVIALMlAQRSPGARITGVEIQPEAAELARRNVALNGLEDRITVIHGDLKEFAaelPPGSFDLVV 113


                  .
gi 1100983887 232 S 232
Cdd:COG4123   114 S 114
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 151-265 2.64e-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: 47.49  E-value: 2.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 151 LCRKLRLQPGEYLLDVGCGWGGLARFAAREFGV-KVFGITLSKEQLALARERVKAEGLEDqVDLQLLDYRDLPQDGRFDK 229
Cdd:COG2813    41 LLEHLPEPLGGRVLDLGCGYGVIGLALAKRNPEaRVTLVDVNARAVELARANAAANGLEN-VEVLWSDGLSGVPDGSFDL 119

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1100983887 230 VVS-----VGMFE--HVGHANLAQYCKTLfgavREGG---LVMNHG 265
Cdd:COG2813   120 ILSnppfhAGRAVdkEVAHALIADAARHL----RPGGelwLVANRH 161
PLN02396 PLN02396
hexaprenyldihydroxybenzoate methyltransferase
 151-259 2.70e-06

hexaprenyldihydroxybenzoate methyltransferase


Pssm-ID: 178018 [Multi-domain]  Cd Length: 322  Bit Score: 48.96  E-value: 2.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 151 LCRKLRLQP-------GEYLLDVGCGWGGLARFAAReFGVKVFGITLSKEQLALARERVKAEGLEDQVDLQLLDYRDLPQ 223
Cdd:PLN02396  116 LCRHFSKDPssakpfeGLKFIDIGCGGGLLSEPLAR-MGATVTGVDAVDKNVKIARLHADMDPVTSTIEYLCTTAEKLAD 194

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1100983887 224 DGR-FDKVVSVGMFEHVghANLAQYCKTLFGAVREGG 259
Cdd:PLN02396  195 EGRkFDAVLSLEVIEHV--ANPAEFCKSLSALTIPNG 229
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 155-262 8.47e-06

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 45.50  E-value: 8.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 155 LRLQPGEYLLDVGCGWGGLARfAAREFGVKVFGITLSKEQLALARERVKAEGLEDQVDLQLldyrdlpqDGRFDKVVSVG 234
Cdd:pfam13489  18 PKLPSPGRVLDFGCGTGIFLR-LLRAQGFSVTGVDPSPIAIERALLNVRFDQFDEQEAAVP--------AGKFDVIVARE 88

                          90       100
                  ....*....|....*....|....*...
gi 1100983887 235 MFEHVghANLAQYCKTLFGAVREGGLVM 262
Cdd:pfam13489  89 VLEHV--PDPPALLRQIAALLKPGGLLL 114
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
 151-261 1.46e-05

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: 46.29  E-value: 1.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 151 LCRKLRLQPGEYLLDVGCGwGGLARFA---AREFGVKVFGITLSKEQLALARE----RV---KAEGLEDQVdlqlldyRD 220
Cdd:COG0604   131 LFDRGRLKPGETVLVHGAA-GGVGSAAvqlAKALGARVIATASSPEKAELLRAlgadHVidyREEDFAERV-------RA 202

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1100983887 221 LPQDGRFDKVvsvgmFEHVGHANLAQycktLFGAVREGGLV 261
Cdd:COG0604   203 LTGGRGVDVV-----LDTVGGDTLAR----SLRALAPGGRL 234
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 124-257 1.78e-05

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 45.90  E-value: 1.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 124 QDMAYSCGYFETGSESIDQAQQDKFRHLCRKLRLQPGEYLLDVGCGWGGLARFaAREFGVKVFGITLSKEQLALARERVK 203
Cdd:PRK10258    7 QAIAAAFGRAAAHYEQHAELQRQSADALLAMLPQRKFTHVLDAGCGPGWMSRY-WRERGSQVTALDLSPPMLAQARQKDA 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1100983887 204 AEgledqvDLQLLDYRDLP-QDGRFDKVVSvgmfehvghaNLA-QYCKTLFGAVRE 257
Cdd:PRK10258   86 AD------HYLAGDIESLPlATATFDLAWS----------NLAvQWCGNLSTALRE 125
arsM PRK11873
arsenite methyltransferase;
156-232 2.36e-05

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 45.71  E-value: 2.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 156 RLQPGEYLLDVGCGwGGLARF-AAREFGV--KVFGITLSKEQLALARERVKAEGLEDqVDLQLLDYRDLP-QDGRFDKVV 231
Cdd:PRK11873   74 ELKPGETVLDLGSG-GGFDCFlAARRVGPtgKVIGVDMTPEMLAKARANARKAGYTN-VEFRLGEIEALPvADNSVDVII 151


                  .
gi 1100983887 232 S 232
Cdd:PRK11873  152 S 152
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 164-232 2.37e-05

Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 45.53  E-value: 2.37e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1100983887 164 LDVGCGWGGLARFAAREF-GVKVFGITLSKEQLALARERVKAEGLEDQVDLQLLD-YRDLPQDGRFDKVVS 232
Cdd:COG2890   117 LDLGTGSGAIALALAKERpDARVTAVDISPDALAVARRNAERLGLEDRVRFLQGDlFEPLPGDGRFDLIVS 187
PRK06202 PRK06202
hypothetical protein; Provisional
 148-249 2.05e-04

hypothetical protein; Provisional


Pssm-ID: 180466 [Multi-domain]  Cd Length: 232  Bit Score: 42.29  E-value: 2.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 148 FRHLCRkLRLQPGE--YLLDVGCGwGG-----LARFAARE-FGVKVFGITLSKEQLALARERVKAEGledqVDLQLLDYR 219
Cdd:PRK06202   48 YRRLLR-PALSADRplTLLDIGCG-GGdlaidLARWARRDgLRLEVTAIDPDPRAVAFARANPRRPG----VTFRQAVSD 121

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1100983887 220 DLPQDG-RFDKVVSVGMFEHVGHANLAQYCK 249
Cdd:PRK06202  122 ELVAEGeRFDVVTSNHFLHHLDDAEVVRLLA 152
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 164-242 2.65e-04

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: 41.42  E-value: 2.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 164 LDVGCGWGGLARFAAREFG-VKVFGITLSKEQLALARERVKAEGLED----QVDLqlldYRDLPqDGRFDKVVSVGMFeH 238
Cdd:pfam05175  36 LDLGCGAGVLGAALAKESPdAELTMVDINARALESARENLAANGLENgevvASDV----YSGVE-DGKFDLIISNPPF-H 109


                  ....
gi 1100983887 239 VGHA 242
Cdd:pfam05175 110 AGLA 113
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 156-266 4.39e-04

Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal protein L11 methyltransferase (EC:2.1.1.-) sequences.


Pssm-ID: 428888 [Multi-domain]  Cd Length: 294  Bit Score: 41.87  E-value: 4.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 156 RLQPGEYLLDVGCGWGGLArFAAREFGVK-VFGITLSKEQLALARERVKAEGLEDQVDLQLLDyrDLPQdGRFDKVVsvg 234
Cdd:pfam06325 158 LVKPGESVLDVGCGSGILA-IAALKLGAKkVVGVDIDPVAVRAAKENAELNGVEARLEVYLPG--DLPK-EKADVVV--- 230

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1100983887 235 mfehvghAN-LA----QYCKTLFGAVREGGLVMNHGI 266
Cdd:pfam06325 231 -------ANiLAdpliELAPDIYALVKPGGYLILSGI 260
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
155-288 5.31e-04

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


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 40.81  E-value: 5.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 155 LRLQPGEYLLDVGCGWGGLARFAAREFGVK--VFGITLSKEQLALARERVKAEGLeDQVDLQLLD-YRDLPQDGRFDKVv 231
Cdd:pfam01135  69 LELKPGMRVLEIGSGSGYLTACFARMVGEVgrVVSIEHIPELVEIARRNLEKLGL-ENVIVVVGDgRQGWPEFAPYDAI- 146

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1100983887 232 svgmfeHVGhANLAQYCKTLFGAVREGG-LVMnhgitakhtdgrPVGRGAGEFIERYV 288
Cdd:pfam01135 147 ------HVG-AAAPEIPEALIDQLKEGGrLVI------------PVGPNGNQVLQQFD 185
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
 155-248 7.88e-04

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 40.72  E-value: 7.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 155 LRLQPGEYLLDVGCGWGGLARFAAREFGVKVFGITLSKEQLALARERVKAeglEDQVDLQLLDY--RDLPQDgRFDKVVS 232
Cdd:PTZ00098   48 IELNENSKVLDIGSGLGGGCKYINEKYGAHVHGVDICEKMVNIAKLRNSD---KNKIEFEANDIlkKDFPEN-TFDMIYS 123

                          90
                  ....*....|....*....
gi 1100983887 233 VGMFEHVGHAN---LAQYC 248
Cdd:PTZ00098  124 RDAILHLSYADkkkLFEKC 142
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
158-232 1.34e-03

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 40.02  E-value: 1.34e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1100983887 158 QPGEYLLDVGCGWGGLARFAAREFGVKVFGITLSKEQLALARERVKAEGLEDQVDLQLLDYRDLPQDGRFDKVVS 232
Cdd:COG4076    34 KPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNPDIAAVARRIIAANGLSDRITVINADATDLDLPEKADVIIS 108
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
 153-200 1.77e-03

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


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 40.10  E-value: 1.77e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1100983887 153 RKLRLQPGEYLLDVGCgwGGLARFA---AREFGVKVFGITLSKEQLALARE 200
Cdd:COG1064   156 RRAGVGPGDRVAVIGA--GGLGHLAvqiAKALGAEVIAVDRSPEKLELARE 204
MetW pfam07021
Methionine biosynthesis protein MetW; This family consists of several bacterial and one ...
 157-231 5.73e-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: 37.82  E-value: 5.73e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1100983887 157 LQPGEYLLDVGCGWGGLARFAAREFGVKVFGITLSKEQLAlareRVKAEGL---EDQVDLQLLDYrdlpQDGRFDKVV 231
Cdd:pfam07021  11 IPPGSRVLDLGCGDGTLLYLLKEEKGVDGYGIELDAAGVA----ECVAKGLyviQGDLDEGLEHF----PDKSFDYVI 80
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 151-270 6.59e-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: 38.07  E-value: 6.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100983887 151 LCRKLRLQPGEYLLDVGCGwgGLARFA---AREFGVKVFGITLSKEQLALARErVKAEGLEDQVDLQLLDYRDLPQDGRF 227
Cdd:cd05188   126 LRRAGVLKPGDTVLVLGAG--GVGLLAaqlAKAAGARVIVTDRSDEKLELAKE-LGADHVIDYKEEDLEEELRLTGGGGA 202

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1100983887 228 DKVvsvgmFEHVGHANLAQyckTLFGAVREGGLVMNHGITAKH 270
Cdd:cd05188   203 DVV-----IDAVGGPETLA---QALRLLRPGGRIVVVGGTSGG 237
 
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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