|
Name |
Accession |
Description |
Interval |
E-value |
| cyclopro_CfaB |
NF040703 |
C17 cyclopropane fatty acid synthase CfaB; |
13-388 |
4.95e-115 |
|
C17 cyclopropane fatty acid synthase CfaB;
Pssm-ID: 468667 [Multi-domain] Cd Length: 393 Bit Score: 340.43 E-value: 4.95e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488227243 13 RSFSLPVEVNYWDGttKQYgDTDTPPQIKINIHEEIPMKEITSNASLALGEAYVDHRIEIEGSIQALIN--DAYQQAnsf 90
Cdd:NF040703 10 RNLQLPLRLRLWDG--KQL-DLGPSPRVTLVVKDPSLLSQLTHPSLDLLGSAYVEGRLDLEGPIMEVIRvgDELSQA--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488227243 91 LRGKDYLKwLPKKEKHTKQKNKEDIHAHYDLGNDFYKLWLDPTLTYSCAYFNTPEDTLEQAQINKVHHILDKLFIKEGET 170
Cdd:NF040703 84 LLGDDDEA-PPERTAHDKATDAAAISYHYDLSNDFYALWLDPDMVYSCAYFETGTEDLAQAQQAKLRHLCRKLRLQPGER 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488227243 171 LLDIGCGWGTLMFTAAKEYNVKATGITLSEEQYDLITKRIKEEHLEDKCRVLLMDYRELKG-ETFDHITSVGMFEHVGSE 249
Cdd:NF040703 163 LLDVGCGWGGLARFAAREFGVEVFGITLSKEQLKLARERVAAEGLQDRVQLELLDYRDLPQdGRFDKVVSVGMFEHVGHA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488227243 250 NLEGYFKVVKDLLKPKGTALIHGIS------RQQGGATNAWINKYIFPGGYVPGVTELVDNITKNDLQLIDLESLRRDYQ 323
Cdd:NF040703 243 NLPLYCQRLFGAVRPGGLVMNHGITarhtdgRPVGRGAGEFIGRYVFPHGELPHLATITASISEAGLEVVDVESLRLHYA 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488227243 324 LTLEHWTKNFHQVQDQVTKEMGDSFYRMWDLYLQACAASFESSNIDVIQYLLVQP---GNNDIPMHRA 388
Cdd:NF040703 323 RTLEHWSARLEARLDEAARLVPERALRIWRLYLAGCAYGFARGWINLHQILAVKPladGSHELPWTRA 390
|
|
| CMAS |
pfam02353 |
Mycolic acid cyclopropane synthetase; This family consist of ... |
108-373 |
2.97e-114 |
|
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: 333.91 E-value: 2.97e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488227243 108 KQKNKEDIHAHYDLGNDFYKLWLDPTLTYSCAYFNTPEDTLEQAQINKVHHILDKLFIKEGETLLDIGCGWGTLMFTAAK 187
Cdd:pfam02353 2 KTRDAENIQAHYDLSNDFFALFLDPTMTYSCAYFERPDMTLEEAQQAKLDLILDKLGLKPGMTLLDIGCGWGGLMRRAAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488227243 188 EYNVKATGITLSEEQYDLITKRIKEEHLEDKCRVLLMDYRELKGEtFDHITSVGMFEHVGSENLEGYFKVVKDLLKPKGT 267
Cdd:pfam02353 82 RYDVNVVGLTLSKNQYKLARKRVAAEGLARKVEVLLQDYRDFDEP-FDRIVSVGMFEHVGHENYDTFFKKLYNLLPPGGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488227243 268 ALIHGI------SRQQGGATNAWINKYIFPGGYVPGVTELVDNITKNDLQLIDLESLRRDYQLTLEHWTKNFHQVQDQVT 341
Cdd:pfam02353 161 MLLHTItglhpdETSERGLPLKFIDKYIFPGGELPSISMIVESSSEAGFTVEDVESLRPHYAKTLDLWAENLQANKDEAI 240
|
250 260 270
....*....|....*....|....*....|..
gi 488227243 342 KEMGDSFYRMWDLYLQACAASFESSNIDVIQY 373
Cdd:pfam02353 241 ALQSEEFYRMWMLYLTGCAVAFRIGYIDVHQF 272
|
|
| PRK11705 |
PRK11705 |
cyclopropane fatty acyl phospholipid synthase; |
42-379 |
5.36e-89 |
|
cyclopropane fatty acyl phospholipid synthase;
Pssm-ID: 183282 Cd Length: 383 Bit Score: 273.65 E-value: 5.36e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488227243 42 INIHEEIPMKEITSNASLALGEAYVD------------HRIeiegsIQALINdayQQANSFLRgkDYLKWLPKK--EKHT 107
Cdd:PRK11705 39 IQVHNPRFFKRVLQEGSLGLGESYMDgwwdcdrldeffSRV-----LRAGLD---EKLPHHLK--DTLRILRARlfNLQS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488227243 108 KQKNKEDIHAHYDLGNDFYKLWLDPTLTYSCAYFNTpEDTLEQAQINKVHHILDKLFIKEGETLLDIGCGWGTLMFTAAK 187
Cdd:PRK11705 109 KKRAWIVGKEHYDLGNDLFEAMLDPRMQYSCGYWKD-ADTLEEAQEAKLDLICRKLQLKPGMRVLDIGCGWGGLARYAAE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488227243 188 EYNVKATGITLSEEQYDLITKRIKEEHLEdkcrVLLMDYRELKGeTFDHITSVGMFEHVGSENLEGYFKVVKDLLKPKGT 267
Cdd:PRK11705 188 HYGVSVVGVTISAEQQKLAQERCAGLPVE----IRLQDYRDLNG-QFDRIVSVGMFEHVGPKNYRTYFEVVRRCLKPDGL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488227243 268 ALIHGI-SRQQGGATNAWINKYIFPGGYVPGVTELVDNiTKNDLQLIDLESLRRDYQLTLEHWTKNFHQVQDQVTKEMGD 346
Cdd:PRK11705 263 FLLHTIgSNKTDTNVDPWINKYIFPNGCLPSVRQIAQA-SEGLFVMEDWHNFGADYDRTLMAWHENFEAAWPELADNYSE 341
|
330 340 350
....*....|....*....|....*....|...
gi 488227243 347 SFYRMWDLYLQACAASFESSNIDVIQYLLVQPG 379
Cdd:PRK11705 342 RFYRMWRYYLLSCAGAFRARDIQLWQVVFSPRG 374
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
117-272 |
8.78e-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: 8.78e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488227243 117 AHYDLGNDFYKLWLDPTLTYSCAYFNTPEDTLEQAQINKVHHILDKLFIKEGETLLDIGCGWGTLMFTAAKEYNVKATGI 196
Cdd:COG2230 1 HHYDLGNDFYRLFLDPTMTYSCAYFEDPDDTLEEAQEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488227243 197 TLSEEQYDLITKRIKEEHLEDKCRVLLMDYRELKG-ETFDHITSVGMFEHVGSENLEGYFKVVKDLLKPKGTALIHG 272
Cdd:COG2230 81 TLSPEQLEYARERAAEAGLADRVEVRLADYRDLPAdGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLLHT 157
|
|
| mycolic_MTase |
NF040660 |
cyclopropane mycolic acid synthase family methyltransferase; Members of this family include ... |
113-377 |
1.36e-64 |
|
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: 207.70 E-value: 1.36e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488227243 113 EDIHAHYDLGNDFYKLWLDPTLTYSCAYFNTPEDTLEQAQINKVHHILDKLFIKEGETLLDIGCGWGTLMFTAAKEYNVK 192
Cdd:NF040660 6 EDVQAHYDLSDDFFALFLDPTQTYSCAYFERDDMTLEEAQIAKIDLALGKLNLEPGMTLLDIGCGWGATMRRAVEKYDVN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488227243 193 ATGITLSEEQYDLITKRIKEEHLEDKCRVLLMDYRELKgETFDHITSVGMFEHVGSENLEGYFKVVKDLLKPKGTALIHG 272
Cdd:NF040660 86 VVGLTLSKNQAAHVQQVLDEIDTPRSRRVLLQGWEEFD-EPVDRIVSIGAFEHFGHERYDDFFKRAYNILPADGRMLLHT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488227243 273 IS-------RQQGGATNAWINKY-------IFPGGYVPGVTELVDNITKNDLQLIDLESLRRDYQLTLEHWTKNFHQVQD 338
Cdd:NF040660 165 ITglhrkemHERGLPLTMELARFikfivteIFPGGRLPSIEMVVEHAEKAGFTVTRVQSLQPHYARTLDLWADALQAHKD 244
|
250 260 270
....*....|....*....|....*....|....*....
gi 488227243 339 QVTKEMGDSFYRMWDLYLQACAASFESSNIDVIQYLLVQ 377
Cdd:NF040660 245 EAIAIQSEEVYERYMKYLTGCAKLFRDGYIDVNQFTLAK 283
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
170-271 |
3.28e-12 |
|
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).
Pssm-ID: 100107 [Multi-domain] Cd Length: 107 Bit Score: 62.45 E-value: 3.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488227243 170 TLLDIGCGWGTLMFTAAKEYNVKATGITLSEEQYDLItKRIKEEHLEDKCRVLLMDYREL---KGETFDHITSVGMFEHV 246
Cdd:cd02440 1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELA-RKAAAALLADNVEVLKGDAEELppeADESFDVIISDPPLHHL 79
|
90 100
....*....|....*....|....*
gi 488227243 247 GsENLEGYFKVVKDLLKPKGTALIH 271
Cdd:cd02440 80 V-EDLARFLEEARRLLKPGGVLVLT 103
|
|
| PKS_MT |
smart00828 |
Methyltransferase in polyketide synthase (PKS) enzymes; |
172-234 |
3.73e-03 |
|
Methyltransferase in polyketide synthase (PKS) enzymes;
Pssm-ID: 214839 [Multi-domain] Cd Length: 224 Bit Score: 38.55 E-value: 3.73e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488227243 172 LDIGCGWGTLMFTAAKEY-NVKATGITLSEEQYDLITKRIKEEHLEDKCRVLlmdYRELKGETF 234
Cdd:smart00828 4 LDFGCGYGSDLIDLAERHpHLQLHGYTISPEQAEVGRERIRALGLQGRIRIF---YRDSAKDPF 64
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| cyclopro_CfaB |
NF040703 |
C17 cyclopropane fatty acid synthase CfaB; |
13-388 |
4.95e-115 |
|
C17 cyclopropane fatty acid synthase CfaB;
Pssm-ID: 468667 [Multi-domain] Cd Length: 393 Bit Score: 340.43 E-value: 4.95e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488227243 13 RSFSLPVEVNYWDGttKQYgDTDTPPQIKINIHEEIPMKEITSNASLALGEAYVDHRIEIEGSIQALIN--DAYQQAnsf 90
Cdd:NF040703 10 RNLQLPLRLRLWDG--KQL-DLGPSPRVTLVVKDPSLLSQLTHPSLDLLGSAYVEGRLDLEGPIMEVIRvgDELSQA--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488227243 91 LRGKDYLKwLPKKEKHTKQKNKEDIHAHYDLGNDFYKLWLDPTLTYSCAYFNTPEDTLEQAQINKVHHILDKLFIKEGET 170
Cdd:NF040703 84 LLGDDDEA-PPERTAHDKATDAAAISYHYDLSNDFYALWLDPDMVYSCAYFETGTEDLAQAQQAKLRHLCRKLRLQPGER 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488227243 171 LLDIGCGWGTLMFTAAKEYNVKATGITLSEEQYDLITKRIKEEHLEDKCRVLLMDYRELKG-ETFDHITSVGMFEHVGSE 249
Cdd:NF040703 163 LLDVGCGWGGLARFAAREFGVEVFGITLSKEQLKLARERVAAEGLQDRVQLELLDYRDLPQdGRFDKVVSVGMFEHVGHA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488227243 250 NLEGYFKVVKDLLKPKGTALIHGIS------RQQGGATNAWINKYIFPGGYVPGVTELVDNITKNDLQLIDLESLRRDYQ 323
Cdd:NF040703 243 NLPLYCQRLFGAVRPGGLVMNHGITarhtdgRPVGRGAGEFIGRYVFPHGELPHLATITASISEAGLEVVDVESLRLHYA 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488227243 324 LTLEHWTKNFHQVQDQVTKEMGDSFYRMWDLYLQACAASFESSNIDVIQYLLVQP---GNNDIPMHRA 388
Cdd:NF040703 323 RTLEHWSARLEARLDEAARLVPERALRIWRLYLAGCAYGFARGWINLHQILAVKPladGSHELPWTRA 390
|
|
| CMAS |
pfam02353 |
Mycolic acid cyclopropane synthetase; This family consist of ... |
108-373 |
2.97e-114 |
|
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: 333.91 E-value: 2.97e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488227243 108 KQKNKEDIHAHYDLGNDFYKLWLDPTLTYSCAYFNTPEDTLEQAQINKVHHILDKLFIKEGETLLDIGCGWGTLMFTAAK 187
Cdd:pfam02353 2 KTRDAENIQAHYDLSNDFFALFLDPTMTYSCAYFERPDMTLEEAQQAKLDLILDKLGLKPGMTLLDIGCGWGGLMRRAAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488227243 188 EYNVKATGITLSEEQYDLITKRIKEEHLEDKCRVLLMDYRELKGEtFDHITSVGMFEHVGSENLEGYFKVVKDLLKPKGT 267
Cdd:pfam02353 82 RYDVNVVGLTLSKNQYKLARKRVAAEGLARKVEVLLQDYRDFDEP-FDRIVSVGMFEHVGHENYDTFFKKLYNLLPPGGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488227243 268 ALIHGI------SRQQGGATNAWINKYIFPGGYVPGVTELVDNITKNDLQLIDLESLRRDYQLTLEHWTKNFHQVQDQVT 341
Cdd:pfam02353 161 MLLHTItglhpdETSERGLPLKFIDKYIFPGGELPSISMIVESSSEAGFTVEDVESLRPHYAKTLDLWAENLQANKDEAI 240
|
250 260 270
....*....|....*....|....*....|..
gi 488227243 342 KEMGDSFYRMWDLYLQACAASFESSNIDVIQY 373
Cdd:pfam02353 241 ALQSEEFYRMWMLYLTGCAVAFRIGYIDVHQF 272
|
|
| PRK11705 |
PRK11705 |
cyclopropane fatty acyl phospholipid synthase; |
42-379 |
5.36e-89 |
|
cyclopropane fatty acyl phospholipid synthase;
Pssm-ID: 183282 Cd Length: 383 Bit Score: 273.65 E-value: 5.36e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488227243 42 INIHEEIPMKEITSNASLALGEAYVD------------HRIeiegsIQALINdayQQANSFLRgkDYLKWLPKK--EKHT 107
Cdd:PRK11705 39 IQVHNPRFFKRVLQEGSLGLGESYMDgwwdcdrldeffSRV-----LRAGLD---EKLPHHLK--DTLRILRARlfNLQS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488227243 108 KQKNKEDIHAHYDLGNDFYKLWLDPTLTYSCAYFNTpEDTLEQAQINKVHHILDKLFIKEGETLLDIGCGWGTLMFTAAK 187
Cdd:PRK11705 109 KKRAWIVGKEHYDLGNDLFEAMLDPRMQYSCGYWKD-ADTLEEAQEAKLDLICRKLQLKPGMRVLDIGCGWGGLARYAAE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488227243 188 EYNVKATGITLSEEQYDLITKRIKEEHLEdkcrVLLMDYRELKGeTFDHITSVGMFEHVGSENLEGYFKVVKDLLKPKGT 267
Cdd:PRK11705 188 HYGVSVVGVTISAEQQKLAQERCAGLPVE----IRLQDYRDLNG-QFDRIVSVGMFEHVGPKNYRTYFEVVRRCLKPDGL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488227243 268 ALIHGI-SRQQGGATNAWINKYIFPGGYVPGVTELVDNiTKNDLQLIDLESLRRDYQLTLEHWTKNFHQVQDQVTKEMGD 346
Cdd:PRK11705 263 FLLHTIgSNKTDTNVDPWINKYIFPNGCLPSVRQIAQA-SEGLFVMEDWHNFGADYDRTLMAWHENFEAAWPELADNYSE 341
|
330 340 350
....*....|....*....|....*....|...
gi 488227243 347 SFYRMWDLYLQACAASFESSNIDVIQYLLVQPG 379
Cdd:PRK11705 342 RFYRMWRYYLLSCAGAFRARDIQLWQVVFSPRG 374
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
117-272 |
8.78e-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: 8.78e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488227243 117 AHYDLGNDFYKLWLDPTLTYSCAYFNTPEDTLEQAQINKVHHILDKLFIKEGETLLDIGCGWGTLMFTAAKEYNVKATGI 196
Cdd:COG2230 1 HHYDLGNDFYRLFLDPTMTYSCAYFEDPDDTLEEAQEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488227243 197 TLSEEQYDLITKRIKEEHLEDKCRVLLMDYRELKG-ETFDHITSVGMFEHVGSENLEGYFKVVKDLLKPKGTALIHG 272
Cdd:COG2230 81 TLSPEQLEYARERAAEAGLADRVEVRLADYRDLPAdGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLLHT 157
|
|
| mycolic_MTase |
NF040660 |
cyclopropane mycolic acid synthase family methyltransferase; Members of this family include ... |
113-377 |
1.36e-64 |
|
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: 207.70 E-value: 1.36e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488227243 113 EDIHAHYDLGNDFYKLWLDPTLTYSCAYFNTPEDTLEQAQINKVHHILDKLFIKEGETLLDIGCGWGTLMFTAAKEYNVK 192
Cdd:NF040660 6 EDVQAHYDLSDDFFALFLDPTQTYSCAYFERDDMTLEEAQIAKIDLALGKLNLEPGMTLLDIGCGWGATMRRAVEKYDVN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488227243 193 ATGITLSEEQYDLITKRIKEEHLEDKCRVLLMDYRELKgETFDHITSVGMFEHVGSENLEGYFKVVKDLLKPKGTALIHG 272
Cdd:NF040660 86 VVGLTLSKNQAAHVQQVLDEIDTPRSRRVLLQGWEEFD-EPVDRIVSIGAFEHFGHERYDDFFKRAYNILPADGRMLLHT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488227243 273 IS-------RQQGGATNAWINKY-------IFPGGYVPGVTELVDNITKNDLQLIDLESLRRDYQLTLEHWTKNFHQVQD 338
Cdd:NF040660 165 ITglhrkemHERGLPLTMELARFikfivteIFPGGRLPSIEMVVEHAEKAGFTVTRVQSLQPHYARTLDLWADALQAHKD 244
|
250 260 270
....*....|....*....|....*....|....*....
gi 488227243 339 QVTKEMGDSFYRMWDLYLQACAASFESSNIDVIQYLLVQ 377
Cdd:NF040660 245 EAIAIQSEEVYERYMKYLTGCAKLFRDGYIDVNQFTLAK 283
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
172-266 |
1.11e-19 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 83.00 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488227243 172 LDIGCGWGTLMFTAAKEYNVKATGITLSEEQYDLITKRIKEEHLedKCRVLLMDYREL--KGETFDHITSVGMFEHVGSE 249
Cdd:pfam13649 2 LDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAEDLpfPDGSFDLVVSSGVLHHLPDP 79
|
90
....*....|....*..
gi 488227243 250 NLEGYFKVVKDLLKPKG 266
Cdd:pfam13649 80 DLEAALREIARVLKPGG 96
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
157-290 |
8.03e-16 |
|
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: 73.87 E-value: 8.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488227243 157 HHILDKLFIKEGETLLDIGCGWGTLMFTAAkEYNVKATGITLSEEQYDLITKRIKEEHLedKCRVLLMDYREL--KGETF 234
Cdd:COG2226 12 EALLAALGLRPGARVLDLGCGTGRLALALA-ERGARVTGVDISPEMLELARERAAEAGL--NVEFVVGDAEDLpfPDGSF 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 488227243 235 DHITSVGMFEHVgsENLEGYFKVVKDLLKPKGTALIHGISRQQGGATNAWINKYIF 290
Cdd:COG2226 89 DLVISSFVLHHL--PDPERALAEIARVLKPGGRLVVVDFSPPDLAELEELLAEAGF 142
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
155-270 |
1.54e-15 |
|
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis
Pssm-ID: 441829 [Multi-domain] Cd Length: 126 Bit Score: 72.36 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488227243 155 KVHHILDKLfIKEGETLLDIGCGWGTLMFTAAKEyNVKATGITLSEEQYDLITKRIKEEHLedkcRVLLMDYREL--KGE 232
Cdd:COG2227 13 RLAALLARL-LPAGGRVLDVGCGTGRLALALARR-GADVTGVDISPEALEIARERAAELNV----DFVQGDLEDLplEDG 86
|
90 100 110
....*....|....*....|....*....|....*...
gi 488227243 233 TFDHITSVGMFEHVgsENLEGYFKVVKDLLKPKGTALI 270
Cdd:COG2227 87 SFDLVICSEVLEHL--PDPAALLRELARLLKPGGLLLL 122
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
166-277 |
9.15e-15 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 72.26 E-value: 9.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488227243 166 KEGETLLDIGCGWGTLMFTAAKEYNVKATGITLSEEQYDLITKRIKEEHLeDKCRVLLMDYRELKG---ETFDHITSVGM 242
Cdd:COG0500 25 PKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAGL-GNVEFLVADLAELDPlpaESFDLVVAFGV 103
|
90 100 110
....*....|....*....|....*....|....*
gi 488227243 243 FEHVGSENLEGYFKVVKDLLKPKGTALIHGISRQQ 277
Cdd:COG0500 104 LHHLPPEEREALLRELARALKPGGVLLLSASDAAA 138
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
170-271 |
3.28e-12 |
|
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).
Pssm-ID: 100107 [Multi-domain] Cd Length: 107 Bit Score: 62.45 E-value: 3.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488227243 170 TLLDIGCGWGTLMFTAAKEYNVKATGITLSEEQYDLItKRIKEEHLEDKCRVLLMDYREL---KGETFDHITSVGMFEHV 246
Cdd:cd02440 1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELA-RKAAAALLADNVEVLKGDAEELppeADESFDVIISDPPLHHL 79
|
90 100
....*....|....*....|....*
gi 488227243 247 GsENLEGYFKVVKDLLKPKGTALIH 271
Cdd:cd02440 80 V-EDLARFLEEARRLLKPGGVLVLT 103
|
|
| TrmN6 |
COG4123 |
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ... |
165-271 |
4.29e-12 |
|
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: 65.17 E-value: 4.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488227243 165 IKEGETLLDIGCGWGTL-MFTAAKEYNVKATGITLSEEQYDLITKRIKEEHLEDKCRVLLMDYRE----LKGETFDHITS 239
Cdd:COG4123 35 VKKGGRVLDLGTGTGVIaLMLAQRSPGARITGVEIQPEAAELARRNVALNGLEDRITVIHGDLKEfaaeLPPGSFDLVVS 114
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 488227243 240 ------VGMFE-----------HVGSENLEGYFKVVKDLLKPKGT-ALIH 271
Cdd:COG4123 115 nppyfkAGSGRkspdearaiarHEDALTLEDLIRAAARLLKPGGRfALIH 164
|
|
| Methyltransf_11 |
pfam08241 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
172-270 |
2.66e-11 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 462406 [Multi-domain] Cd Length: 94 Bit Score: 59.60 E-value: 2.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488227243 172 LDIGCGWGtLMFTAAKEYNVKATGITLSEEQYDLITKRIKEEHLEdkcrVLLMDYREL--KGETFDHITSVGMFEHVgsE 249
Cdd:pfam08241 1 LDVGCGTG-LLTELLARLGARVTGVDISPEMLELAREKAPREGLT----FVVGDAEDLpfPDNSFDLVLSSEVLHHV--E 73
|
90 100
....*....|....*....|.
gi 488227243 250 NLEGYFKVVKDLLKPKGTALI 270
Cdd:pfam08241 74 DPERALREIARVLKPGGILII 94
|
|
| Methyltransf_12 |
pfam08242 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
172-266 |
1.49e-10 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 57.38 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488227243 172 LDIGCGWGTLMFTAAKEY-NVKATGITLSEEQYDLITKRIKEEHLED--KCRVLLMDYRELKGETFDHITSVGMFEHVgs 248
Cdd:pfam08242 1 LEIGCGTGTLLRALLEALpGLEYTGLDISPAALEAARERLAALGLLNavRVELFQLDLGELDPGSFDVVVASNVLHHL-- 78
|
90
....*....|....*...
gi 488227243 249 ENLEGYFKVVKDLLKPKG 266
Cdd:pfam08242 79 ADPRAVLRNIRRLLKPGG 96
|
|
| COG4976 |
COG4976 |
Predicted methyltransferase, contains TPR repeat [General function prediction only]; |
110-266 |
7.81e-09 |
|
Predicted methyltransferase, contains TPR repeat [General function prediction only];
Pssm-ID: 444001 [Multi-domain] Cd Length: 181 Bit Score: 54.62 E-value: 7.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488227243 110 KNKEDIHAHYDlgnDFYKLWlDPTLTYSCAYfNTPEDTLEqaqinkvhHILDKLFIKEGETLLDIGCG---WGTLMFTAA 186
Cdd:COG4976 2 ALDAYVEALFD---QYADSY-DAALVEDLGY-EAPALLAE--------ELLARLPPGPFGRVLDLGCGtglLGEALRPRG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488227243 187 KEYnvkaTGITLSEEQYDlitkRIKEEHLEDkcRVLLMDYRELK--GETFDHITSVGMFEHVGseNLEGYFKVVKDLLKP 264
Cdd:COG4976 69 YRL----TGVDLSEEMLA----KAREKGVYD--RLLVADLADLAepDGRFDLIVAADVLTYLG--DLAAVFAGVARALKP 136
|
..
gi 488227243 265 KG 266
Cdd:COG4976 137 GG 138
|
|
| Methyltransf_23 |
pfam13489 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
158-271 |
3.26e-07 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 404385 [Multi-domain] Cd Length: 162 Bit Score: 49.73 E-value: 3.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488227243 158 HILDKLF--IKEGETLLDIGCGWGTLMfTAAKEYNVKATGITLSEEQYDLIT-KRIKEEHLEDKCRVllmdyrelKGETF 234
Cdd:pfam13489 11 DLLLRLLpkLPSPGRVLDFGCGTGIFL-RLLRAQGFSVTGVDPSPIAIERALlNVRFDQFDEQEAAV--------PAGKF 81
|
90 100 110
....*....|....*....|....*....|....*..
gi 488227243 235 DHITSVGMFEHVgsENLEGYFKVVKDLLKPKGTALIH 271
Cdd:pfam13489 82 DVIVAREVLEHV--PDPPALLRQIAALLKPGGLLLLS 116
|
|
| Tam |
COG4106 |
Trans-aconitate methyltransferase [Energy production and conversion]; |
167-270 |
1.16e-06 |
|
Trans-aconitate methyltransferase [Energy production and conversion];
Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 46.36 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488227243 167 EGETLLDIGCGWGTLMFTAAKEY-NVKATGITLSEEqydLITK-RikeEHLEDkCRVLLMDYRELK-GETFDHITSVGMF 243
Cdd:COG4106 1 PPRRVLDLGCGTGRLTALLAERFpGARVTGVDLSPE---MLARaR---ARLPN-VRFVVADLRDLDpPEPFDLVVSNAAL 73
|
90 100
....*....|....*....|....*..
gi 488227243 244 EHVgsENLEGYFKVVKDLLKPKGTALI 270
Cdd:COG4106 74 HWL--PDHAALLARLAAALAPGGVLAV 98
|
|
| PRK08317 |
PRK08317 |
hypothetical protein; Provisional |
157-270 |
1.25e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 181382 [Multi-domain] Cd Length: 241 Bit Score: 49.16 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488227243 157 HHILDKLFIKEGETLLDIGCGWGTLMFTAAKEYNV--KATGITLSEEQYDLITKRIKEEHLEDKCRVLLMDYRELKGETF 234
Cdd:PRK08317 9 ARTFELLAVQPGDRVLDVGCGPGNDARELARRVGPegRVVGIDRSEAMLALAKERAAGLGPNVEFVRGDADGLPFPDGSF 88
|
90 100 110
....*....|....*....|....*....|....*.
gi 488227243 235 DHITSVGMFEHVgsENLEGYFKVVKDLLKPKGTALI 270
Cdd:PRK08317 89 DAVRSDRVLQHL--EDPARALAEIARVLRPGGRVVV 122
|
|
| RsmC |
COG2813 |
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ... |
160-270 |
4.67e-05 |
|
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA G1207 methylase RsmC is part of the Pathway/BioSystem: 16S rRNA modification
Pssm-ID: 442062 [Multi-domain] Cd Length: 191 Bit Score: 43.64 E-value: 4.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488227243 160 LDKLFIKEGETLLDIGCGWGTLMFTAAKEYnvKATGITLSEEQYD--LITKRIKEEHLEDKCRVLLMD-YRELKGETFDH 236
Cdd:COG2813 42 LEHLPEPLGGRVLDLGCGYGVIGLALAKRN--PEARVTLVDVNARavELARANAAANGLENVEVLWSDgLSGVPDGSFDL 119
|
90 100 110
....*....|....*....|....*....|....*....
gi 488227243 237 ITS-----VGMfeHVGSENLEGYFKVVKDLLKPKGTALI 270
Cdd:COG2813 120 ILSnppfhAGR--AVDKEVAHALIADAARHLRPGGELWL 156
|
|
| Methyltransf_31 |
pfam13847 |
Methyltransferase domain; This family appears to have methyltransferase activity. |
165-270 |
1.16e-04 |
|
Methyltransferase domain; This family appears to have methyltransferase activity.
Pssm-ID: 463998 [Multi-domain] Cd Length: 150 Bit Score: 42.02 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488227243 165 IKEGETLLDIGCGWGTLMFTAAKEYNVKA--TGITLSEE--QYDlitKRIKEEHLEDKCRVLLMDYREL----KGETFDH 236
Cdd:pfam13847 1 IDKGMRVLDLGCGTGHLSFELAEELGPNAevVGIDISEEaiEKA---RENAQKLGFDNVEFEQGDIEELpellEDDKFDV 77
|
90 100 110
....*....|....*....|....*....|....
gi 488227243 237 ITSVGMFEHVGseNLEGYFKVVKDLLKPKGTALI 270
Cdd:pfam13847 78 VISNCVLNHIP--DPDKVLQEILRVLKPGGRLII 109
|
|
| PRK09328 |
PRK09328 |
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional |
156-283 |
1.52e-03 |
|
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
Pssm-ID: 236467 [Multi-domain] Cd Length: 275 Bit Score: 40.15 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488227243 156 VHHILDKLFIKEGETLLDIGCGWGTLMFTAAKEY-NVKATGITLSEEQYDlITKRIKEEHLEDKCRVLLMD-YRELKGET 233
Cdd:PRK09328 97 VEWALEALLLKEPLRVLDLGTGSGAIALALAKERpDAEVTAVDISPEALA-VARRNAKHGLGARVEFLQGDwFEPLPGGR 175
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488227243 234 FDHITS----------------VGMFE-HV----GSENLEGYFKVVK---DLLKPKGTALI-HGIsrQQGGATNA 283
Cdd:PRK09328 176 FDLIVSnppyipeadihllqpeVRDHEpHLalfgGEDGLDFYRRIIEqapRYLKPGGWLLLeIGY--DQGEAVRA 248
|
|
| PLN02244 |
PLN02244 |
tocopherol O-methyltransferase |
150-270 |
2.95e-03 |
|
tocopherol O-methyltransferase
Pssm-ID: 215135 [Multi-domain] Cd Length: 340 Bit Score: 39.34 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488227243 150 QAQINKVHHIL-----DKLFIKEGETLLDIGCGWGTLMFTAAKEYNVKATGITLSEEQYDLITKRIKEEHLEDKCRVLLM 224
Cdd:PLN02244 96 QAQIRMIEESLawagvPDDDEKRPKRIVDVGCGIGGSSRYLARKYGANVKGITLSPVQAARANALAAAQGLSDKVSFQVA 175
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 488227243 225 DYRELKGET--FDHITSVGMFEHVGSENlegyfKVVKDLL---KPKGTALI 270
Cdd:PLN02244 176 DALNQPFEDgqFDLVWSMESGEHMPDKR-----KFVQELArvaAPGGRIII 221
|
|
| PRK07580 |
PRK07580 |
Mg-protoporphyrin IX methyl transferase; Validated |
168-237 |
3.58e-03 |
|
Mg-protoporphyrin IX methyl transferase; Validated
Pssm-ID: 236059 [Multi-domain] Cd Length: 230 Bit Score: 38.66 E-value: 3.58e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488227243 168 GETLLDIGCGWGTLMFTAAKE-YNVKATGItlSEEQYDLITKRIKEEHLEDKCRVLLMDYRELKGEtFDHI 237
Cdd:PRK07580 64 GLRILDAGCGVGSLSIPLARRgAKVVASDI--SPQMVEEARERAPEAGLAGNITFEVGDLESLLGR-FDTV 131
|
|
| PKS_MT |
smart00828 |
Methyltransferase in polyketide synthase (PKS) enzymes; |
172-234 |
3.73e-03 |
|
Methyltransferase in polyketide synthase (PKS) enzymes;
Pssm-ID: 214839 [Multi-domain] Cd Length: 224 Bit Score: 38.55 E-value: 3.73e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488227243 172 LDIGCGWGTLMFTAAKEY-NVKATGITLSEEQYDLITKRIKEEHLEDKCRVLlmdYRELKGETF 234
Cdd:smart00828 4 LDFGCGYGSDLIDLAERHpHLQLHGYTISPEQAEVGRERIRALGLQGRIRIF---YRDSAKDPF 64
|
|
| PLN02336 |
PLN02336 |
phosphoethanolamine N-methyltransferase |
160-270 |
4.01e-03 |
|
phosphoethanolamine N-methyltransferase
Pssm-ID: 177970 [Multi-domain] Cd Length: 475 Bit Score: 38.96 E-value: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488227243 160 LDKLFIKEGETLLDIGCGWGTLMFTAAKEYNVKATGITLSeeqYDLITKRIkEEHLEDKCRVLL----MDYRELKGETFD 235
Cdd:PLN02336 259 VDKLDLKPGQKVLDVGCGIGGGDFYMAENFDVHVVGIDLS---VNMISFAL-ERAIGRKCSVEFevadCTKKTYPDNSFD 334
|
90 100 110
....*....|....*....|....*....|....*
gi 488227243 236 HITSVGMFEHVgsENLEGYFKVVKDLLKPKGTALI 270
Cdd:PLN02336 335 VIYSRDTILHI--QDKPALFRSFFKWLKPGGKVLI 367
|
|
| PTZ00098 |
PTZ00098 |
phosphoethanolamine N-methyltransferase; Provisional |
145-270 |
6.83e-03 |
|
phosphoethanolamine N-methyltransferase; Provisional
Pssm-ID: 173391 [Multi-domain] Cd Length: 263 Bit Score: 38.03 E-value: 6.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488227243 145 EDTLEQAQINKVHHILDKLFIKEGETLLDIGCGWGTLMFTAAKEYNVKATGITLSEEQYDLITKRIKeehleDKCRVLLM 224
Cdd:PTZ00098 30 EDYISSGGIEATTKILSDIELNENSKVLDIGSGLGGGCKYINEKYGAHVHGVDICEKMVNIAKLRNS-----DKNKIEFE 104
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 488227243 225 DYRELKGE----TFDHITSVGMFEHVGSENLEGYFKVVKDLLKPKGTALI 270
Cdd:PTZ00098 105 ANDILKKDfpenTFDMIYSRDAILHLSYADKKKLFEKCYKWLKPNGILLI 154
|
|
| |
