|
Name |
Accession |
Description |
Interval |
E-value |
| CMAS |
pfam02353 |
Mycolic acid cyclopropane synthetase; This family consist of ... |
106-372 |
4.58e-113 |
|
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: 331.21 E-value: 4.58e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488322222 106 SKKRSQEDIHSHYDLGNDFYKKWLDQTMTYSCAYFKTPEDTLEQAQVNKVHHILDKLFIKEGDTLLDIGCGWGTLILTAV 185
Cdd:pfam02353 1 SKTRDAENIQAHYDLSNDFFALFLDPTMTYSCAYFERPDMTLEEAQQAKLDLILDKLGLKPGMTLLDIGCGWGGLMRRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488322222 186 KEYGAKATGITLSEEQFHHIRHIIEKEGLQDRMTVKLMDYRDLKGEsFDHITSVGMFEHVGAENLHEYFDVVQRNLAPKG 265
Cdd:pfam02353 81 ERYDVNVVGLTLSKNQYKLARKRVAAEGLARKVEVLLQDYRDFDEP-FDRIVSVGMFEHVGHENYDTFFKKLYNLLPPGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488322222 266 TALIHGI------SRQQGGAKNAWINRYIFPGGYIPGVTELVGHMTENDLQVIDLESLRRDYQLTLEHWTKNFHNIEAEI 339
Cdd:pfam02353 160 LMLLHTItglhpdETSERGLPLKFIDKYIFPGGELPSISMIVESSSEAGFTVEDVESLRPHYAKTLDLWAENLQANKDEA 239
|
250 260 270
....*....|....*....|....*....|...
gi 488322222 340 VDEKGERFYRMWDLYLQACAASFQASNIDVIQY 372
Cdd:pfam02353 240 IALQSEEFYRMWMLYLTGCAVAFRIGYIDVHQF 272
|
|
| cyclopro_CfaB |
NF040703 |
C17 cyclopropane fatty acid synthase CfaB; |
20-377 |
1.52e-106 |
|
C17 cyclopropane fatty acid synthase CfaB;
Pssm-ID: 468667 [Multi-domain] Cd Length: 393 Bit Score: 318.86 E-value: 1.52e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488322222 20 QVTYWDGTVKEYGQgsgDPVFKIVFNEKIPVKDLlNNASL-TLGEAYMDRKIEIEGDI-----------QALIYDvynqK 87
Cdd:NF040703 17 RLRLWDGKQLDLGP---SPRVTLVVKDPSLLSQL-THPSLdLLGSAYVEGRLDLEGPImevirvgdelsQALLGD----D 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488322222 88 DSFLHnakfikwlPKESHSKKRSQEDIHSHYDLGNDFYKKWLDQTMTYSCAYFKTPEDTLEQAQVNKVHHILDKLFIKEG 167
Cdd:NF040703 89 DEAPP--------ERTAHDKATDAAAISYHYDLSNDFYALWLDPDMVYSCAYFETGTEDLAQAQQAKLRHLCRKLRLQPG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488322222 168 DTLLDIGCGWGTLILTAVKEYGAKATGITLSEEQFHHIRHIIEKEGLQDRMTVKLMDYRDLKG-ESFDHITSVGMFEHVG 246
Cdd:NF040703 161 ERLLDVGCGWGGLARFAAREFGVEVFGITLSKEQLKLARERVAAEGLQDRVQLELLDYRDLPQdGRFDKVVSVGMFEHVG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488322222 247 AENLHEYFDVVQRNLAPKGTALIHGIS------RQQGGAKNAWINRYIFPGGYIPGVTELVGHMTENDLQVIDLESLRRD 320
Cdd:NF040703 241 HANLPLYCQRLFGAVRPGGLVMNHGITarhtdgRPVGRGAGEFIGRYVFPHGELPHLATITASISEAGLEVVDVESLRLH 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488322222 321 YQLTLEHWTKnfhNIEAEIVDEKG---ERFYRMWDLYLQACAASFQASNIDVIQYLLVHP 377
Cdd:NF040703 321 YARTLEHWSA---RLEARLDEAARlvpERALRIWRLYLAGCAYGFARGWINLHQILAVKP 377
|
|
| PRK11705 |
PRK11705 |
cyclopropane fatty acyl phospholipid synthase; |
48-374 |
2.26e-92 |
|
cyclopropane fatty acyl phospholipid synthase;
Pssm-ID: 183282 Cd Length: 383 Bit Score: 282.12 E-value: 2.26e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488322222 48 IPVKD------LLNNASLTLGEAYMDrkieieG--DIQALiydvynqkDSFLH-------NAKFIKWLPKESH------- 105
Cdd:PRK11705 39 IQVHNprffkrVLQEGSLGLGESYMD------GwwDCDRL--------DEFFSrvlraglDEKLPHHLKDTLRilrarlf 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488322222 106 ---SKKRSQEDIHSHYDLGNDFYKKWLDQTMTYSCAYFKTpEDTLEQAQVNKVHHILDKLFIKEGDTLLDIGCGWGTLIL 182
Cdd:PRK11705 105 nlqSKKRAWIVGKEHYDLGNDLFEAMLDPRMQYSCGYWKD-ADTLEEAQEAKLDLICRKLQLKPGMRVLDIGCGWGGLAR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488322222 183 TAVKEYGAKATGITLSEEQFHHIRhiiEK-EGLQdrMTVKLMDYRDLKGeSFDHITSVGMFEHVGAENLHEYFDVVQRNL 261
Cdd:PRK11705 184 YAAEHYGVSVVGVTISAEQQKLAQ---ERcAGLP--VEIRLQDYRDLNG-QFDRIVSVGMFEHVGPKNYRTYFEVVRRCL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488322222 262 APKGTALIHGI-SRQQGGAKNAWINRYIFPGGYIPGVTELvGHMTENDLQVIDLESLRRDYQLTLEHWTKNFHNIEAEIV 340
Cdd:PRK11705 258 KPDGLFLLHTIgSNKTDTNVDPWINKYIFPNGCLPSVRQI-AQASEGLFVMEDWHNFGADYDRTLMAWHENFEAAWPELA 336
|
330 340 350
....*....|....*....|....*....|....
gi 488322222 341 DEKGERFYRMWDLYLQACAASFQASNIDVIQYLL 374
Cdd:PRK11705 337 DNYSERFYRMWRYYLLSCAGAFRARDIQLWQVVF 370
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
116-271 |
1.83e-78 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 238.68 E-value: 1.83e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488322222 116 SHYDLGNDFYKKWLDQTMTYSCAYFKTPEDTLEQAQVNKVHHILDKLFIKEGDTLLDIGCGWGTLILTAVKEYGAKATGI 195
Cdd:COG2230 1 HHYDLGNDFYRLFLDPTMTYSCAYFEDPDDTLEEAQEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488322222 196 TLSEEQFHHIRHIIEKEGLQDRMTVKLMDYRDLKG-ESFDHITSVGMFEHVGAENLHEYFDVVQRNLAPKGTALIHG 271
Cdd:COG2230 81 TLSPEQLEYARERAAEAGLADRVEVRLADYRDLPAdGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLLHT 157
|
|
| mycolic_MTase |
NF040660 |
cyclopropane mycolic acid synthase family methyltransferase; Members of this family include ... |
112-375 |
7.80e-60 |
|
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: 195.37 E-value: 7.80e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488322222 112 EDIHSHYDLGNDFYKKWLDQTMTYSCAYFKTPEDTLEQAQVNKVHHILDKLFIKEGDTLLDIGCGWGTLILTAVKEYGAK 191
Cdd:NF040660 6 EDVQAHYDLSDDFFALFLDPTQTYSCAYFERDDMTLEEAQIAKIDLALGKLNLEPGMTLLDIGCGWGATMRRAVEKYDVN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488322222 192 ATGITLSEEQFHHIRHIIEKEGLQDRMTVKLMDYRDLKgESFDHITSVGMFEHVGAENLHEYFDVVQRNLAPKGTALIHG 271
Cdd:NF040660 86 VVGLTLSKNQAAHVQQVLDEIDTPRSRRVLLQGWEEFD-EPVDRIVSIGAFEHFGHERYDDFFKRAYNILPADGRMLLHT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488322222 272 IS-------RQQGGAKNAWINRY-------IFPGGYIPGVTELVGHMTENDLQVIDLESLRRDYQLTLEHWTKNFHNIEA 337
Cdd:NF040660 165 ITglhrkemHERGLPLTMELARFikfivteIFPGGRLPSIEMVVEHAEKAGFTVTRVQSLQPHYARTLDLWADALQAHKD 244
|
250 260 270
....*....|....*....|....*....|....*...
gi 488322222 338 EIVDEKGERFYRMWDLYLQACAASFQASNIDVIQYLLV 375
Cdd:NF040660 245 EAIAIQSEEVYERYMKYLTGCAKLFRDGYIDVNQFTLA 282
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
169-270 |
3.73e-11 |
|
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: 59.37 E-value: 3.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488322222 169 TLLDIGCGWGTLILTAVKEYGAKATGITLSEEQFHHIRhIIEKEGLQDRMTVKLMDYRDL---KGESFDHITSVGMFEHV 245
Cdd:cd02440 1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELAR-KAAAALLADNVEVLKGDAEELppeADESFDVIISDPPLHHL 79
|
90 100
....*....|....*....|....*
gi 488322222 246 gAENLHEYFDVVQRNLAPKGTALIH 270
Cdd:cd02440 80 -VEDLARFLEEARRLLKPGGVLVLT 103
|
|
| PKS_MT |
smart00828 |
Methyltransferase in polyketide synthase (PKS) enzymes; |
171-233 |
3.06e-04 |
|
Methyltransferase in polyketide synthase (PKS) enzymes;
Pssm-ID: 214839 [Multi-domain] Cd Length: 224 Bit Score: 41.63 E-value: 3.06e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488322222 171 LDIGCGWGT-LILTAVKEYGAKATGITLSEEQFHHIRHIIEKEGLQDRMTVKlmdYRDLKGESF 233
Cdd:smart00828 4 LDFGCGYGSdLIDLAERHPHLQLHGYTISPEQAEVGRERIRALGLQGRIRIF---YRDSAKDPF 64
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CMAS |
pfam02353 |
Mycolic acid cyclopropane synthetase; This family consist of ... |
106-372 |
4.58e-113 |
|
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: 331.21 E-value: 4.58e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488322222 106 SKKRSQEDIHSHYDLGNDFYKKWLDQTMTYSCAYFKTPEDTLEQAQVNKVHHILDKLFIKEGDTLLDIGCGWGTLILTAV 185
Cdd:pfam02353 1 SKTRDAENIQAHYDLSNDFFALFLDPTMTYSCAYFERPDMTLEEAQQAKLDLILDKLGLKPGMTLLDIGCGWGGLMRRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488322222 186 KEYGAKATGITLSEEQFHHIRHIIEKEGLQDRMTVKLMDYRDLKGEsFDHITSVGMFEHVGAENLHEYFDVVQRNLAPKG 265
Cdd:pfam02353 81 ERYDVNVVGLTLSKNQYKLARKRVAAEGLARKVEVLLQDYRDFDEP-FDRIVSVGMFEHVGHENYDTFFKKLYNLLPPGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488322222 266 TALIHGI------SRQQGGAKNAWINRYIFPGGYIPGVTELVGHMTENDLQVIDLESLRRDYQLTLEHWTKNFHNIEAEI 339
Cdd:pfam02353 160 LMLLHTItglhpdETSERGLPLKFIDKYIFPGGELPSISMIVESSSEAGFTVEDVESLRPHYAKTLDLWAENLQANKDEA 239
|
250 260 270
....*....|....*....|....*....|...
gi 488322222 340 VDEKGERFYRMWDLYLQACAASFQASNIDVIQY 372
Cdd:pfam02353 240 IALQSEEFYRMWMLYLTGCAVAFRIGYIDVHQF 272
|
|
| cyclopro_CfaB |
NF040703 |
C17 cyclopropane fatty acid synthase CfaB; |
20-377 |
1.52e-106 |
|
C17 cyclopropane fatty acid synthase CfaB;
Pssm-ID: 468667 [Multi-domain] Cd Length: 393 Bit Score: 318.86 E-value: 1.52e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488322222 20 QVTYWDGTVKEYGQgsgDPVFKIVFNEKIPVKDLlNNASL-TLGEAYMDRKIEIEGDI-----------QALIYDvynqK 87
Cdd:NF040703 17 RLRLWDGKQLDLGP---SPRVTLVVKDPSLLSQL-THPSLdLLGSAYVEGRLDLEGPImevirvgdelsQALLGD----D 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488322222 88 DSFLHnakfikwlPKESHSKKRSQEDIHSHYDLGNDFYKKWLDQTMTYSCAYFKTPEDTLEQAQVNKVHHILDKLFIKEG 167
Cdd:NF040703 89 DEAPP--------ERTAHDKATDAAAISYHYDLSNDFYALWLDPDMVYSCAYFETGTEDLAQAQQAKLRHLCRKLRLQPG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488322222 168 DTLLDIGCGWGTLILTAVKEYGAKATGITLSEEQFHHIRHIIEKEGLQDRMTVKLMDYRDLKG-ESFDHITSVGMFEHVG 246
Cdd:NF040703 161 ERLLDVGCGWGGLARFAAREFGVEVFGITLSKEQLKLARERVAAEGLQDRVQLELLDYRDLPQdGRFDKVVSVGMFEHVG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488322222 247 AENLHEYFDVVQRNLAPKGTALIHGIS------RQQGGAKNAWINRYIFPGGYIPGVTELVGHMTENDLQVIDLESLRRD 320
Cdd:NF040703 241 HANLPLYCQRLFGAVRPGGLVMNHGITarhtdgRPVGRGAGEFIGRYVFPHGELPHLATITASISEAGLEVVDVESLRLH 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488322222 321 YQLTLEHWTKnfhNIEAEIVDEKG---ERFYRMWDLYLQACAASFQASNIDVIQYLLVHP 377
Cdd:NF040703 321 YARTLEHWSA---RLEARLDEAARlvpERALRIWRLYLAGCAYGFARGWINLHQILAVKP 377
|
|
| PRK11705 |
PRK11705 |
cyclopropane fatty acyl phospholipid synthase; |
48-374 |
2.26e-92 |
|
cyclopropane fatty acyl phospholipid synthase;
Pssm-ID: 183282 Cd Length: 383 Bit Score: 282.12 E-value: 2.26e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488322222 48 IPVKD------LLNNASLTLGEAYMDrkieieG--DIQALiydvynqkDSFLH-------NAKFIKWLPKESH------- 105
Cdd:PRK11705 39 IQVHNprffkrVLQEGSLGLGESYMD------GwwDCDRL--------DEFFSrvlraglDEKLPHHLKDTLRilrarlf 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488322222 106 ---SKKRSQEDIHSHYDLGNDFYKKWLDQTMTYSCAYFKTpEDTLEQAQVNKVHHILDKLFIKEGDTLLDIGCGWGTLIL 182
Cdd:PRK11705 105 nlqSKKRAWIVGKEHYDLGNDLFEAMLDPRMQYSCGYWKD-ADTLEEAQEAKLDLICRKLQLKPGMRVLDIGCGWGGLAR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488322222 183 TAVKEYGAKATGITLSEEQFHHIRhiiEK-EGLQdrMTVKLMDYRDLKGeSFDHITSVGMFEHVGAENLHEYFDVVQRNL 261
Cdd:PRK11705 184 YAAEHYGVSVVGVTISAEQQKLAQ---ERcAGLP--VEIRLQDYRDLNG-QFDRIVSVGMFEHVGPKNYRTYFEVVRRCL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488322222 262 APKGTALIHGI-SRQQGGAKNAWINRYIFPGGYIPGVTELvGHMTENDLQVIDLESLRRDYQLTLEHWTKNFHNIEAEIV 340
Cdd:PRK11705 258 KPDGLFLLHTIgSNKTDTNVDPWINKYIFPNGCLPSVRQI-AQASEGLFVMEDWHNFGADYDRTLMAWHENFEAAWPELA 336
|
330 340 350
....*....|....*....|....*....|....
gi 488322222 341 DEKGERFYRMWDLYLQACAASFQASNIDVIQYLL 374
Cdd:PRK11705 337 DNYSERFYRMWRYYLLSCAGAFRARDIQLWQVVF 370
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
116-271 |
1.83e-78 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 238.68 E-value: 1.83e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488322222 116 SHYDLGNDFYKKWLDQTMTYSCAYFKTPEDTLEQAQVNKVHHILDKLFIKEGDTLLDIGCGWGTLILTAVKEYGAKATGI 195
Cdd:COG2230 1 HHYDLGNDFYRLFLDPTMTYSCAYFEDPDDTLEEAQEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488322222 196 TLSEEQFHHIRHIIEKEGLQDRMTVKLMDYRDLKG-ESFDHITSVGMFEHVGAENLHEYFDVVQRNLAPKGTALIHG 271
Cdd:COG2230 81 TLSPEQLEYARERAAEAGLADRVEVRLADYRDLPAdGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLLHT 157
|
|
| mycolic_MTase |
NF040660 |
cyclopropane mycolic acid synthase family methyltransferase; Members of this family include ... |
112-375 |
7.80e-60 |
|
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: 195.37 E-value: 7.80e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488322222 112 EDIHSHYDLGNDFYKKWLDQTMTYSCAYFKTPEDTLEQAQVNKVHHILDKLFIKEGDTLLDIGCGWGTLILTAVKEYGAK 191
Cdd:NF040660 6 EDVQAHYDLSDDFFALFLDPTQTYSCAYFERDDMTLEEAQIAKIDLALGKLNLEPGMTLLDIGCGWGATMRRAVEKYDVN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488322222 192 ATGITLSEEQFHHIRHIIEKEGLQDRMTVKLMDYRDLKgESFDHITSVGMFEHVGAENLHEYFDVVQRNLAPKGTALIHG 271
Cdd:NF040660 86 VVGLTLSKNQAAHVQQVLDEIDTPRSRRVLLQGWEEFD-EPVDRIVSIGAFEHFGHERYDDFFKRAYNILPADGRMLLHT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488322222 272 IS-------RQQGGAKNAWINRY-------IFPGGYIPGVTELVGHMTENDLQVIDLESLRRDYQLTLEHWTKNFHNIEA 337
Cdd:NF040660 165 ITglhrkemHERGLPLTMELARFikfivteIFPGGRLPSIEMVVEHAEKAGFTVTRVQSLQPHYARTLDLWADALQAHKD 244
|
250 260 270
....*....|....*....|....*....|....*...
gi 488322222 338 EIVDEKGERFYRMWDLYLQACAASFQASNIDVIQYLLV 375
Cdd:NF040660 245 EAIAIQSEEVYERYMKYLTGCAKLFRDGYIDVNQFTLA 282
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
171-265 |
5.16e-19 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 81.07 E-value: 5.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488322222 171 LDIGCGWGTLILTAVKEYGAKATGITLSEEQFHHIRHIIEKEGLqdRMTVKLMDYRDL--KGESFDHITSVGMFEHVGAE 248
Cdd:pfam13649 2 LDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAEDLpfPDGSFDLVVSSGVLHHLPDP 79
|
90
....*....|....*..
gi 488322222 249 NLHEYFDVVQRNLAPKG 265
Cdd:pfam13649 80 DLEAALREIARVLKPGG 96
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
156-274 |
1.51e-15 |
|
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis
Pssm-ID: 441828 [Multi-domain] Cd Length: 143 Bit Score: 73.10 E-value: 1.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488322222 156 HHILDKLFIKEGDTLLDIGCGWGTLILtAVKEYGAKATGITLSEEQFHHIRHIIEKEGLqdRMTVKLMDYRDL--KGESF 233
Cdd:COG2226 12 EALLAALGLRPGARVLDLGCGTGRLAL-ALAERGARVTGVDISPEMLELARERAAEAGL--NVEFVVGDAEDLpfPDGSF 88
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 488322222 234 DHITSVGMFEHVgaENLHEYFDVVQRNLAPKGTALIHGISR 274
Cdd:COG2226 89 DLVISSFVLHHL--PDPERALAEIARVLKPGGRLVVVDFSP 127
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
154-269 |
2.40e-14 |
|
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: 69.28 E-value: 2.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488322222 154 KVHHILDKLfIKEGDTLLDIGCGWGTLiLTAVKEYGAKATGITLSEEQFHHIRHIIEKEGLqdrmTVKLMDYRDL--KGE 231
Cdd:COG2227 13 RLAALLARL-LPAGGRVLDVGCGTGRL-ALALARRGADVTGVDISPEALEIARERAAELNV----DFVQGDLEDLplEDG 86
|
90 100 110
....*....|....*....|....*....|....*...
gi 488322222 232 SFDHITSVGMFEHVgaENLHEYFDVVQRNLAPKGTALI 269
Cdd:COG2227 87 SFDLVICSEVLEHL--PDPAALLRELARLLKPGGLLLL 122
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
165-276 |
3.83e-14 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 70.72 E-value: 3.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488322222 165 KEGDTLLDIGCGWGTLILTAVKEYGAKATGITLSEEQFHHIRHIIEKEGLqDRMTVKLMDYRDLKG---ESFDHITSVGM 241
Cdd:COG0500 25 PKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAGL-GNVEFLVADLAELDPlpaESFDLVVAFGV 103
|
90 100 110
....*....|....*....|....*....|....*
gi 488322222 242 FEHVGAENLHEYFDVVQRNLAPKGTALIHGISRQQ 276
Cdd:COG0500 104 LHHLPPEEREALLRELARALKPGGVLLLSASDAAA 138
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
169-270 |
3.73e-11 |
|
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: 59.37 E-value: 3.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488322222 169 TLLDIGCGWGTLILTAVKEYGAKATGITLSEEQFHHIRhIIEKEGLQDRMTVKLMDYRDL---KGESFDHITSVGMFEHV 245
Cdd:cd02440 1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELAR-KAAAALLADNVEVLKGDAEELppeADESFDVIISDPPLHHL 79
|
90 100
....*....|....*....|....*
gi 488322222 246 gAENLHEYFDVVQRNLAPKGTALIH 270
Cdd:cd02440 80 -VEDLARFLEEARRLLKPGGVLVLT 103
|
|
| Methyltransf_11 |
pfam08241 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
171-269 |
7.39e-10 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 462406 [Multi-domain] Cd Length: 94 Bit Score: 55.36 E-value: 7.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488322222 171 LDIGCGWGtLILTAVKEYGAKATGITLSEEQFHHIRHIIEKEGLQDRmtvkLMDYRDL--KGESFDHITSVGMFEHVgaE 248
Cdd:pfam08241 1 LDVGCGTG-LLTELLARLGARVTGVDISPEMLELAREKAPREGLTFV----VGDAEDLpfPDNSFDLVLSSEVLHHV--E 73
|
90 100
....*....|....*....|.
gi 488322222 249 NLHEYFDVVQRNLAPKGTALI 269
Cdd:pfam08241 74 DPERALREIARVLKPGGILII 94
|
|
| COG4976 |
COG4976 |
Predicted methyltransferase, contains TPR repeat [General function prediction only]; |
149-265 |
1.10e-09 |
|
Predicted methyltransferase, contains TPR repeat [General function prediction only];
Pssm-ID: 444001 [Multi-domain] Cd Length: 181 Bit Score: 57.32 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488322222 149 QAQVNKVHHILDKLFIKEGDTLLDIGCGWGtLILTAVKEYGAKATGITLSEEQfhhIRHIIEKeGLQDRMTVklMDYRDL 228
Cdd:COG4976 29 EAPALLAEELLARLPPGPFGRVLDLGCGTG-LLGEALRPRGYRLTGVDLSEEM---LAKAREK-GVYDRLLV--ADLADL 101
|
90 100 110
....*....|....*....|....*....|....*....
gi 488322222 229 K--GESFDHITSVGMFEHVGaeNLHEYFDVVQRNLAPKG 265
Cdd:COG4976 102 AepDGRFDLIVAADVLTYLG--DLAAVFAGVARALKPGG 138
|
|
| Methyltransf_12 |
pfam08242 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
171-265 |
4.90e-09 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 53.14 E-value: 4.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488322222 171 LDIGCGWGTLILTAVKEY-GAKATGITLSEEQFHHIRHIIEKEGLQD--RMTVKLMDYRDLKGESFDHITSVGMFEHVga 247
Cdd:pfam08242 1 LEIGCGTGTLLRALLEALpGLEYTGLDISPAALEAARERLAALGLLNavRVELFQLDLGELDPGSFDVVVASNVLHHL-- 78
|
90
....*....|....*...
gi 488322222 248 ENLHEYFDVVQRNLAPKG 265
Cdd:pfam08242 79 ADPRAVLRNIRRLLKPGG 96
|
|
| TrmN6 |
COG4123 |
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ... |
164-270 |
1.64e-08 |
|
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: 54.77 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488322222 164 IKEGDTLLDIGCGWGTL-ILTAVKEYGAKATGITLSEEQFHHIRHIIEKEGLQDRMTVKLMDYRD----LKGESFDHITS 238
Cdd:COG4123 35 VKKGGRVLDLGTGTGVIaLMLAQRSPGARITGVEIQPEAAELARRNVALNGLEDRITVIHGDLKEfaaeLPPGSFDLVVS 114
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 488322222 239 ------VGMFE-----------HVGAENLHEYFDVVQRNLAPKGT-ALIH 270
Cdd:COG4123 115 nppyfkAGSGRkspdearaiarHEDALTLEDLIRAAARLLKPGGRfALIH 164
|
|
| Methyltransf_23 |
pfam13489 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
157-270 |
1.48e-07 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 404385 [Multi-domain] Cd Length: 162 Bit Score: 50.50 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488322222 157 HILDKLF--IKEGDTLLDIGCGWGTLiLTAVKEYGAKATGITLSEEQfhhirhiIEKEGLQDRMTVKLMDYRDLKGESFD 234
Cdd:pfam13489 11 DLLLRLLpkLPSPGRVLDFGCGTGIF-LRLLRAQGFSVTGVDPSPIA-------IERALLNVRFDQFDEQEAAVPAGKFD 82
|
90 100 110
....*....|....*....|....*....|....*.
gi 488322222 235 HITSVGMFEHVgaENLHEYFDVVQRNLAPKGTALIH 270
Cdd:pfam13489 83 VIVAREVLEHV--PDPPALLRQIAALLKPGGLLLLS 116
|
|
| Tam |
COG4106 |
Trans-aconitate methyltransferase [Energy production and conversion]; |
166-269 |
4.01e-07 |
|
Trans-aconitate methyltransferase [Energy production and conversion];
Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 47.90 E-value: 4.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488322222 166 EGDTLLDIGCGWGTLILTAVKEY-GAKATGITLSEEQFHHIRHiiekegLQDRMTVKLMDYRDLK-GESFDHITSVGMFE 243
Cdd:COG4106 1 PPRRVLDLGCGTGRLTALLAERFpGARVTGVDLSPEMLARARA------RLPNVRFVVADLRDLDpPEPFDLVVSNAALH 74
|
90 100
....*....|....*....|....*.
gi 488322222 244 HVgaENLHEYFDVVQRNLAPKGTALI 269
Cdd:COG4106 75 WL--PDHAALLARLAAALAPGGVLAV 98
|
|
| PLN02244 |
PLN02244 |
tocopherol O-methyltransferase |
165-269 |
4.21e-06 |
|
tocopherol O-methyltransferase
Pssm-ID: 215135 [Multi-domain] Cd Length: 340 Bit Score: 48.20 E-value: 4.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488322222 165 KEGDTLLDIGCGWGTLILTAVKEYGAKATGITLSEEQFHHIRHIIEKEGLQDRMTVKLMDYRDLKGE--SFDHITSVGMF 242
Cdd:PLN02244 117 KRPKRIVDVGCGIGGSSRYLARKYGANVKGITLSPVQAARANALAAAQGLSDKVSFQVADALNQPFEdgQFDLVWSMESG 196
|
90 100
....*....|....*....|....*..
gi 488322222 243 EHVgaENLHEYFDVVQRNLAPKGTALI 269
Cdd:PLN02244 197 EHM--PDKRKFVQELARVAAPGGRIII 221
|
|
| PKS_MT |
smart00828 |
Methyltransferase in polyketide synthase (PKS) enzymes; |
171-233 |
3.06e-04 |
|
Methyltransferase in polyketide synthase (PKS) enzymes;
Pssm-ID: 214839 [Multi-domain] Cd Length: 224 Bit Score: 41.63 E-value: 3.06e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488322222 171 LDIGCGWGT-LILTAVKEYGAKATGITLSEEQFHHIRHIIEKEGLQDRMTVKlmdYRDLKGESF 233
Cdd:smart00828 4 LDFGCGYGSdLIDLAERHPHLQLHGYTISPEQAEVGRERIRALGLQGRIRIF---YRDSAKDPF 64
|
|
| Methyltransf_31 |
pfam13847 |
Methyltransferase domain; This family appears to have methyltransferase activity. |
164-269 |
5.41e-04 |
|
Methyltransferase domain; This family appears to have methyltransferase activity.
Pssm-ID: 463998 [Multi-domain] Cd Length: 150 Bit Score: 40.09 E-value: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488322222 164 IKEGDTLLDIGCGWGTLILTAVKEYG--AKATGITLSEEQFHHIRHIIEKEGLqDRMTVKLMDYRDL----KGESFDHIT 237
Cdd:pfam13847 1 IDKGMRVLDLGCGTGHLSFELAEELGpnAEVVGIDISEEAIEKARENAQKLGF-DNVEFEQGDIEELpellEDDKFDVVI 79
|
90 100 110
....*....|....*....|....*....|..
gi 488322222 238 SVGMFEHVGaeNLHEYFDVVQRNLAPKGTALI 269
Cdd:pfam13847 80 SNCVLNHIP--DPDKVLQEILRVLKPGGRLII 109
|
|
| PRK08317 |
PRK08317 |
hypothetical protein; Provisional |
156-269 |
9.78e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 181382 [Multi-domain] Cd Length: 241 Bit Score: 40.31 E-value: 9.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488322222 156 HHILDKLFIKEGDTLLDIGCGWGTLILTAVKEYGA--KATGITLSEEQFHHIRHIIEKEGLQDRMTVKLMDYRDLKGESF 233
Cdd:PRK08317 9 ARTFELLAVQPGDRVLDVGCGPGNDARELARRVGPegRVVGIDRSEAMLALAKERAAGLGPNVEFVRGDADGLPFPDGSF 88
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 488322222 234 DHITSVGMFEHVgaEN----LHEyfdvVQRNLAPKGTALI 269
Cdd:PRK08317 89 DAVRSDRVLQHL--EDparaLAE----IARVLRPGGRVVV 122
|
|
| RsmC |
COG2813 |
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ... |
159-269 |
2.33e-03 |
|
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA G1207 methylase RsmC is part of the Pathway/BioSystem: 16S rRNA modification
Pssm-ID: 442062 [Multi-domain] Cd Length: 191 Bit Score: 38.63 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488322222 159 LDKLFIKEGDTLLDIGCGWGTLILTAVKEYGAKAtgITLSEEQFHHI---RHIIEKEGLQDrMTVKLMD-YRDLKGESFD 234
Cdd:COG2813 42 LEHLPEPLGGRVLDLGCGYGVIGLALAKRNPEAR--VTLVDVNARAVelaRANAAANGLEN-VEVLWSDgLSGVPDGSFD 118
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 488322222 235 HITS-----VGMFEHVGAenLHEYFDVVQRNLAPKGTALI 269
Cdd:COG2813 119 LILSnppfhAGRAVDKEV--AHALIADAARHLRPGGELWL 156
|
|
| PrmA |
pfam06325 |
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ... |
163-276 |
2.40e-03 |
|
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: 39.56 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488322222 163 FIKEGDTLLDIGCGWGTLILTAVKEYGAKATGITLSEEQFHHIRHIIEKEGLQDRMTVKLMDyrDLKGESFDhitsvGMF 242
Cdd:pfam06325 158 LVKPGESVLDVGCGSGILAIAALKLGAKKVVGVDIDPVAVRAAKENAELNGVEARLEVYLPG--DLPKEKAD-----VVV 230
|
90 100 110
....*....|....*....|....*....|....
gi 488322222 243 EHVGAENLHEYFDVVQRNLAPKGTALIHGISRQQ 276
Cdd:pfam06325 231 ANILADPLIELAPDIYALVKPGGYLILSGILKEQ 264
|
|
| cbiT |
PRK00377 |
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional |
159-220 |
6.25e-03 |
|
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
Pssm-ID: 234740 Cd Length: 198 Bit Score: 37.47 E-value: 6.25e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488322222 159 LDKLFIKEGDTLLDIGCGWGTLILTA---VKEyGAKATGITLSEEQFHHIRHIIEKEGLQDRMTV 220
Cdd:PRK00377 33 LSKLRLRKGDMILDIGCGTGSVTVEAsllVGE-TGKVYAVDKDEKAINLTRRNAEKFGVLNNIVL 96
|
|
| PTZ00098 |
PTZ00098 |
phosphoethanolamine N-methyltransferase; Provisional |
144-269 |
7.74e-03 |
|
phosphoethanolamine N-methyltransferase; Provisional
Pssm-ID: 173391 [Multi-domain] Cd Length: 263 Bit Score: 37.64 E-value: 7.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488322222 144 EDTLEQAQVNKVHHILDKLFIKEGDTLLDIGCGWGTLILTAVKEYGAKATGITLSEEQFHhirhiIEKEGLQDRMTVKL- 222
Cdd:PTZ00098 30 EDYISSGGIEATTKILSDIELNENSKVLDIGSGLGGGCKYINEKYGAHVHGVDICEKMVN-----IAKLRNSDKNKIEFe 104
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 488322222 223 -MDY--RDLKGESFDHITSVGMFEHVGAENLHEYFDVVQRNLAPKGTALI 269
Cdd:PTZ00098 105 aNDIlkKDFPENTFDMIYSRDAILHLSYADKKKLFEKCYKWLKPNGILLI 154
|
|
| |
