|
Name |
Accession |
Description |
Interval |
E-value |
| CMAS |
pfam02353 |
Mycolic acid cyclopropane synthetase; This family consist of ... |
108-375 |
2.79e-122 |
|
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: 354.71 E-value: 2.79e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 108 SQKQSREDIHSHYDIGNDFYNKWLDPTMTYSCAYFEHEDMTLEEAQIAKVHHILDKLNSKPGGRLLDIGCGWGTLMFKAV 187
Cdd:pfam02353 1 SKTRDAENIQAHYDLSNDFFALFLDPTMTYSCAYFERPDMTLEEAQQAKLDLILDKLGLKPGMTLLDIGCGWGGLMRRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 188 QEYGLSAVGVTLSEEQYYYVRKKADDLGLSDKVKVYLVDYRDLkEEPFDYITSVGMFEHVGKENLEMYFQKVSDYLKPNG 267
Cdd:pfam02353 81 ERYDVNVVGLTLSKNQYKLARKRVAAEGLARKVEVLLQDYRDF-DEPFDRIVSVGMFEHVGHENYDTFFKKLYNLLPPGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 268 RALIHGITGQHR-----GAGVDPFIEKYIFPGGYIPNIAENVEHIMTAGLQMDDLEPLRRHYQKTLEIWNENYLEVFDEV 342
Cdd:pfam02353 160 LMLLHTITGLHPdetseRGLPLKFIDKYIFPGGELPSISMIVESSSEAGFTVEDVESLRPHYAKTLDLWAENLQANKDEA 239
|
250 260 270
....*....|....*....|....*....|...
gi 545594585 343 EKEMGRPFARMWTLYLQACAASFEAGNIDVVQY 375
Cdd:pfam02353 240 IALQSEEFYRMWMLYLTGCAVAFRIGYIDVHQF 272
|
|
| cyclopro_CfaB |
NF040703 |
C17 cyclopropane fatty acid synthase CfaB; |
18-391 |
6.29e-105 |
|
C17 cyclopropane fatty acid synthase CfaB;
Pssm-ID: 468667 [Multi-domain] Cd Length: 393 Bit Score: 315.01 E-value: 6.29e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 18 IPIAVTYWDGKTEKYGEgETQVHITFNKKFSFSELSSmPTL-VLAEAYMNEEIEIEGSIQELVTSAYRKAGSFLTDQSGf 96
Cdd:NF040703 14 LPLRLRLWDGKQLDLGP-SPRVTLVVKDPSLLSQLTH-PSLdLLGSAYVEGRLDLEGPIMEVIRVGDELSQALLGDDDE- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 97 gksMIKLLGNHSQKQSREDIHSHYDIGNDFYNKWLDPTMTYSCAYFEHEDMTLEEAQIAKVHHILDKLNSKPGGRLLDIG 176
Cdd:NF040703 91 ---APPERTAHDKATDAAAISYHYDLSNDFYALWLDPDMVYSCAYFETGTEDLAQAQQAKLRHLCRKLRLQPGERLLDVG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 177 CGWGTLMFKAVQEYGLSAVGVTLSEEQYYYVRKKADDLGLSDKVKVYLVDYRDLK-EEPFDYITSVGMFEHVGKENLEMY 255
Cdd:NF040703 168 CGWGGLARFAAREFGVEVFGITLSKEQLKLARERVAAEGLQDRVQLELLDYRDLPqDGRFDKVVSVGMFEHVGHANLPLY 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 256 FQKVSDYLKPNGRALIHGITGQH-------RGAGvdPFIEKYIFPGGYIPNIAENVEHIMTAGLQMDDLEPLRRHYQKTL 328
Cdd:NF040703 248 CQRLFGAVRPGGLVMNHGITARHtdgrpvgRGAG--EFIGRYVFPHGELPHLATITASISEAGLEVVDVESLRLHYARTL 325
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545594585 329 EIWNENYLEVFDEVEKEMGRPFARMWTLYLQACAASFEAGNIDVVQYLLTK--GASGQGLPMTRE 391
Cdd:NF040703 326 EHWSARLEARLDEAARLVPERALRIWRLYLAGCAYGFARGWINLHQILAVKplADGSHELPWTRA 390
|
|
| PRK11705 |
PRK11705 |
cyclopropane fatty acyl phospholipid synthase; |
108-379 |
1.37e-94 |
|
cyclopropane fatty acyl phospholipid synthase;
Pssm-ID: 183282 Cd Length: 383 Bit Score: 288.28 E-value: 1.37e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 108 SQKQSREDIHSHYDIGNDFYNKWLDPTMTYSCAYFEHEDmTLEEAQIAKVHHILDKLNSKPGGRLLDIGCGWGTLMFKAV 187
Cdd:PRK11705 108 SKKRAWIVGKEHYDLGNDLFEAMLDPRMQYSCGYWKDAD-TLEEAQEAKLDLICRKLQLKPGMRVLDIGCGWGGLARYAA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 188 QEYGLSAVGVTLSEEQYYYVRKKADDLglsdKVKVYLVDYRDLKEePFDYITSVGMFEHVGKENLEMYFQKVSDYLKPNG 267
Cdd:PRK11705 187 EHYGVSVVGVTISAEQQKLAQERCAGL----PVEIRLQDYRDLNG-QFDRIVSVGMFEHVGPKNYRTYFEVVRRCLKPDG 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 268 RALIHGITGQHRGAGVDPFIEKYIFPGGYIPNIAenveHIMTA--GLQ-MDDLEPLRRHYQKTLEIWNENYLEVFDEVEK 344
Cdd:PRK11705 262 LFLLHTIGSNKTDTNVDPWINKYIFPNGCLPSVR----QIAQAseGLFvMEDWHNFGADYDRTLMAWHENFEAAWPELAD 337
|
250 260 270
....*....|....*....|....*....|....*
gi 545594585 345 EMGRPFARMWTLYLQACAASFEAGNIDVVQYLLTK 379
Cdd:PRK11705 338 NYSERFYRMWRYYLLSCAGAFRARDIQLWQVVFSP 372
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
118-273 |
4.19e-81 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 245.61 E-value: 4.19e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 118 SHYDIGNDFYNKWLDPTMTYSCAYFEHEDMTLEEAQIAKVHHILDKLNSKPGGRLLDIGCGWGTLMFKAVQEYGLSAVGV 197
Cdd:COG2230 1 HHYDLGNDFYRLFLDPTMTYSCAYFEDPDDTLEEAQEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545594585 198 TLSEEQYYYVRKKADDLGLSDKVKVYLVDYRDL-KEEPFDYITSVGMFEHVGKENLEMYFQKVSDYLKPNGRALIHG 273
Cdd:COG2230 81 TLSPEQLEYARERAAEAGLADRVEVRLADYRDLpADGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLLHT 157
|
|
| mycolic_MTase |
NF040660 |
cyclopropane mycolic acid synthase family methyltransferase; Members of this family include ... |
114-379 |
3.15e-79 |
|
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: 245.45 E-value: 3.15e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 114 EDIHSHYDIGNDFYNKWLDPTMTYSCAYFEHEDMTLEEAQIAKVHHILDKLNSKPGGRLLDIGCGWGTLMFKAVQEYGLS 193
Cdd:NF040660 6 EDVQAHYDLSDDFFALFLDPTQTYSCAYFERDDMTLEEAQIAKIDLALGKLNLEPGMTLLDIGCGWGATMRRAVEKYDVN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 194 AVGVTLSEEQYYYVRKKADDLGLSDKVKVYLVDYRDLkEEPFDYITSVGMFEHVGKENLEMYFQKVSDYLKPNGRALIHG 273
Cdd:NF040660 86 VVGLTLSKNQAAHVQQVLDEIDTPRSRRVLLQGWEEF-DEPVDRIVSIGAFEHFGHERYDDFFKRAYNILPADGRMLLHT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 274 ITGQHRGAGVD-------------PFIEKYIFPGGYIPNIAENVEHIMTAGLQMDDLEPLRRHYQKTLEIWNENYLEVFD 340
Cdd:NF040660 165 ITGLHRKEMHErglpltmelarfiKFIVTEIFPGGRLPSIEMVVEHAEKAGFTVTRVQSLQPHYARTLDLWADALQAHKD 244
|
250 260 270
....*....|....*....|....*....|....*....
gi 545594585 341 EVEKEMGRPFARMWTLYLQACAASFEAGNIDVVQYLLTK 379
Cdd:NF040660 245 EAIAIQSEEVYERYMKYLTGCAKLFRDGYIDVNQFTLAK 283
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
171-272 |
1.96e-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: 60.52 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 171 RLLDIGCGWGTLMFKAVQEYGLSAVGVTLSEEQYYYVRKKAdDLGLSDKVKVYLVDYRDL---KEEPFDYITSVGMFEHV 247
Cdd:cd02440 1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAA-AALLADNVEVLKGDAEELppeADESFDVIISDPPLHHL 79
|
90 100
....*....|....*....|....*
gi 545594585 248 gKENLEMYFQKVSDYLKPNGRALIH 272
Cdd:cd02440 80 -VEDLARFLEEARRLLKPGGVLVLT 103
|
|
| PKS_MT |
smart00828 |
Methyltransferase in polyketide synthase (PKS) enzymes; |
171-271 |
4.90e-06 |
|
Methyltransferase in polyketide synthase (PKS) enzymes;
Pssm-ID: 214839 [Multi-domain] Cd Length: 224 Bit Score: 47.41 E-value: 4.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 171 RLLDIGCGWGT-LMFKAVQEYGLSAVGVTLSEEQYYYVRKKADDLGLSDKVKVYlvdYRDLKEEPF-DYITSVGMFEHVG 248
Cdd:smart00828 2 RVLDFGCGYGSdLIDLAERHPHLQLHGYTISPEQAEVGRERIRALGLQGRIRIF---YRDSAKDPFpDTYDLVFGFEVIH 78
|
90 100
....*....|....*....|....*..
gi 545594585 249 ----KENLemyFQKVSDYLKPNGRALI 271
Cdd:smart00828 79 hikdKMDL---FSNISRHLKDGGHLVL 102
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CMAS |
pfam02353 |
Mycolic acid cyclopropane synthetase; This family consist of ... |
108-375 |
2.79e-122 |
|
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: 354.71 E-value: 2.79e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 108 SQKQSREDIHSHYDIGNDFYNKWLDPTMTYSCAYFEHEDMTLEEAQIAKVHHILDKLNSKPGGRLLDIGCGWGTLMFKAV 187
Cdd:pfam02353 1 SKTRDAENIQAHYDLSNDFFALFLDPTMTYSCAYFERPDMTLEEAQQAKLDLILDKLGLKPGMTLLDIGCGWGGLMRRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 188 QEYGLSAVGVTLSEEQYYYVRKKADDLGLSDKVKVYLVDYRDLkEEPFDYITSVGMFEHVGKENLEMYFQKVSDYLKPNG 267
Cdd:pfam02353 81 ERYDVNVVGLTLSKNQYKLARKRVAAEGLARKVEVLLQDYRDF-DEPFDRIVSVGMFEHVGHENYDTFFKKLYNLLPPGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 268 RALIHGITGQHR-----GAGVDPFIEKYIFPGGYIPNIAENVEHIMTAGLQMDDLEPLRRHYQKTLEIWNENYLEVFDEV 342
Cdd:pfam02353 160 LMLLHTITGLHPdetseRGLPLKFIDKYIFPGGELPSISMIVESSSEAGFTVEDVESLRPHYAKTLDLWAENLQANKDEA 239
|
250 260 270
....*....|....*....|....*....|...
gi 545594585 343 EKEMGRPFARMWTLYLQACAASFEAGNIDVVQY 375
Cdd:pfam02353 240 IALQSEEFYRMWMLYLTGCAVAFRIGYIDVHQF 272
|
|
| cyclopro_CfaB |
NF040703 |
C17 cyclopropane fatty acid synthase CfaB; |
18-391 |
6.29e-105 |
|
C17 cyclopropane fatty acid synthase CfaB;
Pssm-ID: 468667 [Multi-domain] Cd Length: 393 Bit Score: 315.01 E-value: 6.29e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 18 IPIAVTYWDGKTEKYGEgETQVHITFNKKFSFSELSSmPTL-VLAEAYMNEEIEIEGSIQELVTSAYRKAGSFLTDQSGf 96
Cdd:NF040703 14 LPLRLRLWDGKQLDLGP-SPRVTLVVKDPSLLSQLTH-PSLdLLGSAYVEGRLDLEGPIMEVIRVGDELSQALLGDDDE- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 97 gksMIKLLGNHSQKQSREDIHSHYDIGNDFYNKWLDPTMTYSCAYFEHEDMTLEEAQIAKVHHILDKLNSKPGGRLLDIG 176
Cdd:NF040703 91 ---APPERTAHDKATDAAAISYHYDLSNDFYALWLDPDMVYSCAYFETGTEDLAQAQQAKLRHLCRKLRLQPGERLLDVG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 177 CGWGTLMFKAVQEYGLSAVGVTLSEEQYYYVRKKADDLGLSDKVKVYLVDYRDLK-EEPFDYITSVGMFEHVGKENLEMY 255
Cdd:NF040703 168 CGWGGLARFAAREFGVEVFGITLSKEQLKLARERVAAEGLQDRVQLELLDYRDLPqDGRFDKVVSVGMFEHVGHANLPLY 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 256 FQKVSDYLKPNGRALIHGITGQH-------RGAGvdPFIEKYIFPGGYIPNIAENVEHIMTAGLQMDDLEPLRRHYQKTL 328
Cdd:NF040703 248 CQRLFGAVRPGGLVMNHGITARHtdgrpvgRGAG--EFIGRYVFPHGELPHLATITASISEAGLEVVDVESLRLHYARTL 325
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545594585 329 EIWNENYLEVFDEVEKEMGRPFARMWTLYLQACAASFEAGNIDVVQYLLTK--GASGQGLPMTRE 391
Cdd:NF040703 326 EHWSARLEARLDEAARLVPERALRIWRLYLAGCAYGFARGWINLHQILAVKplADGSHELPWTRA 390
|
|
| PRK11705 |
PRK11705 |
cyclopropane fatty acyl phospholipid synthase; |
108-379 |
1.37e-94 |
|
cyclopropane fatty acyl phospholipid synthase;
Pssm-ID: 183282 Cd Length: 383 Bit Score: 288.28 E-value: 1.37e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 108 SQKQSREDIHSHYDIGNDFYNKWLDPTMTYSCAYFEHEDmTLEEAQIAKVHHILDKLNSKPGGRLLDIGCGWGTLMFKAV 187
Cdd:PRK11705 108 SKKRAWIVGKEHYDLGNDLFEAMLDPRMQYSCGYWKDAD-TLEEAQEAKLDLICRKLQLKPGMRVLDIGCGWGGLARYAA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 188 QEYGLSAVGVTLSEEQYYYVRKKADDLglsdKVKVYLVDYRDLKEePFDYITSVGMFEHVGKENLEMYFQKVSDYLKPNG 267
Cdd:PRK11705 187 EHYGVSVVGVTISAEQQKLAQERCAGL----PVEIRLQDYRDLNG-QFDRIVSVGMFEHVGPKNYRTYFEVVRRCLKPDG 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 268 RALIHGITGQHRGAGVDPFIEKYIFPGGYIPNIAenveHIMTA--GLQ-MDDLEPLRRHYQKTLEIWNENYLEVFDEVEK 344
Cdd:PRK11705 262 LFLLHTIGSNKTDTNVDPWINKYIFPNGCLPSVR----QIAQAseGLFvMEDWHNFGADYDRTLMAWHENFEAAWPELAD 337
|
250 260 270
....*....|....*....|....*....|....*
gi 545594585 345 EMGRPFARMWTLYLQACAASFEAGNIDVVQYLLTK 379
Cdd:PRK11705 338 NYSERFYRMWRYYLLSCAGAFRARDIQLWQVVFSP 372
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
118-273 |
4.19e-81 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 245.61 E-value: 4.19e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 118 SHYDIGNDFYNKWLDPTMTYSCAYFEHEDMTLEEAQIAKVHHILDKLNSKPGGRLLDIGCGWGTLMFKAVQEYGLSAVGV 197
Cdd:COG2230 1 HHYDLGNDFYRLFLDPTMTYSCAYFEDPDDTLEEAQEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545594585 198 TLSEEQYYYVRKKADDLGLSDKVKVYLVDYRDL-KEEPFDYITSVGMFEHVGKENLEMYFQKVSDYLKPNGRALIHG 273
Cdd:COG2230 81 TLSPEQLEYARERAAEAGLADRVEVRLADYRDLpADGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLLHT 157
|
|
| mycolic_MTase |
NF040660 |
cyclopropane mycolic acid synthase family methyltransferase; Members of this family include ... |
114-379 |
3.15e-79 |
|
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: 245.45 E-value: 3.15e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 114 EDIHSHYDIGNDFYNKWLDPTMTYSCAYFEHEDMTLEEAQIAKVHHILDKLNSKPGGRLLDIGCGWGTLMFKAVQEYGLS 193
Cdd:NF040660 6 EDVQAHYDLSDDFFALFLDPTQTYSCAYFERDDMTLEEAQIAKIDLALGKLNLEPGMTLLDIGCGWGATMRRAVEKYDVN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 194 AVGVTLSEEQYYYVRKKADDLGLSDKVKVYLVDYRDLkEEPFDYITSVGMFEHVGKENLEMYFQKVSDYLKPNGRALIHG 273
Cdd:NF040660 86 VVGLTLSKNQAAHVQQVLDEIDTPRSRRVLLQGWEEF-DEPVDRIVSIGAFEHFGHERYDDFFKRAYNILPADGRMLLHT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 274 ITGQHRGAGVD-------------PFIEKYIFPGGYIPNIAENVEHIMTAGLQMDDLEPLRRHYQKTLEIWNENYLEVFD 340
Cdd:NF040660 165 ITGLHRKEMHErglpltmelarfiKFIVTEIFPGGRLPSIEMVVEHAEKAGFTVTRVQSLQPHYARTLDLWADALQAHKD 244
|
250 260 270
....*....|....*....|....*....|....*....
gi 545594585 341 EVEKEMGRPFARMWTLYLQACAASFEAGNIDVVQYLLTK 379
Cdd:NF040660 245 EAIAIQSEEVYERYMKYLTGCAKLFRDGYIDVNQFTLAK 283
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
173-267 |
9.17e-20 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 83.38 E-value: 9.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 173 LDIGCGWGTLMFKAVQEYGLSAVGVTLSEEQYYYVRKKADDLGLsdKVKVYLVDYRDL--KEEPFDYITSVGMFEHVGKE 250
Cdd:pfam13649 2 LDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAEDLpfPDGSFDLVVSSGVLHHLPDP 79
|
90
....*....|....*..
gi 545594585 251 NLEMYFQKVSDYLKPNG 267
Cdd:pfam13649 80 DLEAALREIARVLKPGG 96
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
155-271 |
6.99e-18 |
|
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: 79.29 E-value: 6.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 155 AKVHHILDKLnSKPGGRLLDIGCGWGTLMfKAVQEYGLSAVGVTLSEEQYYYVRKKADDLGlsdkVKVYLVDYRDL--KE 232
Cdd:COG2227 12 RRLAALLARL-LPAGGRVLDVGCGTGRLA-LALARRGADVTGVDISPEALEIARERAAELN----VDFVQGDLEDLplED 85
|
90 100 110
....*....|....*....|....*....|....*....
gi 545594585 233 EPFDYITSVGMFEHVgkENLEMYFQKVSDYLKPNGRALI 271
Cdd:COG2227 86 GSFDLVICSEVLEHL--PDPAALLRELARLLKPGGLLLL 122
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
158-271 |
5.14e-17 |
|
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: 77.34 E-value: 5.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 158 HHILDKLNSKPGGRLLDIGCGWGTLMFkAVQEYGLSAVGVTLSEEQYYYVRKKADDLGLsdKVKVYLVDYRDL--KEEPF 235
Cdd:COG2226 12 EALLAALGLRPGARVLDLGCGTGRLAL-ALAERGARVTGVDISPEMLELARERAAEAGL--NVEFVVGDAEDLpfPDGSF 88
|
90 100 110
....*....|....*....|....*....|....*.
gi 545594585 236 DYITSVGMFEHVgkENLEMYFQKVSDYLKPNGRALI 271
Cdd:COG2226 89 DLVISSFVLHHL--PDPERALAEIARVLKPGGRLVV 122
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
167-273 |
1.78e-16 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 77.26 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 167 KPGGRLLDIGCGWGTLMFKAVQEYGLSAVGVTLSEEQYYYVRKKADDLGLSdKVKVYLVDYRDLKE---EPFDYITSVGM 243
Cdd:COG0500 25 PKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAGLG-NVEFLVADLAELDPlpaESFDLVVAFGV 103
|
90 100 110
....*....|....*....|....*....|
gi 545594585 244 FEHVGKENLEMYFQKVSDYLKPNGRALIHG 273
Cdd:COG0500 104 LHHLPPEEREALLRELARALKPGGVLLLSA 133
|
|
| COG4976 |
COG4976 |
Predicted methyltransferase, contains TPR repeat [General function prediction only]; |
156-268 |
8.72e-12 |
|
Predicted methyltransferase, contains TPR repeat [General function prediction only];
Pssm-ID: 444001 [Multi-domain] Cd Length: 181 Bit Score: 63.48 E-value: 8.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 156 KVHHILDKLNSKPGGRLLDIGCGWGtLMFKAVQEYGLSAVGVTLSEEqyyyVRKKADDLGLSDkvKVYLVDYRDLKE--E 233
Cdd:COG4976 34 LAEELLARLPPGPFGRVLDLGCGTG-LLGEALRPRGYRLTGVDLSEE----MLAKAREKGVYD--RLLVADLADLAEpdG 106
|
90 100 110
....*....|....*....|....*....|....*
gi 545594585 234 PFDYITSVGMFEHVGkeNLEMYFQKVSDYLKPNGR 268
Cdd:COG4976 107 RFDLIVAADVLTYLG--DLAAVFAGVARALKPGGL 139
|
|
| Methyltransf_11 |
pfam08241 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
173-271 |
9.45e-12 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 462406 [Multi-domain] Cd Length: 94 Bit Score: 60.76 E-value: 9.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 173 LDIGCGWGtLMFKAVQEYGLSAVGVTLSEEQYYYVRKKADDlglsDKVKVYLVDYRDL--KEEPFDYITSVGMFEHVgkE 250
Cdd:pfam08241 1 LDVGCGTG-LLTELLARLGARVTGVDISPEMLELAREKAPR----EGLTFVVGDAEDLpfPDNSFDLVLSSEVLHHV--E 73
|
90 100
....*....|....*....|.
gi 545594585 251 NLEMYFQKVSDYLKPNGRALI 271
Cdd:pfam08241 74 DPERALREIARVLKPGGILII 94
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
171-272 |
1.96e-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: 60.52 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 171 RLLDIGCGWGTLMFKAVQEYGLSAVGVTLSEEQYYYVRKKAdDLGLSDKVKVYLVDYRDL---KEEPFDYITSVGMFEHV 247
Cdd:cd02440 1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAA-AALLADNVEVLKGDAEELppeADESFDVIISDPPLHHL 79
|
90 100
....*....|....*....|....*
gi 545594585 248 gKENLEMYFQKVSDYLKPNGRALIH 272
Cdd:cd02440 80 -VEDLARFLEEARRLLKPGGVLVLT 103
|
|
| Methyltransf_23 |
pfam13489 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
167-272 |
2.47e-11 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 404385 [Multi-domain] Cd Length: 162 Bit Score: 61.68 E-value: 2.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 167 KPGGRLLDIGCGWGTLMfKAVQEYGLSAVGVTLSEEQYYYVRKKADDlglsdkvKVYLVDYRDLKEEPFDYITSVGMFEH 246
Cdd:pfam13489 21 PSPGRVLDFGCGTGIFL-RLLRAQGFSVTGVDPSPIAIERALLNVRF-------DQFDEQEAAVPAGKFDVIVAREVLEH 92
|
90 100
....*....|....*....|....*.
gi 545594585 247 VgkENLEMYFQKVSDYLKPNGRALIH 272
Cdd:pfam13489 93 V--PDPPALLRQIAALLKPGGLLLLS 116
|
|
| Methyltransf_12 |
pfam08242 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
173-268 |
8.28e-11 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 58.15 E-value: 8.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 173 LDIGCGWGTLMFKAVQEY-GLSAVGVTLSEEQYYYVRKKADDLGLSDKVKVYLVDYRDLKEEP--FDYITSVGMFEHVgk 249
Cdd:pfam08242 1 LEIGCGTGTLLRALLEALpGLEYTGLDISPAALEAARERLAALGLLNAVRVELFQLDLGELDPgsFDVVVASNVLHHL-- 78
|
90
....*....|....*....
gi 545594585 250 ENLEMYFQKVSDYLKPNGR 268
Cdd:pfam08242 79 ADPRAVLRNIRRLLKPGGV 97
|
|
| Tam |
COG4106 |
Trans-aconitate methyltransferase [Energy production and conversion]; |
168-271 |
5.39e-10 |
|
Trans-aconitate methyltransferase [Energy production and conversion];
Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 55.99 E-value: 5.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 168 PGGRLLDIGCGWGTLMFKAVQEY-GLSAVGVTLSEEQYYYVRKKADDlglsdkVKVYLVDYRDLK-EEPFDYITSVGMFE 245
Cdd:COG4106 1 PPRRVLDLGCGTGRLTALLAERFpGARVTGVDLSPEMLARARARLPN------VRFVVADLRDLDpPEPFDLVVSNAALH 74
|
90 100
....*....|....*....|....*.
gi 545594585 246 HVgkENLEMYFQKVSDYLKPNGRALI 271
Cdd:COG4106 75 WL--PDHAALLARLAAALAPGGVLAV 98
|
|
| RsmC |
COG2813 |
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ... |
161-271 |
3.99e-09 |
|
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: 55.97 E-value: 3.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 161 LDKLNSKPGGRLLDIGCGWGTLMFKAVQEYGLSAvgVTLSEEQY---YYVRKKADDLGLSDkVKVYLVD-YRDLKEEPFD 236
Cdd:COG2813 42 LEHLPEPLGGRVLDLGCGYGVIGLALAKRNPEAR--VTLVDVNAravELARANAAANGLEN-VEVLWSDgLSGVPDGSFD 118
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 545594585 237 YITS-----VGMfeHVGKENLEMYFQKVSDYLKPNGRALI 271
Cdd:COG2813 119 LILSnppfhAGR--AVDKEVAHALIADAARHLRPGGELWL 156
|
|
| Methyltransf_31 |
pfam13847 |
Methyltransferase domain; This family appears to have methyltransferase activity. |
167-271 |
5.37e-09 |
|
Methyltransferase domain; This family appears to have methyltransferase activity.
Pssm-ID: 463998 [Multi-domain] Cd Length: 150 Bit Score: 54.73 E-value: 5.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 167 KPGGRLLDIGCGWGTLMFKAVQEYGLSA--VGVTLSEEQYYYVRKKADDLGLSDkVKVYLVDYRDLKE----EPFDYITS 240
Cdd:pfam13847 2 DKGMRVLDLGCGTGHLSFELAEELGPNAevVGIDISEEAIEKARENAQKLGFDN-VEFEQGDIEELPElledDKFDVVIS 80
|
90 100 110
....*....|....*....|....*....|.
gi 545594585 241 VGMFEHVGkeNLEMYFQKVSDYLKPNGRALI 271
Cdd:pfam13847 81 NCVLNHIP--DPDKVLQEILRVLKPGGRLII 109
|
|
| ubiE |
PRK00216 |
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ... |
162-271 |
1.96e-06 |
|
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;
Pssm-ID: 234689 [Multi-domain] Cd Length: 239 Bit Score: 48.61 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 162 DKLNSKPGGRLLDIGCGWGTLMFKAVQEYGLSA--VGVTLSEEQYYYVRKKADDLGLSDKVKVYLVDYRDL--KEEPFDY 237
Cdd:PRK00216 45 KWLGVRPGDKVLDLACGTGDLAIALAKAVGKTGevVGLDFSEGMLAVGREKLRDLGLSGNVEFVQGDAEALpfPDNSFDA 124
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 545594585 238 ITsVGmFehvGKENL--------EMYfqKVsdyLKPNGRALI 271
Cdd:PRK00216 125 VT-IA-F---GLRNVpdidkalrEMY--RV---LKPGGRLVI 156
|
|
| PKS_MT |
smart00828 |
Methyltransferase in polyketide synthase (PKS) enzymes; |
171-271 |
4.90e-06 |
|
Methyltransferase in polyketide synthase (PKS) enzymes;
Pssm-ID: 214839 [Multi-domain] Cd Length: 224 Bit Score: 47.41 E-value: 4.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 171 RLLDIGCGWGT-LMFKAVQEYGLSAVGVTLSEEQYYYVRKKADDLGLSDKVKVYlvdYRDLKEEPF-DYITSVGMFEHVG 248
Cdd:smart00828 2 RVLDFGCGYGSdLIDLAERHPHLQLHGYTISPEQAEVGRERIRALGLQGRIRIF---YRDSAKDPFpDTYDLVFGFEVIH 78
|
90 100
....*....|....*....|....*..
gi 545594585 249 ----KENLemyFQKVSDYLKPNGRALI 271
Cdd:smart00828 79 hikdKMDL---FSNISRHLKDGGHLVL 102
|
|
| MTS |
pfam05175 |
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ... |
161-271 |
6.99e-06 |
|
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: 46.04 E-value: 6.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 161 LDKLNSKPGGRLLDIGCGWGTLMFKAVQEYGlsAVGVTLSEEQYYYV---RKKADDLGLsDKVKVYLVD-YRDLKEEPFD 236
Cdd:pfam05175 24 LEHLPKDLSGKVLDLGCGAGVLGAALAKESP--DAELTMVDINARALesaRENLAANGL-ENGEVVASDvYSGVEDGKFD 100
|
90 100 110
....*....|....*....|....*....|....*....
gi 545594585 237 YITSVGMFeHVGKEN----LEMYFQKVSDYLKPNGRALI 271
Cdd:pfam05175 101 LIISNPPF-HAGLATtynvAQRFIADAKRHLRPGGELWI 138
|
|
| TrmN6 |
COG4123 |
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ... |
167-272 |
7.28e-06 |
|
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: 46.68 E-value: 7.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 167 KPGGRLLDIGCGWGTLMFKAVQEY-GLSAVGVTLSEEQYYYVRKKADDLGLSDKVKVYLVDYRDLKE----EPFDYITS- 240
Cdd:COG4123 36 KKGGRVLDLGTGTGVIALMLAQRSpGARITGVEIQPEAAELARRNVALNGLEDRITVIHGDLKEFAAelppGSFDLVVSn 115
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 545594585 241 -----VGMFE-----------HVGKENLEMYFQKVSDYLKPNGR-ALIH 272
Cdd:COG4123 116 ppyfkAGSGRkspdearaiarHEDALTLEDLIRAAARLLKPGGRfALIH 164
|
|
| PLN02336 |
PLN02336 |
phosphoethanolamine N-methyltransferase |
161-271 |
1.25e-05 |
|
phosphoethanolamine N-methyltransferase
Pssm-ID: 177970 [Multi-domain] Cd Length: 475 Bit Score: 47.05 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 161 LDKLNSKPGGRLLDIGCGWGTLMFKAVQEYGLSAVGVTLSEEQYYYVRKKAddLGLSDKVKVYLVD--YRDLKEEPFDYI 238
Cdd:PLN02336 259 VDKLDLKPGQKVLDVGCGIGGGDFYMAENFDVHVVGIDLSVNMISFALERA--IGRKCSVEFEVADctKKTYPDNSFDVI 336
|
90 100 110
....*....|....*....|....*....|...
gi 545594585 239 TSVGMFEHVgkENLEMYFQKVSDYLKPNGRALI 271
Cdd:PLN02336 337 YSRDTILHI--QDKPALFRSFFKWLKPGGKVLI 367
|
|
| PRK08317 |
PRK08317 |
hypothetical protein; Provisional |
158-271 |
1.54e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 181382 [Multi-domain] Cd Length: 241 Bit Score: 46.08 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 158 HHILDKLNSKPGGRLLDIGCGWGTL---MFKAVQEYGLsAVGVTLSEEQYYYVRKKADDLGLsdKVKVYLVDYRDLK--E 232
Cdd:PRK08317 9 ARTFELLAVQPGDRVLDVGCGPGNDareLARRVGPEGR-VVGIDRSEAMLALAKERAAGLGP--NVEFVRGDADGLPfpD 85
|
90 100 110
....*....|....*....|....*....|....*....
gi 545594585 233 EPFDYITSVGMFEHVgkENLEMYFQKVSDYLKPNGRALI 271
Cdd:PRK08317 86 GSFDAVRSDRVLQHL--EDPARALAEIARVLRPGGRVVV 122
|
|
| PTZ00098 |
PTZ00098 |
phosphoethanolamine N-methyltransferase; Provisional |
160-271 |
2.65e-05 |
|
phosphoethanolamine N-methyltransferase; Provisional
Pssm-ID: 173391 [Multi-domain] Cd Length: 263 Bit Score: 45.35 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 160 ILDKLNSKPGGRLLDIGCGWGTLMFKAVQEYGLSAVGVTLSEEQYYYVRKKADDlglSDKVKVYLVDY--RDLKEEPFDY 237
Cdd:PTZ00098 44 ILSDIELNENSKVLDIGSGLGGGCKYINEKYGAHVHGVDICEKMVNIAKLRNSD---KNKIEFEANDIlkKDFPENTFDM 120
|
90 100 110
....*....|....*....|....*....|....
gi 545594585 238 ITSVGMFEHVGKENLEMYFQKVSDYLKPNGRALI 271
Cdd:PTZ00098 121 IYSRDAILHLSYADKKKLFEKCYKWLKPNGILLI 154
|
|
| TPMT |
pfam05724 |
Thiopurine S-methyltransferase (TPMT); This family consists of thiopurine S-methyltransferase ... |
149-323 |
1.41e-04 |
|
Thiopurine S-methyltransferase (TPMT); This family consists of thiopurine S-methyltransferase proteins from both eukaryotes and prokaryotes. Thiopurine S-methyltransferase (TPMT) is a cytosolic enzyme that catalyzes S-methylation of aromatic and heterocyclic sulfhydryl compounds, including anticancer and immunosuppressive thiopurines.
Pssm-ID: 399030 Cd Length: 218 Bit Score: 42.80 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 149 LEEAQIAKVHHiLDKLNSKPGGRLLDIGCGwGTLMFKAVQEYGLSAVGVTLSEEQyyyVRKKADDLGLSDKVK------- 221
Cdd:pfam05724 19 QEGVNPLLVRH-WDALKLPPGLRVLVPLCG-KALDMVWLAEQGHFVVGVEISELA---VEKFFAEAGLSPPITelsgfke 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 222 -------VYLVDYRDLKEE---PFDYITSVGMFEHVGKENLEMYFQKVSDYLKPNGRALIhgITgqhrgagVDPFIEKYI 291
Cdd:pfam05724 94 yssgnisLYCGDFFTLPREelgKFDLIYDRAALCALPPEMRPRYAKQMYELLPPGGRGLL--IT-------LDYPQTDHE 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 545594585 292 FPGGYIPniAENVEHIMTAGLQM------DDLEPLRRH 323
Cdd:pfam05724 165 GPPFSVP--AAELEALFGGGWKVaelereDALVPEPRF 200
|
|
| PLN02244 |
PLN02244 |
tocopherol O-methyltransferase |
171-279 |
1.91e-03 |
|
tocopherol O-methyltransferase
Pssm-ID: 215135 [Multi-domain] Cd Length: 340 Bit Score: 40.11 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 171 RLLDIGCGWGTLMFKAVQEYGLSAVGVTLSEEQyyyvRKKADDL----GLSDKVKVYLVDYRDL--KEEPFDYITSVGMF 244
Cdd:PLN02244 121 RIVDVGCGIGGSSRYLARKYGANVKGITLSPVQ----AARANALaaaqGLSDKVSFQVADALNQpfEDGQFDLVWSMESG 196
|
90 100 110
....*....|....*....|....*....|....*
gi 545594585 245 EHVgkENLEMYFQKVSDYLKPNGRALIhgITGQHR 279
Cdd:PLN02244 197 EHM--PDKRKFVQELARVAAPGGRIII--VTWCHR 227
|
|
| cbiT |
PRK00377 |
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional |
147-275 |
3.06e-03 |
|
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
Pssm-ID: 234740 Cd Length: 198 Bit Score: 38.62 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 147 MTLEEAQIAKvhhiLDKLNSKPGGRLLDIGCGWGTLMFKA---VQEYGlSAVGVTLSEEQYYYVRKKADDLGLSDKVKVY 223
Cdd:PRK00377 23 MTKEEIRALA----LSKLRLRKGDMILDIGCGTGSVTVEAsllVGETG-KVYAVDKDEKAINLTRRNAEKFGVLNNIVLI 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 545594585 224 LVDYRDLK---EEPFDYITSVGmfehvGKENLEMYFQKVSDYLKPNGRALIHGIT 275
Cdd:PRK00377 98 KGEAPEILftiNEKFDRIFIGG-----GSEKLKEIISASWEIIKKGGRIVIDAIL 147
|
|
| threonine_DH_like |
cd08234 |
L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ... |
138-286 |
3.76e-03 |
|
L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent formation of 2-amino-3-ketobutyrate from L-threonine, via NAD(H)-dependent oxidation. THD is a member of the zinc-requiring, medium chain NAD(H)-dependent alcohol dehydrogenase family (MDR). MDRs have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose.
Pssm-ID: 176196 [Multi-domain] Cd Length: 334 Bit Score: 39.05 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 138 SCAYFEHEDMTLEEAQ----IAKVHHILDKLNSKPGGRLLDIGCGW-GTLMFKAVQEYGLSAV-GVTLSEEQyyyvRKKA 211
Cdd:cd08234 125 KQVYKIPDNLSFEEAAlaepLSCAVHGLDLLGIKPGDSVLVFGAGPiGLLLAQLLKLNGASRVtVAEPNEEK----LELA 200
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545594585 212 DDLGLSDKV---KVYLVDYRDLKEEPFDYItsvgmFEHVG-KENLEMYFqkvsDYLKPNGRALIHGITGQHRGAGVDPF 286
Cdd:cd08234 201 KKLGATETVdpsREDPEAQKEDNPYGFDVV-----IEATGvPKTLEQAI----EYARRGGTVLVFGVYAPDARVSISPF 270
|
|
| PRK09328 |
PRK09328 |
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional |
157-275 |
4.18e-03 |
|
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
Pssm-ID: 236467 [Multi-domain] Cd Length: 275 Bit Score: 38.60 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 157 VHHILDKLNSKPGGRLLDIGCGWGTLmfkAV---QEY-GLSAVGVTLSEEQYYYVRKKAdDLGLSDKVKVYLVD-YRDLK 231
Cdd:PRK09328 97 VEWALEALLLKEPLRVLDLGTGSGAI---ALalaKERpDAEVTAVDISPEALAVARRNA-KHGLGARVEFLQGDwFEPLP 172
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545594585 232 EEPFD-------YITS---------VGMFE-H---VGKEN-LEMY---FQKVSDYLKPNGRALI-HGIT 275
Cdd:PRK09328 173 GGRFDlivsnppYIPEadihllqpeVRDHEpHlalFGGEDgLDFYrriIEQAPRYLKPGGWLLLeIGYD 241
|
|
| HemK |
COG2890 |
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ... |
157-273 |
4.32e-03 |
|
Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];
Pssm-ID: 442135 [Multi-domain] Cd Length: 282 Bit Score: 38.59 E-value: 4.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 157 VHHILDKLNSKPGGRLLDIGCGWG----TL--MFKAVQeyglsAVGVTLSEEQYYYVRKKADDLGLSDKVKVYLVD-YRD 229
Cdd:COG2890 101 VELALALLPAGAPPRVLDLGTGSGaialALakERPDAR-----VTAVDISPDALAVARRNAERLGLEDRVRFLQGDlFEP 175
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545594585 230 LKE-EPFD-------YITS---------VGMFE-H---VGKEN-LEMY---FQKVSDYLKPNGRALI-HG 273
Cdd:COG2890 176 LPGdGRFDlivsnppYIPEdeiallppeVRDHEpRlalDGGEDgLDFYrriIAQAPRLLKPGGWLLLeIG 245
|
|
| |
