|
Name |
Accession |
Description |
Interval |
E-value |
| CMAS |
pfam02353 |
Mycolic acid cyclopropane synthetase; This family consist of ... |
104-370 |
1.03e-117 |
|
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: 343.15 E-value: 1.03e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 104 SEKKSQQDIQSHYDVGNDFYKMWLDPTMTYSCAYFKHDTDTLEEAQIHKVHHIIQKLNPQPGKTLLDIGCGWGTLMLTAA 183
Cdd:pfam02353 1 SKTRDAENIQAHYDLSNDFFALFLDPTMTYSCAYFERPDMTLEEAQQAKLDLILDKLGLKPGMTLLDIGCGWGGLMRRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 184 KEYGLKVVGVTLSQEQYNLVAQRIKDEGLSDVAEVRLQDYRELgDETFDYITSVGMFEHVGKDNLAMYFERVNHYLKADG 263
Cdd:pfam02353 81 ERYDVNVVGLTLSKNQYKLARKRVAAEGLARKVEVLLQDYRDF-DEPFDRIVSVGMFEHVGHENYDTFFKKLYNLLPPGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 264 VALLHGITR------QQGGATNGWLDKYIFPGGYVPGMTENLQHIVDAGLQVADVETLRRHYQRTTEIWDKNFNAKRAAI 337
Cdd:pfam02353 160 LMLLHTITGlhpdetSERGLPLKFIDKYIFPGGELPSISMIVESSSEAGFTVEDVESLRPHYAKTLDLWAENLQANKDEA 239
|
250 260 270
....*....|....*....|....*....|...
gi 1969439119 338 EEKMGVRFTRMWDLYLQACAASFQSGNIDVMQY 370
Cdd:pfam02353 240 IALQSEEFYRMWMLYLTGCAVAFRIGYIDVHQF 272
|
|
| cyclopro_CfaB |
NF040703 |
C17 cyclopropane fatty acid synthase CfaB; |
13-389 |
2.81e-115 |
|
C17 cyclopropane fatty acid synthase CfaB;
Pssm-ID: 468667 [Multi-domain] Cd Length: 393 Bit Score: 341.59 E-value: 2.81e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 13 HSFNMPVTVNYWDGSSETYGEgTPEVTVTFKEAIPMREITKNASIALGEAYMDGKIEIDGSIQKLIESAYESAESFFNNS 92
Cdd:NF040703 10 RNLQLPLRLRLWDGKQLDLGP-SPRVTLVVKDPSLLSQLTHPSLDLLGSAYVEGRLDLEGPIMEVIRVGDELSQALLGDD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 93 KFKkFMPKQSHSEKKSQQDIQSHYDVGNDFYKMWLDPTMTYSCAYFKHDTDTLEEAQIHKVHHIIQKLNPQPGKTLLDIG 172
Cdd:NF040703 89 DEA-PPERTAHDKATDAAAISYHYDLSNDFYALWLDPDMVYSCAYFETGTEDLAQAQQAKLRHLCRKLRLQPGERLLDVG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 173 CGWGTLMLTAAKEYGLKVVGVTLSQEQYNLVAQRIKDEGLSDVAEVRLQDYREL-GDETFDYITSVGMFEHVGKDNLAMY 251
Cdd:NF040703 168 CGWGGLARFAAREFGVEVFGITLSKEQLKLARERVAAEGLQDRVQLELLDYRDLpQDGRFDKVVSVGMFEHVGHANLPLY 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 252 FERVNHYLKADGVALLHGIT------RQQGGATNGWLDKYIFPGGYVPGMTENLQHIVDAGLQVADVETLRRHYQRTTEI 325
Cdd:NF040703 248 CQRLFGAVRPGGLVMNHGITarhtdgRPVGRGAGEFIGRYVFPHGELPHLATITASISEAGLEVVDVESLRLHYARTLEH 327
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1969439119 326 WDKNFNAKRAAIEEKMGVRFTRMWDLYLQACAASFQSGNIDVMQYLVTK--GASSRTLPMTRKYMY 389
Cdd:NF040703 328 WSARLEARLDEAARLVPERALRIWRLYLAGCAYGFARGWINLHQILAVKplADGSHELPWTRADLY 393
|
|
| PRK11705 |
PRK11705 |
cyclopropane fatty acyl phospholipid synthase; |
56-374 |
1.18e-94 |
|
cyclopropane fatty acyl phospholipid synthase;
Pssm-ID: 183282 Cd Length: 383 Bit Score: 288.28 E-value: 1.18e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 56 SIALGEAYMDGKIEID------------GSIQKLIESAYESAESF----FNnskfkkfmpKQSHseKKSQQDIQSHYDVG 119
Cdd:PRK11705 55 SLGLGESYMDGWWDCDrldeffsrvlraGLDEKLPHHLKDTLRILrarlFN---------LQSK--KRAWIVGKEHYDLG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 120 NDFYKMWLDPTMTYSCAYFKhDTDTLEEAQIHKVHHIIQKLNPQPGKTLLDIGCGWGTLMLTAAKEYGLKVVGVTLSQEQ 199
Cdd:PRK11705 124 NDLFEAMLDPRMQYSCGYWK-DADTLEEAQEAKLDLICRKLQLKPGMRVLDIGCGWGGLARYAAEHYGVSVVGVTISAEQ 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 200 YNLVAQRIKdeGLsDVaEVRLQDYRELgDETFDYITSVGMFEHVGKDNLAMYFERVNHYLKADGVALLHGI-TRQQGGAT 278
Cdd:PRK11705 203 QKLAQERCA--GL-PV-EIRLQDYRDL-NGQFDRIVSVGMFEHVGPKNYRTYFEVVRRCLKPDGLFLLHTIgSNKTDTNV 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 279 NGWLDKYIFPGGYVPgmteNLQHIVDA--GLQV-ADVETLRRHYQRTTEIWDKNFNAKRAAIEEKMGVRFTRMWDLYLQA 355
Cdd:PRK11705 278 DPWINKYIFPNGCLP----SVRQIAQAseGLFVmEDWHNFGADYDRTLMAWHENFEAAWPELADNYSERFYRMWRYYLLS 353
|
330
....*....|....*....
gi 1969439119 356 CAASFQSGNIDVMQYLVTK 374
Cdd:PRK11705 354 CAGAFRARDIQLWQVVFSP 372
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
114-269 |
4.10e-82 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 248.31 E-value: 4.10e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 114 SHYDVGNDFYKMWLDPTMTYSCAYFKHDTDTLEEAQIHKVHHIIQKLNPQPGKTLLDIGCGWGTLMLTAAKEYGLKVVGV 193
Cdd:COG2230 1 HHYDLGNDFYRLFLDPTMTYSCAYFEDPDDTLEEAQEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1969439119 194 TLSQEQYNLVAQRIKDEGLSDVAEVRLQDYRELG-DETFDYITSVGMFEHVGKDNLAMYFERVNHYLKADGVALLHG 269
Cdd:COG2230 81 TLSPEQLEYARERAAEAGLADRVEVRLADYRDLPaDGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLLHT 157
|
|
| mycolic_MTase |
NF040660 |
cyclopropane mycolic acid synthase family methyltransferase; Members of this family include ... |
110-374 |
7.81e-74 |
|
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: 231.58 E-value: 7.81e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 110 QDIQSHYDVGNDFYKMWLDPTMTYSCAYFKHDTDTLEEAQIHKVHHIIQKLNPQPGKTLLDIGCGWGTLMLTAAKEYGLK 189
Cdd:NF040660 6 EDVQAHYDLSDDFFALFLDPTQTYSCAYFERDDMTLEEAQIAKIDLALGKLNLEPGMTLLDIGCGWGATMRRAVEKYDVN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 190 VVGVTLSQEQYNLVAQRIKDEGLSDVAEVRLQDYRELgDETFDYITSVGMFEHVGKDNLAMYFERVNHYLKADGVALLHG 269
Cdd:NF040660 86 VVGLTLSKNQAAHVQQVLDEIDTPRSRRVLLQGWEEF-DEPVDRIVSIGAFEHFGHERYDDFFKRAYNILPADGRMLLHT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 270 IT-------RQQGGATNGWLDKY-------IFPGGYVPGMTENLQHIVDAGLQVADVETLRRHYQRTTEIWDKNFNA-KR 334
Cdd:NF040660 165 ITglhrkemHERGLPLTMELARFikfivteIFPGGRLPSIEMVVEHAEKAGFTVTRVQSLQPHYARTLDLWADALQAhKD 244
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1969439119 335 AAIE---EKMGVRFTRmwdlYLQACAASFQSGNIDVMQYLVTK 374
Cdd:NF040660 245 EAIAiqsEEVYERYMK----YLTGCAKLFRDGYIDVNQFTLAK 283
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
167-268 |
2.98e-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: 62.83 E-value: 2.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 167 TLLDIGCGWGTLMLTAAKEYGLKVVGVTLSQEQYNLvAQRIKDEGLSDVAEVRLQDYREL---GDETFDYITSVGMFEHV 243
Cdd:cd02440 1 RVLDLGCGTGALALALASGPGARVTGVDISPVALEL-ARKAAAALLADNVEVLKGDAEELppeADESFDVIISDPPLHHL 79
|
90 100
....*....|....*....|....*
gi 1969439119 244 GKDNLAMyFERVNHYLKADGVALLH 268
Cdd:cd02440 80 VEDLARF-LEEARRLLKPGGVLVLT 103
|
|
| PKS_MT |
smart00828 |
Methyltransferase in polyketide synthase (PKS) enzymes; |
166-276 |
3.61e-08 |
|
Methyltransferase in polyketide synthase (PKS) enzymes;
Pssm-ID: 214839 [Multi-domain] Cd Length: 224 Bit Score: 53.57 E-value: 3.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 166 KTLLDIGCGWGTLMLTAAKEYG-LKVVGVTLSQEQYNLVAQRIKDEGLSDVAEVRlqdYRELGDETFDyitsvgmfehvG 244
Cdd:smart00828 1 KRVLDFGCGYGSDLIDLAERHPhLQLHGYTISPEQAEVGRERIRALGLQGRIRIF---YRDSAKDPFP-----------D 66
|
90 100 110
....*....|....*....|....*....|....
gi 1969439119 245 KDNLAMYFERVNHYlkADGVALLHGITR--QQGG 276
Cdd:smart00828 67 TYDLVFGFEVIHHI--KDKMDLFSNISRhlKDGG 98
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CMAS |
pfam02353 |
Mycolic acid cyclopropane synthetase; This family consist of ... |
104-370 |
1.03e-117 |
|
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: 343.15 E-value: 1.03e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 104 SEKKSQQDIQSHYDVGNDFYKMWLDPTMTYSCAYFKHDTDTLEEAQIHKVHHIIQKLNPQPGKTLLDIGCGWGTLMLTAA 183
Cdd:pfam02353 1 SKTRDAENIQAHYDLSNDFFALFLDPTMTYSCAYFERPDMTLEEAQQAKLDLILDKLGLKPGMTLLDIGCGWGGLMRRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 184 KEYGLKVVGVTLSQEQYNLVAQRIKDEGLSDVAEVRLQDYRELgDETFDYITSVGMFEHVGKDNLAMYFERVNHYLKADG 263
Cdd:pfam02353 81 ERYDVNVVGLTLSKNQYKLARKRVAAEGLARKVEVLLQDYRDF-DEPFDRIVSVGMFEHVGHENYDTFFKKLYNLLPPGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 264 VALLHGITR------QQGGATNGWLDKYIFPGGYVPGMTENLQHIVDAGLQVADVETLRRHYQRTTEIWDKNFNAKRAAI 337
Cdd:pfam02353 160 LMLLHTITGlhpdetSERGLPLKFIDKYIFPGGELPSISMIVESSSEAGFTVEDVESLRPHYAKTLDLWAENLQANKDEA 239
|
250 260 270
....*....|....*....|....*....|...
gi 1969439119 338 EEKMGVRFTRMWDLYLQACAASFQSGNIDVMQY 370
Cdd:pfam02353 240 IALQSEEFYRMWMLYLTGCAVAFRIGYIDVHQF 272
|
|
| cyclopro_CfaB |
NF040703 |
C17 cyclopropane fatty acid synthase CfaB; |
13-389 |
2.81e-115 |
|
C17 cyclopropane fatty acid synthase CfaB;
Pssm-ID: 468667 [Multi-domain] Cd Length: 393 Bit Score: 341.59 E-value: 2.81e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 13 HSFNMPVTVNYWDGSSETYGEgTPEVTVTFKEAIPMREITKNASIALGEAYMDGKIEIDGSIQKLIESAYESAESFFNNS 92
Cdd:NF040703 10 RNLQLPLRLRLWDGKQLDLGP-SPRVTLVVKDPSLLSQLTHPSLDLLGSAYVEGRLDLEGPIMEVIRVGDELSQALLGDD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 93 KFKkFMPKQSHSEKKSQQDIQSHYDVGNDFYKMWLDPTMTYSCAYFKHDTDTLEEAQIHKVHHIIQKLNPQPGKTLLDIG 172
Cdd:NF040703 89 DEA-PPERTAHDKATDAAAISYHYDLSNDFYALWLDPDMVYSCAYFETGTEDLAQAQQAKLRHLCRKLRLQPGERLLDVG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 173 CGWGTLMLTAAKEYGLKVVGVTLSQEQYNLVAQRIKDEGLSDVAEVRLQDYREL-GDETFDYITSVGMFEHVGKDNLAMY 251
Cdd:NF040703 168 CGWGGLARFAAREFGVEVFGITLSKEQLKLARERVAAEGLQDRVQLELLDYRDLpQDGRFDKVVSVGMFEHVGHANLPLY 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 252 FERVNHYLKADGVALLHGIT------RQQGGATNGWLDKYIFPGGYVPGMTENLQHIVDAGLQVADVETLRRHYQRTTEI 325
Cdd:NF040703 248 CQRLFGAVRPGGLVMNHGITarhtdgRPVGRGAGEFIGRYVFPHGELPHLATITASISEAGLEVVDVESLRLHYARTLEH 327
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1969439119 326 WDKNFNAKRAAIEEKMGVRFTRMWDLYLQACAASFQSGNIDVMQYLVTK--GASSRTLPMTRKYMY 389
Cdd:NF040703 328 WSARLEARLDEAARLVPERALRIWRLYLAGCAYGFARGWINLHQILAVKplADGSHELPWTRADLY 393
|
|
| PRK11705 |
PRK11705 |
cyclopropane fatty acyl phospholipid synthase; |
56-374 |
1.18e-94 |
|
cyclopropane fatty acyl phospholipid synthase;
Pssm-ID: 183282 Cd Length: 383 Bit Score: 288.28 E-value: 1.18e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 56 SIALGEAYMDGKIEID------------GSIQKLIESAYESAESF----FNnskfkkfmpKQSHseKKSQQDIQSHYDVG 119
Cdd:PRK11705 55 SLGLGESYMDGWWDCDrldeffsrvlraGLDEKLPHHLKDTLRILrarlFN---------LQSK--KRAWIVGKEHYDLG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 120 NDFYKMWLDPTMTYSCAYFKhDTDTLEEAQIHKVHHIIQKLNPQPGKTLLDIGCGWGTLMLTAAKEYGLKVVGVTLSQEQ 199
Cdd:PRK11705 124 NDLFEAMLDPRMQYSCGYWK-DADTLEEAQEAKLDLICRKLQLKPGMRVLDIGCGWGGLARYAAEHYGVSVVGVTISAEQ 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 200 YNLVAQRIKdeGLsDVaEVRLQDYRELgDETFDYITSVGMFEHVGKDNLAMYFERVNHYLKADGVALLHGI-TRQQGGAT 278
Cdd:PRK11705 203 QKLAQERCA--GL-PV-EIRLQDYRDL-NGQFDRIVSVGMFEHVGPKNYRTYFEVVRRCLKPDGLFLLHTIgSNKTDTNV 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 279 NGWLDKYIFPGGYVPgmteNLQHIVDA--GLQV-ADVETLRRHYQRTTEIWDKNFNAKRAAIEEKMGVRFTRMWDLYLQA 355
Cdd:PRK11705 278 DPWINKYIFPNGCLP----SVRQIAQAseGLFVmEDWHNFGADYDRTLMAWHENFEAAWPELADNYSERFYRMWRYYLLS 353
|
330
....*....|....*....
gi 1969439119 356 CAASFQSGNIDVMQYLVTK 374
Cdd:PRK11705 354 CAGAFRARDIQLWQVVFSP 372
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
114-269 |
4.10e-82 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 248.31 E-value: 4.10e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 114 SHYDVGNDFYKMWLDPTMTYSCAYFKHDTDTLEEAQIHKVHHIIQKLNPQPGKTLLDIGCGWGTLMLTAAKEYGLKVVGV 193
Cdd:COG2230 1 HHYDLGNDFYRLFLDPTMTYSCAYFEDPDDTLEEAQEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1969439119 194 TLSQEQYNLVAQRIKDEGLSDVAEVRLQDYRELG-DETFDYITSVGMFEHVGKDNLAMYFERVNHYLKADGVALLHG 269
Cdd:COG2230 81 TLSPEQLEYARERAAEAGLADRVEVRLADYRDLPaDGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLLHT 157
|
|
| mycolic_MTase |
NF040660 |
cyclopropane mycolic acid synthase family methyltransferase; Members of this family include ... |
110-374 |
7.81e-74 |
|
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: 231.58 E-value: 7.81e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 110 QDIQSHYDVGNDFYKMWLDPTMTYSCAYFKHDTDTLEEAQIHKVHHIIQKLNPQPGKTLLDIGCGWGTLMLTAAKEYGLK 189
Cdd:NF040660 6 EDVQAHYDLSDDFFALFLDPTQTYSCAYFERDDMTLEEAQIAKIDLALGKLNLEPGMTLLDIGCGWGATMRRAVEKYDVN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 190 VVGVTLSQEQYNLVAQRIKDEGLSDVAEVRLQDYRELgDETFDYITSVGMFEHVGKDNLAMYFERVNHYLKADGVALLHG 269
Cdd:NF040660 86 VVGLTLSKNQAAHVQQVLDEIDTPRSRRVLLQGWEEF-DEPVDRIVSIGAFEHFGHERYDDFFKRAYNILPADGRMLLHT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 270 IT-------RQQGGATNGWLDKY-------IFPGGYVPGMTENLQHIVDAGLQVADVETLRRHYQRTTEIWDKNFNA-KR 334
Cdd:NF040660 165 ITglhrkemHERGLPLTMELARFikfivteIFPGGRLPSIEMVVEHAEKAGFTVTRVQSLQPHYARTLDLWADALQAhKD 244
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1969439119 335 AAIE---EKMGVRFTRmwdlYLQACAASFQSGNIDVMQYLVTK 374
Cdd:NF040660 245 EAIAiqsEEVYERYMK----YLTGCAKLFRDGYIDVNQFTLAK 283
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
169-263 |
1.12e-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: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 169 LDIGCGWGTLMLTAAKEYGLKVVGVTLSQEQYNLVAQRIKDEGLSdvAEVRLQDYREL--GDETFDYITSVGMFEHVGKD 246
Cdd:pfam13649 2 LDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLN--VEFVQGDAEDLpfPDGSFDLVVSSGVLHHLPDP 79
|
90
....*....|....*..
gi 1969439119 247 NLAMYFERVNHYLKADG 263
Cdd:pfam13649 80 DLEAALREIARVLKPGG 96
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
154-287 |
1.89e-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: 78.50 E-value: 1.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 154 HHIIQKLNPQPGKTLLDIGCGWGTLMLTAAkEYGLKVVGVTLSQEQYNLVAQRIKDEGLSdvAEVRLQDYREL--GDETF 231
Cdd:COG2226 12 EALLAALGLRPGARVLDLGCGTGRLALALA-ERGARVTGVDISPEMLELARERAAEAGLN--VEFVVGDAEDLpfPDGSF 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1969439119 232 DYITSVGMFEHVgkDNLAMYFERVNHYLKADGVALLHGITRQQGGATNGWLDKYIF 287
Cdd:COG2226 89 DLVISSFVLHHL--PDPERALAEIARVLKPGGRLVVVDFSPPDLAELEELLAEAGF 142
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
152-267 |
4.18e-16 |
|
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: 74.28 E-value: 4.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 152 KVHHIIQKLNPqPGKTLLDIGCGWGTLMLTAAKEyGLKVVGVTLSQEQYNLVAQRIKDEGLsdvaEVRLQDYREL--GDE 229
Cdd:COG2227 13 RLAALLARLLP-AGGRVLDVGCGTGRLALALARR-GADVTGVDISPEALEIARERAAELNV----DFVQGDLEDLplEDG 86
|
90 100 110
....*....|....*....|....*....|....*...
gi 1969439119 230 TFDYITSVGMFEHVgkDNLAMYFERVNHYLKADGVALL 267
Cdd:COG2227 87 SFDLVICSEVLEHL--PDPAALLRELARLLKPGGLLLL 122
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
163-269 |
3.52e-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: 3.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 163 QPGKTLLDIGCGWGTLMLTAAKEYGLKVVGVTLSQEQYNLVAQRIKDEGLSDVaEVRLQDYRELG---DETFDYITSVGM 239
Cdd:COG0500 25 PKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAGLGNV-EFLVADLAELDplpAESFDLVVAFGV 103
|
90 100 110
....*....|....*....|....*....|
gi 1969439119 240 FEHVGKDNLAMYFERVNHYLKADGVALLHG 269
Cdd:COG0500 104 LHHLPPEEREALLRELARALKPGGVLLLSA 133
|
|
| COG4976 |
COG4976 |
Predicted methyltransferase, contains TPR repeat [General function prediction only]; |
151-264 |
5.95e-13 |
|
Predicted methyltransferase, contains TPR repeat [General function prediction only];
Pssm-ID: 444001 [Multi-domain] Cd Length: 181 Bit Score: 66.56 E-value: 5.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 151 HKVHHIIQKLNPQPGKTLLDIGCGWGtLMLTAAKEYGLKVVGVTLSQEQYNLVAQRikdeGLSDvaEVRLQDYREL--GD 228
Cdd:COG4976 33 LLAEELLARLPPGPFGRVLDLGCGTG-LLGEALRPRGYRLTGVDLSEEMLAKAREK----GVYD--RLLVADLADLaePD 105
|
90 100 110
....*....|....*....|....*....|....*.
gi 1969439119 229 ETFDYITSVGMFEHVGkdNLAMYFERVNHYLKADGV 264
Cdd:COG4976 106 GRFDLIVAADVLTYLG--DLAAVFAGVARALKPGGL 139
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
167-268 |
2.98e-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: 62.83 E-value: 2.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 167 TLLDIGCGWGTLMLTAAKEYGLKVVGVTLSQEQYNLvAQRIKDEGLSDVAEVRLQDYREL---GDETFDYITSVGMFEHV 243
Cdd:cd02440 1 RVLDLGCGTGALALALASGPGARVTGVDISPVALEL-ARKAAAALLADNVEVLKGDAEELppeADESFDVIISDPPLHHL 79
|
90 100
....*....|....*....|....*
gi 1969439119 244 GKDNLAMyFERVNHYLKADGVALLH 268
Cdd:cd02440 80 VEDLARF-LEEARRLLKPGGVLVLT 103
|
|
| Methyltransf_11 |
pfam08241 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
169-267 |
1.56e-11 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 462406 [Multi-domain] Cd Length: 94 Bit Score: 60.37 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 169 LDIGCGWGtLMLTAAKEYGLKVVGVTLSQEQYNLVAQRIKDEGLsdvaEVRLQDYRELG--DETFDYITSVGMFEHVgkD 246
Cdd:pfam08241 1 LDVGCGTG-LLTELLARLGARVTGVDISPEMLELAREKAPREGL----TFVVGDAEDLPfpDNSFDLVLSSEVLHHV--E 73
|
90 100
....*....|....*....|.
gi 1969439119 247 NLAMYFERVNHYLKADGVALL 267
Cdd:pfam08241 74 DPERALREIARVLKPGGILII 94
|
|
| Methyltransf_12 |
pfam08242 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
169-264 |
2.11e-11 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 60.07 E-value: 2.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 169 LDIGCGWGTLMLTAAKEY-GLKVVGVTLSQEQYNLVAQRIKDEGLSDVAEVRLQDYR--ELGDETFDYITSVGMFEHVgk 245
Cdd:pfam08242 1 LEIGCGTGTLLRALLEALpGLEYTGLDISPAALEAARERLAALGLLNAVRVELFQLDlgELDPGSFDVVVASNVLHHL-- 78
|
90
....*....|....*....
gi 1969439119 246 DNLAMYFERVNHYLKADGV 264
Cdd:pfam08242 79 ADPRAVLRNIRRLLKPGGV 97
|
|
| ubiE |
PRK00216 |
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ... |
150-235 |
3.31e-10 |
|
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;
Pssm-ID: 234689 [Multi-domain] Cd Length: 239 Bit Score: 59.78 E-value: 3.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 150 IHKV--HHIIQKLNPQPGKTLLDIGCGWGTLMLTAAKEYGL--KVVGVTLSQEQYNLVAQRIKDEGLSDVAEVRLQDYRE 225
Cdd:PRK00216 35 LHRVwrRKTIKWLGVRPGDKVLDLACGTGDLAIALAKAVGKtgEVVGLDFSEGMLAVGREKLRDLGLSGNVEFVQGDAEA 114
|
90
....*....|..
gi 1969439119 226 L--GDETFDYIT 235
Cdd:PRK00216 115 LpfPDNSFDAVT 126
|
|
| Methyltransf_23 |
pfam13489 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
145-268 |
8.92e-10 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 404385 [Multi-domain] Cd Length: 162 Bit Score: 57.05 E-value: 8.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 145 LEEAQIHKVHHIIQKL--NPQPGKTLLDIGCGWGTlMLTAAKEYGLKVVGVTLSQEQYNLVAQRIKDEGLSDVAEVRLQD 222
Cdd:pfam13489 1 YAHQRERLLADLLLRLlpKLPSPGRVLDFGCGTGI-FLRLLRAQGFSVTGVDPSPIAIERALLNVRFDQFDEQEAAVPAG 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1969439119 223 yrelgdeTFDYITSVGMFEHVgkDNLAMYFERVNHYLKADGVALLH 268
Cdd:pfam13489 80 -------KFDVIVAREVLEHV--PDPPALLRQIAALLKPGGLLLLS 116
|
|
| PRK08317 |
PRK08317 |
hypothetical protein; Provisional |
154-243 |
6.30e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 181382 [Multi-domain] Cd Length: 241 Bit Score: 56.10 E-value: 6.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 154 HHIIQKLNPQPGKTLLDIGCGWGTLMLTAAKEYGL--KVVGVTLSQEQYNLVAQRIKDEGLSdvAEVRLQDYREL--GDE 229
Cdd:PRK08317 9 ARTFELLAVQPGDRVLDVGCGPGNDARELARRVGPegRVVGIDRSEAMLALAKERAAGLGPN--VEFVRGDADGLpfPDG 86
|
90
....*....|....
gi 1969439119 230 TFDYITSVGMFEHV 243
Cdd:PRK08317 87 SFDAVRSDRVLQHL 100
|
|
| PKS_MT |
smart00828 |
Methyltransferase in polyketide synthase (PKS) enzymes; |
166-276 |
3.61e-08 |
|
Methyltransferase in polyketide synthase (PKS) enzymes;
Pssm-ID: 214839 [Multi-domain] Cd Length: 224 Bit Score: 53.57 E-value: 3.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 166 KTLLDIGCGWGTLMLTAAKEYG-LKVVGVTLSQEQYNLVAQRIKDEGLSDVAEVRlqdYRELGDETFDyitsvgmfehvG 244
Cdd:smart00828 1 KRVLDFGCGYGSDLIDLAERHPhLQLHGYTISPEQAEVGRERIRALGLQGRIRIF---YRDSAKDPFP-----------D 66
|
90 100 110
....*....|....*....|....*....|....
gi 1969439119 245 KDNLAMYFERVNHYlkADGVALLHGITR--QQGG 276
Cdd:smart00828 67 TYDLVFGFEVIHHI--KDKMDLFSNISRhlKDGG 98
|
|
| Tam |
COG4106 |
Trans-aconitate methyltransferase [Energy production and conversion]; |
164-267 |
4.92e-08 |
|
Trans-aconitate methyltransferase [Energy production and conversion];
Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 50.59 E-value: 4.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 164 PGKTLLDIGCGWGTLMLTAAKEY-GLKVVGVTLSQEQYNLVAQRikdegLSDVaEVRLQDYRELG-DETFDYITSVGMFE 241
Cdd:COG4106 1 PPRRVLDLGCGTGRLTALLAERFpGARVTGVDLSPEMLARARAR-----LPNV-RFVVADLRDLDpPEPFDLVVSNAALH 74
|
90 100
....*....|....*....|....*.
gi 1969439119 242 HVgkDNLAMYFERVNHYLKADGVALL 267
Cdd:COG4106 75 WL--PDHAALLARLAAALAPGGVLAV 98
|
|
| RsmC |
COG2813 |
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ... |
157-267 |
5.91e-07 |
|
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: 49.42 E-value: 5.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 157 IQKLNPQPGKTLLDIGCGWGTLMLTAAKEY-GLKVVGV-------TLSQEqyNLVAQRIKDeglsdvAEVRLQD-YRELG 227
Cdd:COG2813 42 LEHLPEPLGGRVLDLGCGYGVIGLALAKRNpEARVTLVdvnaravELARA--NAAANGLEN------VEVLWSDgLSGVP 113
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1969439119 228 DETFDYITS-----VGMfeHVGKDNLAMYFERVNHYLKADGVALL 267
Cdd:COG2813 114 DGSFDLILSnppfhAGR--AVDKEVAHALIADAARHLRPGGELWL 156
|
|
| PRK09328 |
PRK09328 |
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional |
141-278 |
2.03e-06 |
|
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
Pssm-ID: 236467 [Multi-domain] Cd Length: 275 Bit Score: 49.00 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 141 DTDTLeeaqihkVHHIIQKLNPQPGKTLLDIGCGWGTLMLTAAKEY-GLKVVGVTLSQEQYNlVAQRIKDEGLSDVAEVR 219
Cdd:PRK09328 92 ETEEL-------VEWALEALLLKEPLRVLDLGTGSGAIALALAKERpDAEVTAVDISPEALA-VARRNAKHGLGARVEFL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 220 LQD-YRELGDETFD-------YITS---------VGMFE-HV----GKDNLAMY---FERVNHYLKADGVALL-HGITrq 273
Cdd:PRK09328 164 QGDwFEPLPGGRFDlivsnppYIPEadihllqpeVRDHEpHLalfgGEDGLDFYrriIEQAPRYLKPGGWLLLeIGYD-- 241
|
....*
gi 1969439119 274 QGGAT 278
Cdd:PRK09328 242 QGEAV 246
|
|
| TrmN6 |
COG4123 |
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ... |
161-236 |
3.10e-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: 47.83 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 161 NPQPGKTLLDIGCGWGT--LMLtAAKEYGLKVVGVTLSQEQYNLvAQR-IKDEGLSDVAEVRLQDYRE----LGDETFDY 233
Cdd:COG4123 34 PVKKGGRVLDLGTGTGViaLML-AQRSPGARITGVEIQPEAAEL-ARRnVALNGLEDRITVIHGDLKEfaaeLPPGSFDL 111
|
...
gi 1969439119 234 ITS 236
Cdd:COG4123 112 VVS 114
|
|
| MTS |
pfam05175 |
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ... |
157-246 |
2.86e-05 |
|
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit methyltransferase C as well as other methyltransferases.
Pssm-ID: 428349 [Multi-domain] Cd Length: 170 Bit Score: 44.12 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 157 IQKLNPQPGKTLLDIGCGWGTLMLTAAKEYG-LKVVGVTLSQE-----QYNLVAQRIkdeglsDVAEVRLQD-YRELGDE 229
Cdd:pfam05175 24 LEHLPKDLSGKVLDLGCGAGVLGAALAKESPdAELTMVDINARalesaRENLAANGL------ENGEVVASDvYSGVEDG 97
|
90
....*....|....*..
gi 1969439119 230 TFDYITSVGMFeHVGKD 246
Cdd:pfam05175 98 KFDLIISNPPF-HAGLA 113
|
|
| Methyltransf_31 |
pfam13847 |
Methyltransferase domain; This family appears to have methyltransferase activity. |
164-264 |
3.65e-05 |
|
Methyltransferase domain; This family appears to have methyltransferase activity.
Pssm-ID: 463998 [Multi-domain] Cd Length: 150 Bit Score: 43.56 E-value: 3.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 164 PGKTLLDIGCGWGTLMLTAAKEYGL--KVVGVTLSQEQYNLVAQRIKDEGLSDVaEVRLQDYREL----GDETFDYITSV 237
Cdd:pfam13847 3 KGMRVLDLGCGTGHLSFELAEELGPnaEVVGIDISEEAIEKARENAQKLGFDNV-EFEQGDIEELpellEDDKFDVVISN 81
|
90 100
....*....|....*....|....*..
gi 1969439119 238 GMFEHVGkdNLAMYFERVNHYLKADGV 264
Cdd:pfam13847 82 CVLNHIP--DPDKVLQEILRVLKPGGR 106
|
|
| HemK |
COG2890 |
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ... |
153-278 |
3.76e-05 |
|
Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];
Pssm-ID: 442135 [Multi-domain] Cd Length: 282 Bit Score: 45.14 E-value: 3.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 153 VHHIIQKLNPQPGKTLLDIGCGWGTLMLTAAKEY-GLKVVGVTLSQEQYNlVAQR-IKDEGLSDVAEVRLQDYRE--LGD 228
Cdd:COG2890 101 VELALALLPAGAPPRVLDLGTGSGAIALALAKERpDARVTAVDISPDALA-VARRnAERLGLEDRVRFLQGDLFEplPGD 179
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1969439119 229 ETFD-------YITS---------VGMFE-HV----GKDNLAMY---FERVNHYLKADGVALL-HGItrQQGGAT 278
Cdd:COG2890 180 GRFDlivsnppYIPEdeiallppeVRDHEpRLaldgGEDGLDFYrriIAQAPRLLKPGGWLLLeIGE--DQGEAV 252
|
|
| PLN02244 |
PLN02244 |
tocopherol O-methyltransferase |
166-243 |
1.51e-04 |
|
tocopherol O-methyltransferase
Pssm-ID: 215135 [Multi-domain] Cd Length: 340 Bit Score: 43.58 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 166 KTLLDIGCGWGTLMLTAAKEYGLKVVGVTLSQEQynlvAQR----IKDEGLSDVAEVRLQDYREL--GDETFDYITSVGM 239
Cdd:PLN02244 120 KRIVDVGCGIGGSSRYLARKYGANVKGITLSPVQ----AARanalAAAQGLSDKVSFQVADALNQpfEDGQFDLVWSMES 195
|
....
gi 1969439119 240 FEHV 243
Cdd:PLN02244 196 GEHM 199
|
|
| PRK07580 |
PRK07580 |
Mg-protoporphyrin IX methyl transferase; Validated |
157-243 |
1.78e-04 |
|
Mg-protoporphyrin IX methyl transferase; Validated
Pssm-ID: 236059 [Multi-domain] Cd Length: 230 Bit Score: 42.52 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 157 IQKLNPQPGKTLLDIGCGWGTLMLTAAKEyGLKVVGVTLSQEQYNLVAQRIKDEGLSDVAEVRLQDYRELGdetfdyits 236
Cdd:PRK07580 56 LPADGDLTGLRILDAGCGVGSLSIPLARR-GAKVVASDISPQMVEEARERAPEAGLAGNITFEVGDLESLL--------- 125
|
....*..
gi 1969439119 237 vGMFEHV 243
Cdd:PRK07580 126 -GRFDTV 131
|
|
| PLN02336 |
PLN02336 |
phosphoethanolamine N-methyltransferase |
157-267 |
3.62e-04 |
|
phosphoethanolamine N-methyltransferase
Pssm-ID: 177970 [Multi-domain] Cd Length: 475 Bit Score: 42.43 E-value: 3.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 157 IQKLNPQPGKTLLDIGCGWGTLMLTAAKEYGLKVVGVTLSQEQYNLVAQRIKdeGLSDVAEVRLQD--YRELGDETFDYI 234
Cdd:PLN02336 259 VDKLDLKPGQKVLDVGCGIGGGDFYMAENFDVHVVGIDLSVNMISFALERAI--GRKCSVEFEVADctKKTYPDNSFDVI 336
|
90 100 110
....*....|....*....|....*....|...
gi 1969439119 235 TSVGMFEHVgKDNLAMyFERVNHYLKADGVALL 267
Cdd:PLN02336 337 YSRDTILHI-QDKPAL-FRSFFKWLKPGGKVLI 367
|
|
| PTZ00098 |
PTZ00098 |
phosphoethanolamine N-methyltransferase; Provisional |
156-267 |
8.41e-04 |
|
phosphoethanolamine N-methyltransferase; Provisional
Pssm-ID: 173391 [Multi-domain] Cd Length: 263 Bit Score: 40.72 E-value: 8.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 156 IIQKLNPQPGKTLLDIGCGWGTLMLTAAKEYGLKVVGVTLSQEQYNLVAQRIKDEG--LSDVAEVRLQDYRElgdETFDY 233
Cdd:PTZ00098 44 ILSDIELNENSKVLDIGSGLGGGCKYINEKYGAHVHGVDICEKMVNIAKLRNSDKNkiEFEANDILKKDFPE---NTFDM 120
|
90 100 110
....*....|....*....|....*....|....
gi 1969439119 234 ITSVGMFEHVGKDNLAMYFERVNHYLKADGVALL 267
Cdd:PTZ00098 121 IYSRDAILHLSYADKKKLFEKCYKWLKPNGILLI 154
|
|
| Gcd14 |
COG2519 |
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ... |
156-232 |
3.74e-03 |
|
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 N-methylase Trm61 is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 442009 [Multi-domain] Cd Length: 249 Bit Score: 38.60 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 156 IIQKLNPQPGKTLLDIGCGWGTL---MLTAAKEYGlKVVGVTLSQEQYNLVAQRIKDEGLSDVAEVRLQDYRE-LGDETF 231
Cdd:COG2519 83 IIARLDIFPGARVLEAGTGSGALtlaLARAVGPEG-KVYSYERREDFAEIARKNLERFGLPDNVELKLGDIREgIDEGDV 161
|
.
gi 1969439119 232 D 232
Cdd:COG2519 162 D 162
|
|
| MDR |
cd05188 |
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ... |
163-287 |
4.26e-03 |
|
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.
Pssm-ID: 176178 [Multi-domain] Cd Length: 271 Bit Score: 38.46 E-value: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 163 QPGKTLLDIGCG-WGTLMLTAAKEYGLKVVGVTLSQEQYNLVAQRIKDEGLSDVAEVRLQDYRELGDETFDYItsvgmFE 241
Cdd:cd05188 133 KPGDTVLVLGAGgVGLLAAQLAKAAGARVIVTDRSDEKLELAKELGADHVIDYKEEDLEEELRLTGGGGADVV-----ID 207
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1969439119 242 HVGKD---NLAMYFervnhyLKADGVALLHGITrqQGGATNGWLDKYIF 287
Cdd:cd05188 208 AVGGPetlAQALRL------LRPGGRIVVVGGT--SGGPPLDDLRRLLF 248
|
|
| Ubie_methyltran |
pfam01209 |
ubiE/COQ5 methyltransferase family; |
149-235 |
4.57e-03 |
|
ubiE/COQ5 methyltransferase family;
Pssm-ID: 395966 [Multi-domain] Cd Length: 228 Bit Score: 38.19 E-value: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 149 QIHKV--HHIIQKLNPQPGKTLLDIGCGWG--TLMLTAAKEYGLKVVGVTLSQEQYNLVAQRIKDEGLSDVaEVRLQDYR 224
Cdd:pfam01209 25 GIHRLwkDFTMKCMGVKRGNKFLDVAGGTGdwTFGLSDSAGSSGKVVGLDINENMLKEGEKKAKEEGKYNI-EFLQGNAE 103
|
90
....*....|...
gi 1969439119 225 ELG--DETFDYIT 235
Cdd:pfam01209 104 ELPfeDDSFDIVT 116
|
|
| MetW |
pfam07021 |
Methionine biosynthesis protein MetW; This family consists of several bacterial and one ... |
154-234 |
6.90e-03 |
|
Methionine biosynthesis protein MetW; This family consists of several bacterial and one archaeal methionine biosynthesis MetW proteins. Biosynthesis of methionine from homoserine in Pseudomonas putida takes place in three steps. The first step is the acylation of homoserine to yield an acyl-L-homoserine. This reaction is catalyzed by the products of the metXW genes and is equivalent to the first step in enterobacteria, gram-positive bacteria and fungi, except that in these microorganizms the reaction is catalyzed by a single polypeptide (the product of the metA gene in Escherichia coli and the met5 gene product in Neurospora crassa). In Pseudomonas putida, as in gram-positive bacteria and certain fungi, the second and third steps are a direct sulfhydrylation that converts the O-acyl-L-homoserine into homocysteine and further methylation to yield methionine. The latter reaction can be mediated by either of the two methionine synthetases present in the cells.
Pssm-ID: 399779 Cd Length: 193 Bit Score: 37.43 E-value: 6.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969439119 154 HHIIQKLNPqPGKTLLDIGCGWGTLMLTAAKEYGLKVVGVTLSQEQYNLVAQRikdeGLSDVAEVRLQDYRELGDETFDY 233
Cdd:pfam07021 4 FRYILEWIP-PGSRVLDLGCGDGTLLYLLKEEKGVDGYGIELDAAGVAECVAK----GLYVIQGDLDEGLEHFPDKSFDY 78
|
.
gi 1969439119 234 I 234
Cdd:pfam07021 79 V 79
|
|
| PRK13771 |
PRK13771 |
putative alcohol dehydrogenase; Provisional |
153-205 |
9.03e-03 |
|
putative alcohol dehydrogenase; Provisional
Pssm-ID: 184316 [Multi-domain] Cd Length: 334 Bit Score: 37.71 E-value: 9.03e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1969439119 153 VHHIIQKLNPQPGKTLLDIGCGWGTLM--LTAAKEYGLKVVGVTLSQEQYNLVAQ 205
Cdd:PRK13771 151 VYRGLRRAGVKKGETVLVTGAGGGVGIhaIQVAKALGAKVIAVTSSESKAKIVSK 205
|
|
| |
