|
Name |
Accession |
Description |
Interval |
E-value |
| mycolic_MTase |
NF040660 |
cyclopropane mycolic acid synthase family methyltransferase; Members of this family include ... |
31-313 |
0e+00 |
|
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: 555.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FK7_A 31 TRTRFEDIQAHYDVSDDFFALFQDPTRTYSCAYFEPPELTLEEAQYAKVDLNLDKLDLKPGMTLLDIGCGWGTTMRRAVE 110
Cdd:NF040660 1 LRPHFEDVQAHYDLSDDFFALFLDPTQTYSCAYFERDDMTLEEAQIAKIDLALGKLNLEPGMTLLDIGCGWGATMRRAVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FK7_A 111 RFDVNVIGLTLSKNQHARCEQVLASIDTNRSRQVLLQGWEDFAEPVDRIVSIEAFEHFGHENYDDFFKRCFNIMPADGRM 190
Cdd:NF040660 81 KYDVNVVGLTLSKNQAAHVQQVLDEIDTPRSRRVLLQGWEEFDEPVDRIVSIGAFEHFGHERYDDFFKRAYNILPADGRM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FK7_A 191 TVQSSVSYHPYEMAARGKKLSFETARFIKFIVTEIFPGGRLPSTEMMVEHGEKAGFTVPEPLSLRPHYIKTLRIWGDTLQ 270
Cdd:NF040660 161 LLHTITGLHRKEMHERGLPLTMELARFIKFIVTEIFPGGRLPSIEMVVEHAEKAGFTVTRVQSLQPHYARTLDLWADALQ 240
|
250 260 270 280
....*....|....*....|....*....|....*....|...
2FK7_A 271 SNKDKAIEVTSEEVYNRYMKYLRGCEHYFTDEMLDCSLVTYLK 313
Cdd:NF040660 241 AHKDEAIAIQSEEVYERYMKYLTGCAKLFRDGYIDVNQFTLAK 283
|
|
| CMAS |
pfam02353 |
Mycolic acid cyclopropane synthetase; This family consist of ... |
30-307 |
2.29e-169 |
|
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: 471.04 E-value: 2.29e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FK7_A 30 KTRTRFEDIQAHYDVSDDFFALFQDPTRTYSCAYFEPPELTLEEAQYAKVDLNLDKLDLKPGMTLLDIGCGWGTTMRRAV 109
Cdd:pfam02353 1 SKTRDAENIQAHYDLSNDFFALFLDPTMTYSCAYFERPDMTLEEAQQAKLDLILDKLGLKPGMTLLDIGCGWGGLMRRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FK7_A 110 ERFDVNVIGLTLSKNQHARCEQVLASIDTNRSRQVLLQGWEDFAEPVDRIVSIEAFEHFGHENYDDFFKRCFNIMPADGR 189
Cdd:pfam02353 81 ERYDVNVVGLTLSKNQYKLARKRVAAEGLARKVEVLLQDYRDFDEPFDRIVSVGMFEHVGHENYDTFFKKLYNLLPPGGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FK7_A 190 MTVQSSVSYHPYEMAARGKKLsfetarfiKFIVTEIFPGGRLPSTEMMVEHGEKAGFTVPEPLSLRPHYIKTLRIWGDTL 269
Cdd:pfam02353 161 MLLHTITGLHPDETSERGLPL--------KFIDKYIFPGGELPSISMIVESSSEAGFTVEDVESLRPHYAKTLDLWAENL 232
|
250 260 270
....*....|....*....|....*....|....*...
2FK7_A 270 QSNKDKAIEVTSEEVYNRYMKYLRGCEHYFTDEMLDCS 307
Cdd:pfam02353 233 QANKDEAIALQSEEFYRMWMLYLTGCAVAFRIGYIDVH 270
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
40-194 |
1.12e-65 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 203.62 E-value: 1.12e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FK7_A 40 AHYDVSDDFFALFQDPTRTYSCAYFEPPELTLEEAQYAKVDLNLDKLDLKPGMTLLDIGCGWGTTMRRAVERFDVNVIGL 119
Cdd:COG2230 1 HHYDLGNDFYRLFLDPTMTYSCAYFEDPDDTLEEAQEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
2FK7_A 120 TLSKNQHARCEQVLASIDTNRSRQVLLQGWEDFA--EPVDRIVSIEAFEHFGHENYDDFFKRCFNIMPADGRMTVQS 194
Cdd:COG2230 81 TLSPEQLEYARERAAEAGLADRVEVRLADYRDLPadGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLLHT 157
|
|
| cyclopro_CfaB |
NF040703 |
C17 cyclopropane fatty acid synthase CfaB; |
36-299 |
8.31e-54 |
|
C17 cyclopropane fatty acid synthase CfaB;
Pssm-ID: 468667 [Multi-domain] Cd Length: 393 Bit Score: 180.58 E-value: 8.31e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FK7_A 36 EDIQAHYDVSDDFFALFQDPTRTYSCAYFEPPELTLEEAQYAKVDLNLDKLDLKPGMTLLDIGCGWGTTMRRAVERFDVN 115
Cdd:NF040703 105 AAISYHYDLSNDFYALWLDPDMVYSCAYFETGTEDLAQAQQAKLRHLCRKLRLQPGERLLDVGCGWGGLARFAAREFGVE 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FK7_A 116 VIGLTLSKNQHARCEQVLAsiDTNRSRQVLLQ--------GWEDFaepvDRIVSIEAFEHFGHENYDDFFKRCFNIMPAD 187
Cdd:NF040703 185 VFGITLSKEQLKLARERVA--AEGLQDRVQLElldyrdlpQDGRF----DKVVSVGMFEHVGHANLPLYCQRLFGAVRPG 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FK7_A 188 GRmtvqssVSYHPYemaargkklsfeTARFI----------KFIVTEIFPGGRLPSTEMMVEHGEKAGFTVPEPLSLRPH 257
Cdd:NF040703 259 GL------VMNHGI------------TARHTdgrpvgrgagEFIGRYVFPHGELPHLATITASISEAGLEVVDVESLRLH 320
|
250 260 270 280
....*....|....*....|....*....|....*....|..
2FK7_A 258 YIKTLRIWGDTLQSNKDKAIEVTSEEVYNRYMKYLRGCEHYF 299
Cdd:NF040703 321 YARTLEHWSARLEARLDEAARLVPERALRIWRLYLAGCAYGF 362
|
|
| PRK11705 |
PRK11705 |
cyclopropane fatty acyl phospholipid synthase; |
39-265 |
1.52e-47 |
|
cyclopropane fatty acyl phospholipid synthase;
Pssm-ID: 183282 Cd Length: 383 Bit Score: 163.87 E-value: 1.52e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FK7_A 39 QAHYDVSDDFFALFQDPTRTYSCAYFEPPElTLEEAQYAKVDLNLDKLDLKPGMTLLDIGCGWGTTMRRAVERFDVNVIG 118
Cdd:PRK11705 117 KEHYDLGNDLFEAMLDPRMQYSCGYWKDAD-TLEEAQEAKLDLICRKLQLKPGMRVLDIGCGWGGLARYAAEHYGVSVVG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FK7_A 119 LTLSKNQHARCEQVLASIDTNrsrqVLLQGWEDFAEPVDRIVSIEAFEHFGHENYDDFF---KRCfniMPADGRM---TV 192
Cdd:PRK11705 196 VTISAEQQKLAQERCAGLPVE----IRLQDYRDLNGQFDRIVSVGMFEHVGPKNYRTYFevvRRC---LKPDGLFllhTI 268
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
2FK7_A 193 QSSVSYHPyemaargkklsfeTARFI-KFivteIFPGGRLPSTEMMVEHGEkaGFTVPEPL-SLRPHYIKTLRIW 265
Cdd:PRK11705 269 GSNKTDTN-------------VDPWInKY----IFPNGCLPSVRQIAQASE--GLFVMEDWhNFGADYDRTLMAW 324
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
93-193 |
1.96e-08 |
|
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: 51.66 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FK7_A 93 TLLDIGCGWGTTMRRAVERFDVNVIGLTLSKNQHARCEQVLASIDTNRSRqVLLQGWEDFA----EPVDRIVSIEAFEHF 168
Cdd:cd02440 1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVE-VLKGDAEELPpeadESFDVIISDPPLHHL 79
|
90 100
....*....|....*....|....*
2FK7_A 169 gHENYDDFFKRCFNIMPADGRMTVQ 193
Cdd:cd02440 80 -VEDLARFLEEARRLLKPGGVLVLT 103
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| mycolic_MTase |
NF040660 |
cyclopropane mycolic acid synthase family methyltransferase; Members of this family include ... |
31-313 |
0e+00 |
|
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: 555.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FK7_A 31 TRTRFEDIQAHYDVSDDFFALFQDPTRTYSCAYFEPPELTLEEAQYAKVDLNLDKLDLKPGMTLLDIGCGWGTTMRRAVE 110
Cdd:NF040660 1 LRPHFEDVQAHYDLSDDFFALFLDPTQTYSCAYFERDDMTLEEAQIAKIDLALGKLNLEPGMTLLDIGCGWGATMRRAVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FK7_A 111 RFDVNVIGLTLSKNQHARCEQVLASIDTNRSRQVLLQGWEDFAEPVDRIVSIEAFEHFGHENYDDFFKRCFNIMPADGRM 190
Cdd:NF040660 81 KYDVNVVGLTLSKNQAAHVQQVLDEIDTPRSRRVLLQGWEEFDEPVDRIVSIGAFEHFGHERYDDFFKRAYNILPADGRM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FK7_A 191 TVQSSVSYHPYEMAARGKKLSFETARFIKFIVTEIFPGGRLPSTEMMVEHGEKAGFTVPEPLSLRPHYIKTLRIWGDTLQ 270
Cdd:NF040660 161 LLHTITGLHRKEMHERGLPLTMELARFIKFIVTEIFPGGRLPSIEMVVEHAEKAGFTVTRVQSLQPHYARTLDLWADALQ 240
|
250 260 270 280
....*....|....*....|....*....|....*....|...
2FK7_A 271 SNKDKAIEVTSEEVYNRYMKYLRGCEHYFTDEMLDCSLVTYLK 313
Cdd:NF040660 241 AHKDEAIAIQSEEVYERYMKYLTGCAKLFRDGYIDVNQFTLAK 283
|
|
| CMAS |
pfam02353 |
Mycolic acid cyclopropane synthetase; This family consist of ... |
30-307 |
2.29e-169 |
|
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: 471.04 E-value: 2.29e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FK7_A 30 KTRTRFEDIQAHYDVSDDFFALFQDPTRTYSCAYFEPPELTLEEAQYAKVDLNLDKLDLKPGMTLLDIGCGWGTTMRRAV 109
Cdd:pfam02353 1 SKTRDAENIQAHYDLSNDFFALFLDPTMTYSCAYFERPDMTLEEAQQAKLDLILDKLGLKPGMTLLDIGCGWGGLMRRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FK7_A 110 ERFDVNVIGLTLSKNQHARCEQVLASIDTNRSRQVLLQGWEDFAEPVDRIVSIEAFEHFGHENYDDFFKRCFNIMPADGR 189
Cdd:pfam02353 81 ERYDVNVVGLTLSKNQYKLARKRVAAEGLARKVEVLLQDYRDFDEPFDRIVSVGMFEHVGHENYDTFFKKLYNLLPPGGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FK7_A 190 MTVQSSVSYHPYEMAARGKKLsfetarfiKFIVTEIFPGGRLPSTEMMVEHGEKAGFTVPEPLSLRPHYIKTLRIWGDTL 269
Cdd:pfam02353 161 MLLHTITGLHPDETSERGLPL--------KFIDKYIFPGGELPSISMIVESSSEAGFTVEDVESLRPHYAKTLDLWAENL 232
|
250 260 270
....*....|....*....|....*....|....*...
2FK7_A 270 QSNKDKAIEVTSEEVYNRYMKYLRGCEHYFTDEMLDCS 307
Cdd:pfam02353 233 QANKDEAIALQSEEFYRMWMLYLTGCAVAFRIGYIDVH 270
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
40-194 |
1.12e-65 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 203.62 E-value: 1.12e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FK7_A 40 AHYDVSDDFFALFQDPTRTYSCAYFEPPELTLEEAQYAKVDLNLDKLDLKPGMTLLDIGCGWGTTMRRAVERFDVNVIGL 119
Cdd:COG2230 1 HHYDLGNDFYRLFLDPTMTYSCAYFEDPDDTLEEAQEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
2FK7_A 120 TLSKNQHARCEQVLASIDTNRSRQVLLQGWEDFA--EPVDRIVSIEAFEHFGHENYDDFFKRCFNIMPADGRMTVQS 194
Cdd:COG2230 81 TLSPEQLEYARERAAEAGLADRVEVRLADYRDLPadGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLLHT 157
|
|
| cyclopro_CfaB |
NF040703 |
C17 cyclopropane fatty acid synthase CfaB; |
36-299 |
8.31e-54 |
|
C17 cyclopropane fatty acid synthase CfaB;
Pssm-ID: 468667 [Multi-domain] Cd Length: 393 Bit Score: 180.58 E-value: 8.31e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FK7_A 36 EDIQAHYDVSDDFFALFQDPTRTYSCAYFEPPELTLEEAQYAKVDLNLDKLDLKPGMTLLDIGCGWGTTMRRAVERFDVN 115
Cdd:NF040703 105 AAISYHYDLSNDFYALWLDPDMVYSCAYFETGTEDLAQAQQAKLRHLCRKLRLQPGERLLDVGCGWGGLARFAAREFGVE 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FK7_A 116 VIGLTLSKNQHARCEQVLAsiDTNRSRQVLLQ--------GWEDFaepvDRIVSIEAFEHFGHENYDDFFKRCFNIMPAD 187
Cdd:NF040703 185 VFGITLSKEQLKLARERVA--AEGLQDRVQLElldyrdlpQDGRF----DKVVSVGMFEHVGHANLPLYCQRLFGAVRPG 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FK7_A 188 GRmtvqssVSYHPYemaargkklsfeTARFI----------KFIVTEIFPGGRLPSTEMMVEHGEKAGFTVPEPLSLRPH 257
Cdd:NF040703 259 GL------VMNHGI------------TARHTdgrpvgrgagEFIGRYVFPHGELPHLATITASISEAGLEVVDVESLRLH 320
|
250 260 270 280
....*....|....*....|....*....|....*....|..
2FK7_A 258 YIKTLRIWGDTLQSNKDKAIEVTSEEVYNRYMKYLRGCEHYF 299
Cdd:NF040703 321 YARTLEHWSARLEARLDEAARLVPERALRIWRLYLAGCAYGF 362
|
|
| PRK11705 |
PRK11705 |
cyclopropane fatty acyl phospholipid synthase; |
39-265 |
1.52e-47 |
|
cyclopropane fatty acyl phospholipid synthase;
Pssm-ID: 183282 Cd Length: 383 Bit Score: 163.87 E-value: 1.52e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FK7_A 39 QAHYDVSDDFFALFQDPTRTYSCAYFEPPElTLEEAQYAKVDLNLDKLDLKPGMTLLDIGCGWGTTMRRAVERFDVNVIG 118
Cdd:PRK11705 117 KEHYDLGNDLFEAMLDPRMQYSCGYWKDAD-TLEEAQEAKLDLICRKLQLKPGMRVLDIGCGWGGLARYAAEHYGVSVVG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FK7_A 119 LTLSKNQHARCEQVLASIDTNrsrqVLLQGWEDFAEPVDRIVSIEAFEHFGHENYDDFF---KRCfniMPADGRM---TV 192
Cdd:PRK11705 196 VTISAEQQKLAQERCAGLPVE----IRLQDYRDLNGQFDRIVSVGMFEHVGPKNYRTYFevvRRC---LKPDGLFllhTI 268
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
2FK7_A 193 QSSVSYHPyemaargkklsfeTARFI-KFivteIFPGGRLPSTEMMVEHGEkaGFTVPEPL-SLRPHYIKTLRIW 265
Cdd:PRK11705 269 GSNKTDTN-------------VDPWInKY----IFPNGCLPSVRQIAQASE--GLFVMEDWhNFGADYDRTLMAW 324
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
95-181 |
4.62e-12 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 61.43 E-value: 4.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FK7_A 95 LDIGCGWGTTMRRAVERFDVNVIGLTLSKNQHARCEQVLASIDTN-RSRQVLLQGWEDFAEPVDRIVSIEAFEHFGHENY 173
Cdd:pfam13649 2 LDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLNvEFVQGDAEDLPFPDGSFDLVVSSGVLHHLPDPDL 81
|
....*...
2FK7_A 174 DDFFKRCF 181
Cdd:pfam13649 82 EAALREIA 89
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
74-192 |
4.76e-10 |
|
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: 56.93 E-value: 4.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FK7_A 74 AQYAKVDLNLDKLDLKPGMTLLDIGCGWGTTMRRAVERfDVNVIGLTLSKNQHARCEQVLASIDTNRSrqvLLQG-WED- 151
Cdd:COG2226 6 ARYDGREALLAALGLRPGARVLDLGCGTGRLALALAER-GARVTGVDISPEMLELARERAAEAGLNVE---FVVGdAEDl 81
|
90 100 110 120
....*....|....*....|....*....|....*....|...
2FK7_A 152 -FA-EPVDRIVSIEAFEHFghENYDDFFKRCFNIMPADGRMTV 192
Cdd:COG2226 82 pFPdGSFDLVISSFVLHHL--PDPERALAEIARVLKPGGRLVV 122
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
88-190 |
1.46e-08 |
|
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: 52.33 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FK7_A 88 LKPGMTLLDIGCGWGTTMRRAVERFdVNVIGLTLSKNQHARCEQVLASIDTNrsrqVLLQGWEDFA---EPVDRIVSIEA 164
Cdd:COG2227 22 LPAGGRVLDVGCGTGRLALALARRG-ADVTGVDISPEALEIARERAAELNVD----FVQGDLEDLPledGSFDLVICSEV 96
|
90 100
....*....|....*....|....*.
2FK7_A 165 FEHFghENYDDFFKRCFNIMPADGRM 190
Cdd:COG2227 97 LEHL--PDPAALLRELARLLKPGGLL 120
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
93-193 |
1.96e-08 |
|
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: 51.66 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FK7_A 93 TLLDIGCGWGTTMRRAVERFDVNVIGLTLSKNQHARCEQVLASIDTNRSRqVLLQGWEDFA----EPVDRIVSIEAFEHF 168
Cdd:cd02440 1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVE-VLKGDAEELPpeadESFDVIISDPPLHHL 79
|
90 100
....*....|....*....|....*
2FK7_A 169 gHENYDDFFKRCFNIMPADGRMTVQ 193
Cdd:cd02440 80 -VEDLARFLEEARRLLKPGGVLVLT 103
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
72-189 |
3.74e-07 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 49.91 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FK7_A 72 EEAQYAKVDLNLDKLDLKPGMTLLDIGCGWGTTMRRAVERFDVNVIGLTLSKN--QHARCEQVLASIDTNRSRQVLLQGW 149
Cdd:COG0500 8 DELLPGLAALLALLERLPKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEaiALARARAAKAGLGNVEFLVADLAEL 87
|
90 100 110 120
....*....|....*....|....*....|....*....|.
2FK7_A 150 EDF-AEPVDRIVSIEAFEHFGHENYDDFFKRCFNIMPADGR 189
Cdd:COG0500 88 DPLpAESFDLVVAFGVLHHLPPEEREALLRELARALKPGGV 128
|
|
| Tam |
COG4106 |
Trans-aconitate methyltransferase [Energy production and conversion]; |
90-193 |
1.31e-06 |
|
Trans-aconitate methyltransferase [Energy production and conversion];
Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 45.97 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FK7_A 90 PGMTLLDIGCGWGTTMRRAVERF-DVNVIGLTLSKNQHARCEQVLASIDTnrsRQVLLQGWeDFAEPVDRIVSIEAFEHF 168
Cdd:COG4106 1 PPRRVLDLGCGTGRLTALLAERFpGARVTGVDLSPEMLARARARLPNVRF---VVADLRDL-DPPEPFDLVVSNAALHWL 76
|
90 100
....*....|....*....|....*
2FK7_A 169 ghENYDDFFKRCFNIMPADGRMTVQ 193
Cdd:COG4106 77 --PDHAALLARLAAALAPGGVLAVQ 99
|
|
| PLN02336 |
PLN02336 |
phosphoethanolamine N-methyltransferase |
83-124 |
2.73e-06 |
|
phosphoethanolamine N-methyltransferase
Pssm-ID: 177970 [Multi-domain] Cd Length: 475 Bit Score: 48.59 E-value: 2.73e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
2FK7_A 83 LDKLDLKPGMTLLDIGCGWGTTMRRAVERFDVNVIGLTLSKN 124
Cdd:PLN02336 259 VDKLDLKPGQKVLDVGCGIGGGDFYMAENFDVHVVGIDLSVN 300
|
|
| Methyltransf_23 |
pfam13489 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
86-248 |
1.07e-05 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 404385 [Multi-domain] Cd Length: 162 Bit Score: 44.73 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FK7_A 86 LDLKPGMTLLDIGCGWGTTMRRAVERFdVNVIGLTLSKNQHARceqvlaSIDTNRSRQVLLQGWEDFAEPVDRIVSIEAF 165
Cdd:pfam13489 18 PKLPSPGRVLDFGCGTGIFLRLLRAQG-FSVTGVDPSPIAIER------ALLNVRFDQFDEQEAAVPAGKFDVIVAREVL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FK7_A 166 EHFghENYDDFFKRCFNIMPADGRMTVQSSVSYHPYEMAARGKKLSFETARFIKFivteiFPGGRLpsTEMMvehgEKAG 245
Cdd:pfam13489 91 EHV--PDPPALLRQIAALLKPGGLLLLSTPLASDEADRLLLEWPYLRPRNGHISL-----FSARSL--KRLL----EEAG 157
|
...
2FK7_A 246 FTV 248
Cdd:pfam13489 158 FEV 160
|
|
| Methyltransf_11 |
pfam08241 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
95-190 |
3.66e-05 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 462406 [Multi-domain] Cd Length: 94 Bit Score: 41.88 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FK7_A 95 LDIGCGWGTTMRRAVERFdVNVIGLTLSKNQHARCEQvlasiDTNRSRQVLLQG------WEDfaEPVDRIVSIEAFEHF 168
Cdd:pfam08241 1 LDVGCGTGLLTELLARLG-ARVTGVDISPEMLELARE-----KAPREGLTFVVGdaedlpFPD--NSFDLVLSSEVLHHV 72
|
90 100
....*....|....*....|..
2FK7_A 169 ghENYDDFFKRCFNIMPADGRM 190
Cdd:pfam08241 73 --EDPERALREIARVLKPGGIL 92
|
|
| Methyltransf_12 |
pfam08242 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
95-189 |
5.50e-05 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 41.58 E-value: 5.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FK7_A 95 LDIGCGWGTTMRRAVERF-DVNVIGLTLSKNQHARCEQVLASI---DTNRSRQVLLQGWEDFAEPVDRIVSIEAFEHFgh 170
Cdd:pfam08242 1 LEIGCGTGTLLRALLEALpGLEYTGLDISPAALEAARERLAALgllNAVRVELFQLDLGELDPGSFDVVVASNVLHHL-- 78
|
90
....*....|....*....
2FK7_A 171 ENYDDFFKRCFNIMPADGR 189
Cdd:pfam08242 79 ADPRAVLRNIRRLLKPGGV 97
|
|
| PCMT |
pfam01135 |
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT); |
83-159 |
1.30e-03 |
|
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
Pssm-ID: 395902 [Multi-domain] Cd Length: 205 Bit Score: 39.27 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FK7_A 83 LDKLDLKPGMTLLDIGCGWG---TTMRRAVERfDVNVIGLtlsknQHAR--CEQVLASIDTNRSRQVLL------QGWED 151
Cdd:pfam01135 66 LELLELKPGMRVLEIGSGSGyltACFARMVGE-VGRVVSI-----EHIPelVEIARRNLEKLGLENVIVvvgdgrQGWPE 139
|
....*...
2FK7_A 152 FAePVDRI 159
Cdd:pfam01135 140 FA-PYDAI 146
|
|
| RsmC |
COG2813 |
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ... |
83-209 |
3.41e-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: 37.86 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FK7_A 83 LDKLDLKPGMTLLDIGCGWGttmrraverfdvnVIGLTLSK-NQHARC------EQVLAS----IDTNRSRQV------L 145
Cdd:COG2813 42 LEHLPEPLGGRVLDLGCGYG-------------VIGLALAKrNPEARVtlvdvnARAVELaranAAANGLENVevlwsdG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FK7_A 146 LQGWEDfaEPVDRIVS---IeafeHFGHENYDD----FFKRCFNIMPADGRMTV--QSSVSYHP--------YEMAARGK 208
Cdd:COG2813 109 LSGVPD--GSFDLILSnppF----HAGRAVDKEvahaLIADAARHLRPGGELWLvaNRHLPYERkleelfgnVEVLARNK 182
|
.
2FK7_A 209 K 209
Cdd:COG2813 183 G 183
|
|
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