|
Name |
Accession |
Description |
Interval |
E-value |
| CMAS |
pfam02353 |
Mycolic acid cyclopropane synthetase; This family consist of ... |
125-385 |
1.13e-113 |
|
Mycolic acid cyclopropane synthetase; This family consist of Cyclopropane-fatty-acyl-phospholipid synthase or CFA synthase EC:2.1.1.79 this enzyme catalyze the reaction: S-adenosyl-L-methionine + phospholipid olefinic fatty acid <=> S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid.
Pssm-ID: 396777 [Multi-domain] Cd Length: 272 Bit Score: 333.52 E-value: 1.13e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 125 EEIHAHYDISNDFYRLWLDDTMTYSCAYFANEKDTLTQAQENKVQHILKKLNPKPGKTLVDIGCGWGTLMLTACEQYQLK 204
Cdd:pfam02353 7 ENIQAHYDLSNDFFALFLDPTMTYSCAYFERPDMTLEEAQQAKLDLILDKLGLKPGMTLLDIGCGWGGLMRRAAERYDVN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 205 VTGITLSEEQYNYVQEQIEKRNLQDRAEVLLMDYRNLKGRhFDYVTSVGMFEHVGSQELPNYFQIVSDLLSEGGNALIHG 284
Cdd:pfam02353 87 VVGLTLSKNQYKLARKRVAAEGLARKVEVLLQDYRDFDEP-FDRIVSVGMFEHVGHENYDTFFKKLYNLLPPGGLMLLHT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 285 ITS------QQNGGTDPWLDKYIFPGGYIPSMVEILEDTRSAGLQLFDLETLRRHYQKTLECWTDNFHQCKDEVLKMEGE 358
Cdd:pfam02353 166 ITGlhpdetSERGLPLKFIDKYIFPGGELPSISMIVESSSEAGFTVEDVESLRPHYAKTLDLWAENLQANKDEAIALQSE 245
|
250 260
....*....|....*....|....*..
gi 497158116 359 RFYRMWDAYLQACAGSFAAGNIDCCQY 385
Cdd:pfam02353 246 EFYRMWMLYLTGCAVAFRIGYIDVHQF 272
|
|
| cyclopro_CfaB |
NF040703 |
C17 cyclopropane fatty acid synthase CfaB; |
63-404 |
6.13e-96 |
|
C17 cyclopropane fatty acid synthase CfaB;
Pssm-ID: 468667 [Multi-domain] Cd Length: 393 Bit Score: 292.67 E-value: 6.13e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 63 LGEAYMDGLVDVEGenrPLERLVEFAYEMMLKLQQNAtwtkwvSTTMKVKQkfhRHTPSENKEEIHAHYDISNDFYRLWL 142
Cdd:NF040703 55 LGSAYVEGRLDLEG---PIMEVIRVGDELSQALLGDD------DEAPPERT---AHDKATDAAAISYHYDLSNDFYALWL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 143 DDTMTYSCAYFANEKDTLTQAQENKVQHILKKLNPKPGKTLVDIGCGWGTLMLTACEQYQLKVTGITLSEEQYNYVQEQI 222
Cdd:NF040703 123 DPDMVYSCAYFETGTEDLAQAQQAKLRHLCRKLRLQPGERLLDVGCGWGGLARFAAREFGVEVFGITLSKEQLKLARERV 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 223 EKRNLQDRAEVLLMDYRNLKGR-HFDYVTSVGMFEHVGSQELPNYFQIVSDLLSEGGNALIHGITS------QQNGGTDP 295
Cdd:NF040703 203 AAEGLQDRVQLELLDYRDLPQDgRFDKVVSVGMFEHVGHANLPLYCQRLFGAVRPGGLVMNHGITArhtdgrPVGRGAGE 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 296 WLDKYIFPGGYIPSMVEILEDTRSAGLQLFDLETLRRHYQKTLECWTDNFHQCKDEVLKMEGERFYRMWDAYLQACAGSF 375
Cdd:NF040703 283 FIGRYVFPHGELPHLATITASISEAGLEVVDVESLRLHYARTLEHWSARLEARLDEAARLVPERALRIWRLYLAGCAYGF 362
|
330 340 350
....*....|....*....|....*....|..
gi 497158116 376 AAGNIDCCQYLLTKgP---SGMNLPMTREYMY 404
Cdd:NF040703 363 ARGWINLHQILAVK-PladGSHELPWTRADLY 393
|
|
| PRK11705 |
PRK11705 |
cyclopropane fatty acyl phospholipid synthase; |
52-389 |
9.74e-90 |
|
cyclopropane fatty acyl phospholipid synthase;
Pssm-ID: 183282 Cd Length: 383 Bit Score: 276.34 E-value: 9.74e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 52 KDCMKKGvSMYLGEAYMDGLVDVEgenrpleRLVEFAYEMM---LKLQQNATWTKWVSTTM-KVkqkFHRHTPSENKEEI 127
Cdd:PRK11705 48 KRVLQEG-SLGLGESYMDGWWDCD-------RLDEFFSRVLragLDEKLPHHLKDTLRILRaRL---FNLQSKKRAWIVG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 128 HAHYDISNDFYRLWLDDTMTYSCAYFaNEKDTLTQAQENKVQHILKKLNPKPGKTLVDIGCGWGTLMLTACEQYQLKVTG 207
Cdd:PRK11705 117 KEHYDLGNDLFEAMLDPRMQYSCGYW-KDADTLEEAQEAKLDLICRKLQLKPGMRVLDIGCGWGGLARYAAEHYGVSVVG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 208 ITLSEEQYNYVQEQIEKRNLqdraEVLLMDYRNLKGRhFDYVTSVGMFEHVGSQELPNYFQIVSDLLSEGGNALIHGITS 287
Cdd:PRK11705 196 VTISAEQQKLAQERCAGLPV----EIRLQDYRDLNGQ-FDRIVSVGMFEHVGPKNYRTYFEVVRRCLKPDGLFLLHTIGS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 288 QQNG-GTDPWLDKYIFPGGYIPSMVEILEDTRSaglqLF---DLETLRRHYQKTLECWTDNFHQCKDEVLKMEGERFYRM 363
Cdd:PRK11705 271 NKTDtNVDPWINKYIFPNGCLPSVRQIAQASEG----LFvmeDWHNFGADYDRTLMAWHENFEAAWPELADNYSERFYRM 346
|
330 340
....*....|....*....|....*.
gi 497158116 364 WDAYLQACAGSFAAGNIDCCQYLLTK 389
Cdd:PRK11705 347 WRYYLLSCAGAFRARDIQLWQVVFSP 372
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
129-284 |
1.15e-75 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 232.13 E-value: 1.15e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 129 AHYDISNDFYRLWLDDTMTYSCAYFANEKDTLTQAQENKVQHILKKLNPKPGKTLVDIGCGWGTLMLTACEQYQLKVTGI 208
Cdd:COG2230 1 HHYDLGNDFYRLFLDPTMTYSCAYFEDPDDTLEEAQEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497158116 209 TLSEEQYNYVQEQIEKRNLQDRAEVLLMDYRNLKG-RHFDYVTSVGMFEHVGSQELPNYFQIVSDLLSEGGNALIHG 284
Cdd:COG2230 81 TLSPEQLEYARERAAEAGLADRVEVRLADYRDLPAdGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLLHT 157
|
|
| mycolic_MTase |
NF040660 |
cyclopropane mycolic acid synthase family methyltransferase; Members of this family include ... |
125-389 |
1.62e-71 |
|
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: 226.19 E-value: 1.62e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 125 EEIHAHYDISNDFYRLWLDDTMTYSCAYFANEKDTLTQAQENKVQHILKKLNPKPGKTLVDIGCGWGTLMLTACEQYQLK 204
Cdd:NF040660 6 EDVQAHYDLSDDFFALFLDPTQTYSCAYFERDDMTLEEAQIAKIDLALGKLNLEPGMTLLDIGCGWGATMRRAVEKYDVN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 205 VTGITLSEEQYNYVQEQIEKRNLQDRAEVLLMDYRNLKgRHFDYVTSVGMFEHVGSQELPNYFQIVSDLLSEGGNALIHG 284
Cdd:NF040660 86 VVGLTLSKNQAAHVQQVLDEIDTPRSRRVLLQGWEEFD-EPVDRIVSIGAFEHFGHERYDDFFKRAYNILPADGRMLLHT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 285 ITS------QQNGGTDP-WLDKY-------IFPGGYIPSMVEILEDTRSAGLQLFDLETLRRHYQKTLECWTDNFHQCKD 350
Cdd:NF040660 165 ITGlhrkemHERGLPLTmELARFikfivteIFPGGRLPSIEMVVEHAEKAGFTVTRVQSLQPHYARTLDLWADALQAHKD 244
|
250 260 270
....*....|....*....|....*....|....*....
gi 497158116 351 EVLKMEGERFYRMWDAYLQACAGSFAAGNIDCCQYLLTK 389
Cdd:NF040660 245 EAIAIQSEEVYERYMKYLTGCAKLFRDGYIDVNQFTLAK 283
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
182-278 |
8.00e-09 |
|
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: 52.82 E-value: 8.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 182 TLVDIGCGWGTLMLTACEQYQLKVTGITLSEEQYNYVQeQIEKRNLQDRAEVLLMDYRNL---KGRHFDYVTSVGMFEHV 258
Cdd:cd02440 1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELAR-KAAAALLADNVEVLKGDAEELppeADESFDVIISDPPLHHL 79
|
90 100
....*....|....*....|
gi 497158116 259 GsQELPNYFQIVSDLLSEGG 278
Cdd:cd02440 80 V-EDLARFLEEARRLLKPGG 98
|
|
| PKS_MT |
smart00828 |
Methyltransferase in polyketide synthase (PKS) enzymes; |
185-278 |
1.50e-04 |
|
Methyltransferase in polyketide synthase (PKS) enzymes;
Pssm-ID: 214839 [Multi-domain] Cd Length: 224 Bit Score: 42.79 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 185 DIGCGWGTLMLTACEQY-QLKVTGITLSEEQYNYVQEQIEKRNLQDRAEVLlmdYRNLKGRHF-DYVTSVGMFEHVGS-Q 261
Cdd:smart00828 5 DFGCGYGSDLIDLAERHpHLQLHGYTISPEQAEVGRERIRALGLQGRIRIF---YRDSAKDPFpDTYDLVFGFEVIHHiK 81
|
90
....*....|....*..
gi 497158116 262 ELPNYFQIVSDLLSEGG 278
Cdd:smart00828 82 DKMDLFSNISRHLKDGG 98
|
|
| CbiT |
TIGR02469 |
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ... |
171-229 |
3.26e-03 |
|
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes the CbiT methylase which is responsible, in part (along with CbiE), for methylating precorrin-6y (or cobalt-precorrin-6y) at both the 5 and 15 positions as well as the concomitant decarbozylation at C-12. In many organisms, this protein is fused to the CbiE subunit. The fused protein, when found in organisms catalyzing the oxidative version of the cobalamin biosynthesis pathway, is called CobL. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
Pssm-ID: 274148 [Multi-domain] Cd Length: 124 Bit Score: 37.31 E-value: 3.26e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 171 ILKKLNPKPGKTLVDIGCGWGTLMLTACEQY-QLKVTGITLSEEqynyVQEQIEkRNLQD 229
Cdd:TIGR02469 11 TLAKLRLRPGDVLWDIGAGTGSVTIEAARLVpNGRVYAIERNPE----ALDLIE-RNLRR 65
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CMAS |
pfam02353 |
Mycolic acid cyclopropane synthetase; This family consist of ... |
125-385 |
1.13e-113 |
|
Mycolic acid cyclopropane synthetase; This family consist of Cyclopropane-fatty-acyl-phospholipid synthase or CFA synthase EC:2.1.1.79 this enzyme catalyze the reaction: S-adenosyl-L-methionine + phospholipid olefinic fatty acid <=> S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid.
Pssm-ID: 396777 [Multi-domain] Cd Length: 272 Bit Score: 333.52 E-value: 1.13e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 125 EEIHAHYDISNDFYRLWLDDTMTYSCAYFANEKDTLTQAQENKVQHILKKLNPKPGKTLVDIGCGWGTLMLTACEQYQLK 204
Cdd:pfam02353 7 ENIQAHYDLSNDFFALFLDPTMTYSCAYFERPDMTLEEAQQAKLDLILDKLGLKPGMTLLDIGCGWGGLMRRAAERYDVN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 205 VTGITLSEEQYNYVQEQIEKRNLQDRAEVLLMDYRNLKGRhFDYVTSVGMFEHVGSQELPNYFQIVSDLLSEGGNALIHG 284
Cdd:pfam02353 87 VVGLTLSKNQYKLARKRVAAEGLARKVEVLLQDYRDFDEP-FDRIVSVGMFEHVGHENYDTFFKKLYNLLPPGGLMLLHT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 285 ITS------QQNGGTDPWLDKYIFPGGYIPSMVEILEDTRSAGLQLFDLETLRRHYQKTLECWTDNFHQCKDEVLKMEGE 358
Cdd:pfam02353 166 ITGlhpdetSERGLPLKFIDKYIFPGGELPSISMIVESSSEAGFTVEDVESLRPHYAKTLDLWAENLQANKDEAIALQSE 245
|
250 260
....*....|....*....|....*..
gi 497158116 359 RFYRMWDAYLQACAGSFAAGNIDCCQY 385
Cdd:pfam02353 246 EFYRMWMLYLTGCAVAFRIGYIDVHQF 272
|
|
| cyclopro_CfaB |
NF040703 |
C17 cyclopropane fatty acid synthase CfaB; |
63-404 |
6.13e-96 |
|
C17 cyclopropane fatty acid synthase CfaB;
Pssm-ID: 468667 [Multi-domain] Cd Length: 393 Bit Score: 292.67 E-value: 6.13e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 63 LGEAYMDGLVDVEGenrPLERLVEFAYEMMLKLQQNAtwtkwvSTTMKVKQkfhRHTPSENKEEIHAHYDISNDFYRLWL 142
Cdd:NF040703 55 LGSAYVEGRLDLEG---PIMEVIRVGDELSQALLGDD------DEAPPERT---AHDKATDAAAISYHYDLSNDFYALWL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 143 DDTMTYSCAYFANEKDTLTQAQENKVQHILKKLNPKPGKTLVDIGCGWGTLMLTACEQYQLKVTGITLSEEQYNYVQEQI 222
Cdd:NF040703 123 DPDMVYSCAYFETGTEDLAQAQQAKLRHLCRKLRLQPGERLLDVGCGWGGLARFAAREFGVEVFGITLSKEQLKLARERV 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 223 EKRNLQDRAEVLLMDYRNLKGR-HFDYVTSVGMFEHVGSQELPNYFQIVSDLLSEGGNALIHGITS------QQNGGTDP 295
Cdd:NF040703 203 AAEGLQDRVQLELLDYRDLPQDgRFDKVVSVGMFEHVGHANLPLYCQRLFGAVRPGGLVMNHGITArhtdgrPVGRGAGE 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 296 WLDKYIFPGGYIPSMVEILEDTRSAGLQLFDLETLRRHYQKTLECWTDNFHQCKDEVLKMEGERFYRMWDAYLQACAGSF 375
Cdd:NF040703 283 FIGRYVFPHGELPHLATITASISEAGLEVVDVESLRLHYARTLEHWSARLEARLDEAARLVPERALRIWRLYLAGCAYGF 362
|
330 340 350
....*....|....*....|....*....|..
gi 497158116 376 AAGNIDCCQYLLTKgP---SGMNLPMTREYMY 404
Cdd:NF040703 363 ARGWINLHQILAVK-PladGSHELPWTRADLY 393
|
|
| PRK11705 |
PRK11705 |
cyclopropane fatty acyl phospholipid synthase; |
52-389 |
9.74e-90 |
|
cyclopropane fatty acyl phospholipid synthase;
Pssm-ID: 183282 Cd Length: 383 Bit Score: 276.34 E-value: 9.74e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 52 KDCMKKGvSMYLGEAYMDGLVDVEgenrpleRLVEFAYEMM---LKLQQNATWTKWVSTTM-KVkqkFHRHTPSENKEEI 127
Cdd:PRK11705 48 KRVLQEG-SLGLGESYMDGWWDCD-------RLDEFFSRVLragLDEKLPHHLKDTLRILRaRL---FNLQSKKRAWIVG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 128 HAHYDISNDFYRLWLDDTMTYSCAYFaNEKDTLTQAQENKVQHILKKLNPKPGKTLVDIGCGWGTLMLTACEQYQLKVTG 207
Cdd:PRK11705 117 KEHYDLGNDLFEAMLDPRMQYSCGYW-KDADTLEEAQEAKLDLICRKLQLKPGMRVLDIGCGWGGLARYAAEHYGVSVVG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 208 ITLSEEQYNYVQEQIEKRNLqdraEVLLMDYRNLKGRhFDYVTSVGMFEHVGSQELPNYFQIVSDLLSEGGNALIHGITS 287
Cdd:PRK11705 196 VTISAEQQKLAQERCAGLPV----EIRLQDYRDLNGQ-FDRIVSVGMFEHVGPKNYRTYFEVVRRCLKPDGLFLLHTIGS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 288 QQNG-GTDPWLDKYIFPGGYIPSMVEILEDTRSaglqLF---DLETLRRHYQKTLECWTDNFHQCKDEVLKMEGERFYRM 363
Cdd:PRK11705 271 NKTDtNVDPWINKYIFPNGCLPSVRQIAQASEG----LFvmeDWHNFGADYDRTLMAWHENFEAAWPELADNYSERFYRM 346
|
330 340
....*....|....*....|....*.
gi 497158116 364 WDAYLQACAGSFAAGNIDCCQYLLTK 389
Cdd:PRK11705 347 WRYYLLSCAGAFRARDIQLWQVVFSP 372
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
129-284 |
1.15e-75 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 232.13 E-value: 1.15e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 129 AHYDISNDFYRLWLDDTMTYSCAYFANEKDTLTQAQENKVQHILKKLNPKPGKTLVDIGCGWGTLMLTACEQYQLKVTGI 208
Cdd:COG2230 1 HHYDLGNDFYRLFLDPTMTYSCAYFEDPDDTLEEAQEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497158116 209 TLSEEQYNYVQEQIEKRNLQDRAEVLLMDYRNLKG-RHFDYVTSVGMFEHVGSQELPNYFQIVSDLLSEGGNALIHG 284
Cdd:COG2230 81 TLSPEQLEYARERAAEAGLADRVEVRLADYRDLPAdGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLLHT 157
|
|
| mycolic_MTase |
NF040660 |
cyclopropane mycolic acid synthase family methyltransferase; Members of this family include ... |
125-389 |
1.62e-71 |
|
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: 226.19 E-value: 1.62e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 125 EEIHAHYDISNDFYRLWLDDTMTYSCAYFANEKDTLTQAQENKVQHILKKLNPKPGKTLVDIGCGWGTLMLTACEQYQLK 204
Cdd:NF040660 6 EDVQAHYDLSDDFFALFLDPTQTYSCAYFERDDMTLEEAQIAKIDLALGKLNLEPGMTLLDIGCGWGATMRRAVEKYDVN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 205 VTGITLSEEQYNYVQEQIEKRNLQDRAEVLLMDYRNLKgRHFDYVTSVGMFEHVGSQELPNYFQIVSDLLSEGGNALIHG 284
Cdd:NF040660 86 VVGLTLSKNQAAHVQQVLDEIDTPRSRRVLLQGWEEFD-EPVDRIVSIGAFEHFGHERYDDFFKRAYNILPADGRMLLHT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 285 ITS------QQNGGTDP-WLDKY-------IFPGGYIPSMVEILEDTRSAGLQLFDLETLRRHYQKTLECWTDNFHQCKD 350
Cdd:NF040660 165 ITGlhrkemHERGLPLTmELARFikfivteIFPGGRLPSIEMVVEHAEKAGFTVTRVQSLQPHYARTLDLWADALQAHKD 244
|
250 260 270
....*....|....*....|....*....|....*....
gi 497158116 351 EVLKMEGERFYRMWDAYLQACAGSFAAGNIDCCQYLLTK 389
Cdd:NF040660 245 EAIAIQSEEVYERYMKYLTGCAKLFRDGYIDVNQFTLAK 283
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
185-278 |
7.76e-17 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 75.29 E-value: 7.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 185 DIGCGWGTLMLTACEQYQLKVTGITLSEEQYNYVQEQIEKRNLqdRAEVLLMDYRNL--KGRHFDYVTSVGMFEHVGSQE 262
Cdd:pfam13649 3 DLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAEDLpfPDGSFDLVVSSGVLHHLPDPD 80
|
90
....*....|....*.
gi 497158116 263 LPNYFQIVSDLLSEGG 278
Cdd:pfam13649 81 LEAALREIARVLKPGG 96
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
169-302 |
6.01e-13 |
|
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: 65.79 E-value: 6.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 169 QHILKKLNPKPGKTLVDIGCGWGTLMLTACEQyQLKVTGITLSEEQYNYVQEQIEKRNLqdRAEVLLMDYRNL--KGRHF 246
Cdd:COG2226 12 EALLAALGLRPGARVLDLGCGTGRLALALAER-GARVTGVDISPEMLELARERAAEAGL--NVEFVVGDAEDLpfPDGSF 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 497158116 247 DYVTSVGMFEHVgsQELPNYFQIVSDLLSEGGNALIHGITSQQNGGTDPWLDKYIF 302
Cdd:COG2226 89 DLVISSFVLHHL--PDPERALAEIARVLKPGGRLVVVDFSPPDLAELEELLAEAGF 142
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
178-289 |
1.32e-12 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 66.09 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 178 KPGKTLVDIGCGWGTLMLTACEQYQLKVTGITLSEEQYNYVQEQIEKRNLqDRAEVLLMDYRNLKG---RHFDYVTSVGM 254
Cdd:COG0500 25 PKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAGL-GNVEFLVADLAELDPlpaESFDLVVAFGV 103
|
90 100 110
....*....|....*....|....*....|....*
gi 497158116 255 FEHVGSQELPNYFQIVSDLLSEGGNALIHGITSQQ 289
Cdd:COG0500 104 LHHLPPEEREALLRELARALKPGGVLLLSASDAAA 138
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
165-278 |
3.21e-12 |
|
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: 63.11 E-value: 3.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 165 ENKVQHILKKLNPkPGKTLVDIGCGWGTLMLtACEQYQLKVTGITLSEEQYNYVQEQIEKRNLqdraEVLLMDYRNL--K 242
Cdd:COG2227 11 DRRLAALLARLLP-AGGRVLDVGCGTGRLAL-ALARRGADVTGVDISPEALEIARERAAELNV----DFVQGDLEDLplE 84
|
90 100 110
....*....|....*....|....*....|....*.
gi 497158116 243 GRHFDYVTSVGMFEHVgsQELPNYFQIVSDLLSEGG 278
Cdd:COG2227 85 DGSFDLVICSEVLEHL--PDPAALLRELARLLKPGG 118
|
|
| COG4976 |
COG4976 |
Predicted methyltransferase, contains TPR repeat [General function prediction only]; |
122-278 |
1.27e-11 |
|
Predicted methyltransferase, contains TPR repeat [General function prediction only];
Pssm-ID: 444001 [Multi-domain] Cd Length: 181 Bit Score: 63.09 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 122 ENKEEIHAHYDISNDFYRLWLDDTMTYscayfanekdtltQAQENKVQHILKKLNPKPGKTLVDIGCG---WGTLMLTAC 198
Cdd:COG4976 2 ALDAYVEALFDQYADSYDAALVEDLGY-------------EAPALLAEELLARLPPGPFGRVLDLGCGtglLGEALRPRG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 199 eqyqLKVTGITLSEEQYnyvqEQIEKRNLQDRaeVLLMDYRNLK--GRHFDYVTSVGMFEHVGsqELPNYFQIVSDLLSE 276
Cdd:COG4976 69 ----YRLTGVDLSEEML----AKAREKGVYDR--LLVADLADLAepDGRFDLIVAADVLTYLG--DLAAVFAGVARALKP 136
|
..
gi 497158116 277 GG 278
Cdd:COG4976 137 GG 138
|
|
| Methyltransf_23 |
pfam13489 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
165-332 |
1.86e-09 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 404385 [Multi-domain] Cd Length: 162 Bit Score: 56.28 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 165 ENKVQHILKKL--NPKPGKTLVDIGCGWGTlMLTACEQYQLKVTGITLSEEQynyvqeqIEKRNLQDRAEVLLMDYRNLK 242
Cdd:pfam13489 6 ERLLADLLLRLlpKLPSPGRVLDFGCGTGI-FLRLLRAQGFSVTGVDPSPIA-------IERALLNVRFDQFDEQEAAVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 243 GRHFDYVTSVGMFEHVgsQELPNYFQIVSDLLSEGGNALIHgiTSQQNGGTDPWLDK--YIFPggyipsmveiledtRSA 320
Cdd:pfam13489 78 AGKFDVIVAREVLEHV--PDPPALLRQIAALLKPGGLLLLS--TPLASDEADRLLLEwpYLRP--------------RNG 139
|
170
....*....|..
gi 497158116 321 GLQLFDLETLRR 332
Cdd:pfam13489 140 HISLFSARSLKR 151
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
182-278 |
8.00e-09 |
|
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: 52.82 E-value: 8.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 182 TLVDIGCGWGTLMLTACEQYQLKVTGITLSEEQYNYVQeQIEKRNLQDRAEVLLMDYRNL---KGRHFDYVTSVGMFEHV 258
Cdd:cd02440 1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELAR-KAAAALLADNVEVLKGDAEELppeADESFDVIISDPPLHHL 79
|
90 100
....*....|....*....|
gi 497158116 259 GsQELPNYFQIVSDLLSEGG 278
Cdd:cd02440 80 V-EDLARFLEEARRLLKPGG 98
|
|
| Tam |
COG4106 |
Trans-aconitate methyltransferase [Energy production and conversion]; |
179-278 |
1.94e-08 |
|
Trans-aconitate methyltransferase [Energy production and conversion];
Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 51.75 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 179 PGKTLVDIGCGWGTLMLTACEQY-QLKVTGITLSEeqynyvqEQIEK-RNLQDRAEVLLMDYRNLK-GRHFDYVTSVGMF 255
Cdd:COG4106 1 PPRRVLDLGCGTGRLTALLAERFpGARVTGVDLSP-------EMLARaRARLPNVRFVVADLRDLDpPEPFDLVVSNAAL 73
|
90 100
....*....|....*....|...
gi 497158116 256 EHVgsQELPNYFQIVSDLLSEGG 278
Cdd:COG4106 74 HWL--PDHAALLARLAAALAPGG 94
|
|
| Methyltransf_12 |
pfam08242 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
184-278 |
7.55e-08 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 50.06 E-value: 7.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 184 VDIGCGWGTLMLTACEQY-QLKVTGITLSEEQYNYVQEQIEKRNLQD--RAEVLLMDYRNLKGRHFDYVTSVGMFEHVGs 260
Cdd:pfam08242 1 LEIGCGTGTLLRALLEALpGLEYTGLDISPAALEAARERLAALGLLNavRVELFQLDLGELDPGSFDVVVASNVLHHLA- 79
|
90
....*....|....*...
gi 497158116 261 qELPNYFQIVSDLLSEGG 278
Cdd:pfam08242 80 -DPRAVLRNIRRLLKPGG 96
|
|
| Methyltransf_11 |
pfam08241 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
184-258 |
2.30e-06 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 462406 [Multi-domain] Cd Length: 94 Bit Score: 45.73 E-value: 2.30e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497158116 184 VDIGCGWGtLMLTACEQYQLKVTGITLSEEQYNYVQEQIEKRNLqdraEVLLMDYRNL--KGRHFDYVTSVGMFEHV 258
Cdd:pfam08241 1 LDVGCGTG-LLTELLARLGARVTGVDISPEMLELAREKAPREGL----TFVVGDAEDLpfPDNSFDLVLSSEVLHHV 72
|
|
| ubiE |
PRK00216 |
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ... |
115-250 |
6.08e-06 |
|
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;
Pssm-ID: 234689 [Multi-domain] Cd Length: 239 Bit Score: 47.07 E-value: 6.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 115 FHRHTPSENKEEIHA-------HYDISNDF-----YRLWLDDTMtyscayfanekdtltqaqenkvqhilKKLNPKPGKT 182
Cdd:PRK00216 1 FMTVAEEEKQEKVAEmfdsiapKYDLMNDLlsfglHRVWRRKTI--------------------------KWLGVRPGDK 54
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497158116 183 LVDIGCGWGTLMLTACEQYQL--KVTGITLSEEQYNYVQEQIEKRNLQDRAEVLLMDYRNL--KGRHFDYVT 250
Cdd:PRK00216 55 VLDLACGTGDLAIALAKAVGKtgEVVGLDFSEGMLAVGREKLRDLGLSGNVEFVQGDAEALpfPDNSFDAVT 126
|
|
| TrmN6 |
COG4123 |
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ... |
176-283 |
6.97e-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: 47.06 E-value: 6.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 176 NPKPGKTLVDIGCGWGT--LMLtACEQYQLKVTGITLSEEQYNYVQEQIEKRNLQDRAEVLLMDYRN----LKGRHFDYV 249
Cdd:COG4123 34 PVKKGGRVLDLGTGTGViaLML-AQRSPGARITGVEIQPEAAELARRNVALNGLEDRITVIHGDLKEfaaeLPPGSFDLV 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 497158116 250 TS------VGMFE-----------HVGSQELPNYFQIVSDLLSEGGN-ALIH 283
Cdd:COG4123 113 VSnppyfkAGSGRkspdearaiarHEDALTLEDLIRAAARLLKPGGRfALIH 164
|
|
| PRK09328 |
PRK09328 |
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional |
168-251 |
5.85e-05 |
|
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
Pssm-ID: 236467 [Multi-domain] Cd Length: 275 Bit Score: 44.38 E-value: 5.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 168 VQHILKKLNPKPGKTLVDIGCGWGTLMLT-ACEQYQLKVTGITLSEEQYNYVQEQIeKRNLQDRAEVLLMD-YRNLKGRH 245
Cdd:PRK09328 97 VEWALEALLLKEPLRVLDLGTGSGAIALAlAKERPDAEVTAVDISPEALAVARRNA-KHGLGARVEFLQGDwFEPLPGGR 175
|
....*.
gi 497158116 246 FDYVTS 251
Cdd:PRK09328 176 FDLIVS 181
|
|
| PKS_MT |
smart00828 |
Methyltransferase in polyketide synthase (PKS) enzymes; |
185-278 |
1.50e-04 |
|
Methyltransferase in polyketide synthase (PKS) enzymes;
Pssm-ID: 214839 [Multi-domain] Cd Length: 224 Bit Score: 42.79 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 185 DIGCGWGTLMLTACEQY-QLKVTGITLSEEQYNYVQEQIEKRNLQDRAEVLlmdYRNLKGRHF-DYVTSVGMFEHVGS-Q 261
Cdd:smart00828 5 DFGCGYGSDLIDLAERHpHLQLHGYTISPEQAEVGRERIRALGLQGRIRIF---YRDSAKDPFpDTYDLVFGFEVIHHiK 81
|
90
....*....|....*..
gi 497158116 262 ELPNYFQIVSDLLSEGG 278
Cdd:smart00828 82 DKMDLFSNISRHLKDGG 98
|
|
| RsmC |
COG2813 |
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ... |
172-249 |
2.04e-04 |
|
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: 42.10 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 172 LKKLNPKPGKTLVDIGCGWGTLMLTACEQY-QLKVTG-------ITLSEEqyNYvqeqieKRNLQDRAEVLLMD-YRNLK 242
Cdd:COG2813 42 LEHLPEPLGGRVLDLGCGYGVIGLALAKRNpEARVTLvdvnaraVELARA--NA------AANGLENVEVLWSDgLSGVP 113
|
....*..
gi 497158116 243 GRHFDYV 249
Cdd:COG2813 114 DGSFDLI 120
|
|
| PRK08317 |
PRK08317 |
hypothetical protein; Provisional |
169-258 |
6.37e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 181382 [Multi-domain] Cd Length: 241 Bit Score: 41.08 E-value: 6.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 169 QHILKKLNPKPGKTLVDIGCGWGTLmltACEQYQL-----KVTGITLSEEQYNYVQEQIEkrNLQDRAEVLLMDYRNLKG 243
Cdd:PRK08317 9 ARTFELLAVQPGDRVLDVGCGPGND---ARELARRvgpegRVVGIDRSEAMLALAKERAA--GLGPNVEFVRGDADGLPF 83
|
90
....*....|....*..
gi 497158116 244 R--HFDYVTSVGMFEHV 258
Cdd:PRK08317 84 PdgSFDAVRSDRVLQHL 100
|
|
| PLN02244 |
PLN02244 |
tocopherol O-methyltransferase |
119-273 |
1.79e-03 |
|
tocopherol O-methyltransferase
Pssm-ID: 215135 [Multi-domain] Cd Length: 340 Bit Score: 40.11 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 119 TPSENKEEIHAHYDISNDFY-RLWlDDTMTYscAYFANEKDT--LTQAQENKVQHILK-----KLNPKPGKTLVDIGCGW 190
Cdd:PLN02244 53 ATADLKEGIAEFYDESSGVWeDVW-GEHMHH--GYYDPGASRgdHRQAQIRMIEESLAwagvpDDDEKRPKRIVDVGCGI 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 191 GTLMLTACEQYQLKVTGITLSEEQYNYVQEQIEKRNLQDRAEVLLMDYRNL--KGRHFDYVTSVGMFEHVgsqelPNYFQ 268
Cdd:PLN02244 130 GGSSRYLARKYGANVKGITLSPVQAARANALAAAQGLSDKVSFQVADALNQpfEDGQFDLVWSMESGEHM-----PDKRK 204
|
....*
gi 497158116 269 IVSDL 273
Cdd:PLN02244 205 FVQEL 209
|
|
| PLN02336 |
PLN02336 |
phosphoethanolamine N-methyltransferase |
174-282 |
2.33e-03 |
|
phosphoethanolamine N-methyltransferase
Pssm-ID: 177970 [Multi-domain] Cd Length: 475 Bit Score: 40.12 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 174 KLNPKPGKTLVDIGCGWGTLMLTACEQYQLKVTGITLSEEQYNYVQEQIEKRNLQDRAEVLLMDYRNLKGRHFDYVTSVG 253
Cdd:PLN02336 261 KLDLKPGQKVLDVGCGIGGGDFYMAENFDVHVVGIDLSVNMISFALERAIGRKCSVEFEVADCTKKTYPDNSFDVIYSRD 340
|
90 100
....*....|....*....|....*....
gi 497158116 254 MFEHVgsQELPNYFQIVSDLLSEGGNALI 282
Cdd:PLN02336 341 TILHI--QDKPALFRSFFKWLKPGGKVLI 367
|
|
| Methyltransf_31 |
pfam13847 |
Methyltransferase domain; This family appears to have methyltransferase activity. |
177-278 |
2.85e-03 |
|
Methyltransferase domain; This family appears to have methyltransferase activity.
Pssm-ID: 463998 [Multi-domain] Cd Length: 150 Bit Score: 38.17 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 177 PKPGKTLVDIGCGWGTLMLTACEQ--YQLKVTGITLSEEQYNYVQEQIEKRNLQ----DRAEVLLMDyRNLKGRHFDYVT 250
Cdd:pfam13847 1 IDKGMRVLDLGCGTGHLSFELAEElgPNAEVVGIDISEEAIEKARENAQKLGFDnvefEQGDIEELP-ELLEDDKFDVVI 79
|
90 100
....*....|....*....|....*...
gi 497158116 251 SVGMFEHVGSQELpnYFQIVSDLLSEGG 278
Cdd:pfam13847 80 SNCVLNHIPDPDK--VLQEILRVLKPGG 105
|
|
| CbiT |
TIGR02469 |
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ... |
171-229 |
3.26e-03 |
|
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes the CbiT methylase which is responsible, in part (along with CbiE), for methylating precorrin-6y (or cobalt-precorrin-6y) at both the 5 and 15 positions as well as the concomitant decarbozylation at C-12. In many organisms, this protein is fused to the CbiE subunit. The fused protein, when found in organisms catalyzing the oxidative version of the cobalamin biosynthesis pathway, is called CobL. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
Pssm-ID: 274148 [Multi-domain] Cd Length: 124 Bit Score: 37.31 E-value: 3.26e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 171 ILKKLNPKPGKTLVDIGCGWGTLMLTACEQY-QLKVTGITLSEEqynyVQEQIEkRNLQD 229
Cdd:TIGR02469 11 TLAKLRLRPGDVLWDIGAGTGSVTIEAARLVpNGRVYAIERNPE----ALDLIE-RNLRR 65
|
|
| TrmR |
COG4122 |
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ... |
178-284 |
3.42e-03 |
|
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; tRNA 5-hydroxyU34 O-methylase TrmR/YrrM is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 443298 Cd Length: 173 Bit Score: 38.24 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 178 KPGKTLVDIGCGWG--TL-MLTACEQyQLKVTGITLSEEQYNYVQEQIEKRNLQDRAEVLLMD----YRNLKGRHFDYVt 250
Cdd:COG4122 15 LGAKRILEIGTGTGysTLwLARALPD-DGRLTTIEIDPERAAIARENFARAGLADRIRLILGDalevLPRLADGPFDLV- 92
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 497158116 251 svgmF---EHvgsQELPNYFQIVSDLLSEGG-----NALIHG 284
Cdd:COG4122 93 ----FidaDK---SNYPDYLELALPLLRPGGlivadNVLWHG 127
|
|
| PRK06202 |
PRK06202 |
hypothetical protein; Provisional |
182-277 |
5.29e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 180466 [Multi-domain] Cd Length: 232 Bit Score: 38.06 E-value: 5.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497158116 182 TLVDIGCGWG----TLMLTACEQ-YQLKVTGITLSEEQYNYVQEQIEKRNLQDRAEV---LLMDyrnlkGRHFDYVTSVG 253
Cdd:PRK06202 63 TLLDIGCGGGdlaiDLARWARRDgLRLEVTAIDPDPRAVAFARANPRRPGVTFRQAVsdeLVAE-----GERFDVVTSNH 137
|
90 100
....*....|....*....|....
gi 497158116 254 MFEHVGSQELPNYFQiVSDLLSEG 277
Cdd:PRK06202 138 FLHHLDDAEVVRLLA-DSAALARR 160
|
|
| |
