|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11705 |
PRK11705 |
cyclopropane fatty acyl phospholipid synthase; |
1-382 |
0e+00 |
|
cyclopropane fatty acyl phospholipid synthase;
Pssm-ID: 183282 Cd Length: 383 Bit Score: 786.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 1 MSNVCIVDDISEKNEWRRITQELLHQASITINGTEPWDIQINDSRFFKRVLQQGSLGLGESYMEGWWDCPRLDMFFHRIL 80
Cdd:PRK11705 1 MSSSCIEEVSVPDDNWYRIANELLARAGITINGSRPWDIQVHNPRFFKRVLQEGSLGLGESYMDGWWDCDRLDEFFSRVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 81 AARLDEQRPSRWRDLMRIALARLVNLQSRKRAWQVGKVHYDLGNDLFSHMLDPYMQYSCGYWKQADTLEEAQQHKLALIC 160
Cdd:PRK11705 81 RAGLDEKLPHHLKDTLRILRARLFNLQSKKRAWIVGKEHYDLGNDLFEAMLDPRMQYSCGYWKDADTLEEAQEAKLDLIC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 161 EKLQLKPGMTLLDIGCGWGGLAVYAAQHYGVTVHGITISAEQKAFIEERCGELDIHILLQDYRDLHQQYDRIVSVGMFEH 240
Cdd:PRK11705 161 RKLQLKPGMRVLDIGCGWGGLARYAAEHYGVSVVGVTISAEQQKLAQERCAGLPVEIRLQDYRDLNGQFDRIVSVGMFEH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 241 VGPKNYADYFEMADRCLKPDGLFLLHTIGSNTTAHNVDPWINKYIFPNGCLPSIKQIASTSEPYFVMEDWHNFGADYDKT 320
Cdd:PRK11705 241 VGPKNYRTYFEVVRRCLKPDGLFLLHTIGSNKTDTNVDPWINKYIFPNGCLPSVRQIAQASEGLFVMEDWHNFGADYDRT 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1718143695 321 LMAWLARFNTAWPQLAADYSPAFRRMFSYYLTACAGAFRARNIQLWQVLFS-RGVTHGLCVPR 382
Cdd:PRK11705 321 LMAWHENFEAAWPELADNYSERFYRMWRYYLLSCAGAFRARDIQLWQVVFSpRGVEGGYRVPR 383
|
|
| CMAS |
pfam02353 |
Mycolic acid cyclopropane synthetase; This family consist of ... |
108-368 |
6.54e-126 |
|
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: 363.57 E-value: 6.54e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 108 SRKRAWQVGKVHYDLGNDLFSHMLDPYMQYSCGYWKQAD-TLEEAQQHKLALICEKLQLKPGMTLLDIGCGWGGLAVYAA 186
Cdd:pfam02353 1 SKTRDAENIQAHYDLSNDFFALFLDPTMTYSCAYFERPDmTLEEAQQAKLDLILDKLGLKPGMTLLDIGCGWGGLMRRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 187 QHYGVTVHGITISAEQKAFIEERCGELD----IHILLQDYRDLHQQYDRIVSVGMFEHVGPKNYADYFEMADRCLKPDGL 262
Cdd:pfam02353 81 ERYDVNVVGLTLSKNQYKLARKRVAAEGlarkVEVLLQDYRDFDEPFDRIVSVGMFEHVGHENYDTFFKKLYNLLPPGGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 263 FLLHTIGS-----NTTAHNVDPWINKYIFPNGCLPSIKQIAST-SEPYFVMEDWHNFGADYDKTLMAWLARFNTAWPQLA 336
Cdd:pfam02353 161 MLLHTITGlhpdeTSERGLPLKFIDKYIFPGGELPSISMIVESsSEAGFTVEDVESLRPHYAKTLDLWAENLQANKDEAI 240
|
250 260 270
....*....|....*....|....*....|..
gi 1718143695 337 ADYSPAFRRMFSYYLTACAGAFRARNIQLWQV 368
Cdd:pfam02353 241 ALQSEEFYRMWMLYLTGCAVAFRIGYIDVHQF 272
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
119-267 |
4.00e-80 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 242.53 E-value: 4.00e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 119 HYDLGNDLFSHMLDPYMQYSCGYWKQAD-TLEEAQQHKLALICEKLQLKPGMTLLDIGCGWGGLAVYAAQHYGVTVHGIT 197
Cdd:COG2230 2 HYDLGNDFYRLFLDPTMTYSCAYFEDPDdTLEEAQEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGVT 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1718143695 198 ISAEQKAFIEERCGELD----IHILLQDYRDL--HQQYDRIVSVGMFEHVGPKNYADYFEMADRCLKPDGLFLLHT 267
Cdd:COG2230 82 LSPEQLEYARERAAEAGladrVEVRLADYRDLpaDGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLLHT 157
|
|
| cyclopro_CfaB |
NF040703 |
C17 cyclopropane fatty acid synthase CfaB; |
119-369 |
1.58e-66 |
|
C17 cyclopropane fatty acid synthase CfaB;
Pssm-ID: 468667 [Multi-domain] Cd Length: 393 Bit Score: 215.63 E-value: 1.58e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 119 HYDLGNDLFSHMLDPYMQYSCGYWKQA-DTLEEAQQHKLALICEKLQLKPGMTLLDIGCGWGGLAVYAAQHYGVTVHGIT 197
Cdd:NF040703 110 HYDLSNDFYALWLDPDMVYSCAYFETGtEDLAQAQQAKLRHLCRKLRLQPGERLLDVGCGWGGLARFAAREFGVEVFGIT 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 198 ISAEQKAFIEERCGE--LD--IHILLQDYRDLHQ--QYDRIVSVGMFEHVGPKNYADYFEMADRCLKPDGLFLLHTIgsn 271
Cdd:NF040703 190 LSKEQLKLARERVAAegLQdrVQLELLDYRDLPQdgRFDKVVSVGMFEHVGHANLPLYCQRLFGAVRPGGLVMNHGI--- 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 272 tTAHNVD---------PWINKYIFPNGCLPSIKQI-ASTSEPYFVMEDWHNFGADYDKTLMAWLARFNTAWPQLAADYSP 341
Cdd:NF040703 267 -TARHTDgrpvgrgagEFIGRYVFPHGELPHLATItASISEAGLEVVDVESLRLHYARTLEHWSARLEARLDEAARLVPE 345
|
250 260
....*....|....*....|....*...
gi 1718143695 342 AFRRMFSYYLTACAGAFRARNIQLWQVL 369
Cdd:NF040703 346 RALRIWRLYLAGCAYGFARGWINLHQIL 373
|
|
| mycolic_MTase |
NF040660 |
cyclopropane mycolic acid synthase family methyltransferase; Members of this family include ... |
119-368 |
1.73e-57 |
|
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: 188.82 E-value: 1.73e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 119 HYDLGNDLFSHMLDPYMQYSCGYWKQAD-TLEEAQQHKLALICEKLQLKPGMTLLDIGCGWGGLAVYAAQHYGVTVHGIT 197
Cdd:NF040660 11 HYDLSDDFFALFLDPTQTYSCAYFERDDmTLEEAQIAKIDLALGKLNLEPGMTLLDIGCGWGATMRRAVEKYDVNVVGLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 198 ISAEQKAFIEERCGELDI----HILLQDYRDLHQQYDRIVSVGMFEHVGPKNYADYFEMADRCLKPDGLFLLHTIGSNTT 273
Cdd:NF040660 91 LSKNQAAHVQQVLDEIDTprsrRVLLQGWEEFDEPVDRIVSIGAFEHFGHERYDDFFKRAYNILPADGRMLLHTITGLHR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 274 AHNVD-------------PWINKYIFPNGCLPSIKQIASTSEPY-FVMEDWHNFGADYDKTLMAWLARFNTAWPQLAADY 339
Cdd:NF040660 171 KEMHErglpltmelarfiKFIVTEIFPGGRLPSIEMVVEHAEKAgFTVTRVQSLQPHYARTLDLWADALQAHKDEAIAIQ 250
|
250 260
....*....|....*....|....*....
gi 1718143695 340 SPAFRRMFSYYLTACAGAFRARNIQLWQV 368
Cdd:NF040660 251 SEEVYERYMKYLTGCAKLFRDGYIDVNQF 279
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
170-266 |
2.61e-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: 2.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 170 TLLDIGCGWGGLAVYAAQHYGVTVHGITISAEQKAFIEE---RCGELDIHILLQDYRDLH----QQYDRIVSVGMFEHVg 242
Cdd:cd02440 1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKaaaALLADNVEVLKGDAEELPpeadESFDVIISDPPLHHL- 79
|
90 100
....*....|....*....|....
gi 1718143695 243 PKNYADYFEMADRCLKPDGLFLLH 266
Cdd:cd02440 80 VEDLARFLEEARRLLKPGGVLVLT 103
|
|
| PKS_MT |
smart00828 |
Methyltransferase in polyketide synthase (PKS) enzymes; |
172-272 |
4.35e-07 |
|
Methyltransferase in polyketide synthase (PKS) enzymes;
Pssm-ID: 214839 [Multi-domain] Cd Length: 224 Bit Score: 50.49 E-value: 4.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 172 LDIGCGWG-GLAVYAAQHYGVTVHGITISAEQKAFIEERCGELdihiLLQD-----YRDLHQQ-----YDRIVSVGMFEH 240
Cdd:smart00828 4 LDFGCGYGsDLIDLAERHPHLQLHGYTISPEQAEVGRERIRAL----GLQGririfYRDSAKDpfpdtYDLVFGFEVIHH 79
|
90 100 110
....*....|....*....|....*....|..
gi 1718143695 241 VgpKNYADYFEMADRCLKPDGLFLLHTIGSNT 272
Cdd:smart00828 80 I--KDKMDLFSNISRHLKDGGHLVLADFIANL 109
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11705 |
PRK11705 |
cyclopropane fatty acyl phospholipid synthase; |
1-382 |
0e+00 |
|
cyclopropane fatty acyl phospholipid synthase;
Pssm-ID: 183282 Cd Length: 383 Bit Score: 786.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 1 MSNVCIVDDISEKNEWRRITQELLHQASITINGTEPWDIQINDSRFFKRVLQQGSLGLGESYMEGWWDCPRLDMFFHRIL 80
Cdd:PRK11705 1 MSSSCIEEVSVPDDNWYRIANELLARAGITINGSRPWDIQVHNPRFFKRVLQEGSLGLGESYMDGWWDCDRLDEFFSRVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 81 AARLDEQRPSRWRDLMRIALARLVNLQSRKRAWQVGKVHYDLGNDLFSHMLDPYMQYSCGYWKQADTLEEAQQHKLALIC 160
Cdd:PRK11705 81 RAGLDEKLPHHLKDTLRILRARLFNLQSKKRAWIVGKEHYDLGNDLFEAMLDPRMQYSCGYWKDADTLEEAQEAKLDLIC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 161 EKLQLKPGMTLLDIGCGWGGLAVYAAQHYGVTVHGITISAEQKAFIEERCGELDIHILLQDYRDLHQQYDRIVSVGMFEH 240
Cdd:PRK11705 161 RKLQLKPGMRVLDIGCGWGGLARYAAEHYGVSVVGVTISAEQQKLAQERCAGLPVEIRLQDYRDLNGQFDRIVSVGMFEH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 241 VGPKNYADYFEMADRCLKPDGLFLLHTIGSNTTAHNVDPWINKYIFPNGCLPSIKQIASTSEPYFVMEDWHNFGADYDKT 320
Cdd:PRK11705 241 VGPKNYRTYFEVVRRCLKPDGLFLLHTIGSNKTDTNVDPWINKYIFPNGCLPSVRQIAQASEGLFVMEDWHNFGADYDRT 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1718143695 321 LMAWLARFNTAWPQLAADYSPAFRRMFSYYLTACAGAFRARNIQLWQVLFS-RGVTHGLCVPR 382
Cdd:PRK11705 321 LMAWHENFEAAWPELADNYSERFYRMWRYYLLSCAGAFRARDIQLWQVVFSpRGVEGGYRVPR 383
|
|
| CMAS |
pfam02353 |
Mycolic acid cyclopropane synthetase; This family consist of ... |
108-368 |
6.54e-126 |
|
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: 363.57 E-value: 6.54e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 108 SRKRAWQVGKVHYDLGNDLFSHMLDPYMQYSCGYWKQAD-TLEEAQQHKLALICEKLQLKPGMTLLDIGCGWGGLAVYAA 186
Cdd:pfam02353 1 SKTRDAENIQAHYDLSNDFFALFLDPTMTYSCAYFERPDmTLEEAQQAKLDLILDKLGLKPGMTLLDIGCGWGGLMRRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 187 QHYGVTVHGITISAEQKAFIEERCGELD----IHILLQDYRDLHQQYDRIVSVGMFEHVGPKNYADYFEMADRCLKPDGL 262
Cdd:pfam02353 81 ERYDVNVVGLTLSKNQYKLARKRVAAEGlarkVEVLLQDYRDFDEPFDRIVSVGMFEHVGHENYDTFFKKLYNLLPPGGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 263 FLLHTIGS-----NTTAHNVDPWINKYIFPNGCLPSIKQIAST-SEPYFVMEDWHNFGADYDKTLMAWLARFNTAWPQLA 336
Cdd:pfam02353 161 MLLHTITGlhpdeTSERGLPLKFIDKYIFPGGELPSISMIVESsSEAGFTVEDVESLRPHYAKTLDLWAENLQANKDEAI 240
|
250 260 270
....*....|....*....|....*....|..
gi 1718143695 337 ADYSPAFRRMFSYYLTACAGAFRARNIQLWQV 368
Cdd:pfam02353 241 ALQSEEFYRMWMLYLTGCAVAFRIGYIDVHQF 272
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
119-267 |
4.00e-80 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 242.53 E-value: 4.00e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 119 HYDLGNDLFSHMLDPYMQYSCGYWKQAD-TLEEAQQHKLALICEKLQLKPGMTLLDIGCGWGGLAVYAAQHYGVTVHGIT 197
Cdd:COG2230 2 HYDLGNDFYRLFLDPTMTYSCAYFEDPDdTLEEAQEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGVT 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1718143695 198 ISAEQKAFIEERCGELD----IHILLQDYRDL--HQQYDRIVSVGMFEHVGPKNYADYFEMADRCLKPDGLFLLHT 267
Cdd:COG2230 82 LSPEQLEYARERAAEAGladrVEVRLADYRDLpaDGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLLHT 157
|
|
| cyclopro_CfaB |
NF040703 |
C17 cyclopropane fatty acid synthase CfaB; |
119-369 |
1.58e-66 |
|
C17 cyclopropane fatty acid synthase CfaB;
Pssm-ID: 468667 [Multi-domain] Cd Length: 393 Bit Score: 215.63 E-value: 1.58e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 119 HYDLGNDLFSHMLDPYMQYSCGYWKQA-DTLEEAQQHKLALICEKLQLKPGMTLLDIGCGWGGLAVYAAQHYGVTVHGIT 197
Cdd:NF040703 110 HYDLSNDFYALWLDPDMVYSCAYFETGtEDLAQAQQAKLRHLCRKLRLQPGERLLDVGCGWGGLARFAAREFGVEVFGIT 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 198 ISAEQKAFIEERCGE--LD--IHILLQDYRDLHQ--QYDRIVSVGMFEHVGPKNYADYFEMADRCLKPDGLFLLHTIgsn 271
Cdd:NF040703 190 LSKEQLKLARERVAAegLQdrVQLELLDYRDLPQdgRFDKVVSVGMFEHVGHANLPLYCQRLFGAVRPGGLVMNHGI--- 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 272 tTAHNVD---------PWINKYIFPNGCLPSIKQI-ASTSEPYFVMEDWHNFGADYDKTLMAWLARFNTAWPQLAADYSP 341
Cdd:NF040703 267 -TARHTDgrpvgrgagEFIGRYVFPHGELPHLATItASISEAGLEVVDVESLRLHYARTLEHWSARLEARLDEAARLVPE 345
|
250 260
....*....|....*....|....*...
gi 1718143695 342 AFRRMFSYYLTACAGAFRARNIQLWQVL 369
Cdd:NF040703 346 RALRIWRLYLAGCAYGFARGWINLHQIL 373
|
|
| mycolic_MTase |
NF040660 |
cyclopropane mycolic acid synthase family methyltransferase; Members of this family include ... |
119-368 |
1.73e-57 |
|
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: 188.82 E-value: 1.73e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 119 HYDLGNDLFSHMLDPYMQYSCGYWKQAD-TLEEAQQHKLALICEKLQLKPGMTLLDIGCGWGGLAVYAAQHYGVTVHGIT 197
Cdd:NF040660 11 HYDLSDDFFALFLDPTQTYSCAYFERDDmTLEEAQIAKIDLALGKLNLEPGMTLLDIGCGWGATMRRAVEKYDVNVVGLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 198 ISAEQKAFIEERCGELDI----HILLQDYRDLHQQYDRIVSVGMFEHVGPKNYADYFEMADRCLKPDGLFLLHTIGSNTT 273
Cdd:NF040660 91 LSKNQAAHVQQVLDEIDTprsrRVLLQGWEEFDEPVDRIVSIGAFEHFGHERYDDFFKRAYNILPADGRMLLHTITGLHR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 274 AHNVD-------------PWINKYIFPNGCLPSIKQIASTSEPY-FVMEDWHNFGADYDKTLMAWLARFNTAWPQLAADY 339
Cdd:NF040660 171 KEMHErglpltmelarfiKFIVTEIFPGGRLPSIEMVVEHAEKAgFTVTRVQSLQPHYARTLDLWADALQAHKDEAIAIQ 250
|
250 260
....*....|....*....|....*....
gi 1718143695 340 SPAFRRMFSYYLTACAGAFRARNIQLWQV 368
Cdd:NF040660 251 SEEVYERYMKYLTGCAKLFRDGYIDVNQF 279
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
172-261 |
1.07e-20 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 85.69 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 172 LDIGCGWGGLAVYAAQHYGVTVHGITISAEQKAFIEERCGE--LDIHILLQDYRDLH---QQYDRIVSVGMFEHVGPKNY 246
Cdd:pfam13649 2 LDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEagLNVEFVQGDAEDLPfpdGSFDLVVSSGVLHHLPDPDL 81
|
90
....*....|....*
gi 1718143695 247 ADYFEMADRCLKPDG 261
Cdd:pfam13649 82 EAALREIARVLKPGG 96
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
165-268 |
6.73e-20 |
|
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: 84.68 E-value: 6.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 165 LKPGMTLLDIGCGWGGLAVYAAQHyGVTVHGITISAEQKAFIEERCGELDIHILLQDYRDL---HQQYDRIVSVGMFEHV 241
Cdd:COG2227 22 LPAGGRVLDVGCGTGRLALALARR-GADVTGVDISPEALEIARERAAELNVDFVQGDLEDLpleDGSFDLVICSEVLEHL 100
|
90 100
....*....|....*....|....*..
gi 1718143695 242 gpKNYADYFEMADRCLKPDGLFLLHTI 268
Cdd:COG2227 101 --PDPAALLRELARLLKPGGLLLLSTP 125
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
149-265 |
1.03e-17 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 80.73 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 149 EEAQQHKLALICEKLQLKPGMTLLDIGCGWGGLAVYAAQHYGVTVHGITISAEQKAFIEERCGELD---IHILLQDYRDL 225
Cdd:COG0500 8 DELLPGLAALLALLERLPKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAGlgnVEFLVADLAEL 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1718143695 226 H----QQYDRIVSVGMFEHVGPKNYADYFEMADRCLKPDGLFLL 265
Cdd:COG0500 88 DplpaESFDLVVAFGVLHHLPPEEREALLRELARALKPGGVLLL 131
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
159-269 |
3.82e-15 |
|
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis
Pssm-ID: 441828 [Multi-domain] Cd Length: 143 Bit Score: 71.95 E-value: 3.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 159 ICEKLQLKPGMTLLDIGCGWGGLAVYAAQHyGVTVHGITISAEQKAFIEERCGE--LDIHILLQDYRDLH---QQYDRIV 233
Cdd:COG2226 14 LLAALGLRPGARVLDLGCGTGRLALALAER-GARVTGVDISPEMLELARERAAEagLNVEFVVGDAEDLPfpdGSFDLVI 92
|
90 100 110
....*....|....*....|....*....|....*.
gi 1718143695 234 SVGMFEHVgpKNYADYFEMADRCLKPDGLFLLHTIG 269
Cdd:COG2226 93 SSFVLHHL--PDPERALAEIARVLKPGGRLVVVDFS 126
|
|
| Methyltransf_11 |
pfam08241 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
172-265 |
4.31e-15 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 462406 [Multi-domain] Cd Length: 94 Bit Score: 70.00 E-value: 4.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 172 LDIGCGWGGLAVYAAQhYGVTVHGITISAEQKAFIEERCGELDIHILLQDYRDL---HQQYDRIVSVGMFEHVgpKNYAD 248
Cdd:pfam08241 1 LDVGCGTGLLTELLAR-LGARVTGVDISPEMLELAREKAPREGLTFVVGDAEDLpfpDNSFDLVLSSEVLHHV--EDPER 77
|
90
....*....|....*..
gi 1718143695 249 YFEMADRCLKPDGLFLL 265
Cdd:pfam08241 78 ALREIARVLKPGGILII 94
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
170-266 |
2.61e-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: 2.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 170 TLLDIGCGWGGLAVYAAQHYGVTVHGITISAEQKAFIEE---RCGELDIHILLQDYRDLH----QQYDRIVSVGMFEHVg 242
Cdd:cd02440 1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKaaaALLADNVEVLKGDAEELPpeadESFDVIISDPPLHHL- 79
|
90 100
....*....|....*....|....
gi 1718143695 243 PKNYADYFEMADRCLKPDGLFLLH 266
Cdd:cd02440 80 VEDLARFLEEARRLLKPGGVLVLT 103
|
|
| COG4976 |
COG4976 |
Predicted methyltransferase, contains TPR repeat [General function prediction only]; |
150-265 |
3.06e-12 |
|
Predicted methyltransferase, contains TPR repeat [General function prediction only];
Pssm-ID: 444001 [Multi-domain] Cd Length: 181 Bit Score: 64.63 E-value: 3.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 150 EAQQHKLALICEKLQLKPGMTLLDIGCGWGGLAVYAAQHyGVTVHGITISAEQKAFIEERCgeLDIHILLQDYRDLHQ-- 227
Cdd:COG4976 29 EAPALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPR-GYRLTGVDLSEEMLAKAREKG--VYDRLLVADLADLAEpd 105
|
90 100 110
....*....|....*....|....*....|....*....
gi 1718143695 228 -QYDRIVSVGMFEHVGpkNYADYFEMADRCLKPDGLFLL 265
Cdd:COG4976 106 gRFDLIVAADVLTYLG--DLAAVFAGVARALKPGGLFIF 142
|
|
| Methyltransf_23 |
pfam13489 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
165-298 |
2.82e-10 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 404385 [Multi-domain] Cd Length: 162 Bit Score: 58.59 E-value: 2.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 165 LKPGMTLLDIGCGWGGLAVYAAQHyGVTVHGITISAEQkafiEERCGELDIHIL--LQDYRDLHQQYDRIVSVGMFEHVg 242
Cdd:pfam13489 20 LPSPGRVLDFGCGTGIFLRLLRAQ-GFSVTGVDPSPIA----IERALLNVRFDQfdEQEAAVPAGKFDVIVAREVLEHV- 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1718143695 243 pKNYADYFEMADRCLKPDGLFLLHTIGSNTTAHNVDPWiNKYIFPNG---CLPSIKQIA 298
Cdd:pfam13489 94 -PDPPALLRQIAALLKPGGLLLLSTPLASDEADRLLLE-WPYLRPRNghiSLFSARSLK 150
|
|
| Tam |
COG4106 |
Trans-aconitate methyltransferase [Energy production and conversion]; |
167-265 |
1.25e-09 |
|
Trans-aconitate methyltransferase [Energy production and conversion];
Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 54.83 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 167 PGMTLLDIGCGWGGLAVYAAQHY-GVTVHGITISAEQKAFIEERCGelDIHILLQDYRDL--HQQYDRIVSVGMFEHVgp 243
Cdd:COG4106 1 PPRRVLDLGCGTGRLTALLAERFpGARVTGVDLSPEMLARARARLP--NVRFVVADLRDLdpPEPFDLVVSNAALHWL-- 76
|
90 100
....*....|....*....|..
gi 1718143695 244 KNYADYFEMADRCLKPDGLFLL 265
Cdd:COG4106 77 PDHAALLARLAAALAPGGVLAV 98
|
|
| Methyltransf_12 |
pfam08242 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
172-263 |
1.22e-08 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 51.98 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 172 LDIGCGWGGLAVYAAQHY-GVTVHGITISAEQKAFIEERCGELDIHILLQ---DYRDLHQQ----YDRIVSVGMFEHVGP 243
Cdd:pfam08242 1 LEIGCGTGTLLRALLEALpGLEYTGLDISPAALEAARERLAALGLLNAVRvelFQLDLGELdpgsFDVVVASNVLHHLAD 80
|
90 100
....*....|....*....|
gi 1718143695 244 KnyADYFEMADRCLKPDGLF 263
Cdd:pfam08242 81 P--RAVLRNIRRLLKPGGVL 98
|
|
| PKS_MT |
smart00828 |
Methyltransferase in polyketide synthase (PKS) enzymes; |
172-272 |
4.35e-07 |
|
Methyltransferase in polyketide synthase (PKS) enzymes;
Pssm-ID: 214839 [Multi-domain] Cd Length: 224 Bit Score: 50.49 E-value: 4.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 172 LDIGCGWG-GLAVYAAQHYGVTVHGITISAEQKAFIEERCGELdihiLLQD-----YRDLHQQ-----YDRIVSVGMFEH 240
Cdd:smart00828 4 LDFGCGYGsDLIDLAERHPHLQLHGYTISPEQAEVGRERIRAL----GLQGririfYRDSAKDpfpdtYDLVFGFEVIHH 79
|
90 100 110
....*....|....*....|....*....|..
gi 1718143695 241 VgpKNYADYFEMADRCLKPDGLFLLHTIGSNT 272
Cdd:smart00828 80 I--KDKMDLFSNISRHLKDGGHLVLADFIANL 109
|
|
| PLN02336 |
PLN02336 |
phosphoethanolamine N-methyltransferase |
161-209 |
1.34e-06 |
|
phosphoethanolamine N-methyltransferase
Pssm-ID: 177970 [Multi-domain] Cd Length: 475 Bit Score: 50.13 E-value: 1.34e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1718143695 161 EKLQLKPGMTLLDIGCGWGGLAVYAAQHYGVTVHGITISAEQKAFIEER 209
Cdd:PLN02336 260 DKLDLKPGQKVLDVGCGIGGGDFYMAENFDVHVVGIDLSVNMISFALER 308
|
|
| Methyltransf_31 |
pfam13847 |
Methyltransferase domain; This family appears to have methyltransferase activity. |
165-265 |
3.65e-06 |
|
Methyltransferase domain; This family appears to have methyltransferase activity.
Pssm-ID: 463998 [Multi-domain] Cd Length: 150 Bit Score: 46.26 E-value: 3.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 165 LKPGMTLLDIGCGWGGLAVYAAQHYG--VTVHGITISAEQKAFIEERCGEL----------DIHILLQDYRDlhQQYDRI 232
Cdd:pfam13847 1 IDKGMRVLDLGCGTGHLSFELAEELGpnAEVVGIDISEEAIEKARENAQKLgfdnvefeqgDIEELPELLED--DKFDVV 78
|
90 100 110
....*....|....*....|....*....|...
gi 1718143695 233 VSVGMFEHVGpkNYADYFEMADRCLKPDGLFLL 265
Cdd:pfam13847 79 ISNCVLNHIP--DPDKVLQEILRVLKPGGRLII 109
|
|
| PTZ00098 |
PTZ00098 |
phosphoethanolamine N-methyltransferase; Provisional |
159-265 |
4.45e-06 |
|
phosphoethanolamine N-methyltransferase; Provisional
Pssm-ID: 173391 [Multi-domain] Cd Length: 263 Bit Score: 47.66 E-value: 4.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 159 ICEKLQLKPGMTLLDIGCGWGGLAVYAAQHYGVTVHGITISAEQKAFIEERCGELD------IHILLQDYRDlhQQYDRI 232
Cdd:PTZ00098 44 ILSDIELNENSKVLDIGSGLGGGCKYINEKYGAHVHGVDICEKMVNIAKLRNSDKNkiefeaNDILKKDFPE--NTFDMI 121
|
90 100 110
....*....|....*....|....*....|...
gi 1718143695 233 VSVGMFEHVGPKNYADYFEMADRCLKPDGLFLL 265
Cdd:PTZ00098 122 YSRDAILHLSYADKKKLFEKCYKWLKPNGILLI 154
|
|
| PRK08317 |
PRK08317 |
hypothetical protein; Provisional |
161-279 |
2.24e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 181382 [Multi-domain] Cd Length: 241 Bit Score: 45.31 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 161 EKLQLKPGMTLLDIGCGWGGLAVYAAQHYGVT--VHGITISAEQKAFIEER-CGELDIHILLQD------YRDlhQQYDR 231
Cdd:PRK08317 13 ELLAVQPGDRVLDVGCGPGNDARELARRVGPEgrVVGIDRSEAMLALAKERaAGLGPNVEFVRGdadglpFPD--GSFDA 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1718143695 232 IVSVGMFEHV-GPKNYADyfEMAdRCLKPDG-LFLLHTIGSNTTAHNVDP 279
Cdd:PRK08317 91 VRSDRVLQHLeDPARALA--EIA-RVLRPGGrVVVLDTDWDTLVWHSGDR 137
|
|
| RsmC |
COG2813 |
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ... |
161-265 |
4.66e-05 |
|
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: 43.64 E-value: 4.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 161 EKLQLKPGMTLLDIGCGWGGLAVYAAQHYGV-TVHGITI------SAEQKAfieERCGELDIHILLQDYRD--LHQQYDR 231
Cdd:COG2813 43 EHLPEPLGGRVLDLGCGYGVIGLALAKRNPEaRVTLVDVnaraveLARANA---AANGLENVEVLWSDGLSgvPDGSFDL 119
|
90 100 110
....*....|....*....|....*....|....*...
gi 1718143695 232 IVSVGMFeHVGPKNYAD----YFEMADRCLKPDGLFLL 265
Cdd:COG2813 120 ILSNPPF-HAGRAVDKEvahaLIADAARHLRPGGELWL 156
|
|
| FtsJ |
pfam01728 |
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ... |
154-265 |
6.74e-05 |
|
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal sources FtsJ is a methyltransferase, but actually has no effect on cell division. FtsJ's substrate is the 23S rRNA. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. This family also includes the N terminus of flaviviral NS5 protein. It has been hypothesized that the N-terminal domain of NS5 is a methyltransferase involved in viral RNA capping.
Pssm-ID: 426399 Cd Length: 179 Bit Score: 42.96 E-value: 6.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 154 HKLALICEKLQ-LKPGMTLLDIGCGWGGLAVYAAQHYGVTVHGITI----------------------SAEQKAFIEERC 210
Cdd:pfam01728 7 YKLLEIDEKFGlLKPGKTVLDLGAAPGGWSQVALQRGAGKVVGVDLgpmqlwkprndpgvtfiqgdirDPETLDLLEELL 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1718143695 211 GELdIHILLQD---YRDLHQQYDRIVSVGMFEHVgpknyadyFEMADRCLKPDGLFLL 265
Cdd:pfam01728 87 GRK-VDLVLSDgspFISGNKVLDHLRSLDLVKAA--------LEVALELLRKGGNFVC 135
|
|
| CobL |
COG2242 |
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ... |
157-208 |
6.90e-05 |
|
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 441843 [Multi-domain] Cd Length: 403 Bit Score: 44.39 E-value: 6.90e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1718143695 157 ALICEKLQLKPGMTLLDIGCGWGGLAVYAA-QHYGVTVHGITISAEQKAFIEE 208
Cdd:COG2242 237 ALTLAKLALRPGDVLWDIGAGSGSVSIEAArLAPGGRVYAIERDPERAALIRA 289
|
|
| PLN02244 |
PLN02244 |
tocopherol O-methyltransferase |
144-204 |
7.08e-05 |
|
tocopherol O-methyltransferase
Pssm-ID: 215135 [Multi-domain] Cd Length: 340 Bit Score: 44.35 E-value: 7.08e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1718143695 144 QADTLEEAQqhKLALICEKLQLKPgMTLLDIGCGWGGLAVYAAQHYGVTVHGITISAEQKA 204
Cdd:PLN02244 98 QIRMIEESL--AWAGVPDDDEKRP-KRIVDVGCGIGGSSRYLARKYGANVKGITLSPVQAA 155
|
|
| ubiE |
PRK00216 |
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ... |
119-264 |
8.61e-05 |
|
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;
Pssm-ID: 234689 [Multi-domain] Cd Length: 239 Bit Score: 43.60 E-value: 8.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 119 HYDLGNDLFSHMLDPYmqyscgyWKQAdtleeaqqhklalICEKLQLKPGMTLLDIGCGWGGLAVYAAQHYGVTVH--GI 196
Cdd:PRK00216 23 KYDLMNDLLSFGLHRV-------WRRK-------------TIKWLGVRPGDKVLDLACGTGDLAIALAKAVGKTGEvvGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 197 TIS------AEQKAfiEERCGELDIHILLQDYRDL---HQQYDrIVSVGmFehvGPKNYADYF----EMAdRCLKPDGLF 263
Cdd:PRK00216 83 DFSegmlavGREKL--RDLGLSGNVEFVQGDAEALpfpDNSFD-AVTIA-F---GLRNVPDIDkalrEMY-RVLKPGGRL 154
|
.
gi 1718143695 264 L 264
Cdd:PRK00216 155 V 155
|
|
| TrmN6 |
COG4123 |
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ... |
165-263 |
2.24e-04 |
|
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: 42.44 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 165 LKPGMTLLDIGCGWGGLAVYAAQHY-GVTVHGITISAE-----QKAF----IEERcgeldIHILLQDYRDL-----HQQY 229
Cdd:COG4123 35 VKKGGRVLDLGTGTGVIALMLAQRSpGARITGVEIQPEaaelaRRNValngLEDR-----ITVIHGDLKEFaaelpPGSF 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1718143695 230 DRIVS------VGMFE-----------HVGPKNYADYFEMADRCLKPDGLF 263
Cdd:COG4123 110 DLVVSnppyfkAGSGRkspdearaiarHEDALTLEDLIRAAARLLKPGGRF 160
|
|
| PCMT |
pfam01135 |
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT); |
152-190 |
4.15e-04 |
|
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
Pssm-ID: 395902 [Multi-domain] Cd Length: 205 Bit Score: 41.20 E-value: 4.15e-04
10 20 30
....*....|....*....|....*....|....*....
gi 1718143695 152 QQHKLALICEKLQLKPGMTLLDIGCGWGGLAVYAAQHYG 190
Cdd:pfam01135 58 APHMHAMMLELLELKPGMRVLEIGSGSGYLTACFARMVG 96
|
|
| PRK09328 |
PRK09328 |
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional |
161-265 |
1.05e-03 |
|
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
Pssm-ID: 236467 [Multi-domain] Cd Length: 275 Bit Score: 40.53 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 161 EKLQLKPGMTLLDIGCGWGGLAVYAAQHY-GVTVHGITIS------AEQKAfieERCGELDIHILLQDYRD--LHQQYDR 231
Cdd:PRK09328 102 EALLLKEPLRVLDLGTGSGAIALALAKERpDAEVTAVDISpealavARRNA---KHGLGARVEFLQGDWFEplPGGRFDL 178
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1718143695 232 IVS----------------VGMFE-HV----GPKNYADY---FEMADRCLKPDGLFLL 265
Cdd:PRK09328 179 IVSnppyipeadihllqpeVRDHEpHLalfgGEDGLDFYrriIEQAPRYLKPGGWLLL 236
|
|
| PRK13942 |
PRK13942 |
protein-L-isoaspartate O-methyltransferase; Provisional |
154-213 |
2.64e-03 |
|
protein-L-isoaspartate O-methyltransferase; Provisional
Pssm-ID: 184409 Cd Length: 212 Bit Score: 38.84 E-value: 2.64e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 154 HKLALICEKLQLKPGMTLLDIGCGWGGLAVYAAQHYGVTVHGITIsaeqkafieERCGEL 213
Cdd:PRK13942 63 HMVAIMCELLDLKEGMKVLEIGTGSGYHAAVVAEIVGKSGKVVTI---------ERIPEL 113
|
|
| Qor |
COG0604 |
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ... |
161-269 |
4.23e-03 |
|
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and conversion, General function prediction only];
Pssm-ID: 440369 [Multi-domain] Cd Length: 322 Bit Score: 38.59 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 161 EKLQLKPGMTLLDIGCGwGGLAVYAAQ---HYGVTVHGITISAEQKAFIEERCGEldiHILlqDYR--DLHQQ------- 228
Cdd:COG0604 133 DRGRLKPGETVLVHGAA-GGVGSAAVQlakALGARVIATASSPEKAELLRALGAD---HVI--DYReeDFAERvraltgg 206
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1718143695 229 --YDRIvsvgmFEHVGpknyADYFEMADRCLKPDGLFLlhTIG 269
Cdd:COG0604 207 rgVDVV-----LDTVG----GDTLARSLRALAPGGRLV--SIG 238
|
|
| SpeE |
COG0421 |
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism]; |
174-270 |
6.19e-03 |
|
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
Pssm-ID: 440190 [Multi-domain] Cd Length: 195 Bit Score: 37.50 E-value: 6.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718143695 174 IGCGWGGLAVYAAQHYGVT-VHGITISAEQ----KAFIEERCGELD---IHILLQD---Y-RDLHQQYDrIVSVGMFEHV 241
Cdd:COG0421 44 IGGGDGGLARELLKHPPVErVDVVEIDPEVvelaREYFPLLAPAFDdprLRVVIGDgraFlREAEESYD-VIIVDLTDPV 122
|
90 100 110
....*....|....*....|....*....|..
gi 1718143695 242 GPKNY---ADYFEMADRCLKPDGLFLLHTIGS 270
Cdd:COG0421 123 GPAEGlftREFYEDCRRALKPGGVLVVNLGSP 154
|
|
|