|
Name |
Accession |
Description |
Interval |
E-value |
| CMAS |
pfam02353 |
Mycolic acid cyclopropane synthetase; This family consist of ... |
117-374 |
8.22e-69 |
|
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: 220.28 E-value: 8.22e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713325 117 SNEFFGLFMDDTMMYSSAVFK---VTIKNFQNEKNTSFNRKGEDKEEPYeVLEIGCGWGTLAIEVVKRTGCKYTGFTLSI 193
Cdd:pfam02353 16 SNDFFALFLDPTMTYSCAYFErpdMTLEEAQQAKLDLILDKLGLKPGMT-LLDIGCGWGGLMRRAAERYDVNVVGLTLSK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713325 194 EQLKYVEEKVKEAGLQERITFKLCDYRQLcdTQKYDRIISCEMIEHVGHKFMETFFSHCEAALAEDGIFVLQ-FTAIPEE 272
Cdd:pfam02353 95 NQYKLARKRVAAEGLARKVEVLLQDYRDF--DEPFDRIVSVGMFEHVGHENYDTFFKKLYNLLPPGGLMLLHtITGLHPD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713325 273 LYDESRLTSGFITEYIFPGGCLPSLARVTSAMaSSSRLCIENVENIGIHYYPTLRYWRKNLLERQKQIIDLgFDEKFLRT 352
Cdd:pfam02353 173 ETSERGLPLKFIDKYIFPGGELPSISMIVESS-SEAGFTVEDVESLRPHYAKTLDLWAENLQANKDEAIAL-QSEEFYRM 250
|
250 260
....*....|....*....|..
gi 1063713325 353 WEYYFDYCAAGFKTLTLRNYQI 374
Cdd:pfam02353 251 WMLYLTGCAVAFRIGYIDVHQF 272
|
|
| PRK11705 |
PRK11705 |
cyclopropane fatty acyl phospholipid synthase; |
34-380 |
1.44e-53 |
|
cyclopropane fatty acyl phospholipid synthase;
Pssm-ID: 183282 Cd Length: 383 Bit Score: 183.90 E-value: 1.44e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713325 34 LKIHSPQFYWKVMTLADLGLADAYINGDFS------FVDK----------DSGLLNLIMILIAnrdlnsRKSNLAKKRGW 97
Cdd:PRK11705 39 IQVHNPRFFKRVLQEGSLGLGESYMDGWWDcdrldeFFSRvlragldeklPHHLKDTLRILRA------RLFNLQSKKRA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713325 98 WTpvfltasLASATYYLkhSNEFFGLFMDDTMMYSSAVFK--VTIKNFQNEKNTSFNRK-----GEdkeepyEVLEIGCG 170
Cdd:PRK11705 113 WI-------VGKEHYDL--GNDLFEAMLDPRMQYSCGYWKdaDTLEEAQEAKLDLICRKlqlkpGM------RVLDIGCG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713325 171 WGTLAIEVVKRTGCKYTGFTLSIEQLKYVEEKVkeAGLQerITFKLCDYRQLcdTQKYDRIISCEMIEHVGHKFMETFFS 250
Cdd:PRK11705 178 WGGLARYAAEHYGVSVVGVTISAEQQKLAQERC--AGLP--VEIRLQDYRDL--NGQFDRIVSVGMFEHVGPKNYRTYFE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713325 251 HCEAALAEDGIFVLQftAIPEELYDESrlTSGFITEYIFPGGCLPSLARVTSamASSSRLCIENVENIGIHYYPTLRYWR 330
Cdd:PRK11705 252 VVRRCLKPDGLFLLH--TIGSNKTDTN--VDPWINKYIFPNGCLPSVRQIAQ--ASEGLFVMEDWHNFGADYDRTLMAWH 325
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1063713325 331 KNLLERQKQIIDlGFDEKFLRTWEYYFDYCAAGFKTLTLRNYQIVFSRPG 380
Cdd:PRK11705 326 ENFEAAWPELAD-NYSERFYRMWRYYLLSCAGAFRARDIQLWQVVFSPRG 374
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
117-266 |
7.15e-50 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 167.03 E-value: 7.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713325 117 SNEFFGLFMDDTMMYSSAVFK---VTIKNFQNEKNTSFNRKGEDKEEPyEVLEIGCGWGTLAIEVVKRTGCKYTGFTLSI 193
Cdd:COG2230 6 GNDFYRLFLDPTMTYSCAYFEdpdDTLEEAQEAKLDLILRKLGLKPGM-RVLDIGCGWGGLALYLARRYGVRVTGVTLSP 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063713325 194 EQLKYVEEKVKEAGLQERITFKLCDYRQLCDTQKYDRIISCEMIEHVGHKFMETFFSHCEAALAEDGIFVLQF 266
Cdd:COG2230 85 EQLEYARERAAEAGLADRVEVRLADYRDLPADGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLLHT 157
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
164-266 |
7.69e-13 |
|
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: 64.76 E-value: 7.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713325 164 VLEIGCGWGTLAIEVVKRTGCKYTGFTLSIEQLKYVeEKVKEAGLQERITFKLCDYRQL--CDTQKYDRIISCEMIEHVG 241
Cdd:cd02440 2 VLDLGCGTGALALALASGPGARVTGVDISPVALELA-RKAAAALLADNVEVLKGDAEELppEADESFDVIISDPPLHHLV 80
|
90 100
....*....|....*....|....*
gi 1063713325 242 HKFMEtFFSHCEAALAEDGIFVLQF 266
Cdd:cd02440 81 EDLAR-FLEEARRLLKPGGVLVLTL 104
|
|
| PKS_MT |
smart00828 |
Methyltransferase in polyketide synthase (PKS) enzymes; |
164-285 |
7.15e-09 |
|
Methyltransferase in polyketide synthase (PKS) enzymes;
Pssm-ID: 214839 [Multi-domain] Cd Length: 224 Bit Score: 55.89 E-value: 7.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713325 164 VLEIGCGWGTLAIEVVKRTG-CKYTGFTLSIEQLKYVEEKVKEAGLQERITFKLCDYRQLCDTQKYDRIISCEMIEHVGH 242
Cdd:smart00828 3 VLDFGCGYGSDLIDLAERHPhLQLHGYTISPEQAEVGRERIRALGLQGRIRIFYRDSAKDPFPDTYDLVFGFEVIHHIKD 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1063713325 243 KfmETFFSHCEAALAEDGIFVL-QFTAIPEELYDESRLTSGFIT 285
Cdd:smart00828 83 K--MDLFSNISRHLKDGGHLVLaDFIANLLSAIEHEETTSYLVT 124
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CMAS |
pfam02353 |
Mycolic acid cyclopropane synthetase; This family consist of ... |
117-374 |
8.22e-69 |
|
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: 220.28 E-value: 8.22e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713325 117 SNEFFGLFMDDTMMYSSAVFK---VTIKNFQNEKNTSFNRKGEDKEEPYeVLEIGCGWGTLAIEVVKRTGCKYTGFTLSI 193
Cdd:pfam02353 16 SNDFFALFLDPTMTYSCAYFErpdMTLEEAQQAKLDLILDKLGLKPGMT-LLDIGCGWGGLMRRAAERYDVNVVGLTLSK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713325 194 EQLKYVEEKVKEAGLQERITFKLCDYRQLcdTQKYDRIISCEMIEHVGHKFMETFFSHCEAALAEDGIFVLQ-FTAIPEE 272
Cdd:pfam02353 95 NQYKLARKRVAAEGLARKVEVLLQDYRDF--DEPFDRIVSVGMFEHVGHENYDTFFKKLYNLLPPGGLMLLHtITGLHPD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713325 273 LYDESRLTSGFITEYIFPGGCLPSLARVTSAMaSSSRLCIENVENIGIHYYPTLRYWRKNLLERQKQIIDLgFDEKFLRT 352
Cdd:pfam02353 173 ETSERGLPLKFIDKYIFPGGELPSISMIVESS-SEAGFTVEDVESLRPHYAKTLDLWAENLQANKDEAIAL-QSEEFYRM 250
|
250 260
....*....|....*....|..
gi 1063713325 353 WEYYFDYCAAGFKTLTLRNYQI 374
Cdd:pfam02353 251 WMLYLTGCAVAFRIGYIDVHQF 272
|
|
| PRK11705 |
PRK11705 |
cyclopropane fatty acyl phospholipid synthase; |
34-380 |
1.44e-53 |
|
cyclopropane fatty acyl phospholipid synthase;
Pssm-ID: 183282 Cd Length: 383 Bit Score: 183.90 E-value: 1.44e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713325 34 LKIHSPQFYWKVMTLADLGLADAYINGDFS------FVDK----------DSGLLNLIMILIAnrdlnsRKSNLAKKRGW 97
Cdd:PRK11705 39 IQVHNPRFFKRVLQEGSLGLGESYMDGWWDcdrldeFFSRvlragldeklPHHLKDTLRILRA------RLFNLQSKKRA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713325 98 WTpvfltasLASATYYLkhSNEFFGLFMDDTMMYSSAVFK--VTIKNFQNEKNTSFNRK-----GEdkeepyEVLEIGCG 170
Cdd:PRK11705 113 WI-------VGKEHYDL--GNDLFEAMLDPRMQYSCGYWKdaDTLEEAQEAKLDLICRKlqlkpGM------RVLDIGCG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713325 171 WGTLAIEVVKRTGCKYTGFTLSIEQLKYVEEKVkeAGLQerITFKLCDYRQLcdTQKYDRIISCEMIEHVGHKFMETFFS 250
Cdd:PRK11705 178 WGGLARYAAEHYGVSVVGVTISAEQQKLAQERC--AGLP--VEIRLQDYRDL--NGQFDRIVSVGMFEHVGPKNYRTYFE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713325 251 HCEAALAEDGIFVLQftAIPEELYDESrlTSGFITEYIFPGGCLPSLARVTSamASSSRLCIENVENIGIHYYPTLRYWR 330
Cdd:PRK11705 252 VVRRCLKPDGLFLLH--TIGSNKTDTN--VDPWINKYIFPNGCLPSVRQIAQ--ASEGLFVMEDWHNFGADYDRTLMAWH 325
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1063713325 331 KNLLERQKQIIDlGFDEKFLRTWEYYFDYCAAGFKTLTLRNYQIVFSRPG 380
Cdd:PRK11705 326 ENFEAAWPELAD-NYSERFYRMWRYYLLSCAGAFRARDIQLWQVVFSPRG 374
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
117-266 |
7.15e-50 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 167.03 E-value: 7.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713325 117 SNEFFGLFMDDTMMYSSAVFK---VTIKNFQNEKNTSFNRKGEDKEEPyEVLEIGCGWGTLAIEVVKRTGCKYTGFTLSI 193
Cdd:COG2230 6 GNDFYRLFLDPTMTYSCAYFEdpdDTLEEAQEAKLDLILRKLGLKPGM-RVLDIGCGWGGLALYLARRYGVRVTGVTLSP 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063713325 194 EQLKYVEEKVKEAGLQERITFKLCDYRQLCDTQKYDRIISCEMIEHVGHKFMETFFSHCEAALAEDGIFVLQF 266
Cdd:COG2230 85 EQLEYARERAAEAGLADRVEVRLADYRDLPADGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLLHT 157
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
164-260 |
9.50e-19 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 81.07 E-value: 9.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713325 164 VLEIGCGWGTLAIEVVKRTGCKYTGFTLSIEQLKYVEEKVKEAGLqeRITFKLCDYRQL-CDTQKYDRIISCEMIEHVGH 242
Cdd:pfam13649 1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAEDLpFPDGSFDLVVSSGVLHHLPD 78
|
90
....*....|....*...
gi 1063713325 243 KFMETFFSHCEAALAEDG 260
Cdd:pfam13649 79 PDLEAALREIARVLKPGG 96
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
156-279 |
1.89e-16 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 77.65 E-value: 1.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713325 156 EDKEEPYEVLEIGCGWGTLAIEVVKRTGCKYTGFTLSIEQLKYVEEKVKEAGLqERITFKLCDYRQLCD--TQKYDRIIS 233
Cdd:COG0500 22 ERLPKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAGL-GNVEFLVADLAELDPlpAESFDLVVA 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1063713325 234 CEMIEHVGHKFMETFFSHCEAALAEDGIFVLQFTAIPEELYDESRL 279
Cdd:COG0500 101 FGVLHHLPPEEREALLRELARALKPGGVLLLSASDAAAALSLARLL 146
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
164-266 |
1.19e-14 |
|
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: 70.43 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713325 164 VLEIGCGWGTLAIEVVKRtGCKYTGFTLSIEQLKYVEEKVKEAglqeRITFKLCDYRQL-CDTQKYDRIISCEMIEHVGH 242
Cdd:COG2227 28 VLDVGCGTGRLALALARR-GADVTGVDISPEALEIARERAAEL----NVDFVQGDLEDLpLEDGSFDLVICSEVLEHLPD 102
|
90 100
....*....|....*....|....
gi 1063713325 243 kfMETFFSHCEAALAEDGIFVLQF 266
Cdd:COG2227 103 --PAALLRELARLLKPGGLLLLST 124
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
164-283 |
9.47e-14 |
|
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: 68.10 E-value: 9.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713325 164 VLEIGCGWGTLAIEVVKRtGCKYTGFTLSIEQLKYVEEKVKEAGLqeRITFKLCDYRQL-CDTQKYDRIISCEMIEHVGH 242
Cdd:COG2226 26 VLDLGCGTGRLALALAER-GARVTGVDISPEMLELARERAAEAGL--NVEFVVGDAEDLpFPDGSFDLVISSFVLHHLPD 102
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1063713325 243 KfmETFFSHCEAALAEDGIFVLQFTAIPEELYDESRLTS-GF 283
Cdd:COG2226 103 P--ERALAEIARVLKPGGRLVVVDFSPPDLAELEELLAEaGF 142
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
164-266 |
7.69e-13 |
|
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: 64.76 E-value: 7.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713325 164 VLEIGCGWGTLAIEVVKRTGCKYTGFTLSIEQLKYVeEKVKEAGLQERITFKLCDYRQL--CDTQKYDRIISCEMIEHVG 241
Cdd:cd02440 2 VLDLGCGTGALALALASGPGARVTGVDISPVALELA-RKAAAALLADNVEVLKGDAEELppEADESFDVIISDPPLHHLV 80
|
90 100
....*....|....*....|....*
gi 1063713325 242 HKFMEtFFSHCEAALAEDGIFVLQF 266
Cdd:cd02440 81 EDLAR-FLEEARRLLKPGGVLVLTL 104
|
|
| PKS_MT |
smart00828 |
Methyltransferase in polyketide synthase (PKS) enzymes; |
164-285 |
7.15e-09 |
|
Methyltransferase in polyketide synthase (PKS) enzymes;
Pssm-ID: 214839 [Multi-domain] Cd Length: 224 Bit Score: 55.89 E-value: 7.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713325 164 VLEIGCGWGTLAIEVVKRTG-CKYTGFTLSIEQLKYVEEKVKEAGLQERITFKLCDYRQLCDTQKYDRIISCEMIEHVGH 242
Cdd:smart00828 3 VLDFGCGYGSDLIDLAERHPhLQLHGYTISPEQAEVGRERIRALGLQGRIRIFYRDSAKDPFPDTYDLVFGFEVIHHIKD 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1063713325 243 KfmETFFSHCEAALAEDGIFVL-QFTAIPEELYDESRLTSGFIT 285
Cdd:smart00828 83 K--MDLFSNISRHLKDGGHLVLaDFIANLLSAIEHEETTSYLVT 124
|
|
| COG4976 |
COG4976 |
Predicted methyltransferase, contains TPR repeat [General function prediction only]; |
164-264 |
2.16e-08 |
|
Predicted methyltransferase, contains TPR repeat [General function prediction only];
Pssm-ID: 444001 [Multi-domain] Cd Length: 181 Bit Score: 53.85 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713325 164 VLEIGCGWGTLAIEVVKRtGCKYTGFTLSIEQLkyveEKVKEAGLQerITFKLCDYRQLCDT-QKYDRIISCEMIEHVGH 242
Cdd:COG4976 50 VLDLGCGTGLLGEALRPR-GYRLTGVDLSEEML----AKAREKGVY--DRLLVADLADLAEPdGRFDLIVAADVLTYLGD 122
|
90 100
....*....|....*....|..
gi 1063713325 243 kfMETFFSHCEAALAEDGIFVL 264
Cdd:COG4976 123 --LAAVFAGVARALKPGGLFIF 142
|
|
| Tam |
COG4106 |
Trans-aconitate methyltransferase [Energy production and conversion]; |
164-266 |
2.55e-08 |
|
Trans-aconitate methyltransferase [Energy production and conversion];
Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 51.36 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713325 164 VLEIGCGWGTLAIEVVKR-TGCKYTGFTLSIEQLKYVEEKVkeaglqERITFKLCDYRQLCDTQKYDRIISCEMIEHVGH 242
Cdd:COG4106 5 VLDLGCGTGRLTALLAERfPGARVTGVDLSPEMLARARARL------PNVRFVVADLRDLDPPEPFDLVVSNAALHWLPD 78
|
90 100
....*....|....*....|....
gi 1063713325 243 kfMETFFSHCEAALAEDGIFVLQF 266
Cdd:COG4106 79 --HAALLARLAAALAPGGVLAVQV 100
|
|
| Methyltransf_12 |
pfam08242 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
165-262 |
3.08e-08 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 51.21 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713325 165 LEIGCGWGTLAIEVVKR-TGCKYTGFTLSIEQLKYVEEKVKEAGLQ--ERITFKLCDyRQLCDTQKYDRIISCEMIEHVG 241
Cdd:pfam08242 1 LEIGCGTGTLLRALLEAlPGLEYTGLDISPAALEAARERLAALGLLnaVRVELFQLD-LGELDPGSFDVVVASNVLHHLA 79
|
90 100
....*....|....*....|.
gi 1063713325 242 HkfMETFFSHCEAALAEDGIF 262
Cdd:pfam08242 80 D--PRAVLRNIRRLLKPGGVL 98
|
|
| Methyltransf_11 |
pfam08241 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
165-264 |
5.02e-07 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 462406 [Multi-domain] Cd Length: 94 Bit Score: 47.66 E-value: 5.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713325 165 LEIGCGWGtLAIEVVKRTGCKYTGFTLSIEQLKYVEEKVKEAGLqeriTFKLCDYRQLC-DTQKYDRIISCEMIEHVghK 243
Cdd:pfam08241 1 LDVGCGTG-LLTELLARLGARVTGVDISPEMLELAREKAPREGL----TFVVGDAEDLPfPDNSFDLVLSSEVLHHV--E 73
|
90 100
....*....|....*....|.
gi 1063713325 244 FMETFFSHCEAALAEDGIFVL 264
Cdd:pfam08241 74 DPERALREIARVLKPGGILII 94
|
|
| Methyltransf_23 |
pfam13489 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
152-265 |
1.98e-06 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 404385 [Multi-domain] Cd Length: 162 Bit Score: 47.81 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713325 152 NRKGEDKEEPYEVLEIGCGWGTLAIEvVKRTGCKYTGFTLSIEQLKYVEEKVKEAGLQERItfklcdyrQLCDTQKYDRI 231
Cdd:pfam13489 14 LRLLPKLPSPGRVLDFGCGTGIFLRL-LRAQGFSVTGVDPSPIAIERALLNVRFDQFDEQE--------AAVPAGKFDVI 84
|
90 100 110
....*....|....*....|....*....|....*.
gi 1063713325 232 ISCEMIEHVG--HKFMETFFSHceaaLAEDGIFVLQ 265
Cdd:pfam13489 85 VAREVLEHVPdpPALLRQIAAL----LKPGGLLLLS 116
|
|
| PLN02244 |
PLN02244 |
tocopherol O-methyltransferase |
155-245 |
3.80e-06 |
|
tocopherol O-methyltransferase
Pssm-ID: 215135 [Multi-domain] Cd Length: 340 Bit Score: 48.59 E-value: 3.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713325 155 GEDKEEPYEVLEIGCGWGTLAIEVVKRTGCKYTGFTLSIEQLKYVEEKVKEAGLQERITFKLCD-YRQLCDTQKYDRIIS 233
Cdd:PLN02244 113 DDDEKRPKRIVDVGCGIGGSSRYLARKYGANVKGITLSPVQAARANALAAAQGLSDKVSFQVADaLNQPFEDGQFDLVWS 192
|
90
....*....|....
gi 1063713325 234 CEMIEHV--GHKFM 245
Cdd:PLN02244 193 MESGEHMpdKRKFV 206
|
|
| Methyltransf_31 |
pfam13847 |
Methyltransferase domain; This family appears to have methyltransferase activity. |
158-282 |
3.02e-04 |
|
Methyltransferase domain; This family appears to have methyltransferase activity.
Pssm-ID: 463998 [Multi-domain] Cd Length: 150 Bit Score: 40.86 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713325 158 KEEPYEVLEIGCGWGTLAIEVVKRTG--CKYTGFTLSIEQLKYVEEKVKEAGLqERITFKLCDYRQLCDT---QKYDRII 232
Cdd:pfam13847 1 IDKGMRVLDLGCGTGHLSFELAEELGpnAEVVGIDISEEAIEKARENAQKLGF-DNVEFEQGDIEELPELledDKFDVVI 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063713325 233 SCEMIEHVGH--KFMETFFShceaALAEDGIFVLQ----FTAIPEELYDESRLTSG 282
Cdd:pfam13847 80 SNCVLNHIPDpdKVLQEILR----VLKPGGRLIISdpdsLAELPAHVKEDSTYYAG 131
|
|
| Spermine_synth |
pfam01564 |
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ... |
155-275 |
9.07e-04 |
|
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family includes spermidine synthase that catalyzes the fifth (last) step in the biosynthesis of spermidine from arginine, and spermine synthase.
Pssm-ID: 396237 [Multi-domain] Cd Length: 183 Bit Score: 40.00 E-value: 9.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713325 155 GEDKEEPYEVLEIGCGWGTLAIEVVKRTgckytgftlSIEQLKYVE--EKV-----------KEAGLQERITFKLCD-YR 220
Cdd:pfam01564 13 LCSHPNPKKVLIIGGGDGGVLREVVKHP---------SVEKITLVDidEKVidfskkflpslAIGFQDPRVKVVIGDgFK 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063713325 221 QLCDTQ-KYDRIIScEMIEHVG---HKFMETFFSHCEAALAEDGIFVLQFTAIPEELYD 275
Cdd:pfam01564 84 FLKDYLnTFDVIIV-DSTDPVGpaeNLFSKPFFDLLKKALKEDGVFITQAESPWLHLEL 141
|
|
| TrmN6 |
COG4123 |
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ... |
164-264 |
2.36e-03 |
|
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: 39.36 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713325 164 VLEIGCGWGTLAIEVVKRT-GCKYTGftlsIE-QLKYVE---EKVKEAGLQERITFKLCDYRQLCD---TQKYDRIIS-- 233
Cdd:COG4123 41 VLDLGTGTGVIALMLAQRSpGARITG----VEiQPEAAElarRNVALNGLEDRITVIHGDLKEFAAelpPGSFDLVVSnp 116
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1063713325 234 ----------CEMIE-----HVGHKFMETFFSHCEAALAEDGIFVL 264
Cdd:COG4123 117 pyfkagsgrkSPDEAraiarHEDALTLEDLIRAAARLLKPGGRFAL 162
|
|
| Gcd14 |
COG2519 |
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ... |
164-232 |
7.15e-03 |
|
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 N-methylase Trm61 is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 442009 [Multi-domain] Cd Length: 249 Bit Score: 38.22 E-value: 7.15e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063713325 164 VLEIGCGWGTLAI---EVVKRTGcKYTGFTLSIEQLKYVEEKVKEAGLQERITFKLCDYRQLCDTQKYDRII 232
Cdd:COG2519 95 VLEAGTGSGALTLalaRAVGPEG-KVYSYERREDFAEIARKNLERFGLPDNVELKLGDIREGIDEGDVDAVF 165
|
|
| |
