|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02336 |
PLN02336 |
phosphoethanolamine N-methyltransferase |
30-251 |
1.15e-49 |
|
phosphoethanolamine N-methyltransferase
Pssm-ID: 177970 [Multi-domain] Cd Length: 475 Bit Score: 176.48 E-value: 1.15e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564740 30 KYSDKPDTNSMMLNHSAEELESSDRADILASLPLLHNKDVVDIGAGIGRFTTVLAETARWVLSTDFIDSFIKKNQERNAH 109
Cdd:PLN02336 2 EHSVDLTVEAMMLDSKASDLDKEERPEILSLLPPYEGKSVLELGAGIGRFTGELAKKAGQVIALDFIESVIKKNESINGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564740 110 LGNINYQVGDAV--GLKMESNSVDLVFTNWLMMYLSDEETVEFIFNCMRWLRSHGIVHLRESCSEPStGRSKAKSmhdta 187
Cdd:PLN02336 82 YKNVKFMCADVTspDLNISDGSVDLIFSNWLLMYLSDKEVENLAERMVKWLKVGGYIFFRESCFHQS-GDSKRKN----- 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32564740 188 naNPTHYRFSSLYINLLRAIRYRDVDNKLWRFNVQWSCSVPTYIKRSNNWRQVHWLAEKVPAED 251
Cdd:PLN02336 156 --NPTHYREPRFYTKVFKECHTRDEDGNSFELSLVGCKCIGAYVKNKKNQNQICWLWQKVSSTN 217
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
54-168 |
2.23e-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: 73.10 E-value: 2.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564740 54 RADILASLPLLHNKDVVDIGAGIGRFTTVLAETARWVLSTDFIDSFIKKNQERNAHLG-NINYQVGDAVGLKMESNSVDL 132
Cdd:COG2226 11 REALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGlNVEFVVGDAEDLPFPDGSFDL 90
|
90 100 110
....*....|....*....|....*....|....*.
gi 32564740 133 VFTNWLMMYLSDEEtvEFIFNCMRWLRSHGIVHLRE 168
Cdd:COG2226 91 VISSFVLHHLPDPE--RALAEIARVLKPGGRLVVVD 124
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
69-162 |
5.06e-15 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 70.29 E-value: 5.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564740 69 VVDIGAGIGRFTTVLAETARW-VLSTDFIDSFIKKNQERNAHLG-NINYQVGDAVGLKMESNSVDLVFTNWLMMYLSDEE 146
Cdd:pfam13649 1 VLDLGCGTGRLTLALARRGGArVTGVDLSPEMLERARERAAEAGlNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLPDPD 80
|
90
....*....|....*.
gi 32564740 147 TVEFIFNCMRWLRSHG 162
Cdd:pfam13649 81 LEAALREIARVLKPGG 96
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
68-166 |
3.91e-08 |
|
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).
Pssm-ID: 100107 [Multi-domain] Cd Length: 107 Bit Score: 51.28 E-value: 3.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564740 68 DVVDIGAGIGRFTTVLAETARW-VLSTDFIDSFIKKNQERNAHLG--NINYQVGDAV-GLKMESNSVDLVFTNWLMMYLs 143
Cdd:cd02440 1 RVLDLGCGTGALALALASGPGArVTGVDISPVALELARKAAAALLadNVEVLKGDAEeLPPEADESFDVIISDPPLHHL- 79
|
90 100
....*....|....*....|...
gi 32564740 144 DEETVEFIFNCMRWLRSHGIVHL 166
Cdd:cd02440 80 VEDLARFLEEARRLLKPGGVLVL 102
|
|
| rADc |
smart00650 |
Ribosomal RNA adenine dimethylases; |
69-136 |
2.90e-03 |
|
Ribosomal RNA adenine dimethylases;
Pssm-ID: 128898 Cd Length: 169 Bit Score: 38.65 E-value: 2.90e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32564740 69 VVDIGAGIGRFTTVLAETARWVLSTDfIDS-FIKKNQERNAHLGNINYQVGDAVGLKMESNSVDLVFTN 136
Cdd:smart00650 17 VLEIGPGKGALTEELLERAKRVTAIE-IDPrLAPRLREKFAAADNLTVIHGDALKFDLPKLQPYKVVGN 84
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02336 |
PLN02336 |
phosphoethanolamine N-methyltransferase |
30-251 |
1.15e-49 |
|
phosphoethanolamine N-methyltransferase
Pssm-ID: 177970 [Multi-domain] Cd Length: 475 Bit Score: 176.48 E-value: 1.15e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564740 30 KYSDKPDTNSMMLNHSAEELESSDRADILASLPLLHNKDVVDIGAGIGRFTTVLAETARWVLSTDFIDSFIKKNQERNAH 109
Cdd:PLN02336 2 EHSVDLTVEAMMLDSKASDLDKEERPEILSLLPPYEGKSVLELGAGIGRFTGELAKKAGQVIALDFIESVIKKNESINGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564740 110 LGNINYQVGDAV--GLKMESNSVDLVFTNWLMMYLSDEETVEFIFNCMRWLRSHGIVHLRESCSEPStGRSKAKSmhdta 187
Cdd:PLN02336 82 YKNVKFMCADVTspDLNISDGSVDLIFSNWLLMYLSDKEVENLAERMVKWLKVGGYIFFRESCFHQS-GDSKRKN----- 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32564740 188 naNPTHYRFSSLYINLLRAIRYRDVDNKLWRFNVQWSCSVPTYIKRSNNWRQVHWLAEKVPAED 251
Cdd:PLN02336 156 --NPTHYREPRFYTKVFKECHTRDEDGNSFELSLVGCKCIGAYVKNKKNQNQICWLWQKVSSTN 217
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
54-168 |
2.23e-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: 73.10 E-value: 2.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564740 54 RADILASLPLLHNKDVVDIGAGIGRFTTVLAETARWVLSTDFIDSFIKKNQERNAHLG-NINYQVGDAVGLKMESNSVDL 132
Cdd:COG2226 11 REALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGlNVEFVVGDAEDLPFPDGSFDL 90
|
90 100 110
....*....|....*....|....*....|....*.
gi 32564740 133 VFTNWLMMYLSDEEtvEFIFNCMRWLRSHGIVHLRE 168
Cdd:COG2226 91 VISSFVLHHLPDPE--RALAEIARVLKPGGRLVVVD 124
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
69-162 |
5.06e-15 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 70.29 E-value: 5.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564740 69 VVDIGAGIGRFTTVLAETARW-VLSTDFIDSFIKKNQERNAHLG-NINYQVGDAVGLKMESNSVDLVFTNWLMMYLSDEE 146
Cdd:pfam13649 1 VLDLGCGTGRLTLALARRGGArVTGVDLSPEMLERARERAAEAGlNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLPDPD 80
|
90
....*....|....*.
gi 32564740 147 TVEFIFNCMRWLRSHG 162
Cdd:pfam13649 81 LEAALREIARVLKPGG 96
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
41-166 |
1.98e-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: 63.88 E-value: 1.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564740 41 MLNHSAEELESSDRADILASLpLLHNKDVVDIGAGIGRFTTVLAETARWVLSTDFIDSFIKKNQERNAHLgNINYQVGDA 120
Cdd:COG2227 1 MSDPDARDFWDRRLAALLARL-LPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAEL-NVDFVQGDL 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 32564740 121 VGLKMESNSVDLVFTNWLMMYLSDEEtvEFIFNCMRWLRSHGIVHL 166
Cdd:COG2227 79 EDLPLEDGSFDLVICSEVLEHLPDPA--ALLRELARLLKPGGLLLL 122
|
|
| Methyltransf_11 |
pfam08241 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
70-164 |
3.16e-11 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 462406 [Multi-domain] Cd Length: 94 Bit Score: 59.60 E-value: 3.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564740 70 VDIGAGIGRFTTVLAETARWVLSTDFIDSFIKKNQERNAHLGnINYQVGDAVGLKMESNSVDLVFTNWLMMYLSDeeTVE 149
Cdd:pfam08241 1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREG-LTFVVGDAEDLPFPDNSFDLVLSSEVLHHVED--PER 77
|
90
....*....|....*
gi 32564740 150 FIFNCMRWLRSHGIV 164
Cdd:pfam08241 78 ALREIARVLKPGGIL 92
|
|
| COG4976 |
COG4976 |
Predicted methyltransferase, contains TPR repeat [General function prediction only]; |
25-164 |
2.27e-09 |
|
Predicted methyltransferase, contains TPR repeat [General function prediction only];
Pssm-ID: 444001 [Multi-domain] Cd Length: 181 Bit Score: 56.55 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564740 25 KSFWDKYSDKPDTnsMMLNHSAEELESSDRADILASLPLLHNKDVVDIGAGIGRFTTVLAETARWVLSTDFIDSFIKKNQ 104
Cdd:COG4976 8 EALFDQYADSYDA--ALVEDLGYEAPALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAR 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564740 105 ERNAHlgnINYQVGDAVGLKMESNSVDLVFTNWLMMYLSDeeTVEFIFNCMRWLRSHGIV 164
Cdd:COG4976 86 EKGVY---DRLLVADLADLAEPDGRFDLIVAADVLTYLGD--LAAVFAGVARALKPGGLF 140
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
55-166 |
5.14e-09 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 56.08 E-value: 5.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564740 55 ADILASLPLL-HNKDVVDIGAGIGRFTTVLAETARW-VLSTDFIDSFIKKNQERN--AHLGNINYQVGDAVGLK-MESNS 129
Cdd:COG0500 15 AALLALLERLpKGGRVLDLGCGTGRNLLALAARFGGrVIGIDLSPEAIALARARAakAGLGNVEFLVADLAELDpLPAES 94
|
90 100 110
....*....|....*....|....*....|....*..
gi 32564740 130 VDLVFTNWLMMYLSDEETVEFIFNCMRWLRSHGIVHL 166
Cdd:COG0500 95 FDLVVAFGVLHHLPPEEREALLRELARALKPGGVLLL 131
|
|
| Methyltransf_PK |
pfam05891 |
AdoMet dependent proline di-methyltransferase; This protein is expressed in the tail neuron ... |
66-168 |
1.14e-08 |
|
AdoMet dependent proline di-methyltransferase; This protein is expressed in the tail neuron PVT and in uterine cells in C. elegans [worm-base]. In Saccharomyces cerevisiae this is AdoMet dependent proline di-methyltransferase. This enzyme catalyzes the di-methylation of ribosomal proteins Rpl12 and Rps25 at N-terminal proline residues. The methyltransferases described here specifically recognize the N-terminal X-Pro-Lys sequence motif, and they may account for nearly all previously described eukaryotic protein N-terminal methylation reactions. A number of other yeast and human proteins also share the recognition motif and may be similarly modified. As with other methyltransferases, this family carries the characteriztic GxGxG motif.
Pssm-ID: 461771 Cd Length: 218 Bit Score: 55.46 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564740 66 NKDVVDIGAGIGRFT-TVLAETARWVLSTDFIDSFIKKNQErnaHLGNINYQVGD--AVGLKM---ESNSVDLVFTNWLM 139
Cdd:pfam05891 56 HLVALDCGAGIGRVTkNLLLPLFSKVDLVEPVEDFIEKAKE---YLAEGKKKVGNffCVGLQDftpEEGRYDLIWIQWCI 132
|
90 100
....*....|....*....|....*....
gi 32564740 140 MYLSDEETVEFIFNCMRWLRSHGIVHLRE 168
Cdd:pfam05891 133 GHLTDEDLVAFLKRCKGGLKPNGFIVVKE 161
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
68-166 |
3.91e-08 |
|
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).
Pssm-ID: 100107 [Multi-domain] Cd Length: 107 Bit Score: 51.28 E-value: 3.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564740 68 DVVDIGAGIGRFTTVLAETARW-VLSTDFIDSFIKKNQERNAHLG--NINYQVGDAV-GLKMESNSVDLVFTNWLMMYLs 143
Cdd:cd02440 1 RVLDLGCGTGALALALASGPGArVTGVDISPVALELARKAAAALLadNVEVLKGDAEeLPPEADESFDVIISDPPLHHL- 79
|
90 100
....*....|....*....|...
gi 32564740 144 DEETVEFIFNCMRWLRSHGIVHL 166
Cdd:cd02440 80 VEDLARFLEEARRLLKPGGVLVL 102
|
|
| Tam |
COG4106 |
Trans-aconitate methyltransferase [Energy production and conversion]; |
69-164 |
4.43e-07 |
|
Trans-aconitate methyltransferase [Energy production and conversion];
Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 47.90 E-value: 4.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564740 69 VVDIGAGIGRFTTVLAEtaRW----VLSTDFIDSFIKKNQERnahLGNINYQVGDAVGLKMESnSVDLVFTNWLMMYLSD 144
Cdd:COG4106 5 VLDLGCGTGRLTALLAE--RFpgarVTGVDLSPEMLARARAR---LPNVRFVVADLRDLDPPE-PFDLVVSNAALHWLPD 78
|
90 100
....*....|....*....|
gi 32564740 145 EETVefIFNCMRWLRSHGIV 164
Cdd:COG4106 79 HAAL--LARLAAALAPGGVL 96
|
|
| PTZ00098 |
PTZ00098 |
phosphoethanolamine N-methyltransferase; Provisional |
57-172 |
4.56e-05 |
|
phosphoethanolamine N-methyltransferase; Provisional
Pssm-ID: 173391 [Multi-domain] Cd Length: 263 Bit Score: 44.96 E-value: 4.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564740 57 ILASLPLLHNKDVVDIGAGIGRFTTVLAET-ARWVLSTDFIDSFIKKNQERNAHLGNINYQVGDAVGLKMESNSVDLVFT 135
Cdd:PTZ00098 44 ILSDIELNENSKVLDIGSGLGGGCKYINEKyGAHVHGVDICEKMVNIAKLRNSDKNKIEFEANDILKKDFPENTFDMIYS 123
|
90 100 110
....*....|....*....|....*....|....*..
gi 32564740 136 NWLMMYLSDEETVEFIFNCMRWLRSHGIVHLRESCSE 172
Cdd:PTZ00098 124 RDAILHLSYADKKKLFEKCYKWLKPNGILLITDYCAD 160
|
|
| Methyltransf_31 |
pfam13847 |
Methyltransferase domain; This family appears to have methyltransferase activity. |
66-172 |
6.93e-05 |
|
Methyltransferase domain; This family appears to have methyltransferase activity.
Pssm-ID: 463998 [Multi-domain] Cd Length: 150 Bit Score: 42.79 E-value: 6.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564740 66 NKDVVDIGAGIGRFTTVLAETARW---VLSTDFIDSFIKKNQERNAHLG--NINYQVGDAVGLKM--ESNSVDLVFTNWL 138
Cdd:pfam13847 4 GMRVLDLGCGTGHLSFELAEELGPnaeVVGIDISEEAIEKARENAQKLGfdNVEFEQGDIEELPEllEDDKFDVVISNCV 83
|
90 100 110
....*....|....*....|....*....|....
gi 32564740 139 MMYLSDeeTVEFIFNCMRWLRSHGIVHLRESCSE 172
Cdd:pfam13847 84 LNHIPD--PDKVLQEILRVLKPGGRLIISDPDSL 115
|
|
| Methyltransf_12 |
pfam08242 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
70-164 |
4.00e-04 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 39.66 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564740 70 VDIGAGIGRFT-TVLAETARW-VLSTDFIDSFIKKNQERNAHLG-----NINYQVGDAvgLKMESNSVDLVFTNWLMMYL 142
Cdd:pfam08242 1 LEIGCGTGTLLrALLEALPGLeYTGLDISPAALEAARERLAALGllnavRVELFQLDL--GELDPGSFDVVVASNVLHHL 78
|
90 100
....*....|....*....|..
gi 32564740 143 SDeeTVEFIFNCMRWLRSHGIV 164
Cdd:pfam08242 79 AD--PRAVLRNIRRLLKPGGVL 98
|
|
| rADc |
smart00650 |
Ribosomal RNA adenine dimethylases; |
69-136 |
2.90e-03 |
|
Ribosomal RNA adenine dimethylases;
Pssm-ID: 128898 Cd Length: 169 Bit Score: 38.65 E-value: 2.90e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32564740 69 VVDIGAGIGRFTTVLAETARWVLSTDfIDS-FIKKNQERNAHLGNINYQVGDAVGLKMESNSVDLVFTN 136
Cdd:smart00650 17 VLEIGPGKGALTEELLERAKRVTAIE-IDPrLAPRLREKFAAADNLTVIHGDALKFDLPKLQPYKVVGN 84
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
24-166 |
5.28e-03 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 37.60 E-value: 5.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32564740 24 FKSFWD---KYSdkpdtnSMMLNHSAEELESSDRA---DILASLPLLHNKDVVDIGAGIGRFTTVLAETARW-VLSTDFI 96
Cdd:COG2230 10 YRLFLDptmTYS------CAYFEDPDDTLEEAQEAkldLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVrVTGVTLS 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32564740 97 DSFIKKNQERNAHLG---NINYQVGDAVGLKMEsNSVDLVFTNWLMMYLSDEETVEFIFNCMRWLRSHGIVHL 166
Cdd:COG2230 84 PEQLEYARERAAEAGladRVEVRLADYRDLPAD-GQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLL 155
|
|
| |
