|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02336 |
PLN02336 |
phosphoethanolamine N-methyltransferase |
15-236 |
7.54e-50 |
|
phosphoethanolamine N-methyltransferase
Pssm-ID: 177970 [Multi-domain] Cd Length: 475 Bit Score: 176.48 E-value: 7.54e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972243425 15 KYSDKPDTNSMMLNHSAEELESSDRADILASLPLLHNKDVVDIGAGIGRFTTVLAETARWVLSTDFIDSFIKKNQERNAH 94
Cdd:PLN02336 2 EHSVDLTVEAMMLDSKASDLDKEERPEILSLLPPYEGKSVLELGAGIGRFTGELAKKAGQVIALDFIESVIKKNESINGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972243425 95 LGNINYQVGDAV--GLKMESNSVDLVFTNWLMMYLSDEETVEFIFNCMRWLRSHGIVHLRESCSEPStGRSKAKSmhdta 172
Cdd:PLN02336 82 YKNVKFMCADVTspDLNISDGSVDLIFSNWLLMYLSDKEVENLAERMVKWLKVGGYIFFRESCFHQS-GDSKRKN----- 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1972243425 173 naNPTHYRFSSLYINLLRAIRYRDVDNKLWRFNVQWSCSVPTYIKRSNNWRQVHWLAEKVPAED 236
Cdd:PLN02336 156 --NPTHYREPRFYTKVFKECHTRDEDGNSFELSLVGCKCIGAYVKNKKNQNQICWLWQKVSSTN 217
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
39-153 |
2.12e-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: 2.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972243425 39 RADILASLPLLHNKDVVDIGAGIGRFTTVLAETARWVLSTDFIDSFIKKNQERNAHLG-NINYQVGDAVGLKMESNSVDL 117
Cdd:COG2226 11 REALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGlNVEFVVGDAEDLPFPDGSFDL 90
|
90 100 110
....*....|....*....|....*....|....*.
gi 1972243425 118 VFTNWLMMYLSDEEtvEFIFNCMRWLRSHGIVHLRE 153
Cdd:COG2226 91 VISSFVLHHLPDPE--RALAEIARVLKPGGRLVVVD 124
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
54-147 |
4.86e-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: 4.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972243425 54 VVDIGAGIGRFTTVLAETARW-VLSTDFIDSFIKKNQERNAHLG-NINYQVGDAVGLKMESNSVDLVFTNWLMMYLSDEE 131
Cdd:pfam13649 1 VLDLGCGTGRLTLALARRGGArVTGVDLSPEMLERARERAAEAGlNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLPDPD 80
|
90
....*....|....*.
gi 1972243425 132 TVEFIFNCMRWLRSHG 147
Cdd:pfam13649 81 LEAALREIARVLKPGG 96
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
53-151 |
3.77e-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: 3.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972243425 53 DVVDIGAGIGRFTTVLAETARW-VLSTDFIDSFIKKNQERNAHLG--NINYQVGDAV-GLKMESNSVDLVFTNWLMMYLs 128
Cdd:cd02440 1 RVLDLGCGTGALALALASGPGArVTGVDISPVALELARKAAAALLadNVEVLKGDAEeLPPEADESFDVIISDPPLHHL- 79
|
90 100
....*....|....*....|...
gi 1972243425 129 DEETVEFIFNCMRWLRSHGIVHL 151
Cdd:cd02440 80 VEDLARFLEEARRLLKPGGVLVL 102
|
|
| rADc |
smart00650 |
Ribosomal RNA adenine dimethylases; |
54-121 |
2.79e-03 |
|
Ribosomal RNA adenine dimethylases;
Pssm-ID: 128898 Cd Length: 169 Bit Score: 38.65 E-value: 2.79e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1972243425 54 VVDIGAGIGRFTTVLAETARWVLSTDfIDS-FIKKNQERNAHLGNINYQVGDAVGLKMESNSVDLVFTN 121
Cdd:smart00650 17 VLEIGPGKGALTEELLERAKRVTAIE-IDPrLAPRLREKFAAADNLTVIHGDALKFDLPKLQPYKVVGN 84
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02336 |
PLN02336 |
phosphoethanolamine N-methyltransferase |
15-236 |
7.54e-50 |
|
phosphoethanolamine N-methyltransferase
Pssm-ID: 177970 [Multi-domain] Cd Length: 475 Bit Score: 176.48 E-value: 7.54e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972243425 15 KYSDKPDTNSMMLNHSAEELESSDRADILASLPLLHNKDVVDIGAGIGRFTTVLAETARWVLSTDFIDSFIKKNQERNAH 94
Cdd:PLN02336 2 EHSVDLTVEAMMLDSKASDLDKEERPEILSLLPPYEGKSVLELGAGIGRFTGELAKKAGQVIALDFIESVIKKNESINGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972243425 95 LGNINYQVGDAV--GLKMESNSVDLVFTNWLMMYLSDEETVEFIFNCMRWLRSHGIVHLRESCSEPStGRSKAKSmhdta 172
Cdd:PLN02336 82 YKNVKFMCADVTspDLNISDGSVDLIFSNWLLMYLSDKEVENLAERMVKWLKVGGYIFFRESCFHQS-GDSKRKN----- 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1972243425 173 naNPTHYRFSSLYINLLRAIRYRDVDNKLWRFNVQWSCSVPTYIKRSNNWRQVHWLAEKVPAED 236
Cdd:PLN02336 156 --NPTHYREPRFYTKVFKECHTRDEDGNSFELSLVGCKCIGAYVKNKKNQNQICWLWQKVSSTN 217
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
39-153 |
2.12e-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: 2.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972243425 39 RADILASLPLLHNKDVVDIGAGIGRFTTVLAETARWVLSTDFIDSFIKKNQERNAHLG-NINYQVGDAVGLKMESNSVDL 117
Cdd:COG2226 11 REALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGlNVEFVVGDAEDLPFPDGSFDL 90
|
90 100 110
....*....|....*....|....*....|....*.
gi 1972243425 118 VFTNWLMMYLSDEEtvEFIFNCMRWLRSHGIVHLRE 153
Cdd:COG2226 91 VISSFVLHHLPDPE--RALAEIARVLKPGGRLVVVD 124
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
54-147 |
4.86e-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: 4.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972243425 54 VVDIGAGIGRFTTVLAETARW-VLSTDFIDSFIKKNQERNAHLG-NINYQVGDAVGLKMESNSVDLVFTNWLMMYLSDEE 131
Cdd:pfam13649 1 VLDLGCGTGRLTLALARRGGArVTGVDLSPEMLERARERAAEAGlNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLPDPD 80
|
90
....*....|....*.
gi 1972243425 132 TVEFIFNCMRWLRSHG 147
Cdd:pfam13649 81 LEAALREIARVLKPGG 96
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
26-151 |
1.91e-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: 1.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972243425 26 MLNHSAEELESSDRADILASLpLLHNKDVVDIGAGIGRFTTVLAETARWVLSTDFIDSFIKKNQERNAHLgNINYQVGDA 105
Cdd:COG2227 1 MSDPDARDFWDRRLAALLARL-LPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAEL-NVDFVQGDL 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1972243425 106 VGLKMESNSVDLVFTNWLMMYLSDEEtvEFIFNCMRWLRSHGIVHL 151
Cdd:COG2227 79 EDLPLEDGSFDLVICSEVLEHLPDPA--ALLRELARLLKPGGLLLL 122
|
|
| Methyltransf_11 |
pfam08241 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
55-149 |
3.05e-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: 3.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972243425 55 VDIGAGIGRFTTVLAETARWVLSTDFIDSFIKKNQERNAHLGnINYQVGDAVGLKMESNSVDLVFTNWLMMYLSDeeTVE 134
Cdd:pfam08241 1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREG-LTFVVGDAEDLPFPDNSFDLVLSSEVLHHVED--PER 77
|
90
....*....|....*
gi 1972243425 135 FIFNCMRWLRSHGIV 149
Cdd:pfam08241 78 ALREIARVLKPGGIL 92
|
|
| COG4976 |
COG4976 |
Predicted methyltransferase, contains TPR repeat [General function prediction only]; |
10-149 |
2.17e-09 |
|
Predicted methyltransferase, contains TPR repeat [General function prediction only];
Pssm-ID: 444001 [Multi-domain] Cd Length: 181 Bit Score: 56.55 E-value: 2.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972243425 10 KSFWDKYSDKPDTnsMMLNHSAEELESSDRADILASLPLLHNKDVVDIGAGIGRFTTVLAETARWVLSTDFIDSFIKKNQ 89
Cdd:COG4976 8 EALFDQYADSYDA--ALVEDLGYEAPALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAR 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972243425 90 ERNAHlgnINYQVGDAVGLKMESNSVDLVFTNWLMMYLSDeeTVEFIFNCMRWLRSHGIV 149
Cdd:COG4976 86 EKGVY---DRLLVADLADLAEPDGRFDLIVAADVLTYLGD--LAAVFAGVARALKPGGLF 140
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
40-151 |
4.92e-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: 4.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972243425 40 ADILASLPLL-HNKDVVDIGAGIGRFTTVLAETARW-VLSTDFIDSFIKKNQERN--AHLGNINYQVGDAVGLK-MESNS 114
Cdd:COG0500 15 AALLALLERLpKGGRVLDLGCGTGRNLLALAARFGGrVIGIDLSPEAIALARARAakAGLGNVEFLVADLAELDpLPAES 94
|
90 100 110
....*....|....*....|....*....|....*..
gi 1972243425 115 VDLVFTNWLMMYLSDEETVEFIFNCMRWLRSHGIVHL 151
Cdd:COG0500 95 FDLVVAFGVLHHLPPEEREALLRELARALKPGGVLLL 131
|
|
| Methyltransf_PK |
pfam05891 |
AdoMet dependent proline di-methyltransferase; This protein is expressed in the tail neuron ... |
51-153 |
1.24e-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: 55.08 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972243425 51 NKDVVDIGAGIGRFT-TVLAETARWVLSTDFIDSFIKKNQErnaHLGNINYQVGD--AVGLKM---ESNSVDLVFTNWLM 124
Cdd:pfam05891 56 HLVALDCGAGIGRVTkNLLLPLFSKVDLVEPVEDFIEKAKE---YLAEGKKKVGNffCVGLQDftpEEGRYDLIWIQWCI 132
|
90 100
....*....|....*....|....*....
gi 1972243425 125 MYLSDEETVEFIFNCMRWLRSHGIVHLRE 153
Cdd:pfam05891 133 GHLTDEDLVAFLKRCKGGLKPNGFIVVKE 161
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
53-151 |
3.77e-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: 3.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972243425 53 DVVDIGAGIGRFTTVLAETARW-VLSTDFIDSFIKKNQERNAHLG--NINYQVGDAV-GLKMESNSVDLVFTNWLMMYLs 128
Cdd:cd02440 1 RVLDLGCGTGALALALASGPGArVTGVDISPVALELARKAAAALLadNVEVLKGDAEeLPPEADESFDVIISDPPLHHL- 79
|
90 100
....*....|....*....|...
gi 1972243425 129 DEETVEFIFNCMRWLRSHGIVHL 151
Cdd:cd02440 80 VEDLARFLEEARRLLKPGGVLVL 102
|
|
| Tam |
COG4106 |
Trans-aconitate methyltransferase [Energy production and conversion]; |
54-149 |
4.28e-07 |
|
Trans-aconitate methyltransferase [Energy production and conversion];
Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 47.90 E-value: 4.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972243425 54 VVDIGAGIGRFTTVLAEtaRW----VLSTDFIDSFIKKNQERnahLGNINYQVGDAVGLKMESnSVDLVFTNWLMMYLSD 129
Cdd:COG4106 5 VLDLGCGTGRLTALLAE--RFpgarVTGVDLSPEMLARARAR---LPNVRFVVADLRDLDPPE-PFDLVVSNAALHWLPD 78
|
90 100
....*....|....*....|
gi 1972243425 130 EETVefIFNCMRWLRSHGIV 149
Cdd:COG4106 79 HAAL--LARLAAALAPGGVL 96
|
|
| PTZ00098 |
PTZ00098 |
phosphoethanolamine N-methyltransferase; Provisional |
42-157 |
4.52e-05 |
|
phosphoethanolamine N-methyltransferase; Provisional
Pssm-ID: 173391 [Multi-domain] Cd Length: 263 Bit Score: 44.96 E-value: 4.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972243425 42 ILASLPLLHNKDVVDIGAGIGRFTTVLAET-ARWVLSTDFIDSFIKKNQERNAHLGNINYQVGDAVGLKMESNSVDLVFT 120
Cdd:PTZ00098 44 ILSDIELNENSKVLDIGSGLGGGCKYINEKyGAHVHGVDICEKMVNIAKLRNSDKNKIEFEANDILKKDFPENTFDMIYS 123
|
90 100 110
....*....|....*....|....*....|....*..
gi 1972243425 121 NWLMMYLSDEETVEFIFNCMRWLRSHGIVHLRESCSE 157
Cdd:PTZ00098 124 RDAILHLSYADKKKLFEKCYKWLKPNGILLITDYCAD 160
|
|
| Methyltransf_31 |
pfam13847 |
Methyltransferase domain; This family appears to have methyltransferase activity. |
51-157 |
6.66e-05 |
|
Methyltransferase domain; This family appears to have methyltransferase activity.
Pssm-ID: 463998 [Multi-domain] Cd Length: 150 Bit Score: 42.79 E-value: 6.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972243425 51 NKDVVDIGAGIGRFTTVLAETARW---VLSTDFIDSFIKKNQERNAHLG--NINYQVGDAVGLKM--ESNSVDLVFTNWL 123
Cdd:pfam13847 4 GMRVLDLGCGTGHLSFELAEELGPnaeVVGIDISEEAIEKARENAQKLGfdNVEFEQGDIEELPEllEDDKFDVVISNCV 83
|
90 100 110
....*....|....*....|....*....|....
gi 1972243425 124 MMYLSDeeTVEFIFNCMRWLRSHGIVHLRESCSE 157
Cdd:pfam13847 84 LNHIPD--PDKVLQEILRVLKPGGRLIISDPDSL 115
|
|
| Methyltransf_12 |
pfam08242 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
55-149 |
3.86e-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: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972243425 55 VDIGAGIGRFT-TVLAETARW-VLSTDFIDSFIKKNQERNAHLG-----NINYQVGDAvgLKMESNSVDLVFTNWLMMYL 127
Cdd:pfam08242 1 LEIGCGTGTLLrALLEALPGLeYTGLDISPAALEAARERLAALGllnavRVELFQLDL--GELDPGSFDVVVASNVLHHL 78
|
90 100
....*....|....*....|..
gi 1972243425 128 SDeeTVEFIFNCMRWLRSHGIV 149
Cdd:pfam08242 79 AD--PRAVLRNIRRLLKPGGVL 98
|
|
| rADc |
smart00650 |
Ribosomal RNA adenine dimethylases; |
54-121 |
2.79e-03 |
|
Ribosomal RNA adenine dimethylases;
Pssm-ID: 128898 Cd Length: 169 Bit Score: 38.65 E-value: 2.79e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1972243425 54 VVDIGAGIGRFTTVLAETARWVLSTDfIDS-FIKKNQERNAHLGNINYQVGDAVGLKMESNSVDLVFTN 121
Cdd:smart00650 17 VLEIGPGKGALTEELLERAKRVTAIE-IDPrLAPRLREKFAAADNLTVIHGDALKFDLPKLQPYKVVGN 84
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
9-151 |
5.08e-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: 5.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972243425 9 FKSFWD---KYSdkpdtnSMMLNHSAEELESSDRA---DILASLPLLHNKDVVDIGAGIGRFTTVLAETARW-VLSTDFI 81
Cdd:COG2230 10 YRLFLDptmTYS------CAYFEDPDDTLEEAQEAkldLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVrVTGVTLS 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1972243425 82 DSFIKKNQERNAHLG---NINYQVGDAVGLKMEsNSVDLVFTNWLMMYLSDEETVEFIFNCMRWLRSHGIVHL 151
Cdd:COG2230 84 PEQLEYARERAAEAGladRVEVRLADYRDLPAD-GQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLL 155
|
|
| RsmC |
COG2813 |
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ... |
36-121 |
9.67e-03 |
|
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA G1207 methylase RsmC is part of the Pathway/BioSystem: 16S rRNA modification
Pssm-ID: 442062 [Multi-domain] Cd Length: 191 Bit Score: 37.09 E-value: 9.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972243425 36 SSDRADI-----LASLPLLHNKDVVDIGAGIGRFTTVLAEtARWVLSTDFID-SFI-----KKNQERNaHLGNINYQVGD 104
Cdd:COG2813 30 SRDRLDIgtrllLEHLPEPLGGRVLDLGCGYGVIGLALAK-RNPEARVTLVDvNARavelaRANAAAN-GLENVEVLWSD 107
|
90
....*....|....*..
gi 1972243425 105 aVGLKMESNSVDLVFTN 121
Cdd:COG2813 108 -GLSGVPDGSFDLILSN 123
|
|
| |
