NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|17537905|ref|NP_494991|]
View 

Phosphoethanolamine N-methyltransferase 1 [Caenorhabditis elegans]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 1009176)

class I SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor; similar to Caenorhabditis elegans phosphoethanolamine N-methyltransferase 1

CATH:  3.40.50.150
EC:  2.1.1.-
PubMed:  12504684|12826405
SCOP:  3000118

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PLN02336 super family cl31863
phosphoethanolamine N-methyltransferase
39-260 1.28e-49

phosphoethanolamine N-methyltransferase


The actual alignment was detected with superfamily member PLN02336:

Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 176.48  E-value: 1.28e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537905   39 KYSDKPDTNSMMLNHSAEELESSDRADILASLPLLHNKDVVDIGAGIGRFTTVLAETARWVLSTDFIDSFIKKNQERNAH 118
Cdd:PLN02336   2 EHSVDLTVEAMMLDSKASDLDKEERPEILSLLPPYEGKSVLELGAGIGRFTGELAKKAGQVIALDFIESVIKKNESINGH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537905  119 LGNINYQVGDAV--GLKMESNSVDLVFTNWLMMYLSDEETVEFIFNCMRWLRSHGIVHLRESCSEPStGRSKAKSmhdta 196
Cdd:PLN02336  82 YKNVKFMCADVTspDLNISDGSVDLIFSNWLLMYLSDKEVENLAERMVKWLKVGGYIFFRESCFHQS-GDSKRKN----- 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17537905  197 naNPTHYRFSSLYINLLRAIRYRDVDNKLWRFNVQWSCSVPTYIKRSNNWRQVHWLAEKVPAED 260
Cdd:PLN02336 156 --NPTHYREPRFYTKVFKECHTRDEDGNSFELSLVGCKCIGAYVKNKKNQNQICWLWQKVSSTN 217
 
Name Accession Description Interval E-value
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
39-260 1.28e-49

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 176.48  E-value: 1.28e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537905   39 KYSDKPDTNSMMLNHSAEELESSDRADILASLPLLHNKDVVDIGAGIGRFTTVLAETARWVLSTDFIDSFIKKNQERNAH 118
Cdd:PLN02336   2 EHSVDLTVEAMMLDSKASDLDKEERPEILSLLPPYEGKSVLELGAGIGRFTGELAKKAGQVIALDFIESVIKKNESINGH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537905  119 LGNINYQVGDAV--GLKMESNSVDLVFTNWLMMYLSDEETVEFIFNCMRWLRSHGIVHLRESCSEPStGRSKAKSmhdta 196
Cdd:PLN02336  82 YKNVKFMCADVTspDLNISDGSVDLIFSNWLLMYLSDKEVENLAERMVKWLKVGGYIFFRESCFHQS-GDSKRKN----- 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17537905  197 naNPTHYRFSSLYINLLRAIRYRDVDNKLWRFNVQWSCSVPTYIKRSNNWRQVHWLAEKVPAED 260
Cdd:PLN02336 156 --NPTHYREPRFYTKVFKECHTRDEDGNSFELSLVGCKCIGAYVKNKKNQNQICWLWQKVSSTN 217
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
63-177 2.28e-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: 2.28e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537905  63 RADILASLPLLHNKDVVDIGAGIGRFTTVLAETARWVLSTDFIDSFIKKNQERNAHLG-NINYQVGDAVGLKMESNSVDL 141
Cdd:COG2226  11 REALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGlNVEFVVGDAEDLPFPDGSFDL 90
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 17537905 142 VFTNWLMMYLSDEEtvEFIFNCMRWLRSHGIVHLRE 177
Cdd:COG2226  91 VISSFVLHHLPDPE--RALAEIARVLKPGGRLVVVD 124
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
78-171 5.17e-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: 5.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537905    78 VVDIGAGIGRFTTVLAETARW-VLSTDFIDSFIKKNQERNAHLG-NINYQVGDAVGLKMESNSVDLVFTNWLMMYLSDEE 155
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGArVTGVDLSPEMLERARERAAEAGlNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLPDPD 80
                          90
                  ....*....|....*.
gi 17537905   156 TVEFIFNCMRWLRSHG 171
Cdd:pfam13649  81 LEAALREIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
77-175 4.00e-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: 4.00e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537905  77 DVVDIGAGIGRFTTVLAETARW-VLSTDFIDSFIKKNQERNAHLG--NINYQVGDAV-GLKMESNSVDLVFTNWLMMYLs 152
Cdd:cd02440   1 RVLDLGCGTGALALALASGPGArVTGVDISPVALELARKAAAALLadNVEVLKGDAEeLPPEADESFDVIISDPPLHHL- 79
                        90       100
                ....*....|....*....|...
gi 17537905 153 DEETVEFIFNCMRWLRSHGIVHL 175
Cdd:cd02440  80 VEDLARFLEEARRLLKPGGVLVL 102
rADc smart00650
Ribosomal RNA adenine dimethylases;
78-145 2.97e-03

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 38.65  E-value: 2.97e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17537905     78 VVDIGAGIGRFTTVLAETARWVLSTDfIDS-FIKKNQERNAHLGNINYQVGDAVGLKMESNSVDLVFTN 145
Cdd:smart00650  17 VLEIGPGKGALTEELLERAKRVTAIE-IDPrLAPRLREKFAAADNLTVIHGDALKFDLPKLQPYKVVGN 84
 
Name Accession Description Interval E-value
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
39-260 1.28e-49

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 176.48  E-value: 1.28e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537905   39 KYSDKPDTNSMMLNHSAEELESSDRADILASLPLLHNKDVVDIGAGIGRFTTVLAETARWVLSTDFIDSFIKKNQERNAH 118
Cdd:PLN02336   2 EHSVDLTVEAMMLDSKASDLDKEERPEILSLLPPYEGKSVLELGAGIGRFTGELAKKAGQVIALDFIESVIKKNESINGH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537905  119 LGNINYQVGDAV--GLKMESNSVDLVFTNWLMMYLSDEETVEFIFNCMRWLRSHGIVHLRESCSEPStGRSKAKSmhdta 196
Cdd:PLN02336  82 YKNVKFMCADVTspDLNISDGSVDLIFSNWLLMYLSDKEVENLAERMVKWLKVGGYIFFRESCFHQS-GDSKRKN----- 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17537905  197 naNPTHYRFSSLYINLLRAIRYRDVDNKLWRFNVQWSCSVPTYIKRSNNWRQVHWLAEKVPAED 260
Cdd:PLN02336 156 --NPTHYREPRFYTKVFKECHTRDEDGNSFELSLVGCKCIGAYVKNKKNQNQICWLWQKVSSTN 217
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
63-177 2.28e-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: 2.28e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537905  63 RADILASLPLLHNKDVVDIGAGIGRFTTVLAETARWVLSTDFIDSFIKKNQERNAHLG-NINYQVGDAVGLKMESNSVDL 141
Cdd:COG2226  11 REALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGlNVEFVVGDAEDLPFPDGSFDL 90
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 17537905 142 VFTNWLMMYLSDEEtvEFIFNCMRWLRSHGIVHLRE 177
Cdd:COG2226  91 VISSFVLHHLPDPE--RALAEIARVLKPGGRLVVVD 124
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
78-171 5.17e-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: 5.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537905    78 VVDIGAGIGRFTTVLAETARW-VLSTDFIDSFIKKNQERNAHLG-NINYQVGDAVGLKMESNSVDLVFTNWLMMYLSDEE 155
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGArVTGVDLSPEMLERARERAAEAGlNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLPDPD 80
                          90
                  ....*....|....*.
gi 17537905   156 TVEFIFNCMRWLRSHG 171
Cdd:pfam13649  81 LEAALREIARVLKPGG 96
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
50-175 2.03e-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: 2.03e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537905  50 MLNHSAEELESSDRADILASLpLLHNKDVVDIGAGIGRFTTVLAETARWVLSTDFIDSFIKKNQERNAHLgNINYQVGDA 129
Cdd:COG2227   1 MSDPDARDFWDRRLAALLARL-LPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAEL-NVDFVQGDL 78
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 17537905 130 VGLKMESNSVDLVFTNWLMMYLSDEEtvEFIFNCMRWLRSHGIVHL 175
Cdd:COG2227  79 EDLPLEDGSFDLVICSEVLEHLPDPA--ALLRELARLLKPGGLLLL 122
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
79-173 3.22e-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: 3.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537905    79 VDIGAGIGRFTTVLAETARWVLSTDFIDSFIKKNQERNAHLGnINYQVGDAVGLKMESNSVDLVFTNWLMMYLSDeeTVE 158
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREG-LTFVVGDAEDLPFPDNSFDLVLSSEVLHHVED--PER 77
                          90
                  ....*....|....*
gi 17537905   159 FIFNCMRWLRSHGIV 173
Cdd:pfam08241  78 ALREIARVLKPGGIL 92
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
34-173 2.32e-09

Predicted methyltransferase, contains TPR repeat [General function prediction only];


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 56.55  E-value: 2.32e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537905  34 KSFWDKYSDKPDTnsMMLNHSAEELESSDRADILASLPLLHNKDVVDIGAGIGRFTTVLAETARWVLSTDFIDSFIKKNQ 113
Cdd:COG4976   8 EALFDQYADSYDA--ALVEDLGYEAPALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAR 85
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537905 114 ERNAHlgnINYQVGDAVGLKMESNSVDLVFTNWLMMYLSDeeTVEFIFNCMRWLRSHGIV 173
Cdd:COG4976  86 EKGVY---DRLLVADLADLAEPDGRFDLIVAADVLTYLGD--LAAVFAGVARALKPGGLF 140
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
64-175 5.27e-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: 5.27e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537905  64 ADILASLPLL-HNKDVVDIGAGIGRFTTVLAETARW-VLSTDFIDSFIKKNQERN--AHLGNINYQVGDAVGLK-MESNS 138
Cdd:COG0500  15 AALLALLERLpKGGRVLDLGCGTGRNLLALAARFGGrVIGIDLSPEAIALARARAakAGLGNVEFLVADLAELDpLPAES 94
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 17537905 139 VDLVFTNWLMMYLSDEETVEFIFNCMRWLRSHGIVHL 175
Cdd:COG0500  95 FDLVVAFGVLHHLPPEEREALLRELARALKPGGVLLL 131
Methyltransf_PK pfam05891
AdoMet dependent proline di-methyltransferase; This protein is expressed in the tail neuron ...
75-177 1.28e-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: 1.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537905    75 NKDVVDIGAGIGRFT-TVLAETARWVLSTDFIDSFIKKNQErnaHLGNINYQVGD--AVGLKM---ESNSVDLVFTNWLM 148
Cdd:pfam05891  56 HLVALDCGAGIGRVTkNLLLPLFSKVDLVEPVEDFIEKAKE---YLAEGKKKVGNffCVGLQDftpEEGRYDLIWIQWCI 132
                          90       100
                  ....*....|....*....|....*....
gi 17537905   149 MYLSDEETVEFIFNCMRWLRSHGIVHLRE 177
Cdd:pfam05891 133 GHLTDEDLVAFLKRCKGGLKPNGFIVVKE 161
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
77-175 4.00e-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: 4.00e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537905  77 DVVDIGAGIGRFTTVLAETARW-VLSTDFIDSFIKKNQERNAHLG--NINYQVGDAV-GLKMESNSVDLVFTNWLMMYLs 152
Cdd:cd02440   1 RVLDLGCGTGALALALASGPGArVTGVDISPVALELARKAAAALLadNVEVLKGDAEeLPPEADESFDVIISDPPLHHL- 79
                        90       100
                ....*....|....*....|...
gi 17537905 153 DEETVEFIFNCMRWLRSHGIVHL 175
Cdd:cd02440  80 VEDLARFLEEARRLLKPGGVLVL 102
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
78-173 4.52e-07

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 47.90  E-value: 4.52e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537905  78 VVDIGAGIGRFTTVLAEtaRW----VLSTDFIDSFIKKNQERnahLGNINYQVGDAVGLKMESnSVDLVFTNWLMMYLSD 153
Cdd:COG4106   5 VLDLGCGTGRLTALLAE--RFpgarVTGVDLSPEMLARARAR---LPNVRFVVADLRDLDPPE-PFDLVVSNAALHWLPD 78
                        90       100
                ....*....|....*....|
gi 17537905 154 EETVefIFNCMRWLRSHGIV 173
Cdd:COG4106  79 HAAL--LARLAAALAPGGVL 96
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
66-181 5.17e-05

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 44.96  E-value: 5.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537905   66 ILASLPLLHNKDVVDIGAGIGRFTTVLAET-ARWVLSTDFIDSFIKKNQERNAHLGNINYQVGDAVGLKMESNSVDLVFT 144
Cdd:PTZ00098  44 ILSDIELNENSKVLDIGSGLGGGCKYINEKyGAHVHGVDICEKMVNIAKLRNSDKNKIEFEANDILKKDFPENTFDMIYS 123
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 17537905  145 NWLMMYLSDEETVEFIFNCMRWLRSHGIVHLRESCSE 181
Cdd:PTZ00098 124 RDAILHLSYADKKKLFEKCYKWLKPNGILLITDYCAD 160
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
78-181 7.65e-05

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 42.79  E-value: 7.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537905    78 VVDIGAGIGRFTTVLAETARW---VLSTDFIDSFIKKNQERNAHLG--NINYQVGDAVGLKM--ESNSVDLVFTNWLMMY 150
Cdd:pfam13847   7 VLDLGCGTGHLSFELAEELGPnaeVVGIDISEEAIEKARENAQKLGfdNVEFEQGDIEELPEllEDDKFDVVISNCVLNH 86
                          90       100       110
                  ....*....|....*....|....*....|.
gi 17537905   151 LSDeeTVEFIFNCMRWLRSHGIVHLRESCSE 181
Cdd:pfam13847  87 IPD--PDKVLQEILRVLKPGGRLIISDPDSL 115
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
79-173 4.09e-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: 4.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537905    79 VDIGAGIGRFT-TVLAETARW-VLSTDFIDSFIKKNQERNAHLG-----NINYQVGDAvgLKMESNSVDLVFTNWLMMYL 151
Cdd:pfam08242   1 LEIGCGTGTLLrALLEALPGLeYTGLDISPAALEAARERLAALGllnavRVELFQLDL--GELDPGSFDVVVASNVLHHL 78
                          90       100
                  ....*....|....*....|..
gi 17537905   152 SDeeTVEFIFNCMRWLRSHGIV 173
Cdd:pfam08242  79 AD--PRAVLRNIRRLLKPGGVL 98
rADc smart00650
Ribosomal RNA adenine dimethylases;
78-145 2.97e-03

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 38.65  E-value: 2.97e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17537905     78 VVDIGAGIGRFTTVLAETARWVLSTDfIDS-FIKKNQERNAHLGNINYQVGDAVGLKMESNSVDLVFTN 145
Cdd:smart00650  17 VLEIGPGKGALTEELLERAKRVTAIE-IDPrLAPRLREKFAAADNLTVIHGDALKFDLPKLQPYKVVGN 84
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
33-175 5.40e-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: 5.40e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537905  33 FKSFWD---KYSdkpdtnSMMLNHSAEELESSDRA---DILASLPLLHNKDVVDIGAGIGRFTTVLAETARW-VLSTDFI 105
Cdd:COG2230  10 YRLFLDptmTYS------CAYFEDPDDTLEEAQEAkldLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVrVTGVTLS 83
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17537905 106 DSFIKKNQERNAHLG---NINYQVGDAVGLKMEsNSVDLVFTNWLMMYLSDEETVEFIFNCMRWLRSHGIVHL 175
Cdd:COG2230  84 PEQLEYARERAAEAGladRVEVRLADYRDLPAD-GQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLL 155
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH