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Conserved domains on  [gi|6322533|ref|NP_012607|]
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bifunctional phosphatidyl-N-methylethanolamine N-methyltransferase/phosphatidyl-N-dimethylethanolamine N-methyltransferase [Saccharomyces cerevisiae S288C]

Protein Classification

PEMT/PEM2 family methyltransferase( domain architecture ID 10514660)

PEMT/PEM2 family methyltransferase is involved in the methylation pathway of phosphatidylcholine biosynthesis, such as phosphatidylethanolamine N-methyltransferase (PEMT) that catalyzes the first step of the pathway, the SAM-dependent methylation of\n phosphatidylethanolamine (PE) to phosphatidylmonomethylethanolamine (PMME)

EC:  2.1.1.-
Gene Ontology:  GO:0008757|GO:0032259|GO:0006656|GO:1904047
PubMed:  2445736

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PEMT pfam04191
Phospholipid methyltransferase; The S. cerevisiae phospholipid methyltransferase (EC:2.1.1.16) ...
 100-199 9.57e-48

Phospholipid methyltransferase; The S. cerevisiae phospholipid methyltransferase (EC:2.1.1.16) has a broad substrate specificity of unsaturated phospholipids.


:

Pssm-ID: 461218 [Multi-domain]  Cd Length: 105  Bit Score: 151.95  E-value: 9.57e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322533    100 LGVALFGLGQVLVLSSMYKLGITGTYLGDYFGILMDERVTGFPFNVSNNPMYQGSTLSFLGIALYKGKPAGLVVSAVVYF 179
Cdd:pfam04191   5 LGLLLIALGLWLVLSSYRALGIFGTFYGDFFGILMDKLVTGGPYRYLNNPMYVGGTLGFLGLALITGSPAGLLLALLVLL 84

                          90       100
                  ....*....|....*....|.
gi 6322533    180 MYKIAL-RWEEPFTAMIYANR 199
Cdd:pfam04191  85 VYFIALkFVEEPHMAKIYGKR 105
 
Name Accession Description Interval E-value
PEMT pfam04191
Phospholipid methyltransferase; The S. cerevisiae phospholipid methyltransferase (EC:2.1.1.16) ...
 100-199 9.57e-48

Phospholipid methyltransferase; The S. cerevisiae phospholipid methyltransferase (EC:2.1.1.16) has a broad substrate specificity of unsaturated phospholipids.


Pssm-ID: 461218 [Multi-domain]  Cd Length: 105  Bit Score: 151.95  E-value: 9.57e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322533    100 LGVALFGLGQVLVLSSMYKLGITGTYLGDYFGILMDERVTGFPFNVSNNPMYQGSTLSFLGIALYKGKPAGLVVSAVVYF 179
Cdd:pfam04191   5 LGLLLIALGLWLVLSSYRALGIFGTFYGDFFGILMDKLVTGGPYRYLNNPMYVGGTLGFLGLALITGSPAGLLLALLVLL 84

                          90       100
                  ....*....|....*....|.
gi 6322533    180 MYKIAL-RWEEPFTAMIYANR 199
Cdd:pfam04191  85 VYFIALkFVEEPHMAKIYGKR 105
PLN02797 PLN02797
phosphatidyl-N-dimethylethanolamine N-methyltransferase
 102-160 1.90e-05

phosphatidyl-N-dimethylethanolamine N-methyltransferase


Pssm-ID: 178394  Cd Length: 164  Bit Score: 43.21  E-value: 1.90e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 6322533   102 VALFGLGQVLVLSSMYKLGITGTYLGDYFGiLMDERVTGFPFNVSNNPMYQGSTLSFLG 160
Cdd:PLN02797  70 WPLFAFGQFLNFRVYQLLGEAGTYYGVRFG-KNIPWVTEFPFGVIRDPQYVGSILSLLA 127
 
Name Accession Description Interval E-value
PEMT pfam04191
Phospholipid methyltransferase; The S. cerevisiae phospholipid methyltransferase (EC:2.1.1.16) ...
 100-199 9.57e-48

Phospholipid methyltransferase; The S. cerevisiae phospholipid methyltransferase (EC:2.1.1.16) has a broad substrate specificity of unsaturated phospholipids.


Pssm-ID: 461218 [Multi-domain]  Cd Length: 105  Bit Score: 151.95  E-value: 9.57e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322533    100 LGVALFGLGQVLVLSSMYKLGITGTYLGDYFGILMDERVTGFPFNVSNNPMYQGSTLSFLGIALYKGKPAGLVVSAVVYF 179
Cdd:pfam04191   5 LGLLLIALGLWLVLSSYRALGIFGTFYGDFFGILMDKLVTGGPYRYLNNPMYVGGTLGFLGLALITGSPAGLLLALLVLL 84

                          90       100
                  ....*....|....*....|.
gi 6322533    180 MYKIAL-RWEEPFTAMIYANR 199
Cdd:pfam04191  85 VYFIALkFVEEPHMAKIYGKR 105
PLN02797 PLN02797
phosphatidyl-N-dimethylethanolamine N-methyltransferase
 102-160 1.90e-05

phosphatidyl-N-dimethylethanolamine N-methyltransferase


Pssm-ID: 178394  Cd Length: 164  Bit Score: 43.21  E-value: 1.90e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 6322533   102 VALFGLGQVLVLSSMYKLGITGTYLGDYFGiLMDERVTGFPFNVSNNPMYQGSTLSFLG 160
Cdd:PLN02797  70 WPLFAFGQFLNFRVYQLLGEAGTYYGVRFG-KNIPWVTEFPFGVIRDPQYVGSILSLLA 127
 
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.
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