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Conserved domains on  [gi|22538482|ref|NP_009100|]
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phosphatidylethanolamine N-methyltransferase isoform 2 [Homo sapiens]

Protein Classification

PEMT/PEM2 methyltransferase family protein( domain architecture ID 10514660)

PEMT/PEM2 methyltransferase family similar to Saccharomyces cerevisiae phosphatidylethanolamine N-methyltransferase (PEMT) and phosphatidyl-N-methylethanolamine N-methyltransferase (PLMT/PEM2)

EC:  2.1.1.-
Gene Ontology:  GO:0008168|GO:0032259|GO:0006656

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) ...
 108-191 4.14e-27

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: 98.79  E-value: 4.14e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538482   108 FFALGFAGTFLGDYFGILKEARVTVFPFNILDNPMYWGSTANYLGWAIMHASPTGLLLTVLVALTYIVALLY-EEPFTAE 186
Cdd:pfam04191  21 YRALGIFGTFYGDFFGILMDKLVTGGPYRYLNNPMYVGGTLGFLGLALITGSPAGLLLALLVLLVYFIALKFvEEPHMAK 100


                  ....*
gi 22538482   187 IYRQK 191
Cdd:pfam04191 101 IYGKR 105
 
Name Accession Description Interval E-value
PEMT pfam04191
Phospholipid methyltransferase; The S. cerevisiae phospholipid methyltransferase (EC:2.1.1.16) ...
 108-191 4.14e-27

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: 98.79  E-value: 4.14e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538482   108 FFALGFAGTFLGDYFGILKEARVTVFPFNILDNPMYWGSTANYLGWAIMHASPTGLLLTVLVALTYIVALLY-EEPFTAE 186
Cdd:pfam04191  21 YRALGIFGTFYGDFFGILMDKLVTGGPYRYLNNPMYVGGTLGFLGLALITGSPAGLLLALLVLLVYFIALKFvEEPHMAK 100


                  ....*
gi 22538482   187 IYRQK 191
Cdd:pfam04191 101 IYGKR 105
 
Name Accession Description Interval E-value
PEMT pfam04191
Phospholipid methyltransferase; The S. cerevisiae phospholipid methyltransferase (EC:2.1.1.16) ...
 108-191 4.14e-27

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: 98.79  E-value: 4.14e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538482   108 FFALGFAGTFLGDYFGILKEARVTVFPFNILDNPMYWGSTANYLGWAIMHASPTGLLLTVLVALTYIVALLY-EEPFTAE 186
Cdd:pfam04191  21 YRALGIFGTFYGDFFGILMDKLVTGGPYRYLNNPMYVGGTLGFLGLALITGSPAGLLLALLVLLVYFIALKFvEEPHMAK 100


                  ....*
gi 22538482   187 IYRQK 191
Cdd:pfam04191 101 IYGKR 105
 
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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