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Conserved domains on  [gi|568972176|ref|XP_006532541|]
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phosphatidylethanolamine N-methyltransferase isoform X1 [Mus musculus]

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) ...
 115-217 6.64e-42

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: 137.69  E-value: 6.64e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972176  115 TYFLGLAFLGWGFVFVLSSFYALGFTGTFLGDYFGILKESRVTTFPFSVLDNPMYWGSTANYLGWALMHASPTGLLLTVL 194
Cdd:pfam04191   2 RLILGLLLIALGLWLVLSSYRALGIFGTFYGDFFGILMDKLVTGGPYRYLNNPMYVGGTLGFLGLALITGSPAGLLLALL 81

                          90       100
                  ....*....|....*....|....
gi 568972176  195 VAIVYVVALLY-EEPFTAEIYRQK 217
Cdd:pfam04191  82 VLLVYFIALKFvEEPHMAKIYGKR 105
 
Name Accession Description Interval E-value
PEMT pfam04191
Phospholipid methyltransferase; The S. cerevisiae phospholipid methyltransferase (EC:2.1.1.16) ...
 115-217 6.64e-42

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: 137.69  E-value: 6.64e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972176  115 TYFLGLAFLGWGFVFVLSSFYALGFTGTFLGDYFGILKESRVTTFPFSVLDNPMYWGSTANYLGWALMHASPTGLLLTVL 194
Cdd:pfam04191   2 RLILGLLLIALGLWLVLSSYRALGIFGTFYGDFFGILMDKLVTGGPYRYLNNPMYVGGTLGFLGLALITGSPAGLLLALL 81

                          90       100
                  ....*....|....*....|....
gi 568972176  195 VAIVYVVALLY-EEPFTAEIYRQK 217
Cdd:pfam04191  82 VLLVYFIALKFvEEPHMAKIYGKR 105
STE14 COG2020
Protein-S-isoprenylcysteine O-methyltransferase Ste14 [Posttranslational modification, protein ...
 119-214 9.03e-11

Protein-S-isoprenylcysteine O-methyltransferase Ste14 [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441623 [Multi-domain]  Cd Length: 113  Bit Score: 57.09  E-value: 9.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972176 119 GLAFLGWGFVFVLSSFYALGFTGTFLGDyfgILKESR-VTTFPFSVLDNPMYWGSTANYLGWALMHASPTGLLLTVLVAI 197
Cdd:COG2020    2 GLVLILLGLLLRLWAVLTLGRSWTTLVP---PRKAHRlVTTGPYRYVRHPMYLGFLLLLLGLALLLGSLLALLLALLLLL 78

                         90
                 ....*....|....*..
gi 568972176 198 VYVVALLYEEPFTAEIY 214
Cdd:COG2020   79 LYVLRIRREERRLRARF 95
 
Name Accession Description Interval E-value
PEMT pfam04191
Phospholipid methyltransferase; The S. cerevisiae phospholipid methyltransferase (EC:2.1.1.16) ...
 115-217 6.64e-42

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: 137.69  E-value: 6.64e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972176  115 TYFLGLAFLGWGFVFVLSSFYALGFTGTFLGDYFGILKESRVTTFPFSVLDNPMYWGSTANYLGWALMHASPTGLLLTVL 194
Cdd:pfam04191   2 RLILGLLLIALGLWLVLSSYRALGIFGTFYGDFFGILMDKLVTGGPYRYLNNPMYVGGTLGFLGLALITGSPAGLLLALL 81

                          90       100
                  ....*....|....*....|....
gi 568972176  195 VAIVYVVALLY-EEPFTAEIYRQK 217
Cdd:pfam04191  82 VLLVYFIALKFvEEPHMAKIYGKR 105
STE14 COG2020
Protein-S-isoprenylcysteine O-methyltransferase Ste14 [Posttranslational modification, protein ...
 119-214 9.03e-11

Protein-S-isoprenylcysteine O-methyltransferase Ste14 [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441623 [Multi-domain]  Cd Length: 113  Bit Score: 57.09  E-value: 9.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568972176 119 GLAFLGWGFVFVLSSFYALGFTGTFLGDyfgILKESR-VTTFPFSVLDNPMYWGSTANYLGWALMHASPTGLLLTVLVAI 197
Cdd:COG2020    2 GLVLILLGLLLRLWAVLTLGRSWTTLVP---PRKAHRlVTTGPYRYVRHPMYLGFLLLLLGLALLLGSLLALLLALLLLL 78

                         90
                 ....*....|....*..
gi 568972176 198 VYVVALLYEEPFTAEIY 214
Cdd:COG2020   79 LYVLRIRREERRLRARF 95
 
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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