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Conserved domains on  [gi|568942760|ref|XP_006506616|]
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phosphatidate cytidylyltransferase, mitochondrial isoform X2 [Mus musculus]

Protein Classification

phosphatidate cytidylyltransferase( domain architecture ID 141745)

phosphatidate cytidylyltransferase catalyzes the conversion of phosphatidic acid (PA) to CDP-diacylglycerol (CDP-DAG), an essential intermediate in the synthesis of phosphatidylglycerol, cardiolipin and phosphatidylinositol

EC:  2.7.7.41
Gene Ontology:  GO:0004605|GO:0032049|GO:0016024

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Tam41_Mmp37 super family cl20372
Phosphatidate cytidylyltransferase, mitochondrial; Tam41 also known as MMp37 is a ...
7-185 1.43e-76

Phosphatidate cytidylyltransferase, mitochondrial; Tam41 also known as MMp37 is a mitochondrial phosphatidate cytidylyltransferase (CDP-DAG synthase)(EC:2.7.7.41) that catalyzes the formation of CDP-diacylglycerol (CDP-DAG) from phosphatidic acid (PA) in the mitochondrial inner membrane. It is required for the biosynthesis of the dimeric phospholipid cardiolipin, which stabilizes supercomplexes of the mitochondrial respiratory chain in the mitochondrial inner membrane. It is suggested that the N-terminal portion of Tam41 may possess the NTase (Nucleotide Transferase) fold, which is consistent with the CDP-DAG synthase function of Tam41. Furthermore, it has been shown that Tam41/MMP37 proteins possess the NTase fold but they have only one active site carboxylate and thus probably are not able to carry out enzymatic reaction. These potentially non-active members of NTase fold superfamily may bind ATP, hydrolysis of which is necessary for the translocation of proteins through the membrane.


The actual alignment was detected with superfamily member pfam09139:

Pssm-ID: 462690  Cd Length: 322  Bit Score: 232.03  E-value: 1.43e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942760    7 LRAALDKNLRSAVTTACLMLPESFSEEDLFIEIAGLSYSGDFRMVIGEEKSKVLNIVKPNVGHFRELYESILQKDPQVVY 86
Cdd:pfam09139 135 LRLANQVNLKSALRAALLLLPEKFTEEELYETIAGLSYMGDFRMLFGENPNKVNNIVSGQLHHFRKLYAPLLGILPNVDF 214
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942760   87 --------KMHQGQLEIDKSPEGQFTQLMTLPRTLQQQINHIMDPPGRNRDVEETLL-QVAQDPDCGDVVRLAISSIVRP 157
Cdd:pfam09139 215 lkdpfhsfIHWGVTLEQDMSPIARLNLLRLLPKLLRQKLYFQYQRKRHVRRDGEIFLrAIAYDDLLREVVQKAIRKIVRW 294
                         170       180
                  ....*....|....*....|....*...
gi 568942760  158 SSIRQSTKGLFTAGMKKSVIYSSRKLNK 185
Cdd:pfam09139 295 SSTRQSIKGILTAGLTKSVRYATEKRKK 322
 
Name Accession Description Interval E-value
Tam41_Mmp37 pfam09139
Phosphatidate cytidylyltransferase, mitochondrial; Tam41 also known as MMp37 is a ...
7-185 1.43e-76

Phosphatidate cytidylyltransferase, mitochondrial; Tam41 also known as MMp37 is a mitochondrial phosphatidate cytidylyltransferase (CDP-DAG synthase)(EC:2.7.7.41) that catalyzes the formation of CDP-diacylglycerol (CDP-DAG) from phosphatidic acid (PA) in the mitochondrial inner membrane. It is required for the biosynthesis of the dimeric phospholipid cardiolipin, which stabilizes supercomplexes of the mitochondrial respiratory chain in the mitochondrial inner membrane. It is suggested that the N-terminal portion of Tam41 may possess the NTase (Nucleotide Transferase) fold, which is consistent with the CDP-DAG synthase function of Tam41. Furthermore, it has been shown that Tam41/MMP37 proteins possess the NTase fold but they have only one active site carboxylate and thus probably are not able to carry out enzymatic reaction. These potentially non-active members of NTase fold superfamily may bind ATP, hydrolysis of which is necessary for the translocation of proteins through the membrane.


Pssm-ID: 462690  Cd Length: 322  Bit Score: 232.03  E-value: 1.43e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942760    7 LRAALDKNLRSAVTTACLMLPESFSEEDLFIEIAGLSYSGDFRMVIGEEKSKVLNIVKPNVGHFRELYESILQKDPQVVY 86
Cdd:pfam09139 135 LRLANQVNLKSALRAALLLLPEKFTEEELYETIAGLSYMGDFRMLFGENPNKVNNIVSGQLHHFRKLYAPLLGILPNVDF 214
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942760   87 --------KMHQGQLEIDKSPEGQFTQLMTLPRTLQQQINHIMDPPGRNRDVEETLL-QVAQDPDCGDVVRLAISSIVRP 157
Cdd:pfam09139 215 lkdpfhsfIHWGVTLEQDMSPIARLNLLRLLPKLLRQKLYFQYQRKRHVRRDGEIFLrAIAYDDLLREVVQKAIRKIVRW 294
                         170       180
                  ....*....|....*....|....*...
gi 568942760  158 SSIRQSTKGLFTAGMKKSVIYSSRKLNK 185
Cdd:pfam09139 295 SSTRQSIKGILTAGLTKSVRYATEKRKK 322
 
Name Accession Description Interval E-value
Tam41_Mmp37 pfam09139
Phosphatidate cytidylyltransferase, mitochondrial; Tam41 also known as MMp37 is a ...
7-185 1.43e-76

Phosphatidate cytidylyltransferase, mitochondrial; Tam41 also known as MMp37 is a mitochondrial phosphatidate cytidylyltransferase (CDP-DAG synthase)(EC:2.7.7.41) that catalyzes the formation of CDP-diacylglycerol (CDP-DAG) from phosphatidic acid (PA) in the mitochondrial inner membrane. It is required for the biosynthesis of the dimeric phospholipid cardiolipin, which stabilizes supercomplexes of the mitochondrial respiratory chain in the mitochondrial inner membrane. It is suggested that the N-terminal portion of Tam41 may possess the NTase (Nucleotide Transferase) fold, which is consistent with the CDP-DAG synthase function of Tam41. Furthermore, it has been shown that Tam41/MMP37 proteins possess the NTase fold but they have only one active site carboxylate and thus probably are not able to carry out enzymatic reaction. These potentially non-active members of NTase fold superfamily may bind ATP, hydrolysis of which is necessary for the translocation of proteins through the membrane.


Pssm-ID: 462690  Cd Length: 322  Bit Score: 232.03  E-value: 1.43e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942760    7 LRAALDKNLRSAVTTACLMLPESFSEEDLFIEIAGLSYSGDFRMVIGEEKSKVLNIVKPNVGHFRELYESILQKDPQVVY 86
Cdd:pfam09139 135 LRLANQVNLKSALRAALLLLPEKFTEEELYETIAGLSYMGDFRMLFGENPNKVNNIVSGQLHHFRKLYAPLLGILPNVDF 214
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942760   87 --------KMHQGQLEIDKSPEGQFTQLMTLPRTLQQQINHIMDPPGRNRDVEETLL-QVAQDPDCGDVVRLAISSIVRP 157
Cdd:pfam09139 215 lkdpfhsfIHWGVTLEQDMSPIARLNLLRLLPKLLRQKLYFQYQRKRHVRRDGEIFLrAIAYDDLLREVVQKAIRKIVRW 294
                         170       180
                  ....*....|....*....|....*...
gi 568942760  158 SSIRQSTKGLFTAGMKKSVIYSSRKLNK 185
Cdd:pfam09139 295 SSTRQSIKGILTAGLTKSVRYATEKRKK 322
 
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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