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Conserved domains on  [gi|1007892835|ref|NP_001308224|]
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phosphatidate cytidylyltransferase, mitochondrial isoform d [Homo sapiens]

Protein Classification

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 ...
 1-161 6.23e-68

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: 209.30  E-value: 6.23e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007892835   1 MLPESFSEEDLFIEIAGLSYSGDFRMVVGEDKTKVLNIVKPNIAHFRELYGSILQENPQVVYK-----SQQGW---LEID 72
Cdd:pfam09139 153 LLPEKFTEEELYETIAGLSYMGDFRMLFGENPNKVNNIVSGQLHHFRKLYAPLLGILPNVDFLkdpfhSFIHWgvtLEQD 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007892835  73 KSPEGQFTQLMTLPKTLQQQINHIMDPPGKNR-DVEETLFQVAHDPDCGDVVRLGLSAIVRPSSIRQSTKGIFTAGLKKS 151
Cdd:pfam09139 233 MSPIARLNLLRLLPKLLRQKLYFQYQRKRHVRrDGEIFLRAIAYDDLLREVVQKAIRKIVRWSSTRQSIKGILTAGLTKS 312

                         170
                  ....*....|
gi 1007892835 152 VIYSSLKLHK 161
Cdd:pfam09139 313 VRYATEKRKK 322
 
Name Accession Description Interval E-value
Tam41_Mmp37 pfam09139
Phosphatidate cytidylyltransferase, mitochondrial; Tam41 also known as MMp37 is a ...
 1-161 6.23e-68

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: 209.30  E-value: 6.23e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007892835   1 MLPESFSEEDLFIEIAGLSYSGDFRMVVGEDKTKVLNIVKPNIAHFRELYGSILQENPQVVYK-----SQQGW---LEID 72
Cdd:pfam09139 153 LLPEKFTEEELYETIAGLSYMGDFRMLFGENPNKVNNIVSGQLHHFRKLYAPLLGILPNVDFLkdpfhSFIHWgvtLEQD 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007892835  73 KSPEGQFTQLMTLPKTLQQQINHIMDPPGKNR-DVEETLFQVAHDPDCGDVVRLGLSAIVRPSSIRQSTKGIFTAGLKKS 151
Cdd:pfam09139 233 MSPIARLNLLRLLPKLLRQKLYFQYQRKRHVRrDGEIFLRAIAYDDLLREVVQKAIRKIVRWSSTRQSIKGILTAGLTKS 312

                         170
                  ....*....|
gi 1007892835 152 VIYSSLKLHK 161
Cdd:pfam09139 313 VRYATEKRKK 322
 
Name Accession Description Interval E-value
Tam41_Mmp37 pfam09139
Phosphatidate cytidylyltransferase, mitochondrial; Tam41 also known as MMp37 is a ...
 1-161 6.23e-68

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: 209.30  E-value: 6.23e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007892835   1 MLPESFSEEDLFIEIAGLSYSGDFRMVVGEDKTKVLNIVKPNIAHFRELYGSILQENPQVVYK-----SQQGW---LEID 72
Cdd:pfam09139 153 LLPEKFTEEELYETIAGLSYMGDFRMLFGENPNKVNNIVSGQLHHFRKLYAPLLGILPNVDFLkdpfhSFIHWgvtLEQD 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007892835  73 KSPEGQFTQLMTLPKTLQQQINHIMDPPGKNR-DVEETLFQVAHDPDCGDVVRLGLSAIVRPSSIRQSTKGIFTAGLKKS 151
Cdd:pfam09139 233 MSPIARLNLLRLLPKLLRQKLYFQYQRKRHVRrDGEIFLRAIAYDDLLREVVQKAIRKIVRWSSTRQSIKGILTAGLTKS 312

                         170
                  ....*....|
gi 1007892835 152 VIYSSLKLHK 161
Cdd:pfam09139 313 VRYATEKRKK 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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