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Conserved domains on  [gi|20270367|ref|NP_620162|]
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phosphatidate cytidylyltransferase, mitochondrial isoform b precursor [Homo sapiens]

Protein Classification

phosphatidate cytidylyltransferase( domain architecture ID 10557553)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Tam41_Mmp37 pfam09139
Phosphatidate cytidylyltransferase, mitochondrial; Tam41 also known as MMp37 is a ...
 13-303 1.35e-141

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: 402.29  E-value: 1.35e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20270367    13 FRKILSHFPEELSLAFVYGSGVYRQAGPSSDQKNAMLDFVFTVDDPVAWHSKNLKKNWSHYSFLKVLGPKIITSIQNNYG 92
Cdd:pfam09139   1 LRRILRFFPAPIRYAFAYGSGVFPQEGYAQPGSKPMIDFIFAVDDPQHWHSLNLKQNPHHYSFLAYLGSYAISLVQDYFG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20270367    93 AGVYYNSLIMCNGRLIKYGVISTNVLIEDLLNWNNLYIAGRLQKPVKIISvnEDVTLRSALDRNLKSAVTAAFLMLPESF 172
Cdd:pfam09139  81 AGVYFNPYVPVNGMLIKYGVVSTDDLCDDLLDWDTLYLAGRLQKPVKILR--DDPRLRLANQVNLKSALRAALLLLPEKF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20270367   173 SEEDLFIEIAGLSYSGDFRMVVGEDKTKVLNIVKPNIAHFRELYGSILQENPQVVYK-----SQQGW---LEIDKSPEGQ 244
Cdd:pfam09139 159 TEEELYETIAGLSYMGDFRMLFGENPNKVNNIVSGQLHHFRKLYAPLLGILPNVDFLkdpfhSFIHWgvtLEQDMSPIAR 238

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 20270367   245 FTQLMTLPKTLQQQINHIMDPPGKNR-DVEETLFQVAHDPDCGDVVRLGLKKSVIYSSLK 303
Cdd:pfam09139 239 LNLLRLLPKLLRQKLYFQYQRKRHVRrDGEIFLRAIAYDDLLREVVQKAIRKIVRWSSTR 298
 
Name Accession Description Interval E-value
Tam41_Mmp37 pfam09139
Phosphatidate cytidylyltransferase, mitochondrial; Tam41 also known as MMp37 is a ...
 13-303 1.35e-141

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: 402.29  E-value: 1.35e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20270367    13 FRKILSHFPEELSLAFVYGSGVYRQAGPSSDQKNAMLDFVFTVDDPVAWHSKNLKKNWSHYSFLKVLGPKIITSIQNNYG 92
Cdd:pfam09139   1 LRRILRFFPAPIRYAFAYGSGVFPQEGYAQPGSKPMIDFIFAVDDPQHWHSLNLKQNPHHYSFLAYLGSYAISLVQDYFG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20270367    93 AGVYYNSLIMCNGRLIKYGVISTNVLIEDLLNWNNLYIAGRLQKPVKIISvnEDVTLRSALDRNLKSAVTAAFLMLPESF 172
Cdd:pfam09139  81 AGVYFNPYVPVNGMLIKYGVVSTDDLCDDLLDWDTLYLAGRLQKPVKILR--DDPRLRLANQVNLKSALRAALLLLPEKF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20270367   173 SEEDLFIEIAGLSYSGDFRMVVGEDKTKVLNIVKPNIAHFRELYGSILQENPQVVYK-----SQQGW---LEIDKSPEGQ 244
Cdd:pfam09139 159 TEEELYETIAGLSYMGDFRMLFGENPNKVNNIVSGQLHHFRKLYAPLLGILPNVDFLkdpfhSFIHWgvtLEQDMSPIAR 238

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 20270367   245 FTQLMTLPKTLQQQINHIMDPPGKNR-DVEETLFQVAHDPDCGDVVRLGLKKSVIYSSLK 303
Cdd:pfam09139 239 LNLLRLLPKLLRQKLYFQYQRKRHVRrDGEIFLRAIAYDDLLREVVQKAIRKIVRWSSTR 298
 
Name Accession Description Interval E-value
Tam41_Mmp37 pfam09139
Phosphatidate cytidylyltransferase, mitochondrial; Tam41 also known as MMp37 is a ...
 13-303 1.35e-141

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: 402.29  E-value: 1.35e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20270367    13 FRKILSHFPEELSLAFVYGSGVYRQAGPSSDQKNAMLDFVFTVDDPVAWHSKNLKKNWSHYSFLKVLGPKIITSIQNNYG 92
Cdd:pfam09139   1 LRRILRFFPAPIRYAFAYGSGVFPQEGYAQPGSKPMIDFIFAVDDPQHWHSLNLKQNPHHYSFLAYLGSYAISLVQDYFG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20270367    93 AGVYYNSLIMCNGRLIKYGVISTNVLIEDLLNWNNLYIAGRLQKPVKIISvnEDVTLRSALDRNLKSAVTAAFLMLPESF 172
Cdd:pfam09139  81 AGVYFNPYVPVNGMLIKYGVVSTDDLCDDLLDWDTLYLAGRLQKPVKILR--DDPRLRLANQVNLKSALRAALLLLPEKF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20270367   173 SEEDLFIEIAGLSYSGDFRMVVGEDKTKVLNIVKPNIAHFRELYGSILQENPQVVYK-----SQQGW---LEIDKSPEGQ 244
Cdd:pfam09139 159 TEEELYETIAGLSYMGDFRMLFGENPNKVNNIVSGQLHHFRKLYAPLLGILPNVDFLkdpfhSFIHWgvtLEQDMSPIAR 238

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 20270367   245 FTQLMTLPKTLQQQINHIMDPPGKNR-DVEETLFQVAHDPDCGDVVRLGLKKSVIYSSLK 303
Cdd:pfam09139 239 LNLLRLLPKLLRQKLYFQYQRKRHVRrDGEIFLRAIAYDDLLREVVQKAIRKIVRWSSTR 298
 
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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