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Conserved domains on  [gi|768018104|ref|XP_011527305|]
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phosphatidate phosphatase LPIN3 isoform X8 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Lipin_N pfam04571
lipin, N-terminal conserved region; Mutations in the lipin gene lead to fatty liver dystrophy ...
 1-107 1.48e-64

lipin, N-terminal conserved region; Mutations in the lipin gene lead to fatty liver dystrophy in mice. The protein has been shown to be phosphorylated by the TOR Ser/Thr protein kinases in response to insulin stimulation. The conserved region is found at the N-terminus of the member proteins.


:

Pssm-ID: 461356  Cd Length: 103  Bit Score: 209.70  E-value: 1.48e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018104    1 MNYVGQlaetVFGTVKELYRGLNPATLSGGIDVLVVKQVDGSFRCSPFHVRFGKLGVLRSREKVVDIELNGEPVDLHMKL 80
Cdd:pfam04571   1 MNYVGK----LFGSVSELYNSINPATLSGAIDVIVVEQPDGTLACSPFHVRFGKLGVLRSREKVVDIEVNGEPVDLHMKL 76

                          90       100
                  ....*....|....*....|....*..
gi 768018104   81 GDSGEAFFVQELESDDEHVPPGLCTSP 107
Cdd:pfam04571  77 GESGEAFFVFETEDDEEDVPDYLQTSP 103
LNS2 super family cl46352
LNS2 (Lipin/Ned1/Smp2); This domain is found in Saccharomyces cerevisiae protein SMP2, ...
 593-693 1.21e-58

LNS2 (Lipin/Ned1/Smp2); This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal lipin domain (Pfam: PF04571). SMP2 (also known as PAH1) is involved in plasmid maintenance and respiration, and has been identified as a Mg2+-dependent phosphatidate phosphatase (EC:3.1.3.4) that contains a haloacid dehalogenase (HAD)-like domain. Lipin proteins are involved in adipose tissue development and insulin resistance.


The actual alignment was detected with superfamily member pfam08235:

Pssm-ID: 480692  Cd Length: 226  Bit Score: 198.50  E-value: 1.21e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018104  593 KSLRLSSDQIRRLNLQEGANDVVFSVTTQYQGTCRCKATIYLWKWDDKVVISDIDGTITKSDALGHILPQLGKDWTHQGI 672
Cdd:pfam08235   1 KSLRLTSEQLKSLNLKPGANTITFSVTTQYQGTQRVEANIYLWKWDDKIVISDIDGTITKSDALGHILPMIGKDWTHPGV 80

                          90       100
                  ....*....|....*....|.
gi 768018104  673 TSLYHKIQLIRAHLLACSRRG 693
Cdd:pfam08235  81 AKLYSKIKRNGYKILYLSARA 101
Lipin_mid pfam16876
Lipin/Ned1/Smp2 multi-domain protein middle domain; This is a middle domain of lipins. Overall ...
 439-532 9.68e-44

Lipin/Ned1/Smp2 multi-domain protein middle domain; This is a middle domain of lipins. Overall the enzyme acts as a magnesium-dependent phosphatidate phosphatase enzyme that catalyzes the conversion of phosphatidic acid to diacylglycerol during triglyceride, phosphatidylcholine and phosphatidylethanolamine biosynthesis. EC:5.2.1.8.


:

Pssm-ID: 465292  Cd Length: 98  Bit Score: 152.83  E-value: 9.68e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018104  439 IALSLCGGLA--DSRDISLEKFNQHSVSYQDLTKNPGLLDDPNLVVKINGKHYNWAVAAPMILSLQAFQKNLPKSTMDKL 516
Cdd:pfam16876   1 VELSLCGGLLqgQNEEISDEAFEEHKVTYEDFCKNPSILNDPNLVVRIGGKYYNWAVAAPILLSMQAFQKPLPDDAIEQL 80

                          90
                  ....*....|....*...
gi 768018104  517 --EREKMPRKGGRWWFSW 532
Cdd:pfam16876  81 ikEARKNPKKGRRSWFSW 98
 
Name Accession Description Interval E-value
Lipin_N pfam04571
lipin, N-terminal conserved region; Mutations in the lipin gene lead to fatty liver dystrophy ...
 1-107 1.48e-64

lipin, N-terminal conserved region; Mutations in the lipin gene lead to fatty liver dystrophy in mice. The protein has been shown to be phosphorylated by the TOR Ser/Thr protein kinases in response to insulin stimulation. The conserved region is found at the N-terminus of the member proteins.


Pssm-ID: 461356  Cd Length: 103  Bit Score: 209.70  E-value: 1.48e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018104    1 MNYVGQlaetVFGTVKELYRGLNPATLSGGIDVLVVKQVDGSFRCSPFHVRFGKLGVLRSREKVVDIELNGEPVDLHMKL 80
Cdd:pfam04571   1 MNYVGK----LFGSVSELYNSINPATLSGAIDVIVVEQPDGTLACSPFHVRFGKLGVLRSREKVVDIEVNGEPVDLHMKL 76

                          90       100
                  ....*....|....*....|....*..
gi 768018104   81 GDSGEAFFVQELESDDEHVPPGLCTSP 107
Cdd:pfam04571  77 GESGEAFFVFETEDDEEDVPDYLQTSP 103
LNS2 pfam08235
LNS2 (Lipin/Ned1/Smp2); This domain is found in Saccharomyces cerevisiae protein SMP2, ...
 593-693 1.21e-58

LNS2 (Lipin/Ned1/Smp2); This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal lipin domain (Pfam: PF04571). SMP2 (also known as PAH1) is involved in plasmid maintenance and respiration, and has been identified as a Mg2+-dependent phosphatidate phosphatase (EC:3.1.3.4) that contains a haloacid dehalogenase (HAD)-like domain. Lipin proteins are involved in adipose tissue development and insulin resistance.


Pssm-ID: 462403  Cd Length: 226  Bit Score: 198.50  E-value: 1.21e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018104  593 KSLRLSSDQIRRLNLQEGANDVVFSVTTQYQGTCRCKATIYLWKWDDKVVISDIDGTITKSDALGHILPQLGKDWTHQGI 672
Cdd:pfam08235   1 KSLRLTSEQLKSLNLKPGANTITFSVTTQYQGTQRVEANIYLWKWDDKIVISDIDGTITKSDALGHILPMIGKDWTHPGV 80

                          90       100
                  ....*....|....*....|.
gi 768018104  673 TSLYHKIQLIRAHLLACSRRG 693
Cdd:pfam08235  81 AKLYSKIKRNGYKILYLSARA 101
Lipin_mid pfam16876
Lipin/Ned1/Smp2 multi-domain protein middle domain; This is a middle domain of lipins. Overall ...
 439-532 9.68e-44

Lipin/Ned1/Smp2 multi-domain protein middle domain; This is a middle domain of lipins. Overall the enzyme acts as a magnesium-dependent phosphatidate phosphatase enzyme that catalyzes the conversion of phosphatidic acid to diacylglycerol during triglyceride, phosphatidylcholine and phosphatidylethanolamine biosynthesis. EC:5.2.1.8.


Pssm-ID: 465292  Cd Length: 98  Bit Score: 152.83  E-value: 9.68e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018104  439 IALSLCGGLA--DSRDISLEKFNQHSVSYQDLTKNPGLLDDPNLVVKINGKHYNWAVAAPMILSLQAFQKNLPKSTMDKL 516
Cdd:pfam16876   1 VELSLCGGLLqgQNEEISDEAFEEHKVTYEDFCKNPSILNDPNLVVRIGGKYYNWAVAAPILLSMQAFQKPLPDDAIEQL 80

                          90
                  ....*....|....*...
gi 768018104  517 --EREKMPRKGGRWWFSW 532
Cdd:pfam16876  81 ikEARKNPKKGRRSWFSW 98
LNS2 smart00775
This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal ...
 641-680 4.22e-20

This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal lipin domain and phosphatidylinositol transfer proteins; SMP2 is involved in plasmid maintenance and respiration. Lipin proteins are involved in adipose tissue development and insulin resistance.


Pssm-ID: 197870  Cd Length: 157  Bit Score: 87.71  E-value: 4.22e-20
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 768018104   641 VVISDIDGTITKSDALGHILPQLGKDWTHQGITSLYHKIQ 680
Cdd:smart00775   1 IVISDIDGTITKSDVLGHVVPIIGKDWTHPGVAKLYRDIQ 40
 
Name Accession Description Interval E-value
Lipin_N pfam04571
lipin, N-terminal conserved region; Mutations in the lipin gene lead to fatty liver dystrophy ...
 1-107 1.48e-64

lipin, N-terminal conserved region; Mutations in the lipin gene lead to fatty liver dystrophy in mice. The protein has been shown to be phosphorylated by the TOR Ser/Thr protein kinases in response to insulin stimulation. The conserved region is found at the N-terminus of the member proteins.


Pssm-ID: 461356  Cd Length: 103  Bit Score: 209.70  E-value: 1.48e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018104    1 MNYVGQlaetVFGTVKELYRGLNPATLSGGIDVLVVKQVDGSFRCSPFHVRFGKLGVLRSREKVVDIELNGEPVDLHMKL 80
Cdd:pfam04571   1 MNYVGK----LFGSVSELYNSINPATLSGAIDVIVVEQPDGTLACSPFHVRFGKLGVLRSREKVVDIEVNGEPVDLHMKL 76

                          90       100
                  ....*....|....*....|....*..
gi 768018104   81 GDSGEAFFVQELESDDEHVPPGLCTSP 107
Cdd:pfam04571  77 GESGEAFFVFETEDDEEDVPDYLQTSP 103
LNS2 pfam08235
LNS2 (Lipin/Ned1/Smp2); This domain is found in Saccharomyces cerevisiae protein SMP2, ...
 593-693 1.21e-58

LNS2 (Lipin/Ned1/Smp2); This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal lipin domain (Pfam: PF04571). SMP2 (also known as PAH1) is involved in plasmid maintenance and respiration, and has been identified as a Mg2+-dependent phosphatidate phosphatase (EC:3.1.3.4) that contains a haloacid dehalogenase (HAD)-like domain. Lipin proteins are involved in adipose tissue development and insulin resistance.


Pssm-ID: 462403  Cd Length: 226  Bit Score: 198.50  E-value: 1.21e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018104  593 KSLRLSSDQIRRLNLQEGANDVVFSVTTQYQGTCRCKATIYLWKWDDKVVISDIDGTITKSDALGHILPQLGKDWTHQGI 672
Cdd:pfam08235   1 KSLRLTSEQLKSLNLKPGANTITFSVTTQYQGTQRVEANIYLWKWDDKIVISDIDGTITKSDALGHILPMIGKDWTHPGV 80

                          90       100
                  ....*....|....*....|.
gi 768018104  673 TSLYHKIQLIRAHLLACSRRG 693
Cdd:pfam08235  81 AKLYSKIKRNGYKILYLSARA 101
Lipin_mid pfam16876
Lipin/Ned1/Smp2 multi-domain protein middle domain; This is a middle domain of lipins. Overall ...
 439-532 9.68e-44

Lipin/Ned1/Smp2 multi-domain protein middle domain; This is a middle domain of lipins. Overall the enzyme acts as a magnesium-dependent phosphatidate phosphatase enzyme that catalyzes the conversion of phosphatidic acid to diacylglycerol during triglyceride, phosphatidylcholine and phosphatidylethanolamine biosynthesis. EC:5.2.1.8.


Pssm-ID: 465292  Cd Length: 98  Bit Score: 152.83  E-value: 9.68e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018104  439 IALSLCGGLA--DSRDISLEKFNQHSVSYQDLTKNPGLLDDPNLVVKINGKHYNWAVAAPMILSLQAFQKNLPKSTMDKL 516
Cdd:pfam16876   1 VELSLCGGLLqgQNEEISDEAFEEHKVTYEDFCKNPSILNDPNLVVRIGGKYYNWAVAAPILLSMQAFQKPLPDDAIEQL 80

                          90
                  ....*....|....*...
gi 768018104  517 --EREKMPRKGGRWWFSW 532
Cdd:pfam16876  81 ikEARKNPKKGRRSWFSW 98
LNS2 smart00775
This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal ...
 641-680 4.22e-20

This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal lipin domain and phosphatidylinositol transfer proteins; SMP2 is involved in plasmid maintenance and respiration. Lipin proteins are involved in adipose tissue development and insulin resistance.


Pssm-ID: 197870  Cd Length: 157  Bit Score: 87.71  E-value: 4.22e-20
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 768018104   641 VVISDIDGTITKSDALGHILPQLGKDWTHQGITSLYHKIQ 680
Cdd:smart00775   1 IVISDIDGTITKSDVLGHVVPIIGKDWTHPGVAKLYRDIQ 40
 
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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