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Conserved domains on  [gi|1958782925|ref|XP_038968127|]
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phosphatidate phosphatase LPIN1 isoform X4 [Rattus norvegicus]

Protein Classification

phosphatidate phosphatase( domain architecture ID 11151321)

phosphatidate phosphatase is a magnesium-dependent enzyme which catalyzes the conversion of phosphatidic acid to diacylglycerol during triglyceride, phosphatidylcholine and phosphatidylethanolamine biosynthesis and therefore controls the metabolism of fatty acids at different levels

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LNS2 pfam08235
LNS2 (Lipin/Ned1/Smp2); This domain is found in Saccharomyces cerevisiae protein SMP2, ...
 708-933 5.06e-141

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: 419.99  E-value: 5.06e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782925 708 KTLRLTSEQLKSLKLKNGPNDVVFSVTTQYQGTCRCEGTIYLWNWDDKVIISDIDGTITRSDTLGHILPTLGKDWTHQGI 787
Cdd:pfam08235   1 KSLRLTSEQLKSLNLKPGANTITFSVTTQYQGTQRVEANIYLWKWDDKIVISDIDGTITKSDALGHILPMIGKDWTHPGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782925 788 AKLYHKVSQNGYKFLYCSARAIGMADMTRGYLHWVNERGTVLPQGPLLLSPSSLFSALHREVIEKKPEKFKVQCLTDIKN 867
Cdd:pfam08235  81 AKLYSKIKRNGYKILYLSARAIGQADLTREYLKNVTQDGYKLPDGPVLLSPDRLFSALHREVILRKPEVFKIACLRDIKS 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958782925 868 LFFPNTEPFYAAFGNRPADVYSYKQVGVSLNRIFTVNPKGELVQEHAKTNISSYVRLCEVVDHVFP 933
Cdd:pfam08235 161 LFPPDVNPFYAGFGNRITDVISYRAVGIPESRIFTINPKGELRHELLKTYKSSYLSLNELVDHMFP 226
Lipin_N pfam04571
lipin, N-terminal conserved region; Mutations in the lipin gene lead to fatty liver dystrophy ...
 50-156 6.29e-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: 210.47  E-value: 6.29e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782925  50 MNYVGQlagqVFVTVKELYKGLNPATLSGCIDIIVVRQPNGSLQCSPFHVRFGKMGVLRSREKVVDIEINGESVDLHMKL 129
Cdd:pfam04571   1 MNYVGK----LFGSVSELYNSINPATLSGAIDVIVVEQPDGTLACSPFHVRFGKLGVLRSREKVVDIEVNGEPVDLHMKL 76

                          90       100
                  ....*....|....*....|....*..
gi 1958782925 130 GDNGEAFFVQETDNDQEVIPMYLATSP 156
Cdd:pfam04571  77 GESGEAFFVFETEDDEEDVPDYLQTSP 103
Lipin_mid pfam16876
Lipin/Ned1/Smp2 multi-domain protein middle domain; This is a middle domain of lipins. Overall ...
 546-639 1.18e-43

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: 153.21  E-value: 1.18e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782925 546 IAISLCGGLS--DHREITKDAFLEQAVSYQQFADNPAIIDDPNLVVKIGNKYYNWTTAAPLLLAMQAFQKPLPKATVESI 623
Cdd:pfam16876   1 VELSLCGGLLqgQNEEISDEAFEEHKVTYEDFCKNPSILNDPNLVVRIGGKYYNWAVAAPILLSMQAFQKPLPDDAIEQL 80

                          90
                  ....*....|....*...
gi 1958782925 624 MRD--KMPKKGGRWWFSW 639
Cdd:pfam16876  81 IKEarKNPKKGRRSWFSW 98
 
Name Accession Description Interval E-value
LNS2 pfam08235
LNS2 (Lipin/Ned1/Smp2); This domain is found in Saccharomyces cerevisiae protein SMP2, ...
 708-933 5.06e-141

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: 419.99  E-value: 5.06e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782925 708 KTLRLTSEQLKSLKLKNGPNDVVFSVTTQYQGTCRCEGTIYLWNWDDKVIISDIDGTITRSDTLGHILPTLGKDWTHQGI 787
Cdd:pfam08235   1 KSLRLTSEQLKSLNLKPGANTITFSVTTQYQGTQRVEANIYLWKWDDKIVISDIDGTITKSDALGHILPMIGKDWTHPGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782925 788 AKLYHKVSQNGYKFLYCSARAIGMADMTRGYLHWVNERGTVLPQGPLLLSPSSLFSALHREVIEKKPEKFKVQCLTDIKN 867
Cdd:pfam08235  81 AKLYSKIKRNGYKILYLSARAIGQADLTREYLKNVTQDGYKLPDGPVLLSPDRLFSALHREVILRKPEVFKIACLRDIKS 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958782925 868 LFFPNTEPFYAAFGNRPADVYSYKQVGVSLNRIFTVNPKGELVQEHAKTNISSYVRLCEVVDHVFP 933
Cdd:pfam08235 161 LFPPDVNPFYAGFGNRITDVISYRAVGIPESRIFTINPKGELRHELLKTYKSSYLSLNELVDHMFP 226
LNS2 smart00775
This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal ...
 756-912 2.04e-77

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: 249.50  E-value: 2.04e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782925  756 VIISDIDGTITRSDTLGHILPTLGKDWTHQGIAKLYHKVSQNGYKFLYCSARAIGMADMTRGYLHWVNERGTVLPQGPLL 835
Cdd:smart00775   1 IVISDIDGTITKSDVLGHVVPIIGKDWTHPGVAKLYRDIQNNGYKILYLTARPIGQADRTRSYLSQIKQDGHNLPHGPVL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958782925  836 LSPSSLFSALHREVIEKKPEKFKVQCLTDIKNLFFPNTEPFYAAFGNRPADVYSYKQVGVSLNRIFTVNPKGELVQE 912
Cdd:smart00775  81 LSPDRLFAALHREVISKKPEVFKIACLRDIKNLFPPQGNPFYAGFGNRITDVISYSAVGIPPSRIFTINPKGEVHQE 157
Lipin_N pfam04571
lipin, N-terminal conserved region; Mutations in the lipin gene lead to fatty liver dystrophy ...
 50-156 6.29e-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: 210.47  E-value: 6.29e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782925  50 MNYVGQlagqVFVTVKELYKGLNPATLSGCIDIIVVRQPNGSLQCSPFHVRFGKMGVLRSREKVVDIEINGESVDLHMKL 129
Cdd:pfam04571   1 MNYVGK----LFGSVSELYNSINPATLSGAIDVIVVEQPDGTLACSPFHVRFGKLGVLRSREKVVDIEVNGEPVDLHMKL 76

                          90       100
                  ....*....|....*....|....*..
gi 1958782925 130 GDNGEAFFVQETDNDQEVIPMYLATSP 156
Cdd:pfam04571  77 GESGEAFFVFETEDDEEDVPDYLQTSP 103
Lipin_mid pfam16876
Lipin/Ned1/Smp2 multi-domain protein middle domain; This is a middle domain of lipins. Overall ...
 546-639 1.18e-43

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: 153.21  E-value: 1.18e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782925 546 IAISLCGGLS--DHREITKDAFLEQAVSYQQFADNPAIIDDPNLVVKIGNKYYNWTTAAPLLLAMQAFQKPLPKATVESI 623
Cdd:pfam16876   1 VELSLCGGLLqgQNEEISDEAFEEHKVTYEDFCKNPSILNDPNLVVRIGGKYYNWAVAAPILLSMQAFQKPLPDDAIEQL 80

                          90
                  ....*....|....*...
gi 1958782925 624 MRD--KMPKKGGRWWFSW 639
Cdd:pfam16876  81 IKEarKNPKKGRRSWFSW 98
 
Name Accession Description Interval E-value
LNS2 pfam08235
LNS2 (Lipin/Ned1/Smp2); This domain is found in Saccharomyces cerevisiae protein SMP2, ...
 708-933 5.06e-141

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: 419.99  E-value: 5.06e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782925 708 KTLRLTSEQLKSLKLKNGPNDVVFSVTTQYQGTCRCEGTIYLWNWDDKVIISDIDGTITRSDTLGHILPTLGKDWTHQGI 787
Cdd:pfam08235   1 KSLRLTSEQLKSLNLKPGANTITFSVTTQYQGTQRVEANIYLWKWDDKIVISDIDGTITKSDALGHILPMIGKDWTHPGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782925 788 AKLYHKVSQNGYKFLYCSARAIGMADMTRGYLHWVNERGTVLPQGPLLLSPSSLFSALHREVIEKKPEKFKVQCLTDIKN 867
Cdd:pfam08235  81 AKLYSKIKRNGYKILYLSARAIGQADLTREYLKNVTQDGYKLPDGPVLLSPDRLFSALHREVILRKPEVFKIACLRDIKS 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958782925 868 LFFPNTEPFYAAFGNRPADVYSYKQVGVSLNRIFTVNPKGELVQEHAKTNISSYVRLCEVVDHVFP 933
Cdd:pfam08235 161 LFPPDVNPFYAGFGNRITDVISYRAVGIPESRIFTINPKGELRHELLKTYKSSYLSLNELVDHMFP 226
LNS2 smart00775
This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal ...
 756-912 2.04e-77

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: 249.50  E-value: 2.04e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782925  756 VIISDIDGTITRSDTLGHILPTLGKDWTHQGIAKLYHKVSQNGYKFLYCSARAIGMADMTRGYLHWVNERGTVLPQGPLL 835
Cdd:smart00775   1 IVISDIDGTITKSDVLGHVVPIIGKDWTHPGVAKLYRDIQNNGYKILYLTARPIGQADRTRSYLSQIKQDGHNLPHGPVL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958782925  836 LSPSSLFSALHREVIEKKPEKFKVQCLTDIKNLFFPNTEPFYAAFGNRPADVYSYKQVGVSLNRIFTVNPKGELVQE 912
Cdd:smart00775  81 LSPDRLFAALHREVISKKPEVFKIACLRDIKNLFPPQGNPFYAGFGNRITDVISYSAVGIPPSRIFTINPKGEVHQE 157
Lipin_N pfam04571
lipin, N-terminal conserved region; Mutations in the lipin gene lead to fatty liver dystrophy ...
 50-156 6.29e-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: 210.47  E-value: 6.29e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782925  50 MNYVGQlagqVFVTVKELYKGLNPATLSGCIDIIVVRQPNGSLQCSPFHVRFGKMGVLRSREKVVDIEINGESVDLHMKL 129
Cdd:pfam04571   1 MNYVGK----LFGSVSELYNSINPATLSGAIDVIVVEQPDGTLACSPFHVRFGKLGVLRSREKVVDIEVNGEPVDLHMKL 76

                          90       100
                  ....*....|....*....|....*..
gi 1958782925 130 GDNGEAFFVQETDNDQEVIPMYLATSP 156
Cdd:pfam04571  77 GESGEAFFVFETEDDEEDVPDYLQTSP 103
Lipin_mid pfam16876
Lipin/Ned1/Smp2 multi-domain protein middle domain; This is a middle domain of lipins. Overall ...
 546-639 1.18e-43

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: 153.21  E-value: 1.18e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782925 546 IAISLCGGLS--DHREITKDAFLEQAVSYQQFADNPAIIDDPNLVVKIGNKYYNWTTAAPLLLAMQAFQKPLPKATVESI 623
Cdd:pfam16876   1 VELSLCGGLLqgQNEEISDEAFEEHKVTYEDFCKNPSILNDPNLVVRIGGKYYNWAVAAPILLSMQAFQKPLPDDAIEQL 80

                          90
                  ....*....|....*...
gi 1958782925 624 MRD--KMPKKGGRWWFSW 639
Cdd:pfam16876  81 IKEarKNPKKGRRSWFSW 98
 
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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