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Conserved domains on  [gi|1958763181|ref|XP_038961449|]
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phosphatidate phosphatase LPIN3 isoform X1 [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, ...
 586-811 8.16e-159

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: 461.98  E-value: 8.16e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958763181 586 KSLRLSSNQIRCLNLNEGANDVVFSVTTQYQGTCRCKATIYLWNWDDKVVISDIDGTITKSDALGHILPQLGKDWTHQGI 665
Cdd:pfam08235   1 KSLRLTSEQLKSLNLKPGANTITFSVTTQYQGTQRVEANIYLWKWDDKIVISDIDGTITKSDALGHILPMIGKDWTHPGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958763181 666 TSLYHKIHLNGYKFLYCSARAIGMAHLTKGYLQWVSEHGCGLPKGPILLSPSSLFSALHREVIEKKPEVFKVACLSDIQQ 745
Cdd:pfam08235  81 AKLYSKIKRNGYKILYLSARAIGQADLTREYLKNVTQDGYKLPDGPVLLSPDRLFSALHREVILRKPEVFKIACLRDIKS 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958763181 746 LFLPQRQPFYAAFGNRPNDVFAYRQVGLPESRIFTVNPRGELIQELIKNHKSTYQRLGEVVELLFP 811
Cdd:pfam08235 161 LFPPDVNPFYAGFGNRITDVISYRAVGIPESRIFTINPKGELRHELLKTYKSSYLSLNELVDHMFP 226
Lipin_N pfam04571
lipin, N-terminal conserved region; Mutations in the lipin gene lead to fatty liver dystrophy ...
 1-107 1.35e-65

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: 213.55  E-value: 1.35e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958763181   1 MNYVGQlaetVFGTVKELYRGLNPATLSGGIDVLVVKQVDGSFRCSPFHVRFGKLGVLRSREKVVDIEINGEPVDLHMKL 80
Cdd:pfam04571   1 MNYVGK----LFGSVSELYNSINPATLSGAIDVIVVEQPDGTLACSPFHVRFGKLGVLRSREKVVDIEVNGEPVDLHMKL 76

                          90       100
                  ....*....|....*....|....*..
gi 1958763181  81 GDSGEAFFVQELDSDEEDVPPRLCTSP 107
Cdd:pfam04571  77 GESGEAFFVFETEDDEEDVPDYLQTSP 103
Lipin_mid pfam16876
Lipin/Ned1/Smp2 multi-domain protein middle domain; This is a middle domain of lipins. Overall ...
 432-525 5.41e-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: 153.98  E-value: 5.41e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958763181 432 IELSLCGGLA--DTRDISLEKFTQHMVSYEDLTKNPGLLDDPNLVVKINEKHYNWAVAAPMILSLQAFQKNLPESTVDKL 509
Cdd:pfam16876   1 VELSLCGGLLqgQNEEISDEAFEEHKVTYEDFCKNPSILNDPNLVVRIGGKYYNWAVAAPILLSMQAFQKPLPDDAIEQL 80

                          90
                  ....*....|....*...
gi 1958763181 510 QKE--KMPRKGGRWWFSW 525
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, ...
 586-811 8.16e-159

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: 461.98  E-value: 8.16e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958763181 586 KSLRLSSNQIRCLNLNEGANDVVFSVTTQYQGTCRCKATIYLWNWDDKVVISDIDGTITKSDALGHILPQLGKDWTHQGI 665
Cdd:pfam08235   1 KSLRLTSEQLKSLNLKPGANTITFSVTTQYQGTQRVEANIYLWKWDDKIVISDIDGTITKSDALGHILPMIGKDWTHPGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958763181 666 TSLYHKIHLNGYKFLYCSARAIGMAHLTKGYLQWVSEHGCGLPKGPILLSPSSLFSALHREVIEKKPEVFKVACLSDIQQ 745
Cdd:pfam08235  81 AKLYSKIKRNGYKILYLSARAIGQADLTREYLKNVTQDGYKLPDGPVLLSPDRLFSALHREVILRKPEVFKIACLRDIKS 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958763181 746 LFLPQRQPFYAAFGNRPNDVFAYRQVGLPESRIFTVNPRGELIQELIKNHKSTYQRLGEVVELLFP 811
Cdd:pfam08235 161 LFPPDVNPFYAGFGNRITDVISYRAVGIPESRIFTINPKGELRHELLKTYKSSYLSLNELVDHMFP 226
LNS2 smart00775
This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal ...
 634-790 7.58e-93

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: 288.40  E-value: 7.58e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958763181  634 VVISDIDGTITKSDALGHILPQLGKDWTHQGITSLYHKIHLNGYKFLYCSARAIGMAHLTKGYLQWVSEHGCGLPKGPIL 713
Cdd:smart00775   1 IVISDIDGTITKSDVLGHVVPIIGKDWTHPGVAKLYRDIQNNGYKILYLTARPIGQADRTRSYLSQIKQDGHNLPHGPVL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958763181  714 LSPSSLFSALHREVIEKKPEVFKVACLSDIQQLFLPQRQPFYAAFGNRPNDVFAYRQVGLPESRIFTVNPRGELIQE 790
Cdd:smart00775  81 LSPDRLFAALHREVISKKPEVFKIACLRDIKNLFPPQGNPFYAGFGNRITDVISYSAVGIPPSRIFTINPKGEVHQE 157
Lipin_N pfam04571
lipin, N-terminal conserved region; Mutations in the lipin gene lead to fatty liver dystrophy ...
 1-107 1.35e-65

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: 213.55  E-value: 1.35e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958763181   1 MNYVGQlaetVFGTVKELYRGLNPATLSGGIDVLVVKQVDGSFRCSPFHVRFGKLGVLRSREKVVDIEINGEPVDLHMKL 80
Cdd:pfam04571   1 MNYVGK----LFGSVSELYNSINPATLSGAIDVIVVEQPDGTLACSPFHVRFGKLGVLRSREKVVDIEVNGEPVDLHMKL 76

                          90       100
                  ....*....|....*....|....*..
gi 1958763181  81 GDSGEAFFVQELDSDEEDVPPRLCTSP 107
Cdd:pfam04571  77 GESGEAFFVFETEDDEEDVPDYLQTSP 103
Lipin_mid pfam16876
Lipin/Ned1/Smp2 multi-domain protein middle domain; This is a middle domain of lipins. Overall ...
 432-525 5.41e-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: 153.98  E-value: 5.41e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958763181 432 IELSLCGGLA--DTRDISLEKFTQHMVSYEDLTKNPGLLDDPNLVVKINEKHYNWAVAAPMILSLQAFQKNLPESTVDKL 509
Cdd:pfam16876   1 VELSLCGGLLqgQNEEISDEAFEEHKVTYEDFCKNPSILNDPNLVVRIGGKYYNWAVAAPILLSMQAFQKPLPDDAIEQL 80

                          90
                  ....*....|....*...
gi 1958763181 510 QKE--KMPRKGGRWWFSW 525
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, ...
 586-811 8.16e-159

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: 461.98  E-value: 8.16e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958763181 586 KSLRLSSNQIRCLNLNEGANDVVFSVTTQYQGTCRCKATIYLWNWDDKVVISDIDGTITKSDALGHILPQLGKDWTHQGI 665
Cdd:pfam08235   1 KSLRLTSEQLKSLNLKPGANTITFSVTTQYQGTQRVEANIYLWKWDDKIVISDIDGTITKSDALGHILPMIGKDWTHPGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958763181 666 TSLYHKIHLNGYKFLYCSARAIGMAHLTKGYLQWVSEHGCGLPKGPILLSPSSLFSALHREVIEKKPEVFKVACLSDIQQ 745
Cdd:pfam08235  81 AKLYSKIKRNGYKILYLSARAIGQADLTREYLKNVTQDGYKLPDGPVLLSPDRLFSALHREVILRKPEVFKIACLRDIKS 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958763181 746 LFLPQRQPFYAAFGNRPNDVFAYRQVGLPESRIFTVNPRGELIQELIKNHKSTYQRLGEVVELLFP 811
Cdd:pfam08235 161 LFPPDVNPFYAGFGNRITDVISYRAVGIPESRIFTINPKGELRHELLKTYKSSYLSLNELVDHMFP 226
LNS2 smart00775
This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal ...
 634-790 7.58e-93

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: 288.40  E-value: 7.58e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958763181  634 VVISDIDGTITKSDALGHILPQLGKDWTHQGITSLYHKIHLNGYKFLYCSARAIGMAHLTKGYLQWVSEHGCGLPKGPIL 713
Cdd:smart00775   1 IVISDIDGTITKSDVLGHVVPIIGKDWTHPGVAKLYRDIQNNGYKILYLTARPIGQADRTRSYLSQIKQDGHNLPHGPVL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958763181  714 LSPSSLFSALHREVIEKKPEVFKVACLSDIQQLFLPQRQPFYAAFGNRPNDVFAYRQVGLPESRIFTVNPRGELIQE 790
Cdd:smart00775  81 LSPDRLFAALHREVISKKPEVFKIACLRDIKNLFPPQGNPFYAGFGNRITDVISYSAVGIPPSRIFTINPKGEVHQE 157
Lipin_N pfam04571
lipin, N-terminal conserved region; Mutations in the lipin gene lead to fatty liver dystrophy ...
 1-107 1.35e-65

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: 213.55  E-value: 1.35e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958763181   1 MNYVGQlaetVFGTVKELYRGLNPATLSGGIDVLVVKQVDGSFRCSPFHVRFGKLGVLRSREKVVDIEINGEPVDLHMKL 80
Cdd:pfam04571   1 MNYVGK----LFGSVSELYNSINPATLSGAIDVIVVEQPDGTLACSPFHVRFGKLGVLRSREKVVDIEVNGEPVDLHMKL 76

                          90       100
                  ....*....|....*....|....*..
gi 1958763181  81 GDSGEAFFVQELDSDEEDVPPRLCTSP 107
Cdd:pfam04571  77 GESGEAFFVFETEDDEEDVPDYLQTSP 103
Lipin_mid pfam16876
Lipin/Ned1/Smp2 multi-domain protein middle domain; This is a middle domain of lipins. Overall ...
 432-525 5.41e-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: 153.98  E-value: 5.41e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958763181 432 IELSLCGGLA--DTRDISLEKFTQHMVSYEDLTKNPGLLDDPNLVVKINEKHYNWAVAAPMILSLQAFQKNLPESTVDKL 509
Cdd:pfam16876   1 VELSLCGGLLqgQNEEISDEAFEEHKVTYEDFCKNPSILNDPNLVVRIGGKYYNWAVAAPILLSMQAFQKPLPDDAIEQL 80

                          90
                  ....*....|....*...
gi 1958763181 510 QKE--KMPRKGGRWWFSW 525
Cdd:pfam16876  81 IKEarKNPKKGRRSWFSW 98
APP1_cat pfam09949
Phosphatidate phosphatase APP1, catalytic domain; This entry represents a conserved region ...
 635-752 2.13e-03

Phosphatidate phosphatase APP1, catalytic domain; This entry represents a conserved region found in Phosphatidate phosphatase APP1 from yeast, which contains the catalytic motif DXDX(T/V), present in other Mg+2-dependent phosphatases. This domain has a weak sequence similarity to the haloacid dehalogenase-like domain. APP1 catalyzes the dephosphorylation of phosphatidate to yield diacylglycerol and may play a role in vesicular trafficking through its phosphatidate phosphatase activity at cortical actin patches.


Pssm-ID: 462930  Cd Length: 153  Bit Score: 39.40  E-value: 2.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958763181 635 VISDIDGTITKSDALGhilPQLG----------KDWTHQGITSLYHKIH-LNGYKFLYCSARAIGMAHLTKGYLQwvsEH 703
Cdd:pfam09949   1 VISDIDDTIKVTGVTS---PLRAlfntffvnalTRVPIPGMPELYRALSaSPGNPFFYVSNSPWNLYPFLRDFLE---RH 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958763181 704 gcGLPKGPILL-----SPSSLFSALHREVIEkkpevFKVACLSDIQQLFlPQRQ 752
Cdd:pfam09949  75 --GYPPGSLLLrdygsTDTSLLRSGLTPSAE-----HKRASIERILRDF-PNRK 120
 
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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