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Conserved domains on  [gi|387593287|gb|EIJ88311|]
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hypothetical protein NEQG_01755 [Nematocida parisii ERTm3]

Protein Classification

lipin family protein( domain architecture ID 11894216)

lipin family protein acts as a phosphatidate phosphatase that catalyzes the conversion of phosphatidic acid to diacylglycerol

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, ...
 241-460 1.03e-106

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: 315.99  E-value: 1.03e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387593287  241 REVYLPDTYIEKMHLVPGPNKTVYRLS----GTPIfLTCNIYLWNETDKIIISDIDGTVTKSDIVGYIYGAMGKDWTHLG 316
Cdd:pfam08235   1 KSLRLTSEQLKSLNLKPGANTITFSVTtqyqGTQR-VEANIYLWKWDDKIVISDIDGTITKSDALGHILPMIGKDWTHPG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387593287  317 IAALYNKIVENGYKIVYLSSRPIGHIGFTKAYLERVEQEEQNLPAGPVILFPGRLLSAIYREMV-QGPEEFKISVISEIK 395
Cdd:pfam08235  80 VAKLYSKIKRNGYKILYLSARAIGQADLTREYLKNVTQDGYKLPDGPVLLSPDRLFSALHREVIlRKPEVFKIACLRDIK 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 387593287  396 GLMSQGR--IYAGFGNKESDRIAYEVCEIDPGRIFIVNTMSEISTGRKGIVKLTHCSLYDIVDGVFP 460
Cdd:pfam08235 160 SLFPPDVnpFYAGFGNRITDVISYRAVGIPESRIFTINPKGELRHELLKTYKSSYLSLNELVDHMFP 226
Lipin_N super family cl04599
lipin, N-terminal conserved region; Mutations in the lipin gene lead to fatty liver dystrophy ...
 1-84 4.82e-15

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.


The actual alignment was detected with superfamily member pfam04571:

Pssm-ID: 461356  Cd Length: 103  Bit Score: 70.65  E-value: 4.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387593287    1 MNFVGRVFNSVTDLYKDMHPGQISGANDIIVCKTAKG-FHSTGFHARFGNVQSFKTSREVI-LTVNDRVVNVEARLDREG 78
Cdd:pfam04571   1 MNYVGKLFGSVSELYNSINPATLSGAIDVIVVEQPDGtLACSPFHVRFGKLGVLRSREKVVdIEVNGEPVDLHMKLGESG 80


                  ....*.
gi 387593287   79 NVFFSF 84
Cdd:pfam04571  81 EAFFVF 86
 
Name Accession Description Interval E-value
LNS2 pfam08235
LNS2 (Lipin/Ned1/Smp2); This domain is found in Saccharomyces cerevisiae protein SMP2, ...
 241-460 1.03e-106

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: 315.99  E-value: 1.03e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387593287  241 REVYLPDTYIEKMHLVPGPNKTVYRLS----GTPIfLTCNIYLWNETDKIIISDIDGTVTKSDIVGYIYGAMGKDWTHLG 316
Cdd:pfam08235   1 KSLRLTSEQLKSLNLKPGANTITFSVTtqyqGTQR-VEANIYLWKWDDKIVISDIDGTITKSDALGHILPMIGKDWTHPG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387593287  317 IAALYNKIVENGYKIVYLSSRPIGHIGFTKAYLERVEQEEQNLPAGPVILFPGRLLSAIYREMV-QGPEEFKISVISEIK 395
Cdd:pfam08235  80 VAKLYSKIKRNGYKILYLSARAIGQADLTREYLKNVTQDGYKLPDGPVLLSPDRLFSALHREVIlRKPEVFKIACLRDIK 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 387593287  396 GLMSQGR--IYAGFGNKESDRIAYEVCEIDPGRIFIVNTMSEISTGRKGIVKLTHCSLYDIVDGVFP 460
Cdd:pfam08235 160 SLFPPDVnpFYAGFGNRITDVISYRAVGIPESRIFTINPKGELRHELLKTYKSSYLSLNELVDHMFP 226
LNS2 smart00775
This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal ...
 286-436 1.58e-56

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: 184.40  E-value: 1.58e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387593287   286 IIISDIDGTVTKSDIVGYIYGAMGKDWTHLGIAALYNKIVENGYKIVYLSSRPIGHIGFTKAYLERVEQEEQNLPAGPVI 365
Cdd:smart00775   1 IVISDIDGTITKSDVLGHVVPIIGKDWTHPGVAKLYRDIQNNGYKILYLTARPIGQADRTRSYLSQIKQDGHNLPHGPVL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 387593287   366 LFPGRLLSAIYRE-MVQGPEEFKISVISEIKGLMSQGR--IYAGFGNKESDRIAYEVCEIDPGRIFIVNTMSEI 436
Cdd:smart00775  81 LSPDRLFAALHREvISKKPEVFKIACLRDIKNLFPPQGnpFYAGFGNRITDVISYSAVGIPPSRIFTINPKGEV 154
Lipin_N pfam04571
lipin, N-terminal conserved region; Mutations in the lipin gene lead to fatty liver dystrophy ...
 1-84 4.82e-15

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: 70.65  E-value: 4.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387593287    1 MNFVGRVFNSVTDLYKDMHPGQISGANDIIVCKTAKG-FHSTGFHARFGNVQSFKTSREVI-LTVNDRVVNVEARLDREG 78
Cdd:pfam04571   1 MNYVGKLFGSVSELYNSINPATLSGAIDVIVVEQPDGtLACSPFHVRFGKLGVLRSREKVVdIEVNGEPVDLHMKLGESG 80


                  ....*.
gi 387593287   79 NVFFSF 84
Cdd:pfam04571  81 EAFFVF 86
HAD_PNKP-C cd07502
C-terminal phosphatase domain of T4 polynucleotide kinase/phosphatase (PNKP) and related ...
 285-351 1.87e-03

C-terminal phosphatase domain of T4 polynucleotide kinase/phosphatase (PNKP) and related phosphatases; This family includes the C-terminal domain of the bifunctional enzyme T4 polynucleotide kinase/phosphatase, PNKP. The PNKP phosphatase domain can catalyze the hydrolytic removal of the 3'-phosphoryl of DNA, RNA and deoxynucleoside 3'-monophosphates. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319805  Cd Length: 145  Bit Score: 38.66  E-value: 1.87e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 387593287 285 KIIISDIDGTVTKSDIVGYIYGAMGKDWTHLG-----------IAALYNKIVENGYKIVYLSSRPIGHIGFTKAYLER 351
Cdd:cd07502    2 KAVIFDLDGTLADTNGRQPYLERRPRDWDAFFeaadhdppnapVIELVKESALTGYEIVYLSGRPERYRRDTLRWLAK 79
 
Name Accession Description Interval E-value
LNS2 pfam08235
LNS2 (Lipin/Ned1/Smp2); This domain is found in Saccharomyces cerevisiae protein SMP2, ...
 241-460 1.03e-106

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: 315.99  E-value: 1.03e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387593287  241 REVYLPDTYIEKMHLVPGPNKTVYRLS----GTPIfLTCNIYLWNETDKIIISDIDGTVTKSDIVGYIYGAMGKDWTHLG 316
Cdd:pfam08235   1 KSLRLTSEQLKSLNLKPGANTITFSVTtqyqGTQR-VEANIYLWKWDDKIVISDIDGTITKSDALGHILPMIGKDWTHPG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387593287  317 IAALYNKIVENGYKIVYLSSRPIGHIGFTKAYLERVEQEEQNLPAGPVILFPGRLLSAIYREMV-QGPEEFKISVISEIK 395
Cdd:pfam08235  80 VAKLYSKIKRNGYKILYLSARAIGQADLTREYLKNVTQDGYKLPDGPVLLSPDRLFSALHREVIlRKPEVFKIACLRDIK 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 387593287  396 GLMSQGR--IYAGFGNKESDRIAYEVCEIDPGRIFIVNTMSEISTGRKGIVKLTHCSLYDIVDGVFP 460
Cdd:pfam08235 160 SLFPPDVnpFYAGFGNRITDVISYRAVGIPESRIFTINPKGELRHELLKTYKSSYLSLNELVDHMFP 226
LNS2 smart00775
This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal ...
 286-436 1.58e-56

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: 184.40  E-value: 1.58e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387593287   286 IIISDIDGTVTKSDIVGYIYGAMGKDWTHLGIAALYNKIVENGYKIVYLSSRPIGHIGFTKAYLERVEQEEQNLPAGPVI 365
Cdd:smart00775   1 IVISDIDGTITKSDVLGHVVPIIGKDWTHPGVAKLYRDIQNNGYKILYLTARPIGQADRTRSYLSQIKQDGHNLPHGPVL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 387593287   366 LFPGRLLSAIYRE-MVQGPEEFKISVISEIKGLMSQGR--IYAGFGNKESDRIAYEVCEIDPGRIFIVNTMSEI 436
Cdd:smart00775  81 LSPDRLFAALHREvISKKPEVFKIACLRDIKNLFPPQGnpFYAGFGNRITDVISYSAVGIPPSRIFTINPKGEV 154
Lipin_N pfam04571
lipin, N-terminal conserved region; Mutations in the lipin gene lead to fatty liver dystrophy ...
 1-84 4.82e-15

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: 70.65  E-value: 4.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387593287    1 MNFVGRVFNSVTDLYKDMHPGQISGANDIIVCKTAKG-FHSTGFHARFGNVQSFKTSREVI-LTVNDRVVNVEARLDREG 78
Cdd:pfam04571   1 MNYVGKLFGSVSELYNSINPATLSGAIDVIVVEQPDGtLACSPFHVRFGKLGVLRSREKVVdIEVNGEPVDLHMKLGESG 80


                  ....*.
gi 387593287   79 NVFFSF 84
Cdd:pfam04571  81 EAFFVF 86
Acid_phosphat_B pfam03767
HAD superfamily, subfamily IIIB (Acid phosphatase); This family proteins includes acid ...
 285-351 3.94e-04

HAD superfamily, subfamily IIIB (Acid phosphatase); This family proteins includes acid phosphatases and a number of vegetative storage proteins.


Pssm-ID: 397712  Cd Length: 213  Bit Score: 41.58  E-value: 3.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387593287  285 KIIISDIDGTVTkSDIVGYIYGAMGKD---------WTHLGIAA-------LYNKIVENGYKIVYLSSRPIGHIGFTKAY 348
Cdd:pfam03767  61 DAVVFDIDETVL-SNSPYYAYHGYGGEpfdpekfdeWVNKGEAPalpgaleLYNYLVELGVKIFFVSGRSEDLRAATVEN 139


                  ...
gi 387593287  349 LER 351
Cdd:pfam03767 140 LKK 142
HAD_PNKP-C cd07502
C-terminal phosphatase domain of T4 polynucleotide kinase/phosphatase (PNKP) and related ...
 285-351 1.87e-03

C-terminal phosphatase domain of T4 polynucleotide kinase/phosphatase (PNKP) and related phosphatases; This family includes the C-terminal domain of the bifunctional enzyme T4 polynucleotide kinase/phosphatase, PNKP. The PNKP phosphatase domain can catalyze the hydrolytic removal of the 3'-phosphoryl of DNA, RNA and deoxynucleoside 3'-monophosphates. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319805  Cd Length: 145  Bit Score: 38.66  E-value: 1.87e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 387593287 285 KIIISDIDGTVTKSDIVGYIYGAMGKDWTHLG-----------IAALYNKIVENGYKIVYLSSRPIGHIGFTKAYLER 351
Cdd:cd07502    2 KAVIFDLDGTLADTNGRQPYLERRPRDWDAFFeaadhdppnapVIELVKESALTGYEIVYLSGRPERYRRDTLRWLAK 79
 
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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