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Conserved domains on  [gi|19115727|ref|NP_594815|]
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lipin, phosphatidate phosphatase Ned1 [Schizosaccharomyces pombe]

Protein Classification

Lipin_N and LNS2 domain-containing protein( domain architecture ID 10518962)

Lipin_N and LNS2 domain-containing protein

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, ...
 334-560 9.14e-154

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: 442.72  E-value: 9.14e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115727   334 KTLRLTSDQLRSLNLKPGKNELSFGVNG---GKAICTANLFFWKHNDPVVISDIDGTITKSDALGHMFTLIGKDWTHAGV 410
Cdd:pfam08235   1 KSLRLTSEQLKSLNLKPGANTITFSVTTqyqGTQRVEANIYLWKWDDKIVISDIDGTITKSDALGHILPMIGKDWTHPGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115727   411 AKLYTDITNNGYKIMYLTSRSVGQADSTRHYLRNIEQNGYSLPDGPVILSPDRTMAALHREVILRKPEVFKMACLRDLCN 490
Cdd:pfam08235  81 AKLYSKIKRNGYKILYLSARAIGQADLTREYLKNVTQDGYKLPDGPVLLSPDRLFSALHREVILRKPEVFKIACLRDIKS 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115727   491 IFalPVPRTPFYAGFGNRITDAISYNHVRVPPTRIFTINSAGEVHIELLQrsGHRSSYVYMNELVDHFFP 560
Cdd:pfam08235 161 LF--PPDVNPFYAGFGNRITDVISYRAVGIPESRIFTINPKGELRHELLK--TYKSSYLSLNELVDHMFP 226
Lipin_N pfam04571
lipin, N-terminal conserved region; Mutations in the lipin gene lead to fatty liver dystrophy ...
 1-100 1.13e-54

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: 181.58  E-value: 1.13e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115727     1 MQYVGRAFDSVTKTWNAINPSTLSGAIDVIVVEQEDKTLACSPFHVRFGKFSLLLPSDKKVEFSVNGQLTGFNMKLGDGG 80
Cdd:pfam04571   1 MNYVGKLFGSVSELYNSINPATLSGAIDVIVVEQPDGTLACSPFHVRFGKLGVLRSREKVVDIEVNGEPVDLHMKLGESG 80

                          90       100
                  ....*....|....*....|...
gi 19115727    81 EAFFVFATE---NAVPRELQTSP 100
Cdd:pfam04571  81 EAFFVFETEddeEDVPDYLQTSP 103
 
Name Accession Description Interval E-value
LNS2 pfam08235
LNS2 (Lipin/Ned1/Smp2); This domain is found in Saccharomyces cerevisiae protein SMP2, ...
 334-560 9.14e-154

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: 442.72  E-value: 9.14e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115727   334 KTLRLTSDQLRSLNLKPGKNELSFGVNG---GKAICTANLFFWKHNDPVVISDIDGTITKSDALGHMFTLIGKDWTHAGV 410
Cdd:pfam08235   1 KSLRLTSEQLKSLNLKPGANTITFSVTTqyqGTQRVEANIYLWKWDDKIVISDIDGTITKSDALGHILPMIGKDWTHPGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115727   411 AKLYTDITNNGYKIMYLTSRSVGQADSTRHYLRNIEQNGYSLPDGPVILSPDRTMAALHREVILRKPEVFKMACLRDLCN 490
Cdd:pfam08235  81 AKLYSKIKRNGYKILYLSARAIGQADLTREYLKNVTQDGYKLPDGPVLLSPDRLFSALHREVILRKPEVFKIACLRDIKS 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115727   491 IFalPVPRTPFYAGFGNRITDAISYNHVRVPPTRIFTINSAGEVHIELLQrsGHRSSYVYMNELVDHFFP 560
Cdd:pfam08235 161 LF--PPDVNPFYAGFGNRITDVISYRAVGIPESRIFTINPKGELRHELLK--TYKSSYLSLNELVDHMFP 226
LNS2 smart00775
This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal ...
 379-537 4.94e-98

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: 297.26  E-value: 4.94e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115727    379 VVISDIDGTITKSDALGHMFTLIGKDWTHAGVAKLYTDITNNGYKIMYLTSRSVGQADSTRHYLRNIEQNGYSLPDGPVI 458
Cdd:smart00775   1 IVISDIDGTITKSDVLGHVVPIIGKDWTHPGVAKLYRDIQNNGYKILYLTARPIGQADRTRSYLSQIKQDGHNLPHGPVL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19115727    459 LSPDRTMAALHREVILRKPEVFKMACLRDLCNIFalPVPRTPFYAGFGNRITDAISYNHVRVPPTRIFTINSAGEVHIE 537
Cdd:smart00775  81 LSPDRLFAALHREVISKKPEVFKIACLRDIKNLF--PPQGNPFYAGFGNRITDVISYSAVGIPPSRIFTINPKGEVHQE 157
Lipin_N pfam04571
lipin, N-terminal conserved region; Mutations in the lipin gene lead to fatty liver dystrophy ...
 1-100 1.13e-54

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: 181.58  E-value: 1.13e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115727     1 MQYVGRAFDSVTKTWNAINPSTLSGAIDVIVVEQEDKTLACSPFHVRFGKFSLLLPSDKKVEFSVNGQLTGFNMKLGDGG 80
Cdd:pfam04571   1 MNYVGKLFGSVSELYNSINPATLSGAIDVIVVEQPDGTLACSPFHVRFGKLGVLRSREKVVDIEVNGEPVDLHMKLGESG 80

                          90       100
                  ....*....|....*....|...
gi 19115727    81 EAFFVFATE---NAVPRELQTSP 100
Cdd:pfam04571  81 EAFFVFETEddeEDVPDYLQTSP 103
HAD_PNKP-C cd07502
C-terminal phosphatase domain of T4 polynucleotide kinase/phosphatase (PNKP) and related ...
 378-476 8.31e-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: 37.12  E-value: 8.31e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115727 378 PVVISDIDGTITKSDALGHMFTLIGKDWT-----------HAGVAKLYTDITNNGYKIMYLTSRSVGQADSTRHYLRNie 446
Cdd:cd07502   2 KAVIFDLDGTLADTNGRQPYLERRPRDWDaffeaadhdppNAPVIELVKESALTGYEIVYLSGRPERYRRDTLRWLAK-- 79

                        90       100       110
                ....*....|....*....|....*....|..
gi 19115727 447 qngYSLPDGPVIL--SPDRTMAALHREVILRK 476
Cdd:cd07502  80 ---HGIPDDALHMrgNADRRKDRRVKLEILRR 108
 
Name Accession Description Interval E-value
LNS2 pfam08235
LNS2 (Lipin/Ned1/Smp2); This domain is found in Saccharomyces cerevisiae protein SMP2, ...
 334-560 9.14e-154

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: 442.72  E-value: 9.14e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115727   334 KTLRLTSDQLRSLNLKPGKNELSFGVNG---GKAICTANLFFWKHNDPVVISDIDGTITKSDALGHMFTLIGKDWTHAGV 410
Cdd:pfam08235   1 KSLRLTSEQLKSLNLKPGANTITFSVTTqyqGTQRVEANIYLWKWDDKIVISDIDGTITKSDALGHILPMIGKDWTHPGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115727   411 AKLYTDITNNGYKIMYLTSRSVGQADSTRHYLRNIEQNGYSLPDGPVILSPDRTMAALHREVILRKPEVFKMACLRDLCN 490
Cdd:pfam08235  81 AKLYSKIKRNGYKILYLSARAIGQADLTREYLKNVTQDGYKLPDGPVLLSPDRLFSALHREVILRKPEVFKIACLRDIKS 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115727   491 IFalPVPRTPFYAGFGNRITDAISYNHVRVPPTRIFTINSAGEVHIELLQrsGHRSSYVYMNELVDHFFP 560
Cdd:pfam08235 161 LF--PPDVNPFYAGFGNRITDVISYRAVGIPESRIFTINPKGELRHELLK--TYKSSYLSLNELVDHMFP 226
LNS2 smart00775
This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal ...
 379-537 4.94e-98

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: 297.26  E-value: 4.94e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115727    379 VVISDIDGTITKSDALGHMFTLIGKDWTHAGVAKLYTDITNNGYKIMYLTSRSVGQADSTRHYLRNIEQNGYSLPDGPVI 458
Cdd:smart00775   1 IVISDIDGTITKSDVLGHVVPIIGKDWTHPGVAKLYRDIQNNGYKILYLTARPIGQADRTRSYLSQIKQDGHNLPHGPVL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19115727    459 LSPDRTMAALHREVILRKPEVFKMACLRDLCNIFalPVPRTPFYAGFGNRITDAISYNHVRVPPTRIFTINSAGEVHIE 537
Cdd:smart00775  81 LSPDRLFAALHREVISKKPEVFKIACLRDIKNLF--PPQGNPFYAGFGNRITDVISYSAVGIPPSRIFTINPKGEVHQE 157
Lipin_N pfam04571
lipin, N-terminal conserved region; Mutations in the lipin gene lead to fatty liver dystrophy ...
 1-100 1.13e-54

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: 181.58  E-value: 1.13e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115727     1 MQYVGRAFDSVTKTWNAINPSTLSGAIDVIVVEQEDKTLACSPFHVRFGKFSLLLPSDKKVEFSVNGQLTGFNMKLGDGG 80
Cdd:pfam04571   1 MNYVGKLFGSVSELYNSINPATLSGAIDVIVVEQPDGTLACSPFHVRFGKLGVLRSREKVVDIEVNGEPVDLHMKLGESG 80

                          90       100
                  ....*....|....*....|...
gi 19115727    81 EAFFVFATE---NAVPRELQTSP 100
Cdd:pfam04571  81 EAFFVFETEddeEDVPDYLQTSP 103
HAD_PNKP-C cd07502
C-terminal phosphatase domain of T4 polynucleotide kinase/phosphatase (PNKP) and related ...
 378-476 8.31e-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: 37.12  E-value: 8.31e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115727 378 PVVISDIDGTITKSDALGHMFTLIGKDWT-----------HAGVAKLYTDITNNGYKIMYLTSRSVGQADSTRHYLRNie 446
Cdd:cd07502   2 KAVIFDLDGTLADTNGRQPYLERRPRDWDaffeaadhdppNAPVIELVKESALTGYEIVYLSGRPERYRRDTLRWLAK-- 79

                        90       100       110
                ....*....|....*....|....*....|..
gi 19115727 447 qngYSLPDGPVIL--SPDRTMAALHREVILRK 476
Cdd:cd07502  80 ---HGIPDDALHMrgNADRRKDRRVKLEILRR 108
 
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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