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Conserved domains on  [gi|320543634|ref|NP_001188878|]
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lipin, isoform G [Drosophila melanogaster]

Protein Classification

Lipin_mid and LNS2 domain-containing protein( domain architecture ID 10928077)

protein containing domains Lipin_N, Lipin_mid, and LNS2

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, ...
687-912 1.11e-144

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: 430.39  E-value: 1.11e-144
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543634   687 KSLRLSSAAIKKLNLKEGMNEIEFSVTTAYQGTTRCKCYLFRWKHNDKVVISDIDGTITKSDVLGHILPMVGKDWAQLGV 766
Cdd:pfam08235    1 KSLRLTSEQLKSLNLKPGANTITFSVTTQYQGTQRVEANIYLWKWDDKIVISDIDGTITKSDALGHILPMIGKDWTHPGV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543634   767 AQLFSKIEQNGYKLLYLSARAIGQSRVTREYLRSIRQGNVMLPDGPLLLNPTSLISAFHREVIEKKPEQFKIACLSDIRD 846
Cdd:pfam08235   81 AKLYSKIKRNGYKILYLSARAIGQADLTREYLKNVTQDGYKLPDGPVLLSPDRLFSALHREVILRKPEVFKIACLRDIKS 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 320543634   847 LFP-DKEPFYAGYGNRINDVWAYRAVGIPIMRIFTINTKGELKHELTQTFQSSgYINQSLEVDEYFP 912
Cdd:pfam08235  161 LFPpDVNPFYAGFGNRITDVISYRAVGIPESRIFTINPKGELRHELLKTYKSS-YLSLNELVDHMFP 226
Lipin_mid pfam16876
Lipin/Ned1/Smp2 multi-domain protein middle domain; This is a middle domain of lipins. Overall ...
489-601 2.69e-41

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: 146.66  E-value: 2.69e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543634   489 VAMSMCGM--SEQGAPPSDEEFDRHLVNYPDVCKSPSIFSSPNLVVRLNGKYYTWMAACPIVMTMITFQKPLTHDAIEQL 566
Cdd:pfam16876    1 VELSLCGGllQGQNEEISDEAFEEHKVTYEDFCKNPSILNDPNLVVRIGGKYYNWAVAAPILLSMQAFQKPLPDDAIEQL 80
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 320543634   567 MSQtvdgkclpgdekqeavaQADNGGQTKRYWWSW 601
Cdd:pfam16876   81 IKE-----------------ARKNPKKGRRSWFSW 98
Lipin_N super family cl04599
lipin, N-terminal conserved region; Mutations in the lipin gene lead to fatty liver dystrophy ...
1-31 1.55e-03

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: 39.06  E-value: 1.55e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 320543634     1 MKLGDSGEAFFVeECLEDEDEELPANLATSP 31
Cdd:pfam04571   74 MKLGESGEAFFV-FETEDDEEDVPDYLQTSP 103
 
Name Accession Description Interval E-value
LNS2 pfam08235
LNS2 (Lipin/Ned1/Smp2); This domain is found in Saccharomyces cerevisiae protein SMP2, ...
687-912 1.11e-144

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: 430.39  E-value: 1.11e-144
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543634   687 KSLRLSSAAIKKLNLKEGMNEIEFSVTTAYQGTTRCKCYLFRWKHNDKVVISDIDGTITKSDVLGHILPMVGKDWAQLGV 766
Cdd:pfam08235    1 KSLRLTSEQLKSLNLKPGANTITFSVTTQYQGTQRVEANIYLWKWDDKIVISDIDGTITKSDALGHILPMIGKDWTHPGV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543634   767 AQLFSKIEQNGYKLLYLSARAIGQSRVTREYLRSIRQGNVMLPDGPLLLNPTSLISAFHREVIEKKPEQFKIACLSDIRD 846
Cdd:pfam08235   81 AKLYSKIKRNGYKILYLSARAIGQADLTREYLKNVTQDGYKLPDGPVLLSPDRLFSALHREVILRKPEVFKIACLRDIKS 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 320543634   847 LFP-DKEPFYAGYGNRINDVWAYRAVGIPIMRIFTINTKGELKHELTQTFQSSgYINQSLEVDEYFP 912
Cdd:pfam08235  161 LFPpDVNPFYAGFGNRITDVISYRAVGIPESRIFTINPKGELRHELLKTYKSS-YLSLNELVDHMFP 226
LNS2 smart00775
This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal ...
735-890 7.68e-90

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: 283.78  E-value: 7.68e-90
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543634    735 VVISDIDGTITKSDVLGHILPMVGKDWAQLGVAQLFSKIEQNGYKLLYLSARAIGQSRVTREYLRSIRQGNVMLPDGPLL 814
Cdd:smart00775    1 IVISDIDGTITKSDVLGHVVPIIGKDWTHPGVAKLYRDIQNNGYKILYLTARPIGQADRTRSYLSQIKQDGHNLPHGPVL 80
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 320543634    815 LNPTSLISAFHREVIEKKPEQFKIACLSDIRDLFP-DKEPFYAGYGNRINDVWAYRAVGIPIMRIFTINTKGELKHE 890
Cdd:smart00775   81 LSPDRLFAALHREVISKKPEVFKIACLRDIKNLFPpQGNPFYAGFGNRITDVISYSAVGIPPSRIFTINPKGEVHQE 157
Lipin_mid pfam16876
Lipin/Ned1/Smp2 multi-domain protein middle domain; This is a middle domain of lipins. Overall ...
489-601 2.69e-41

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: 146.66  E-value: 2.69e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543634   489 VAMSMCGM--SEQGAPPSDEEFDRHLVNYPDVCKSPSIFSSPNLVVRLNGKYYTWMAACPIVMTMITFQKPLTHDAIEQL 566
Cdd:pfam16876    1 VELSLCGGllQGQNEEISDEAFEEHKVTYEDFCKNPSILNDPNLVVRIGGKYYNWAVAAPILLSMQAFQKPLPDDAIEQL 80
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 320543634   567 MSQtvdgkclpgdekqeavaQADNGGQTKRYWWSW 601
Cdd:pfam16876   81 IKE-----------------ARKNPKKGRRSWFSW 98
SMP2 COG5083
Phosphatidate phosphatase PAH1, contains Lipin and LNS2 domains. can be involved in plasmid ...
734-887 3.07e-14

Phosphatidate phosphatase PAH1, contains Lipin and LNS2 domains. can be involved in plasmid maintenance [Lipid transport and metabolism];


Pssm-ID: 444053  Cd Length: 353  Bit Score: 75.27  E-value: 3.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543634  734 KVVISDIDGTITKSDVLGhILPMVGKDWAQL--GVAQLFSKIEQNGYKLLYLSARAIGQSRVTREYLRSirQGnvmLPDG 811
Cdd:COG5083   186 KTVVFDIDGTLTLNDFEG-VGDYLGGETADAhpYAAEVVQAYADKGYRPIYVTGRPYWLAKDTREWLDT--QG---LPPG 259
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 320543634  812 PLLLNPTSlisafhREVIEKKPEQFKIAclsDIRDLFPDKEPFYAGYGNRINDVWAYRAVGIPIMRIFTINTKGEL 887
Cdd:COG5083   260 ILHTTPSA------TGPIGPDTARYKTA---EIQLLIDDGLNIVRAYGNAATDAEAYANAGIPKSETYIIGEDAGL 326
Lipin_N pfam04571
lipin, N-terminal conserved region; Mutations in the lipin gene lead to fatty liver dystrophy ...
1-31 1.55e-03

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: 39.06  E-value: 1.55e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 320543634     1 MKLGDSGEAFFVeECLEDEDEELPANLATSP 31
Cdd:pfam04571   74 MKLGESGEAFFV-FETEDDEEDVPDYLQTSP 103
pseT PHA02530
polynucleotide kinase; Provisional
731-802 4.40e-03

polynucleotide kinase; Provisional


Pssm-ID: 222856 [Multi-domain]  Cd Length: 300  Bit Score: 40.39  E-value: 4.40e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 320543634  731 HNDKVVISDIDGTITKSDVLGHI-LPMVGKDWAQLGVAQLFSKIEQNGYKLLYLSARAIGQSRVTREYLRSIR 802
Cdd:PHA02530  156 GLPKAVIFDIDGTLAKMGGRSPYdWTKVKEDKPNPMVVELVKMYKAAGYEIIVVSGRDGVCEEDTVEWLRQTD 228
 
Name Accession Description Interval E-value
LNS2 pfam08235
LNS2 (Lipin/Ned1/Smp2); This domain is found in Saccharomyces cerevisiae protein SMP2, ...
687-912 1.11e-144

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: 430.39  E-value: 1.11e-144
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543634   687 KSLRLSSAAIKKLNLKEGMNEIEFSVTTAYQGTTRCKCYLFRWKHNDKVVISDIDGTITKSDVLGHILPMVGKDWAQLGV 766
Cdd:pfam08235    1 KSLRLTSEQLKSLNLKPGANTITFSVTTQYQGTQRVEANIYLWKWDDKIVISDIDGTITKSDALGHILPMIGKDWTHPGV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543634   767 AQLFSKIEQNGYKLLYLSARAIGQSRVTREYLRSIRQGNVMLPDGPLLLNPTSLISAFHREVIEKKPEQFKIACLSDIRD 846
Cdd:pfam08235   81 AKLYSKIKRNGYKILYLSARAIGQADLTREYLKNVTQDGYKLPDGPVLLSPDRLFSALHREVILRKPEVFKIACLRDIKS 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 320543634   847 LFP-DKEPFYAGYGNRINDVWAYRAVGIPIMRIFTINTKGELKHELTQTFQSSgYINQSLEVDEYFP 912
Cdd:pfam08235  161 LFPpDVNPFYAGFGNRITDVISYRAVGIPESRIFTINPKGELRHELLKTYKSS-YLSLNELVDHMFP 226
LNS2 smart00775
This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal ...
735-890 7.68e-90

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: 283.78  E-value: 7.68e-90
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543634    735 VVISDIDGTITKSDVLGHILPMVGKDWAQLGVAQLFSKIEQNGYKLLYLSARAIGQSRVTREYLRSIRQGNVMLPDGPLL 814
Cdd:smart00775    1 IVISDIDGTITKSDVLGHVVPIIGKDWTHPGVAKLYRDIQNNGYKILYLTARPIGQADRTRSYLSQIKQDGHNLPHGPVL 80
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 320543634    815 LNPTSLISAFHREVIEKKPEQFKIACLSDIRDLFP-DKEPFYAGYGNRINDVWAYRAVGIPIMRIFTINTKGELKHE 890
Cdd:smart00775   81 LSPDRLFAALHREVISKKPEVFKIACLRDIKNLFPpQGNPFYAGFGNRITDVISYSAVGIPPSRIFTINPKGEVHQE 157
Lipin_mid pfam16876
Lipin/Ned1/Smp2 multi-domain protein middle domain; This is a middle domain of lipins. Overall ...
489-601 2.69e-41

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: 146.66  E-value: 2.69e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543634   489 VAMSMCGM--SEQGAPPSDEEFDRHLVNYPDVCKSPSIFSSPNLVVRLNGKYYTWMAACPIVMTMITFQKPLTHDAIEQL 566
Cdd:pfam16876    1 VELSLCGGllQGQNEEISDEAFEEHKVTYEDFCKNPSILNDPNLVVRIGGKYYNWAVAAPILLSMQAFQKPLPDDAIEQL 80
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 320543634   567 MSQtvdgkclpgdekqeavaQADNGGQTKRYWWSW 601
Cdd:pfam16876   81 IKE-----------------ARKNPKKGRRSWFSW 98
SMP2 COG5083
Phosphatidate phosphatase PAH1, contains Lipin and LNS2 domains. can be involved in plasmid ...
734-887 3.07e-14

Phosphatidate phosphatase PAH1, contains Lipin and LNS2 domains. can be involved in plasmid maintenance [Lipid transport and metabolism];


Pssm-ID: 444053  Cd Length: 353  Bit Score: 75.27  E-value: 3.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543634  734 KVVISDIDGTITKSDVLGhILPMVGKDWAQL--GVAQLFSKIEQNGYKLLYLSARAIGQSRVTREYLRSirQGnvmLPDG 811
Cdd:COG5083   186 KTVVFDIDGTLTLNDFEG-VGDYLGGETADAhpYAAEVVQAYADKGYRPIYVTGRPYWLAKDTREWLDT--QG---LPPG 259
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 320543634  812 PLLLNPTSlisafhREVIEKKPEQFKIAclsDIRDLFPDKEPFYAGYGNRINDVWAYRAVGIPIMRIFTINTKGEL 887
Cdd:COG5083   260 ILHTTPSA------TGPIGPDTARYKTA---EIQLLIDDGLNIVRAYGNAATDAEAYANAGIPKSETYIIGEDAGL 326
APP1_cat pfam09949
Phosphatidate phosphatase APP1, catalytic domain; This entry represents a conserved region ...
736-851 3.43e-04

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: 42.10  E-value: 3.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320543634   736 VISDIDGTITKSDVLGhilPMVG----------KDWAQLGVAQLFSKI-EQNGYKLLYLSARAIGQSRVTREYLRsirqg 804
Cdd:pfam09949    1 VISDIDDTIKVTGVTS---PLRAlfntffvnalTRVPIPGMPELYRALsASPGNPFFYVSNSPWNLYPFLRDFLE----- 72
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 320543634   805 NVMLPDGPLLLNP-----TSLISAFHrevieKKPEQFKIACLSDIRDLFPDK 851
Cdd:pfam09949   73 RHGYPPGSLLLRDygstdTSLLRSGL-----TPSAEHKRASIERILRDFPNR 119
Lipin_N pfam04571
lipin, N-terminal conserved region; Mutations in the lipin gene lead to fatty liver dystrophy ...
1-31 1.55e-03

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: 39.06  E-value: 1.55e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 320543634     1 MKLGDSGEAFFVeECLEDEDEELPANLATSP 31
Cdd:pfam04571   74 MKLGESGEAFFV-FETEDDEEDVPDYLQTSP 103
pseT PHA02530
polynucleotide kinase; Provisional
731-802 4.40e-03

polynucleotide kinase; Provisional


Pssm-ID: 222856 [Multi-domain]  Cd Length: 300  Bit Score: 40.39  E-value: 4.40e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 320543634  731 HNDKVVISDIDGTITKSDVLGHI-LPMVGKDWAQLGVAQLFSKIEQNGYKLLYLSARAIGQSRVTREYLRSIR 802
Cdd:PHA02530  156 GLPKAVIFDIDGTLAKMGGRSPYdWTKVKEDKPNPMVVELVKMYKAAGYEIIVVSGRDGVCEEDTVEWLRQTD 228
 
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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