phosphatidate phosphatase LPIN2 isoform X3 [Rattus norvegicus]
lipin family protein( domain architecture ID 11151325)
lipin family protein acts as a phosphatidate phosphatase that catalyzes the conversion of phosphatidic acid to diacylglycerol
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, ... |
643-868 | 2.56e-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: 451.96 E-value: 2.56e-154
|
||||||||
Lipin_N | pfam04571 | lipin, N-terminal conserved region; Mutations in the lipin gene lead to fatty liver dystrophy ... |
9-115 | 5.41e-55 | ||||
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: 185.05 E-value: 5.41e-55
|
||||||||
Lipin_mid | pfam16876 | Lipin/Ned1/Smp2 multi-domain protein middle domain; This is a middle domain of lipins. Overall ... |
475-567 | 4.07e-42 | ||||
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: 148.59 E-value: 4.07e-42
|
||||||||
PHA03247 super family | cl33720 | large tegument protein UL36; Provisional |
334-491 | 1.48e-03 | ||||
large tegument protein UL36; Provisional The actual alignment was detected with superfamily member PHA03247: Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 42.62 E-value: 1.48e-03
|
||||||||
WRNPLPNID | pfam15017 | Putative WW-binding domain and destruction box; This short conserved region is a putative ... |
881-899 | 4.01e-03 | ||||
Putative WW-binding domain and destruction box; This short conserved region is a putative destruction-box, with its RxxLxxI sequence motif, though the homology is not absolute. The domain occurs on a number of tumourigenic proteins, on some RNA-binding proteins and serine-threonine regulatory proteins. The second less well-conserved motif, WITPS, is a potential WW domain ligand-binding motif for recruiting proteins to their substrates. WW domains bind tightly to short proline-containing peptides that are typically in regions of native disordered polypeptide, as this family is as it lies between a PIN domain and a zinc-binding domain. : Pssm-ID: 464448 Cd Length: 56 Bit Score: 36.17 E-value: 4.01e-03
|
||||||||
Name | Accession | Description | Interval | E-value | ||||
LNS2 | pfam08235 | LNS2 (Lipin/Ned1/Smp2); This domain is found in Saccharomyces cerevisiae protein SMP2, ... |
643-868 | 2.56e-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: 451.96 E-value: 2.56e-154
|
||||||||
LNS2 | smart00775 | This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal ... |
691-847 | 3.91e-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: 290.33 E-value: 3.91e-93
|
||||||||
Lipin_N | pfam04571 | lipin, N-terminal conserved region; Mutations in the lipin gene lead to fatty liver dystrophy ... |
9-115 | 5.41e-55 | ||||
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: 185.05 E-value: 5.41e-55
|
||||||||
Lipin_mid | pfam16876 | Lipin/Ned1/Smp2 multi-domain protein middle domain; This is a middle domain of lipins. Overall ... |
475-567 | 4.07e-42 | ||||
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: 148.59 E-value: 4.07e-42
|
||||||||
PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
334-491 | 1.48e-03 | ||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 42.62 E-value: 1.48e-03
|
||||||||
WRNPLPNID | pfam15017 | Putative WW-binding domain and destruction box; This short conserved region is a putative ... |
881-899 | 4.01e-03 | ||||
Putative WW-binding domain and destruction box; This short conserved region is a putative destruction-box, with its RxxLxxI sequence motif, though the homology is not absolute. The domain occurs on a number of tumourigenic proteins, on some RNA-binding proteins and serine-threonine regulatory proteins. The second less well-conserved motif, WITPS, is a potential WW domain ligand-binding motif for recruiting proteins to their substrates. WW domains bind tightly to short proline-containing peptides that are typically in regions of native disordered polypeptide, as this family is as it lies between a PIN domain and a zinc-binding domain. Pssm-ID: 464448 Cd Length: 56 Bit Score: 36.17 E-value: 4.01e-03
|
||||||||
Name | Accession | Description | Interval | E-value | ||||
LNS2 | pfam08235 | LNS2 (Lipin/Ned1/Smp2); This domain is found in Saccharomyces cerevisiae protein SMP2, ... |
643-868 | 2.56e-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: 451.96 E-value: 2.56e-154
|
||||||||
LNS2 | smart00775 | This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal ... |
691-847 | 3.91e-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: 290.33 E-value: 3.91e-93
|
||||||||
Lipin_N | pfam04571 | lipin, N-terminal conserved region; Mutations in the lipin gene lead to fatty liver dystrophy ... |
9-115 | 5.41e-55 | ||||
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: 185.05 E-value: 5.41e-55
|
||||||||
Lipin_mid | pfam16876 | Lipin/Ned1/Smp2 multi-domain protein middle domain; This is a middle domain of lipins. Overall ... |
475-567 | 4.07e-42 | ||||
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: 148.59 E-value: 4.07e-42
|
||||||||
PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
334-491 | 1.48e-03 | ||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 42.62 E-value: 1.48e-03
|
||||||||
WRNPLPNID | pfam15017 | Putative WW-binding domain and destruction box; This short conserved region is a putative ... |
881-899 | 4.01e-03 | ||||
Putative WW-binding domain and destruction box; This short conserved region is a putative destruction-box, with its RxxLxxI sequence motif, though the homology is not absolute. The domain occurs on a number of tumourigenic proteins, on some RNA-binding proteins and serine-threonine regulatory proteins. The second less well-conserved motif, WITPS, is a potential WW domain ligand-binding motif for recruiting proteins to their substrates. WW domains bind tightly to short proline-containing peptides that are typically in regions of native disordered polypeptide, as this family is as it lies between a PIN domain and a zinc-binding domain. Pssm-ID: 464448 Cd Length: 56 Bit Score: 36.17 E-value: 4.01e-03
|
||||||||
Blast search parameters | ||||
|