membrane-associated phosphatidylinositol transfer protein 3 isoform X2 [Mus musculus]
Protein Classification
DDHD family phospholipase( domain architecture ID 11139245)
DDHD family phospholipase similar to Homo sapiens phospholipase DDHD1 that hydrolyzes phosphatidic acid, including 1,2-dioleoyl-sn-phosphatidic acid
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| LNS2 | smart00775 | This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal ... |
724-854 | 3.71e-46 | |||||
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: 162.44 E-value: 3.71e-46
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| DDHD | pfam02862 | DDHD domain; The DDHD domain is 180 residues long and contains four conserved residues that ... |
375-578 | 4.06e-44 | |||||
DDHD domain; The DDHD domain is 180 residues long and contains four conserved residues that may form a metal binding site. The domain is named after these four residues. This pattern of conservation of metal binding residues is often seen in phosphoesterase domains. This domain is found in retinal degeneration B proteins, as well as a family of probable phospholipases. It has been shown that this domain is found in a longer C terminal region that binds to PYK2 tyrosine kinase. These proteins have been called N-terminal domain-interacting receptor (Nir1, Nir2 and Nir3). This suggests that this region is involved in functionally important interactions in other members of this family. : Pssm-ID: 460725 Cd Length: 241 Bit Score: 159.91 E-value: 4.06e-44
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| Name | Accession | Description | Interval | E-value | |||||
| LNS2 | smart00775 | This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal ... |
724-854 | 3.71e-46 | |||||
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: 162.44 E-value: 3.71e-46
|
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| DDHD | pfam02862 | DDHD domain; The DDHD domain is 180 residues long and contains four conserved residues that ... |
375-578 | 4.06e-44 | |||||
DDHD domain; The DDHD domain is 180 residues long and contains four conserved residues that may form a metal binding site. The domain is named after these four residues. This pattern of conservation of metal binding residues is often seen in phosphoesterase domains. This domain is found in retinal degeneration B proteins, as well as a family of probable phospholipases. It has been shown that this domain is found in a longer C terminal region that binds to PYK2 tyrosine kinase. These proteins have been called N-terminal domain-interacting receptor (Nir1, Nir2 and Nir3). This suggests that this region is involved in functionally important interactions in other members of this family. Pssm-ID: 460725 Cd Length: 241 Bit Score: 159.91 E-value: 4.06e-44
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| YqfW | COG5663 | Uncharacterized conserved protein YqfW, HAD superfamily [General function prediction only]; |
732-818 | 6.96e-07 | |||||
Uncharacterized conserved protein YqfW, HAD superfamily [General function prediction only]; Pssm-ID: 444382 [Multi-domain] Cd Length: 187 Bit Score: 50.61 E-value: 6.96e-07
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| pseT | PHA02530 | polynucleotide kinase; Provisional |
722-787 | 7.69e-03 | |||||
polynucleotide kinase; Provisional Pssm-ID: 222856 [Multi-domain] Cd Length: 300 Bit Score: 39.62 E-value: 7.69e-03
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| HAD_PNKP-C | cd07502 | C-terminal phosphatase domain of T4 polynucleotide kinase/phosphatase (PNKP) and related ... |
724-820 | 8.25e-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: 37.89 E-value: 8.25e-03
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| Name | Accession | Description | Interval | E-value | |||||
| LNS2 | smart00775 | This domain is found in Saccharomyces cerevisiae protein SMP2, proteins with an N-terminal ... |
724-854 | 3.71e-46 | |||||
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: 162.44 E-value: 3.71e-46
|
|||||||||
| DDHD | pfam02862 | DDHD domain; The DDHD domain is 180 residues long and contains four conserved residues that ... |
375-578 | 4.06e-44 | |||||
DDHD domain; The DDHD domain is 180 residues long and contains four conserved residues that may form a metal binding site. The domain is named after these four residues. This pattern of conservation of metal binding residues is often seen in phosphoesterase domains. This domain is found in retinal degeneration B proteins, as well as a family of probable phospholipases. It has been shown that this domain is found in a longer C terminal region that binds to PYK2 tyrosine kinase. These proteins have been called N-terminal domain-interacting receptor (Nir1, Nir2 and Nir3). This suggests that this region is involved in functionally important interactions in other members of this family. Pssm-ID: 460725 Cd Length: 241 Bit Score: 159.91 E-value: 4.06e-44
|
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| YqfW | COG5663 | Uncharacterized conserved protein YqfW, HAD superfamily [General function prediction only]; |
732-818 | 6.96e-07 | |||||
Uncharacterized conserved protein YqfW, HAD superfamily [General function prediction only]; Pssm-ID: 444382 [Multi-domain] Cd Length: 187 Bit Score: 50.61 E-value: 6.96e-07
|
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| pseT | PHA02530 | polynucleotide kinase; Provisional |
722-787 | 7.69e-03 | |||||
polynucleotide kinase; Provisional Pssm-ID: 222856 [Multi-domain] Cd Length: 300 Bit Score: 39.62 E-value: 7.69e-03
|
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| HAD_PNKP-C | cd07502 | C-terminal phosphatase domain of T4 polynucleotide kinase/phosphatase (PNKP) and related ... |
724-820 | 8.25e-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: 37.89 E-value: 8.25e-03
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| Blast search parameters | ||||
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