MULTISPECIES: patatin family protein [Pseudoalteromonas]
patatin family protein( domain architecture ID 11468705)
patatin family protein similar to Escherichia coli YjjU; the family includes putative phospholipases
List of domain hits
Name | Accession | Description | Interval | E-value | |||||
YjjU | COG4667 | Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism]; |
18-315 | 1.50e-102 | |||||
Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism]; : Pssm-ID: 443704 [Multi-domain] Cd Length: 281 Bit Score: 302.47 E-value: 1.50e-102
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Name | Accession | Description | Interval | E-value | |||||
YjjU | COG4667 | Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism]; |
18-315 | 1.50e-102 | |||||
Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism]; Pssm-ID: 443704 [Multi-domain] Cd Length: 281 Bit Score: 302.47 E-value: 1.50e-102
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Pat_hypo_Ecoli_yjju_like | cd07208 | Hypothetical patatin similar to yjju protein of Escherichia coli; Patatin-like phospholipase ... |
22-311 | 3.53e-80 | |||||
Hypothetical patatin similar to yjju protein of Escherichia coli; Patatin-like phospholipase similar to yjju protein of Escherichia coli. This family predominantly consists of bacterial patatin glycoproteins, and some representatives from eukaryotes and archaea. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein, but it also has the enzymatic activity of a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids. Members of this family have also been found in vertebrates. Pssm-ID: 132847 [Multi-domain] Cd Length: 266 Bit Score: 244.83 E-value: 3.53e-80
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DUF6363 | pfam19890 | Domain of unknown function (DUF6363); This presumed domain is functionally uncharacterized. ... |
249-320 | 2.43e-18 | |||||
Domain of unknown function (DUF6363); This presumed domain is functionally uncharacterized. This domain is found at the C-terminal of patatin-like proteins from bacteria. There is a conserved tyrosine residue and a conserved FxxxPP sequence motif. Pssm-ID: 466223 [Multi-domain] Cd Length: 75 Bit Score: 77.95 E-value: 2.43e-18
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CBASS_lipase | NF041079 | CBASS cGAMP-activated phospholipase; |
26-58 | 9.36e-03 | |||||
CBASS cGAMP-activated phospholipase; Pssm-ID: 469006 [Multi-domain] Cd Length: 317 Bit Score: 37.48 E-value: 9.36e-03
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Name | Accession | Description | Interval | E-value | |||||
YjjU | COG4667 | Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism]; |
18-315 | 1.50e-102 | |||||
Predicted phospholipase, patatin/cPLA2 family [Lipid transport and metabolism]; Pssm-ID: 443704 [Multi-domain] Cd Length: 281 Bit Score: 302.47 E-value: 1.50e-102
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Pat_hypo_Ecoli_yjju_like | cd07208 | Hypothetical patatin similar to yjju protein of Escherichia coli; Patatin-like phospholipase ... |
22-311 | 3.53e-80 | |||||
Hypothetical patatin similar to yjju protein of Escherichia coli; Patatin-like phospholipase similar to yjju protein of Escherichia coli. This family predominantly consists of bacterial patatin glycoproteins, and some representatives from eukaryotes and archaea. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein, but it also has the enzymatic activity of a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids. Members of this family have also been found in vertebrates. Pssm-ID: 132847 [Multi-domain] Cd Length: 266 Bit Score: 244.83 E-value: 3.53e-80
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RssA | COG1752 | Predicted acylesterase/phospholipase RssA, containd patatin domain [General function ... |
15-222 | 7.75e-24 | |||||
Predicted acylesterase/phospholipase RssA, containd patatin domain [General function prediction only]; Pssm-ID: 441358 [Multi-domain] Cd Length: 261 Bit Score: 98.05 E-value: 7.75e-24
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DUF6363 | pfam19890 | Domain of unknown function (DUF6363); This presumed domain is functionally uncharacterized. ... |
249-320 | 2.43e-18 | |||||
Domain of unknown function (DUF6363); This presumed domain is functionally uncharacterized. This domain is found at the C-terminal of patatin-like proteins from bacteria. There is a conserved tyrosine residue and a conserved FxxxPP sequence motif. Pssm-ID: 466223 [Multi-domain] Cd Length: 75 Bit Score: 77.95 E-value: 2.43e-18
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Pat_hypo_Ecoli_Z1214_like | cd07209 | Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase ... |
22-227 | 2.91e-15 | |||||
Hypothetical patatin similar to Z1214 protein of Escherichia coli; Patatin-like phospholipase similar to Z1214 protein of Escherichia coli. This family predominantly consists of bacterial patatin glycoproteins and some representatives from eukaryotes and archaea. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein, but it also has the enzymatic activity of a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids. Members of this family have also been found in vertebrates. Pssm-ID: 132848 [Multi-domain] Cd Length: 215 Bit Score: 73.48 E-value: 2.91e-15
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Patatin | cd07198 | Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows ... |
22-208 | 4.81e-15 | |||||
Patatin-like phospholipase; Patatin is a storage protein of the potato tuber that shows Phospholipase A2 activity (PLA2; EC 3.1.1.4). Patatin catalyzes the nonspecific hydrolysis of phospholipids, glycolipids, sulfolipids, and mono- and diacylglycerols, thereby showing lipid acyl hydrolase activity. The active site includes an oxyanion hole with a conserved GGxR motif; it is found in almost all the members of this family. The catalytic dyad is formed by a serine and an aspartate. Patatin belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Members of this family have been found also in vertebrates. This family includes PNPLA (1-9), TGL (3-5), ExoU-like, and SDP1-like subfamilies. There are some additional hypothetical proteins included in this family. Pssm-ID: 132837 [Multi-domain] Cd Length: 172 Bit Score: 71.99 E-value: 4.81e-15
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Patatin | pfam01734 | Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. ... |
25-212 | 6.76e-14 | |||||
Patatin-like phospholipase; This family consists of various patatin glycoproteins from plants. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein but it also has the enzymatic activity of lipid acyl hydrolase, catalysing the cleavage of fatty acids from membrane lipids. Members of this family have been found also in vertebrates. Pssm-ID: 396341 Cd Length: 190 Bit Score: 69.18 E-value: 6.76e-14
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Pat_PNPLA6_PNPLA7_NTE1_like | cd07205 | Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ... |
20-220 | 9.09e-08 | |||||
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; Patatin-like phospholipase domain containing protein 6 (PNPLA6) and protein 7 (PNPLA7) are included in this family. PNPLA6 is commonly known as Neuropathy Target Esterase (NTE). NTE has at least two functional domains: the N-terminal domain putatively regulatory domain and the C-terminal catalytic domain which shows esterase activity. NTE shows phospholipase activity for lysophosphatidylcholine (LPC) and phosphatidylcholine (PC). Exposure of NTE to organophosphates leads to organophosphate-induced delayed neurotoxicity (OPIDN). OPIDN is a progressive neurological condition that is characterized by weakness, paralysis, pain, and paresthesia. PNPLA7 is an insulin-regulated phospholipase that is homologus to Neuropathy Target Esterase (NTE or PNPLA6) and is also known as NTE-related esterase (NRE). Human NRE is predominantly expressed in prostate, white adipose, and pancreatic tissue. NRE hydrolyzes sn-1 esters in lysophosphatidylcholine and lysophosphatidic acid, but shows no lipase activity with substrates like triacylglycerols (TG), cholesteryl esters, retinyl esters (RE), phosphatidylcholine (PC), or monoacylglycerol (MG). This family includes subfamily of PNPLA6 (NTE) and PNPLA7 (NRE)-like phospholipases. Pssm-ID: 132844 [Multi-domain] Cd Length: 175 Bit Score: 51.39 E-value: 9.09e-08
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PATA | COG3621 | Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function ... |
26-222 | 1.43e-06 | |||||
Patatin-like phospholipase/acyl hydrolase, includes sporulation protein CotR [General function prediction only]; Pssm-ID: 442839 [Multi-domain] Cd Length: 296 Bit Score: 49.13 E-value: 1.43e-06
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Pat_Fungal_NTE1 | cd07227 | Fungal patatin-like phospholipase domain containing protein 6; These are fungal Neuropathy ... |
20-222 | 4.45e-06 | |||||
Fungal patatin-like phospholipase domain containing protein 6; These are fungal Neuropathy Target Esterase (NTE), commonly referred to as NTE1. Patatin-like phospholipase. NTE has at least two functional domains: the N-terminal domain putatively regulatory domain and the C-terminal catalytic domain which shows esterase activity. NTE shows phospholipase activity for lysophosphatidylcholine (LPC) and phosphatidylcholine (PC). Exposure of NTE to organophosphates leads to organophosphate-induced delayed neurotoxicity (OPIDN). OPIDN is a progressive neurological condition that is characterized by weakness, paralysis, pain, and paresthesia. This family includes NTE1 from fungi. Pssm-ID: 132865 [Multi-domain] Cd Length: 269 Bit Score: 47.49 E-value: 4.45e-06
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Pat17_PNPLA8_PNPLA9_like | cd07199 | Patatin-like phospholipase; includes PNPLA8, PNPLA9, and Pat17; Patatin is a storage protein ... |
26-222 | 5.49e-05 | |||||
Patatin-like phospholipase; includes PNPLA8, PNPLA9, and Pat17; Patatin is a storage protein of the potato tuber that shows Phospholipase A2 activity (PLA2; EC 3.1.1.4). Patatin catalyzes the nonspecific hydrolysis of phospholipids, glycolipids, sulfolipids, and mono- and diacylglycerols, thereby showing lipid acyl hydrolase activity. The active site includes an oxyanion hole with a conserved GGxR motif; it is found in almost all the members of this family. The catalytic dyad is formed by a serine and an aspartate. Patatin belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Members of this family have been found also in vertebrates. This family includes subfamily of PNPLA8 (iPLA2-gamma) and PNPLA9 (iPLA2-beta) like phospholipases from human as well as the Pat17 isozyme from Solanum cardiophyllum. Pssm-ID: 132838 [Multi-domain] Cd Length: 258 Bit Score: 43.86 E-value: 5.49e-05
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Patatin_and_cPLA2 | cd01819 | Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ... |
22-59 | 2.23e-03 | |||||
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various patatin glycoproteins from plants. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein, but it also has the enzymatic activity of a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids. Members of this family have also been found in vertebrates. This family also includes the catalytic domain of cytosolic phospholipase A2 (PLA2; EC 3.1.1.4) hydrolyzes the sn-2-acyl ester bond of phospholipids to release arachidonic acid. At the active site, cPLA2 contains a serine nucleophile through which the catalytic mechanism is initiated. The active site is partially covered by a solvent-accessible flexible lid. cPLA2 displays interfacial activation as it exists in both "closed lid" and "open lid" forms. Pssm-ID: 132836 [Multi-domain] Cd Length: 155 Bit Score: 38.17 E-value: 2.23e-03
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CBASS_lipase | NF041079 | CBASS cGAMP-activated phospholipase; |
26-58 | 9.36e-03 | |||||
CBASS cGAMP-activated phospholipase; Pssm-ID: 469006 [Multi-domain] Cd Length: 317 Bit Score: 37.48 E-value: 9.36e-03
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Blast search parameters | ||||
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