group 3 secretory phospholipase A2 precursor [Rattus norvegicus]
PLA2_bee_venom_like and PLA2_group_III_like domain-containing protein( domain architecture ID 10140434)
PLA2_bee_venom_like and PLA2_group_III_like domain-containing protein
List of domain hits
Name | Accession | Description | Interval | E-value | |||
PLA2_bee_venom_like | cd04704 | PLA2_bee_venom_like: A sub-family of Phospholipase A2, similar to bee venom PLA2. PLA2 is a ... |
151-247 | 4.31e-50 | |||
PLA2_bee_venom_like: A sub-family of Phospholipase A2, similar to bee venom PLA2. PLA2 is a super-family of secretory and cytosolic enzymes; the latter are either Ca dependent or Ca independent. Enzymatically active PLA2 cleaves the sn-2 position of the glycerol backbone of phospholipids; secreted PLA2s have also been found to specifically bind to a variety of soluble and membrane proteins in mammals, including receptors. As a toxin, PLA2 is a potent presynaptic neurotoxin which blocks nerve terminals by binding to the nerve membrane and hydrolyzing stable membrane lipids. The products of the hydrolysis cannot form bilayers leading to a change in membrane conformation and ultimately to a block in the release of neurotransmitters. PLA2 may form dimers or oligomers. Bee venom PLA2 has fewer conserved disulfide bridges than most canonical PLA2s. : Pssm-ID: 153093 Cd Length: 97 Bit Score: 166.32 E-value: 4.31e-50
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PLA2_group_III_like | cd04705 | PLA2_group_III_like: A sub-family of Phospholipase A2, similar to human group III PLA2. PLA2 ... |
299-424 | 2.33e-26 | |||
PLA2_group_III_like: A sub-family of Phospholipase A2, similar to human group III PLA2. PLA2 is a super-family of secretory and cytosolic enzymes; the latter are either Ca dependent or Ca independent. Enzymatically active PLA2 cleaves the sn-2 position of the glycerol backbone of phospholipids; secreted PLA2s have also been found to specifically bind to a variety of soluble and membrane proteins in mammals, including receptors. As a toxin, PLA2 is a potent presynaptic neurotoxin which blocks nerve terminals by binding to the nerve membrane and hydrolyzing stable membrane lipids. The products of the hydrolysis cannot form bilayers leading to a change in membrane conformation and ultimately to a block in the release of neurotransmitters. PLA2 may form dimers or oligomers. : Pssm-ID: 153094 Cd Length: 100 Bit Score: 102.60 E-value: 2.33e-26
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Name | Accession | Description | Interval | E-value | |||
PLA2_bee_venom_like | cd04704 | PLA2_bee_venom_like: A sub-family of Phospholipase A2, similar to bee venom PLA2. PLA2 is a ... |
151-247 | 4.31e-50 | |||
PLA2_bee_venom_like: A sub-family of Phospholipase A2, similar to bee venom PLA2. PLA2 is a super-family of secretory and cytosolic enzymes; the latter are either Ca dependent or Ca independent. Enzymatically active PLA2 cleaves the sn-2 position of the glycerol backbone of phospholipids; secreted PLA2s have also been found to specifically bind to a variety of soluble and membrane proteins in mammals, including receptors. As a toxin, PLA2 is a potent presynaptic neurotoxin which blocks nerve terminals by binding to the nerve membrane and hydrolyzing stable membrane lipids. The products of the hydrolysis cannot form bilayers leading to a change in membrane conformation and ultimately to a block in the release of neurotransmitters. PLA2 may form dimers or oligomers. Bee venom PLA2 has fewer conserved disulfide bridges than most canonical PLA2s. Pssm-ID: 153093 Cd Length: 97 Bit Score: 166.32 E-value: 4.31e-50
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Phospholip_A2_2 | pfam05826 | Phospholipase A2; This family consists of several phospholipase A2 like proteins mostly from ... |
152-248 | 2.51e-45 | |||
Phospholipase A2; This family consists of several phospholipase A2 like proteins mostly from insects. Pssm-ID: 461751 Cd Length: 97 Bit Score: 153.84 E-value: 2.51e-45
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PLA2_group_III_like | cd04705 | PLA2_group_III_like: A sub-family of Phospholipase A2, similar to human group III PLA2. PLA2 ... |
299-424 | 2.33e-26 | |||
PLA2_group_III_like: A sub-family of Phospholipase A2, similar to human group III PLA2. PLA2 is a super-family of secretory and cytosolic enzymes; the latter are either Ca dependent or Ca independent. Enzymatically active PLA2 cleaves the sn-2 position of the glycerol backbone of phospholipids; secreted PLA2s have also been found to specifically bind to a variety of soluble and membrane proteins in mammals, including receptors. As a toxin, PLA2 is a potent presynaptic neurotoxin which blocks nerve terminals by binding to the nerve membrane and hydrolyzing stable membrane lipids. The products of the hydrolysis cannot form bilayers leading to a change in membrane conformation and ultimately to a block in the release of neurotransmitters. PLA2 may form dimers or oligomers. Pssm-ID: 153094 Cd Length: 100 Bit Score: 102.60 E-value: 2.33e-26
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PA2c | smart00085 | Phospholipase A2; |
147-245 | 9.98e-05 | |||
Phospholipase A2; Pssm-ID: 214508 Cd Length: 117 Bit Score: 41.81 E-value: 9.98e-05
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Phospholip_A2_2 | pfam05826 | Phospholipase A2; This family consists of several phospholipase A2 like proteins mostly from ... |
358-425 | 5.47e-04 | |||
Phospholipase A2; This family consists of several phospholipase A2 like proteins mostly from insects. Pssm-ID: 461751 Cd Length: 97 Bit Score: 39.05 E-value: 5.47e-04
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Name | Accession | Description | Interval | E-value | |||
PLA2_bee_venom_like | cd04704 | PLA2_bee_venom_like: A sub-family of Phospholipase A2, similar to bee venom PLA2. PLA2 is a ... |
151-247 | 4.31e-50 | |||
PLA2_bee_venom_like: A sub-family of Phospholipase A2, similar to bee venom PLA2. PLA2 is a super-family of secretory and cytosolic enzymes; the latter are either Ca dependent or Ca independent. Enzymatically active PLA2 cleaves the sn-2 position of the glycerol backbone of phospholipids; secreted PLA2s have also been found to specifically bind to a variety of soluble and membrane proteins in mammals, including receptors. As a toxin, PLA2 is a potent presynaptic neurotoxin which blocks nerve terminals by binding to the nerve membrane and hydrolyzing stable membrane lipids. The products of the hydrolysis cannot form bilayers leading to a change in membrane conformation and ultimately to a block in the release of neurotransmitters. PLA2 may form dimers or oligomers. Bee venom PLA2 has fewer conserved disulfide bridges than most canonical PLA2s. Pssm-ID: 153093 Cd Length: 97 Bit Score: 166.32 E-value: 4.31e-50
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Phospholip_A2_2 | pfam05826 | Phospholipase A2; This family consists of several phospholipase A2 like proteins mostly from ... |
152-248 | 2.51e-45 | |||
Phospholipase A2; This family consists of several phospholipase A2 like proteins mostly from insects. Pssm-ID: 461751 Cd Length: 97 Bit Score: 153.84 E-value: 2.51e-45
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PLA2_group_III_like | cd04705 | PLA2_group_III_like: A sub-family of Phospholipase A2, similar to human group III PLA2. PLA2 ... |
299-424 | 2.33e-26 | |||
PLA2_group_III_like: A sub-family of Phospholipase A2, similar to human group III PLA2. PLA2 is a super-family of secretory and cytosolic enzymes; the latter are either Ca dependent or Ca independent. Enzymatically active PLA2 cleaves the sn-2 position of the glycerol backbone of phospholipids; secreted PLA2s have also been found to specifically bind to a variety of soluble and membrane proteins in mammals, including receptors. As a toxin, PLA2 is a potent presynaptic neurotoxin which blocks nerve terminals by binding to the nerve membrane and hydrolyzing stable membrane lipids. The products of the hydrolysis cannot form bilayers leading to a change in membrane conformation and ultimately to a block in the release of neurotransmitters. PLA2 may form dimers or oligomers. Pssm-ID: 153094 Cd Length: 100 Bit Score: 102.60 E-value: 2.33e-26
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PLA2_group_III_like | cd04705 | PLA2_group_III_like: A sub-family of Phospholipase A2, similar to human group III PLA2. PLA2 ... |
172-238 | 5.81e-19 | |||
PLA2_group_III_like: A sub-family of Phospholipase A2, similar to human group III PLA2. PLA2 is a super-family of secretory and cytosolic enzymes; the latter are either Ca dependent or Ca independent. Enzymatically active PLA2 cleaves the sn-2 position of the glycerol backbone of phospholipids; secreted PLA2s have also been found to specifically bind to a variety of soluble and membrane proteins in mammals, including receptors. As a toxin, PLA2 is a potent presynaptic neurotoxin which blocks nerve terminals by binding to the nerve membrane and hydrolyzing stable membrane lipids. The products of the hydrolysis cannot form bilayers leading to a change in membrane conformation and ultimately to a block in the release of neurotransmitters. PLA2 may form dimers or oligomers. Pssm-ID: 153094 Cd Length: 100 Bit Score: 81.80 E-value: 5.81e-19
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PLA2_like | cd00618 | PLA2_like: Phospholipase A2, a super-family of secretory and cytosolic enzymes; the latter are ... |
153-223 | 4.97e-16 | |||
PLA2_like: Phospholipase A2, a super-family of secretory and cytosolic enzymes; the latter are either Ca dependent or Ca independent. PLA2 cleaves the sn-2 position of the glycerol backbone of phospholipids (PC or phosphatidylethanolamine), usually in a metal-dependent reaction, to generate lysophospholipid (LysoPL) and a free fatty acid (FA). The resulting products are either dietary or used in synthetic pathways for leukotrienes and prostaglandins. Often, arachidonic acid is released as a free fatty acid and acts as second messenger in signaling networks. Secreted PLA2s have also been found to specifically bind to a variety of soluble and membrane proteins in mammals, including receptors. As a toxin, PLA2 is a potent presynaptic neurotoxin which blocks nerve terminals by binding to the nerve membrane and hydrolyzing stable membrane lipids. The products of the hydrolysis (LysoPL and FA) cannot form bilayers leading to a change in membrane conformation and ultimately to a block in the release of neurotransmitters. PLA2 may form dimers or oligomers. Pssm-ID: 153092 Cd Length: 83 Bit Score: 72.98 E-value: 4.97e-16
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PLA2_like | cd00618 | PLA2_like: Phospholipase A2, a super-family of secretory and cytosolic enzymes; the latter are ... |
343-403 | 3.12e-05 | |||
PLA2_like: Phospholipase A2, a super-family of secretory and cytosolic enzymes; the latter are either Ca dependent or Ca independent. PLA2 cleaves the sn-2 position of the glycerol backbone of phospholipids (PC or phosphatidylethanolamine), usually in a metal-dependent reaction, to generate lysophospholipid (LysoPL) and a free fatty acid (FA). The resulting products are either dietary or used in synthetic pathways for leukotrienes and prostaglandins. Often, arachidonic acid is released as a free fatty acid and acts as second messenger in signaling networks. Secreted PLA2s have also been found to specifically bind to a variety of soluble and membrane proteins in mammals, including receptors. As a toxin, PLA2 is a potent presynaptic neurotoxin which blocks nerve terminals by binding to the nerve membrane and hydrolyzing stable membrane lipids. The products of the hydrolysis (LysoPL and FA) cannot form bilayers leading to a change in membrane conformation and ultimately to a block in the release of neurotransmitters. PLA2 may form dimers or oligomers. Pssm-ID: 153092 Cd Length: 83 Bit Score: 42.55 E-value: 3.12e-05
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PA2c | smart00085 | Phospholipase A2; |
147-245 | 9.98e-05 | |||
Phospholipase A2; Pssm-ID: 214508 Cd Length: 117 Bit Score: 41.81 E-value: 9.98e-05
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Phospholip_A2_2 | pfam05826 | Phospholipase A2; This family consists of several phospholipase A2 like proteins mostly from ... |
358-425 | 5.47e-04 | |||
Phospholipase A2; This family consists of several phospholipase A2 like proteins mostly from insects. Pssm-ID: 461751 Cd Length: 97 Bit Score: 39.05 E-value: 5.47e-04
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Blast search parameters | ||||
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