torsin-1A-interacting protein 2-like [Delphinapterus leucas]
LAP1_N and LAP1_C domain-containing protein( domain architecture ID 12064345)
LAP1_N and LAP1_C domain-containing protein
List of domain hits
Name | Accession | Description | Interval | E-value | ||||
LAP1_C | pfam05609 | Lamina-associated polypeptide 1, AAA+ activator domain; Torsin-1A-interacting proteins 1 and 2 ... |
237-469 | 2.03e-170 | ||||
Lamina-associated polypeptide 1, AAA+ activator domain; Torsin-1A-interacting proteins 1 and 2 (TOIP 1/2), also known as LAP1 proteins (Lamina-associated polypeptide 1) are type 2 integral membrane proteins with a single membrane-spanning region of the inner nuclear membrane. These proteins interact with and activate Torsin A, an AAA+ ATPase localized to the endoplasmic reticulum (ER) through a perinuclear domain and forms a heterohexameric (LAP1-Torsin)3 ring that targets Torsin to the nuclear envelope. LAP1 has an atypical AAA+ fold and provides an arginine finger to the Torsin A active site to promote its ATPase activity. A single mutation in Torsin A causes early onset primary dystonia, a painful and severely disabling neuromuscular disease. This entry represents the C-terminal AAA+ activator domain of LAP1. : Pssm-ID: 461691 Cd Length: 233 Bit Score: 478.51 E-value: 2.03e-170
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LAP1_N | pfam20443 | Lamina-associated polypeptide 1, N-terminal; Torsin-1A-interacting proteins 1 and 2 (TOIP 1/2) ... |
1-220 | 5.84e-88 | ||||
Lamina-associated polypeptide 1, N-terminal; Torsin-1A-interacting proteins 1 and 2 (TOIP 1/2) also known as LAP1 proteins (Lamina-associated polypeptide 1) are type 2 integral membrane proteins with a single membrane-spanning region of the inner nuclear membrane. These proteins interact with and activate Torsin A, an AAA+ ATPase localized to the endoplasmic reticulum (ER) through a perinuclear domain, and forms a heterohexameric (LAP1-Torsin)3 ring that targets Torsin to the nuclear envelope. LAP1 has an atypical AAA+ fold and provides an arginine finger to the Torsin A active site to promote its ATPase activity. A single mutation in Torsin A causes early onset primary dystonia, a painful and severely disabling neuromuscular disease. This entry represents the N-terminal domain of LAP1 which contains transmembrane helices. : Pssm-ID: 466592 Cd Length: 238 Bit Score: 268.62 E-value: 5.84e-88
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Name | Accession | Description | Interval | E-value | ||||
LAP1_C | pfam05609 | Lamina-associated polypeptide 1, AAA+ activator domain; Torsin-1A-interacting proteins 1 and 2 ... |
237-469 | 2.03e-170 | ||||
Lamina-associated polypeptide 1, AAA+ activator domain; Torsin-1A-interacting proteins 1 and 2 (TOIP 1/2), also known as LAP1 proteins (Lamina-associated polypeptide 1) are type 2 integral membrane proteins with a single membrane-spanning region of the inner nuclear membrane. These proteins interact with and activate Torsin A, an AAA+ ATPase localized to the endoplasmic reticulum (ER) through a perinuclear domain and forms a heterohexameric (LAP1-Torsin)3 ring that targets Torsin to the nuclear envelope. LAP1 has an atypical AAA+ fold and provides an arginine finger to the Torsin A active site to promote its ATPase activity. A single mutation in Torsin A causes early onset primary dystonia, a painful and severely disabling neuromuscular disease. This entry represents the C-terminal AAA+ activator domain of LAP1. Pssm-ID: 461691 Cd Length: 233 Bit Score: 478.51 E-value: 2.03e-170
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LAP1_N | pfam20443 | Lamina-associated polypeptide 1, N-terminal; Torsin-1A-interacting proteins 1 and 2 (TOIP 1/2) ... |
1-220 | 5.84e-88 | ||||
Lamina-associated polypeptide 1, N-terminal; Torsin-1A-interacting proteins 1 and 2 (TOIP 1/2) also known as LAP1 proteins (Lamina-associated polypeptide 1) are type 2 integral membrane proteins with a single membrane-spanning region of the inner nuclear membrane. These proteins interact with and activate Torsin A, an AAA+ ATPase localized to the endoplasmic reticulum (ER) through a perinuclear domain, and forms a heterohexameric (LAP1-Torsin)3 ring that targets Torsin to the nuclear envelope. LAP1 has an atypical AAA+ fold and provides an arginine finger to the Torsin A active site to promote its ATPase activity. A single mutation in Torsin A causes early onset primary dystonia, a painful and severely disabling neuromuscular disease. This entry represents the N-terminal domain of LAP1 which contains transmembrane helices. Pssm-ID: 466592 Cd Length: 238 Bit Score: 268.62 E-value: 5.84e-88
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Name | Accession | Description | Interval | E-value | ||||
LAP1_C | pfam05609 | Lamina-associated polypeptide 1, AAA+ activator domain; Torsin-1A-interacting proteins 1 and 2 ... |
237-469 | 2.03e-170 | ||||
Lamina-associated polypeptide 1, AAA+ activator domain; Torsin-1A-interacting proteins 1 and 2 (TOIP 1/2), also known as LAP1 proteins (Lamina-associated polypeptide 1) are type 2 integral membrane proteins with a single membrane-spanning region of the inner nuclear membrane. These proteins interact with and activate Torsin A, an AAA+ ATPase localized to the endoplasmic reticulum (ER) through a perinuclear domain and forms a heterohexameric (LAP1-Torsin)3 ring that targets Torsin to the nuclear envelope. LAP1 has an atypical AAA+ fold and provides an arginine finger to the Torsin A active site to promote its ATPase activity. A single mutation in Torsin A causes early onset primary dystonia, a painful and severely disabling neuromuscular disease. This entry represents the C-terminal AAA+ activator domain of LAP1. Pssm-ID: 461691 Cd Length: 233 Bit Score: 478.51 E-value: 2.03e-170
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LAP1_N | pfam20443 | Lamina-associated polypeptide 1, N-terminal; Torsin-1A-interacting proteins 1 and 2 (TOIP 1/2) ... |
1-220 | 5.84e-88 | ||||
Lamina-associated polypeptide 1, N-terminal; Torsin-1A-interacting proteins 1 and 2 (TOIP 1/2) also known as LAP1 proteins (Lamina-associated polypeptide 1) are type 2 integral membrane proteins with a single membrane-spanning region of the inner nuclear membrane. These proteins interact with and activate Torsin A, an AAA+ ATPase localized to the endoplasmic reticulum (ER) through a perinuclear domain, and forms a heterohexameric (LAP1-Torsin)3 ring that targets Torsin to the nuclear envelope. LAP1 has an atypical AAA+ fold and provides an arginine finger to the Torsin A active site to promote its ATPase activity. A single mutation in Torsin A causes early onset primary dystonia, a painful and severely disabling neuromuscular disease. This entry represents the N-terminal domain of LAP1 which contains transmembrane helices. Pssm-ID: 466592 Cd Length: 238 Bit Score: 268.62 E-value: 5.84e-88
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Blast search parameters | ||||
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