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Conserved domains on  [gi|1842154689|ref|XP_034369539|]
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torsin-1A-interacting protein 1 [Arvicanthis niloticus]

Protein Classification

LAP1_N and LAP1_C domain-containing protein( domain architecture ID 12064345)

LAP1_N and LAP1_C domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LAP1_C super family cl28753
Lamina-associated polypeptide 1, AAA+ activator domain; Torsin-1A-interacting proteins 1 and 2 ...
 367-597 4.55e-150

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.


The actual alignment was detected with superfamily member pfam05609:

Pssm-ID: 461691  Cd Length: 233  Bit Score: 431.52  E-value: 4.55e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842154689 367 WFFHTPA--VETT-AVQEFQNQMKELQSKYQSQNEKLWKRGTTFLEKHLNSSLPrPQPAVLLLTAAQDAAEALKCLSEQI 443
Cdd:pfam05609   1 SYYSSPAqqVPTNpALEAFLNQFSQLKDKFPGQSSFLWQRGRKFLQKHLNASHP-TEPATIIFTAAREGRETLKCLSHHI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842154689 444 ADAYSSFRSVRAIRIDGAGKAAQDSDLVKHEVDQELTDGFTNGQNAAVVHRFESLPAGSTLIFYKYCDHENAAFKDVALV 523
Cdd:pfam05609  80 ADAYTSSQKVSAIRIDGAGRALQDSDTVKLEVDQELSSGFENGQKAAVVHRFESLPAGSTLIFYKYCDHENAAFKDVALV 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1842154689 524 LTVLLEEKTLEASLGLKEIEEKVRDFLKVKFTSSSSASSYNHMDPDKLNGLWSRISHLVLPVQPENALKAGSCL 597
Cdd:pfam05609 160 LTVLLEEETLEASVGPRETEEKVRDLLWAKFTNSDTPSSFNHMDSDKLSGLWSRISHLVLPVQPVNAIEEGGCL 233
LAP1_N pfam20443
Lamina-associated polypeptide 1, N-terminal; Torsin-1A-interacting proteins 1 and 2 (TOIP 1/2) ...
 145-364 7.70e-76

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: 241.27  E-value: 7.70e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842154689 145 TSGRGLQDSQSSSEDRGEDEPSSQPVTSQTASKKTV-RTPETSVMSEDPISnLCRPPLRSPRPDSTYQTNGNATMNEREA 223
Cdd:pfam20443   1 MTRRGLRDPPSSEQKDLEDEPSSQTVQSQTVSKKTTeRAQEPPVMSEDPIS-LCRPPLRSLRSDSEVETNGPESADTGDA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842154689 224 TVVQQ-VNFF-----EEGETEDDLESSYSD-----VTLRVRSRESLESRDEAAQAAGHHPESPWGLPHSQDFPAHENQPS 292
Cdd:pfam20443  80 SESPDeVNFSdktehEEGESEQDDEDGHHSpseslGEEKVDPDPSVSPSDQTGRADAQLGSSSWQLPESADFTAASQEPS 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1842154689 293 LLT-SGCQKNPQEWVNQAIRMRARM----AYNNIQKSDFGNQSSSTSRQQAAVQPPNESSVKIKWWLLG--LVAILAMG 364
Cdd:pfam20443 160 ALSdSQSPKHSQEWVEQQDRLRRRLpapeDGSHQQESELLNESPSTSAQDTTRQPKKKSFVKYGSWWLLflVIALLALG 238
 
Name Accession Description Interval E-value
LAP1_C pfam05609
Lamina-associated polypeptide 1, AAA+ activator domain; Torsin-1A-interacting proteins 1 and 2 ...
 367-597 4.55e-150

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: 431.52  E-value: 4.55e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842154689 367 WFFHTPA--VETT-AVQEFQNQMKELQSKYQSQNEKLWKRGTTFLEKHLNSSLPrPQPAVLLLTAAQDAAEALKCLSEQI 443
Cdd:pfam05609   1 SYYSSPAqqVPTNpALEAFLNQFSQLKDKFPGQSSFLWQRGRKFLQKHLNASHP-TEPATIIFTAAREGRETLKCLSHHI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842154689 444 ADAYSSFRSVRAIRIDGAGKAAQDSDLVKHEVDQELTDGFTNGQNAAVVHRFESLPAGSTLIFYKYCDHENAAFKDVALV 523
Cdd:pfam05609  80 ADAYTSSQKVSAIRIDGAGRALQDSDTVKLEVDQELSSGFENGQKAAVVHRFESLPAGSTLIFYKYCDHENAAFKDVALV 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1842154689 524 LTVLLEEKTLEASLGLKEIEEKVRDFLKVKFTSSSSASSYNHMDPDKLNGLWSRISHLVLPVQPENALKAGSCL 597
Cdd:pfam05609 160 LTVLLEEETLEASVGPRETEEKVRDLLWAKFTNSDTPSSFNHMDSDKLSGLWSRISHLVLPVQPVNAIEEGGCL 233
LAP1_N pfam20443
Lamina-associated polypeptide 1, N-terminal; Torsin-1A-interacting proteins 1 and 2 (TOIP 1/2) ...
 145-364 7.70e-76

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: 241.27  E-value: 7.70e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842154689 145 TSGRGLQDSQSSSEDRGEDEPSSQPVTSQTASKKTV-RTPETSVMSEDPISnLCRPPLRSPRPDSTYQTNGNATMNEREA 223
Cdd:pfam20443   1 MTRRGLRDPPSSEQKDLEDEPSSQTVQSQTVSKKTTeRAQEPPVMSEDPIS-LCRPPLRSLRSDSEVETNGPESADTGDA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842154689 224 TVVQQ-VNFF-----EEGETEDDLESSYSD-----VTLRVRSRESLESRDEAAQAAGHHPESPWGLPHSQDFPAHENQPS 292
Cdd:pfam20443  80 SESPDeVNFSdktehEEGESEQDDEDGHHSpseslGEEKVDPDPSVSPSDQTGRADAQLGSSSWQLPESADFTAASQEPS 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1842154689 293 LLT-SGCQKNPQEWVNQAIRMRARM----AYNNIQKSDFGNQSSSTSRQQAAVQPPNESSVKIKWWLLG--LVAILAMG 364
Cdd:pfam20443 160 ALSdSQSPKHSQEWVEQQDRLRRRLpapeDGSHQQESELLNESPSTSAQDTTRQPKKKSFVKYGSWWLLflVIALLALG 238
 
Name Accession Description Interval E-value
LAP1_C pfam05609
Lamina-associated polypeptide 1, AAA+ activator domain; Torsin-1A-interacting proteins 1 and 2 ...
 367-597 4.55e-150

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: 431.52  E-value: 4.55e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842154689 367 WFFHTPA--VETT-AVQEFQNQMKELQSKYQSQNEKLWKRGTTFLEKHLNSSLPrPQPAVLLLTAAQDAAEALKCLSEQI 443
Cdd:pfam05609   1 SYYSSPAqqVPTNpALEAFLNQFSQLKDKFPGQSSFLWQRGRKFLQKHLNASHP-TEPATIIFTAAREGRETLKCLSHHI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842154689 444 ADAYSSFRSVRAIRIDGAGKAAQDSDLVKHEVDQELTDGFTNGQNAAVVHRFESLPAGSTLIFYKYCDHENAAFKDVALV 523
Cdd:pfam05609  80 ADAYTSSQKVSAIRIDGAGRALQDSDTVKLEVDQELSSGFENGQKAAVVHRFESLPAGSTLIFYKYCDHENAAFKDVALV 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1842154689 524 LTVLLEEKTLEASLGLKEIEEKVRDFLKVKFTSSSSASSYNHMDPDKLNGLWSRISHLVLPVQPENALKAGSCL 597
Cdd:pfam05609 160 LTVLLEEETLEASVGPRETEEKVRDLLWAKFTNSDTPSSFNHMDSDKLSGLWSRISHLVLPVQPVNAIEEGGCL 233
LAP1_N pfam20443
Lamina-associated polypeptide 1, N-terminal; Torsin-1A-interacting proteins 1 and 2 (TOIP 1/2) ...
 145-364 7.70e-76

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: 241.27  E-value: 7.70e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842154689 145 TSGRGLQDSQSSSEDRGEDEPSSQPVTSQTASKKTV-RTPETSVMSEDPISnLCRPPLRSPRPDSTYQTNGNATMNEREA 223
Cdd:pfam20443   1 MTRRGLRDPPSSEQKDLEDEPSSQTVQSQTVSKKTTeRAQEPPVMSEDPIS-LCRPPLRSLRSDSEVETNGPESADTGDA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842154689 224 TVVQQ-VNFF-----EEGETEDDLESSYSD-----VTLRVRSRESLESRDEAAQAAGHHPESPWGLPHSQDFPAHENQPS 292
Cdd:pfam20443  80 SESPDeVNFSdktehEEGESEQDDEDGHHSpseslGEEKVDPDPSVSPSDQTGRADAQLGSSSWQLPESADFTAASQEPS 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1842154689 293 LLT-SGCQKNPQEWVNQAIRMRARM----AYNNIQKSDFGNQSSSTSRQQAAVQPPNESSVKIKWWLLG--LVAILAMG 364
Cdd:pfam20443 160 ALSdSQSPKHSQEWVEQQDRLRRRLpapeDGSHQQESELLNESPSTSAQDTTRQPKKKSFVKYGSWWLLflVIALLALG 238
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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