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Conserved domains on  [gi|1799990997|ref|XP_032016760|]
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torsin-1A-interacting protein 2 [Hylobates moloch]

Protein Classification

Graphical summary

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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 ...
 243-475 6.16e-175

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: 490.07  E-value: 6.16e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799990997 243 SYYSSPAQQVLKNPALEAFLAQFSRLKDSFPGQSSFLWQRGRKFLQKHLNASNPTEPATIIFTAAREGRETLKCLSHHVA 322
Cdd:pfam05609   1 SYYSSPAQQVPTNPALEAFLNQFSQLKDKFPGQSSFLWQRGRKFLQKHLNASHPTEPATIIFTAAREGRETLKCLSHHIA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799990997 323 RAYTSSQKVSPIQIDGAGRTWQDSDTVKLLVDLELSYGFENGQKAAVVHHFESFPAGSTLIFYKYCDHENAAFKDVALVL 402
Cdd:pfam05609  81 DAYTSSQKVSAIRIDGAGRALQDSDTVKLEVDQELSSGFENGQKAAVVHRFESLPAGSTLIFYKYCDHENAAFKDVALVL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799990997 403 TVLLEEETLEASVGPRETEEKVRDLLWAKFTNSDTPSSFNHMDSDKLSGLWSRISHLVLPVQPVKSIEEQGCL 475
Cdd:pfam05609 161 TVLLEEETLEASVGPRETEEKVRDLLWAKFTNSDTPSSFNHMDSDKLSGLWSRISHLVLPVQPVNAIEEGGCL 233
LAP1_N pfam20443
Lamina-associated polypeptide 1, N-terminal; Torsin-1A-interacting proteins 1 and 2 (TOIP 1/2) ...
 1-226 1.59e-89

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: 272.86  E-value: 1.59e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799990997   1 MADSGLREPQEDSQKDLENDPSiNSQAQETTIIASNAKEAQILH------------SACGLSKDHqRIETIGPESADTGD 68
Cdd:pfam20443   1 MTRRGLRDPPSSEQKDLEDEPS-SQTVQSQTVSKKTTERAQEPPvmsedpislcrpPLRSLRSDS-EVETNGPESADTGD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799990997  69 KSESPDEANVGkhpkDKIEDENKQSFLDGGKGHHLPSENVGEEPLDPDPSHSPSDKVGRADAHLGSSSVALPKEAsDGTG 148
Cdd:pfam20443  79 ASESPDEVNFS----DKTEHEEGESEQDDEDGHHSPSESLGEEKVDPDPSVSPSDQTGRADAQLGSSSWQLPESA-DFTA 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799990997 149 ASQEPPTtdSQEAQSPGHSSAGQEGEDTLRRRLLVPEAGSHPQQTQKLEEIKE-NAQDTMRQINEKSFWSHGPIFLFFL 226
Cdd:pfam20443 154 ASQEPSA--LSDSQSPKHSQEWVEQQDRLRRRLPAPEDGSHQQESELLNESPStSAQDTTRQPKKKSFVKYGSWWLLFL 230
 
Name Accession Description Interval E-value
LAP1_C pfam05609
Lamina-associated polypeptide 1, AAA+ activator domain; Torsin-1A-interacting proteins 1 and 2 ...
 243-475 6.16e-175

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: 490.07  E-value: 6.16e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799990997 243 SYYSSPAQQVLKNPALEAFLAQFSRLKDSFPGQSSFLWQRGRKFLQKHLNASNPTEPATIIFTAAREGRETLKCLSHHVA 322
Cdd:pfam05609   1 SYYSSPAQQVPTNPALEAFLNQFSQLKDKFPGQSSFLWQRGRKFLQKHLNASHPTEPATIIFTAAREGRETLKCLSHHIA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799990997 323 RAYTSSQKVSPIQIDGAGRTWQDSDTVKLLVDLELSYGFENGQKAAVVHHFESFPAGSTLIFYKYCDHENAAFKDVALVL 402
Cdd:pfam05609  81 DAYTSSQKVSAIRIDGAGRALQDSDTVKLEVDQELSSGFENGQKAAVVHRFESLPAGSTLIFYKYCDHENAAFKDVALVL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799990997 403 TVLLEEETLEASVGPRETEEKVRDLLWAKFTNSDTPSSFNHMDSDKLSGLWSRISHLVLPVQPVKSIEEQGCL 475
Cdd:pfam05609 161 TVLLEEETLEASVGPRETEEKVRDLLWAKFTNSDTPSSFNHMDSDKLSGLWSRISHLVLPVQPVNAIEEGGCL 233
LAP1_N pfam20443
Lamina-associated polypeptide 1, N-terminal; Torsin-1A-interacting proteins 1 and 2 (TOIP 1/2) ...
 1-226 1.59e-89

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: 272.86  E-value: 1.59e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799990997   1 MADSGLREPQEDSQKDLENDPSiNSQAQETTIIASNAKEAQILH------------SACGLSKDHqRIETIGPESADTGD 68
Cdd:pfam20443   1 MTRRGLRDPPSSEQKDLEDEPS-SQTVQSQTVSKKTTERAQEPPvmsedpislcrpPLRSLRSDS-EVETNGPESADTGD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799990997  69 KSESPDEANVGkhpkDKIEDENKQSFLDGGKGHHLPSENVGEEPLDPDPSHSPSDKVGRADAHLGSSSVALPKEAsDGTG 148
Cdd:pfam20443  79 ASESPDEVNFS----DKTEHEEGESEQDDEDGHHSPSESLGEEKVDPDPSVSPSDQTGRADAQLGSSSWQLPESA-DFTA 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799990997 149 ASQEPPTtdSQEAQSPGHSSAGQEGEDTLRRRLLVPEAGSHPQQTQKLEEIKE-NAQDTMRQINEKSFWSHGPIFLFFL 226
Cdd:pfam20443 154 ASQEPSA--LSDSQSPKHSQEWVEQQDRLRRRLPAPEDGSHQQESELLNESPStSAQDTTRQPKKKSFVKYGSWWLLFL 230
 
Name Accession Description Interval E-value
LAP1_C pfam05609
Lamina-associated polypeptide 1, AAA+ activator domain; Torsin-1A-interacting proteins 1 and 2 ...
 243-475 6.16e-175

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: 490.07  E-value: 6.16e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799990997 243 SYYSSPAQQVLKNPALEAFLAQFSRLKDSFPGQSSFLWQRGRKFLQKHLNASNPTEPATIIFTAAREGRETLKCLSHHVA 322
Cdd:pfam05609   1 SYYSSPAQQVPTNPALEAFLNQFSQLKDKFPGQSSFLWQRGRKFLQKHLNASHPTEPATIIFTAAREGRETLKCLSHHIA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799990997 323 RAYTSSQKVSPIQIDGAGRTWQDSDTVKLLVDLELSYGFENGQKAAVVHHFESFPAGSTLIFYKYCDHENAAFKDVALVL 402
Cdd:pfam05609  81 DAYTSSQKVSAIRIDGAGRALQDSDTVKLEVDQELSSGFENGQKAAVVHRFESLPAGSTLIFYKYCDHENAAFKDVALVL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1799990997 403 TVLLEEETLEASVGPRETEEKVRDLLWAKFTNSDTPSSFNHMDSDKLSGLWSRISHLVLPVQPVKSIEEQGCL 475
Cdd:pfam05609 161 TVLLEEETLEASVGPRETEEKVRDLLWAKFTNSDTPSSFNHMDSDKLSGLWSRISHLVLPVQPVNAIEEGGCL 233
LAP1_N pfam20443
Lamina-associated polypeptide 1, N-terminal; Torsin-1A-interacting proteins 1 and 2 (TOIP 1/2) ...
 1-226 1.59e-89

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: 272.86  E-value: 1.59e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799990997   1 MADSGLREPQEDSQKDLENDPSiNSQAQETTIIASNAKEAQILH------------SACGLSKDHqRIETIGPESADTGD 68
Cdd:pfam20443   1 MTRRGLRDPPSSEQKDLEDEPS-SQTVQSQTVSKKTTERAQEPPvmsedpislcrpPLRSLRSDS-EVETNGPESADTGD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799990997  69 KSESPDEANVGkhpkDKIEDENKQSFLDGGKGHHLPSENVGEEPLDPDPSHSPSDKVGRADAHLGSSSVALPKEAsDGTG 148
Cdd:pfam20443  79 ASESPDEVNFS----DKTEHEEGESEQDDEDGHHSPSESLGEEKVDPDPSVSPSDQTGRADAQLGSSSWQLPESA-DFTA 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799990997 149 ASQEPPTtdSQEAQSPGHSSAGQEGEDTLRRRLLVPEAGSHPQQTQKLEEIKE-NAQDTMRQINEKSFWSHGPIFLFFL 226
Cdd:pfam20443 154 ASQEPSA--LSDSQSPKHSQEWVEQQDRLRRRLPAPEDGSHQQESELLNESPStSAQDTTRQPKKKSFVKYGSWWLLFL 230
Mucin-like pfam16058
Mucin-like; This region is found repeated at the C-terminus (C-tail) of bile salt-activated ...
 96-175 1.47e-04

Mucin-like; This region is found repeated at the C-terminus (C-tail) of bile salt-activated lipase, where is O-glycosylated. This region is composed of biased amino acid composition that is likely to be disordered. The region contains many repeats of an approximately 11 residue degenerate repeat.


Pssm-ID: 464997 [Multi-domain]  Cd Length: 94  Bit Score: 40.87  E-value: 1.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799990997  96 DGGKGHHLPSENVGEEPLDP-----DPSHSPSDKVGRADAHLGSSSVALPKEASDGTGASQEPPTTDSQEAQSPGHSSAG 170
Cdd:pfam16058   4 SITEPPRDPSGSYGEPPRAPsssytEPQRDPSSSITEPPADPSSSYTEPPRDPSGSYTEPQRDPSSSSTEPQRDPSSSIT 83


                  ....*
gi 1799990997 171 QEGED 175
Cdd:pfam16058  84 EPPRD 88
 
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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