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Conserved domains on  [gi|1034556008|ref|XP_016855965|]
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torsin-1A-interacting protein 2 isoform X2 [Homo sapiens]

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 pfam05609
Lamina-associated polypeptide 1, AAA+ activator domain; Torsin-1A-interacting proteins 1 and 2 ...
 31-263 0e+00

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: 507.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556008  31 SYYSSPAQQVPKNPALEAFLAQFSQLEDKFPGQSSFLWQRGRKFLQKHLNASNPTEPATIIFTAAREGRETLKCLSHHVA 110
Cdd:pfam05609   1 SYYSSPAQQVPTNPALEAFLNQFSQLKDKFPGQSSFLWQRGRKFLQKHLNASHPTEPATIIFTAAREGRETLKCLSHHIA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556008 111 DAYTSSQKVSPIQIDGAGRTWQDSDTVKLLVDLELSYGFENGQKAAVVHHFESFPAGSTLIFYKYCDHENAAFKDVALVL 190
Cdd:pfam05609  81 DAYTSSQKVSAIRIDGAGRALQDSDTVKLEVDQELSSGFENGQKAAVVHRFESLPAGSTLIFYKYCDHENAAFKDVALVL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034556008 191 TVLLEEETLEASVGPRETEEKVRDLLWAKFTNSDTPTSFNHMDSDKLSGLWSRISHLVLPVQPVSSIEEQGCL 263
Cdd:pfam05609 161 TVLLEEETLEASVGPRETEEKVRDLLWAKFTNSDTPSSFNHMDSDKLSGLWSRISHLVLPVQPVNAIEEGGCL 233
 
Name Accession Description Interval E-value
LAP1_C pfam05609
Lamina-associated polypeptide 1, AAA+ activator domain; Torsin-1A-interacting proteins 1 and 2 ...
 31-263 0e+00

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: 507.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556008  31 SYYSSPAQQVPKNPALEAFLAQFSQLEDKFPGQSSFLWQRGRKFLQKHLNASNPTEPATIIFTAAREGRETLKCLSHHVA 110
Cdd:pfam05609   1 SYYSSPAQQVPTNPALEAFLNQFSQLKDKFPGQSSFLWQRGRKFLQKHLNASHPTEPATIIFTAAREGRETLKCLSHHIA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556008 111 DAYTSSQKVSPIQIDGAGRTWQDSDTVKLLVDLELSYGFENGQKAAVVHHFESFPAGSTLIFYKYCDHENAAFKDVALVL 190
Cdd:pfam05609  81 DAYTSSQKVSAIRIDGAGRALQDSDTVKLEVDQELSSGFENGQKAAVVHRFESLPAGSTLIFYKYCDHENAAFKDVALVL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034556008 191 TVLLEEETLEASVGPRETEEKVRDLLWAKFTNSDTPTSFNHMDSDKLSGLWSRISHLVLPVQPVSSIEEQGCL 263
Cdd:pfam05609 161 TVLLEEETLEASVGPRETEEKVRDLLWAKFTNSDTPSSFNHMDSDKLSGLWSRISHLVLPVQPVNAIEEGGCL 233
 
Name Accession Description Interval E-value
LAP1_C pfam05609
Lamina-associated polypeptide 1, AAA+ activator domain; Torsin-1A-interacting proteins 1 and 2 ...
 31-263 0e+00

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: 507.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556008  31 SYYSSPAQQVPKNPALEAFLAQFSQLEDKFPGQSSFLWQRGRKFLQKHLNASNPTEPATIIFTAAREGRETLKCLSHHVA 110
Cdd:pfam05609   1 SYYSSPAQQVPTNPALEAFLNQFSQLKDKFPGQSSFLWQRGRKFLQKHLNASHPTEPATIIFTAAREGRETLKCLSHHIA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556008 111 DAYTSSQKVSPIQIDGAGRTWQDSDTVKLLVDLELSYGFENGQKAAVVHHFESFPAGSTLIFYKYCDHENAAFKDVALVL 190
Cdd:pfam05609  81 DAYTSSQKVSAIRIDGAGRALQDSDTVKLEVDQELSSGFENGQKAAVVHRFESLPAGSTLIFYKYCDHENAAFKDVALVL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034556008 191 TVLLEEETLEASVGPRETEEKVRDLLWAKFTNSDTPTSFNHMDSDKLSGLWSRISHLVLPVQPVSSIEEQGCL 263
Cdd:pfam05609 161 TVLLEEETLEASVGPRETEEKVRDLLWAKFTNSDTPSSFNHMDSDKLSGLWSRISHLVLPVQPVNAIEEGGCL 233
 
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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