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Conserved domains on  [gi|1958760169|ref|XP_038960324|]
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torsin-1A isoform X1 [Rattus norvegicus]

Protein Classification

Torsin domain-containing protein( domain architecture ID 10533689)

Torsin domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Torsin pfam06309
Torsin; This family consists of several eukaryotic torsin proteins. Torsion dystonia is an ...
 56-170 6.26e-66

Torsin; This family consists of several eukaryotic torsin proteins. Torsion dystonia is an autosomal dominant movement disorder characterized by involuntary, repetitive muscle contractions and twisted postures. The most severe early-onset form of dystonia has been linked to mutations in the human DYT1 (TOR1A) gene encoding a protein termed torsinA. While causative genetic alterations have been identified, the function of torsin proteins and the molecular mechanism underlying dystonia remain unknown. Phylogenetic analysis of the torsin protein family indicates these proteins share distant sequence similarity with the large and diverse family of (pfam00004) proteins. It has been suggested that torsins play a role in effectively managing protein folding and that possible breakdown in a neuroprotective mechanism that is, in part, mediated by torsins may be responsible for the neuronal dysfunction associated with dystonia.


:

Pssm-ID: 399367 [Multi-domain]  Cd Length: 120  Bit Score: 200.26  E-value: 6.26e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760169  56 SLSREALQKDLDNKLFGQHLAKRVILNAVSGFLSNPKPKKPLTLSLHGWTGTGKNFASKIIAENIYEGGLNSDYVHLFVA 135
Cdd:pfam06309   6 SFNYTGLERDLARRLFGQHLVKQLVVRSVKGHWENPKPRKPLVLSFHGWTGTGKNFVAEIIADNLYRDGLRSDYVHHFVA 85

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958760169 136 TLHFPHASNITLYKDQLQMWIRGNVSACARSIFIF 170
Cdd:pfam06309  86 TFHFPHPKYVELYKVELKNQIRGTLRACHRSIFIF 120
 
Name Accession Description Interval E-value
Torsin pfam06309
Torsin; This family consists of several eukaryotic torsin proteins. Torsion dystonia is an ...
 56-170 6.26e-66

Torsin; This family consists of several eukaryotic torsin proteins. Torsion dystonia is an autosomal dominant movement disorder characterized by involuntary, repetitive muscle contractions and twisted postures. The most severe early-onset form of dystonia has been linked to mutations in the human DYT1 (TOR1A) gene encoding a protein termed torsinA. While causative genetic alterations have been identified, the function of torsin proteins and the molecular mechanism underlying dystonia remain unknown. Phylogenetic analysis of the torsin protein family indicates these proteins share distant sequence similarity with the large and diverse family of (pfam00004) proteins. It has been suggested that torsins play a role in effectively managing protein folding and that possible breakdown in a neuroprotective mechanism that is, in part, mediated by torsins may be responsible for the neuronal dysfunction associated with dystonia.


Pssm-ID: 399367 [Multi-domain]  Cd Length: 120  Bit Score: 200.26  E-value: 6.26e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760169  56 SLSREALQKDLDNKLFGQHLAKRVILNAVSGFLSNPKPKKPLTLSLHGWTGTGKNFASKIIAENIYEGGLNSDYVHLFVA 135
Cdd:pfam06309   6 SFNYTGLERDLARRLFGQHLVKQLVVRSVKGHWENPKPRKPLVLSFHGWTGTGKNFVAEIIADNLYRDGLRSDYVHHFVA 85

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958760169 136 TLHFPHASNITLYKDQLQMWIRGNVSACARSIFIF 170
Cdd:pfam06309  86 TFHFPHPKYVELYKVELKNQIRGTLRACHRSIFIF 120
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 62-206 4.42e-05

Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and eukaryotic Heat shock protein 104 (Hsp104) are ATP-dependent molecular chaperones and essential proteins of the heat-shock response. ClpB/Hsp104 ATPases, in concert with the DnaK/Hsp70 chaperone system, disaggregate and reactivate aggregated proteins. This RecA-like_ClpB_Hsp104_like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 42.93  E-value: 4.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760169  62 LQKDLDNKLFGQHLAKRVILNAVSGF---LSNPKpKKPLTLSLHGWTGTGKNFASKIIAENIYEGGLN------SDYVHL 132
Cdd:cd19499     5 LEERLHERVVGQDEAVKAVSDAIRRAragLSDPN-RPIGSFLFLGPTGVGKTELAKALAELLFGDEDNliridmSEYMEK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760169 133 FVATLHFPHASNITLY--KDQLQMWIRGNvsacARSIFIFDEMDKMHAGLIDAIKPFLDYYDVVD----EVSYQKAIFIF 206
Cdd:cd19499    84 HSVSRLIGAPPGYVGYteGGQLTEAVRRK----PYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDshgrTVDFKNTIIIM 159
 
Name Accession Description Interval E-value
Torsin pfam06309
Torsin; This family consists of several eukaryotic torsin proteins. Torsion dystonia is an ...
 56-170 6.26e-66

Torsin; This family consists of several eukaryotic torsin proteins. Torsion dystonia is an autosomal dominant movement disorder characterized by involuntary, repetitive muscle contractions and twisted postures. The most severe early-onset form of dystonia has been linked to mutations in the human DYT1 (TOR1A) gene encoding a protein termed torsinA. While causative genetic alterations have been identified, the function of torsin proteins and the molecular mechanism underlying dystonia remain unknown. Phylogenetic analysis of the torsin protein family indicates these proteins share distant sequence similarity with the large and diverse family of (pfam00004) proteins. It has been suggested that torsins play a role in effectively managing protein folding and that possible breakdown in a neuroprotective mechanism that is, in part, mediated by torsins may be responsible for the neuronal dysfunction associated with dystonia.


Pssm-ID: 399367 [Multi-domain]  Cd Length: 120  Bit Score: 200.26  E-value: 6.26e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760169  56 SLSREALQKDLDNKLFGQHLAKRVILNAVSGFLSNPKPKKPLTLSLHGWTGTGKNFASKIIAENIYEGGLNSDYVHLFVA 135
Cdd:pfam06309   6 SFNYTGLERDLARRLFGQHLVKQLVVRSVKGHWENPKPRKPLVLSFHGWTGTGKNFVAEIIADNLYRDGLRSDYVHHFVA 85

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958760169 136 TLHFPHASNITLYKDQLQMWIRGNVSACARSIFIF 170
Cdd:pfam06309  86 TFHFPHPKYVELYKVELKNQIRGTLRACHRSIFIF 120
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 62-206 4.42e-05

Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and eukaryotic Heat shock protein 104 (Hsp104) are ATP-dependent molecular chaperones and essential proteins of the heat-shock response. ClpB/Hsp104 ATPases, in concert with the DnaK/Hsp70 chaperone system, disaggregate and reactivate aggregated proteins. This RecA-like_ClpB_Hsp104_like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 42.93  E-value: 4.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760169  62 LQKDLDNKLFGQHLAKRVILNAVSGF---LSNPKpKKPLTLSLHGWTGTGKNFASKIIAENIYEGGLN------SDYVHL 132
Cdd:cd19499     5 LEERLHERVVGQDEAVKAVSDAIRRAragLSDPN-RPIGSFLFLGPTGVGKTELAKALAELLFGDEDNliridmSEYMEK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760169 133 FVATLHFPHASNITLY--KDQLQMWIRGNvsacARSIFIFDEMDKMHAGLIDAIKPFLDYYDVVD----EVSYQKAIFIF 206
Cdd:cd19499    84 HSVSRLIGAPPGYVGYteGGQLTEAVRRK----PYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDshgrTVDFKNTIIIM 159
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 80-215 4.23e-03

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 36.74  E-value: 4.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958760169  80 ILNAVSGFLSNPKPKKPLtlsLHGWTGTGKNFASKIIAENIYEGGLNSDYV--HLFVATLHFPHASNITLYKDQlqmwiR 157
Cdd:cd00009     6 AIEALREALELPPPKNLL---LYGPPGTGKTTLARAIANELFRPGAPFLYLnaSDLLEGLVVAELFGHFLVRLL-----F 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958760169 158 GNVSACARSIFIFDEMDKMHAGLIDAIKPFLDYYdVVDEVSYQKAIFIFLRGRKDHRR 215
Cdd:cd00009    78 ELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETL-NDLRIDRENVRVIGATNRPLLGD 134
 
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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