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Conserved domains on  [gi|57527353|ref|NP_001009683|]
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torsin-3A precursor [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 ...
 113-232 9.65e-72

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: 220.29  E-value: 9.65e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57527353   113 GNCRISNNFTGLESDLRVRLHGQHLASKLVLEAVKGYLEMPQVGKALALSFHGWSGTGKNFVARMLVDNLYRDGMRSDCV 192
Cdd:pfam06309   1 GDCRISFNYTGLERDLARRLFGQHLVKQLVVRSVKGHWENPKPRKPLVLSFHGWTGTGKNFVAEIIADNLYRDGLRSDYV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 57527353   193 KMFISTFHFPHPKYVDLYKEDLQRQMQETQRRCQQSTFVF 232
Cdd:pfam06309  81 HHFVATFHFPHPKYVELYKVELKNQIRGTLRACHRSIFIF 120
 
Name Accession Description Interval E-value
Torsin pfam06309
Torsin; This family consists of several eukaryotic torsin proteins. Torsion dystonia is an ...
 113-232 9.65e-72

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: 220.29  E-value: 9.65e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57527353   113 GNCRISNNFTGLESDLRVRLHGQHLASKLVLEAVKGYLEMPQVGKALALSFHGWSGTGKNFVARMLVDNLYRDGMRSDCV 192
Cdd:pfam06309   1 GDCRISFNYTGLERDLARRLFGQHLVKQLVVRSVKGHWENPKPRKPLVLSFHGWTGTGKNFVAEIIADNLYRDGLRSDYV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 57527353   193 KMFISTFHFPHPKYVDLYKEDLQRQMQETQRRCQQSTFVF 232
Cdd:pfam06309  81 HHFVATFHFPHPKYVELYKVELKNQIRGTLRACHRSIFIF 120
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 120-240 6.07e-06

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: 46.40  E-value: 6.07e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57527353 120 NFTGLESDLRVRLHGQHLASKLVLEAVKGY--LEMPQVGKALALSFHGWSGTGKNFVARMLVDNLYRDGMRSDCVKMfiS 197
Cdd:cd19499   1 KLLNLEERLHERVVGQDEAVKAVSDAIRRAraGLSDPNRPIGSFLFLGPTGVGKTELAKALAELLFGDEDNLIRIDM--S 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 57527353 198 TFHFPH---------PKYVDlYKEdlQRQMQETQRRCQQSTFVFDEAEKLHP 240
Cdd:cd19499  79 EYMEKHsvsrligapPGYVG-YTE--GGQLTEAVRRKPYSVVLLDEIEKAHP 127
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 163-278 6.17e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 36.97  E-value: 6.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57527353    163 FHGWSGTGKNFVARMLVDNLYRDGMRS---DCVKMFISTFHFPHPKYVD-----LYKEDLQRQMQETQRRCQQSTFVFDE 234
Cdd:smart00382   7 IVGPPGSGKTTLARALARELGPPGGGViyiDGEDILEEVLDQLLLIIVGgkkasGSGELRLRLALALARKLKPDVLILDE 86

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 57527353    235 AEKLHPGLLELLEPYLEPRSPETHGAELPRAIFLLLSNLGGSVI 278
Cdd:smart00382  87 ITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLG 130
 
Name Accession Description Interval E-value
Torsin pfam06309
Torsin; This family consists of several eukaryotic torsin proteins. Torsion dystonia is an ...
 113-232 9.65e-72

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: 220.29  E-value: 9.65e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57527353   113 GNCRISNNFTGLESDLRVRLHGQHLASKLVLEAVKGYLEMPQVGKALALSFHGWSGTGKNFVARMLVDNLYRDGMRSDCV 192
Cdd:pfam06309   1 GDCRISFNYTGLERDLARRLFGQHLVKQLVVRSVKGHWENPKPRKPLVLSFHGWTGTGKNFVAEIIADNLYRDGLRSDYV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 57527353   193 KMFISTFHFPHPKYVDLYKEDLQRQMQETQRRCQQSTFVF 232
Cdd:pfam06309  81 HHFVATFHFPHPKYVELYKVELKNQIRGTLRACHRSIFIF 120
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 120-240 6.07e-06

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: 46.40  E-value: 6.07e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57527353 120 NFTGLESDLRVRLHGQHLASKLVLEAVKGY--LEMPQVGKALALSFHGWSGTGKNFVARMLVDNLYRDGMRSDCVKMfiS 197
Cdd:cd19499   1 KLLNLEERLHERVVGQDEAVKAVSDAIRRAraGLSDPNRPIGSFLFLGPTGVGKTELAKALAELLFGDEDNLIRIDM--S 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 57527353 198 TFHFPH---------PKYVDlYKEdlQRQMQETQRRCQQSTFVFDEAEKLHP 240
Cdd:cd19499  79 EYMEKHsvsrligapPGYVG-YTE--GGQLTEAVRRKPYSVVLLDEIEKAHP 127
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 163-278 6.17e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 36.97  E-value: 6.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57527353    163 FHGWSGTGKNFVARMLVDNLYRDGMRS---DCVKMFISTFHFPHPKYVD-----LYKEDLQRQMQETQRRCQQSTFVFDE 234
Cdd:smart00382   7 IVGPPGSGKTTLARALARELGPPGGGViyiDGEDILEEVLDQLLLIIVGgkkasGSGELRLRLALALARKLKPDVLILDE 86

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 57527353    235 AEKLHPGLLELLEPYLEPRSPETHGAELPRAIFLLLSNLGGSVI 278
Cdd:smart00382  87 ITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLG 130
 
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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