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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601130454  42 ECDFWPDLPGLECDLAQHLAGQHLAKALVVKSLKAFVQDPAPSKPLVLSLHGWTGTGKSYVSSLLAQHLFRDGLRSPHVH 121
Cdd:pfam06309   2 DCRISFNYTGLERDLARRLFGQHLVKQLVVRSVKGHWENPKPRKPLVLSFHGWTGTGKNFVAEIIADNLYRDGLRSDYVH 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1601130454 122 HFSPIIHFPHPSRTEQYKKELKSWVQGNLTACGRSLFLF 160
Cdd:pfam06309  82 HFVATFHFPHPKYVELYKVELKNQIRGTLRACHRSIFIF 120

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601130454  42 ECDFWPDLPGLECDLAQHLAGQHLAKALVVKSLKAFVQDPAPSKPLVLSLHGWTGTGKSYVSSLLAQHLFRDGLRSPHVH 121
Cdd:pfam06309   2 DCRISFNYTGLERDLARRLFGQHLVKQLVVRSVKGHWENPKPRKPLVLSFHGWTGTGKNFVAEIIADNLYRDGLRSDYVH 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1601130454 122 HFSPIIHFPHPSRTEQYKKELKSWVQGNLTACGRSLFLF 160
Cdd:pfam06309  82 HFVATFHFPHPKYVELYKVELKNQIRGTLRACHRSIFIF 120

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601130454   85 KPLVLSLHGWTGTGKSYVSSLLAQHLFRDGLR------------SPHVHHFSPIIHFPHPSRTEQYKKELKSWVQgnltA 152
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGviyidgedileeVLDQLLLIIVGGKKASGSGELRLRLALALAR----K 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1601130454  153 CGRSLFLFDEMDKLPPGLMEVLQPFLGPSWVVYGTNYRKAIFIFI 197
Cdd:smart00382  77 LKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVIL 121

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601130454  42 ECDFWPDLPGLECDLAQHLAGQHLAKALVVKSLKAFVQDPAPSKPLVLSLHGWTGTGKSYVSSLLAQHLFRDGLRSPHVH 121
Cdd:pfam06309   2 DCRISFNYTGLERDLARRLFGQHLVKQLVVRSVKGHWENPKPRKPLVLSFHGWTGTGKNFVAEIIADNLYRDGLRSDYVH 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1601130454 122 HFSPIIHFPHPSRTEQYKKELKSWVQGNLTACGRSLFLF 160
Cdd:pfam06309  82 HFVATFHFPHPKYVELYKVELKNQIRGTLRACHRSIFIF 120

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601130454  61 AGQHLAKALVVKSLKAfvqdpaPSKPLVLsLHGWTGTGKSYVSSLLAQHLFRDGLrsphvhhfsPIIHFPHPSRTEQYKK 140
Cdd:cd00009     1 VGQEEAIEALREALEL------PPPKNLL-LYGPPGTGKTTLARAIANELFRPGA---------PFLYLNASDLLEGLVV 64

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1601130454 141 ELKSWV------QGNLTACGRSLFLFDEMDKLPPGLMEVLQPFL 178
Cdd:cd00009    65 AELFGHflvrllFELAEKAKPGVLFIDEIDSLSRGAQNALLRVL 108