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Conserved domains on  [gi|85861170|ref|NP_001034286|]
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torsin-1B precursor [Rattus norvegicus]

Protein Classification

P-loop NTPase family protein( domain architecture ID 1562424)

P-loop NTPase (nucleoside triphosphate hydrolase) family protein contains two conserved sequence signatures, the Walker A motif (the P-loop proper) and Walker B motif which bind, respectively, the beta and gamma phosphate moieties of the bound nucleotide (typically ATP or GTP), and a Mg(2+) cation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
 62-176 4.01e-53

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member pfam06309:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 120  Bit Score: 170.60  E-value: 4.01e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85861170    62 PLNTSALKLDLEEKLFGQHLATEVILKALTGFRNNKNPKKPLTLSLHGWAGTGKNFVSQIVAENLYPKGLKSNFVHLFVS 141
Cdd:pfam06309   6 SFNYTGLERDLARRLFGQHLVKQLVVRSVKGHWENPKPRKPLVLSFHGWTGTGKNFVAEIIADNLYRDGLRSDYVHHFVA 85

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 85861170   142 TLHFPHEQKIKLYQDQLQKWIRGNVSACGSSVFIF 176
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 ...
 62-176 4.01e-53

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: 170.60  E-value: 4.01e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85861170    62 PLNTSALKLDLEEKLFGQHLATEVILKALTGFRNNKNPKKPLTLSLHGWAGTGKNFVSQIVAENLYPKGLKSNFVHLFVS 141
Cdd:pfam06309   6 SFNYTGLERDLARRLFGQHLVKQLVVRSVKGHWENPKPRKPLVLSFHGWTGTGKNFVAEIIADNLYRDGLRSDYVHHFVA 85

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 85861170   142 TLHFPHEQKIKLYQDQLQKWIRGNVSACGSSVFIF 176
Cdd:pfam06309  86 TFHFPHPKYVELYKVELKNQIRGTLRACHRSIFIF 120
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 68-216 8.50e-08

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: 51.41  E-value: 8.50e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85861170  68 LKLDLEEKLFGQHLATEVILKALTGFRN-NKNPKKPLT-LSLHGWAGTGKNFVSQIVAENLYpkGLKSNFVHLFVSTLHF 145
Cdd:cd19499   5 LEERLHERVVGQDEAVKAVSDAIRRARAgLSDPNRPIGsFLFLGPTGVGKTELAKALAELLF--GDEDNLIRIDMSEYME 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85861170 146 PHEQKI----------KLYQDQLQKWIRGNvsacGSSVFIFDEMDKLHPGIIDAIKPFLDYYEQVDG----ISYRKAIFI 211
Cdd:cd19499  83 KHSVSRligappgyvgYTEGGQLTEAVRRK----PYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDShgrtVDFKNTIII 158


                ....*
gi 85861170 212 FLSNA 216
Cdd:cd19499 159 MTSNH 163
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 101-244 8.80e-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: 36.20  E-value: 8.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85861170    101 KPLTLSLHGWAGTGKNFVSQIVAENLYPKGLK--------SNFVHLFVSTLHFPHEQKIKLYQDQLQKWIRGNVSACGSS 172
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGviyidgedILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 85861170    173 VFIFDEMDKLHPGIIDAIKPFLDYYEQVDGISYRKAI-FIFLSNAGGDLITKTTLDfwragRKREEIQLKDLE 244
Cdd:smart00382  81 VLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLtVILTTNDEKDLGPALLRR-----RFDRRIVLLLIL 148
 
Name Accession Description Interval E-value
Torsin pfam06309
Torsin; This family consists of several eukaryotic torsin proteins. Torsion dystonia is an ...
 62-176 4.01e-53

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: 170.60  E-value: 4.01e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85861170    62 PLNTSALKLDLEEKLFGQHLATEVILKALTGFRNNKNPKKPLTLSLHGWAGTGKNFVSQIVAENLYPKGLKSNFVHLFVS 141
Cdd:pfam06309   6 SFNYTGLERDLARRLFGQHLVKQLVVRSVKGHWENPKPRKPLVLSFHGWTGTGKNFVAEIIADNLYRDGLRSDYVHHFVA 85

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 85861170   142 TLHFPHEQKIKLYQDQLQKWIRGNVSACGSSVFIF 176
Cdd:pfam06309  86 TFHFPHPKYVELYKVELKNQIRGTLRACHRSIFIF 120
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 68-216 8.50e-08

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: 51.41  E-value: 8.50e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85861170  68 LKLDLEEKLFGQHLATEVILKALTGFRN-NKNPKKPLT-LSLHGWAGTGKNFVSQIVAENLYpkGLKSNFVHLFVSTLHF 145
Cdd:cd19499   5 LEERLHERVVGQDEAVKAVSDAIRRARAgLSDPNRPIGsFLFLGPTGVGKTELAKALAELLF--GDEDNLIRIDMSEYME 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85861170 146 PHEQKI----------KLYQDQLQKWIRGNvsacGSSVFIFDEMDKLHPGIIDAIKPFLDYYEQVDG----ISYRKAIFI 211
Cdd:cd19499  83 KHSVSRligappgyvgYTEGGQLTEAVRRK----PYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDShgrtVDFKNTIII 158


                ....*
gi 85861170 212 FLSNA 216
Cdd:cd19499 159 MTSNH 163
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 77-215 4.18e-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: 37.13  E-value: 4.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85861170  77 FGQHLATEVILKALtgfrnnKNPKKPLTLsLHGWAGTGKNFVSQIVAENLYPKGLKSNFVHLFVSTLHFPHEQKIKLYQD 156
Cdd:cd00009   1 VGQEEAIEALREAL------ELPPPKNLL-LYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHFLV 73

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 85861170 157 QLQKwirGNVSACGSSVFIFDEMDKLHPGIIDAIKPFLDYYEQvDGISYRKAIFIFLSN 215
Cdd:cd00009  74 RLLF---ELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLND-LRIDRENVRVIGATN 128
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 112-243 6.96e-03

AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 36.79  E-value: 6.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85861170   112 GTGKNFVSQIVAENLYpkGLKSNFVHLFVSTLHFPH-----EQK---IKLYQD--QLQKWIRGNvsacGSSVFIFDEMDK 181
Cdd:pfam07724  13 GVGKTELAKALAELLF--GDERALIRIDMSEYMEEHsvsrlIGAppgYVGYEEggQLTEAVRRK----PYSIVLIDEIEK 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 85861170   182 LHPGIIDAIKPFLDY------YEQVdgISYRKAIFIFLSNAGGDLItkttLDFWRAGRKREEIQLKDL 243
Cdd:pfam07724  87 AHPGVQNDLLQILEGgtltdkQGRT--VDFKNTLFIMTGNFGSEKI----SDASRLGDSPDYELLKEE 148
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 101-244 8.80e-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: 36.20  E-value: 8.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85861170    101 KPLTLSLHGWAGTGKNFVSQIVAENLYPKGLK--------SNFVHLFVSTLHFPHEQKIKLYQDQLQKWIRGNVSACGSS 172
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGviyidgedILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 85861170    173 VFIFDEMDKLHPGIIDAIKPFLDYYEQVDGISYRKAI-FIFLSNAGGDLITKTTLDfwragRKREEIQLKDLE 244
Cdd:smart00382  81 VLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLtVILTTNDEKDLGPALLRR-----RFDRRIVLLLIL 148
 
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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