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Conserved domains on  [gi|2024462873|ref|XP_040541704|]
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torsin-4A [Gallus gallus]

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 ...
 269-345 1.75e-13

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: 66.98  E-value: 1.75e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024462873 269 DLDGLEKTMHREVFGQKLAVESIMQLLKDYLATHIHNKPLVLSLNGPTGVGKSHVGWLLAKH-FRSVMDNDFVlQYFV 345
Cdd:pfam06309   8 NYTGLERDLARRLFGQHLVKQLVVRSVKGHWENPKPRKPLVLSFHGWTGTGKNFVAEIIADNlYRDGLRSDYV-HHFV 84
PRK10865 super family cl32594
ATP-dependent chaperone ClpB;
273-458 7.49e-03

ATP-dependent chaperone ClpB;


The actual alignment was detected with superfamily member PRK10865:

Pssm-ID: 182791 [Multi-domain]  Cd Length: 857  Bit Score: 39.06  E-value: 7.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024462873 273 LEKTMHREVFGQKLAVESIMQLLKDYLATHIH-NKPL--VLSLnGPTGVGKSHVGWLLAkHFRSVMDNDFV---LQYFVM 346
Cdd:PRK10865  562 MEQELHHRVIGQNEAVEAVSNAIRRSRAGLSDpNRPIgsFLFL-GPTGVGKTELCKALA-NFMFDSDDAMVridMSEFME 639

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024462873 347 HHCPS---GAAPLTCETDLSKKISDMVTRaeieEKIPLFILDEVELMSPVLLDTLSRFFE-------PNQTNEFLNAIYI 416
Cdd:PRK10865  640 KHSVSrlvGAPPGYVGYEEGGYLTEAVRR----RPYSVILLDEVEKAHPDVFNILLQVLDdgrltdgQGRTVDFRNTVVI 715

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2024462873 417 LISNIGggeitkfviqnasAELLQQRSGA---EELLSVIQPVLTH 458
Cdd:PRK10865  716 MTSNLG-------------SDLIQERFGEldyAHMKELVLGVVSH 747
 
Name Accession Description Interval E-value
Torsin pfam06309
Torsin; This family consists of several eukaryotic torsin proteins. Torsion dystonia is an ...
 269-345 1.75e-13

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: 66.98  E-value: 1.75e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024462873 269 DLDGLEKTMHREVFGQKLAVESIMQLLKDYLATHIHNKPLVLSLNGPTGVGKSHVGWLLAKH-FRSVMDNDFVlQYFV 345
Cdd:pfam06309   8 NYTGLERDLARRLFGQHLVKQLVVRSVKGHWENPKPRKPLVLSFHGWTGTGKNFVAEIIADNlYRDGLRSDYV-HHFV 84
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 269-320 2.90e-04

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: 41.78  E-value: 2.90e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2024462873 269 DLDGLEKTMHREVFGQKLAVESIMQLLKDYLA--THIHNKPLVLSLNGPTGVGK 320
Cdd:cd19499     1 KLLNLEERLHERVVGQDEAVKAVSDAIRRARAglSDPNRPIGSFLFLGPTGVGK 54
clpC CHL00095
Clp protease ATP binding subunit
 273-331 3.32e-03

Clp protease ATP binding subunit


Pssm-ID: 214361 [Multi-domain]  Cd Length: 821  Bit Score: 40.42  E-value: 3.32e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024462873 273 LEKTMHREVFGQKLAVESIMQLLKD-YLATHIHNKPLV-LSLNGPTGVGKSHVGWLLAKHF 331
Cdd:CHL00095  503 MEETLHKRIIGQDEAVVAVSKAIRRaRVGLKNPNRPIAsFLFSGPTGVGKTELTKALASYF 563
PRK10865 PRK10865
ATP-dependent chaperone ClpB;
273-458 7.49e-03

ATP-dependent chaperone ClpB;


Pssm-ID: 182791 [Multi-domain]  Cd Length: 857  Bit Score: 39.06  E-value: 7.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024462873 273 LEKTMHREVFGQKLAVESIMQLLKDYLATHIH-NKPL--VLSLnGPTGVGKSHVGWLLAkHFRSVMDNDFV---LQYFVM 346
Cdd:PRK10865  562 MEQELHHRVIGQNEAVEAVSNAIRRSRAGLSDpNRPIgsFLFL-GPTGVGKTELCKALA-NFMFDSDDAMVridMSEFME 639

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024462873 347 HHCPS---GAAPLTCETDLSKKISDMVTRaeieEKIPLFILDEVELMSPVLLDTLSRFFE-------PNQTNEFLNAIYI 416
Cdd:PRK10865  640 KHSVSrlvGAPPGYVGYEEGGYLTEAVRR----RPYSVILLDEVEKAHPDVFNILLQVLDdgrltdgQGRTVDFRNTVVI 715

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2024462873 417 LISNIGggeitkfviqnasAELLQQRSGA---EELLSVIQPVLTH 458
Cdd:PRK10865  716 MTSNLG-------------SDLIQERFGEldyAHMKELVLGVVSH 747
 
Name Accession Description Interval E-value
Torsin pfam06309
Torsin; This family consists of several eukaryotic torsin proteins. Torsion dystonia is an ...
 269-345 1.75e-13

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: 66.98  E-value: 1.75e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024462873 269 DLDGLEKTMHREVFGQKLAVESIMQLLKDYLATHIHNKPLVLSLNGPTGVGKSHVGWLLAKH-FRSVMDNDFVlQYFV 345
Cdd:pfam06309   8 NYTGLERDLARRLFGQHLVKQLVVRSVKGHWENPKPRKPLVLSFHGWTGTGKNFVAEIIADNlYRDGLRSDYV-HHFV 84
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 269-320 2.90e-04

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: 41.78  E-value: 2.90e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2024462873 269 DLDGLEKTMHREVFGQKLAVESIMQLLKDYLA--THIHNKPLVLSLNGPTGVGK 320
Cdd:cd19499     1 KLLNLEERLHERVVGQDEAVKAVSDAIRRARAglSDPNRPIGSFLFLGPTGVGK 54
clpC CHL00095
Clp protease ATP binding subunit
 273-331 3.32e-03

Clp protease ATP binding subunit


Pssm-ID: 214361 [Multi-domain]  Cd Length: 821  Bit Score: 40.42  E-value: 3.32e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024462873 273 LEKTMHREVFGQKLAVESIMQLLKD-YLATHIHNKPLV-LSLNGPTGVGKSHVGWLLAKHF 331
Cdd:CHL00095  503 MEETLHKRIIGQDEAVVAVSKAIRRaRVGLKNPNRPIAsFLFSGPTGVGKTELTKALASYF 563
PRK10865 PRK10865
ATP-dependent chaperone ClpB;
273-458 7.49e-03

ATP-dependent chaperone ClpB;


Pssm-ID: 182791 [Multi-domain]  Cd Length: 857  Bit Score: 39.06  E-value: 7.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024462873 273 LEKTMHREVFGQKLAVESIMQLLKDYLATHIH-NKPL--VLSLnGPTGVGKSHVGWLLAkHFRSVMDNDFV---LQYFVM 346
Cdd:PRK10865  562 MEQELHHRVIGQNEAVEAVSNAIRRSRAGLSDpNRPIgsFLFL-GPTGVGKTELCKALA-NFMFDSDDAMVridMSEFME 639

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024462873 347 HHCPS---GAAPLTCETDLSKKISDMVTRaeieEKIPLFILDEVELMSPVLLDTLSRFFE-------PNQTNEFLNAIYI 416
Cdd:PRK10865  640 KHSVSrlvGAPPGYVGYEEGGYLTEAVRR----RPYSVILLDEVEKAHPDVFNILLQVLDdgrltdgQGRTVDFRNTVVI 715

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2024462873 417 LISNIGggeitkfviqnasAELLQQRSGA---EELLSVIQPVLTH 458
Cdd:PRK10865  716 MTSNLG-------------SDLIQERFGEldyAHMKELVLGVVSH 747
 
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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