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Conserved domains on  [gi|157821971|ref|NP_001101286|]
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torsin-4A [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 ...
 144-246 4.08e-08

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: 51.57  E-value: 4.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821971  144 DLDGLEKALQRSVFGQPAAVSRIMALLRDYLATHVHSHPLLLALHGPSGVGKSHVGRLLARH-FRAVLEDgALVLQYHAR 222
Cdd:pfam06309   8 NYTGLERDLARRLFGQHLVKQLVVRSVKGHWENPKPRKPLVLSFHGWTGTGKNFVAEIIADNlYRDGLRS-DYVHHFVAT 86

                          90       100
                  ....*....|....*....|....
gi 157821971  223 HHCPELRPVQDCRKELAQRVADVV 246
Cdd:pfam06309  87 FHFPHPKYVELYKVELKNQIRGTL 110
 
Name Accession Description Interval E-value
Torsin pfam06309
Torsin; This family consists of several eukaryotic torsin proteins. Torsion dystonia is an ...
 144-246 4.08e-08

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: 51.57  E-value: 4.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821971  144 DLDGLEKALQRSVFGQPAAVSRIMALLRDYLATHVHSHPLLLALHGPSGVGKSHVGRLLARH-FRAVLEDgALVLQYHAR 222
Cdd:pfam06309   8 NYTGLERDLARRLFGQHLVKQLVVRSVKGHWENPKPRKPLVLSFHGWTGTGKNFVAEIIADNlYRDGLRS-DYVHHFVAT 86

                          90       100
                  ....*....|....*....|....
gi 157821971  223 HHCPELRPVQDCRKELAQRVADVV 246
Cdd:pfam06309  87 FHFPHPKYVELYKVELKNQIRGTL 110
COG2842 COG2842
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons]; ...
 140-277 4.69e-06

Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons];


Pssm-ID: 442090 [Multi-domain]  Cd Length: 254  Bit Score: 47.64  E-value: 4.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821971 140 AQRYDLDGLEKALQRSVFGQPAA---VSRIMALLRDylathVHSHPLLLALHGPSGVGKSHVgrllARHFRAVLEDGALV 216
Cdd:COG2842   10 AKEIGNEKLEAKIARWEAPSFVEtknVRRFAEALDE-----ARALPGIGVVYGESGVGKTTA----AREYANRNPNVIYV 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157821971 217 lqyharhHCPELRPVQDCRKELAQ---------RVADVVAQA-EAEEKTP-LLVLDEAELLPPALLDELHDL 277
Cdd:COG2842   81 -------TASPSWTSKELLEELAEelgipappgTIADLRDRIlERLAGTGrLLIIDEADHLKPKALEELRDI 145
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 185-285 1.23e-05

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: 45.06  E-value: 1.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821971   185 LALHGPSGVGKSHVGRLLARHFRAVLE-----DGALVLQYHARHHCPELRPVQDCRKELAQRVADVVAQAEaEEKTPLLV 259
Cdd:smart00382   5 ILIVGPPGSGKTTLARALARELGPPGGgviyiDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALAR-KLKPDVLI 83

                           90       100
                   ....*....|....*....|....*.
gi 157821971   260 LDEAELLPPALLDELHDLLQPQRSHH 285
Cdd:smart00382  84 LDEITSLLDAEQEALLLLLEELRLLL 109
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 165-279 1.62e-05

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: 44.83  E-value: 1.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821971 165 RIMALLRDYLATHVHSHPLLlalHGPSGVGKSHVGRLLARHfraVLEDGALVLQYHARHHCPELRPVQDCRKELAQRVAD 244
Cdd:cd00009    5 EAIEALREALELPPPKNLLL---YGPPGTGKTTLARAIANE---LFRPGAPFLYLNASDLLEGLVVAELFGHFLVRLLFE 78

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 157821971 245 VVAQAeaeeKTPLLVLDEAELLPPALLDELHDLLQ 279
Cdd:cd00009   79 LAEKA----KPGVLFIDEIDSLSRGAQNALLRVLE 109
clpC CHL00095
Clp protease ATP binding subunit
 148-206 4.77e-03

Clp protease ATP binding subunit


Pssm-ID: 214361 [Multi-domain]  Cd Length: 821  Bit Score: 39.27  E-value: 4.77e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157821971 148 LEKALQRSVFGQPAAVSRIM-ALLRDYLATHVHSHPL---LLAlhGPSGVGKSHVGRLLARHF 206
Cdd:CHL00095 503 MEETLHKRIIGQDEAVVAVSkAIRRARVGLKNPNRPIasfLFS--GPTGVGKTELTKALASYF 563
 
Name Accession Description Interval E-value
Torsin pfam06309
Torsin; This family consists of several eukaryotic torsin proteins. Torsion dystonia is an ...
 144-246 4.08e-08

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: 51.57  E-value: 4.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821971  144 DLDGLEKALQRSVFGQPAAVSRIMALLRDYLATHVHSHPLLLALHGPSGVGKSHVGRLLARH-FRAVLEDgALVLQYHAR 222
Cdd:pfam06309   8 NYTGLERDLARRLFGQHLVKQLVVRSVKGHWENPKPRKPLVLSFHGWTGTGKNFVAEIIADNlYRDGLRS-DYVHHFVAT 86

                          90       100
                  ....*....|....*....|....
gi 157821971  223 HHCPELRPVQDCRKELAQRVADVV 246
Cdd:pfam06309  87 FHFPHPKYVELYKVELKNQIRGTL 110
AAA_22 pfam13401
AAA domain;
178-301 3.17e-07

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 49.26  E-value: 3.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821971  178 VHSHPLLLALHGPSGVGKSHVGRLLARHFRAVlEDGALVLQyharhhCPELRPVQDCRKELAQRV--------------A 243
Cdd:pfam13401   1 IRFGAGILVLTGESGTGKTTLLRRLLEQLPEV-RDSVVFVD------LPSGTSPKDLLRALLRALglplsgrlskeellA 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 157821971  244 DVVAQAEAEEKTPLLVLDEAELLPPALLDELHDLLQPQRShhfhnAIYVLLSGAGGIE 301
Cdd:pfam13401  74 ALQQLLLALAVAVVLIIDEAQHLSLEALEELRDLLNLSSK-----LLQLILVGTPELR 126
COG2842 COG2842
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons]; ...
 140-277 4.69e-06

Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons];


Pssm-ID: 442090 [Multi-domain]  Cd Length: 254  Bit Score: 47.64  E-value: 4.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821971 140 AQRYDLDGLEKALQRSVFGQPAA---VSRIMALLRDylathVHSHPLLLALHGPSGVGKSHVgrllARHFRAVLEDGALV 216
Cdd:COG2842   10 AKEIGNEKLEAKIARWEAPSFVEtknVRRFAEALDE-----ARALPGIGVVYGESGVGKTTA----AREYANRNPNVIYV 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157821971 217 lqyharhHCPELRPVQDCRKELAQ---------RVADVVAQA-EAEEKTP-LLVLDEAELLPPALLDELHDL 277
Cdd:COG2842   81 -------TASPSWTSKELLEELAEelgipappgTIADLRDRIlERLAGTGrLLIIDEADHLKPKALEELRDI 145
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
 164-286 5.99e-06

AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 46.34  E-value: 5.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821971  164 SRIMALLRDYLATHVHSHPLLLALHGPSGVGKSHVGRLLARHFRA--------------------------------VLE 211
Cdd:pfam13191   6 EEELEQLLDALDRVRSGRPPSVLLTGEAGTGKTTLLRELLRALERdggyflrgkcdenlpyspllealtregllrqlLDE 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157821971  212 DGALVLQYHARHHCPELRPVQDCRKELAQRVADV----VAQAEAEEKTPLLVLDEAELLPPALLDELHDLLQPQRSHHF 286
Cdd:pfam13191  86 LESSLLEAWRAALLEALAPVPELPGDLAERLLDLllrlLDLLARGERPLVLVLDDLQWADEASLQLLAALLRLLESLPL 164
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 185-285 1.23e-05

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: 45.06  E-value: 1.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821971   185 LALHGPSGVGKSHVGRLLARHFRAVLE-----DGALVLQYHARHHCPELRPVQDCRKELAQRVADVVAQAEaEEKTPLLV 259
Cdd:smart00382   5 ILIVGPPGSGKTTLARALARELGPPGGgviyiDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALAR-KLKPDVLI 83

                           90       100
                   ....*....|....*....|....*.
gi 157821971   260 LDEAELLPPALLDELHDLLQPQRSHH 285
Cdd:smart00382  84 LDEITSLLDAEQEALLLLLEELRLLL 109
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 165-279 1.62e-05

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: 44.83  E-value: 1.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821971 165 RIMALLRDYLATHVHSHPLLlalHGPSGVGKSHVGRLLARHfraVLEDGALVLQYHARHHCPELRPVQDCRKELAQRVAD 244
Cdd:cd00009    5 EAIEALREALELPPPKNLLL---YGPPGTGKTTLARAIANE---LFRPGAPFLYLNASDLLEGLVVAELFGHFLVRLLFE 78

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 157821971 245 VVAQAeaeeKTPLLVLDEAELLPPALLDELHDLLQ 279
Cdd:cd00009   79 LAEKA----KPGVLFIDEIDSLSRGAQNALLRVLE 109
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 144-204 6.06e-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: 43.32  E-value: 6.06e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157821971 144 DLDGLEKALQRSVFGQPAAVSRIMALLRDYLA--THVHSHPLLLALHGPSGVGKSHVGRLLAR 204
Cdd:cd19499    1 KLLNLEERLHERVVGQDEAVKAVSDAIRRARAglSDPNRPIGSFLFLGPTGVGKTELAKALAE 63
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
 170-296 1.83e-04

Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 442498 [Multi-domain]  Cd Length: 261  Bit Score: 42.85  E-value: 1.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821971 170 LRDYLATHVHSHPLLLALHGPSGVGKShvgrLLARHFRAVLEDGALVLQ-----------YHARHHCPELRPVQDCRKEL 238
Cdd:COG3267   31 ALARLEYALAQGGGFVVLTGEVGTGKT----TLLRRLLERLPDDVKVAYipnpqlspaelLRAIADELGLEPKGASKADL 106

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 157821971 239 AQRVADVVAQAEAEEKTPLLVLDEAELLPPALLDELHDLLQPQrsHHFHNAIYVLLSG 296
Cdd:COG3267  107 LRQLQEFLLELAAAGRRVVLIIDEAQNLPPETLEELRLLSNLE--TDSRKLLQIVLVG 162
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
 184-213 3.03e-03

Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting product gluconate-6-phoshate is an important precursor of gluconate metabolism. GntK acts as a dimmer composed of two identical subunits.


Pssm-ID: 238979 [Multi-domain]  Cd Length: 150  Bit Score: 38.00  E-value: 3.03e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 157821971 184 LLALHGPSGVGKSHVGRLLARHFRAVLEDG 213
Cdd:cd02021    1 IIVVMGVSGSGKSTVGKALAERLGAPFIDG 30
clpC CHL00095
Clp protease ATP binding subunit
 148-206 4.77e-03

Clp protease ATP binding subunit


Pssm-ID: 214361 [Multi-domain]  Cd Length: 821  Bit Score: 39.27  E-value: 4.77e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157821971 148 LEKALQRSVFGQPAAVSRIM-ALLRDYLATHVHSHPL---LLAlhGPSGVGKSHVGRLLARHF 206
Cdd:CHL00095 503 MEETLHKRIIGQDEAVVAVSkAIRRARVGLKNPNRPIasfLFS--GPTGVGKTELTKALASYF 563
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
109-279 7.20e-03

DNA replication protein DnaC [Replication, recombination and repair];


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 37.84  E-value: 7.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821971 109 ERQSRAQRCLLLLVAIVGFQVLNAIENLDDNAQRydldGLEKALqrsvfgqpaavsrIMALLR-DYLATHvhsHPLLLal 187
Cdd:COG1484   47 EVAEREQRRIERRLKAARFPAAKTLEDFDFDAQP----GLDRRQ-------------ILELATlDFIERG---ENLIL-- 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821971 188 HGPSGVGKSHV----GRLLARHFRAVLedgalvlqYharHHCPELrpVQDCRKELAQ-RVADVVAQAeaeEKTPLLVLDE 262
Cdd:COG1484  105 LGPPGTGKTHLaialGHEACRAGYRVR--------F---TTAPDL--VNELKEARADgRLERLLKRL---AKVDLLILDE 168

                        170
                 ....*....|....*....
gi 157821971 263 --AELLPPALLDELHDLLQ 279
Cdd:COG1484  169 lgYLPLDAEGAELLFELIS 187
 
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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