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Conserved domains on  [gi|18859501|ref|NP_572178|]
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torsin, isoform A [Drosophila melanogaster]

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 ...
 55-175 4.34e-63

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: 196.41  E-value: 4.34e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859501    55 DDRNIPARIDELERSLERTLIGQHIVRQHIVPALKAHIASGnKSRKPLVISFHGQPGTGKNFVAEQIADAMYLKGSRSNY 134
Cdd:pfam06309   1 GDCRISFNYTGLERDLARRLFGQHLVKQLVVRSVKGHWENP-KPRKPLVLSFHGWTGTGKNFVAEIIADNLYRDGLRSDY 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 18859501   135 VTKYLGQADFPKESEVSNYRVKINNAVRDTLRSCPRSLFIF 175
Cdd:pfam06309  80 VHHFVATFHFPHPKYVELYKVELKNQIRGTLRACHRSIFIF 120
 
Name Accession Description Interval E-value
Torsin pfam06309
Torsin; This family consists of several eukaryotic torsin proteins. Torsion dystonia is an ...
 55-175 4.34e-63

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: 196.41  E-value: 4.34e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859501    55 DDRNIPARIDELERSLERTLIGQHIVRQHIVPALKAHIASGnKSRKPLVISFHGQPGTGKNFVAEQIADAMYLKGSRSNY 134
Cdd:pfam06309   1 GDCRISFNYTGLERDLARRLFGQHLVKQLVVRSVKGHWENP-KPRKPLVLSFHGWTGTGKNFVAEIIADNLYRDGLRSDY 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 18859501   135 VTKYLGQADFPKESEVSNYRVKINNAVRDTLRSCPRSLFIF 175
Cdd:pfam06309  80 VHHFVATFHFPHPKYVELYKVELKNQIRGTLRACHRSIFIF 120
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 66-214 2.98e-07

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: 49.87  E-value: 2.98e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859501  66 LERSLERTLIGQ-HIVRQhIVPALKAHIA-SGNKSRKPLVISFHGQPGTGKNFVAEQIADAMYlkGSRSNYVTkylgqAD 143
Cdd:cd19499   5 LEERLHERVVGQdEAVKA-VSDAIRRARAgLSDPNRPIGSFLFLGPTGVGKTELAKALAELLF--GDEDNLIR-----ID 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859501 144 FPKESE---VSN-------YR-----VKINNAVRDtlrsCPRSLFIFDEVDKMPSGVFDQLtslvdYNAFVDG--TDN-- 204
Cdd:cd19499  77 MSEYMEkhsVSRligappgYVgytegGQLTEAVRR----KPYSVVLLDEIEKAHPDVQNLL-----LQVLDDGrlTDShg 147

                       170
                ....*....|....*
gi 18859501 205 -----TKAIFIFLSN 214
Cdd:cd19499 148 rtvdfKNTIIIMTSN 162
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 100-224 1.17e-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: 44.67  E-value: 1.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859501    100 KPLVISFHGQPGTGKNFVAEQIA--------DAMYLKGSRSNYVTKYLGQADFPKESEVSNYRVKINNAVRDTLRSCPRS 171
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALArelgppggGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 18859501    172 LFIFDEVDKMPSGVFDQLTSLVDYNAFVDGTDNTKAIFIFLSNTAGSHIASHL 224
Cdd:smart00382  81 VLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPAL 133
cbbX CHL00181
CbbX; Provisional
 62-150 4.49e-03

CbbX; Provisional


Pssm-ID: 177083 [Multi-domain]  Cd Length: 287  Bit Score: 38.16  E-value: 4.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859501   62 RIDELERSLERTLIGQHIVRQHI--VPAL--------KAHIASGNKSrkpLVISFHGQPGTGKNFVAEQIADAMYLKG-- 129
Cdd:CHL00181  13 QIQEVLDILDEELVGLAPVKTRIreIAALllidrlrkNLGLTSSNPG---LHMSFTGSPGTGKTTVALKMADILYKLGyi 89

                         90       100
                 ....*....|....*....|....*....
gi 18859501  130 --------SRSNYVTKYLGQADfPKESEV 150
Cdd:CHL00181  90 kkghlltvTRDDLVGQYIGHTA-PKTKEV 117
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 99-180 6.65e-03

AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 37.97  E-value: 6.65e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859501  99 RKPLVISFHGQPGTGKNFVAEQIADAM---YLKGSRSNYVTKYLGqadfpkESEvsnyrvkinNAVR---DTLRSCPRSL 172
Cdd:COG0464 189 PPPRGLLLYGPPGTGKTLLARALAGELglpLIEVDLSDLVSKYVG------ETE---------KNLRevfDKARGLAPCV 253


                ....*...
gi 18859501 173 FIFDEVDK 180
Cdd:COG0464 254 LFIDEADA 261
 
Name Accession Description Interval E-value
Torsin pfam06309
Torsin; This family consists of several eukaryotic torsin proteins. Torsion dystonia is an ...
 55-175 4.34e-63

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: 196.41  E-value: 4.34e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859501    55 DDRNIPARIDELERSLERTLIGQHIVRQHIVPALKAHIASGnKSRKPLVISFHGQPGTGKNFVAEQIADAMYLKGSRSNY 134
Cdd:pfam06309   1 GDCRISFNYTGLERDLARRLFGQHLVKQLVVRSVKGHWENP-KPRKPLVLSFHGWTGTGKNFVAEIIADNLYRDGLRSDY 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 18859501   135 VTKYLGQADFPKESEVSNYRVKINNAVRDTLRSCPRSLFIF 175
Cdd:pfam06309  80 VHHFVATFHFPHPKYVELYKVELKNQIRGTLRACHRSIFIF 120
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 66-214 2.98e-07

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: 49.87  E-value: 2.98e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859501  66 LERSLERTLIGQ-HIVRQhIVPALKAHIA-SGNKSRKPLVISFHGQPGTGKNFVAEQIADAMYlkGSRSNYVTkylgqAD 143
Cdd:cd19499   5 LEERLHERVVGQdEAVKA-VSDAIRRARAgLSDPNRPIGSFLFLGPTGVGKTELAKALAELLF--GDEDNLIR-----ID 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859501 144 FPKESE---VSN-------YR-----VKINNAVRDtlrsCPRSLFIFDEVDKMPSGVFDQLtslvdYNAFVDG--TDN-- 204
Cdd:cd19499  77 MSEYMEkhsVSRligappgYVgytegGQLTEAVRR----KPYSVVLLDEIEKAHPDVQNLL-----LQVLDDGrlTDShg 147

                       170
                ....*....|....*
gi 18859501 205 -----TKAIFIFLSN 214
Cdd:cd19499 148 rtvdfKNTIIIMTSN 162
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 108-217 3.98e-06

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 45.75  E-value: 3.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859501   108 GQPGTGKNFVAEQIADAmyLKGSRSNYVtkyLGQADFPKESEVSNYRVKINNAVR---DTLRSCPRSLFIF-DEVDKMPS 183
Cdd:pfam07728   6 GPPGTGKTELAERLAAA--LSNRPVFYV---QLTRDTTEEDLFGRRNIDPGGASWvdgPLVRAAREGEIAVlDEINRANP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 18859501   184 GVFDQLTSLVDYN-------AFVDGTDNTKAIFIFLSNTAG 217
Cdd:pfam07728  81 DVLNSLLSLLDERrlllpdgGELVKAAPDGFRLIATMNPLD 121
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 100-224 1.17e-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: 44.67  E-value: 1.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859501    100 KPLVISFHGQPGTGKNFVAEQIA--------DAMYLKGSRSNYVTKYLGQADFPKESEVSNYRVKINNAVRDTLRSCPRS 171
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALArelgppggGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 18859501    172 LFIFDEVDKMPSGVFDQLTSLVDYNAFVDGTDNTKAIFIFLSNTAGSHIASHL 224
Cdd:smart00382  81 VLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPAL 133
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 96-214 2.62e-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: 43.67  E-value: 2.62e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859501  96 NKSRKPLVIsfHGQPGTGKNFVAEQIADAMYLKGSRSNYVTKylgqADFPKESEVSNY-RVKINNAVRDTLRSCPRSLFI 174
Cdd:cd00009  16 LPPPKNLLL--YGPPGTGKTTLARAIANELFRPGAPFLYLNA----SDLLEGLVVAELfGHFLVRLLFELAEKAKPGVLF 89

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 18859501 175 FDEVDKMPSGVFDQLTSLVDYnAFVDGTDNTKAIFIFLSN 214
Cdd:cd00009  90 IDEIDSLSRGAQNALLRVLET-LNDLRIDRENVRVIGATN 128
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 80-213 5.40e-05

proteases similar to RecA; RecA-like NTPases. This family 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. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410889 [Multi-domain]  Cd Length: 158  Bit Score: 43.04  E-value: 5.40e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859501  80 VRQHIVPALKAHIASGNKSRKPLVISFHGQPGTGKNFVAEQIA-----DAMYLKGSRsnYVTKYLGqadfpkESEvsnyr 154
Cdd:cd19481   5 LREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAgelglPLIVVKLSS--LLSKYVG------ESE----- 71

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18859501 155 VKINNAVRDtLRSCPRSLFIFDEVDKMP----SGVFDQLTSLVDyNAFV---DGTDNTKAIFIFLS 213
Cdd:cd19481  72 KNLRKIFER-ARRLAPCILFIDEIDAIGrkrdSSGESGELRRVL-NQLLtelDGVNSRSKVLVIAA 135
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 100-248 3.63e-04

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: 40.64  E-value: 3.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859501   100 KPLV-ISFHGQPGTGKNFVAEQIADAMYLKGSR-----------SNYVTKYLGQADFpkesevsNYRVKINNAVRDTLRS 167
Cdd:pfam07724   1 RPIGsFLFLGPTGVGKTELAKALAELLFGDERAliridmseymeEHSVSRLIGAPPG-------YVGYEEGGQLTEAVRR 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859501   168 CPRSLFIFDEVDKMPSGVFDQLTSLVD-------YNAFVDgTDNTkaIFIFLSNTAGSHIASHLGSvmkNGRLREDTRLS 240
Cdd:pfam07724  74 KPYSIVLIDEIEKAHPGVQNDLLQILEggtltdkQGRTVD-FKNT--LFIMTGNFGSEKISDASRL---GDSPDYELLKE 147


                  ....*...
gi 18859501   241 DFEPLLRK 248
Cdd:pfam07724 148 EVMDLLKK 155
cbbX CHL00181
CbbX; Provisional
 62-150 4.49e-03

CbbX; Provisional


Pssm-ID: 177083 [Multi-domain]  Cd Length: 287  Bit Score: 38.16  E-value: 4.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859501   62 RIDELERSLERTLIGQHIVRQHI--VPAL--------KAHIASGNKSrkpLVISFHGQPGTGKNFVAEQIADAMYLKG-- 129
Cdd:CHL00181  13 QIQEVLDILDEELVGLAPVKTRIreIAALllidrlrkNLGLTSSNPG---LHMSFTGSPGTGKTTVALKMADILYKLGyi 89

                         90       100
                 ....*....|....*....|....*....
gi 18859501  130 --------SRSNYVTKYLGQADfPKESEV 150
Cdd:CHL00181  90 kkghlltvTRDDLVGQYIGHTA-PKTKEV 117
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 63-184 5.35e-03

lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an evolutionarily conserved ATP-dependent serine protease, present in bacteria and eukaryotic mitochondria and peroxisomes, which mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Lon protease is both an ATP-dependent peptidase and a protein-activated ATPase. This RecA-like Lon domain 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: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 37.54  E-value: 5.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859501  63 IDELERSLERTLIGQHIVRQHIVpalkAHIASG--NKSRKPLVISFHGQPGTGKNFVAEQIADAMYLKgsrsnYVTKYLG 140
Cdd:cd19500   1 IKKARKVLDADHYGLEDVKERIL----EYLAVRklKGSMKGPILCLVGPPGVGKTSLGKSIARALGRK-----FVRISLG 71

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 18859501 141 qaDFPKESEVSNYRV--------KINNAVRDTLRSCPrsLFIFDEVDKMPSG 184
Cdd:cd19500  72 --GVRDEAEIRGHRRtyvgampgRIIQALKKAGTNNP--VFLLDEIDKIGSS 119
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 99-180 6.65e-03

AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 37.97  E-value: 6.65e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18859501  99 RKPLVISFHGQPGTGKNFVAEQIADAM---YLKGSRSNYVTKYLGqadfpkESEvsnyrvkinNAVR---DTLRSCPRSL 172
Cdd:COG0464 189 PPPRGLLLYGPPGTGKTLLARALAGELglpLIEVDLSDLVSKYVG------ETE---------KNLRevfDKARGLAPCV 253


                ....*...
gi 18859501 173 FIFDEVDK 180
Cdd:COG0464 254 LFIDEADA 261
 
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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