5XMK

Cryo-EM structure of the ATP-bound Vps4 mutant-E233Q complex with Vta1 (masked)


Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
APF09336,PF17862e5xmkA1 A: alpha arraysX: Histone-likeH: Histone-relatedT: AAA+ ATPase lid domainF: PF09336,PF17862ECOD (1.6)
APF00004,PF09336e5xmkA2 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: PF00004,PF09336ECOD (1.6)
BPF09336,PF17862e5xmkB1 A: alpha arraysX: Histone-likeH: Histone-relatedT: AAA+ ATPase lid domainF: PF09336,PF17862ECOD (1.6)
BPF00004,PF09336e5xmkB2 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: PF00004,PF09336ECOD (1.6)
CPF09336,PF17862e5xmkC2 A: alpha arraysX: Histone-likeH: Histone-relatedT: AAA+ ATPase lid domainF: PF09336,PF17862ECOD (1.6)
CPF00004,PF09336e5xmkC1 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: PF00004,PF09336ECOD (1.6)
DPF09336,PF17862e5xmkD1 A: alpha arraysX: Histone-likeH: Histone-relatedT: AAA+ ATPase lid domainF: PF09336,PF17862ECOD (1.6)
DPF00004,PF09336e5xmkD2 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: PF00004,PF09336ECOD (1.6)
EPF09336,PF17862e5xmkE1 A: alpha arraysX: Histone-likeH: Histone-relatedT: AAA+ ATPase lid domainF: PF09336,PF17862ECOD (1.6)
EPF00004,PF09336e5xmkE2 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: PF00004,PF09336ECOD (1.6)
FPF09336,PF17862e5xmkF1 A: alpha arraysX: Histone-likeH: Histone-relatedT: AAA+ ATPase lid domainF: PF09336,PF17862ECOD (1.6)
FPF00004,PF09336e5xmkF2 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: PF00004,PF09336ECOD (1.6)
GPF18097e5xmkG1 A: alpha bundlesX: Spectrin repeat-likeH: MIT domain (From Topology)T: MIT domainF: PF18097ECOD (1.6)
HPF18097e5xmkH1 A: alpha bundlesX: Spectrin repeat-likeH: MIT domain (From Topology)T: MIT domainF: PF18097ECOD (1.6)
IPF18097e5xmkI1 A: alpha bundlesX: Spectrin repeat-likeH: MIT domain (From Topology)T: MIT domainF: PF18097ECOD (1.6)
JPF18097e5xmkJ1 A: alpha bundlesX: Spectrin repeat-likeH: MIT domain (From Topology)T: MIT domainF: PF18097ECOD (1.6)
KPF18097e5xmkK1 A: alpha bundlesX: Spectrin repeat-likeH: MIT domain (From Topology)T: MIT domainF: PF18097ECOD (1.6)
LPF18097e5xmkL1 A: alpha bundlesX: Spectrin repeat-likeH: MIT domain (From Topology)T: MIT domainF: PF18097ECOD (1.6)
MPF18097e5xmkM1 A: alpha bundlesX: Spectrin repeat-likeH: MIT domain (From Topology)T: MIT domainF: PF18097ECOD (1.6)
NPF18097e5xmkN1 A: alpha bundlesX: Spectrin repeat-likeH: MIT domain (From Topology)T: MIT domainF: PF18097ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B, C, D, E
PF09336Vps4 C terminal oligomerisation domain (Vps4_C)Vps4 C terminal oligomerisation domainThis domain is found at the C terminal of ATPase proteins involved in vacuolar sorting. It forms an alpha helix structure and is required for oligomerisation [1].Domain
A, B, C, D, E
PF17862AAA+ lid domain (AAA_lid_3)AAA+ lid domainThis entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains.Domain
A, B, C, D, E
PF00004ATPase family associated with various cellular activities (AAA) (AAA)ATPase family associated with various cellular activities (AAA)AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes [2].Domain
G, H, I, J, K
PF18097Vta1 C-terminal domain (Vta1_C)Vta1 C-terminal domainThis is the C-terminal domain of Vta1 proteins Pfam:PF04652 . Structural and functional analysis indicate that this C-terminal domain promotes the ATP-dependent double ring assembly of Vps4. Furthermore, it has been shown that it is necessary and suf ...This is the C-terminal domain of Vta1 proteins Pfam:PF04652 . Structural and functional analysis indicate that this C-terminal domain promotes the ATP-dependent double ring assembly of Vps4. Furthermore, it has been shown that it is necessary and sufficient for protein dimerization. Mutations in Lys-299 and Lys-302 completely abolished the ability of Vta1 to stimulate the ATPase activity of Vps4 while mutation in Lys-322 had no effect [1].
Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A, B, C, D, E
Vacuolar protein sorting-associated protein 4
G, H, I, J, K
Vacuolar protein sorting-associated protein VTA1

InterPro: Protein Family Classification InterPro Database Homepage

ChainsAccessionNameType
A, B, C, D, E
IPR003593AAA+ ATPase domainDomain
A, B, C, D, E
IPR003959ATPase, AAA-type, coreDomain
A, B, C, D, E
IPR027417P-loop containing nucleoside triphosphate hydrolaseHomologous Superfamily
A, B, C, D, E
IPR007330MIT domainDomain
A, B, C, D, E
IPR041569AAA ATPase, AAA+ lid domainDomain
A, B, C, D, E
IPR015415Spastin/Vps4, C-terminalDomain
A, B, C, D, E
IPR045253Vacuolar protein sorting-associated protein 4, MIT domainDomain
A, B, C, D, E
IPR003960ATPase, AAA-type, conserved siteConserved Site
A, B, C, D, E
IPR036181MIT domain superfamilyHomologous Superfamily
G, H, I, J, K
IPR039431Vta1/callose synthase, N-terminalDomain
G, H, I, J, K
IPR023175Vta1/Callose synthase, N-terminal domain superfamilyHomologous Superfamily
G, H, I, J, K
IPR041212Vta1, C-terminalDomain
G, H, I, J, K
IPR044538Vacuolar protein sorting-associated protein Vta1-likeFamily