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InterPro: IPR003593 ATPase, AAA+ type, core

Protein matches Help

UniProtKB

Matches:

201599 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR003593 ATPase_AAA+_core

Type

Domain

Signatures Help

Database	ID	Name	Proteins
SMART	SM00382	AAA	201599
Signatures in BioMart

InterPro Relationships Help

Children

IPR000523 Magnesium chelatase, ChlI subunit
IPR000897 Signal recognition particle, SRP54 subunit, GTPase
IPR002078 RNA polymerase sigma factor 54, interaction
IPR003439 ABC transporter-like
IPR003959 ATPase, AAA-type, core
IPR013093 ATPase associated with various cellular activities, AAA-2

Found in

IPR000194 ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain
IPR001208 DNA-dependent ATPase MCM
IPR001482 Type II secretion system protein E
IPR001553 DNA recombination and repair protein RecA/RadB
IPR001957 Chromosomal replication control, initiator DnaA
IPR001984 Peptidase S16, Lon protease, C-terminal
IPR002543 Cell divisionFtsK/SpoIIIE
IPR002611 IstB-like ATP-binding protein
IPR003450 Herpesvirus, replication origin-binding protein
IPR004482 Mg chelatase-related protein
IPR004483 DNA helicase, putative
IPR004487 Clp protease, ATP-binding subunit ClpX
IPR004504 DNA repair protein RadA
IPR004663 Peptidase S16, archaeal lon homologues
IPR004665 Transcription termination factor Rho
IPR004948 Protein of unknown function DUF265
IPR005714 ATPase, type III secretion system, FliI/YscN
IPR005722 ATPase, F1 complex, beta subunit
IPR005726 ATPase, A1 complex, alpha subunit
IPR005736 Reverse gyrase
IPR006321 Pilus retraction protein PilT
IPR006344 Exodeoxyribonuclease V, alpha subunit
IPR006345 DNA helicase, RecD/TraA type
IPR007692 DNA helicase, DnaB type
IPR007694 DNA helicase, DnaB-like, C-terminal
IPR008046 MCM protein 3
IPR008047 MCM protein 4
IPR008050 MCM protein 7
IPR009147 Cystic fibrosis transmembrane conductance regulator
IPR010128 ATPase, type I secretion system, PrtD
IPR010222 RNA helicase, ATP-dependent DEAH box, HrpA type
IPR010230 ATPase SufC, SUF system FeS cluster assembly
IPR011579 ATPase domain, prokaryote
IPR011703 ATPase associated with various cellular activities, AAA-3
IPR011704 ATPase associated with various cellular activities, AAA-5
IPR011938 DNA recombination and repair protein RadA
IPR011939 DNA recombination and repair protein RadB
IPR011940 Meiotic recombinase Dmc1
IPR011941 DNA recombination and repair protein Rad51
IPR012099 Midasin
IPR013305 ABC transporter, ABCB2
IPR013317 Chromosomal replication control, initiator (DnaA)/regulator (Hda)
IPR013369 Type II secretion system gspE
IPR013380 ATPase, type III secretion system, H+-transporting
IPR013462 Gas vesicle protein GvpN
IPR013632 DNA recombination and repair protein Rad51, C-terminal
IPR013765 DNA recombination and repair protein RecA
IPR014217 Sporulation stage III, protein AA
IPR014277 Cell division control protein 6 related, archaea
IPR014588 ATPase, Atu1862 type, predicted
IPR014759 Helicase, superfamily 3, single-stranded RNA virus
IPR016300 ATPase, arsenite-transporting
IPR016366 ATPase chaperone, AAA-type, MoxR, predicted
IPR016467 DNA recombination and repair protein, RecA-like
IPR016527 Origin recognition complex, subunit 4
IPR017466 ATPase, secretion system, PEP-CTERM, predicted
IPR017691 Alternate ATPase, F1 complex, beta subunit
IPR018324 Checkpoint protein Rad24, fungi/metazoa
IPR020005 Flagellar protein export ATPase, FliI
IPR020064 ABC transporter G1-like
IPR020591 Chromosomal replication control, initiator DnaA-like
IPR020793 Origin recognition complex, subunit 1

Contains

IPR003960 ATPase, AAA-type, conserved site
IPR015850 ABC transporter, phosphate import, PstB
IPR015851 ABC transporter, NodI
IPR015854 ABC transporter, lipoprotein release, LolD
IPR015858 ABC transporter, nickel import, NikE
IPR017871 ABC transporter, conserved site
IPR018368 Chaperonin ClpA/B, conserved site
IPR018525 DNA-dependent ATPase MCM, conserved site
IPR020584 DNA recombination/repair protein RecA, conserved site
IPR020588 DNA recombination/repair protein RecA/RadB, ATP-binding domain

GO Term annotation Help

Function

GO:0000166 nucleotide binding
GO:0017111 nucleoside-triphosphatase activity

InterPro annotation

Entry Details in BioMart

Abstract

AAA ATPases (ATPases Associated with diverse cellular Activities) form a large protein family and play a number of roles in the cell including cell-cycle regulation, protein proteolysis and disaggregation, organelle biogenesis and intracellular transport. Some of them function as molecular chaperones, subunits of proteolytic complexes or independent proteases (FtsH, Lon). They also act as DNA helicases and transcription factors [1].

AAA ATPases belong to the AAA+ superfamily of ringshaped P-loop NTPases, which act via the energy-dependent unfolding of macromolecules [2, 3]. There are six major clades of AAA domains (proteasome subunits, metalloproteases, domains D1 and D2 of ATPases with two AAA domains, the MSP1/katanin/spastin group and BCS1 and it homologues), as well as a number of deeply branching minor clades [2].

They assemble into oligomeric assemblies (often hexamers) that form a ring-shaped structure with a central pore. These proteins produce a molecular motor that couples ATP binding and hydrolysis to changes in conformational states that act upon a target substrate, either translocating or remodelling it [4].

They are found in all living organisms and share the common feature of the presence of a highly conserved AAA domain called the AAA module. This domain is responsible for ATP binding and hydrolysis. It contains 200-250 residues, among them there are two classical motifs, Walker A (GX4GKT) and Walker B (HyDE) [1].

More information about these protein can be found at Protein of the Month: AAA ATPases [5]. This entry represents the core domain of the AAA+ ATPases

Structural links Help

PDB - click here

SCOP: a.80.1.1 , b.40.4.14 , c.37.1.10 , c.37.1.11 , c.37.1.12 , c.37.1.19 , c.37.1.20 , i.3.1.1 , j.35.1.1

CATH: 1.10.1140.10 , 1.10.8.10 , 1.10.8.180 , 1.10.8.60 , 1.20.272.10 , 3.40.50.300

Interactions Help

This domain has been experimentally proven to be involved in Protein:Protein interactions.
Representative data is shown with the following example proteins:

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR003593

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O16299 Fidgetin-like protein 1

O75351 Vacuolar protein sorting-associated protein 4B

P00830 ATP synthase subunit beta, mitochondrial

P14576 Signal recognition particle 54 kDa protein

Q8I0P1 Spastin

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR020003	ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain, active site
IPR003959	ATPase, AAA-type, core
IPR000897	Signal recognition particle, SRP54 subunit, GTPase
IPR013822	Signal recognition particle, SRP54 subunit, helical bundle
IPR004100	ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal
IPR003593	ATPase, AAA+ type, core
IPR006325	Signal recognition particle, SRP54 subunit
IPR004125	Signal recognition particle, SRP54 subunit, M-domain
IPR015415	Vps4 oligomerisation, C-terminal
IPR007330	MIT
IPR003960	ATPase, AAA-type, conserved site
IPR005722	ATPase, F1 complex, beta subunit
IPR000793	ATPase, F1/V1/A1 complex, alpha/beta subunit, C-terminal
IPR000194	ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain
IPR018118	ATPase, F1/A1 complex, alpha/beta subunit, N-terminal
	PDB Chain
	ModBase
	CATH Domain
	SWISS-MODEL
	SCOP Domain

Publications Open in usermanual
1.	Kedzierska S. [Structure, function and mechanisms of action of ATPases from the AAA superfamily of proteins] Postepy Biochem. 52 330-8 2006 [PubMed: 17201069]
2.	Frickey T, Lupas AN. Phylogenetic analysis of AAA proteins. J. Struct. Biol. 146 2-10 2004 [PubMed: 15037233] http://dx.doi.org/10.1016/j.jsb.2003.11.020
3.	Ammelburg M, Frickey T, Lupas AN. Classification of AAA+ proteins. J. Struct. Biol. 156 2-11 2006 [PubMed: 16828312]
4.	Smith DM, Benaroudj N, Goldberg A. Proteasomes and their associated ATPases: a destructive combination. J. Struct. Biol. 156 72-83 2006 [PubMed: 16919475]
5.	McDowall J. Protein of the Month - AAA ATPases. 2006

Additional Reading Open in usermanual
	Gerber S, Comellas-Bigler M, Goetz BA, Locher KP. Structural basis of trans-inhibition in a molybdate/tungstate ABC transporter. Science 321 2008 246-50 [PubMed: 18511655] http://dx.doi.org/10.1126/science.1156213
	Joly N, Rappas M, Buck M, Zhang X. Trapping of a transcription complex using a new nucleotide analogue: AMP aluminium fluoride. J. Mol. Biol. 375 2008 1206-11 [PubMed: 18082766] http://dx.doi.org/10.1016/j.jmb.2007.11.050
	Oswald C, Jenewein S, Smits SH, Holland IB, Schmitt L. Water-mediated protein-fluorophore interactions modulate the affinity of an ABC-ATPase/TNP-ADP complex. J. Struct. Biol. 162 2008 85-93 [PubMed: 18155559] http://dx.doi.org/10.1016/j.jsb.2007.11.006
	Davies JM, Brunger AT, Weis WI. Improved structures of full-length p97, an AAA ATPase: implications for mechanisms of nucleotide-dependent conformational change. Structure 16 2008 715-26 [PubMed: 18462676] http://dx.doi.org/10.1016/j.str.2008.02.010
	Fu H, Reis N, Lee Y, Glickman MH, Vierstra RD. Subunit interaction maps for the regulatory particle of the 26S proteasome and the COP9 signalosome. EMBO J. 20 2001 7096-107 [PubMed: 11742986] http://dx.doi.org/10.1093/emboj/20.24.7096
	Kadaba NS, Kaiser JT, Johnson E, Lee A, Rees DC. The high-affinity E. coli methionine ABC transporter: structure and allosteric regulation. Science 321 2008 250-3 [PubMed: 18621668] http://dx.doi.org/10.1126/science.1157987

InterPro 23.1