Protein Domain : IPR010929

Type:  Domain Name:  CDR ABC transporter
Description:  ABC transporters belong to the ATP-Binding Cassette (ABC) superfamily, which uses the hydrolysis of ATP to energise diverse biological systems. ABC transporters minimally consist of two conserved regions: a highly conserved ATP binding cassette (ABC) and a less conserved transmembrane domain (TMD). These can be found on the same protein or on two different ones. Most ABC transporters function as a dimer and therefore are constituted of four domains, two ABC modules and two TMDs.ABC transporters are involved in the export or import of a wide variety of substrates ranging from small ions to macromolecules. The major function of ABC import systems is to provide essential nutrients to bacteria. They are found only in prokaryotes and their four constitutive domains are usually encoded by independent polypeptides (two ABC proteins and two TMD proteins). Prokaryotic importers require additional extracytoplasmic binding proteins (one or more per systems) for function. In contrast, export systems are involved in the extrusion of noxious substances, the export of extracellular toxins and the targeting of membrane components. They are found in all living organisms and in general the TMD is fused to the ABC module in a variety of combinations. Some eukaryotic exporters encode the four domains on the same polypeptide chain [].The ABC module (approximately two hundred amino acid residues) is known to bind and hydrolyse ATP, thereby coupling transport to ATP hydrolysis in a large number of biological processes. The cassette is duplicated in several subfamilies. Its primary sequence is highly conserved, displaying a typical phosphate-binding loop: Walker A, and a magnesium binding site: Walker B. Besides these two regions, three other conserved motifs are present in the ABC cassette: the switch region which contains a histidine loop, postulated to polarise the attaching water molecule for hydrolysis, the signature conserved motif (LSGGQ) specific to the ABC transporter, and the Q-motif (between Walker A and the signature), which interacts with the gamma phosphate through a water bond. The Walker A, Walker B, Q-loop and switch region form the nucleotide binding site [, , ].The 3D structure of a monomeric ABC module adopts a stubby L-shape with two distinct arms. ArmI (mainly beta-strand) contains Walker A and Walker B. The important residues for ATP hydrolysis and/or binding are located in the P-loop. The ATP-binding pocket is located at the extremity of armI. The perpendicular armII contains mostly the alpha helical subdomain with the signature motif. It only seems to be required for structural integrity of the ABC module. ArmII is in direct contact with the TMD. The hinge between armI and armII contains both the histidine loop and the Q-loop, making contact with the gamma phosphate of the ATP molecule. ATP hydrolysis leads to a conformational change that could facilitate ADP release. In the dimer the two ABC cassettes contact each other through hydrophobic interactions at the antiparallel beta-sheet of armI by a two-fold axis [, , , , , ].The ATP-Binding Cassette (ABC) superfamily forms one of the largest of all protein families with a diversity of physiological functions []. Several studies have shown that there is a correlation between the functional characterisation and the phylogenetic classification of the ABC cassette [, ]. More than 50 subfamilies have been described based on a phylogenetic and functional classification [, , ]; (for further information see http://www.tcdb.org/tcdb/index.php?tc=3.A.1).In yeast, the PDR and CDR ABC transporters display extensive sequence homology, and confer resistance to several anti-fungal compounds by actively transporting their substrates out of the cell. These transporters have two homologous halves, each with an N-terminal intracellular hydrophilic region that contains an ATP-binding site, followed by a C-terminal membrane-associated region containing six transmembrane segments []. This entry represents a domain of the PDR/CDR ABC transporter comprising extracellular loop 3, transmembrane segment 6 and a linker region. Short Name:  PDR_CDR_ABC
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0 Child Features

0 Contains

1 Cross References

Identifier
PF06422

0 Found In

4 GO Annotations

GO Term Gene Name
GO:0005524 IPR010929
GO:0042626 IPR010929
GO:0006810 IPR010929
GO:0016021 IPR010929

4 Ontology Annotations

GO Term Gene Name
GO:0005524 IPR010929
GO:0042626 IPR010929
GO:0006810 IPR010929
GO:0016021 IPR010929

0 Parent Features

12 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
Gorai.005G221700.1 A0A0D2PXQ9 PAC:26803382 Gossypium raimondii 348  
64664 I0Z837 PAC:27393316 Coccomyxa subellipsoidea C-169 1531  
Anaoc.0066s0007.1.p PAC:37481191 Anacardium occidentale 599  
Anaoc.0017s0713.1.p PAC:37530787 Anacardium occidentale 642  
evm.model.Scaffold_2065.31 PAC:37904129 Coffea arabica 642  
HORVU5Hr1G051160.13 PAC:38432108 Hordeum vulgare 58  
Lsat_1_v5_gn_1_82081.1 A0A2J6KKP0 PAC:38942801 Lactuca sativa 642  
Gomus.D02G232500.1.p A0A5D2VZR9 PAC:42130585 Gossypium mustelinum 261  
Gobar.D02G227800.1.p A0A5J5SGB2 PAC:42328876 Gossypium barbadense 343  
Gohir.A09G002000.2.p PAC:42425586 Gossypium hirsutum 385  
Zosma05g07350 PAC:50103882 Zostera marina 378  
Ceric.1Z296200.1.p PAC:50597250 Ceratopteris richardii 257  

12 Publications

First Author Title Year Journal Volume Pages PubMed ID
            9872322
            9873074
            11421269
            1282354
            9640644
            11402022
            11080142
            11532960
            11421270
            11470432
            11988180
            12709320