Summary: CDR ABC transporter
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CDR ABC transporter Provide feedback
Corresponds to a region of the PDR/CDR subgroup of ABC transporters comprising extracellular loop 3, transmembrane segment 6 and linker region.
Gauthier C, Weber S, Alarco AM, Alqawi O, Daoud R, Georges E, Raymond M; , Antimicrob Agents Chemother 2003;47:1543-1554.: Functional Similarities and Differences between Candida albicans Cdr1p and Cdr2p Transporters. PUBMED:12709320 EPMC:12709320
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR010929
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 [PUBMED:9873074].
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 [PUBMED:11421269, PUBMED:1282354, PUBMED:9640644].
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 [PUBMED:11988180, PUBMED:11470432, PUBMED:11402022, PUBMED:9872322, PUBMED:11080142, PUBMED:11532960].
The ATP-Binding Cassette (ABC) superfamily forms one of the largest of all protein families with a diversity of physiological functions [PUBMED:9873074]. Several studies have shown that there is a correlation between the functional characterisation and the phylogenetic classification of the ABC cassette [PUBMED:9873074, PUBMED:11421270]. More than 50 subfamilies have been described based on a phylogenetic and functional classification [PUBMED:9873074, PUBMED:11421269, PUBMED:11421270]; (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 [PUBMED:12709320]. This entry represents a domain of the PDR/CDR ABC transporter comprising extracellular loop 3, transmembrane segment 6 and a linker region.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||integral to membrane (GO:0016021)|
|Molecular function||ATP binding (GO:0005524)|
|ATPase activity, coupled to transmembrane movement of substances (GO:0042626)|
|Biological process||transport (GO:0006810)|
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These families are similar to the ABC-2 transporter subfamily, as described in  (Pfam:PF01061). Members of this family are involved in drug transport and resistance. CcmB protein family (Pfam:PF03379) members are also transporters; they are required for haem export into the periplasm .
The clan contains the following 10 members:ABC2_membrane ABC2_membrane_2 ABC2_membrane_3 ABC2_membrane_4 ABC2_membrane_5 ABC2_membrane_6 CcmB DUF3526 DUF3533 PDR_CDR
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Curation and family details
|Seed source:||Pfam-B_1005 (release 8.0)|
|Author:||Gauthier C, Studholme DJ|
|Number in seed:||167|
|Number in full:||1227|
|Average length of the domain:||97.70 aa|
|Average identity of full alignment:||26 %|
|Average coverage of the sequence by the domain:||7.84 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||7|
|Download:||download the raw HMM for this family|
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