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ABC transporter C-terminal domain
This domain is found at the C-terminus of ABC transporters. It has a coiled coil structure with an atypical 3(10)-helix in the alpha-hairpin region. It is involved in DNA_binding [1]. [1]. 22995754. The C-terminal domain of the Uup protein is a DNA-binding coiled. coil motif.. Carlier L, Haase AS, Burgos Zepeda MY, Dassa E, Lequin O;. J Struct Biol. 2012;180:577-584. (from Pfam)
ABC transporter
This domain is an extension of some members of Pfam:PF00005 and other ABC-transporter families. (from Pfam)
ATP-binding cassette domain-containing protein
ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain Pfam:PF00664. These four domains may belong to a single polypeptide as in Swiss:P13569, or belong in different polypeptide chains. [1]. 1864505. Homology between proteins controlling Streptomyces fradiae. tylosin resistance and ATP-binding transport.. Rosteck PR Jr, Reynolds PA, Hershberger CL;. Gene 1991;102:27-32.. [2]. 1977073. Structure and function of haemolysin B,P-glycoprotein and other. members of a novel family of membrane translocators.. Blight MA, Holland IB;. Mol Microbiol 1990;4:873-880.. [3]. 2229036. Binding protein-dependent transport systems.. Higgins CF, Hyde SC, Mimmack MM, Gileadi U, Gill DR, Gallagher. MP;. J Bioenerg Biomembr 1990;22:571-592.. [4]. 9872322. Crystal structure of the ATP-binding subunit of an ABC. transporter.. Hung LW, Wang IX, Nikaido K, Liu PQ, Ames GF, Kim SH;. Nature 1998;396:703-707. (from Pfam)
ABC-F family ATP-binding cassette domain-containing protein
ABC-F family ATP-binding cassette domain-containing protein with duplicated ATPase domains, similar to Caulobacter vibrioides holdfast attachment protein C (also called ATP-binding protein Uup) that binds DNA and has ATPase activity and is implicated in precise excision of transposons
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