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cation transporter dimerization domain-containing protein
ZT_dimer is the dimerisation region of the whole molecule of zinc transporters since the full-length members form a homodimer during activity. The domain lies within the cytoplasm and exhibits an overall structural similarity with the copper metallochaperone Hah1 UniProtKB:O00244, exhibiting an open alpha-beta domain with two alpha helices (H1 and H2) aligned on one side and a three-stranded mixed beta-sheet (S1 to S3) on the other side. The N-terminal part of the members is the Cation_efflux family, Pfam:PF01545 [1]. [1]. 17717154. Structure of the zinc transporter YiiP.. Lu M, Fu D;. Science. 2007;317:1746-1748. (from Pfam)
cation transporter
Members of this family are integral membrane proteins, that are found to increase tolerance to divalent metal ions such as cadmium, zinc, and cobalt. These proteins are thought to be efflux pumps that remove these ions from cells. [1]. 9696746. Molecular characterization of a chromosomal determinant. conferring resistance to zinc and cobalt ions in Staphylococcus. aureus.. Xiong A, Jayaswal RK;. J Bacteriol 1998;180:4024-4029.. [2]. 8829543. Cloning and sequence analysis of czc genes in Alcaligenes sp.. strain CT14.. Kunito T, Kusano T, Oyaizu H, Senoo K, Kanazawa S, Matsumoto S;. Biosci Biotechnol Biochem 1996;60:699-704. (from Pfam)
cation diffusion facilitator family transporter
This HMM describes a broadly distributed family of transporters, a number of which have been shown to transport divalent cations of cobalt, cadmium and/or zinc. The family has six predicted transmembrane domains. Members of the family are variable in length because of variably sized inserts, often containing low-complexity sequence.
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