PROSITE documentation PDOC51901
Archaeal CBS proteins (ACP)-type metal binding (MB) domain profile


An archaeal family of CBS domain (see <PDOC51371>) proteins that are able to function as electron transfer proteins contains a small (~35 amino acids) C-terminal metal-binding (MB) domain containing four cysteine residues arranged in a Cys-X(2)-Cys-X(14-19)-Cys-X(1-4)-Cys motif. The archaeal CBS proteins (ACP)-type MB domain can bind several metals, with iron and zinc being the most abundant metals [1].

The ACP-type MB domain consists of three short β-strands forming a compact anti-parallel β-sheet that packs against the CBS domains (see PDB:1PVM>) [1].

The profile we developed covers the entire ACP-type MB domain.

Last update:

August 2019 / First entry.


Technical section

PROSITE method (with tools and information) covered by this documentation:

ACP_MB, PS51901; Archaeal CBS proteins (ACP)-type metal binding (MB) domain profile  (MATRIX)


1AuthorsProudfoot M. Sanders S.A. Singer A. Zhang R. Brown G. Binkowski A. Xu L. Lukin J.A. Murzin A.G. Joachimiak A. Arrowsmith C.H. Edwards A.M. Savchenko A.V. Yakunin A.F.
TitleBiochemical and structural characterization of a novel family of cystathionine beta-synthase domain proteins fused to a Zn ribbon-like domain.
SourceJ. Mol. Biol. 375:301-315(2008).
PubMed ID18021800

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