{PDOC51901}
{PS51901; ACP_MB}
{BEGIN}
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* Archaeal CBS proteins (ACP)-type metal binding (MB) domain profile *
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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 beta-strands forming a compact
anti-parallel beta-sheet  that  packs  against the CBS domains (see PDB:1PVM>)
[1].

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

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: August 2019 / First entry.

[ 1] Proudfoot 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.
     "Biochemical and structural characterization of a novel family of
     cystathionine beta-synthase domain proteins fused to a Zn ribbon-like
     domain."
     J. Mol. Biol. 375:301-315(2008).
     PubMed=18021800; DOI=10.1016/j.jmb.2007.10.060

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{END}