{PDOC51161}
{PS51161; ATP_CONE}
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* ATP-cone domain profile *
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The ATP-cone  domain  is  an  ATP-binding  module of ~85-90 residues, which is
found in  association  with  other  domains  such  as class I+II and class III
ribonucleotide reductases  (see  <PDOC00084>),  the  P-loop  kinase  or a zinc
ribbon. It can be found as a single copy or in two-three tandem copies [1].

The ATP-cone  is  a  compact,  globular  N-terminal domain which includes four
alpha-helices and  three  beta-strands  (see <PDB:3R1R>). The structure of the
ATP-cone domain  resembles  a cone with the surface formed by the four helices
and the  top  by  a  three-stranded beta-sheet. ATP is bound at the top of the
cone just below the beta-sheet [1].

Some proteins known to contain an ATP-cone domain are listed below:

 - Ribonucleotide reductases (RNRs).
 - Archaeal and deinococcal 2-phophoglycerate kinases (2-PGKs).
 - Bacterial ybaD-like proteins.

The profile we developed covers the entire ATP-cone domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: November 2005 / First entry.

[ 1] Aravind L., Wolf Y.I., Koonin E.V.
     "The ATP-cone: an evolutionarily mobile, ATP-binding regulatory
     domain."
     J. Mol. Microbiol. Biotechnol. 2:191-194(2000).
     PubMed=10939243

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