SMART: Pfam domain ATP-cone

The domain within your query sequence starts at position 1 and ends at position 89; the E-value for the ATP-cone domain shown below is 8.7e-21.

MHVIKRDGRQERVMFDKITSRIQKLCYGLNMDFVDPAQITMKVIQGLYSGVTTVELDTLA
AETAATLTTKHPDYAILAARIAVSNLHKE

ATP-cone

PFAM accession number:	PF03477
Interpro abstract (IPR005144):	The ATP-cone is an evolutionarily mobile, ATP-binding regulatory domain which is found in a variety of proteins including ribonucleotide reductases, phosphoglycerate kinases and transcriptional regulators [ (PUBMED:10939243) ]. In ribonucleotide reductase protein R1 ( P28903 ) from Escherichia coli this domain is located at the N terminus, and is composed mostly of helices [ (PUBMED:8052308) ]. It forms part of the allosteric effector region and contains the general allosteric activity site in a cleft located at the tip of the N-terminal region [ (PUBMED:9309223) ]. This site binds either ATP (activating) or dATP (inhibitory), with the base bound in a hydrophobic pocket and the phosphates bound to basic residues. Substrate binding to this site is thought to affect enzyme activity by altering the relative positions of the two subunits of ribonucleotide reductase.

PFAM accession number:

PF03477

Interpro abstract (IPR005144):

The ATP-cone is an evolutionarily mobile, ATP-binding regulatory domain which is found in a variety of proteins including ribonucleotide reductases, phosphoglycerate kinases and transcriptional regulators [ (PUBMED:10939243) ].

In ribonucleotide reductase protein R1 ( P28903 ) from Escherichia coli this domain is located at the N terminus, and is composed mostly of helices [ (PUBMED:8052308) ]. It forms part of the allosteric effector region and contains the general allosteric activity site in a cleft located at the tip of the N-terminal region [ (PUBMED:9309223) ]. This site binds either ATP (activating) or dATP (inhibitory), with the base bound in a hydrophobic pocket and the phosphates bound to basic residues. Substrate binding to this site is thought to affect enzyme activity by altering the relative positions of the two subunits of ribonucleotide reductase.

This is a PFAM domain. For full annotation and more information, please see the PFAM entry ATP-cone