SMART: Pfam domain DUF525

The domain within your query sequence starts at position 252 and ends at position 338; the E-value for the DUF525 domain shown below is 2.3e-30.

MREAQNSHVYWWRYCIRLENLDSDVVQLRERHWRIFSLSGTLETVRGRGVVGREPVLSKE
QPAFQYSSHVSLQASSGHMWGTFRFER

DUF525

PFAM accession number:	PF04379
Interpro abstract (IPR007474):	The apaG domain is a ~125 amino acids domain present in bacterial apaG proteins and in eukaryotic F-box proteins. The domain is named after the bacterial apaG protein, of which it forms the core. The domain also occurs in the C-terminal part of eukaryotic proteins with an N-terminal F-box domain. The Salmonella typhimurium apaG domain protein corD is involved in Co(2+) resistance and Mg(2+) efflux. Tertiary structures from different apaG proteins show a fold of several beta-sheets. The apaG domain may be involved in protein-protein interactions which could be implicated in substrate-specificity [ (PUBMED:1779764) (PUBMED:10945468) (PUBMED:12522211) (PUBMED:15213450) ].

PFAM accession number:

PF04379

Interpro abstract (IPR007474):

The apaG domain is a ~125 amino acids domain present in bacterial apaG proteins and in eukaryotic F-box proteins. The domain is named after the bacterial apaG protein, of which it forms the core. The domain also occurs in the C-terminal part of eukaryotic proteins with an N-terminal F-box domain. The Salmonella typhimurium apaG domain protein corD is involved in Co(2+) resistance and Mg(2+) efflux. Tertiary structures from different apaG proteins show a fold of several beta-sheets. The apaG domain may be involved in protein-protein interactions which could be implicated in substrate-specificity [ (PUBMED:1779764) (PUBMED:10945468) (PUBMED:12522211) (PUBMED:15213450) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry DUF525