PROSITE documentation PDOC51087
ApaG domain profile


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 (see <PDOC50181>). 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 β-sheets (see <PDB:1XVS>). The apaG domain may be involved in protein-protein interactions which could be implicated in substrate-specificity [1,2,3,4].

Some proteins known to contain an apaG domain:

  • Escherichia coli apaG, a protein that is well-conserved among diverse bacteria.
  • Salmonella typhimurium apaG/corD, involved in Co(2+) sensitivity and Mg(2+) homeostasis [1].
  • Mammalian FBA/F-box only protein 3, a substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex [2].
  • Mammalian PDIP38/POLD2-interacting protein, which interacts with proliferating cell nuclear antigen (PCNA) and the p50 subunit of DNA polymerase delta. It is conserved among metazoans [3].

The profile we developed covers the entire apaG domain.

Last update:

March 2005 / First entry.


Technical section

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

APAG, PS51087; ApaG domain profile  (MATRIX)


1AuthorsGibson M.M. Bagga D.A. Miller C.G. Maguire M.E.
TitleMagnesium transport in Salmonella typhimurium: the influence of new mutations conferring Co2+ resistance on the CorA Mg2+ transport system.
SourceMol. Microbiol. 5:2753-2762(1991).
PubMed ID1779764

2AuthorsIlyin G.P. Rialland M. Pigeon C. Guguen-Guillouzo C.
TitlecDNA cloning and expression analysis of new members of the mammalian F-box protein family.
SourceGenomics 67:40-47(2000).
PubMed ID10945468

3AuthorsLiu L. Rodriguez-Belmonte E.M. Mazloum N. Xie B. Lee M.Y.W.T.
TitleIdentification of a novel protein, PDIP38, that interacts with the p50 subunit of DNA polymerase delta and proliferating cell nuclear antigen.
SourceJ. Biol. Chem. 278:10041-10047(2003).
PubMed ID12522211

4AuthorsKatsuyama A.M. Cicero D.O. Spisni A. Paci M. Farah C.S. Pertinhez T.A.
Title1H, 15N and 13C resonance assignments of the ApaG protein of the phytopathogen Xanthomonas axonopodis pv. citri.
SourceJ. Biomol. NMR 29:423-424(2004).
PubMed ID15213450

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