SMART: Pfam domain GGACT

The domain within your query sequence starts at position 19 and ends at position 143; the E-value for the GGACT domain shown below is 2.2e-11.

YFAYGSNLLTERIHLRNPSAVFCCVARLQDFKLDFGNFQGKMSERWHGGIATIFQSPGDE
VWGVVWRMNKSNISSLDEQEGVKSGVYVVIEIKVSTREGKEITCRSYLMTNYESAPPSPQ
YKKVI

GGACT

PFAM accession number:	PF06094
Interpro abstract (IPR009288):	This entry represents a domain found in a group of gamma-glutamyl cyclotransferases (GGCTs), including AIG2 from Arabidopsis. GGCT is a ubiquitous enzyme found in bacteria, plants, and metazoans from Dictyostelium through to humans. It converts gamma-glutamylamines to free amines and 5-oxoproline [ (PUBMED:20110353) (PUBMED:20851126) (PUBMED:17462573) ]. AIG2 is an Arabidopsis protein that exhibit RPS2- and avrRpt2-dependent induction early after infection with Pseudomonas syringae pv maculicola strain ES4326 carrying avrRpt2 [ (PUBMED:8742710) ]. Its structure consists of a five-stranded beta-barrel surrounded by two alpha-helices and a small beta-sheet. A long flexible alpha-helix protrudes from the structure at the C-terminal end. Conserved residues in a hydrophilic cavity, which are able to bind small ligands, may act as an active site in AIG2-like proteins [ (PUBMED:16754964) ].

PFAM accession number:

PF06094

Interpro abstract (IPR009288):

This entry represents a domain found in a group of gamma-glutamyl cyclotransferases (GGCTs), including AIG2 from Arabidopsis. GGCT is a ubiquitous enzyme found in bacteria, plants, and metazoans from Dictyostelium through to humans. It converts gamma-glutamylamines to free amines and 5-oxoproline [ (PUBMED:20110353) (PUBMED:20851126) (PUBMED:17462573) ].

AIG2 is an Arabidopsis protein that exhibit RPS2- and avrRpt2-dependent induction early after infection with Pseudomonas syringae pv maculicola strain ES4326 carrying avrRpt2 [ (PUBMED:8742710) ]. Its structure consists of a five-stranded beta-barrel surrounded by two alpha-helices and a small beta-sheet. A long flexible alpha-helix protrudes from the structure at the C-terminal end. Conserved residues in a hydrophilic cavity, which are able to bind small ligands, may act as an active site in AIG2-like proteins [ (PUBMED:16754964) ].

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