PROSITE documentation PDOC52031
GG-type lectin domain profile


The GG domain, with two well-conserved glycine residues, is present in eukaryotic FAM3 superfamily (FAM3A, FAM3B, FAM3C and FAM3D), POMGnT1 (protein O-linked mannose β-1,2-N-acetylglucosaminyltransferase), TEM2 proteins as well as phage gp35 proteins. The presence of a GG domain in Bacteriophage gp35 hinge connector of long tail fiber might reflect the horizontal gene transfer from organisms [1,2]. The GG domain is a lectin with carbohydrate-binding activity [3,4].

The GG-type lectin domain exhibits a β-β-α three-layer architecture with two antiparallel β sheets and one layer of short helices (see <PDB:2YOP>. The core of the fold is mainly hydrophobic [2,3,4].

The profile we developed covers the entire GG-type lectin domain.

Last update:

July 2023 / First entry.


Technical section

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

GG_LECTIN, PS52031; GG-type lectin domain profile  (MATRIX)


1AuthorsGuo J. Cheng H. Zhao S. Yu L.
TitleGG: a domain involved in phage LTF apparatus and implicated in human MEB and non-syndromic hearing loss diseases.
SourceFEBS. Lett. 580:581-584(2006).
PubMed ID16406369

2AuthorsJohansson P. Bernstroem J. Gorman T. Oester L. Baeckstroem S. Schweikart F. Xu B. Xue Y. Schiavone L.H.
TitleFAM3B PANDER and FAM3C ILEI represent a distinct class of signaling molecules with a non-cytokine-like fold.
SourceStructure 21:306-313(2013).
PubMed ID23333428

3AuthorsKuwabara N. Manya H. Yamada T. Tateno H. Kanagawa M. Kobayashi K. Akasaka-Manya K. Hirose Y. Mizuno M. Ikeguchi M. Toda T. Hirabayashi J. Senda T. Endo T. Kato R.
TitleCarbohydrate-binding domain of the POMGnT1 stem region modulates O-mannosylation sites of alpha-dystroglycan.
SourceProc. Natl. Acad. Sci. U. S. A. 113:9280-9285(2016).
PubMed ID27493216

4AuthorsNiu M. McGrath M. Sammon D. Gardner S. Morgan R.M. Di Maio A. Liu Y. Bubeck D. Hohenester E.
TitleStructure of the transmembrane protein 2 (TMEM2) ectodomain and its apparent lack of hyaluronidase activity.
SourceWellcome. Open. Res. 8:76-76(2023).
PubMed ID37234743

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