The domain within your query sequence starts at position 473 and ends at position 572; the E-value for the Transglut_C domain shown below is 5.7e-29.

VAMRIRVGDSMSMGNDFDVFAHIGNDTSETRECRLLLCARTVSYNGVLGPECGTEDINLT
LDPYSENSIPLRILYEKYSGCLTESNLIKVRGLLIEPAAN

Transglut_C

Transglut_C
PFAM accession number:PF00927
Interpro abstract (IPR008958):

Synonym(s): Protein-glutamine gamma-glutamyltransferase, Fibrinoligase, TGase

Transglutaminases catalyse the post-translational modification of proteins at glutamine residues, with formation of isopeptide bonds. Members of the transglutaminase family usually have three domains: N-terminal (IPR001102), middle (IPR013808) and C-terminal. The middle domain is usually well conserved, but family members can display major differences in their N- and C-terminal domains, although their overall structure is conserved [(PUBMED:10411627)]. This entry represents the C-terminal domain found in transglutaminases, which consists of an immunoglobulin-like beta-sandwich consisting of seven strands in two sheets with a Greek key topology.

The best known transglutaminase is blood coagulation factor XIII, a plasma tetrameric protein composed of two catalytic A subunits and two non-catalytic B subunits. Factor XIII is responsible for cross-linking fibrin chains, thus stabilising the fibrin clot. Protein-glutamine gamma-glutamyltransferases (EC 2.3.2.13) are calcium-dependent enzymes that catalyse the cross-linking of proteins by promoting the formation of isopeptide bonds between the gamma-carboxyl group of a glutamine in one polypeptide chain and the epsilon-amino group of a lysine in a second polypeptide chain. TGases also catalyse the conjugation of polyamines to proteins [(PUBMED:1683845), (PUBMED:1974250)].

GO process:peptide cross-linking (GO:0018149)
GO function:protein-glutamine gamma-glutamyltransferase activity (GO:0003810)

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