The domain within your query sequence starts at position 578 and ends at position 682; the E-value for the Transglut_C domain shown below is 3.6e-24.

VAMQVEAQDAVMGQDLAVSVVLTNRGSSRRTVKLHLYLCVTYYTGVSGPTFKEAKKEVTL
APGASDSVTMPVAYKEYKPHLVDQGAMLLNVSGHVKESGQVLAKQ

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