The domain within your query sequence starts at position 105 and ends at position 138; the E-value for the C1q domain shown below is 1.5e-6.



PFAM accession number:PF00386
Interpro abstract (IPR001073):

This entry represents the C-terminal domain of C1q. C1q is a subunit of the C1 enzyme complex that activates the serum complement system. C1q comprises 6 A, 6 B and 6 C chains. These share the same topology, each possessing a small, globular N-terminal domain, a collagen-like Gly/Pro-rich central region, and a conserved C-terminal region, the C1q domain [ (PUBMED:1706597) ]. The C1q protein is produced in collagen-producing cells and shows sequence and structural similarity to collagens VIII and X [ (PUBMED:2591537) (PUBMED:2019595) ]. This domain is also found in multimerin and EMILIN proteins.

The C-terminal globular domain of the C1q subcomponents and collagen types VIII and X is important both for the correct folding and alignment of the triple helix and for protein-protein recognition events [ (PUBMED:1867713) ]. For collagen type X it has been suggested that the domain is important for initiation and maintenance of the correct assembly of the protein [ (PUBMED:1860888) ]. The globular head is a trimer of C1q domains. Each individual C1q adopts a 10-strand Jelly-roll fold arranged in two antiparallel 5-stranded beta-sheets [ (PUBMED:22892318) ]. There are two well conserved regions within the C1q domain: an aromatic motif is located within the first half of the domain, the other conserved region is located near the C-terminal extremity.

This is a PFAM domain. For full annotation and more information, please see the PFAM entry C1q