The domain within your query sequence starts at position 533 and ends at position 592; the E-value for the Collagen domain shown below is 2.6e-11.
GIRGMPGSPGGPGNDGKPGPPGSQGESGRPGPPGPSGPRGQPGVMGFPGPKGNDGAPGKN
Collagen |
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PFAM accession number: | PF01391 |
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Interpro abstract (IPR008160): | Members of this family belong to the collagen superfamily [ (PUBMED:8240831) ]. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The sequence is predominantly repeats of the G-X-Y and the polypeptide chains form a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxyproline. Collagens are post-translationally modified by proline hydroxylase to form the hydroxyproline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry Collagen