The domain within your query sequence starts at position 69 and ends at position 154; the E-value for the KR domain shown below is 3.2e-36.



Kringle domain
SMART accession number:SM00130
Description: Named after a Danish pastry. Found in several serine proteases and in ROR-like receptors. Can occur in up to 38 copies (in apolipoprotein(a)). Plasminogen-like kringles possess affinity for free lysine and lysine- containing peptides.
Interpro abstract (IPR000001):

Kringles are autonomous structural domains, found throughout the blood clotting and fibrinolytic proteins. Kringle domains are believed to play a role in binding mediators (e.g., membranes, other proteins or phospholipids), and in the regulation of proteolytic activity [(PUBMED:3886654), (PUBMED:6373375), (PUBMED:2157850)]. Kringle domains [(PUBMED:3131537), (PUBMED:3891096), (PUBMED:1879523)] are characterised by a triple loop, 3-disulphide bridge structure, whose conformation is defined by a number of hydrogen bonds and small pieces of anti-parallel beta-sheet. They are found in a varying number of copies in some plasma proteins including prothrombin and urokinase-type plasminogen activator, which are serine proteases belonging to MEROPS peptidase family S1A.

Family alignment:
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There are 13009 KR domains in 7555 proteins in SMART's nrdb database.

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