BPTI-like superfamily

SCOP classification

• Root: SCOP hierarchy in SUPERFAMILY [ 0] (11)
• Class: Small proteins [ 56992] (85)
  • Usually dominated by metal ligand, heme, and/or disulfide bridges
• Fold: BPTI-like [ 57361]
  • disulfide-rich alpha+beta fold
• Superfamily: BPTI-like [ 57362] (2)
• Families:
  • Small Kunitz-type inhibitors & BPTI-like toxins [ 57363] (12)
  • Soft tick anticoagulant proteins [ 57386] (2)

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Superfamily statistics

	Genomes (95)	UniProt 15.0	PDB chains (SCOP 1.73)
Domains	3,542	2,018	53
Proteins	1,762	1,189	51

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Functional annotation

• General category: Processes_IC
• Detailed category: Proteases

Function annotation of SCOP domain superfamilies

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InterPro annotation

• Cross references: IPR002223 SSF57362 Protein matches
• Abstract:

  The majority of the sequences having this domain belong to the MEROPS inhibitor family I2, clan IB; the Kunitz/bovine pancreatic trypsin inhibitor family, they inhibit proteases of the S1 family [14705960] and are restricted to the metazoa with a single exception: Amsacta moorei entomopoxvirus. They are short (~50 residue) alpha/beta proteins with few secondary structures. The fold is constrained by 3 disulphide bonds. The type example for this family is aprotinin (bovine pancreatic trypsin inhibitor) [1714504] (or basic protease inhibitor), but the family includes numerous other members [1703675, 1593645, 8159751, 1304909], such as snake venom basic protease; mammalian inter-alpha-trypsin inhibitors; trypstatin, a rat mast cell inhibitor of trypsin; a domain found in an alternatively-spliced form of Alzheimer's amyloid beta-protein; domains at the C-termini of the alpha(1) and alpha(3) chains of type VII and type VI collagens; and tissue factor pathway inhibitor precursor.

InterPro database

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