SMART: Pfam domain Kazal

The domain within your query sequence starts at position 44 and ends at position 92; the E-value for the Kazal_1 domain shown below is 6.4e-9.

CIKNIQLCWILSYFKVSEPICGSNQVTYEGECHLCSGILNTPRMSLNTD

Kazal_1

PFAM accession number:	PF00050
Interpro abstract (IPR002350):	Canonical serine proteinase inhibitors are distributed in a wide range of organisms from all kingdoms of life and play crucial role in various physiological mechanisms [ (PUBMED:6996568) ]. They interact from the canonical proteinase-inhibitor binding loop, where P1 residue has a predominant role (the residue at the P1 position contributing the carbonyl portion to the reactive-site peptide bond). These so-called canonical inhibitors bind to their cognate enzymes in the same manner as a good substrate, but are cleaved extremely slowly. Kazal-type inhibitors represent the most studied canonical proteinase inhibitors. Kazal inhibitors are extremely variable at their reactive sites. However, some regularity prevails such as the presence of lysine at position P1 indicating strong inhibition of trypsin [ (PUBMED:10708867) ]. The Kazal inhibitor has six cysteine residues engaged in disulfide bonds arranged as shown in the following schematic representation: +------------------+ \| \| *****************\|* xxxxxxxxCxxxxxxCx#xxxxxCxxxxxxxxxxCxxCxxxxxxxxxxxxxxxxxC \| \| \| \| \| +-------------\|-----------------+ +----------------------------+ 'C': conserved cysteine involved in a disulfide bond. '#': active site residue. '*': position of the pattern. The structure of classical Kazal domains consists of a central alpha helix, which is inserted between two beta-strands and a third that is toward the C terminus [ (PUBMED:6752426) ]. The reactive site P1 and the conformation of the reactive site loop is structurally highly conserved, similar to the canonical conformation of small serine proteinase inhibitors. This entry represents the Kazal domain.
GO function:	protein binding (GO:0005515)

PFAM accession number:

PF00050

Interpro abstract (IPR002350):

Canonical serine proteinase inhibitors are distributed in a wide range of organisms from all kingdoms of life and play crucial role in various physiological mechanisms [ (PUBMED:6996568) ]. They interact from the canonical proteinase-inhibitor binding loop, where P1 residue has a predominant role (the residue at the P1 position contributing the carbonyl portion to the reactive-site peptide bond). These so-called canonical inhibitors bind to their cognate enzymes in the same manner as a good substrate, but are cleaved extremely slowly. Kazal-type inhibitors represent the most studied canonical proteinase inhibitors. Kazal inhibitors are extremely variable at their reactive sites. However, some regularity prevails such as the presence of lysine at position P1 indicating strong inhibition of trypsin [ (PUBMED:10708867) ].

The Kazal inhibitor has six cysteine residues engaged in disulfide bonds arranged as shown in the following schematic representation:


                       +------------------+
                       |                  |
                       *******************|***
        xxxxxxxxCxxxxxxCx#xxxxxCxxxxxxxxxxCxxCxxxxxxxxxxxxxxxxxC
                |              |             |                 |
                |              +-------------|-----------------+
                +----------------------------+

'C': conserved cysteine involved in a disulfide bond.
'#': active site residue.
'*': position of the pattern.

The structure of classical Kazal domains consists of a central alpha helix, which is inserted between two beta-strands and a third that is toward the C terminus [ (PUBMED:6752426) ]. The reactive site P1 and the conformation of the reactive site loop is structurally highly conserved, similar to the canonical conformation of small serine proteinase inhibitors.

This entry represents the Kazal domain.

GO function:

protein binding (GO:0005515)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Kazal_1