SMART: Pfam domain HH

The domain within your query sequence starts at position 66 and ends at position 227; the E-value for the HH_signal domain shown below is 2.7e-88.

RYEGKIARSSERFKELTPNYNPDIIFKDEENTGADRLMTQRCKDRLNSLAISVMNQWPGV
KLRVTEGWDEDGHHSEESLHYEGRAVDITTSDRDRNKYGLLARLAVEAGFDWVYYESKAH
VHCSVKSEHSAAAKTGGCFPAGAQVRLENGERVALSAVKPGD

HH_signal

PFAM accession number:	PF01085
Interpro abstract (IPR000320):	This entry represents the N-terminal domain of hedgehog proteins, which is responsible for signalling following cleavage from the C-terminal domain. Its structure has been solved, and reveals a tetrahedrally coordinated zinc ion that appears to be structurally analogous to the zinc coordination sites of zinc hydrolases, such as thermolysin and carboxypeptidase A [ (PUBMED:7477329) ]. This putative catalytic site represents a distinct activity from the autoprocessing activity that resides in the carboxy-terminal domain. Hedgehog proteins are a family of secreted signal molecules required for embryonic cell differentiation. They are synthesised as inactive precursors with an N-terminal signalling domain linked to a C-terminal autoprocessing domain. The three-dimensional structure of the autolytic domain of the hedgehog protein of shows similarity with the beta-strand core of intein splicing domains. It has hence been termed the hint (Hedgehog/Intein) domain [ (PUBMED:9489693) ].
GO process:	cell-cell signaling (GO:0007267)

PFAM accession number:

PF01085

Interpro abstract (IPR000320):

This entry represents the N-terminal domain of hedgehog proteins, which is responsible for signalling following cleavage from the C-terminal domain. Its structure has been solved, and reveals a tetrahedrally coordinated zinc ion that appears to be structurally analogous to the zinc coordination sites of zinc hydrolases, such as thermolysin and carboxypeptidase A [ (PUBMED:7477329) ]. This putative catalytic site represents a distinct activity from the autoprocessing activity that resides in the carboxy-terminal domain.

Hedgehog proteins are a family of secreted signal molecules required for embryonic cell differentiation. They are synthesised as inactive precursors with an N-terminal signalling domain linked to a C-terminal autoprocessing domain. The three-dimensional structure of the autolytic domain of the hedgehog protein of shows similarity with the beta-strand core of intein splicing domains. It has hence been termed the hint (Hedgehog/Intein) domain [ (PUBMED:9489693) ].

GO process:

cell-cell signaling (GO:0007267)

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