The PRY domain within your query sequence starts at position 453 and ends at position 505, and its E-value is 3.44e-17.

FVKVIFDYNTAHNKVSLSNKYTTASVSDGLQHYRSHPQRFTYCSQVLGLHCYK

PRY
SMART ACC:	SM000589
Description:	associated with SPRY domains
InterPro ACC:	IPR006574
InterPro abstract:	PRY is a 50-60 amino acids domain associated with SPRY domains, adjacent to its N-terminal. The SPRY domain ( IPR003877 ) is a protein-protein interaction module involved in many important signaling pathways [ PUBMED:23139046 expand PRY is a 50-60 amino acids domain associated with SPRY domains, adjacent to its N-terminal. The SPRY domain ( IPR003877 ) is a protein-protein interaction module involved in many important signaling pathways [ PUBMED:23139046 PUBMED:17189197 ]. Distant homologues are domains in butyrophilin/marenostrin/pyrin, evolutionarily more ancient than SPRY/B30.2 counterpart. PRY and SPRY domains are structurally very similar and consist of a β sandwich fold [ PUBMED:23139046 PUBMED:17189197 ]. Ca2+-release from the sarcoplasmic or endoplasmic reticulum, the intracellular Ca2+ store, is mediated by the ryanodine receptor (RyR) and/or the inositol trisphosphate receptor (IP3R). The proteins identified by the PRY domain, clearly fall into 3 sets which can be defined by their combination of signatures: This group contains an immunoglobulin domain N-terminal to the PRY and butyrophilin domains. Butyrophilins are glycoproteins that are expressed on the apical surfaces of secretory cells in lactating mammary tissue and which may function in the secretion of milk-fat droplets. This group contain a RING-finger domain N-terminal to the PRY domain. The RING-finger is a specialised type of Zn-finger of 40 to 60 residues that binds two atoms of zinc, and is probably involved in mediating protein-protein interactions. There are two different variants, the C3HC4-type and a C3H2C3-type, which is clearly related despite the different cysteine/histidine pattern. The latter type is sometimes referred to as 'RING-H2 finger' is not found associated with this group of proteins. This set of proteins are described as TRIM (TRIpartite Motif) family members and are involved in cellular compartmentalisation [ PUBMED:11331580 ]. The TRIM family sequences are defined by a Ring finger domain, a B-box type1 (B1) and a B-box type 2 (B2) followed by a coiled-coil (CC) region [ PUBMED:1412709 ]. Genes belonging to this family are implicated in a variety of processes such as development and cell growth and are involved in human disease. Many of these proteins, with the PRY domain have a number of C-terminal signatures, SPRY, RFP-like (also known as B30.2 domain or PRYSPRY) and butyrophilin domain [ PUBMED:9866204 ]. The third set of proteins have the C-terminal signatures but have no N-terminal RING-finger or immunoglobulin domain signatures. These proteins have not been functionally described. collapse
Family alignment:	View the Family alignment or the Alignment consensus sequence
There are 24 551 PRY domains in 24 280 proteins in SMART's NRDB database.

Taxonomic distribution of proteins containing PRY domains

The tree below includes only several representative species and genera. The complete taxonomic breakdown of all proteins containing PRY domains can be accessed here. Click the counts or percentage values to display the corresponding proteins.

Relevant references for this domain

Primary literature for the PRY domain is listed below. Automatically-derived, secondary literature is also available.

KEGG pathways involving proteins which contain this domain

This information is based on the mapping of SMART genomic protein database to KEGG orthologous groups. Percentages are related to the number of proteins containing a PRY domain which could be assigned to a KEGG orthologous group, and not all proteins containing PRY domains. Please note that proteins can be included in multiple pathways, ie. the numbers below will not add to 100%.

KEGG pathways

KEGG orthologous groups

Some of these KOs are included in the interactive Pathways Explorer overview maps. Select an overview map and click the button below to highlight them in iPath.

3D structures in PDB containing this domain

Links to other resources describing this domain

InterPro	IPR006574