The domain within your query sequence starts at position 209 and ends at position 271; the E-value for the TRP_2 domain shown below is 2.6e-27.

MLTEEDPILRAFELSADLKELSLVEVEFRNDYEELARQCKMFAKDLLAQARNSRELEVIL
NHT

TRP_2

TRP_2
PFAM accession number:PF08344
Interpro abstract (IPR013555):

TRP (transient receptor potential) channels can be described as tetramers formed by subunits with six transmembrane domains and containing cation-selective pores, which in several cases show high calcium permeability. The molecular architecture of TRP channels is reminiscent of voltage-gated channels and comprises six putative transmembrane segments (S1-S6), intracellular N- and C-termini, and a pore-forming reentrant loop between S5 and S6 [(PUBMED:18535090)].

TRP channels represent a superfamily conserved from worms to humans that comprise seven subfamilies [(PUBMED:20025796)]: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin or long TRPs), TRPA (ankyrin), whose only member is the transmembrane protein 1, TRPP(polycystin), TRPML (mucolipin) and TRPN (Nomp-C homologues), which has a single member that can be found in worms, flies, and zebrafish. TRPs are classified essentially according to their primary amino acid sequence rather than selectivity or ligand affinity, due to their heterogenous properties and complex regulation.

TRP channels are involved in many physiological functions, ranging from pure sensory functions, such as pheromone signalling, taste transduction, nociception, and temperature sensation, over homeostatic functions, such as Ca2+ and Mg2+ reabsorption and osmoregulation, to many other motile functions, such as muscle contraction and vaso-motor control [(PUBMED:20861159)].

This domain is found in some Trp proteins, and is generally located C-terminal to ankyrin repeats (IPR002110).

This is a PFAM domain. For full annotation and more information, please see the PFAM entry TRP_2