The domain within your query sequence starts at position 338 and ends at position 586; the E-value for the ERM domain shown below is 2.3e-73.

EQMLREKEELMLRLQDYEQKTKRAEKELSEQIEKALQLEEERRRAQEEAERLEADRMAAL
RAKEELERQAQDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQDDLV
KTKEELHLVMTAPPPPPPPVYEPVNYHVQEGLQDEGAEPMGYSAELSSEGILDDRNEEKR
ITEAEKNERVQRQLLTLSNELSQARDENKRTHNDIIHNENMRQGRDKYKTLRQIRQGNTK
QRIDEFEAM

ERM

ERM
PFAM accession number:PF00769
Interpro abstract (IPR011259): The ERM family consists of three closely-related proteins, ezrin, radixin and moesin [(PUBMED:9048483)]. Ezrin was first identified as a constituent of microvilli [(PUBMED:6885906)], radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions [(PUBMED:2500445)], and moesin as a heparin binding protein [(PUBMED:3046603)]. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain; an extended alpha-helical domain; and a charged C-terminal domain [(PUBMED:9048483)]. Ezrin, radixin and merlin also contain a polyproline region between the helical and C-terminal domains. The N-terminal domain is highly conserved, and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily. ERM proteins crosslink actin filaments with plasma membranes. They co-localise with CD44 at actin filament-plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains [(PUBMED:9048483)].

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