The domain within your query sequence starts at position 23 and ends at position 1103; the E-value for the Strumpellin domain shown below is < 1e-12.

NAIIAEVLRLSEFIPAVFLLKDRADQQRYGDIIFDFSYFKGPEFWESKLEAKPELQDLDE
EFRENNIEIVTRFYLAFQSVHKYIVDLNRYLDDLNEGVYIQQTLETVLLSEDGKQLLCEA
LYLYGVMLLVIDQKIEGEVRERMLVSYYRYSAARSSADSNMDDICKLLRSTGYSSQPGAK
RPPNYPESYFQRVPINETFISMVIGRLRSDDIYNQVSAYPLPEHRSTALANQAAMLYVIL
YFEPSILHTHQAKMREIVDKYFPDNWVISIYMGITVNLADAWEPYKAAKTALNNTLDLAN
VKEQASRYASVSDRVRAQVQQFLKEGYLREEVLLDNIPRLLNCLRDCNVAIRWLMLHTAD
SACDPNNKRLRQIKDQILADSRYNPKILFQLLLDTAQFEFILKEMFKQMLSEKQSKWEHY
KKEGSERMTELADVFSGVKPLTRVEKNENLQAWFREISKQILSLNYDDSTAAGRKTVQLI
QALEEVQEFHQLESNLQVCQFLADTRKFLHQMIRTINIKEEVLITVQIIGDLSFAWQLID
SFTSIMQESIRVNPSMVTKLRATFLKLASALDLPLLRINQANSPDLLSVSQYYSGELVSY
VRKVLQIIPESMFTSLLKIIKLQTHDIMEVPTRLDKDKLRDYAQLGPRYEVAKLTHAISI
FTEGILMMKTTLVGIIKVDPKQLLEDGIRKELVKRVAFALHRGLIFNPRAKPSELMPKLK
ELGATMDGFHRSFEYIQDYVSIYGLKIWQEEVSRIINYNVEQECNNFLRTKIQDWQSMYQ
STHIPIPKFAPVDESITFIGRLCREILRITDPKMTCYIDQLNTWYDVKTHQEVTSSRLFS
EIQTTLGTFGLNGLDRLLCFMIVKELQNFLSMFQKIILKERTVQETLKMLMSAVNPLKSI
VANSSKVYLSAITKTQKIWSAYLEAIMKVGQMQILRQQIANELNSSCRFDSRHLAAALDN
LNKALLADIEAHYRDPSLPYPKEDNTLLYEITAYLEAAGIHNPLNKIYITTKRLPYFPIV
NFLFLIAQLPKLQYNKNLGMVCRKPADPVDWPPLVLGLLTLLKQFHSRYTEQFLALIGQF
I

Strumpellin

Strumpellin
PFAM accession number:PF10266
Interpro abstract (IPR019393):

The WASH (WASP and Scar homologue) complex is present at the surface of endosomes and recruits and activates the Arp2/3 complex to induce mediated actin nucleation. The WASH complex plays a key role in the fission of tubules that serve as transport intermediates during endosome sorting [(PUBMED:19922875)].

The WASH complex consists of several subunits: F-actin-capping protein subunit alpha (CAPZA1, CAPZA2 or CAPZA3), F-actin-capping protein subunit beta (CAPZB), WASH (WASH1, WASH2P, WASH3P, WASH4P, WASH5P or WASH6P), FAM21 (FAM21A, FAM21B or FAM21C), KIAA1033, KIAA0196 (strumpellin) and CCDC53.

Strumpellin contains one known domain called a spectrin repeat that consists of three alpha-helices of a characteristic length wrapped in a left-handed coiled coil. The spectrin proteins have multiple copies of this repeat, which can then form multimers in the cell. Spectrin associates with the cell membrane via spectrin repeats in the ankyrin protein. The spectrin repeat is a structural platform for cytoskeletal protein assemblies. Two closely situated point mutations in human strumpellin lead to the condition of hereditary spastic paraplegia.

GO component:WASH complex (GO:0071203)

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