The domain within your query sequence starts at position 14 and ends at position 282; the E-value for the F-actin_cap_A domain shown below is 3.1e-109.

VRIAAKFITHAPPGEFNEVFNDVRLLLNNDNLLREGAAHAFAQYNMDQFTPVKIEGYDDQ
VLITEHGDLGNSRFLDPRNQISFKFDHLRKEASDPQPEDVDGGLKSWRESCDSALRAYVK
DHYSNGFCTVYAKTIDGQQTIIACIESHQFQPKNFWNGRWRSEWKFTITPPSAQVVGVLK
IQVHYYEDGNVQLVSHKDVQDSVTVSNEIQTTKEFIKIIESAENEYQTAISENYQTMSDT
TFKALRRQLPVTRTKIDWNKILSYKIGKE

F-actin_cap_A

F-actin_cap_A
PFAM accession number:PF01267
Interpro abstract (IPR002189):

The F-actin capping protein binds in a calcium-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike gelsolin and severin this protein does not sever actin filaments. The F-actin capping protein is a heterodimer composed of two unrelated subunits: alpha and beta (see IPR001698). Neither of the subunits shows sequence similarity to other filament-capping proteins [(PUBMED:2341404)].

This entry represent the alpha subunit (CAPZA), which is a protein of about 268 to 286 amino acid residues whose sequence is well conserved in eukaryotic species [(PUBMED:1711931)]. In Drosophila mutations in the alpha and beta subunits cause actin accumulation and subsequent retinal degeneration [(PUBMED:16143599)]. In humans CAPZA is part of the WASH complex that controls the fission of endosomes [(PUBMED:19922875)].

GO process:barbed-end actin filament capping (GO:0051016)
GO component:F-actin capping protein complex (GO:0008290)

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