The domain within your query sequence starts at position 9 and ends at position 153; the E-value for the P16-Arc domain shown below is 2.4e-58.

RFRRVDIDEFDENKFVDEHEEAAAAAGEPGPDPCEVDGLLRQGDMLRAFHAALRNSPINT
KNQAVKERAQGVVLKVLTNFKSSEIEQAVQSLDRNGIDLLMKYIYKGFEKPTENSSAVLL
QWHEKALAVGGLGSIIRVLTARKTV

P16-Arc

P16-Arc
PFAM accession number:PF04699
Interpro abstract (IPR006789):

Arp2/3 binds to pre-existing actin filaments and nucleates new daughter filaments, and thus becomes incorporated into the dynamic actin network at the leading edge of motile cells and other actin-based protrusive structures [(PUBMED:9600938)]. In order to nucleate filaments, Arp2/3 must bind to a member of the N-WASp/SCAR family protein [(PUBMED:9889097)]. Arp2 and Arp3 are thought to be brought together after activation, forming an actin-like nucleus for actin monomers to bind and create a new actin filament. In the absence of an activating protein, Arp2/3 shows very little nucleation activity. Recent research has focused on the binding and hydrolysis of ATP by Arp2 and Arp3 [(PUBMED:11752435)], and crystal structures of the Arp2/3 complex have been solved [(PUBMED:15505213)].

The human Arp2/3 complex consists of ARP2, ARP3, ARPC1B/p41-ARC, ARPC2/p34-ARC, ARPC3/p21-ARC, ARPC4/p20-ARC and ARPC5/p16-ARC. This family represents the ARPC5/p16-ARC subunit.

GO process:regulation of actin filament polymerization (GO:0030833), Arp2/3 complex-mediated actin nucleation (GO:0034314)
GO component:Arp2/3 protein complex (GO:0005885), actin cytoskeleton (GO:0015629)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry P16-Arc