The domain within your query sequence starts at position 4 and ends at position 73; the E-value for the SRP9-21 domain shown below is 6.7e-15.

FQTWEEFSRAAEKLYLADPMKVRVVLKYRHVDGNLCIKVTDDLVCLVYRTDQAQDVKKIE
KFHSQLMRLM

SRP9-21

SRP9-21
PFAM accession number:PF05486
Interpro abstract (IPR039432):

The signal recognition particle (SRP) is a multimeric protein, which along with its conjugate receptor (SR), is involved in targeting secretory proteins to the rough endoplasmic reticulum (RER) membrane in eukaryotes, or to the plasma membrane in prokaryotes [ (PUBMED:17622352) (PUBMED:16469117) ]. SRP recognises the signal sequence of the nascent polypeptide on the ribosome. In eukaryotes this retards its elongation until SRP docks the ribosome-polypeptide complex to the RER membrane via the SR receptor [ (PUBMED:12605305) ]. Eukaryotic SRP consists of six polypeptides (SRP9, SRP14, SRP19, SRP54, SRP68 and SRP72) and a single 300 nucleotide 7S RNA molecule. The RNA component catalyses the interaction of SRP with its SR receptor [ (PUBMED:17507650) ]. In higher eukaryotes, the SRP complex consists of the Alu domain and the S domain linked by the SRP RNA. The Alu domain consists of a heterodimer of SRP9 and SRP14 bound to the 5' and 3' terminal sequences of SRP RNA. This domain is necessary for retarding the elongation of the nascent polypeptide chain, which gives SRP time to dock the ribosome-polypeptide complex to the RER membrane. In archaea, the SRP complex contains 7S RNA like its eukaryotic counterpart, yet only includes two of the six protein subunits found in the eukarytic complex: SRP19 and SRP54 [ (PUBMED:12364595) ].

This domain can be found in human SRP9 protein and its homologues, such as the Srp21 protein from budding yeasts [ (PUBMED:7925282) ]. These proteins are part of the signal recognition particle (SRP) [ (PUBMED:7730321) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry SRP9-21