The domain within your query sequence starts at position 61 and ends at position 165; the E-value for the Rotamase domain shown below is 1.4e-25.

HLLVKHSQSRRPSSWRQEKITRSKEEALELINGYIQKIKSGEEDFESLASQFSDCSSAKA
RGDLGPFSRGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE

Rotamase

Rotamase
PFAM accession number:PF00639
Interpro abstract (IPR000297):

Peptidyl-prolyl cis-trans isomerase (EC 5.2.1.8) (PPIase or rotamase) is an enzyme that accelerates protein folding by catalyzing the cis-trans isomerization of proline imidic peptide bonds in oligopeptides [(PUBMED:2186809)]. Most characterised PPiases belong to two families, the cyclophilin-type and the the FKBP-type. A third family has been discovered [(PUBMED:7925971)]. So far, the only biochemically characterised member of this family is the Escherichia coli protein parvulin (gene ppiC), a small (92 residues) cytoplasmic enzyme that prefers amino acid residues with hydrophobic side chains like leucine and phenylalanine in the P1 position of the peptides substrates.

This entry represents a conserved region that contains a serine which could play a role in the catalytic mechanism of these enzymes

.
GO function:peptidyl-prolyl cis-trans isomerase activity (GO:0003755)

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