The domain within your query sequence starts at position 22 and ends at position 352; the E-value for the Pro_racemase domain shown below is 8.7e-122.

VVDMHTGGEPLRIVHAGCPEVAGPTLLAKRRYMRQHLDYIRRRLVFEPRGHRDMYGAILV
PSELPDAHLGVLFLHNEGYSSMCGHAVLALGRFALDFGLVPAPPKGAREAQVNIHCPCGL
VTAFVECEGGRSCGPVRFHSVPAFVLASDLTVDVPGHGKVLVDIAYGGAFYAFVSAEKLG
LDVCSAKTRDLVDAASALTGAVKAQFKINHPESEDLGFLYGSILTDGKDAYSEEATTNIC
VFADEQVDRSPTGSGVTARIALQYHKGLLQLNQTRAFKSSATGSVFTGCAVREAKCGDFK
AVIVEVAGQAHYTGTANLTVEDGDPLRDGFL

Pro_racemase

• PFAM accession number: PF05544
• Interpro abstract (IPR008794):

  This family consists of proline racemase ( EC 5.1.1.4 ), 4-hydroxyproline epimerase ( EC 5.1.1.8 ), and trans-L-3-hydroxyproline dehydratase ( EC 4.2.1.77 ).

  Proline racemase catalyses the interconversion of L- and D-proline in bacteria [ (PUBMED:3755058) ]. Although the mechanisms of aminoacid racemisation and epimerisation are conserved between proline racemase and hydroxyproline epimerase, substrate specificity partly rely on constraints imposed by certain residues distinctively belonging to the catalytic pocket [ (PUBMED:17849014) ]. A human proline racemase-like gene, lacking a specific cysteine residue critical for racemase activity, has been identified as a trans-3-hydroxy-L-proline dehydratase [ (PUBMED:22528483) ]. This family also contains several proteins that remain uncharacterised.

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