The domain within your query sequence starts at position 319 and ends at position 683; the E-value for the Urocanase domain shown below is 8.7e-144.

RGESMTWAIQCLMFDHREARKKKEVLSLGYHGNVVDLWERLVHELDTTGELLVDLGSDQT
SCHNPFNGGYYPVQLSFSEAQSLMSSNPAAFKHLVQESLRRHVAAINRLAQEKFFFWDYG
NAFLLEAQRAGADVEKKGANKMEFRYPSYVQHIMGDIFSQGFGPFRWVCTSGDPQDLAVT
DHLATSVLEKAIADGVKASVKLQYMDNIRWIREAAKHQLVVGSQARILYSDQKGRVAIAV
AINQAIASGKIKAPVVLSRDHHDVSGTDSPFRETSNIYDGSAFCADMAVQNFVGDACRGA
TWVALHNGGGVGWGEVINGGFGLVLDGTAEAEQKARMMLSWDVSNGVARRCWSGNPKAYE
IICQT

Urocanase

Urocanase
PFAM accession number:PF01175
Interpro abstract (IPR035085):

This entry represents the central domain, with a rossmann-like fold, found in Urocanase.

Urocanase [(PUBMED:7944380)] (also known as imidazolonepropionate hydrolase or urocanate hydratase) is the enzyme that catalyses the second step in the degradation of histidine, the hydration of urocanate into imidazolonepropionate: urocanate + H2O = 4,5-dihydro-4-oxo-5-imidazolepropanoate Urocanase is found in some bacteria (gene hutU) [(PUBMED:4990470)], in the liver of many vertebrates, and has also been found in the plant Trifolium repens (white clover). Urocanase is a protein of about 60 Kd, it binds tightly to NAD+ and uses it as an electrophil cofactor. A conserved cysteine has been found to be important for the catalytic mechanism and could be involved in the binding of the NAD+.

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