The domain within your query sequence starts at position 84 and ends at position 662; the E-value for the Urocanase domain shown below is 2.7e-231.

EMRAYPIDQYPCRTRAAAAIMHMIMNNLDPAVAQFPQELVTYGGNGQVFSNWAQFRLTMS
YLSKMTEEQTLVMYSGHPLGLFPSSPRAPRLVITNGMVIPNYSSRTEYEKLFALGVTMYG
QMTAGSYCYIGPQGIVHGTVLTVLNAGRRYLGIENLAGKVFVTSGLGGMSGAQAKAAAIV
GCIGVIAEVDKAALVKRHRQGWLMEVTDSLDRCIARLREARKKKEVLSLGYHGNVVDLWE
RLVHELDTTGELLVDLGSDQTSCHNPFNGGYYPVQLSFSEAQSLMSSNPAAFKHLVQESL
RRHVAAINRLAQEKFFFWDYGNAFLLEAQRAGADVEKKGANKMEFRYPSYVQHIMGDIFS
QGFGPFRWVCTSGDPQDLAVTDHLATSVLEKAIADGVKASVKLQYMDNIRWIREAAKHQL
VVGSQARILYSDQKGRVAIAVAINQAIASGKIKAPVVLSRDHHDVSGTDSPFRETSNIYD
GSAFCADMAVQNFVGDACRGATWVALHNGGGVGWGEVINGGFGLVLDGTAEAEQKARMML
SWDVSNGVARRCWSGNPKAYEIICQTMQENSGLVVTLPH

Urocanase

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

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 + H 2 O = 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 entry represents the central domain, with a rossmann-like fold, found in Urocanase.

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