The domain within your query sequence starts at position 19 and ends at position 126; the E-value for the dCMP_cyt_deam_1 domain shown below is 5.3e-23.

VQETEKWMEEAMRMAKEALENIEVPVGCLMVYNNEVVGKGRNEVNQTKNATRHAEMVAID
QVLDWCHQHGQSPSTVFEHTVLYVTVEPCIMCAAALRLMKIPLVVYGC

dCMP_cyt_deam_1

dCMP_cyt_deam_1
PFAM accession number:PF00383
Interpro abstract (IPR002125):

Cytidine deaminase (EC 3.5.4.5) (cytidine aminohydrolase) catalyses the hydrolysis of cytidine into uridine and ammonia while deoxycytidylate deaminase (EC 3.5.4.12) (dCMP deaminase) hydrolyses dCMP into dUMP. Both enzymes are known to bind zinc and to require it for their catalytic activity [(PUBMED:1567863), (PUBMED:8428902)]. The deaminases possess either one or two conserved zinc-coordinating (Z) motifs, with the consensus amino acid signature H-x(1)-E-x(24,28)-P-C-x(2,4)-C. This motif is required for catalytic activity. Zinc coordination is mediated by a histidine and two cysteines [(PUBMED:20152150)]. The CMP/dCMP-type deaminase domain consists of a central beta-sheet with one or more alpha helices on each side [(PUBMED:11851403)].

This entry represents the CMP/dCMP-type deaminase domain. Some enzymes, such as riboflavin biosynthesis protein PYRR, have a non-functional deaminase domain that lacks the catalytically essential zinc-binding residues [(PUBMED:23150645)].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry dCMP_cyt_deam_1