The domain within your query sequence starts at position 1970 and ends at position 2004; the E-value for the OTCace_N domain shown below is 4.6e-11.

YELAAKHCRRPVINAGDGVGEHPTQALLDIFTIRE

OTCace_N

OTCace_N
PFAM accession number:PF02729
Interpro abstract (IPR006132):

This entry contains two related enzymes:

  1. Aspartate carbamoyltransferase (EC 2.1.3.2) (ATCase) catalyzes the conversion of aspartate and carbamoyl phosphate to carbamoylaspartate, the second step in the de novo biosynthesis of pyrimidine nucleotides [(PUBMED:3015959)]. In prokaryotes ATCase consists of two subunits: a catalytic chain (gene pyrB) and a regulatory chain (gene pyrI), while in eukaryotes it is a domain in a multi- functional enzyme (called URA2 in yeast, rudimentary in Drosophila, and CAD in mammals [(PUBMED:8098212)]) that also catalyzes other steps of the biosynthesis of pyrimidines.
  2. Ornithine carbamoyltransferase (EC 2.1.3.3) (OTCase) catalyzes the conversion of ornithine and carbamoyl phosphate to citrulline. In mammals this enzyme participates in the urea cycle [(PUBMED:2662961)] and is located in the mitochondrial matrix. In prokaryotes and eukaryotic microorganisms it is involved in the biosynthesis of arginine. In some bacterial species it is also involved in the degradation of arginine [(PUBMED:3109911)] (the arginine deaminase pathway).
It has been shown [(PUBMED:6379651)] that these two enzymes are evolutionary related. The predicted secondary structure of both enzymes are similar and there are some regions of sequence similarities. One of these regions includes three residues which have been shown, by crystallographic studies [(PUBMED:6377306)], to be implicated in binding the phosphoryl group of carbamoyl phosphate and may also play a role in trimerization of the molecules [(PUBMED:10318893)]. The carboxyl-terminal, aspartate/ornithine-binding domain is is described by IPR006131.

GO process:cellular amino acid metabolic process (GO:0006520)
GO function:carboxyl- or carbamoyltransferase activity (GO:0016743)

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