The domain within your query sequence starts at position 1668 and ends at position 2222; the E-value for the Carboxyl_trans domain shown below is 2.7e-175.

PEYPDGRDIIVIGNDITYRIGSFGPQEDLLFLRASELARAEGIPRIYVAANSGARIGLAE
EIRHMFHVAWVDPEDPYKGYKYLYLTPQDYKRVSALNSVHCEHVEDEGESRYKITDIIGK
EEGLGAENLRGSGMIAGESSLAYDEVITISLVTCRAIGIGAYLVRLGQRTIQVENSHLIL
TGAGALNKVLGREVYTSNNQLGGIQIMHNNGVTHSTVCDDFEGVFTVLHWLSYMPKSVHS
SVPLLNSKDPIDRIIEFVPTKAPYDPRWMLAGRPHPTQKGQWLSGFFDYGSFSEIMQPWA
QTVVVGRARLGGIPVGVVAVETRTVELSIPADPANLDSEAKIIQQAGQVWFPDSAFKTYQ
AIKDFNREGLPLMVFANWRGFSGGMKDMYDQVLKFGAYIVDGLRECSQPVMVYIPPQAEL
RGGSWVVIDPTINPRHMEMYADRESRGSVLEPEGTVEIKFRKKDLVKTMRRVDPVYIRLA
ERLGTPELSPTERKELESKLKEREEFLIPIYHQVAVQFADLHDTPGRMQEKGVINDILDW
KTSRTFFYWRLRRLL

Carboxyl_trans

Carboxyl_trans
PFAM accession number:PF01039
Interpro abstract (IPR034733):

All of the members in this family are biotin dependent carboxylases [ (PUBMED:8102604) (PUBMED:8366018) ]. The carboxyl transferase domain carries out the following reaction; transcarboxylation from biotin to an acceptor molecule. There are two recognised types of carboxyl transferase. One of them uses acyl-CoA and the other uses 2-oxoacid as the acceptor molecule of carbon dioxide. All of the members in this family utilise acyl-CoA as the acceptor molecule.

In bacteria, the acetyl coenzyme A carboxylase (ACC) is a complex consisting of two subunits: alpha and beta. This domain also recognizes the bacterial ACC beta-subunit.

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