The domain within your query sequence starts at position 110 and ends at position 449; the E-value for the tRNA-synt_1d domain shown below is 1e-97.

CKYGLKSELFSDLPKKRIVVEFSSPNIAKKFHVGHLRSTIIGNFIANLKEALGHQVTRIN
YIGDWGMQFGLLGTGFQLFGYEEKLQTNPLQHLFDVYVQVNKEATDDKNVTKLAHEFFHR
LEMGDTQALSLWQRFRDLSIEEYTQIYKRLGIYFDEYSGESFYREKSQDVLKLLDSKGLL
QKTAEGNVVVDLSGTGDLSSVCTVMRSDGTSLYATRDLAAAIHRMDKYNFDTMIYVADKG
QRRHFQQVFQMLKIMGYDWAERCQHVPFGIVKGMKTRRGGVTFLEDVLNEVQSRMLQNMA
SIKTTKQLENPQETAERVGLAAVIIQDFRGTLLSDYQFSW

tRNA-synt_1d

tRNA-synt_1d
PFAM accession number:PF00750
Interpro abstract (IPR035684):

Arginyl tRNA synthetase (ArgRS), a class I aminoacyl tRNA synthetase, is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. There are at least three subgroups of ArgRS. One type contains both characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. The second subtype lacks the KMSKS motif; however, it has a lysine N-terminal to the HIGH motif, which serves as the functional counterpart to the second lysine of the KMSKS motif. A third group, which is found primarily in archaea and a few bacteria, lacks both the KMSKS motif and the HIGH loop lysine [(PUBMED:11106639)].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry tRNA-synt_1d