The domain within your query sequence starts at position 124 and ends at position 537; the E-value for the tRNA-synt_1e domain shown below is 2.7e-128.

VFIPQDGKKVTWYCCGPTVYDASHMGHARSYISFDILRRVLRDYFQYDVFYCMNITDIDD
KIIRRARQNYLFEQYREQKPPATQLLKDVRDAMKPFSVKLSETTDPDKRQMLERIQNSVK
LATEPLEQAVRSSLSGEEVDSKVQVLLEEAKDLLSDWLDSTGGSEVTDNSIFSKLPKFWE
EEFHKDMEALNVLPPDVLTRVSEYVPEIVNFVQKIVDNGYGYASNGSVYFDTAKFAASEK
HSYGKLVPEAVGDQKALQEGEGDLSISADRLSEKRSPNDFALWKASKPGEPSWPCPWGKG
RPGWHIECSAMAGTLLGASMDIHGGGFDLRFPHHDNELAQSEAYFENDCWVRYFLHTGHL
TIAGCKMSKSLKNFITIKDALKKHSARQLRLAFLMHSWKDTLDYSSNTMESALQ

tRNA-synt_1e

tRNA-synt_1e
PFAM accession number:PF01406
Interpro abstract (IPR032678):

This entry represents the catalytic (Rossmann-fold) domain found in cysteinyl tRNA synthetases [(PUBMED:22184460)] which is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.

Cysteine-tRNA ligase (also known as cysteinyl-tRNA synthetase) (EC 6.1.1.16) is an alpha monomer and belongs to class Ia [(PUBMED:1992490)]. It aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. It is highly specific despite not possessing the amino acid editing activity characteristic of many other tRNA ligases [(PUBMED:12032090), (PUBMED:10704480), (PUBMED:12458790), (PUBMED:10447505), (PUBMED:7647112), (PUBMED:14665676), (PUBMED:7783224), (PUBMED:11550797), (PUBMED:11310981), (PUBMED:8274143), (PUBMED:2203971), (PUBMED:7479698)].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry tRNA-synt_1e