The domain within your query sequence starts at position 504 and ends at position 681; the E-value for the tRNA-synt_1c_C domain shown below is 4.4e-42.

APRYVALLKKEVVPVNVLDAQEEMKEVARHPKNPDVGLKPVWYSPKVFIEGADAETFSEG
EMVTFINWGNINITKIHKNADGKITSLDAKLNLENKDYKKTTKITWLAESTHALSIPAVC
VTYEHLITKPVLGKDEDFKQYINKDSKHEELMLGDPCLKDLKKGDIIQLQRRGFFICD

tRNA-synt_1c_C

tRNA-synt_1c_C
PFAM accession number:PF03950
Interpro abstract (IPR020059):

The aminoacyl-tRNA synthetase (also known as aminoacyl-tRNA ligase) catalyse the attachment of an amino acid to its cognate transfer RNA molecule in a highly specific two-step reaction [(PUBMED:10704480),(PUBMED:12458790)]. These proteins differ widely in size and oligomeric state, and have limited sequence homology [(PUBMED:2203971)]. The 20 aminoacyl-tRNA synthetases are divided into two classes, I and II. Class I aminoacyl-tRNA synthetases contain a characteristic Rossman fold catalytic domain and are mostly monomeric [(PUBMED:10673435)]. Class II aminoacyl-tRNA synthetases share an anti-parallel beta-sheet fold flanked by alpha-helices [(PUBMED:8364025)], and are mostly dimeric or multimeric, containing at least three conserved regions [(PUBMED:8274143), (PUBMED:2053131), (PUBMED:1852601)]. However, tRNA binding involves an alpha-helical structure that is conserved between class I and class II synthetases. In reactions catalysed by the class I aminoacyl-tRNA synthetases, the aminoacyl group is coupled to the 2'-hydroxyl of the tRNA, while, in class II reactions, the 3'-hydroxyl site is preferred. The synthetases specific for arginine, cysteine, glutamic acid, glutamine, isoleucine, leucine, methionine, tyrosine, tryptophan, valine, and some lysine synthetases (non-eukaryotic group) belong to class I synthetases. The synthetases specific for alanine, asparagine, aspartic acid, glycine, histidine, phenylalanine, proline, serine, threonine,and some lysine synthetases (non-archaeal group), belong to class-II synthetases. Based on their mode of binding to the tRNA acceptor stem, both classes of tRNA synthetases have been subdivided into three subclasses, designated 1a, 1b, 1c and 2a, 2b, 2c [(PUBMED:10447505)].

Glutamate-tRNA ligase (also known as glutamyl-tRNA synthetase; EC 6.1.1.17) is a class Ic ligase and shows several similarities with glutamate-tRNA ligase concerning structure and catalytic properties. It is an alpha2 dimer. To date one crystal structure of a glutamate-tRNA ligase (Thermus thermophilus) has been solved. The molecule has the form of a bent cylinder and consists of four domains. The N-terminal half (domains 1 and 2) contains the 'Rossman fold' typical for class I ligases and resembles the corresponding part of Escherichia coli GlnRS, whereas the C-terminal half exhibits a GluRS-specific structure [(PUBMED:9426192)].

GO process:tRNA aminoacylation for protein translation (GO:0006418)
GO component:cytoplasm (GO:0005737)
GO function:ATP binding (GO:0005524), aminoacyl-tRNA ligase activity (GO:0004812), nucleotide binding (GO:0000166)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry tRNA-synt_1c_C