The domain within your query sequence starts at position 39 and ends at position 120; the E-value for the tRNA_anti-codon domain shown below is 4.2e-9.

VLETGRVTKTKDGHEVRTCKVADKTGSINISVWDDVGNLIQPGDIIRLTKGYASVFKGCL
TLYTGRGGDLQKIGEFCMVYSE

tRNA_anti-codon

• PFAM accession number: PF01336
• Interpro abstract (IPR004365):

  The OB-fold (oligonucleotide/oligosaccharide-binding fold) is found in all three kingdoms and its common architecture presents a binding face that has adapted to bind different ligands. The OB-fold is a five/six-stranded closed beta-barrel formed by 70-80 amino acid residues. The strands are connected by loops of varying length which form the functional appendages of the protein. The majority of OB-fold proteins use the same face for ligand binding or as an active site. Different OB-fold proteins use this 'fold-related binding face' to, variously, bind oligosaccharides, oligonucleotides, proteins, metal ions and catalytic substrates.

  This entry contains OB-fold domains that bind to nucleic acids [ (PUBMED:10829230) ]. It includes the anti-codon binding domain of lysyl, aspartyl, and asparaginyl-tRNA synthetases (See IPR004364 ). Aminoacyl-tRNA synthetases catalyse the addition of an amino acid to the appropriate tRNA molecule EC 6.1.1 . This domain is found in RecG helicase involved in DNA repair. Replication factor A is a heterotrimeric complex, that contains a subunit in this family [ (PUBMED:7760808) (PUBMED:8990123) ]. This domain is also found at the C terminus of bacterial DNA polymerase III alpha chain.

• GO function: nucleic acid binding (GO:0003676)

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