The domain within your query sequence starts at position 126 and ends at position 218; the E-value for the FDX-ACB domain shown below is 1.5e-32.

SKYPAVFNDISFWLPSENYTENDFYDIVRTVGGDLVEKVDLIDKFEHPKTHRTSHCYRIT
YRHMERTLSQREVGNVHQAVQEAAVQLLGVEGR

FDX-ACB

Ferredoxin-fold anticodon binding domain
FDX-ACB
SMART accession number:SM00896
Description: This is the anticodon binding domain found in some phenylalanyl tRNA synthetases. The domain has a ferredoxin fold, consisting of an alpha+beta sandwich with anti-parallel beta-sheets (beta-alpha-beta x2).
Interpro abstract (IPR005121):

Aminoacyl-tRNA synthetases (aaRSs) play a crucial role in the translation of the genetic code by means of covalent attachment of amino acids to their cognate tRNAs. Phenylalanine-tRNA synthetase (PheRS, also known as Phenylalanine-tRNA ligase) is known to be among the most complex enzymes of the aaRS family. Bacterial and mitochondrial PheRSs share a ferredoxin-fold anticodon binding (FDX-ACB) domain, which represents a canonical double split alpha+beta motif having no insertions. The FDX-ACB domain displays a typical RNA recognition fold (RRM) formed by the four-stranded antiparallel beta sheet, with two helices packed against it [(PUBMED:7664121), (PUBMED:9016717), (PUBMED:10049785), (PUBMED:12962494), (PUBMED:18611382)].

Family alignment:
View or

There are 24139 FDX-ACB domains in 24139 proteins in SMART's nrdb database.

Click on the following links for more information.