How does aminoacyl-tRNA synthetase recognize different tRNAs?
You give the answer in your question:


  binding areas that recognize a particular tRNA through unique identity sites at the acceptor stem and/or anticodon loop of the tRNA.


The point is that aminoacyl-tRNA synthetases that recognize tRNAs with different anticodons have to supplement any partial codon recognition with recognition of common features elsewhere, in particular the anticodon loop. Unfortunately this has evolved on a case-by-case basis and there is no simple ‘code’ one can refer to.

Thus, Berg et al. (Chapter 29), in discussing  threonyl-tRNA synthetase, write (my emphasis):


  As expected, the CCA arm extends into the zinc-containing activation
  site, where it is well positioned to accept threonine from threonyl
  adenylate. The enzyme interacts extensively not only with the acceptor
  stem of the tRNA, but also with the anticodon loop. The interactions
  with the anticodon loop are particularly revealing. The bases within
  the sequence CGU of the anticodon each participate in hydrogen bonds
  with the enzyme; those in which G and U take part appear to be more
  important because the C can be replaced by G or U with no loss of
  acylation efficiency.


The four codons for Thr are ACN, so in this case recognition of two bases of the anticodon will identify all tRNAs.

A diagram from Berg et al. showing the multiple interactions in threonine tRNA-synthatase is shown below.