Heat shock protein 90 genes (hsp90s) are multifunctional genes, which are related to biological development, biological defense reactions, environmental stress tolerance and so on. In this research,a heat shock protein 90 gene (Dd-hsp90-1; GenBank Accession: HQ901595) was cloned from Ditylenchus destructor by RT-PCR and RACE. The cDNA sequence consisted of a 2 160 bp open reading frame (ORF) encoding 719 amino acid residues that was franked by a 70 bp 5′ -untranslated region (UTR) and a 117 bp 3′-UTR. The result of intron-exon structure analysis showed that the genomic sequence of Dd-hsp90-1 also contained 9 introns. And all the introns obeyed the GT/AG rule in the splice-site junctions. The molecular weight of Dd-hsp90-1 deduced protein was about 82.79 ku. Dd-hsp90-1 was a single copy gene was highly homologous to other hsp90s. There were consensus amino acid sequences and motifs of HSP90s in the amino acid sequence of deduced protein Dd-HSP90-1. Furthermore,the deduced protein Dd-HSP90-1 also contained five signature sequences and MEEVD motif specific to cytoplasmic HSP90s. All of these demonstrated that Dd-hsp90-1 was an cytoplasmic hsp90. Phylogenetic dendrogram indicated that Dd-hsp90-1 was most closely related to Baursaphelenchus xylophilus hsp90 (ACY01918) with 86.65% sequence identity. It also revealed the differences in the feeding behaviors of plant parasitic nematodes.