Abstract: In order to study the bioinformatics characteristics of cellodextrinase-1（CDT-1） protein excavated from Rumen Microbial Metagenomic Library of Yunnan Gayal（Bos frontalis）, ProtParam, TMHMM Server 2.0, ProtScale, NCBI Conserved Domains, SignalP 5.0, TargetP 2.0, PSORT Ⅱ server, SOPMA, SWISS-MODEL, NetN Glyc 1.0 Server, NetP hos 3.1 Server, NCBI protein BLASTp and MEGA 7.0 and other online analysis tools and software were used to analyze the basic physical and chemical properties, transmembrane region, hydrophilicity/hydrophobicity, protein domain, signal peptide, subcellular localization, secondary structure, tertiary structure, N-terminal glycosylation site, protein serine, threonine and tyrosine phosphorylation sites and system evolution of CDT-1 protein. The results showed that the relative molecular mass of CDT-1 protein was 38 082.24; the theoretical isoelectric point was 4.80; the total number of negatively charged residues was 45; the total number of positively charged residues was 29; and the estimated half-life was 30 h; and the water-type stable lipoprotein was located in extracellular with cell wall and contained a conserved domain composed of α-helix, random coils, extended strands, and β-turns. The tertiary structure homology modeling had a high degree of credibility. It had two N-terminal glycosylation sites and 26 phosphorylation sites, which might have high enzyme activity. CDT-1 protein was highly homologous to the cellulase protein of endoglucanase in the phylogenetic tree. It indicated that the CDT-1 protein was a hydrophilic stable lipoprotein derived from cellulase protein in endoglucanase.