[Objectives] This paper aims to study the function of the ARF7 gene family of Huperzia serrata. [Methods] Based on the full-length transcriptome sequencing results of H serrata, the unigenes of 17 H serrata ARF candidate genes were analyzed using biogenetics technology. [Results] The molecular weight of the ARF7 proteins ranges from 11.28 to 608.54 kDa. HsARF7-4, HsARF7-5, HsARF7-8, HsARF7-9, HsARF7-10, HsARF7-13, HsARF7-16 and HsARF7-17 are basic proteins; all the proteins are unstable; except that HsARF7-6 and HsARF7-15 are hydrophilic, the rest are lipophilic proteins; there are 197 types of cis-acting elements, and 17 of the proteins contain as more as 20 acting elements such as GTGANTG10, CBFHV, GT1CONSENSUS, NODCON2GM, CAATBOX1, MYBCORE, GATABOX, WRKY710S and RAV1AAT; HsARF7-1, HsARF7-2, HsARF7-4, HsARF7-6, HsARF7-8, HsARF7-10, HsARF7-12, HsARF7-14 and HsARF7-16 all have the 6 types of motif predicted; the proteins have domains such as PABP-1234 super family, RRM_SF super family, PRK10263 super family, AUX_IAA super family and MFS super family; the proteins all can cross cell membrane and have no signal peptide, and they are all located in the nucleus. On the level of secondary structure, the proportion of β-sheet is the smallest. In HsARF7-7 and HsARF7-9, α-helix has the largest proportion, and in the remaining proteins, random coil has the largest proportion; and tertiary structure prediction found that HsARF7-1, HsARF7-2, HsARF7-4, HsARF7-14 and HsARF7-17 have a tertiary structure of polyadenylate-binding protein, and HsARF7-7 has a tertiary structure of auxin-induced protein iaa4. [Conclusions] The above analysis results can provide a certain theoretical basis for further research on the biological function and regulatory mechanism of the ARF gene of H serrata in the future, and provide a reference for the study of the growth and development of H serrata. [ABSTRACT FROM AUTHOR]