## 4 Discussion
### Phylogenetic Evolutionary Analysis Based on the Interactive Transcriptome
cerevisiae_ vacuole fusion has been reported by [PERSON] et al. (2014) [76]. In _S. mycoparsitica_, eleven PDR subfamily members (TC 3.A.1.205) of ABC transporters were identified. In _Aspergillus fumigatus_, it was demonstrated that two ABC transporters (ABC-A and ABC-B) shared the highest sequence similarity with Pdr5 in _S. cerevisiae_ yeast [77]. The Pdr5 protein is a plasma membrane-localized pleiotropic ABC efflux transporter of multiple drugs. In addition, the ABC-B role was linked to azole resistance and ABC-B was required for normal pathogenesis of _A. fumigatus_ tested in a _Galeria mellonella_ (greater wax moth) infection model system [77]. The transcript, Sm80002_c1_g4_i2, was annotated to ABC transporter ATP-binding protein ARB1 of _S. cerevisiae_. The ARB1 protein in _S. cerevisiae_ is essential for interacting with ribosomes and functioning in protein synthesis or ribosome biogenesis (stimulation of 40S and 60S ribosome biogenesis) [78]. In _S. mycoparsitica_, the two ABC-F/EF3 subfamily transcripts have close phylogenetic relatedness to mycoparsitic _Trichoderma_ and _Sporothrix_ generalists. It coincides with the ubiquitous nature of ABC-F proteins known as widespread translation factors within prokaryotes and eukaryotes. Interestingly, it was suggested that bacterial ABC-F proteins could mediate increased antibiotic resistance. Moreover, the anti-apoptotic function of ABCF2 has also been proposed during the infection of enteropathogenic _E. coli_[79]. The multidrug transporters ABC-G are involved in multiple functions or mechanisms leading to mycoparasitism such as fungal cell resistance to xenobiotic compounds and steroid transports. This ABC family may provide pesticide resistance, since this transporter is known as conferring resistance to structurally and functionally unrelated compounds including azoles such as itraconazole [80, 81], posaconazole [82], and voriconazole [83]. This class of transporters is conferring resistance to cycloheximide, azoles, and a mycotoxin sporidesmin [84, 85, 86]. Among fungi, ABC-G1-5, ABC-G6, and ABC-G7 have been discovered as the major clusters within ascomycetes and basidiomycetes [87]. In this study, the ABC transporter-CDR4 found in biotrophic mycoparasite _S. mycoparasitica_ belongs to the ABC-G/PDR cluster (TC 3.A.1.205) and might be involved in xenobiotic detoxification by transmembrane export across plasma membrane. [PERSON] et al. (2014) reported that deletion of _abcG5_ in heterotrophic mycoparasite _C. rosea_ resulted in reduced ZEN mycotoxin tolerance and kept its partial ability to protect the barley plant against _F. graminearum_[27]. The _ABCG5_ gene provides instructions for making sterolin-1, which makes up half of a protein called sterolin. Sterolin is a transporter protein, which is a type of protein that moves substances across cell membranes. Although we were unable to perform a comparison of genome assembly size in our study due to the absence of the genome assembly of _S. mycoparasitica_, genome size, gene number and gene turnover were discussed. [PERSON] and [PERSON] (2021) reported significant changes in gene number within the order Hypocreales including mycoparasitic and root symbiotic _Trichoderma_ and plant pathogenic _Fusarium_ species, as well as two other genera having endophytic and entomopathogenic lifestyles [21]. The mycoparasitic _Trichoderma_ tended to have a lower gene number than the plant pathogenic _Fusarium_ (genome size had the same decreasing pattern). In the same manner, the proportion of genus-specific orthogroups was reduced in the _Trichoderma_ as compared with the _Fusarium_ genus. With that, _S. mycoparasitica_ might have the same pattern of reduction in genome size, gene number, and genus-specific orthogroups as inferred from the mycoparasitic lifestyle requiring a fewer number of core genes consisting of smaller genome size, lower gene number, and genus-specific orthogroups due to complementary means (gene turnover and positive selection).