taxonID	type	description	language	source
03CE87A24B73FB4B8C2F060B1B40ECAD.taxon	description	The ASN _ Glycosylation motive is a post-translational modification (glycosylation) area in the residual aspargin (ASN) area. The CAMP _ phospho _ site motif shows the area of phosphorylation using cAMP or cGMP, and the CK 2 _ phospho _ site motif shows the area where casein kinase II phosphorylation occurs (Deihimi et al. 2012) [28]. and is found in the amino acid sequences STKD, TTVD, and tyle (Figure 10 A). The myristyl motif shows the site where the myristylation process is the addition of a myristyl group to a protein at the end of the translation process (Maurer-Stroh et al. 2002) [29]. and is found in the amino acid sequences GTSDAS, GASKTG, GTKDST, GSMNSN and GASTGN (Figure 10 A). The PKC _ phospho _ site motif shows the area where the phosphorylation of protein kinase C occurs (Leonard et al. 2011) [30]. and is found in the amino acid sequences SDK, STK, TAR, TYK, TLK (Figure 10 A). Tracing the motives on the protein sequences of the endoglucanase gene coding for B. thuringiensis from the sample of Sargassum sp. shows the protein motif GH 8 (Figure 12 A; 12 B )). This motif has been identified as a characteristic feature of the glycohydrolase group of enzymes. Other short motifs were also found along the protein sequence, including the ASN _ glycosylation motif, the camp _ phospho _ site motif in the amino acid sequence KRES, the CK 2 _ phospho _ site motif in the amino acid sequence SYYD, SATD, SSLD and SGWD, the MYRISTYL motif in the amino acid sequence GTSEGQ, GMIITV, GSNGTV, GIKASN and GSNIGS and the PKC _ phospho _ site motif in the amino acid sequence SVR, TAR, TFK, SKK, SNK, and SDK (Figure 12 A; 14). Based on In silico analysis of the endoglucanase gene protein sequences in B. subtilis and B. thuringiensis from samples of Eucheuma sp. and Sargassum sp. It can be seen that the two protein sequences have endoglucanase enzyme functional activity of the two bacterial isolates. The protein motives of the two endoglucanase gene sequences are similar, which indicates a close gene relationship between the two Bacillus strains. The catalytic and cellulose binding domains of B. subtilis were GH 5 and CBM 3, whereas those of B. thuriengiensis were GH 8, and no substrate binding domains were found (Table 8).	en	Buwono, Ibnu Dwi, Grandiosa, Roffi (2021): Molecular analysis of functional domain and protein motif of endoglucanase gene in marine bacteria isolated from Eucheuma sp. and Sargassum sp. International Journal of Fisheries and Aquatic Studies 9 (1): 204-213, DOI: 10.22271/fish.2021.v9.i1c.2403, URL: https://doi.org/10.22271/fish.2021.v9.i1c.2403
