And conserved cysteine residues found within the Crustins. (B) Amino acid sequence alignments. Besides Al-crus three and Al-crus 7, Al-crus 7, the sequences utilized in this alignment had been from Penaeus vannamei (QOL09958, QOL09962), Panulirus japonicas the sequences utilised within this alignment were fromAGU01545), Macrobrachium rosenbergii (ACU25385, AFO68120, AGF92153, (ACU25382, Nimbolide In Vitro ACU25383, BBC42585, BBD52151, Penaeus vannamei (QOL09958, QOL09962), Panulirus japonicas (ACU25382, ACU25383, BBC42585, BBD52151, AGU01545), Macrobrachium rosenbergii (ACU25385, AFO68120, AGF92153, ANH22232), ANH22232), Penaeus paulensis (ADF80918), Macrobrachium nipponense (QIV66989), and Neocaridina heteropoda (AYP74901). Penaeus paulensis (ADF80918), Macrobrachium nipponense (QIV66989), and Neocaridina heteropoda (AYP74901). TheTriangles The Gly-rich domain is underlined by a solid black line, as well as the WAP domain is underlined by a strong red line. Gly-rich domain is underlined by a strong black line, and the WAP domain is underlined by a solid reddomain. indicate the 12 conserved cysteine residues identified within the Crustins, such as the WAP line. Triangles indicate the 12 conserved cysteine residues discovered inside the Crustins, like the WAP domain.The deduced amino acid sequences of Al-crus three and Al-crus 7 had been compared using the deduced amino acid sequences of Al-crus and Al-crus sequence was Crustin those of other close Crustins (Figure 1). ForAl-crus 3 3, the closest7 were compared with those Macrobrachium Crustins (Figure 1). For Al-crus 3, the no. QIV66989), having a Crustin from of other close nipponense (NCBI GenBank Charybdotoxin web accession closest sequence was similarfrom 63 at the amino acid level. By contrast, for Al-crus 7, the closest sequence was a ity ofMacrobrachium nipponense (NCBI GenBank accession no. QIV66989), with a similarity of 63 at the amino acid level. By contrast, for Al-crus 7, the closest sequence was a Crustin-like peptide from Homarus americanus (NCBI GenBank accession no. KAG7170693) with a similarity of 82 (Table S2). According to the characteristics on the various Crustin sorts, Al-crus three and Al-crus 7 belonged to kind IIa (Figure 1). There were eight conservedMar. Drugs 2021, 19,four ofcysteine residues within the WAP domain and 12 cysteine residues in the C-terminal region. Amongst the 12 conserved cysteine residues, there were three amino acids between the first two cysteine residues (Cys1 ys2 ), a sequence of 16 or 17 amino acids among Cys4 ys5 , and also a sequence of 82 residues between Cys6 ys7 (Figure 1). Hence, Al-crus three and Al-crus 7 shared about 51 amino acid sequences. Compared together with the other two Crustins of Re-Crustin and Crus1 from other hydrothermal vent shrimps, the identities were 53 and 41 in the amino acid level for Al-crus 3, respectively. For Al-crus 7, the identities were 58 and 47 , respectively. 2.two. Phylogenetic Analysis of Al-crus three and Al-crus 7 WAP domain-containing proteins from diverse species had been chosen from NCBI for phylogenetic tree building with Al-crus three and Al-crus 7. The results showed that these Crustins had been primarily divided into two distinct groups: Group I and Group II. Additionally, there have been four clusters for every group (Figure 2); for Group I, the initial cluster was shrimp Crustins. The Al-crus three and Al-crus 7 examined within this study have been also classified into this cluster. Based on the Crustins present here, all the Crustins within this cluster had been from shrimp. Some Crustins from shrimp had been also classified into other clu.
