And conserved cysteine residues located inside the Crustins. (B) Amino acid sequence alignments. Apart from

And conserved cysteine residues located inside the Crustins. (B) Amino acid sequence alignments. Apart from Al-crus three and Al-crus 7, Al-crus 7, the GS-626510 Epigenetic Reader Domain sequences employed within this alignment were from Penaeus vannamei (ML-SA1 Agonist QOL09958, QOL09962), Panulirus japonicas the sequences utilised in this alignment have been fromAGU01545), Macrobrachium rosenbergii (ACU25385, AFO68120, AGF92153, (ACU25382, 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 strong black line, along with the WAP domain is underlined by a strong red line. Gly-rich domain is underlined by a solid black line, along with the WAP domain is underlined by a solid reddomain. indicate the 12 conserved cysteine residues located inside the Crustins, which includes the WAP line. Triangles indicate the 12 conserved cysteine residues found inside the Crustins, which includes the WAP domain.The deduced amino acid sequences of Al-crus three and Al-crus 7 were compared together with the deduced amino acid sequences of Al-crus and Al-crus sequence was Crustin these of other close Crustins (Figure 1). ForAl-crus three 3, the closest7 have been compared with those Macrobrachium Crustins (Figure 1). For Al-crus three, the no. QIV66989), using a Crustin from of other close nipponense (NCBI GenBank 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), using 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) having a similarity of 82 (Table S2). Based on the qualities with the diverse Crustin types, Al-crus three and Al-crus 7 belonged to kind IIa (Figure 1). There have been eight conservedMar. Drugs 2021, 19,4 ofcysteine residues within the WAP domain and 12 cysteine residues in the C-terminal area. Amongst the 12 conserved cysteine residues, there have been three amino acids in between the very first two cysteine residues (Cys1 ys2 ), a sequence of 16 or 17 amino acids amongst Cys4 ys5 , plus a sequence of 82 residues between Cys6 ys7 (Figure 1). Therefore, Al-crus three and Al-crus 7 shared around 51 amino acid sequences. Compared with all the other two Crustins of Re-Crustin and Crus1 from other hydrothermal vent shrimps, the identities had been 53 and 41 at the amino acid level for Al-crus three, respectively. For Al-crus 7, the identities were 58 and 47 , respectively. 2.2. Phylogenetic Analysis of Al-crus three and Al-crus 7 WAP domain-containing proteins from diverse species have been chosen from NCBI for phylogenetic tree construction with Al-crus three and Al-crus 7. The outcomes showed that these Crustins have been mainly divided into two distinct groups: Group I and Group II. Furthermore, there have been four clusters for each and every group (Figure two); for Group I, the first cluster was shrimp Crustins. The Al-crus three and Al-crus 7 examined within this study had been also classified into this cluster. Determined by the Crustins present here, all the Crustins in this cluster have been from shrimp. Some Crustins from shrimp were also classified into other clu.