1) a) BLASTn i) Identity of gene: CP020133.1 Organism: Saccharomyces cerevisiae ii) E value: 0.0 % identity: 100%b) BLASTx i) Identity of gene: NP_012980.1 Organism: Saccharomyces Cerevisiae S288C ii) E value: 0.0 % identity: 100% 2) a) 4092 a.a b) Features: ATP binding site (CDD:99707), DHC_N1 (CDD: 285571), MT (CDD: 289543) c) i) Functions:ATP binding site: this protein carries three phosphate groups and allows the ATP molecules to interact and break down into ADPDHC_N1: dimers are formed when they connect with other heavy chains and also a basal cargo binding component is formed when connected with intermediate chain-light chain complexesMT / Microtubule-binding stalk of dynein motor: formation of the stalk to assist the ATP-sensitive microtubule binding componentii) Reference for ATP binding site: AAA+ proteins: diversity in function, similarity in structure. Biochem. Soc. Trans. 2008 Feb; 36(Pt 1):72-77Reference for DHC_N1: Interaction mapping of a dynein heavy chain. Identification of dimerization and intermediate-chain binding domains. J. Biol. Chem. 1999 May 28; 274(22):15447-15453Reference for MT: Model for the motor component of dynein heavy chain based on homology to the AAA family of oligomeric ATPases.Structure 2001 Feb 7; 9(2):93-103iii) Cottingham, F. R., & Hoyt, M. A. (1997). Mitotic Spindle Positioning in Saccharomyces cerevisiae Is Accomplished by Antagonistically Acting Microtubule Motor Proteins . The Journal of Cell Biology, 138(5), 1041–1053.3) Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.4) Dynein acts as a motor protein for the intracellular motility down the microtubules in a retrograde motion. ATPase activity also occurs, where ATP is hydrolyzed into ADP. Furthermore, the heavy chains of this protein is significant in the function of the dynein complex. Two functional domains are associated with each heavy chain, and plays a role for its movement. The first functional domain consists of the motor domain that hydrolyzes ATP and joins microtubules by an ATP-sensitive method. The second functional domain consists of the tethering domain which attaches the dynein to its cargo.