ID SODC_CRYBA STANDARD; PRT; 153 AA. AC Q9C0N4; DT 25-OCT-2004 (Rel. 45, Created) DT 25-OCT-2004 (Rel. 45, Last sequence update) DT 10-MAY-2005 (Rel. 47, Last annotation update) DE Superoxide dismutase [Cu-Zn] (EC 1.15.1.1). GN Name=SOD1; OS Cryptococcus bacillisporus (Filobasidiella neoformans var. OS bacillispora). OC Eukaryota; Fungi; Basidiomycota; Hymenomycetes; Heterobasidiomycetes; OC Tremellomycetidae; Tremellales; Tremellaceae; Filobasidiella. OX NCBI_TaxID=37769; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NYS 155B, and wm 780-C; RX MEDLINE=21261961; PubMed=11368899; DOI=10.1016/S0378-1119(01)00408-5; RA Chaturvedi S., Hamilton A.J., Hobby P., Zhu G., Lowry C.V., RA Chaturvedi V.; RT "Molecular cloning, phylogenetic analysis and three-dimensional RT modeling of Cu,Zn superoxide dismutase (CnSOD1) from three varieties RT of Cryptococcus neoformans."; RL Gene 268:41-51(2001). CC -!- FUNCTION: Destroys radicals which are normally produced within the CC cells and which are toxic to biological systems (By similarity). CC -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2). CC -!- COFACTOR: Binds 1 copper ion and 1 zinc ion per subunit (By CC similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasmic (By similarity). CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF248049; AAK31918.1; -; mRNA. DR EMBL; AF248050; AAK31919.1; -; Genomic_DNA. DR EMBL; AF248051; AAK31920.1; -; Genomic_DNA. DR HSSP; P00441; 1OZU. DR InterPro; IPR001424; SOD_CU_ZN. DR Pfam; PF00080; Sod_Cu; 1. DR PRINTS; PR00068; CUZNDISMTASE. DR ProDom; PD000469; SOD_CU_ZN; 1. DR PROSITE; PS00087; SOD_CU_ZN_1; 1. DR PROSITE; PS00332; SOD_CU_ZN_2; 1. KW Antioxidant; Copper; Metal-binding; Oxidoreductase; Zinc. FT INIT_MET 0 0 By similarity. FT METAL 46 46 Copper (By similarity). FT METAL 48 48 Copper (By similarity). FT METAL 63 63 Copper and zinc (By similarity). FT METAL 71 71 Zinc (By similarity). FT METAL 80 80 Zinc (By similarity). FT METAL 83 83 Zinc (By similarity). FT METAL 120 120 Copper (By similarity). FT DISULFID 57 146 By similarity. SQ SEQUENCE 153 AA; 15506 MW; 636C96968C693FAD CRC64; VKAVAVLKGD SPVTGVITFT QEKEGAPVTV SGDIKNLDAN AERGFHVHEF GDNTNGCTSA GPHFNPHGKN HGAPSDSERH VGDLGNVKTD GNGVASVNIS DKSLSLFGPY SIIGRTIVVH AGTDDFGKGG NAESLKTGNA GARAACGVIG ISN //