ID A0A5P2UFG4_KLULC Unreviewed; 337 AA. AC A0A5P2UFG4; DT 22-APR-2020, integrated into UniProtKB/TrEMBL. DT 22-APR-2020, sequence version 1. DT 24-JAN-2024, entry version 10. DE RecName: Full=Superoxide dismutase copper/zinc binding domain-containing protein {ECO:0000259|Pfam:PF00080}; GN ORFNames=KDRO_F02880 {ECO:0000313|EMBL:QEU62360.1}; OS Kluyveromyces lactis (Yeast) (Candida sphaerica). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces. OX NCBI_TaxID=28985 {ECO:0000313|EMBL:QEU62360.1, ECO:0000313|Proteomes:UP000323107}; RN [1] {ECO:0000313|Proteomes:UP000323107} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CBS 2105 {ECO:0000313|Proteomes:UP000323107}; RA Ortiz-Merino R.A., Braun-Galleani S., Wolfe K.H., Morrissey J.P.; RT "Kluyveromyces lactis var. drosophilarum CBS 2105 Genome assembly."; RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases. 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; CP042460; QEU62360.1; -; Genomic_DNA. DR AlphaFoldDB; A0A5P2UFG4; -. DR Proteomes; UP000323107; Chromosome 6. DR GO; GO:0005507; F:copper ion binding; IEA:InterPro. DR GO; GO:0006801; P:superoxide metabolic process; IEA:InterPro. DR Gene3D; 2.60.40.200; Superoxide dismutase, copper/zinc binding domain; 1. DR InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf. DR InterPro; IPR024134; SOD_Cu/Zn_/chaperone. DR InterPro; IPR001424; SOD_Cu_Zn_dom. DR PANTHER; PTHR10003:SF37; CELL SURFACE SUPEROXIDE DISMUTASE [CU-ZN] 4; 1. DR PANTHER; PTHR10003; SUPEROXIDE DISMUTASE CU-ZN -RELATED; 1. DR Pfam; PF00080; Sod_Cu; 1. DR SUPFAM; SSF49329; Cu,Zn superoxide dismutase-like; 1. PE 4: Predicted; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..18 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 19..337 FT /note="Superoxide dismutase copper/zinc binding domain- FT containing protein" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5024912465" FT DOMAIN 50..159 FT /note="Superoxide dismutase copper/zinc binding" FT /evidence="ECO:0000259|Pfam:PF00080" FT REGION 174..286 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 178..233 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 242..286 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 337 AA; 38095 MW; 5C7AA932601A2C77 CRC64; MQQKKLIPIL VTLPMALAGA DRESAPVIYE NPEKACYLAE FPQVGSDKVG GYITFTSLDG IAKVNVRIST LEPKLQYHIH EKPVDPSDPS CESTKEHLNP YNGEVPCGND ISKCEVGDLS GKYGNIDNSY YETEYLDPYL SLIEGDPAFV GGRSITLHYS NGTRYACADI VPCEKLKPSP KPPKEDDPKE KEPKEKEPKD DKSEEEKPKE DKKTKKERKK AKKEEEKKQK EDKKNKKHSD KKNKKHEDDE YSEAEPSVTE EKRVETSFTK KPHHTTSAAL KEGYKEVKNE TDTEWKTDDG HYNGTETDHS TALNDAHNWK RTSSIGSIIA FMMSLLI //