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Database: UniProt
Entry: G3B8N5_CANTC
LinkDB: G3B8N5_CANTC
Original site: G3B8N5_CANTC 
ID   G3B8N5_CANTC            Unreviewed;       299 AA.
AC   G3B8N5;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=Superoxide dismutase copper/zinc binding domain-containing protein {ECO:0000259|Pfam:PF00080};
GN   ORFNames=CANTEDRAFT_108128 {ECO:0000313|EMBL:EGV61775.1};
OS   Candida tenuis (strain ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC
OS   10315 / NRRL Y-1498 / VKM Y-70) (Yeast) (Yamadazyma tenuis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Yamadazyma.
OX   NCBI_TaxID=590646 {ECO:0000313|Proteomes:UP000000707};
RN   [1] {ECO:0000313|EMBL:EGV61775.1, ECO:0000313|Proteomes:UP000000707}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC 10315 /
RC   NRRL Y-1498 / VKM Y-70 {ECO:0000313|Proteomes:UP000000707};
RX   PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA   Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA   Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA   Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA   Barry K.W., Grigoriev I.V., Gasch A.P.;
RT   "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT   production.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
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DR   EMBL; GL996527; EGV61775.1; -; Genomic_DNA.
DR   RefSeq; XP_006687945.1; XM_006687882.1.
DR   AlphaFoldDB; G3B8N5; -.
DR   STRING; 590646.G3B8N5; -.
DR   GeneID; 18246005; -.
DR   KEGG; cten:CANTEDRAFT_108128; -.
DR   eggNOG; ENOG502S5NX; Eukaryota.
DR   HOGENOM; CLU_063073_2_0_1; -.
DR   OrthoDB; 3040041at2759; -.
DR   Proteomes; UP000000707; Unassembled WGS sequence.
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   Reference proteome {ECO:0000313|Proteomes:UP000000707};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..299
FT                   /note="Superoxide dismutase copper/zinc binding domain-
FT                   containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003442804"
FT   DOMAIN          47..159
FT                   /note="Superoxide dismutase copper/zinc binding"
FT                   /evidence="ECO:0000259|Pfam:PF00080"
FT   REGION          230..259
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        231..246
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   299 AA;  32335 MW;  684AC38D5560C11A CRC64;
     MRFQKPILLA LAAALVTAGE APKIKKNPAD VVAVADFPSG GPQKILGNVV FTAKKGKAVN
     VYIDVTKLPK EGGPFQYHIH QQPIGANGDC EASGTHLNPY KASPDCDSQK TDAFCQVGDL
     SGKHGWIDTT CFETKYDDPY LSLNTKSKSN IIGKAIVFHF ANLTKFACAN IEVAGDVRLK
     SLEEEYSRNG NDDLNELKSF VANDYQFVPG QEVFEVAEAH SKRDLGVSQY AEIDEDDNDD
     DTEQTGDVPD CTNSTHHHSG SNYSNFTNLS TIDCENNADS LGWAAIPAIL SGVAAVFLL
//
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