ID A5DV47_LODEL Unreviewed; 247 AA.
AC A5DV47;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 24-JAN-2024, entry version 82.
DE RecName: Full=Superoxide dismutase copper/zinc binding domain-containing protein {ECO:0000259|Pfam:PF00080};
GN ORFNames=LELG_01233 {ECO:0000313|EMBL:EDK43055.1};
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508 {ECO:0000313|EMBL:EDK43055.1, ECO:0000313|Proteomes:UP000001996};
RN [1] {ECO:0000313|EMBL:EDK43055.1, ECO:0000313|Proteomes:UP000001996}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 /
RC NRRL YB-4239 {ECO:0000313|Proteomes:UP000001996};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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DR EMBL; CH981524; EDK43055.1; -; Genomic_DNA.
DR RefSeq; XP_001528713.1; XM_001528663.1.
DR AlphaFoldDB; A5DV47; -.
DR STRING; 379508.A5DV47; -.
DR GeneID; 5235258; -.
DR KEGG; lel:LELG_01233; -.
DR VEuPathDB; FungiDB:LELG_01233; -.
DR eggNOG; ENOG502S5NX; Eukaryota.
DR HOGENOM; CLU_063073_0_0_1; -.
DR InParanoid; A5DV47; -.
DR OMA; IARASFT; -.
DR OrthoDB; 3040041at2759; -.
DR Proteomes; UP000001996; 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; IPR017868; Filamin/ABP280_repeat-like.
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.
DR PROSITE; PS50194; FILAMIN_REPEAT; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000001996};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..247
FT /note="Superoxide dismutase copper/zinc binding domain-
FT containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002681526"
FT REPEAT 1..78
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT DOMAIN 44..167
FT /note="Superoxide dismutase copper/zinc binding"
FT /evidence="ECO:0000259|Pfam:PF00080"
FT REGION 168..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 247 AA; 24115 MW; 86BCA1F3D7BA192E CRC64;
MISSVFKQIV FIALALAGDA PVQTDSSNQE SVVATFSPKG TSEISGTIKF SPASNGSVLV
SVDVSGLPSS GGPFPYHIHE ALVPENGNCT ATGGHFNPFN GSASATEPAA KEVGDLAGRH
GNITTTSDFK TEYVDNYLSL NPDSEAYFGN LSVVIHSSNN SRLTCANLES EESSGTNGGD
GGGASGSNST TGGGGASGSN STTGGGGASG SNSTTGSGGA SGSSTANSAS GLEYGGMVVA
AAVALLI
//
