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Database: UniProt
Entry: A0A0B4I531_METMF
LinkDB: A0A0B4I531_METMF
Original site: A0A0B4I531_METMF 
ID   A0A0B4I531_METMF        Unreviewed;       295 AA.
AC   A0A0B4I531;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Superoxide dismutase, copper/zinc binding domain protein {ECO:0000313|EMBL:KIE03189.1};
DE   Flags: Fragment;
GN   ORFNames=MAJ_00703 {ECO:0000313|EMBL:KIE03189.1};
OS   Metarhizium majus (strain ARSEF 297).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium;
OC   Metarhizium majus.
OX   NCBI_TaxID=1276143 {ECO:0000313|EMBL:KIE03189.1, ECO:0000313|Proteomes:UP000031176};
RN   [1] {ECO:0000313|EMBL:KIE03189.1, ECO:0000313|Proteomes:UP000031176}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 297 {ECO:0000313|EMBL:KIE03189.1,
RC   ECO:0000313|Proteomes:UP000031176};
RX   PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA   Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA   St Leger R.J., Wang C.;
RT   "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT   adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KIE03189.1}.
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DR   EMBL; AZNE01000002; KIE03189.1; -; Genomic_DNA.
DR   RefSeq; XP_014582182.1; XM_014726696.1.
DR   AlphaFoldDB; A0A0B4I531; -.
DR   HOGENOM; CLU_063073_0_0_1; -.
DR   OrthoDB; 3040041at2759; -.
DR   Proteomes; UP000031176; 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:UP000031176};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..295
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002093378"
FT   DOMAIN          56..170
FT                   /note="Superoxide dismutase copper/zinc binding"
FT                   /evidence="ECO:0000259|Pfam:PF00080"
FT   REGION          227..259
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KIE03189.1"
SQ   SEQUENCE   295 AA;  30763 MW;  A124C3BF36927943 CRC64;
     MRVAVAVAAL GAAVNVVRAA DLLPEITDNP LDVIYTATLP QDPFFHAPEL DGNVRGFISA
     AAPPDGVGVR FTVRFENLPK TGGPFAYHLH VNKASNGNCT ATGAHLDPTN RGEKPPCDAG
     SLPSCQAGDL AGKYGKITSD PFIVEYVDKF VSLKEGDATF FGNRSFVIHL ANSTRITCAD
     FVKNDPNIPS APLPGSTSRN NQTYTKTETT TYTQPCACSD QQTSCTTTTA TTSTSTTSTT
     STTSTRSTPA GTGVSSSGVV GPTPSVVIAA AGRSVPGPLL WWVGSVALVI FSHYM
//
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