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Database: UniProt
Entry: A0A2H3IEY5_9EURO
LinkDB: A0A2H3IEY5_9EURO
Original site: A0A2H3IEY5_9EURO 
ID   A0A2H3IEY5_9EURO        Unreviewed;       168 AA.
AC   A0A2H3IEY5;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PCG91883.1};
GN   ORFNames=PENO1_091470 {ECO:0000313|EMBL:PCG91883.1};
OS   Penicillium occitanis (nom. inval.).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=290292 {ECO:0000313|EMBL:PCG91883.1, ECO:0000313|Proteomes:UP000218381};
RN   [1] {ECO:0000313|EMBL:PCG91883.1, ECO:0000313|Proteomes:UP000218381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CL100 {ECO:0000313|EMBL:PCG91883.1,
RC   ECO:0000313|Proteomes:UP000218381};
RX   PubMed=28951729; DOI=10.3389/fmicb.2017.01627;
RA   Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A., Gargouri A.,
RA   Gabaldon T., Roncero M.I.G.;
RT   "Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium
RT   occitanis and Functional Analysis of a Candidate Gene in the Plant Pathogen
RT   Fusarium oxysporum.";
RL   Front. Microbiol. 8:1627-1627(2017).
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:PCG91883.1}.
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DR   EMBL; NPFK01000391; PCG91883.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H3IEY5; -.
DR   STRING; 290292.A0A2H3IEY5; -.
DR   OrthoDB; 3040041at2759; -.
DR   Proteomes; UP000218381; 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   PANTHER; PTHR10003:SF37; CELL SURFACE SUPEROXIDE DISMUTASE [CU-ZN] 4; 1.
DR   PANTHER; PTHR10003; SUPEROXIDE DISMUTASE CU-ZN -RELATED; 1.
DR   SUPFAM; SSF49329; Cu,Zn superoxide dismutase-like; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000218381};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..168
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013823559"
SQ   SEQUENCE   168 AA;  17682 MW;  28EDA1D256B62DD9 CRC64;
     MILSLLLLPS LALSALGQGF TSAPVITNNP PTTYTAIFFD KPSTSVRGDI TASGAPDGVG
     LIFRVNFTGL PANIGSFPYH VHVSPVPTNG DCIAAREHLD PYNRGEQPPC DPSDPATCQV
     GDLSGKHGTA SGTSFFTEYT DFYLSTDPSS NAFVGDKSVV IMMLLVRA
//
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