ID   A0A395HBA7_9EURO        Unreviewed;       591 AA.
AC   A0A395HBA7;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   RecName: Full=L-ascorbate oxidase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BO80DRAFT_397552 {ECO:0000313|EMBL:RAL05197.1};
OS   Aspergillus ibericus CBS 121593.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448316 {ECO:0000313|EMBL:RAL05197.1, ECO:0000313|Proteomes:UP000249402};
RN   [1] {ECO:0000313|EMBL:RAL05197.1, ECO:0000313|Proteomes:UP000249402}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 121593 {ECO:0000313|EMBL:RAL05197.1,
RC   ECO:0000313|Proteomes:UP000249402};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC       {ECO:0000256|ARBA:ARBA00010609}.
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DR   EMBL; KZ824421; RAL05197.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A395HBA7; -.
DR   STRING; 1448316.A0A395HBA7; -.
DR   VEuPathDB; FungiDB:BO80DRAFT_397552; -.
DR   OrthoDB; 449862at2759; -.
DR   Proteomes; UP000249402; Unassembled WGS sequence.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd13850; CuRO_1_Abr2_like; 1.
DR   CDD; cd13876; CuRO_2_Abr2_like; 1.
DR   CDD; cd13898; CuRO_3_Abr2_like; 1.
DR   Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 3.
DR   InterPro; IPR011707; Cu-oxidase-like_N.
DR   InterPro; IPR001117; Cu-oxidase_2nd.
DR   InterPro; IPR011706; Cu-oxidase_C.
DR   InterPro; IPR045087; Cu-oxidase_fam.
DR   InterPro; IPR033138; Cu_oxidase_CS.
DR   InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR   InterPro; IPR008972; Cupredoxin.
DR   PANTHER; PTHR11709:SF488; LACCASE-RELATED; 1.
DR   PANTHER; PTHR11709; MULTI-COPPER OXIDASE; 1.
DR   Pfam; PF00394; Cu-oxidase; 1.
DR   Pfam; PF07731; Cu-oxidase_2; 1.
DR   Pfam; PF07732; Cu-oxidase_3; 1.
DR   SUPFAM; SSF49503; Cupredoxins; 3.
DR   PROSITE; PS00079; MULTICOPPER_OXIDASE1; 2.
DR   PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|ARBA:ARBA00023008};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000249402};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..591
FT                   /note="L-ascorbate oxidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017391888"
FT   DOMAIN          31..144
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07732"
FT   DOMAIN          170..368
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00394"
FT   DOMAIN          459..571
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07731"
SQ   SEQUENCE   591 AA;  65109 MW;  AE6407F08ACB699F CRC64;
     MKISQSRLAL LALCLVQWVS CRVVQFQIDL TWEDVPVAGA LRKAILSNGQ LPGPALWLKQ
     GDDVEFLVNN SMPFATTVHF HGIQQQGTPW SDGVPGLSQD EIQPGDQFLY KWKAADYGSY
     VYHSHVRAQI EDGLYGPIYI EPEDSVERPF ALVSQADEPA MLEAEKHTQP IVISDWRPFP
     SEDILQIQVA SGVENYCSNS ILINGKGSVY CPSQEHINAI TTEAQKQILG NATLTDMACL
     PPQAIVGSYP ADLSKVPKGF YEGCTPSEGP TEVFQVDAAS QYVSYDLISM AGLSSLVFSI
     DEHPMYVYAI DGRYVEPLLV DAVTVPIGSR YSVMVQLKSD PAGDYTVRVA NNYATQLING
     TAVLSYGRST PGQSHPSQPY LNEAGANATT TAVFLNESRV VPFPVETPAL HADRTYILNV
     NTINASYIWT LGNSYPMSNE ELSPPVLFNL SAISPAYSIT TLNNTWVDLI INITTMGQPQ
     HPIHKHSNKY FVIGQGSEPF TYSSVAEAME SIPQNFNLEN PQFRDTFYSP PSNTAPSWLA
     IRYLVENPGP FLLHCHLQMH HTGGLALALL DGVDAWPMDI PEEYRMPVMP V
//