ID   A0A317WCU9_ASPEC        Unreviewed;       596 AA.
AC   A0A317WCU9;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=L-ascorbate oxidase {ECO:0000313|EMBL:PWY84193.1};
GN   ORFNames=BO83DRAFT_433771 {ECO:0000313|EMBL:PWY84193.1};
OS   Aspergillus eucalypticola (strain CBS 122712 / IBT 29274).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448314 {ECO:0000313|EMBL:PWY84193.1, ECO:0000313|Proteomes:UP000246171};
RN   [1] {ECO:0000313|EMBL:PWY84193.1, ECO:0000313|Proteomes:UP000246171}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 122712 {ECO:0000313|EMBL:PWY84193.1,
RC   ECO:0000313|Proteomes:UP000246171};
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 (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC       {ECO:0000256|ARBA:ARBA00010609}.
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:PWY84193.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; MSFU01000002; PWY84193.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A317WCU9; -.
DR   VEuPathDB; FungiDB:BO83DRAFT_433771; -.
DR   OrthoDB; 449862at2759; -.
DR   Proteomes; UP000246171; 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   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..596
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016262887"
FT   DOMAIN          31..143
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07732"
FT   DOMAIN          173..373
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00394"
FT   DOMAIN          465..576
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07731"
SQ   SEQUENCE   596 AA;  65431 MW;  DE1724E94668BFC1 CRC64;
     MSISQSRLAL LALCFVQWVS GRVVQFQLDL TYEDVSVAGD VHKAIVSNGQ IPGPTLWLKQ
     GDDVEFLVNN SMSINTTVHF HGIEQLGTPW SDGVPGLSQE QIKPGEQFLY KWKASQYGSY
     IYHSHTRAQI DDGLYGAIYI EPADSVERPF HLIAGSDADE QQAMLTAEKN TRPVLISDWR
     AFSSHDILQI QTESGVEAYC ANSVLINGKG SVLCPSQEHI NAATTPQQKQ ILGNLTLTDM
     GCLPPTPGVV GPYPYDLSKI PKGFYEGCTP SEGPTEVFKV NSSSRYASFD FISMAGSTSL
     VFSIDEHPMY VYAIDGRYVE PLLVDAVTVP VASRYSVMVP LKSEDQAGDY TIRVANNYAN
     QLINGTGVLS YDTATPKQIG TSQPYINEAG ANATASTVIL NETNVVPFPV VAPATKADRT
     YILNVENANS SYTWTLGNQY PVSNEELRPP VLFNLSSISQ AYSAMTENGT WVDLIINITT
     SGQPQHPIHK HSNKYFVIGT GNQPFIWSSV EEAMKDIPEN FNFENPQMRD TFYSPSSSTG
     PSWLAMRYPI VNPGPFLLHC HLQMHHVGGL ALALLDGVDA WPTDIPEGYR LPVMPI
//