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Database: UniProt
Entry: A0A0P1BAL4_9BASI
LinkDB: A0A0P1BAL4_9BASI
Original site: A0A0P1BAL4_9BASI 
ID   A0A0P1BAL4_9BASI        Unreviewed;       652 AA.
AC   A0A0P1BAL4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Multicopper oxidases {ECO:0000313|EMBL:CEH12479.1};
OS   Ceraceosorus bombacis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Exobasidiomycetes; Ceraceosorales; Ceraceosoraceae; Ceraceosorus.
OX   NCBI_TaxID=401625 {ECO:0000313|EMBL:CEH12479.1, ECO:0000313|Proteomes:UP000054845};
RN   [1] {ECO:0000313|EMBL:CEH12479.1, ECO:0000313|Proteomes:UP000054845}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Magalhaes I.L.F., Oliveira U., Santos F.R., Vidigal T.H.D.A.,
RA   Brescovit A.D., Santos A.J.;
RL   Submitted (SEP-2014) 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; CCYA01000149; CEH12479.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P1BAL4; -.
DR   STRING; 401625.A0A0P1BAL4; -.
DR   OrthoDB; 449862at2759; -.
DR   Proteomes; UP000054845; Unassembled WGS sequence.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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:SF218; FI03373P-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; 1.
DR   PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|ARBA:ARBA00023008};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054845};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..652
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006059358"
FT   DOMAIN          73..171
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07732"
FT   DOMAIN          183..317
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00394"
FT   DOMAIN          471..617
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07731"
SQ   SEQUENCE   652 AA;  72584 MW;  0CFB964AB4D4BE57 CRC64;
     MLSTRRLLHA SCLLAVLLCL SSTPSRAATV KQDVNLRAEL TIPPEDASNV KHVFLDVSQT
     TLWADGQPVP GEPVVNGSSP GPVLRFMKGD FLVIRVTNRM STWNTTMHWH GLTQSMTPIS
     DGVPMVTQWP IPPNTWFEYG MKLRDKGTYY YHPHVDLQQS TAHGAFIVED GEEPPYKYDL
     DKPLILADYY HQPQEELLQG LLGQPFKWAG SAKALLLNGK ALSSAPCNQT LASTYQLDCK
     DAPRNAGKRP EIVHLGHGQT IRLRWIGAQS LMYTKVAIAN HKQRIIEADG TYTKYLEVPD
     MEIGPGQRYS TLVDGKTKEA VEQDGSGGCY WIRLESQWRN PGTFGWALLA YPSCDVDKVL
     AQPQPTPAPI NSTERMLPNS TFGWISGSLT PLKEPSSHQD RMPSDSEVSR RVILNAQQIN
     ILGSMGNYSR WTQNDVWYVE GADQPIGRMA TKVPYLIQLY KRLREAPSWN RAFNTSDNKH
     PKGFDPLAQV WVAKPGEVID IVIINNGSMA SGLTEIHTWH KHGDKHWTLA SGPGNFSVEA
     LAQARSNGQW SDPIPRDTST VWPGPGETIA DPKVVLPAHS SGGWTVLRTK IQHMDLGVWL
     LHCHLIFHAV MGMSTTWALD IPKLGASSSL YDDPDYLEFG RNVTSPYTNM RP
//
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