ID   A0A1K0H5L9_9BASI        Unreviewed;       703 AA.
AC   A0A1K0H5L9;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   08-OCT-2025, entry version 28.
DE   SubName: Full=Related to cell surface ferroxidase {ECO:0000313|EMBL:SAM65069.1};
GN   ORFNames=UBRO2_00955 {ECO:0000313|EMBL:SYW75800.1}, UBRO_08280
GN   {ECO:0000313|EMBL:SAM65069.1};
OS   Ustilago bromivora.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX   NCBI_TaxID=307758 {ECO:0000313|EMBL:SAM65069.1, ECO:0000313|Proteomes:UP000179920};
RN   [1] {ECO:0000313|EMBL:SAM65069.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=UB2112 {ECO:0000313|EMBL:SAM65069.1};
RA   Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA   Babar A., Rosenke K.;
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000179920}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UB2112 {ECO:0000313|Proteomes:UP000179920};
RA   Guldener U., Guldener U.;
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:SYW75800.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=UB2 {ECO:0000313|EMBL:SYW75800.1};
RA   Guldener U.;
RL   Submitted (AUG-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; LT558117; SAM65069.1; -; Genomic_DNA.
DR   EMBL; ULHB01000011; SYW75800.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1K0H5L9; -.
DR   OrthoDB; 2121828at2759; -.
DR   Proteomes; UP000179920; Chromosome i.
DR   Proteomes; UP000658997; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd13857; CuRO_1_Diphenol_Ox; 1.
DR   CDD; cd13886; CuRO_2_MCO_like_1; 1.
DR   CDD; cd13910; CuRO_3_MCO_like_4; 1.
DR   FunFam; 2.60.40.420:FF:000045; Laccase 2; 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:SF414; ADR239WP; 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   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000658997};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        50..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          137..247
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07732"
FT   DOMAIN          285..455
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00394"
FT   DOMAIN          553..665
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07731"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   703 AA;  76784 MW;  EA80473D36DCDC76 CRC64;
     MVAKANLRPE SQQMASEGSI QSLSVAEKDS EGSHPQQPGS EQRKARPRNL LASLGALVCI
     LALTLSLGLG LGLTRKHRTQ SGAATSSSKI VPGATASNLA FIPREQLVDP TQLTLSPTWD
     RNAPPQDRIF NWTLTQVLAN PAGTTKQMRL VNGLYPGPLI EANIGDRIIV HVENKMPVPT
     TIHWHGQYQR GSNEMDGSAG ITECGIAPGT TFTYNWTVQQ SGSYWWHSHY GPTYADGLFG
     PLILHGDDEE FKMTNPDNAT ASQAGVAPTV TIANGIAVRT DYDQDHIFVV NDAYQADSFT
     VAAIAKSKAG PPGGEQGDEP TPDYGMINGL SFSNCGLAPN GTTCISDTPQ GKSAYNFTVP
     ANKRVRMRVI NAGSLATFRF SVDGHNLTVI EADGIEVEPV IVQSLNVMVA QRYSVIIETD
     KPVGAYAVRA EVMDDMFAYD NPFLVMDQYA IMRYESVAAS AQPMTNPSNS TLLNVTETLS
     TSQLVPITRI DAPASNMTTK LVVNFSLNAY SNWHAFFNQT TFTSEMAAQA SLMKSYTFET
     TQRSSSNTSV DAYYNDPDEM IVTNTDVVVM DVIINNLDEG SHPFHLHGYS PFLIGEGAGN
     FQAEDQPNFA AARVNPMRRD VFSVPPFSWM AFRFVADNVG VWPFHCHLMP HMAIGLLMQF
     QVLPDQIAKL PVTDQYYTQC SAVYDWVQQN QNLLTLTGNP GYM
//