ID A0A1S7UJB9_ROSNE Unreviewed; 626 AA.
AC A0A1S7UJB9;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Putative bilirubin oxidase {ECO:0000313|EMBL:GAP83355.2};
DE EC=1.3.1.98 {ECO:0000313|EMBL:GAP83355.2};
DE EC=2.7.4.2 {ECO:0000313|EMBL:GAP83355.2};
GN ORFNames=SAMD00023353_0202930 {ECO:0000313|EMBL:GAP83355.2};
OS Rosellinia necatrix (White root-rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Xylariaceae; Rosellinia.
OX NCBI_TaxID=77044 {ECO:0000313|EMBL:GAP83355.2};
RN [1] {ECO:0000313|EMBL:GAP83355.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W97 {ECO:0000313|EMBL:GAP83355.2};
RA Kanematsu S.;
RT "Draft genome sequence of Rosellinia necatrix.";
RL Submitted (MAR-2016) 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; DF977447; GAP83355.2; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S7UJB9; -.
DR STRING; 77044.A0A1S7UJB9; -.
DR OMA; GMWIIED; -.
DR OrthoDB; 315590at2759; -.
DR Proteomes; UP000054516; Unassembled WGS sequence.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0004631; F:phosphomevalonate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0008762; F:UDP-N-acetylmuramate dehydrogenase activity; IEA:UniProtKB-EC.
DR CDD; cd13889; CuRO_3_BOD; 1.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 3.
DR InterPro; IPR011707; Cu-oxidase-like_N.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR008972; Cupredoxin.
DR PANTHER; PTHR48267:SF1; BILIRUBIN OXIDASE; 1.
DR PANTHER; PTHR48267; CUPREDOXIN SUPERFAMILY PROTEIN; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR SUPFAM; SSF49503; Cupredoxins; 3.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000313|EMBL:GAP83355.2};
KW Reference proteome {ECO:0000313|Proteomes:UP000054516};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:GAP83355.2}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..626
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010554117"
FT DOMAIN 103..211
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 398..523
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
SQ SEQUENCE 626 AA; 69616 MW; 1989727DAA3CF651 CRC64;
MFSKLASLAL VSCLCAGTIA QRTLEYDIPA DEAAALAQVV DDDDSTFSAA RKGDESPEYS
LIYRKPLPIP PVKQPKQIIT NPVTGKDIWY YEIEEKLFTQ QVYPNLMPAT LVGYDGMSPG
PSIVIPRGTE SVVRFVNNAQ RETSVHLHGS PSRAPFDGWA ADITRPGEYK DYYYPNFQSA
RLLWYHDHAL GITAENAYFG LAGAYILTDP AEDALGLPSG YGQFDIPLIL GSKFYNSNGT
LQSQLQEDTS TWGDVIHVNG QPWPYLDVQP RKYRFRFLNT GISRNYALYF ARSTSTSTKL
PFKVIASDSG LLDSPVTSST LLIAVAERYE VVFDFSQFAG QQIELRNLED VGGFGVDDDY
ENTDKVMRFN VAAGAVADPS TVPATLRAVP FPPETAGIDH HFEFHRQHGE WLINGVGFED
AANRVLANVP RGTVEIWELE NSSGGWTHPI HVHLVDFRVI SRTGGDRGVE PYESHGLKDV
VWLAKGETVR VEAHYEPWTG LYMFHCHNLI HEDQDMMAAF NVTMLQGFGY DETTDFSDPE
DDRWDAEPYV LADFRAGAGI FTSAAVKAKV ELLARQQPYS ELDAVTAALD DFWEGKDIGD
PNAALPRRDA TTPAPGPIPR YRRFVV
//