ID A0A0D2D0T1_9EURO Unreviewed; 644 AA.
AC A0A0D2D0T1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=L-ascorbate oxidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV07_05216 {ECO:0000313|EMBL:KIW29399.1};
OS Cladophialophora immunda.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=569365 {ECO:0000313|EMBL:KIW29399.1, ECO:0000313|Proteomes:UP000054466};
RN [1] {ECO:0000313|EMBL:KIW29399.1, ECO:0000313|Proteomes:UP000054466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 83496 {ECO:0000313|EMBL:KIW29399.1,
RC ECO:0000313|Proteomes:UP000054466};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora immunda CBS83496.";
RL Submitted (JAN-2015) 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; KN847042; KIW29399.1; -; Genomic_DNA.
DR RefSeq; XP_016249615.1; XM_016392096.1.
DR AlphaFoldDB; A0A0D2D0T1; -.
DR STRING; 569365.A0A0D2D0T1; -.
DR GeneID; 27344410; -.
DR VEuPathDB; FungiDB:PV07_05216; -.
DR HOGENOM; CLU_006504_3_2_1; -.
DR OrthoDB; 449862at2759; -.
DR Proteomes; UP000054466; 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; cd13854; CuRO_1_MaLCC_like; 1.
DR CDD; cd13880; CuRO_2_MaLCC_like; 1.
DR CDD; cd13901; CuRO_3_MaLCC_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:SF71; LACCASE; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000054466};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..644
FT /note="L-ascorbate oxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002240135"
FT DOMAIN 121..236
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 246..377
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 499..605
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
SQ SEQUENCE 644 AA; 72440 MW; E1AD1E6306F37E45 CRC64;
MVSIWARIVA VFHFILLSPP KEEGPDQRPL SASVHAAFPP QVTVQADDHQ APTPFLPPSA
PRASNFTCEY PDLDGYTFCS TYGDRSCWLK HPDPQKQVYD INTDYENVFP KGKTRQYYIE
VNEKTIRPDG VDRKAMVVND TYPGPWIEAC WGDWLEITVK NNLKTNGTTI HWHGIRQLHT
TASDGVNGIT QCPIAPGETY TYRFRAMQYG TTWYHSHYSL QYGEGVLGPM TIHGPASADY
DEAQPPVLMT DWTHESWYTK WWDNVINGKA RPEPDNILVG GKGTWPASKP SKGFRLDFVK
GTRYLLRLIN TSVDTSFVFS IDNHKIQVIG SDLVPIVPYI TDHVVVGIGQ RYHIIVTANP
RDGKANATYW IRTQPAKGCD PGGTSKIDPR TGIVVYKDTE PVDYPVTFDT TCRDEPYDKL
VPILKWTVGR PSNIAANSQF DIGFDQITAG TEYPANLTRG RFNMYSDTMW LNFTNVTLSQ
NLSAPQAAFN SHSVAVKENS QKDDWVYLLV SGTGIPRSGR TYLPIAHPIH LHGHDFAILQ
QSTKPYRIGG LDLKLDNPPR RDVAFMPRDG YLVLAFKADN PGVWLMHCHI ATHASGGLAM
QIVENGNQTV LDPFDQKQLA HTCKKWKDWA SDKDHRFLQD DSGI
//
