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Database: UniProt
Entry: A0A317XMH2_9BASI
LinkDB: A0A317XMH2_9BASI
Original site: A0A317XMH2_9BASI 
ID   A0A317XMH2_9BASI        Unreviewed;       799 AA.
AC   A0A317XMH2;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=L-ascorbate oxidase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BCV70DRAFT_163380 {ECO:0000313|EMBL:PWY99039.1};
OS   Testicularia cyperi.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Anthracoideaceae; Testicularia.
OX   NCBI_TaxID=1882483 {ECO:0000313|EMBL:PWY99039.1, ECO:0000313|Proteomes:UP000246740};
RN   [1] {ECO:0000313|EMBL:PWY99039.1, ECO:0000313|Proteomes:UP000246740}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 3645 {ECO:0000313|EMBL:PWY99039.1,
RC   ECO:0000313|Proteomes:UP000246740};
RX   PubMed=29771364; DOI=10.1093/molbev/msy072;
RA   Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA   Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA   Spatafora J.W., Aime M.C.;
RT   "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT   clade Ustilaginomycotina.";
RL   Mol. Biol. Evol. 0:0-0(2018).
CC   -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC       {ECO:0000256|ARBA:ARBA00010609}.
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DR   EMBL; KZ819196; PWY99039.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A317XMH2; -.
DR   STRING; 1882483.A0A317XMH2; -.
DR   InParanoid; A0A317XMH2; -.
DR   Proteomes; UP000246740; 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:UP000246740};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..799
FT                   /note="L-ascorbate oxidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016299860"
FT   DOMAIN          79..195
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07732"
FT   DOMAIN          254..423
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00394"
FT   DOMAIN          609..753
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07731"
FT   REGION          444..463
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   799 AA;  86971 MW;  F3A44E7C643CC216 CRC64;
     MAALARLLLA LFWSAICVSA ASLPPRQHPT NLTLGVETRL FTRDVVPSDE QASPARPTTS
     GLAAGEQDAL TVRHYSLVVT EQTIWATCSP ATSSLVYNGT FPGPTLRARA GEILQVRVHN
     HSSRNTTVHF HGLAMRLHPV MDGTHMISQW PITPGHYFDY RIPLTAEDAG TYFYHSHVGL
     QAMTAYGALI VDDPPSTGTD IGTGPATSTA QFDDRVANPN SQAASRPKVH IQADYGLDKT
     GKSSPNAPYA YDEDRVLALG DYWGDHDQDK IAAGLEADPF VWPGSPSSLL LNGVSSVSAE
     RGGLEKACNQ TAVGLLGETC TRAPPGCQTR GFAQLNLDYD KTYRLRFIGA TALMYVSAGI
     LGSDGKTLEK LQLIEADGTY LEKLEVDHIE ITSGQRYSAL YRSKSRLQAQ KDGANGIYWM
     RIESRWRTGP SMWVKIVYND DKKENPSSQM TTASMSPPPP SSQATYLPTE TFGWVTGAMA
     PLRGWSEEMP ADSEVSRTVV IDMQQTPFYG SKKGVRWMQN GASFNEQDPA SATSGASGDG
     VSRYRPYLVN MMVGSVEVPS TYERAFSPQN RWNQDPFQSG LLRLPSSSPR GTTNGAKKTE
     LEMAKKHHLG QGFDDKLGVY VGKPGEVLDI VLVNRPSAIS SSTEMHPWHM HSRKHWTRTI
     QPGSFSFAAL DRLYSSPSSA AFARPIPRDT TVVYASPGAA YLGQTVPNPT HEDGGWSVLR
     YKVDGDNAGM FVLHCHILFH LQMGMATVWA MAPDVLLDRA KPYLPAPSSN ADGNGKSQTQ
     IQGLSPAYLT YATNVDAIA
//
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