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
//