ID A0A1B8B6Q6_FUSPO Unreviewed; 602 AA.
AC A0A1B8B6Q6;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=L-ascorbate oxidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=FPOA_02333 {ECO:0000313|EMBL:OBS28395.1};
OS Fusarium poae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=36050 {ECO:0000313|EMBL:OBS28395.1, ECO:0000313|Proteomes:UP000091967};
RN [1] {ECO:0000313|EMBL:OBS28395.1, ECO:0000313|Proteomes:UP000091967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2516 {ECO:0000313|EMBL:OBS28395.1,
RC ECO:0000313|Proteomes:UP000091967};
RA Vanheule A., Audenaert K., Warris S., Van De Geest H., Schijlen E.,
RA Hofte M., De Saeger S., Haesaert G., Waalwijk C., Van Der Lee T.;
RT "Living apart together: crosstalk between the core and supernumerary
RT genomes in a fungal plant pathogen.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC {ECO:0000256|ARBA:ARBA00010609}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OBS28395.1}.
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DR EMBL; LYXU01000001; OBS28395.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B8B6Q6; -.
DR STRING; 36050.A0A1B8B6Q6; -.
DR OMA; ENIGAWM; -.
DR Proteomes; UP000091967; 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; cd13873; CuRO_2_AAO_like_2; 1.
DR CDD; cd13895; CuRO_3_AAO_like_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 InterPro; IPR035666; MCO_CuRO_3.
DR InterPro; IPR017762; Multicopper_oxidase_fun.
DR NCBIfam; TIGR03390; ascorbOXfungal; 1.
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000091967};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..602
FT /note="L-ascorbate oxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008603675"
FT DOMAIN 37..149
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 159..317
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 417..556
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
SQ SEQUENCE 602 AA; 67649 MW; 2D43810B668FB7EF CRC64;
MLFRCLALLP FLAGAFAKSK VHDDTFTPDY ILEATLDDIK INCKSRSSIT FNGTSPGPTI
YLREEQTTWI RVYNKIPDNN VTVHWHGLSQ RAAPFSDGTP LVSQWPIPVR QFFDYEIRPQ
LGDAGSYFYH SHVGFQILTA YGALVVRDAV KPEYKYDGDI PLIVGDNYAA QDEVIEEGLL
ADPFKWSGEP QAITINGNSG NKSFYDAPDS SCMPHVVHVD PGKVYRLRFI SSTALSMIKL
GIEDHDNFTV IEADGSYTKP AHIDHVQVSS GQRFSYLIKT KTSEEVCGGD KSQYWIRYES
RDRPQVISGY ALLKYQCDEG QNLPKSLPAT SPIELSNSTA DYLEYALEGL SEKNNQAFPR
LSEVTRTVTI QVNQILTTGA YENGTLNGTV AWAQNGLPWK ESVQAERHQV PYLIQVYENG
TTPNYTLALE HHGFDPETKA FPAKVGEVLD IVWENNNGPT GGWDFHPMHV HGYHVYDLGS
GNGTYNATEN EAHFDNFTPV LRDSTNLYRY AVKGVPHHTA GWRAWRIRIT EENIGAWMMH
CHIAQHQVMG MATVWVFGEA DQIRGKFPAP PYTQGYLDYG GSAYGSEDRQ PWVNHYYSNG
DD
//