GenomeNet

Database: UniProt
Entry: A0A1B8B6Q6_FUSPO
LinkDB: A0A1B8B6Q6_FUSPO
Original site: A0A1B8B6Q6_FUSPO 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system