ID A0A0M8N8Z7_9HYPO Unreviewed; 616 AA.
AC A0A0M8N8Z7;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=L-ascorbate oxidase {ECO:0000313|EMBL:KOS22470.1};
GN ORFNames=ESCO_002083 {ECO:0000313|EMBL:KOS22470.1};
OS Escovopsis weberi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Escovopsis.
OX NCBI_TaxID=150374 {ECO:0000313|EMBL:KOS22470.1, ECO:0000313|Proteomes:UP000053831};
RN [1] {ECO:0000313|EMBL:KOS22470.1, ECO:0000313|Proteomes:UP000053831}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA de Man T.J., Stajich J.E., Kubicek C.P., Chenthamara K., Atanasova L.,
RA Druzhinina I.S., Birnbaum S., Barribeau S.M., Teiling C., Suen G.,
RA Currie C., Gerardo N.M.;
RT "The genome of the fungus Escovopsis weberi, a specialized disease agent of
RT ant agriculture.";
RL Submitted (JUL-2015) 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:KOS22470.1}.
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DR EMBL; LGSR01000006; KOS22470.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8N8Z7; -.
DR STRING; 150374.A0A0M8N8Z7; -.
DR OrthoDB; 449862at2759; -.
DR Proteomes; UP000053831; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd04205; CuRO_2_LCC_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: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; 2.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000053831};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 87..201
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 212..355
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 480..587
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
SQ SEQUENCE 616 AA; 68789 MW; 3CACC1A65C654D28 CRC64;
MKAYDEEHEL LPPPIRRNPF SAWLVWLVFT ILLCLFAASL FGFQHKDELR RIISSQDSEQ
LAIKLHPSKH STREPTTLSF QWNITLGTRA PDGVEKLVYL VNGQFPGPTI EARSGDRILV
NVHNGLPDGE GVSIHWHGLR MKGHNAMDGA VGFTQCPIPS GSDFTYDFQI GNEEHGTFWW
HSHSELQLGD GLFGGLVVHQ HRRDRDHVPH DEVLLLVGDW FHRPQAEVAA QYWHAKGLAL
EPVPDSILVN GRGRYNCSMA VPARPVECKK VPLTKMRPLF RKRSSRTRLR VVNTGTIAGL
RLQLDGATLR PIEVDGGCMV DAPSTESVGI LYPGERVDLE VSWRESYTKN PWLNVFLDPE
NFKHQNPALA PNHSFPVIPK TLRGAERKAP LIELEKYQDL TTLPATATVK PVYHNSTQET
ILLYLKTEVL AIEGNKPMGF INRTSWLPSA MPLISEPRST WDSHQFVPLI ESDTDFRPKQ
VTLVLNNLDD GSHPFHMHGY SFEVLSSYQS DYRGHGSYNP FAPPRENDIQ APGRVWNKSP
LRKDTVSVPR RGSVVLSFTA DNPGTWMLHC HMLVHMGTGM AAGIQVGNVS TGAVARSGPT
FDPSAARLCP SAMAGK
//
