ID A0A0G2IFQ0_9PEZI Unreviewed; 523 AA.
AC A0A0G2IFQ0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Putative l-ascorbate oxidase {ECO:0000313|EMBL:KKY39040.1};
GN ORFNames=UCDDA912_g00947 {ECO:0000313|EMBL:KKY39040.1};
OS Diaporthe ampelina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX NCBI_TaxID=1214573 {ECO:0000313|EMBL:KKY39040.1, ECO:0000313|Proteomes:UP000034680};
RN [1] {ECO:0000313|EMBL:KKY39040.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY39040.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY39040.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY39040.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAY-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:KKY39040.1}.
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DR EMBL; LCUC01000040; KKY39040.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2IFQ0; -.
DR STRING; 1214573.A0A0G2IFQ0; -.
DR OrthoDB; 449862at2759; -.
DR Proteomes; UP000034680; 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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000034680}.
FT DOMAIN 1..66
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 77..239
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 345..476
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
SQ SEQUENCE 523 AA; 57522 MW; E81FC231C9FCDC97 CRC64;
MHWHGLAQRM AQFSDGAVLA SQWPIPPLNY FDYEIEALPE DAGTYFYHSH VGMQALTVFG
ALIVEDCAAP PYQYDDERTL LWHEHYKQND SAFEAGLLAA PLVFGGEVQA VLLNGQGVAI
NHTAGEIPGD ASCQLPVVEV EPDKTYRFRF IGATSLSHSI MAFEGHEILT VIAVDGGQYT
QPAATYRMQI GSGQRFDVLF KTKSQAELDA AGKTDFFIQF ETRDRPSVYQ SYGVLRYTGA
GAGGQAPVPS APSTPVFNLT TKTYDWLENT LQPLKPDPDF PTLEEVTRRV VIDVVQLLSP
TTGQTIWQLN GLNWNELVAY PVPLLVDIYL RGEEAVPDYE AAVANGGWDP KNKAYAAKVG
EVLEIVFQNT GSIVNNNGGV DVHPFHAHGA HYYDMGSGNG TYDADATEAA RVEAGYTPVK
RDTTMLYRYE TKTTAGAPAG WRAWRIRIND PGVWMIHCHV LQHMVMGMQS VWVVGNASEI
QKTPTELSQG YFTFGGSVTG NETTDPQVYE QFDHSASTCS ISI
//
