ID M7SF02_EUTLA Unreviewed; 624 AA.
AC M7SF02;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Putative l-ascorbate oxidase protein {ECO:0000313|EMBL:EMR62793.1};
GN ORFNames=UCREL1_10277 {ECO:0000313|EMBL:EMR62793.1};
OS Eutypa lata (strain UCR-EL1) (Grapevine dieback disease fungus) (Eutypa
OS armeniacae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Diatrypaceae; Eutypa.
OX NCBI_TaxID=1287681 {ECO:0000313|EMBL:EMR62793.1, ECO:0000313|Proteomes:UP000012174};
RN [1] {ECO:0000313|Proteomes:UP000012174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR-EL1 {ECO:0000313|Proteomes:UP000012174};
RX PubMed=23723393; DOI=10.1128/genomeA.00228-13;
RA Blanco-Ulate B., Rolshausen P.E., Cantu D.;
RT "Draft genome sequence of the grapevine dieback fungus Eutypa lata UCR-
RT EL1.";
RL Genome Announc. 1:E0022813-E0022813(2013).
CC -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC {ECO:0000256|ARBA:ARBA00010609}.
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DR EMBL; KB707371; EMR62793.1; -; Genomic_DNA.
DR RefSeq; XP_007798122.1; XM_007799931.1.
DR AlphaFoldDB; M7SF02; -.
DR STRING; 1287681.M7SF02; -.
DR KEGG; ela:UCREL1_10277; -.
DR eggNOG; KOG1263; Eukaryota.
DR HOGENOM; CLU_006504_8_3_1; -.
DR OMA; QWPIAPH; -.
DR OrthoDB; 449862at2759; -.
DR Proteomes; UP000012174; 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 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:UP000012174}.
FT DOMAIN 49..162
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 175..329
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 454..581
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
FT REGION 332..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 624 AA; 68537 MW; E1B410EFB4CBF997 CRC64;
MFTLRRSLSD TRAYLPLFAF LGLISAVGGV TTQVHDASFT PGAVLHISAQ NISIGGIERY
STLINESLPA PELRLPEGEV VWIRVYNDMT EQNTTIHWHG LAQAASPFSD GTPLASQWPI
PPQHFFDYEL QVPNGSAGTY FYHSHVGFQA VTAAGPLIIE DKGERPYPTD GERTIFVHGL
WNETDAQVEQ GVNSNPLAWP GETNGIMING KTISDFGIVD DSTAGLAVIE VDPGKTYRLR
FIGSMALSYT ALAFESHDEL QVIEADGSYT KPAPTEIIQI GGGQRFSTLL QTKSCEELRD
LGKLDFYIQT ETRERDYTVT NYAILRYTNT CGSGDSSSSS SSTSFADPLP TDSYPTQKPI
DMPPTINGFL DYQLQPLAPN DFPSASEVTR RVVLNAQVFE DGYYMWRDSN VSWGEGPLGG
AAPHTVPETP YLVGLYLNQT EYLPDYDAAV ANGGVDPRTQ TFPARIGEVL EIVIQNLGAE
SRTGLAAGMI DVHPFHAHGG HVYDAGSGPG PWSSEIMERQ LEGTQPVLRD TTMLFRYNET
AAPFAKSGWR AWRLRIEDPG VWMIHCHWLQ HMAQGMQTVW VFGDAEDILT VPRPEVEGYL
AYGGDVYGNA THDPVAVHFS EVAT
//
