ID A0A0P7ARS3_9HYPO Unreviewed; 568 AA.
AC A0A0P7ARS3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Laccase-2 {ECO:0000313|EMBL:KPM35398.1};
GN ORFNames=AK830_g11182 {ECO:0000313|EMBL:KPM35398.1};
OS Neonectria ditissima.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Neonectria.
OX NCBI_TaxID=78410 {ECO:0000313|EMBL:KPM35398.1, ECO:0000313|Proteomes:UP000050424};
RN [1] {ECO:0000313|EMBL:KPM35398.1, ECO:0000313|Proteomes:UP000050424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R09/05 {ECO:0000313|EMBL:KPM35398.1,
RC ECO:0000313|Proteomes:UP000050424};
RA Gomez-Cortecero A., Harrison R.J., Armitage A.D.;
RT "Draft genome of a European isolate of the apple canker pathogen Neonectria
RT ditissima.";
RL Submitted (SEP-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:KPM35398.1}.
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DR EMBL; LKCW01000255; KPM35398.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7ARS3; -.
DR SMR; A0A0P7ARS3; -.
DR STRING; 78410.A0A0P7ARS3; -.
DR OrthoDB; 449862at2759; -.
DR Proteomes; UP000050424; Unassembled WGS sequence.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd13880; CuRO_2_MaLCC_like; 1.
DR CDD; cd13901; CuRO_3_MaLCC_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; IPR008972; Cupredoxin.
DR PANTHER; PTHR11709; MULTI-COPPER OXIDASE; 1.
DR PANTHER; PTHR11709:SF394; PLASTOCYANIN-LIKE DOMAIN-CONTAINING PROTEIN; 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.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000050424};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..568
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006135010"
FT DOMAIN 74..189
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 200..344
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 412..533
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
SQ SEQUENCE 568 AA; 61997 MW; 929570EB03732624 CRC64;
MSSLLSFVIL AAKLASAASG IGSSLDPALF SRATACDGNT ASTRSEWCDY SIDTDYTTEA
VDSGNTKEYW LELTDVTVAP DGVSRSAMAV NGSIPGPTLF ADWGDTVVIH VTNSLTTSLN
GSSVHWHGIR QNYTNQNDGV TAITQCPLAP GESLTYTWKA LQYGSAWYHS HFGLQAYQGI
FGGIIINGPA TANYDEDLGM VFLNDWDHQT VDELYASAQT SGPPTLDNGL INGTGVWEDD
DETQPRFNVS FTSGTSYRMR LVNAAVDTHW KFSIDNHTMT VIAADLVPIE PFETTIISLG
MGQRYDIIVE ADQADVADNF WMRAIPQSAC SDNESSNNIK GIVYYGDSPS TPSTDGYSYT
DGCDDDTSSV TPYISQDVSD ADWQDLESAT VGKNTAGLFK WYLNSTSMLV DWANPTLTYV
LNGTEEQETD DAVIELSEAS QWVYFVVQTT LGVPHPIHLH GHDFFVLAQG SGTYSSSVTL
NTSNPPRRDT ALLPASGYLV MAWKTDNPGV WLMHCHIGWH TSEGFAVQFI ERRSEIEGIT
DSDTLEDVCT AWSSFQEESE IEQEDSGI
//
