ID   A0A2T3AP96_AMORE        Unreviewed;       621 AA.
AC   A0A2T3AP96;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Multicopper oxidase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=M430DRAFT_111255 {ECO:0000313|EMBL:PSS06752.1};
OS   Amorphotheca resinae ATCC 22711.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Amorphothecaceae; Amorphotheca.
OX   NCBI_TaxID=857342 {ECO:0000313|EMBL:PSS06752.1, ECO:0000313|Proteomes:UP000241818};
RN   [1] {ECO:0000313|EMBL:PSS06752.1, ECO:0000313|Proteomes:UP000241818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22711 {ECO:0000313|EMBL:PSS06752.1,
RC   ECO:0000313|Proteomes:UP000241818};
RX   PubMed=29315638; DOI=10.1111/nph.14974;
RA   Martino E., Morin E., Grelet G.A., Kuo A., Kohler A., Daghino S.,
RA   Barry K.W., Cichocki N., Clum A., Dockter R.B., Hainaut M., Kuo R.C.,
RA   LaButti K., Lindahl B.D., Lindquist E.A., Lipzen A., Khouja H.R.,
RA   Magnuson J., Murat C., Ohm R.A., Singer S.W., Spatafora J.W., Wang M.,
RA   Veneault-Fourrey C., Henrissat B., Grigoriev I.V., Martin F.M., Perotto S.;
RT   "Comparative genomics and transcriptomics depict ericoid mycorrhizal fungi
RT   as versatile saprotrophs and plant mutualists.";
RL   New Phytol. 217:1213-1229(2018).
CC   -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC       {ECO:0000256|ARBA:ARBA00010609}.
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DR   EMBL; KZ679020; PSS06752.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T3AP96; -.
DR   STRING; 857342.A0A2T3AP96; -.
DR   InParanoid; A0A2T3AP96; -.
DR   OrthoDB; 64567at2759; -.
DR   Proteomes; UP000241818; 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; cd13857; CuRO_1_Diphenol_Ox; 1.
DR   CDD; cd13886; CuRO_2_MCO_like_1; 1.
DR   CDD; cd13910; CuRO_3_MCO_like_4; 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:SF515; ADR239WP; 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:UP000241818};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          108..223
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07732"
FT   DOMAIN          234..398
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00394"
FT   DOMAIN          465..603
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07731"
FT   REGION          50..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   621 AA;  68050 MW;  6E6E074C5BDCEEF9 CRC64;
     MQTGELQASP IGKRKYGRPL LLLVGAAIVF VALALGLGLG LGLGLKHHHH AASSSTSGLP
     PSSNPANVSS TTATGAVQSW RRDTAEYNLD MNWDMNAAPT TRVFNLTVSE IQAAPDGVLR
     PVLVFNGQFP GPVIEVNRGD RVLVNVTNEL ANVTTVHWHG LYQNGTNWMD GTAGITQCGI
     PPGTSFLYNF TVDREYGTYW YHSHESTQYT DGLVGPFIVH APEEASLRKD YDFDQIILLQ
     DWYHDLSTAL LPGYLASGNE NAEPVPDNGL IQGTNFFNCS SYGADSGYNC QNNSTQATFV
     VAQNKRYRLR MINTGAFGEF QVSVDNHTLS VIEADATLVQ PVTVNRVPIA VAQRYSVILH
     TNQTATNYWF RAQMNTYCFT SNNAPVLDPD VRALLTYTNT TDEPTHSADW ATALELQCQD
     LSSSDLVPLV PEAAPSPDQT FVVDVSFQIG AYALDKAYIN STTWVPSKIP TVNQAISGLH
     ADNSTFNANG LSSAFGPSQF VISVPEIQVI DVLVNSLDEG AHPFHLHGHK FWIMASGSSG
     VFDWSTYQDL NTTNPMKRDT MTIDAYGWAL IRFVADNPGL WAFHCHISWH MEAGLLMQFQ
     TRNDLMKDWT LPSDVAALCN G
//