ID   A0A2J6PM31_9HELO        Unreviewed;       620 AA.
AC   A0A2J6PM31;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Multicopper oxidase {ECO:0000313|EMBL:PMD15059.1};
GN   ORFNames=NA56DRAFT_582698 {ECO:0000313|EMBL:PMD15059.1};
OS   Hyaloscypha hepaticicola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Hyaloscyphaceae; Hyaloscypha.
OX   NCBI_TaxID=2082293 {ECO:0000313|EMBL:PMD15059.1, ECO:0000313|Proteomes:UP000235672};
RN   [1] {ECO:0000313|EMBL:PMD15059.1, ECO:0000313|Proteomes:UP000235672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 7357 {ECO:0000313|EMBL:PMD15059.1,
RC   ECO:0000313|Proteomes:UP000235672};
RG   DOE Joint Genome Institute;
RA   Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA   Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA   Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA   Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA   Martin F., Perotto S.;
RT   "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC       {ECO:0000256|ARBA:ARBA00010609}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KZ613516; PMD15059.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2J6PM31; -.
DR   STRING; 1745343.A0A2J6PM31; -.
DR   OrthoDB; 537265at2759; -.
DR   Proteomes; UP000235672; Unassembled WGS sequence.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006811; P:monoatomic ion transport; IEA:InterPro.
DR   CDD; cd13877; CuRO_2_Fet3p_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   InterPro; IPR044130; CuRO_2_Fet3-like.
DR   PANTHER; PTHR11709:SF361; IRON TRANSPORT MULTICOPPER OXIDASE FET3; 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:UP000235672}.
FT   DOMAIN          88..202
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07732"
FT   DOMAIN          214..362
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00394"
FT   DOMAIN          424..553
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07731"
FT   REGION          1..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   620 AA;  67691 MW;  3A7036774C78DF63 CRC64;
     MYNNLNPVIV PSSSTSQSST SSTSSTSSHA TTSSHSTSSS SSSTTLVTST KTSSTTPFTA
     CSTIKTTATS AAATTNPRPI LRTYNWNIEW VNAAPDGYER AFVGINGQWP LPVLSANIGD
     TIKIDIYNGL GNETTSLHFH GIHQGNTTFE DGAAMVSQCP IAPGESFVTE FVLTQSGTYW
     YHAHVGGQYI DGFRGPLIVR DNTVLKNYGQ IDGEYTLSLT DVYHVEAPYL INYYLSANNY
     NGAEPVPDSA LINEGQNTKF DITPGQTYMF HVVNMGAIAG QFLQFDQHNM TIIEADGVYT
     QPYEVSQLFV AVAQRYTVLV TALPSSCENF AIVSQFLTDM FDSSVTPAGQ QPTCTAYLVY
     NSAAPLPAPF TLTPQPWDDT LLVPYDQQPL WDSSDVNYVY LTVDFEQNDW GSNRAAMNGL
     TYISQKVPTF FSALTAPAAY QQNPQIYGQV NAQVVQYGQV VEIDLNNHDT RAHPFHLHGH
     QFQIINRAGN EPMWPGLYSA PAAPMRRDTV VVYPGVGITL RFIANNPGVW LFHCHTEFHV
     EAGMTATFIE APDVMVARKP YVPNSHRDVC DAQGIPRQGN AGGDDTNWLD LSNANTEPSQ
     TYYGALINGP AVNPYTGGPD
//