ID   Q6QNN5_PHACH            Unreviewed;       297 AA.
AC   Q6QNN5;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   19-JAN-2022, entry version 55.
DE   SubName: Full=Multicopper oxidase 3B-I6 splice variant {ECO:0000313|EMBL:AAS21666.1};
GN   Name=mco3 {ECO:0000313|EMBL:AAS21666.1};
OS   Phanerodontia chrysosporium (White-rot fungus) (Sporotrichum pruinosum).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Phanerochaetaceae; Phanerodontia.
OX   NCBI_TaxID=2822231 {ECO:0000313|EMBL:AAS21666.1};
RN   [1] {ECO:0000313|EMBL:AAS21666.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BKM-1767 {ECO:0000313|EMBL:AAS21666.1};
RA   Larrondo L.F., Gonzalez B., Cullen D., Vicuna R.;
RT   "Characterization of a multicopper oxidase gene cluster in Phanerochaete
RT   chrysosporium and evidence of altered splicing of the mco transcripts.";
RL   Submitted (JAN-2004) 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; AY532146; AAS21666.1; -; mRNA.
DR   VEuPathDB; FungiDB:AGR57_8975; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   Gene3D; 2.60.40.420; -; 1.
DR   InterPro; IPR045087; Cu-oxidase_fam.
DR   InterPro; IPR011707; Cu-oxidase_N.
DR   InterPro; IPR008972; Cupredoxin.
DR   PANTHER; PTHR11709; PTHR11709; 1.
DR   Pfam; PF07732; Cu-oxidase_3; 1.
DR   SUPFAM; SSF49503; SSF49503; 1.
PE   2: Evidence at transcript level;
KW   Copper {ECO:0000256|ARBA:ARBA00023008};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        39..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          103..214
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07732"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..30
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   297 AA;  32416 MW;  2C3A61763CC023BE CRC64;
     MAAAEDIAPE EKVALLEPHS NHDTQSASPR RRRPHAAHAA LLAVFLLGVA LLALGVWGTY
     ASSPRGPSLP RELQRTPHTH FALDGLRGQP PQTRSHAFVV SEVEGAPDGV RKPMLVVNGM
     YPGPTIEANQ GDRVVVKVTN MLENRTTIHW HGLFQNGTNY YDGTAAITEC GIPPGQTLVY
     NFTLGEFSGT TWWHAHYSTQ YTDGITGALV VHPTDPLPAS IPPWDGDLVV QVSDLYHTFS
     PVLLERFLSV SPPALRPTRH TAVLREPPAA AAWWRTIVAL RSTDDTAFFG NDVTPFC
//