ID A0A0D1Y0V1_EXOME Unreviewed; 741 AA.
AC A0A0D1Y0V1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KIV94131.1};
GN ORFNames=PV10_05279 {ECO:0000313|EMBL:KIV94131.1};
OS Exophiala mesophila (Black yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=212818 {ECO:0000313|EMBL:KIV94131.1, ECO:0000313|Proteomes:UP000054302};
RN [1] {ECO:0000313|EMBL:KIV94131.1, ECO:0000313|Proteomes:UP000054302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 40295 {ECO:0000313|EMBL:KIV94131.1,
RC ECO:0000313|Proteomes:UP000054302};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala mesophila CBS40295.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC {ECO:0000256|ARBA:ARBA00010609}.
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DR EMBL; KN847522; KIV94131.1; -; Genomic_DNA.
DR RefSeq; XP_016225705.1; XM_016369917.1.
DR AlphaFoldDB; A0A0D1Y0V1; -.
DR STRING; 212818.A0A0D1Y0V1; -.
DR GeneID; 27323124; -.
DR VEuPathDB; FungiDB:PV10_05279; -.
DR HOGENOM; CLU_006504_5_1_1; -.
DR OrthoDB; 449862at2759; -.
DR Proteomes; UP000054302; Unassembled WGS sequence.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd13850; CuRO_1_Abr2_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 PANTHER; PTHR11709:SF488; LACCASE-RELATED; 1.
DR PANTHER; PTHR11709; MULTI-COPPER OXIDASE; 1.
DR Pfam; PF00394; Cu-oxidase; 1.
DR Pfam; PF07731; Cu-oxidase_2; 2.
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:UP000054302};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..741
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002236804"
FT DOMAIN 35..144
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 362..465
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 556..639
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
FT DOMAIN 653..686
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
SQ SEQUENCE 741 AA; 81158 MW; EC26A4BDB7AD2626 CRC64;
MLSYPHLIVL LACSAVQNAL AASRSYELTL STGIRSPDGF AREVYLINNQ QPGPLIEAEE
GDDLEIFVQN DLPVETTIHW HGLLQRGTPD MDGVPGVTQF PIPPGGNFTY RFSTADEYGF
YWYHSHFRAY YNDALRGPLL IHPSPSRPRP FKTLAQSSSE FDMMLQVERS GTILLLSDWY
HRLSDRIYDE YFTTGAFPQC VDSLLANGRG RVQCLPQNIL EAGPGLGLES NIANDPHDPD
AMSMAMESST TSGMGMASMS MDTASMPALT TDAMSMSMRK RSDHTASPST GTAMSDMSAM
SSTLTSMATM GSSTASVGTE DQTMSTTVDM PQMTLGPRGC SPPMMFRPGF NASSLPLETC
TNTTSELFTF TADASRGWTA LHLVNAGAVS RLSVSLDGHS MFVYEADGLY VTLQEVQVLH
ISIGQRYSVM IRLDQNPGDY SFRFAAYPYG DMQQVIEGQA ILSYQNMTNN TNMTMMSRMV
SPWMLVNGSA TSGTVELDDQ TLAPFMGNTA PSGAANVTRH FAINQTDIVT WVANREPFVE
PARPIIYGSV SDGWNATTTL LTPANATVDI IMKVANDSMD TMGHPMHLHG HKFWFLGSGE
GDFPFESVTD APSSMINLQN PPYRDTIDLP PSGWAVIRCA KRLFGGSLKF TNVLRYITDN
PGAWLFHCHV QWHLVSGMAV VLVENEERMM DMVGSIQNAF NNPATNNSQA EGTSAASTLS
GNCPRQYLSF LFSLLLLFVL L
//