ID   Q50H78_9PEZI            Unreviewed;       594 AA.
AC   Q50H78;
DT   07-JUN-2005, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2005, sequence version 1.
DT   14-DEC-2022, entry version 61.
DE   SubName: Full=Laccase I {ECO:0000313|EMBL:AAY33970.1};
OS   Neohortaea acidophila.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Neohortaea.
OX   NCBI_TaxID=245834 {ECO:0000313|EMBL:AAY33970.1};
RN   [1] {ECO:0000313|EMBL:AAY33970.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=15796994; DOI=10.1016/j.femsle.2005.03.007;
RA   Tetsch L., Bend J., Janssen M., Holker U.;
RT   "Evidence for functional laccases in the acidophilic ascomycete Hortaea
RT   acidophila and isolation of laccase-specific gene fragments.";
RL   FEMS Microbiol. Lett. 245:161-168(2005).
RN   [2] {ECO:0000313|EMBL:AAY33970.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Tetsch L., Janssen M., Hoelker U.;
RT   "In search of the laccase genes of Hortaea acidophila.";
RL   Submitted (MAY-2005) 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; AY351908; AAY33970.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q50H78; -.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.420; -; 3.
DR   InterPro; IPR001117; Cu-oxidase.
DR   InterPro; IPR011706; Cu-oxidase_C.
DR   InterPro; IPR045087; Cu-oxidase_fam.
DR   InterPro; IPR011707; Cu-oxidase_N.
DR   InterPro; IPR033138; Cu_oxidase_CS.
DR   InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR   InterPro; IPR008972; Cupredoxin.
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   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..594
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004248245"
FT   DOMAIN          95..209
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07732"
FT   DOMAIN          224..337
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00394"
FT   DOMAIN          438..567
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07731"
SQ   SEQUENCE   594 AA;  64494 MW;  2655A79B9C447C9B CRC64;
     MAAHLLLGAL MLGSALAISY HKPAWIPLGD SLSPRLGQDV TNGNGVLGTL DAPRLAKFLP
     DTHASRHRRK GYSPTDIGIG DVPVTGVTRY YNFTITEQNI APDGVVRSGM VVNGGYPGPT
     IEANWGDYFE ISVVNALPNE GTSIHWHGLI QHETPYMDGV PGIVQCPIAP GGNFTYRFRA
     DLYGTSFYHS HYSAQYTGGI YGAMIIHGPT ENAQYDEDIG PVLLNDWYHL PPPQSNNNLI
     NGKMNVSRQR CTPNAGISKF TFQSGKTYRL RLINAGAEGM QKFSIDGHTM TVIANDFVPL
     KPYQTDVVTL GIGQRSDIIV TATGKAGQSY WMRSDLGLNA LSNPAGCTNN DGVSPLALAA
     IYYEGADTNS VPTTNSTVPE SSIQSCMNDP LNMTVPYYSL TPSTTPAMSQ NIDITFASNG
     TNYLFYMNNS TFRADYNDPI LLEAKLGQTV FPAEENVIST GNASSVRFVL YNYAFTGAHP
     MHMHGHNYWV LAEGYGTWDG TVTNAGNPQR RDVQLLPPAQ VNADLVVTSP SYIVLQFNAD
     NPGVWPLHCH IAWHVSAGLY VSILENPTAI KSMHIPKPAA WTGKDVPDQI DSGL
//