ID   A0A059JED5_TRIIM        Unreviewed;       652 AA.
AC   A0A059JED5;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=Laccase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=H109_02147 {ECO:0000313|EMBL:KDB26048.1};
OS   Trichophyton interdigitale (strain MR816).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=1215338 {ECO:0000313|EMBL:KDB26048.1, ECO:0000313|Proteomes:UP000024533};
RN   [1] {ECO:0000313|EMBL:KDB26048.1, ECO:0000313|Proteomes:UP000024533}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR816 {ECO:0000313|EMBL:KDB26048.1,
RC   ECO:0000313|Proteomes:UP000024533};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C.A., White T.C., Graser Y., Martinez-Rossi N., Heitman J.,
RA   Young S.K., Zeng Q., Gargeya S., Abouelleil A., Alvarado L., Chapman S.B.,
RA   Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., Martinez D., Murphy C., Pearson M.D.,
RA   Persinoti G., Poon T., Priest M., Roberts A.D., Saif S., Shea T.D.,
RA   Sykes S.N., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Trichophyton interdigitale MR816.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC       {ECO:0000256|ARBA:ARBA00010609}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KDB26048.1}.
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DR   EMBL; AOKY01000162; KDB26048.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A059JED5; -.
DR   STRING; 1215338.A0A059JED5; -.
DR   HOGENOM; CLU_006504_3_2_1; -.
DR   OMA; LIRCEYP; -.
DR   Proteomes; UP000024533; 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; cd13854; CuRO_1_MaLCC_like; 1.
DR   CDD; cd13880; CuRO_2_MaLCC_like; 1.
DR   CDD; cd13901; CuRO_3_MaLCC_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:SF71; LACCASE; 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:UP000024533};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..652
FT                   /note="Laccase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001574852"
FT   DOMAIN          116..231
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07732"
FT   DOMAIN          243..372
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00394"
FT   DOMAIN          487..607
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07731"
SQ   SEQUENCE   652 AA;  73678 MW;  ED7E2BAF42F168AC CRC64;
     MKSLNLIPRS SLKRLGLAAL YIGSALAWPE PHGAPSRNVP RDDFPLFNPL PSTDLNTRLI
     RCEYPSMKGW TYSNKKNGDW LKYVGSKPGD ITEYNIDTDN DKYVPQGITR KYHLEVTDES
     VNMDGTMFDQ AKVFNKQYPG PWIQACWGDD LEITVTNKLK HNGTAIHWHG IRMMENMFND
     GVPGVTQCPI PPGSSMTYRF KASQYGSSWY HSHYSLQYAD GLFGPMTIHG PTSAGYDKAV
     DPLLMTDHLH SSAFEEYHKE LEGKPPLMDS IILNGKGDYD QTGDLKKKYR TVLKPGKKYL
     LRLINTSVAT TFVFSIDGHK FQVVGSDFVP IEPYVTDHIA VGTGQRYHII LEGLSEEEAR
     KNGRYWVRTT PAKGCSKFAP GRGTDDRTGV IYYNKDDGVS PTTEIGAFSL DCRDEPLEKL
     VPKVKWTVPD PGLNMVGAFE KPADVQLGKW HRPGYPDTGN LVSNWEFGPS PMWINYSEPI
     IKNLDKESFP STWVVYPADN YVNDKWVYLV ITGKKLKQLS SQVAVAHPIH LHGHDFVLLQ
     QSMEPWDSTK VNLKLDNPPR RDVTLLPAGG FIVIAFKPDN PGSWLLHCHI AWHVSAGLAL
     QVLERKEDLK ALTVNNPDFD FMQENCRRWD AWHSDKTNYW NPSGHFQDDS GV
//