ID A0A319EY38_9EURO Unreviewed; 600 AA.
AC A0A319EY38;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=Laccase TilA {ECO:0008006|Google:ProtNLM};
GN ORFNames=BO71DRAFT_396861 {ECO:0000313|EMBL:PYH96732.1};
OS Aspergillus ellipticus CBS 707.79.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448320 {ECO:0000313|EMBL:PYH96732.1, ECO:0000313|Proteomes:UP000247810};
RN [1] {ECO:0000313|EMBL:PYH96732.1, ECO:0000313|Proteomes:UP000247810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 707.79 {ECO:0000313|EMBL:PYH96732.1,
RC ECO:0000313|Proteomes:UP000247810};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) 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; KZ825834; PYH96732.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A319EY38; -.
DR STRING; 1448320.A0A319EY38; -.
DR Proteomes; UP000247810; 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 CDD; cd13876; CuRO_2_Abr2_like; 1.
DR CDD; cd13898; CuRO_3_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; 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:UP000247810};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..600
FT /note="Laccase TilA"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016392543"
FT DOMAIN 41..154
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 181..369
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 471..585
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
SQ SEQUENCE 600 AA; 66310 MW; D68AAC48CB0EBC6D CRC64;
MHPFRYGLLL LASVLCLVSW ANGNAVHVRS TSNTVRFNVT LTWEDWAPAG VPRKMILMNG
QFPGPTLQLR EGDDVEFLVI NNIPSNATVH FHGIEQLDTP WSDGVPGLSQ KPILPGGRFL
YKWRALQYGS YFYHAHTRGQ IEDGLYGPIY IRPDDSVEKP FHLIANKTSD LQAMQAAEEK
TTPLMLSDWR QLTSEEVWQG EEASGLDAYC ANALLINGKG SISCPGQQAY NYLASAAQKQ
ILGNQSMTDT GCISPMLASA QGDFPHNYSA IPPFMFYGCV PGNGGTEHFL VDPSAKYVSY
DLISAAGVSM ITFSIDEHSM YVYAIDGRYI EPTLVDAVTI ANGNRYSVLV KLDKPAGTYS
VRTANSGINQ ILSANATLTY DTPVQKQQRP SVASIDIHGS IVSSNYTLLN ETTIVPFPVV
VPSQDVAQTH VLKIDHYNAS YRWRMGNSSL PLALETEAPL LYYPSTADPD LTIKSLNGTW
IDLIFHVAGD LEPPHPIHKH NNKYFVIGQG TGAWNYSSVA EAMRYIPESF NLKTPQIRDT
FTTPAAVTED TWLALRYHVV NPGAWLLHCH IQVHLSGGMG LALLDGVDEW PEIPEEYRID
//
