ID A0A2P8AJ46_9PEZI Unreviewed; 619 AA.
AC A0A2P8AJ46;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=laccase {ECO:0000256|ARBA:ARBA00012297};
DE EC=1.10.3.2 {ECO:0000256|ARBA:ARBA00012297};
GN ORFNames=B9Z65_604 {ECO:0000313|EMBL:PSK60454.1};
OS Elsinoe australis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Myriangiales; Elsinoaceae; Elsinoe.
OX NCBI_TaxID=40998 {ECO:0000313|EMBL:PSK60454.1, ECO:0000313|Proteomes:UP000243723};
RN [1] {ECO:0000313|EMBL:PSK60454.1, ECO:0000313|Proteomes:UP000243723}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NL1 {ECO:0000313|EMBL:PSK60454.1,
RC ECO:0000313|Proteomes:UP000243723};
RA Cheng Q.;
RT "Draft genome sequence of Elsinoe australis.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000256|ARBA:ARBA00001935};
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:PSK60454.1}.
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DR EMBL; NHZQ01000003; PSK60454.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P8AJ46; -.
DR STRING; 40998.A0A2P8AJ46; -.
DR Proteomes; UP000243723; 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:SF87; 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:UP000243723};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..619
FT /note="laccase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015119891"
FT DOMAIN 106..221
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 235..379
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 460..586
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
SQ SEQUENCE 619 AA; 67223 MW; 7C435195CA4A363C CRC64;
MYTSTLLAGC LSLLATCASA QGGAGHKYLH GADGMGRMVR QHKQIVKKQA PSLVADGAAS
PTLVADGACT HGPRNRACWR DGFSVATDFD QKHPTNGKTR TYNFEISEAP CNPDGNGEVM
CQLVNGQYPG PVLWAEWGDY LSINVKNSLP ANGTSLHWHG IRQLNSPGSD GVNGITECPI
APGDSFTYEF QATQFGTSWY HSHFSVQYGA GVAGPIVIDG PATANYDIDL GSFWVTDWYY
EGAWNLNVQA LQALQQGGGP SPADTILVNG TGKSANGGSY AQVTLQPGKK HRLRLINPSV
DNYIRVKLDN HPLTIISADF IPTTPMPNND WILFGPGQRY DVVFGANATA GSYWFRAEVA
GDCLSSNNGK GRAVFTYEGQ QPTEPADSNE APPQDGCNEL LPVPFWKQPV DSATFDNQVE
DLTVALTQAS FTTNGKNLVA WALNFTAMNI DWGYPTLQYV MDGNNSFPKS YDVIEIPNQG
TWTYWIVQTL QNTLGPDAIA APPPPHPIHL HGHDFFVIGH GNGQFDRASA ALNFNNPPRR
DTATLPSKGW LALAFPANNP GTWLMHCHIA VHIGQGLGVQ FLESKNQIVM PDQGKFKSQC
DNWNKFQAGM PYKKYDSGL
//
