ID A0A409XD95_PSICY Unreviewed; 518 AA.
AC A0A409XD95;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=laccase {ECO:0000256|ARBA:ARBA00012297};
DE EC=1.10.3.2 {ECO:0000256|ARBA:ARBA00012297};
GN ORFNames=CVT25_008549 {ECO:0000313|EMBL:PPQ88742.1};
OS Psilocybe cyanescens.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Strophariaceae; Psilocybe.
OX NCBI_TaxID=93625 {ECO:0000313|EMBL:PPQ88742.1, ECO:0000313|Proteomes:UP000283269};
RN [1] {ECO:0000313|EMBL:PPQ88742.1, ECO:0000313|Proteomes:UP000283269}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2631 {ECO:0000313|EMBL:PPQ88742.1,
RC ECO:0000313|Proteomes:UP000283269};
RX PubMed=30283667; DOI=10.1002/evl3.42;
RA Reynolds H.T., Vijayakumar V., Gluck-Thaler E., Korotkin H.B.,
RA Matheny P.B., Slot J.C.;
RT "Horizontal gene cluster transfer increased hallucinogenic mushroom
RT diversity.";
RL Evol. Lett. 2:88-101(2018).
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000256|ARBA:ARBA00001935};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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:PPQ88742.1}.
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DR EMBL; NHYD01002038; PPQ88742.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A409XD95; -.
DR STRING; 93625.A0A409XD95; -.
DR InParanoid; A0A409XD95; -.
DR OrthoDB; 64567at2759; -.
DR Proteomes; UP000283269; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd13903; CuRO_3_Tv-LCC_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; MULTI-COPPER OXIDASE; 1.
DR PANTHER; PTHR11709:SF394; PLASTOCYANIN-LIKE DOMAIN-CONTAINING PROTEIN; 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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000283269};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..518
FT /note="laccase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019405106"
FT DOMAIN 54..154
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 166..307
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 369..489
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
SQ SEQUENCE 518 AA; 55437 MW; 1DF0F2DB8BC827C3 CRC64;
MHPAIKIVAL LSASTRALAA IGPSTSLFIG NKVISPDGFN RSAVLAGGTS TGIQFPGPAI
TAQKGEAFNI NVVDQLTDTT MLITTSIHWH GFFQQNSSWA DGPVGVNQCP ISPGHSFLYQ
FSDPNQAGTY WYHSHHATQY CDGLRGPIVV YDPQDPHLNE YDIDDESTII TLADWYHTPS
PSAGTLPKSD ATLINGVGRF AGGPAVPLTV ITVEQNKRYR FRLVSMSCDP NFTFNIDGHT
MTIIEVDGVN VKPLVVDSIQ IFAGQRYSFV LNANQTPGSY WIRANPNVAN IIGFDGGVNS
AILRYAGLPA VDPTTSLSIS NPLVETNLHP LSGAAVPGVP TLGAADVNLN LNIVFNGKAF
TVNNATFQPP TLPVLLQILS KQVAPQDLLP SGSVYPLPPN SVVELSLPGG SAGSPHPIHL
HGHNFHVIRS AGSTVYNYVD PVIRDVVSIG SAGDNVTIRF ATDNAGPWIL HCHIDWHLQL
GLAVVFAEDI PTISNSQHPP AYDDLCPTYN ALPPQVFN
//
