ID A0A2R6S6R3_9APHY Unreviewed; 544 AA.
AC A0A2R6S6R3;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=laccase {ECO:0000256|ARBA:ARBA00012297};
DE EC=1.10.3.2 {ECO:0000256|ARBA:ARBA00012297};
DE Flags: Fragment;
GN ORFNames=PHLCEN_2v267 {ECO:0000313|EMBL:PSS37889.1};
OS Hermanssonia centrifuga.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Meruliaceae; Hermanssonia.
OX NCBI_TaxID=98765 {ECO:0000313|EMBL:PSS37889.1, ECO:0000313|Proteomes:UP000186601};
RN [1] {ECO:0000313|EMBL:PSS37889.1, ECO:0000313|Proteomes:UP000186601}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FBCC195 {ECO:0000313|EMBL:PSS37889.1,
RC ECO:0000313|Proteomes:UP000186601};
RA Granchi Z., Peng M., de Vries R.P., Hilden K., Makela M.R., Grigoriev I.,
RA Riley R.;
RT "Genome sequence of the basidiomycete white-rot fungus Phlebia
RT centrifuga.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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:PSS37889.1}.
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DR EMBL; MLYV02000026; PSS37889.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R6S6R3; -.
DR STRING; 98765.A0A2R6S6R3; -.
DR Proteomes; UP000186601; 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; cd13856; CuRO_1_Tv-LCC_like; 1.
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; 2.
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:UP000186601}.
FT DOMAIN 72..190
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 202..344
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 411..533
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
FT NON_TER 544
FT /evidence="ECO:0000313|EMBL:PSS37889.1"
SQ SEQUENCE 544 AA; 58945 MW; AE5F8496C4FD52F8 CRC64;
MDQHCLAQGA GINWRLYSQP NLKLTASNPL KHIQHLTENM QSLRRFFTLA AACLPVLVHG
AIGPIADLAI VNAEVNPDGF SRQAVLAGGT FPGPVITGTK GANFQINVMD QLTNETMLKT
TTVHWHGIAQ HGTNWADGTG FVTQCPIASG DSFLYDFDVP NQAGTFWYHS HLSLQYCDGL
RGAMIVYDPE DPHADLYDVD DESTIITLSD WYHAPVETIP VPPTVDSTLI NGLGRYPSGP
SSELAVIDVE AGKRYRFRLI AMACNPYYTF SIDGHNMTII EVDGVNSQPL LIDSLNIYAG
QRYSFVLEAN QPVGNYWVRS EPNAPNLSGF DNGINSAILR YVGASEAEPT SLQSASVMPL
YEYNLHPLDN PAAPGLKYTG GVDYALNLNL GFNGTPGEGG YFVINEATFN PPTVPVLLQI
LSGAQYAQEL LPAGSVYGLP MNASIELTIP PGAAPDGPHP FHLHGTTFSV VRSAGSDVYN
YDNPIRRDTV STGTAATDNV TIRWETNTPG PWFLHCHIDF HLKAGMAIVF AEDMPDIASA
NPVP
//