ID A0A2A9NIK4_9AGAR Unreviewed; 524 AA.
AC A0A2A9NIK4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=laccase {ECO:0000256|ARBA:ARBA00012297};
DE EC=1.10.3.2 {ECO:0000256|ARBA:ARBA00012297};
GN ORFNames=AMATHDRAFT_67578 {ECO:0000313|EMBL:PFH47532.1};
OS Amanita thiersii Skay4041.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Pluteineae; Amanitaceae; Amanita.
OX NCBI_TaxID=703135 {ECO:0000313|EMBL:PFH47532.1, ECO:0000313|Proteomes:UP000242287};
RN [1] {ECO:0000313|EMBL:PFH47532.1, ECO:0000313|Proteomes:UP000242287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SKay4041 {ECO:0000313|EMBL:PFH47532.1,
RC ECO:0000313|Proteomes:UP000242287};
RG DOE Joint Genome Institute;
RA Hess J., Skrede I., Wolfe B., LaButti K., Ohm R.A., Grigoriev I.V.,
RA Pringle A.;
RT "Transposable element dynamics among asymbiotic and ectomycorrhizal Amanita
RT fungi.";
RL Submitted (FEB-2014) 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}.
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DR EMBL; KZ302106; PFH47532.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A9NIK4; -.
DR STRING; 703135.A0A2A9NIK4; -.
DR OrthoDB; 64567at2759; -.
DR Proteomes; UP000242287; 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; 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:UP000242287};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..524
FT /note="laccase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011976019"
FT DOMAIN 30..145
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 157..305
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 363..487
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
SQ SEQUENCE 524 AA; 57634 MW; 840BBF7940BEB8B4 CRC64;
MLGFLLAPFA LVAPVLCATR NYELTLTNEF ISPNGINRSA VLANKQLPGP LITAHKNDEL
RVKVINRLTD KTMAQGTSIH WHGLLQHRSA TQDGAAWVTQ CPIAAGDDFL YHFNVEQTGT
YWYHSHITTQ YCDGLRGPIV VYDENDPLRH LYDVDDENTV ITLGDWLDIP SPQAFVTLVN
PETTLINGRG RHPNSNSSPP PPLSIINVKP NTRYRFRLVN VACVAGFDFS IDGHKMNVIE
TDGTETIPSR AVDGITIWAG QRVSVIVKTD QKVDNYWIRA KPIIVPSNPS NETGVNAAIL
RYQGASNADP TTSQSGSNFA HEEDLIPLKP SFDIAGKPDV KLNFNIGLNA DATAFAMNGH
TFTPPTVPVL LQILSGKADP LDLMPKDSVI VLPRNKLIEI TIPGGSIQAP HPFHLHGHKF
AVVRSAGSTR VNTLLPPFRD VVNTGAELSD NVTIRFRTDN PGPWIMHCHV DFHLEAGLAV
VFAEDPKGQV HGNESVEVDK AWKDLCPKWD STKEGKQFSI SDLF
//
