ID   LAC1_THACU              Reviewed;         576 AA.
AC   P56193;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-NOV-2008, entry version 55.
DE   RecName: Full=Laccase-1;
DE            EC=1.10.3.2;
DE   AltName: Full=Benzenediol:oxygen oxidoreductase 1;
DE   AltName: Full=Urishiol oxidase 1;
DE   AltName: Full=Diphenol oxidase 1;
DE   Flags: Precursor;
GN   Name=LCC1;
OS   Thanatephorus cucumeris (Black scurf of potato) (Rhizoctonia solani).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Cantharellales; Ceratobasidiaceae; Thanatephorus.
OX   NCBI_TaxID=107832;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=R22;
RX   MEDLINE=96171523; PubMed=8598061; DOI=10.1007/s002940050061;
RA   Wahleithner J.A., Xu F., Brown K.M., Brown S.H., Golightly E.J.,
RA   Halkier T., Kauppinen S., Pederson A., Schneider P.;
RT   "The identification and characterization of four laccases from the
RT   plant pathogenic fungus Rhizoctonia solani.";
RL   Curr. Genet. 29:395-403(1996).
CC   -!- FUNCTION: Lignin degradation and detoxification of lignin-derived
CC       products (Probable).
CC   -!- CATALYTIC ACTIVITY: 4 benzenediol + O(2) = 4 benzosemiquinone + 2
CC       H(2)O.
CC   -!- COFACTOR: Binds 4 copper ions per monomer (By similarity).
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6;
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: In mycelia, at a lower level than LCC4.
CC   -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC   -!- SIMILARITY: Contains 3 plastocyanin-like domains.
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DR   EMBL; Z54275; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; S68117; S68117.
DR   HSSP; Q9Y780; 1HFU.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0008471; F:laccase activity; IEA:EC.
DR   GO; GO:0046274; P:lignin catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001117; Cu-oxidase.
DR   InterPro; IPR011706; Cu-oxidase_2.
DR   InterPro; IPR011707; Cu-oxidase_3.
DR   InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR   InterPro; IPR008972; Cupredoxin.
DR   Gene3D; G3DSA:2.60.40.420; Cupredoxin; 3.
DR   Pfam; PF00394; Cu-oxidase; 1.
DR   Pfam; PF07731; Cu-oxidase_2; 1.
DR   Pfam; PF07732; Cu-oxidase_3; 1.
DR   PROSITE; PS00079; MULTICOPPER_OXIDASE1; 1.
DR   PROSITE; PS00080; MULTICOPPER_OXIDASE2; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Copper; Glycoprotein; Lignin degradation; Metal-binding;
KW   Oxidoreductase; Repeat; Secreted; Signal.
FT   SIGNAL        1     19       Potential.
FT   CHAIN        20    576       Laccase-1.
FT                                /FTId=PRO_0000002935.
FT   DOMAIN       21    145       Plastocyanin-like 1.
FT   DOMAIN      157    304       Plastocyanin-like 2.
FT   DOMAIN      376    576       Plastocyanin-like 3.
FT   METAL        82     82       Copper 1; type 2 (By similarity).
FT   METAL        84     84       Copper 2; type 3 (By similarity).
FT   METAL       127    127       Copper 2; type 3 (By similarity).
FT   METAL       129    129       Copper 3; type 3 (By similarity).
FT   METAL       471    471       Copper 4; type 1 (By similarity).
FT   METAL       474    474       Copper 1; type 2 (By similarity).
FT   METAL       476    476       Copper 3; type 3 (By similarity).
FT   METAL       523    523       Copper 3; type 3 (By similarity).
FT   METAL       524    524       Copper 4; type 1 (By similarity).
FT   METAL       525    525       Copper 2; type 3 (By similarity).
FT   METAL       529    529       Copper 4; type 1 (By similarity).
FT   CARBOHYD     41     41       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    182    182       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    228    228       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    294    294       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    368    368       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   576 AA;  64377 MW;  CE5E32918038AE48 CRC64;
     MARTTFLVSV SLFVSAVLAR TVEYGLKISD GEIAPDGVKR NATLVNGGYP GPLIFANKGD
     TLKVKVQNKL TNPEMYRTTS IHWHGLLQHR NADDDGPSFV TQCPIVPRES YTYTIPLDDQ
     TGTYWYHSHL SSQYVDGLRG PLVIYDPKDP HRRLYDVDDE KTVLIIGDWY HESSKAILAS
     GNITRQRPVS ATINGKGRFD PDNTPANPDT LYTLKVKRGK RYRLRVINSS EIASFRFSVE
     GHKVTVIAAD GVSTKPYQVD AFDILAGQRI DCVVEANQEP DTYWINAPLT NVPNKTAQAL
     LVYEEDRRPY HPPKGPYRKW SVSEAIIKYW NHKHKHGRGL LSGHGGLKAR MIEGSHHLHS
     RSVVKRQNET TTVVMDESKL VPLEYPGAAC GSKPADLVLD LTFGLNFATG HWMINGIPYE
     SPKIPTLLKI LTDEDGVTES DFTKEEHTVI LPKNKCIEFN IKGNSGIPIT HPVHLHGHTW
     DVVQFGNNPP NYVNPPRRDV VGSTDAGVRI QFKTDNPGPW FLHCHIDWHL EEGFAMVFAE
     APEAVKGGPK SVAVDSQWEG LCGKYDNWLK SNPGQL
//