ID   LAC2_AGABI              Reviewed;         520 AA.
AC   Q12542;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-NOV-2008, entry version 51.
DE   RecName: Full=Laccase-2;
DE            EC=1.10.3.2;
DE   AltName: Full=Laccase II;
DE   AltName: Full=Benzenediol:oxygen oxidoreductase 2;
DE   AltName: Full=Urishiol oxidase 2;
DE   AltName: Full=Diphenol oxidase 2;
DE   Flags: Precursor;
GN   Name=lcc2;
OS   Agaricus bisporus (Common mushroom).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Agaricomycetidae; Agaricales; Agaricaceae; Agaricus.
OX   NCBI_TaxID=5341;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=D649;
RX   MEDLINE=93367392; PubMed=8360614;
RA   Perry C.R., Smith M., Britnell C.H., Wood D.A., Thurston C.F.;
RT   "Identification of two laccase genes in the cultivated mushroom
RT   Agaricus bisporus.";
RL   J. Gen. Microbiol. 139:1209-1218(1993).
CC   -!- FUNCTION: Lignin degradation and detoxification of lignin-derived
CC       products (By similarity).
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   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC   -!- SIMILARITY: Contains 3 plastocyanin-like domains.
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DR   EMBL; L10663; AAA17035.1; -; mRNA.
DR   HSSP; Q12718; 1GYC.
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; 2.
DR   PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE   1: Evidence at protein level;
KW   Copper; Direct protein sequencing; Glycoprotein; Lignin degradation;
KW   Metal-binding; Oxidoreductase; Repeat; Secreted; Signal.
FT   SIGNAL        1     19
FT   CHAIN        20    520       Laccase-2.
FT                                /FTId=PRO_0000002919.
FT   DOMAIN       21    145       Plastocyanin-like 1.
FT   DOMAIN      157    305       Plastocyanin-like 2.
FT   DOMAIN      375    488       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       417    417       Copper 4; type 1 (By similarity).
FT   METAL       420    420       Copper 1; type 2 (By similarity).
FT   METAL       422    422       Copper 3; type 3 (By similarity).
FT   METAL       470    470       Copper 3; type 3 (By similarity).
FT   METAL       471    471       Copper 4; type 1 (By similarity).
FT   METAL       472    472       Copper 2; type 3 (By similarity).
FT   METAL       476    476       Copper 4; type 1 (By similarity).
FT   CARBOHYD    108    108       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    241    241       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    299    299       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    454    454       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    492    492       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   520 AA;  57823 MW;  EF100145F0A697AA CRC64;
     MRFSNAFVLV AACISSVLAD TKTFNFDLVN TRLAPDGFER DTVVINGEFP GTLVQVNKGD
     SVRIPVNNKL TSSTMRRSVS IHWHGFFQAR TSGQDGPAFV NQCPQPPNTT FTYEFSVADE
     SGTFWYHSHL STQYCDGLRG AFVVYDPEDP LGHLYDVDDE TTVITLAEWY HVLAPDINNE
     FFSSGIIPVQ DSGLINGKGR FNGGPETPFA VVNVEQGKRY RFRVIAISCR PFFTFSVDNH
     NLTFMEADSV EHDPVEIQNV DIYAAQRVSV ILNANQPVDN YWMRAPMTGG NPDRNPNLNI
     SLTLAILRYK GAPEVEPTTV NVPGHKLLDQ EMHPIAQEGP GKLGDGPPDK HITLNIAQPN
     APFFDINGIS YISPTVPVLL QILSGAKRPE DVLPSEQIFF VPKNSLIEVN IPGEGAHPFH
     LHGHNFDVVL ASNDDTFNFV NPPRRDVYPI NGGNTTFRFF TDNPGAWFLH CHIDWHLEAG
     LAIVFAEAPE DNVSGPQSQI TPQDWLDLCP EYNAIEPEFQ
//