ID   LAC16_ORYSJ             Reviewed;         467 AA.
AC   Q7XE50;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   04-NOV-2008, entry version 37.
DE   RecName: Full=Putative laccase-16;
DE            EC=1.10.3.2;
DE   AltName: Full=Benzenediol:oxygen oxidoreductase 16;
DE   AltName: Full=Urishiol oxidase 16;
DE   AltName: Full=Diphenol oxidase 16;
GN   Name=LAC16; OrderedLocusNames=Os10g0437400, LOC_Os10g30140;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade;
OC   Ehrhartoideae; Oryzeae; Oryza.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   MEDLINE=22677351; PubMed=12791992; DOI=10.1126/science.1083523;
RA   Yu Y., Rambo T., Currie J., Saski C., Kim H.-R., Collura K.,
RA   Thompson S., Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S.,
RA   Henry D., Oates R., Palmer M., Pries G., Gibson J., Anderson H.,
RA   Paradkar M., Crane L., Dale J., Carver M.B., Wood T., Frisch D.,
RA   Engler F., Soderlund C., Palmer L.E., Teytelman L., Nascimento L.,
RA   De la Bastide M., Spiegel L., Ware D., O'Shaughnessy A., Dike S.,
RA   Dedhia N., Preston R., Huang E., Ferraro K., Kuit K., Miller B.,
RA   Zutavern T., Katzenberger F., Muller S., Balija V., Martienssen R.A.,
RA   Stein L., Minx P., Johnson D., Cordum H., Mardis E., Cheng Z.,
RA   Jiang J., Wilson R., McCombie W.R., Wing R.A., Yuan Q., Ouyang S.,
RA   Liu J., Jones K.M., Gansberger K., Moffat K., Hill J., Tsitrin T.,
RA   Overton L., Bera J., Kim M., Jin S., Tallon L., Ciecko A., Pai G.,
RA   Van Aken S., Utterback T., Reidmuller S., Bormann J., Feldblyum T.,
RA   Hsiao J., Zismann V., Blunt S., de Vazeille A.R., Shaffer T., Koo H.,
RA   Suh B., Yang Q., Haas B., Peterson J., Pertea M., Volfovsky N.,
RA   Wortman J., White O., Salzberg S.L., Fraser C.M., Buell C.R.,
RA   Messing J., Song R., Fuks G., Llaca V., Kovchak S., Young S.,
RA   Bowers J.E., Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A.;
RT   "In-depth view of structure, activity, and evolution of rice
RT   chromosome 10.";
RL   Science 300:1566-1569(2003).
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, extracellular space, apoplast
CC       (Potential).
CC   -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC   -!- SIMILARITY: Contains 3 plastocyanin-like domains.
CC   -!- CAUTION: Lacks the signal peptide, which is one of the conserved
CC       features of the laccases.
CC   -!- CAUTION: Could be the product of a pseudogene.
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DR   EMBL; DP000086; AAP53940.1; -; Genomic_DNA.
DR   HSSP; P37064; 1AOZ.
DR   NMPDR; fig|39947.1.peg.13165; -.
DR   Gramene; Q7XE50; -.
DR   GO; GO:0048046; C:apoplast; IEA:UniProtKB-KW.
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   InterPro; IPR002035; VWF_A.
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   PRINTS; PR00453; VWFADOMAIN.
DR   PROSITE; PS00079; MULTICOPPER_OXIDASE1; 1.
DR   PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE   5: Uncertain;
KW   Apoplast; Copper; Lignin degradation; Metal-binding; Oxidoreductase;
KW   Repeat; Secreted.
FT   CHAIN         1    467       Putative laccase-16.
FT                                /FTId=PRO_0000291900.
FT   DOMAIN        7     88       Plastocyanin-like 1.
FT   DOMAIN       98    225       Plastocyanin-like 2.
FT   DOMAIN      318    451       Plastocyanin-like 3.
FT   METAL        22     22       Copper 1 (By similarity).
FT   METAL        24     24       Copper 2 (By similarity).
FT   METAL        67     67       Copper 2 (By similarity).
FT   METAL        69     69       Copper 3 (By similarity).
FT   METAL       368    368       Copper 4 (By similarity).
FT   METAL       371    371       Copper 1 (By similarity).
FT   METAL       373    373       Copper 3 (By similarity).
FT   METAL       430    430       Copper 3 (By similarity).
FT   METAL       431    431       Copper 4 (By similarity).
FT   METAL       432    432       Copper 2 (By similarity).
FT   METAL       436    436       Copper 4 (By similarity).
FT   METAL       441    441       Copper 4 (By similarity).
SQ   SEQUENCE   467 AA;  52187 MW;  93F9411A5D6E1C21 CRC64;
     MDRKGIVLGS KLAVFSMILL WHRHGVDQPR NPWSDGPEFI TQCPIRPCGN FTYQVILFEE
     EGTLWWHAHS DFDRATVHGA IVIHPKHGTT FPFNKPDKEI PIILSEWWND DVENVLDEAK
     RTGGDQGNTY LLRVINTGLT NDMFFAVAGH CLTVVSIDAR YTKPLTVDYI MIAPGQTMDV
     LLEANRTLGS NSRYYMAARA FITLPVDTIP FNNSTATAIV EYTDSPTARP PGPPEFPLLL
     PAIKDEDAAM AFVDERMLID IDVNFLPCDT TNATNKLCKG PQGNQFAASL NNVSFESPAI
     DVLDAYYYGS GRGVYEEDFP NKPVNAFVNP TGDNGGRPLL TKRGTKVKVV EYGTVVEVVF
     QDLSSENHPM HLHGFAFYVV GRGSGTFDER RDPATYNLVD PPFQNTVSVP KSSWAAIRFR
     ADNPGVWFMH CHFDRHVVWG MDTVFIVKDG KTPQAQMLPR PPNMPEC
//