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Database: UniProt
Entry: A0A368SA93_SETIT
LinkDB: A0A368SA93_SETIT
Original site: A0A368SA93_SETIT 
ID   A0A368SA93_SETIT        Unreviewed;       592 AA.
AC   A0A368SA93;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=laccase {ECO:0000256|ARBA:ARBA00012297};
DE            EC=1.10.3.2 {ECO:0000256|ARBA:ARBA00012297};
GN   ORFNames=SETIT_8G211500v2 {ECO:0000313|EMBL:RCV39291.1};
OS   Setaria italica (Foxtail millet) (Panicum italicum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Panicodae; Paniceae; Cenchrinae; Setaria.
OX   NCBI_TaxID=4555 {ECO:0000313|EMBL:RCV39291.1};
RN   [1] {ECO:0000313|EMBL:RCV39291.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Yugu1 {ECO:0000313|EMBL:RCV39291.1};
RX   PubMed=22580951; DOI=10.1038/nbt.2196;
RA   Bennetzen J.L., Schmutz J., Wang H., Percifield R., Hawkins J.,
RA   Pontaroli A.C., Estep M., Feng L., Vaughn J.N., Grimwood J., Jenkins J.,
RA   Barry K., Lindquist E., Hellsten U., Deshpande S., Wang X., Wu X.,
RA   Mitros T., Triplett J., Yang X., Ye C.Y., Mauro-Herrera M., Wang L., Li P.,
RA   Sharma M., Sharma R., Ronald P.C., Panaud O., Kellogg E.A., Brutnell T.P.,
RA   Doust A.N., Tuskan G.A., Rokhsar D., Devos K.M.;
RT   "Reference genome sequence of the model plant Setaria.";
RL   Nat. Biotechnol. 30:555-561(2012).
RN   [2] {ECO:0000313|EMBL:RCV39291.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Yugu1 {ECO:0000313|EMBL:RCV39291.1};
RA   Noorani M.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Lignin degradation and detoxification of lignin-derived
CC       products. {ECO:0000256|ARBA:ARBA00002075}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4 hydroquinone + O2 = 4 benzosemiquinone + 2 H2O;
CC         Xref=Rhea:RHEA:11276, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:17594, ChEBI:CHEBI:17977; EC=1.10.3.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00000349};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|ARBA:ARBA00001935};
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC       {ECO:0000256|ARBA:ARBA00004271}.
CC   -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC       {ECO:0000256|ARBA:ARBA00010609}.
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DR   EMBL; CM003535; RCV39291.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A368SA93; -.
DR   GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0052716; F:hydroquinone:oxygen oxidoreductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046274; P:lignin catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd13849; CuRO_1_LCC_plant; 1.
DR   CDD; cd13875; CuRO_2_LCC_plant; 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; IPR008972; Cupredoxin.
DR   InterPro; IPR034288; CuRO_1_LCC.
DR   InterPro; IPR034285; CuRO_2_LCC.
DR   PANTHER; PTHR11709:SF521; LACCASE-15; 1.
DR   PANTHER; PTHR11709; MULTI-COPPER OXIDASE; 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.
PE   3: Inferred from homology;
KW   Apoplast {ECO:0000256|ARBA:ARBA00022523};
KW   Lignin degradation {ECO:0000256|ARBA:ARBA00023185};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           33..592
FT                   /note="laccase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016959755"
FT   DOMAIN          41..154
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07732"
FT   DOMAIN          168..301
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00394"
FT   DOMAIN          456..570
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07731"
FT   REGION          329..352
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   592 AA;  65018 MW;  49E0D50968A57E99 CRC64;
     MVSMESRSLL AAAPALAVAI IFLSTTAPLA RAASVEHTFV VNQTKMTRLC KETLVTVVNG
     QLPGPTIEVT EGDSVTVHVV NRSPYNITIH WHGVKQFRNC WADGVPMVTQ YPIQPNKDFT
     YRFNVVGQEG TLWWHAHVPG LRATLHGAFI IRPRLGAESY PFPKPHKEIP VIIGDWWEED
     LAEMARNMTK GIFLSYASAS TVNGLVGDLF NCSGVTKEGY VLDVEPGKTY LLRIINAGLF
     SEFYLKIAGH KFTVVAADAN YVSPFTTDVI AIAAGETVDA LLIANAAPGR YYMVALPNQA
     PLPDTQTPEY ATRGMVRYKV SHSTCTSSTT VSSCQGTEEE EKGYRGTSGD APIVPKMPDI
     HDTITSFYFH GNLTSLHHQG QLPVQQQVDE RLFIVLGLGT ICKKGQFCKR GSSDEDLLVA
     TMNNASFQHP TAIPTPLLEA HYYHTGLINA TTQELPKGPP KLFNFTDEAL IPFGPKEMQL
     EPTYKATLVR RFRHGAVVEI VFQSTAILQG DSNPMHLHGH DMIVLAQGLG NYDPAKAVAT
     YNLVNPLIKN TVLVPNLGWI AIRFVANNPG GHGSCIATMS FIYQWAWQQS LL
//
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