ID A0A368RD50_SETIT Unreviewed; 577 AA.
AC A0A368RD50;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Laccase {ECO:0000256|ARBA:ARBA00012297, ECO:0000256|RuleBase:RU361119};
DE EC=1.10.3.2 {ECO:0000256|ARBA:ARBA00012297, ECO:0000256|RuleBase:RU361119};
DE AltName: Full=Benzenediol:oxygen oxidoreductase {ECO:0000256|RuleBase:RU361119};
DE AltName: Full=Diphenol oxidase {ECO:0000256|RuleBase:RU361119};
DE AltName: Full=Urishiol oxidase {ECO:0000256|RuleBase:RU361119};
GN ORFNames=SETIT_5G382700v2 {ECO:0000313|EMBL:RCV28147.1};
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:RCV28147.1};
RN [1] {ECO:0000313|EMBL:RCV28147.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Yugu1 {ECO:0000313|EMBL:RCV28147.1};
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:RCV28147.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Yugu1 {ECO:0000313|EMBL:RCV28147.1};
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 ECO:0000256|RuleBase:RU361119}.
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 ECO:0000256|RuleBase:RU361119};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000256|RuleBase:RU361119};
CC Note=Binds 4 Cu cations per monomer. {ECO:0000256|RuleBase:RU361119};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000256|ARBA:ARBA00004271, ECO:0000256|RuleBase:RU361119}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC {ECO:0000256|ARBA:ARBA00010609, ECO:0000256|RuleBase:RU361119}.
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DR EMBL; CM003532; RCV28147.1; -; Genomic_DNA.
DR RefSeq; XP_004970586.2; XM_004970529.2.
DR AlphaFoldDB; A0A368RD50; -.
DR SMR; A0A368RD50; -.
DR GeneID; 101780834; -.
DR KEGG; sita:101780834; -.
DR OrthoDB; 449862at2759; -.
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 CDD; cd13897; CuRO_3_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; IPR033138; Cu_oxidase_CS.
DR InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR034288; CuRO_1_LCC.
DR InterPro; IPR034285; CuRO_2_LCC.
DR InterPro; IPR034289; CuRO_3_LCC.
DR InterPro; IPR017761; Laccase.
DR NCBIfam; TIGR03389; laccase; 1.
DR PANTHER; PTHR11709:SF339; LACCASE-6; 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.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 1.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 3: Inferred from homology;
KW Apoplast {ECO:0000256|ARBA:ARBA00022523, ECO:0000256|RuleBase:RU361119};
KW Copper {ECO:0000256|RuleBase:RU361119};
KW Lignin degradation {ECO:0000256|ARBA:ARBA00023185,
KW ECO:0000256|RuleBase:RU361119};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361119};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361119};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU361119};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU361119};
KW Signal {ECO:0000256|RuleBase:RU361119}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|RuleBase:RU361119"
FT CHAIN 27..577
FT /note="Laccase"
FT /evidence="ECO:0000256|RuleBase:RU361119"
FT /id="PRO_5016485301"
FT DOMAIN 52..150
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 164..290
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 419..559
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
SQ SEQUENCE 577 AA; 62330 MW; F8063BCA2FA661DB CRC64;
MHFGIMPGSW LILVLAVSSA AVLAHAATVE HTFNVATLCW PRISQPGDVS ITAVDGVPGP
VIEAYEGDTV VVHVINDSPH NVTIHWHGVI QRGTPWADGP EMVTQCPIRP GTRYTYRFNV
SGQEGTLWWH AHASFLRATV HGALIIRPRA GAGAYPFPTP DGEAVVLLGE WWNDENAISS
NVIADAYTIN GKPGDLYAGE TTANRSAKFE VTRNSTYLLR IINAALNTAF FFKVAGHTFT
VVAADASYTT SYETDVIVIA PGQTVDALMA ADASPGRYYM AISSYQSAFP PPPGGFNGNV
TTSLVEYAGA AAPGGGQQAP ALPDTPEPTD TDTANRFYTG LTALVRPGMP RVPLTVDTRM
FVTVGLGLRY PPCEPTQTTP CQPIPVATMN NQSFVLPRAM SMLDARYRNT PDGVYTRDFP
DRPPVEFDYT NRTEMVVGGA AAALLFPGTP ATKVRKLEYN ATVEMVLQNT ALVGRESHPM
HLHGFDFFVL AQGFGNYDDA TGSQQFNLRN PQERNTIAVP TGGWAVIRFV ADNPGMWFMH
CHIDSHLSIG LGMVFEVEDG PTPDTKLPPP PADLPQC
//