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Database: UniProt
Entry: A0A368RD50_SETIT
LinkDB: A0A368RD50_SETIT
Original site: A0A368RD50_SETIT 
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
//
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