ID M7ZXZ0_TRIUA Unreviewed; 708 AA.
AC M7ZXZ0;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
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=TRIUR3_26891 {ECO:0000313|EMBL:EMS64521.1};
OS Triticum urartu (Red wild einkorn) (Crithodium urartu).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4572 {ECO:0000313|EMBL:EMS64521.1};
RN [1] {ECO:0000313|EMBL:EMS64521.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23535596; DOI=10.1038/nature11997;
RA Ling H.Q., Zhao S., Liu D., Wang J., Sun H., Zhang C., Fan H., Li D.,
RA Dong L., Tao Y., Gao C., Wu H., Li Y., Cui Y., Guo X., Zheng S., Wang B.,
RA Yu K., Liang Q., Yang W., Lou X., Chen J., Feng M., Jian J., Zhang X.,
RA Luo G., Jiang Y., Liu J., Wang Z., Sha Y., Zhang B., Wu H., Tang D.,
RA Shen Q., Xue P., Zou S., Wang X., Liu X., Wang F., Yang Y., An X., Dong Z.,
RA Zhang K., Zhang X., Luo M.C., Dvorak J., Tong Y., Wang J., Yang H., Li Z.,
RA Wang D., Zhang A., Wang J.;
RT "Draft genome of the wheat A-genome progenitor Triticum urartu.";
RL Nature 496:87-90(2013).
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|RuleBase:RU361119}.
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DR EMBL; KD055429; EMS64521.1; -; Genomic_DNA.
DR AlphaFoldDB; M7ZXZ0; -.
DR STRING; 4572.M7ZXZ0; -.
DR eggNOG; KOG1075; Eukaryota.
DR eggNOG; KOG1263; Eukaryota.
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:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:InterPro.
DR GO; GO:0046274; P:lignin catabolic process; IEA:UniProtKB-KW.
DR CDD; cd13875; CuRO_2_LCC_plant; 1.
DR CDD; cd06222; RNase_H_like; 1.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 2.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR InterPro; IPR001117; Cu-oxidase_2nd.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR034285; CuRO_2_LCC.
DR InterPro; IPR017761; Laccase.
DR InterPro; IPR044730; RNase_H-like_dom_plant.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR002156; RNaseH_domain.
DR InterPro; IPR036397; RNaseH_sf.
DR NCBIfam; TIGR03389; laccase; 1.
DR PANTHER; PTHR11709:SF266; LACCASE-4; 1.
DR PANTHER; PTHR11709; MULTI-COPPER OXIDASE; 1.
DR Pfam; PF00394; Cu-oxidase; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF13456; RVT_3; 1.
DR SUPFAM; SSF49503; Cupredoxins; 3.
DR SUPFAM; SSF53098; Ribonuclease H-like; 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|RuleBase:RU361119};
KW Oxidoreductase {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..25
FT /evidence="ECO:0000256|RuleBase:RU361119"
FT CHAIN 26..708
FT /note="Laccase"
FT /evidence="ECO:0000256|RuleBase:RU361119"
FT /id="PRO_5010896389"
FT DOMAIN 91..243
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 364..465
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
FT DOMAIN 588..707
FT /note="RNase H type-1"
FT /evidence="ECO:0000259|Pfam:PF13456"
SQ SEQUENCE 708 AA; 77732 MW; A905B14A3C655DD7 CRC64;
MAISSRFLAP CSVLMATLML LIVQAQSITR HYDFNVQMAN VTRLCASKSV VTRGTLWWHA
HISWLRATVY GAIVILPKLG VPYPFVAPHK EVPLLFGEWW RADTEAVVSQ ALRTGGAPNI
SDAFTINGLP GPLYNCSAKD TFKLKVKPGK TYMLRLINAA LNDELFFSVA NHTLTIVEVD
AVYVKPFTVK TLIISPGQTT NVLLTAKPFY PKANFYMSAA PYSVIRPGTF DSTTVAGILE
YHNPRSASES SFDKDLPLFR PTMPRFNDTG LVTNFTSKLR SLATPQYPAA VPQSVDKRFF
FTVGLGTRPC PVNATCQGPT NTTQFAAAIN NISLVLPSTA LLQSHFTGVS RGVYGSNFPT
TPLSQFNYTG VSPNNTNVAT GTKLLVLPFN ATVELVMQDT SILGIESHPL HLHGFNFFVV
GQGFGNYDPV NDPTRFNLVD PVERNTVGVP AGGWVAIRFL ADNPDIMHAL FTCPRAAEVW
RCLHLDGFVE EACDTDRAGS AALDYILCAP QRQTLIHEIP AQLLILVGIW YIWWERRQHV
HGEEVQTPVQ AAQSIAALAA NYLKATKKNA VVRSCRWRKP QEDFVKLNVD ASFHADDLQG
AVGAVLRDCR GGFIASSNER LEHVVDVETA EAHALRHGIL LAQRMGITKL IVESDCLEVI
NTMNNGGFTA SGSAAIYSDC LVFIIGYTSV SFVHCPRKTN YVAHVLVR
//
