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Protein

Laccase-20

Gene

LAC20

Organism
Oryza sativa subsp. indica (Rice)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Lignin degradation and detoxification of lignin-derived products.By similarity

Catalytic activityi

4 benzenediol + O2 = 4 benzosemiquinone + 2 H2O.

Cofactori

Cu cationBy similarityNote: Binds 4 Cu cations per monomer.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi81 – 811Copper 1By similarity
Metal bindingi83 – 831Copper 2By similarity
Metal bindingi126 – 1261Copper 2By similarity
Metal bindingi128 – 1281Copper 3By similarity
Metal bindingi478 – 4781Copper 4Sequence Analysis
Metal bindingi481 – 4811Copper 1By similarity
Metal bindingi483 – 4831Copper 3By similarity
Metal bindingi540 – 5401Copper 3By similarity
Metal bindingi541 – 5411Copper 4Sequence Analysis
Metal bindingi542 – 5421Copper 2By similarity
Metal bindingi546 – 5461Copper 4Sequence Analysis
Metal bindingi551 – 5511Copper 4Sequence Analysis

GO - Molecular functioni

  1. copper ion binding Source: InterPro
  2. hydroquinone:oxygen oxidoreductase activity Source: UniProtKB-EC

GO - Biological processi

  1. lignin catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Lignin degradation

Keywords - Ligandi

Copper, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Laccase-20 (EC:1.10.3.2)
Alternative name(s):
Benzenediol:oxygen oxidoreductase 20
Diphenol oxidase 20
Urishiol oxidase 20
Gene namesi
Name:LAC20
ORF Names:OsI_020915
OrganismiOryza sativa subsp. indica (Rice)
Taxonomic identifieri39946 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladeEhrhartoideaeOryzeaeOryza
ProteomesiUP000007015 Componenti: Chromosome 6

Organism-specific databases

GrameneiA2Y9C2.

Subcellular locationi

GO - Cellular componenti

  1. apoplast Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Apoplast, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 580557Laccase-20PRO_0000291906Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi36 – 361N-linked (GlcNAc...)Sequence Analysis
Glycosylationi42 – 421N-linked (GlcNAc...)Sequence Analysis
Glycosylationi115 – 1151N-linked (GlcNAc...)Sequence Analysis
Glycosylationi200 – 2001N-linked (GlcNAc...)Sequence Analysis
Glycosylationi339 – 3391N-linked (GlcNAc...)Sequence Analysis
Glycosylationi392 – 3921N-linked (GlcNAc...)Sequence Analysis
Glycosylationi429 – 4291N-linked (GlcNAc...)Sequence Analysis
Glycosylationi460 – 4601N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Interactioni

Protein-protein interaction databases

STRINGi39947.LOC_Os11g42220.1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini31 – 147117Plastocyanin-like 1Add
BLAST
Domaini156 – 310155Plastocyanin-like 2Add
BLAST
Domaini419 – 561143Plastocyanin-like 3Add
BLAST

Sequence similaritiesi

Belongs to the multicopper oxidase family.Curated
Contains 3 plastocyanin-like domains.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiCOG2132.
HOGENOMiHOG000241916.
OMAiFITECPI.

Family and domain databases

Gene3Di2.60.40.420. 4 hits.
InterProiIPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR002355. Cu_oxidase_Cu_BS.
IPR008972. Cupredoxin.
[Graphical view]
PfamiPF00394. Cu-oxidase. 1 hit.
PF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 1 hit.
[Graphical view]
SUPFAMiSSF49503. SSF49503. 3 hits.
PROSITEiPS00079. MULTICOPPER_OXIDASE1. 1 hit.
PS00080. MULTICOPPER_OXIDASE2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

A2Y9C2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVASLLCTVA VAVLAVAAVG GEAGVVEHTF VVHEMNVTHL CNTTKIFVVN
60 70 80 90 100
GQLPGPTVDV TEGDTVVVHV VNKIPHGLTI HWHGVRQLRS CWADGAGFIT
110 120 130 140 150
ECPIPPGSER TYRFNVTDQV GTLWWHAHVT CLRSTINGAF IIRPRDGKYP
160 170 180 190 200
FPTPVKDVPI IIGEWWELDL VELDRRMRDG NFDDNPLSAT INGKLGDLSN
210 220 230 240 250
CSGIVEESFV LNVKHGESYL LRVINTAFFS EYYFKVAGHT FTVVGADGNY
260 270 280 290 300
LTPFKTDMVT VAPGEAIDVL MVADAPPAHY HMIVLANQPP EPDPQIPEYI
310 320 330 340 350
SRGLVRYTSA DANNNGLPVP MPIMPNQHNT MPSYYFHANL TGLMHPKHRR
360 370 380 390 400
VPMHVDERIF IILGLGTICR GRKHTCKRQR SLETIELSTM NNVSFTHPYT
410 420 430 440 450
TALLERYYDG TPEGVYTEDF PVRPPRPYNY TNPALIPPGP LEEVLEPTFK
460 470 480 490 500
ATKLKRFKYN TSVEIIFQSS TLLMSDSNPM HLHGYDVFLL AQGLGSFNAK
510 520 530 540 550
RDIRKFNYHN PQLRNTILVP RGGWAAVRFI TDNPGMWYLH CHFEFHIIMG
560 570 580
MATAFIVEDG PTPETSLPPP PPEFKRCDAS
Length:580
Mass (Da):64,907
Last modified:March 20, 2007 - v1
Checksum:i5482B2ED2D717F67
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CM000131 Genomic DNA. Translation: EAY99682.1.

Genome annotation databases

EnsemblPlantsiBGIOSGA021911-TA; BGIOSGA021911-PA; BGIOSGA021911.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CM000131 Genomic DNA. Translation: EAY99682.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi39947.LOC_Os11g42220.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiBGIOSGA021911-TA; BGIOSGA021911-PA; BGIOSGA021911.

Organism-specific databases

GrameneiA2Y9C2.

Phylogenomic databases

eggNOGiCOG2132.
HOGENOMiHOG000241916.
OMAiFITECPI.

Family and domain databases

Gene3Di2.60.40.420. 4 hits.
InterProiIPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR002355. Cu_oxidase_Cu_BS.
IPR008972. Cupredoxin.
[Graphical view]
PfamiPF00394. Cu-oxidase. 1 hit.
PF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 1 hit.
[Graphical view]
SUPFAMiSSF49503. SSF49503. 3 hits.
PROSITEiPS00079. MULTICOPPER_OXIDASE1. 1 hit.
PS00080. MULTICOPPER_OXIDASE2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The genomes of Oryza sativa: a history of duplications."
    Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.
    , Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.
    PLoS Biol. 3:266-281(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. 93-11.

Entry informationi

Entry nameiLAC20_ORYSI
AccessioniPrimary (citable) accession number: A2Y9C2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: March 20, 2007
Last modified: April 1, 2015
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.