ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q12570


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name LAC1_BOTFU
Primary accession number Q12570
Secondary accession number Q96WN0
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on December 12, 2006 (Sequence version 3)
Annotations were last modified on    November 4, 2008 (Entry version 50)
Name and origin of the protein
Protein name Laccase-1 [Precursor]
Synonyms EC 1.10.3.2
Benzenediol:oxygen oxidoreductase 1
Urishiol oxidase 1
Diphenol oxidase 1
Gene name
Name: lcc1
Synonyms: lac1
From
Botryotinia fuckeliana (Noble rot fungus) (Botrytis cinerea) [TaxID: 40559] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes; Helotiales; Sclerotiniaceae; Botryotinia.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
STRAIN=SAS56;
PubMed=11929539 [NCBI, ExPASy, EBI, Israel, Japan]
Schouten A., Wagemakers L., Stefanato F.L., van der Kaaij R.M., van Kan J.A.L.;
"Resveratrol acts as a natural profungicide and induces self-intoxication by a specific laccase.";
Mol. Microbiol. 43:883-894(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 115-561.
STRAIN=SAS56;
Cantone F.A., Staples R.C.;
"A laccase cDNA from Botrytis cinerea.";
Phytopathology 83:1383-1383(1993).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF243854; AAK77952.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U20192; AAB41823.1; ALT_SEQ; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
HSSP Q9Y780; 1HFU. [HSSP ENTRY / PDB]
ModBase Q12570.
Ontologies
GO
GO:0005576; Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0008471; Molecular function: laccase activity (inferred from electronic annotation from EC).
GO:0046274; Biological process: lignin catabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR001117; Cu-oxidase.
IPR011706; Cu-oxidase_2.
IPR011707; Cu-oxidase_3.
IPR002355; Cu_oxidase_Cu_BS.
Graphical view of domain structure.
Pfam PF00394; Cu-oxidase; 1.
PF07731; Cu-oxidase_2; 1.
PF07732; Cu-oxidase_3; 1.
Pfam graphical view of domain structure.
PROSITE PS00079; MULTICOPPER_OXIDASE1; 1.
PS00080; MULTICOPPER_OXIDASE2; 1.
BLOCKS Q12570.
ProtoNet Q12570.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Copper; Glycoprotein; Lignin degradation; Metal-binding; Oxidoreductase; Repeat; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    20  20     Potential. 
CHAIN   21   561  541     Laccase-1. PRO_0000085584
DOMAIN   68   185  118     Plastocyanin-like 1. 
DOMAIN   191   337  147     Plastocyanin-like 2. 
DOMAIN   396   525  130     Plastocyanin-like 3. 
METAL   119   119        Copper 1; type 2 (By similarity). 
METAL   121   121        Copper 2; type 3 (By similarity). 
METAL   163   163        Copper 2; type 3 (By similarity). 
METAL   165   165        Copper 3; type 3 (By similarity). 
METAL   445   445        Copper 4; type 1 (By similarity). 
METAL   448   448        Copper 1; type 2 (By similarity). 
METAL   450   450        Copper 3; type 3 (By similarity). 
METAL   504   504        Copper 3; type 3 (By similarity). 
METAL   505   505        Copper 4; type 1 (By similarity). 
METAL   506   506        Copper 2; type 3 (By similarity). 
METAL   510   510        Copper 4; type 1 (By similarity). 
CARBOHYD   71    71        N-linked (GlcNAc...) (Potential). 
CARBOHYD   87    87        N-linked (GlcNAc...) (Potential). 
CARBOHYD   114   114        N-linked (GlcNAc...) (Potential). 
CARBOHYD   226   226        N-linked (GlcNAc...) (Potential). 
CARBOHYD   284   284        N-linked (GlcNAc...) (Potential). 
CARBOHYD   327   327        N-linked (GlcNAc...) (Potential). 
CARBOHYD   391   391        N-linked (GlcNAc...) (Potential). 
CARBOHYD   398   398        N-linked (GlcNAc...) (Potential). 
CONFLICT   117   118        SI -> TM (in Ref. 2; AAB41823). 
CONFLICT   372   372        V -> I (in Ref. 2; AAB41823). 
CONFLICT   429   429        N -> K (in Ref. 2; AAB41823). 
CONFLICT   481   481        M -> L (in Ref. 2; AAB41823). 
CONFLICT   484   484        P -> S (in Ref. 2; AAB41823). 
CONFLICT   511   511        A -> V (in Ref. 2; AAB41823). 
CONFLICT   547   547        A -> G (in Ref. 2; AAB41823). 
Sequence information
Length: 561 AA [This is the length of the unprocessed precursor] Molecular weight: 60337 Da [This is the MW of the unprocessed precursor] CRC64: 7F366B289EF73C23 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKNSFFSSLA KFASLSLAFA LPTAEVIPSA LEERQSCANT ATTRSCWGQY SASTNSYTTV 

        70         80         90        100        110        120 
PKTGYWLVVQ NTTLSADGVS RPTLNFNGTI PGPQITADWG DDVIVHVTNK LTSNGTSIHW 

       130        140        150        160        170        180 
HGIRQLNNAQ YDGVPGITQC PIAPGGTLTY KFHADNYGSS WYHSHFILQY GDGLFGPLVI 

       190        200        210        220        230        240 
NGPATANYDV DLGMLFLNDW NHVPVQSLWD KAKTGAPPTL LTGLMNGTNT YNGAGKKFQT 

       250        260        270        280        290        300 
TFTPGLKYRI RVVNTAVDGH FQFSIDGHSF QVIAMDFVPI VPYNATSILV SIAQRYDIIV 

       310        320        330        340        350        360 
TANAAVGNYW IRAGWQTACS GNTNAANITG ILRYTGSSST ADPTTTSTVT ASTSCLDEPL 

       370        380        390        400        410        420 
ASLVPFVPIN PVASSIMKTT LTTGGGQWLF NGSSLLLNWT DPTLLTVLNS GNIWPTEYNV 

       430        440        450        460        470        480 
IPIESTTANK GWAVLAISGP NGPNHPIHLH GHDFWTLSQG TGAYTATTAL NLVNPPRRDV 

       490        500        510        520        530        540 
MTLPTGGHLV IAFQIDNPGS WLMHCHIAWH ASEGLALQFV ESESSILPTI GTADVSTFQN 

       550        560 
TCAAWKAWTP TEPFPQDDSG I 

Q12570 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!