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UniProtKB - O59896 (LAC1_PYCCI)
Protein
Laccase
Gene
LCC3-1
Organism
Pycnoporus cinnabarinus (Cinnabar-red polypore) (Trametes cinnabarina)
Status
Functioni
Lignin degradation and detoxification of lignin-derived products (By similarity).
Cleaves the C-C and C-O bonds of some phenolic lignin model compounds (such as O- and P-quinols, aminophenols and phenylenediamine) (PubMed:8919775).
May also be involved in synthesis of phenoxazinone pigments (PubMed:9572949).
1 PublicationBy similarity1 PublicationCatalytic activityi
- EC:1.10.3.2By similarity
Cofactori
Cu cationBy similarityNote: Binds 4 Cu cations per monomer.By similarity
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 85 | Copper 1; type 2By similarity | 1 | |
Metal bindingi | 87 | Copper 2; type 3By similarity | 1 | |
Metal bindingi | 130 | Copper 2; type 3By similarity | 1 | |
Metal bindingi | 132 | Copper 3; type 3By similarity | 1 | |
Metal bindingi | 416 | Copper 4; type 1By similarity | 1 | |
Metal bindingi | 419 | Copper 1; type 2By similarity | 1 | |
Metal bindingi | 421 | Copper 3; type 3By similarity | 1 | |
Metal bindingi | 471 | Copper 3; type 3By similarity | 1 | |
Metal bindingi | 472 | Copper 4; type 1By similarity | 1 | |
Metal bindingi | 473 | Copper 2; type 3By similarity | 1 | |
Metal bindingi | 477 | Copper 4; type 1By similarity | 1 |
GO - Molecular functioni
- copper ion binding Source: InterPro
- hydroquinone:oxygen oxidoreductase activity Source: UniProtKB-EC
GO - Biological processi
- lignin catabolic process Source: UniProtKB-KW
Keywordsi
Molecular function | Oxidoreductase |
Biological process | Lignin degradation |
Ligand | Copper, Metal-binding |
Protein family/group databases
CAZyi | AA1, Auxiliary Activities 1 |
Names & Taxonomyi
Protein namesi | Recommended name: Laccase (EC:1.10.3.2By similarity)Alternative name(s): Benzenediol:oxygen oxidoreductase Diphenol oxidase Ligninolytic phenoloxidase Urishiol oxidase |
Gene namesi | Name:LCC3-1 Synonyms:LAC3, LCC1 |
Organismi | Pycnoporus cinnabarinus (Cinnabar-red polypore) (Trametes cinnabarina) |
Taxonomic identifieri | 5643 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Agaricomycetes › Polyporales › Polyporaceae › Trametes |
Subcellular locationi
Extracellular region or secreted
- Secreted By similarity
Extracellular region or secreted
- extracellular region Source: UniProtKB-SubCell
Keywords - Cellular componenti
SecretedPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 21 | 1 PublicationAdd BLAST | 21 | |
ChainiPRO_0000002934 | 22 – 518 | LaccaseAdd BLAST | 497 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 72 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 75 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 106 ↔ 507 | By similarity | ||
Disulfide bondi | 138 ↔ 226 | By similarity | ||
Glycosylationi | 229 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 354 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 362 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 398 | N-linked (GlcNAc...) asparagineSequence analysis | 1 |
Keywords - PTMi
Disulfide bond, GlycoproteinExpressioni
Inductioni
By lignosulfonate, veratryl alcohol and 2,5-xylidine.1 Publication
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 23 – 148 | Plastocyanin-like 1Add BLAST | 126 | |
Domaini | 160 – 302 | Plastocyanin-like 2Add BLAST | 143 | |
Domaini | 369 – 489 | Plastocyanin-like 3Add BLAST | 121 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 308 – 330 | DisorderedSequence analysisAdd BLAST | 23 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 308 – 323 | Polar residuesSequence analysisAdd BLAST | 16 |
Sequence similaritiesi
Belongs to the multicopper oxidase family.Curated
Keywords - Domaini
Repeat, SignalFamily and domain databases
Gene3Di | 2.60.40.420, 3 hits |
InterProi | View protein in InterPro IPR001117, Cu-oxidase IPR011706, Cu-oxidase_C IPR045087, Cu-oxidase_fam IPR011707, Cu-oxidase_N IPR033138, Cu_oxidase_CS IPR008972, Cupredoxin |
PANTHERi | PTHR11709, PTHR11709, 1 hit |
Pfami | View protein in Pfam PF00394, Cu-oxidase, 1 hit PF07731, Cu-oxidase_2, 1 hit PF07732, Cu-oxidase_3, 1 hit |
SUPFAMi | SSF49503, SSF49503, 3 hits |
PROSITEi | View protein in PROSITE PS00079, MULTICOPPER_OXIDASE1, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
O59896-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MSRFQSLLSF VLVSLAAVAN AAIGPVADLT LTNAAVSPDG FSREAVVVNG
60 70 80 90 100
ITPAPLIAGQ KGDRFQLNVI DNLTNHTMLK TTSIHWHGFF QHGTNWADGV
110 120 130 140 150
SFVNQCPIAS GHSFLYDFQV PDQAGTFWYH SHLSTQYCDG LRGPFVVYDP
160 170 180 190 200
NDPQASLYDI DNDDTVITLA DWYHVAAKLG PRFPLGADAT LINGLGRSPG
210 220 230 240 250
TTTADLAVIK VTQGKRYRFR LVSLSCDPNH TFSIDGHTMT VIEADSVNTQ
260 270 280 290 300
PLEVDSIQIF AAQRYSFVLD ASQPVDNYWI RANPAFGNVG FAGGINSAIL
310 320 330 340 350
RYDGAPEVEP TTTQTTSTKP LNEADLHPLT PMPVPGRPEA GGVDKPLNMV
360 370 380 390 400
FNFNGTNFFI NNHSFVPPSV PVLLQILSGA QAAQDLVPDG SVYVLPSNSS
410 420 430 440 450
IEISFPATAN APGTPHPFHL HGHTFAVVRS AGSSEYNYDN PIFRDVVSTG
460 470 480 490 500
QPGDNVTIRF QTNNPGPWFL HCHIDFHLEA GFAVVLAEDT PDTAAVNPVP
510
QSWSDLCPIY DALDPSDL
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 348 | N → S in AAN71597 (Ref. 2) Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF025481 Genomic DNA Translation: AAC39469.1 AY147188 Genomic DNA Translation: AAN71597.1 AJ420334 mRNA Translation: CAD12461.1 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF025481 Genomic DNA Translation: AAC39469.1 AY147188 Genomic DNA Translation: AAN71597.1 AJ420334 mRNA Translation: CAD12461.1 |
3D structure databases
SMRi | O59896 |
ModBasei | Search... |
Protein family/group databases
CAZyi | AA1, Auxiliary Activities 1 |
Family and domain databases
Gene3Di | 2.60.40.420, 3 hits |
InterProi | View protein in InterPro IPR001117, Cu-oxidase IPR011706, Cu-oxidase_C IPR045087, Cu-oxidase_fam IPR011707, Cu-oxidase_N IPR033138, Cu_oxidase_CS IPR008972, Cupredoxin |
PANTHERi | PTHR11709, PTHR11709, 1 hit |
Pfami | View protein in Pfam PF00394, Cu-oxidase, 1 hit PF07731, Cu-oxidase_2, 1 hit PF07732, Cu-oxidase_3, 1 hit |
SUPFAMi | SSF49503, SSF49503, 3 hits |
PROSITEi | View protein in PROSITE PS00079, MULTICOPPER_OXIDASE1, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | LAC1_PYCCI | |
Accessioni | O59896Primary (citable) accession number: O59896 Secondary accession number(s): Q8J1Y2, Q8WZN9 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | September 19, 2003 |
Last sequence update: | August 1, 1998 | |
Last modified: | February 23, 2022 | |
This is version 92 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Direct protein sequencingDocuments
- SIMILARITY comments
Index of protein domains and families