Laccase 1 - Coprinopsis cinerea (Inky cap fungus)

Preferred order of sections

Names and origin

Protein names

Submitted name:
Laccase 1 EMBL AAD30964.1
EC=1.10.3.2 EMBL AAD30964.1

Gene names

Name:

lcc1 EMBL AAD30964.1

Organism

Coprinopsis cinerea (Inky cap fungus) (Hormographiella aspergillata) EMBL AAD30964.1

Taxonomic identifier

5346 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Agaricomycetes › Agaricomycetidae › Agaricales › Psathyrellaceae › Coprinopsis

Protein attributes

Sequence length	539 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Ligand	Copper SAAS SAAS011706 PDB 1HFU PDB 1A65 Metal-binding SAAS SAAS011706 PDB 1HFU PDB 1A65
Molecular function	Oxidoreductase SAAS SAAS011706 EMBL AAD30964.1
Technical term	3D-structure PDB 1HFU PDB 1A65
Gene Ontology (GO)
Molecular_function	copper ion binding Inferred from electronic annotation. Source: InterPro hydroquinone:oxygen oxidoreductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Sites

Metal binding

84

1

Copper 1; via pros nitrogen PDB 1HFU PDB 1A65

Metal binding

127

1

Copper 1; via tele nitrogen PDB 1HFU PDB 1A65

Metal binding

129

1

Copper 2; via tele nitrogen PDB 1HFU PDB 1A65

Metal binding

414

1

Copper 3; via pros nitrogen PDB 1HFU PDB 1A65

Metal binding

417

1

Copper 2; via tele nitrogen PDB 1HFU PDB 1A65

Metal binding

419

1

Copper 2; via tele nitrogen PDB 1HFU PDB 1A65

Metal binding

469

1

Copper 2; via tele nitrogen PDB 1HFU PDB 1A65

Metal binding

470

1

Copper 3 PDB 1HFU PDB 1A65

Metal binding

471

1

Copper 1; via tele nitrogen PDB 1HFU PDB 1A65

Metal binding

475

1

Copper 3; via pros nitrogen PDB 1HFU PDB 1A65

Binding site

175

1

Mannose; via carbonyl oxygen PDB 1HFU

Binding site

520

1

Mannose PDB 1HFU

Site

469

1

Important for catalytic activity PDB 1A65

Site

470

1

Important for catalytic activity PDB 1A65

Site

471

1

Important for catalytic activity PDB 1A65

Amino acid modifications

Glycosylation

361

1

N-linked (GlcNAc...) PDB 1A65

Sequences

Sequence

Length

Mass (Da)

Tools

Q9Y780 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: FC45584BBE6142A9
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FASTA

539

58,385

        10         20         30         40         50         60 
MFKNLLSFAL LAISVANAQI VNSVDTMTLT NANVSPDGFT RAGILVNGVH GPLIRGGKND 

        70         80         90        100        110        120 
NFELNVVNDL DNPTMLRPTS IHWHGLFQRG TNWADGADGV NQCPISPGHA FLYKFTPAGH 

       130        140        150        160        170        180 
AGTFWYHSHF GTQYCDGLRG PMVIYDDNDP HAALYDEDDE NTIITLADWY HIPAPSIQGA 

       190        200        210        220        230        240 
AQPDATLING KGRYVGGPAA ELSIVNVEQG KKYRMRLISL SCDPNWQFSI DGHELTIIEV 

       250        260        270        280        290        300 
DGQLTEPHTV DRLQIFTGQR YSFVLDANQP VDNYWIRAQP NKGRNGLAGT FANGVNSAIL 

       310        320        330        340        350        360 
RYAGAANADP TTSANPNPAQ LNEADLHALI DPAAPGIPTP GAADVNLRFQ LGFSGGRFTI 

       370        380        390        400        410        420 
NGTAYESPSV PTLLQIMSGA QSANDLLPAG SVYELPRNQV VELVVPAGVL GGPHPFHLHG 

       430        440        450        460        470        480 
HAFSVVRSAG SSTYNFVNPV KRDVVSLGVT GDEVTIRFVT DNPGPWFFHC HIEFHLMNGL 

       490        500        510        520        530 
AIVFAEDMAN TVDANNPPVE WAQLCEIYDD LPPEATSIQT VVRRAEPTGF SAKFRREGL

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References

[1]	"Crystal structure of the type-2 Cu depleted laccase from Coprinus cinereus at 2.2 A resolution." Ducros V., Brzozowski A.M., Wilson K.S., Brown S.H., Ostergaard P., Schneider P., Yaver D.S., Pedersen A.H., Davies G.J. Nat. Struct. Biol. 5:310-316(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS) OF 19-522 IN COMPLEX WITH COPPER, ACTIVE SITE, GLYCOSYLATION AT ASN-361.
[2]	"Molecular characterization of laccase genes from the basidiomycete Coprinus cinereus and heterologous expression of the laccase lcc1." Yaver D.S., Overjero M.D., Xu F., Nelson B.A., Brown K.M., Halkier T., Bernauer S., Brown S.H., Kauppinen S. Appl. Environ. Microbiol. 65:4943-4948(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: A3387 EMBL AAD30964.1.
[3]	"Structure of the laccase from Coprinus cinereus at 1.68 A resolution: evidence for different 'type 2 Cu-depleted' isoforms." Ducros V., Brzozowski A.M., Wilson K.S., Ostergaard P., Schneider P., Svendson A., Davies G.J. Acta Crystallogr. D 57:333-336(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) OF 20-521 IN COMPLEX WITH COPPER AND MANNOSE.
[4]	"The laccase gene family in Coprinopsis cinerea (Coprinus cinereus)." Hoegger P.J., Navarro-Gonzalez M., Kilaru S., Hoffmann M., Westbrook E.D., Kues U. Curr. Genet. 45:9-18(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: AT8 EMBL AAR01241.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF118267 Genomic DNA. Translation: AAD30964.1.
AY338756 Genomic DNA. Translation: AAR01241.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A65	X-ray	2.23	A	19-522	[»]
1HFU	X-ray	1.68	A	20-521	[»]

SMR

Q9Y780. Positions 19-522.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

2.60.40.420. 3 hits.

InterPro

IPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR002355. Cu_oxidase_Cu_BS.
IPR008972. Cupredoxin.
[Graphical view]

Pfam

PF00394. Cu-oxidase. 1 hit.
PF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 1 hit.
[Graphical view]

SUPFAM

SSF49503. Cupredoxin. 3 hits.

PROSITE

PS00079. MULTICOPPER_OXIDASE1. 2 hits.
PS00080. MULTICOPPER_OXIDASE2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9Y780.

Entry information

Entry name

Q9Y780_COPCI

Accession

Primary (citable) accession number: Q9Y780

Entry history

Integrated into UniProtKB/TrEMBL:	November 1, 1999
Last sequence update:	November 1, 1999
Last modified:	May 1, 2013
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)