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Protein
Submitted name:

Laccase 1

Gene

lcc1

Organism
Coprinopsis cinerea (Inky cap fungus) (Hormographiella aspergillata)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi84 – 841Copper 1; via pros nitrogenCombined sources
Metal bindingi127 – 1271Copper 1; via tele nitrogenCombined sources
Metal bindingi129 – 1291Copper 2; via tele nitrogenCombined sources
Binding sitei175 – 1751Mannose; via carbonyl oxygenCombined sources
Metal bindingi414 – 4141Copper 3; via pros nitrogenCombined sources
Metal bindingi417 – 4171Copper 2; via tele nitrogenCombined sources
Metal bindingi419 – 4191Copper 2; via tele nitrogenCombined sources
Metal bindingi469 – 4691Copper 2; via tele nitrogenCombined sources
Sitei469 – 4691Important for catalytic activityCombined sources
Metal bindingi470 – 4701Copper 3Combined sources
Sitei470 – 4701Important for catalytic activityCombined sources
Metal bindingi471 – 4711Copper 1; via tele nitrogenCombined sources
Sitei471 – 4711Important for catalytic activityCombined sources
Metal bindingi475 – 4751Copper 3; via pros nitrogenCombined sources
Binding sitei520 – 5201MannoseCombined sources

GO - Molecular functioni

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

Keywords - Molecular functioni

OxidoreductaseSAAS annotationImported

Keywords - Ligandi

CopperCombined sources, Metal-bindingCombined sources

Names & Taxonomyi

Protein namesi
Submitted name:
Laccase 1Imported (EC:1.10.3.2Imported)
Gene namesi
Name:lcc1Imported
OrganismiCoprinopsis cinerea (Inky cap fungus) (Hormographiella aspergillata)Imported
Taxonomic identifieri5346 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesPsathyrellaceaeCoprinopsis

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi103 ↔ 505Combined sources
Disulfide bondi135 ↔ 222Combined sources
Glycosylationi361 – 3611N-linked (GlcNAc...)Combined sources

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A65X-ray2.23A19-522[»]
1HFUX-ray1.68A20-521[»]
ProteinModelPortaliQ9Y780.
SMRiQ9Y780. Positions 19-522.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y780.

Family & Domainsi

Family and domain databases

Gene3Di2.60.40.420. 3 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. 2 hits.
PS00080. MULTICOPPER_OXIDASE2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Y780-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFKNLLSFAL LAISVANAQI VNSVDTMTLT NANVSPDGFT RAGILVNGVH
60 70 80 90 100
GPLIRGGKND NFELNVVNDL DNPTMLRPTS IHWHGLFQRG TNWADGADGV
110 120 130 140 150
NQCPISPGHA FLYKFTPAGH AGTFWYHSHF GTQYCDGLRG PMVIYDDNDP
160 170 180 190 200
HAALYDEDDE NTIITLADWY HIPAPSIQGA AQPDATLING KGRYVGGPAA
210 220 230 240 250
ELSIVNVEQG KKYRMRLISL SCDPNWQFSI DGHELTIIEV DGQLTEPHTV
260 270 280 290 300
DRLQIFTGQR YSFVLDANQP VDNYWIRAQP NKGRNGLAGT FANGVNSAIL
310 320 330 340 350
RYAGAANADP TTSANPNPAQ LNEADLHALI DPAAPGIPTP GAADVNLRFQ
360 370 380 390 400
LGFSGGRFTI NGTAYESPSV PTLLQIMSGA QSANDLLPAG SVYELPRNQV
410 420 430 440 450
VELVVPAGVL GGPHPFHLHG HAFSVVRSAG SSTYNFVNPV KRDVVSLGVT
460 470 480 490 500
GDEVTIRFVT DNPGPWFFHC HIEFHLMNGL AIVFAEDMAN TVDANNPPVE
510 520 530
WAQLCEIYDD LPPEATSIQT VVRRAEPTGF SAKFRREGL
Length:539
Mass (Da):58,385
Last modified:October 31, 1999 - v1
Checksum:iFC45584BBE6142A9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF118267 Genomic DNA. Translation: AAD30964.1.
AY338756 Genomic DNA. Translation: AAR01241.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF118267 Genomic DNA. Translation: AAD30964.1.
AY338756 Genomic DNA. Translation: AAR01241.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A65X-ray2.23A19-522[»]
1HFUX-ray1.68A20-521[»]
ProteinModelPortaliQ9Y780.
SMRiQ9Y780. Positions 19-522.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y780.

Family and domain databases

Gene3Di2.60.40.420. 3 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. 2 hits.
PS00080. MULTICOPPER_OXIDASE2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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(1997) [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(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: A3387Imported.
  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(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) OF 20-521 IN COMPLEX WITH COPPER AND MANNOSE, ACTIVE SITE.
  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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: AT8Imported.

Entry informationi

Entry nameiQ9Y780_COPCI
AccessioniPrimary (citable) accession number: Q9Y780
Entry historyi
Integrated into UniProtKB/TrEMBL: October 31, 1999
Last sequence update: October 31, 1999
Last modified: March 31, 2015
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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.