Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9Y780 (Q9Y780_COPCI) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Protein attributes

Sequence length539 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Metal binding841Copper 1; via pros nitrogen PDB 1HFU PDB 1A65
Metal binding1271Copper 1; via tele nitrogen PDB 1HFU PDB 1A65
Metal binding1291Copper 2; via tele nitrogen PDB 1HFU PDB 1A65
Metal binding4141Copper 3; via pros nitrogen PDB 1HFU PDB 1A65
Metal binding4171Copper 2; via tele nitrogen PDB 1HFU PDB 1A65
Metal binding4191Copper 2; via tele nitrogen PDB 1HFU PDB 1A65
Metal binding4691Copper 2; via tele nitrogen PDB 1HFU PDB 1A65
Metal binding4701Copper 3 PDB 1HFU PDB 1A65
Metal binding4711Copper 1; via tele nitrogen PDB 1HFU PDB 1A65
Metal binding4751Copper 3; via pros nitrogen PDB 1HFU PDB 1A65
Binding site1751Mannose; via carbonyl oxygen PDB 1HFU
Binding site5201Mannose PDB 1HFU
Site4691Important for catalytic activity PDB 1A65
Site4701Important for catalytic activity PDB 1A65
Site4711Important for catalytic activity PDB 1A65

Amino acid modifications

Glycosylation3611N-linked (GlcNAc...)

Sequences

Sequence LengthMass (Da)Tools
Q9Y780 [UniParc].

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

FASTA53958,385
        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 

« Hide

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1A65X-ray2.23A19-522[»]
1HFUX-ray1.68A20-521[»]
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.60.40.420. 3 hits.
InterProIPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR002355. Cu_oxidase_Cu_BS.
IPR008972. Cupredoxin.
[Graphical view]
PfamPF00394. Cu-oxidase. 1 hit.
PF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 1 hit.
[Graphical view]
SUPFAMSSF49503. SSF49503. 3 hits.
PROSITEPS00079. MULTICOPPER_OXIDASE1. 2 hits.
PS00080. MULTICOPPER_OXIDASE2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9Y780.

Entry information

Entry nameQ9Y780_COPCI
AccessionPrimary (citable) accession number: Q9Y780
Entry history
Integrated into UniProtKB/TrEMBL: November 1, 1999
Last sequence update: November 1, 1999
Last modified: June 11, 2014
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)