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Protein
Submitted name:

Laccase

Gene

lac1

Organism
Coriolopsis gallica
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Cofactori

Cu cationSAAS annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi85 – 851Copper 1; via tele nitrogenCombined sources
Metal bindingi85 – 851Copper 2Combined sources
Metal bindingi87 – 871Copper 2; via pros nitrogenCombined sources
Metal bindingi130 – 1301Copper 2; via tele nitrogenCombined sources
Metal bindingi132 – 1321Copper 3; via tele nitrogenCombined sources
Metal bindingi415 – 4151Copper 4; via pros nitrogenCombined sources
Metal bindingi418 – 4181Copper 1; via tele nitrogenCombined sources
Metal bindingi418 – 4181Copper 3; via tele nitrogenCombined sources
Metal bindingi420 – 4201Copper 3; via tele nitrogenCombined sources
Metal bindingi470 – 4701Copper 3; via tele nitrogenCombined sources
Metal bindingi471 – 4711Copper 4Combined sources
Metal bindingi472 – 4721Copper 2; via tele nitrogenCombined sources
Metal bindingi476 – 4761Copper 4; via pros nitrogenCombined sources

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

OxidoreductaseSAAS annotationImported

Keywords - Ligandi

CopperCombined sourcesSAAS annotation, Metal-bindingCombined sourcesSAAS annotation

Protein family/group databases

CAZyiAA1. Auxiliary Activities 1.

Names & Taxonomyi

Protein namesi
Submitted name:
LaccaseImported (EC:1.10.3.2Imported)
Gene namesi
Name:lac1Imported
OrganismiCoriolopsis gallicaImported
Taxonomic identifieri76126 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesPolyporalesCoriolopsis

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence analysisAdd
BLAST
Chaini22 – 517496Sequence analysisPRO_5007700015Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi75 – 751N-linked (GlcNAc...)Combined sourcesCAR_5007700013
Disulfide bondi106 ↔ 506Combined sources
Disulfide bondi138 ↔ 225Combined sources
Glycosylationi454 – 4541N-linked (GlcNAc...)Combined sourcesCAR_5007700014

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4A2DX-ray2.30A22-517[»]
4A2EX-ray1.80A22-517[»]
4A2FX-ray1.90A22-517[»]
4A2GX-ray1.80A22-517[»]
4A2HX-ray2.30A22-517[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini32 – 151120Plastocyanin-likeInterPro annotationAdd
BLAST
Domaini164 – 304141Plastocyanin-likeInterPro annotationAdd
BLAST
Domaini365 – 488124Plastocyanin-likeInterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the multicopper oxidase family.SAAS annotation

Keywords - Domaini

SignalSequence analysis

Family and domain databases

Gene3Di2.60.40.420. 3 hits.
InterProiIPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR033138. Cu_oxidase_CS.
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. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q1W6B1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARFQSLLTF ITLSLVASVY AAIGPVADLT ISNGAVSPYG FSRQAILVND
60 70 80 90 100
VFPSPLITGN KGDRFQLNVI DNMTNHTMLK STSIHWHGFF QHGTNWADGP
110 120 130 140 150
AFVNQCPIST GHAFLYDFQV PDQAGTFWYH SHLSTQYCDG LRGPIVVYDP
160 170 180 190 200
QDPHKSLYDV DDDSTVITLA DWYHLAARVG PAIPTADATL INGLGRSINT
210 220 230 240 250
LNADLAVITV TKGKRYRFRL VSLSCDPNHT FSIDGHSLTV IEADSVNLKP
260 270 280 290 300
HTVDSIQIFA AQRYSFVLNA DQDVDNYWIR ALPNSGNTNF DGGVNSAILR
310 320 330 340 350
YDGAAPVEPT TSQAPSTNPL VESALTTLEG TAAPGSPTPG GVDLALNMAF
360 370 380 390 400
GFAGGRFSIN GASFTPPTVP VLLQILSGAQ SAQDLLPTGS VYSLPANADI
410 420 430 440 450
EISLPATTAA PGFPHPFHLH GHAFAVVRSA GSSTYNYENP VYRDVVSTGS
460 470 480 490 500
PGDNVTIRFR TDNPGPWFLH CHIDFHLEAG FAVVMAEDIP DVAATNPVPQ
510
AWSDLCPTYD ALSPDDQ
Length:517
Mass (Da):55,531
Last modified:May 2, 2006 - v1
Checksum:i7C1D6C4A67144259
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ431715 Genomic DNA. Translation: ABD93940.1.
DQ431716 mRNA. Translation: ABD93941.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ431715 Genomic DNA. Translation: ABD93940.1.
DQ431716 mRNA. Translation: ABD93941.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4A2DX-ray2.30A22-517[»]
4A2EX-ray1.80A22-517[»]
4A2FX-ray1.90A22-517[»]
4A2GX-ray1.80A22-517[»]
4A2HX-ray2.30A22-517[»]
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiAA1. Auxiliary Activities 1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di2.60.40.420. 3 hits.
InterProiIPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR033138. Cu_oxidase_CS.
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. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning and sequence analysis of a laccase gene from mutated strain SAH-12 of white rot fungus Trametes gallica."
    Huang Q.-M., Yang W.-S., Xie J.
    Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: SAH-12Imported.
  2. "Structural changes caused by radiation-induced reduction and radiolysis: the effect of X-ray absorbed dose in a fungal multicopper oxidase."
    De la Mora E., Lovett J.E., Blanford C.F., Garman E.F., Valderrama B., Rudino-Pinera E.
    Acta Crystallogr. D 68:564-577(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 22-517 IN COMPLEX WITH COPPER, GLYCOSYLATION AT ASN-75 AND ASN-454, DISULFIDE BONDS.

Entry informationi

Entry nameiQ1W6B1_9APHY
AccessioniPrimary (citable) accession number: Q1W6B1
Entry historyi
Integrated into UniProtKB/TrEMBL: May 2, 2006
Last sequence update: May 2, 2006
Last modified: July 6, 2016
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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 one 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.