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Protein
Submitted name:

Laccase

Gene

lcc1

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

Functioni

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi64Copper 1; via tele nitrogenCombined sources1
Metal bindingi66Copper 2; via pros nitrogenCombined sources1
Metal bindingi109Copper 2; via tele nitrogenCombined sources1
Metal bindingi111Copper 3; via tele nitrogenCombined sources1
Metal bindingi341CalciumCombined sources1
Metal bindingi367CalciumCombined sources1
Metal bindingi394Copper 4; via pros nitrogenCombined sources1
Metal bindingi397Copper 1; via tele nitrogenCombined sources1
Metal bindingi399Copper 3; via tele nitrogenCombined sources1
Metal bindingi451Copper 3; via tele nitrogenCombined sources1
Metal bindingi452Copper 4Combined sources1
Metal bindingi453Copper 2; via tele nitrogenCombined sources1
Metal bindingi457Copper 4; via pros nitrogenCombined sources1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

OxidoreductaseImported

Keywords - Ligandi

CalciumCombined sources, CopperCombined sources, Metal-bindingCombined sourcesSAAS annotation

Enzyme and pathway databases

BRENDAi1.10.3.2. 2974.

Protein family/group databases

CAZyiAA1. Auxiliary Activities 1.

Names & Taxonomyi

Protein namesi
Submitted name:
LaccaseImported (EC:1.10.3.2Imported)
Gene namesi
Name:lcc1Imported
OrganismiLentinus tigrinusImported
Taxonomic identifieri5365 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesPolyporalesLentinaceaeLentinus

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi117 ↔ 205Combined sources
GlycosylationiCAR_5005389918376N-linked (GlcNAc...)Combined sources1

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2QT6X-ray1.50A/B1-463[»]
ProteinModelPortaliQ5EBY5.
SMRiQ5EBY5.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5EBY5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini10 – 130Plastocyanin-likeInterPro annotationAdd BLAST121
Domaini142 – 283Plastocyanin-likeInterPro annotationAdd BLAST142
Domaini344 – 463Plastocyanin-likeInterPro annotationAdd BLAST120

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: Fragment.

Q5EBY5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
AVGPVADLTV TNANISPDGF ERAAIVVNNV FPAPLITGNM GDNFQLNLVN
60 70 80 90 100
QMTNHTMLKT TSIHWHGFFQ KGTNWADGPA FINQCPIASG NSFLYDFQVP
110 120 130 140 150
GQAGTFWYHS HLSTQYCDGL RGPFVVYDPN DPHANLYDVD DESTVITLAD
160 170 180 190 200
WYHVAAKLGP RFPLGADSTL INGLGRSTST PTADLAVISV TKGKRYRFRL
210 220 230 240 250
VSLSCDPNYT FSIDSHQLTV IEADGVSTQP VTVDSIQIFA AQRYSFVLNA
260 270 280 290 300
NQDVDNYWIR ANPNFGTTGF ADGVNSAILR YDDADPVEPV TNQTGTTLLL
310 320 330 340 350
ETDLHPLTSM PVPGNPTQGG ADLNLNMAFN FDGTNFFING ESFTPPTVPV
360 370 380 390 400
LLQIISGANT AQDLLPSGSV YSLPSNSSIE ITFPATTAAP GAPHPFHLHG
410 420 430 440 450
HVFAVVRSAG STSYNYDDPV WRDVVSTGTP QAGDNVTIRF QTDNPGPWFL
460
HCHIDFHLEA GFA
Length:463
Mass (Da):50,146
Last modified:March 15, 2005 - v1
Checksum:i33CBEBA6B0606754
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei1Imported1
Non-terminal residuei463Imported1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY914796 Genomic DNA. Translation: AAX07469.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY914796 Genomic DNA. Translation: AAX07469.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2QT6X-ray1.50A/B1-463[»]
ProteinModelPortaliQ5EBY5.
SMRiQ5EBY5.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiAA1. Auxiliary Activities 1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi1.10.3.2. 2974.

Miscellaneous databases

EvolutionaryTraceiQ5EBY5.

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...

Entry informationi

Entry nameiQ5EBY5_9APHY
AccessioniPrimary (citable) accession number: Q5EBY5
Entry historyi
Integrated into UniProtKB/TrEMBL: March 15, 2005
Last sequence update: March 15, 2005
Last modified: November 30, 2016
This is version 52 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.