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Protein
Submitted name:

Laccase B

Gene

lac1

Organism
Trametes versicolor (White-rot fungus) (Coriolus versicolor)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi85Copper 1; via tele nitrogenCombined sources1
Metal bindingi87Copper 2; via pros nitrogenCombined sources1
Metal bindingi130Copper 2; via tele nitrogenCombined sources1
Metal bindingi132Copper 3; via tele nitrogenCombined sources1
Binding sitei176N-acetyl-D-glucosamine; via amide nitrogenCombined sources1
Binding sitei238N-acetyl-D-glucosamineCombined sources1
Metal bindingi416Copper 4; via pros nitrogenCombined sources1
Metal bindingi419Copper 1; via tele nitrogenCombined sources1
Metal bindingi421Copper 3; via tele nitrogenCombined sources1
Binding sitei457N-acetyl-D-glucosamineCombined sources1
Metal bindingi473Copper 3; via tele nitrogenCombined sources1
Metal bindingi474Copper 4Combined sources1
Metal bindingi475Copper 2; via tele nitrogenCombined sources1
Metal bindingi479Copper 4; via pros nitrogenCombined sources1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

OxidoreductaseSAAS annotationImported

Keywords - Ligandi

CopperCombined sourcesSAAS annotation, Metal-bindingCombined sourcesSAAS annotation

Enzyme and pathway databases

BRENDAi1.10.3.2. 1626.

Protein family/group databases

CAZyiAA1. Auxiliary Activities 1.

Names & Taxonomyi

Protein namesi
Submitted name:
Laccase BImported (EC:1.10.3.2Imported)
Gene namesi
Name:lac1Imported
OrganismiTrametes versicolor (White-rot fungus) (Coriolus versicolor)Imported
Taxonomic identifieri5325 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesPolyporalesTrametes

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Sequence analysisAdd BLAST21
ChainiPRO_500432162222 – 520Sequence analysisAdd BLAST499

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi106 ↔ 509Combined sources
Disulfide bondi138 ↔ 226Combined sources

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KYAX-ray2.40A/B/C/D22-520[»]
ProteinModelPortaliQ96UT7.
SMRiQ96UT7.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96UT7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini31 – 151Plastocyanin-likeInterPro annotationAdd BLAST121
Domaini164 – 305Plastocyanin-likeInterPro annotationAdd BLAST142
Domaini366 – 491Plastocyanin-likeInterPro annotationAdd BLAST126

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni75 – 77N-acetyl-D-glucosamine bindingCombined sources3
Regioni354 – 357N-acetyl-D-glucosamine bindingCombined sources4

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q96UT7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRFHSLFAF VVASLTAVAH AGIGPVADLT ITNAAVSPDG FSRQAVVVNG
60 70 80 90 100
GTPGPLITGN MGDRFQLNVI DNLTNHTMLK STSIHWHGFF QKGTNWADGP
110 120 130 140 150
AFINQCPISS GHSFLYDFQV PDQAGTFWYH SHLSTQYCDG LRGPFVVYDP
160 170 180 190 200
NDPAADLYDV DNDDTVITLV DWYHVAAKLG PAFPLGADAT LINGKGRSPS
210 220 230 240 250
TTTADLSVIS VTPGKRYRFR LVSLSCDPNY TFSIDGHNMT IIETDSINTA
260 270 280 290 300
PLVVDSIQIF AAQRYSFVLE ANQAVDNYWI RANPNFGNVG FTGGINSAIL
310 320 330 340 350
RYDGAAAVEP TTTQTTSTAP LNEVNLHPLV ATAVPGSPVA GGVDLAINMA
360 370 380 390 400
FNFNGTNFFI NGASFTPPTV PVLLQIISGA QNAQDLLPSG SVYSLPSNAD
410 420 430 440 450
IEISFPATAA APGAPHPFHL HGHAFAVVRS AGSTVYNYDN PIFRDVVSTG
460 470 480 490 500
TPAAGDNVTI RFRTDNPGPW FLHCHIDFHL EAGFAVVFAE DIPDVASANP
510 520
VPQAWSDLCP TYDARDPSDQ
Length:520
Mass (Da):55,576
Last modified:December 1, 2001 - v1
Checksum:iF3241CB929C247F9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF414109 mRNA. Translation: AAL07440.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF414109 mRNA. Translation: AAL07440.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KYAX-ray2.40A/B/C/D22-520[»]
ProteinModelPortaliQ96UT7.
SMRiQ96UT7.
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. 1626.

Miscellaneous databases

EvolutionaryTraceiQ96UT7.

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 nameiQ96UT7_TRAVE
AccessioniPrimary (citable) accession number: Q96UT7
Entry historyi
Integrated into UniProtKB/TrEMBL: December 1, 2001
Last sequence update: December 1, 2001
Last modified: November 30, 2016
This is version 78 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.