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Protein
Submitted name:

Laccase

Gene
N/A
Organism
Botrytis aclada
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi126 – 1261Copper 1; via pros nitrogenCombined sources
Metal bindingi168 – 1681Copper 1; via tele nitrogenCombined sources
Metal bindingi170 – 1701Copper 2; via tele nitrogenCombined sources
Metal bindingi463 – 4631Copper 3; via pros nitrogenCombined sources
Metal bindingi466 – 4661Copper 2; via pros nitrogenCombined sources
Metal bindingi468 – 4681Copper 2; via tele nitrogenCombined sources
Metal bindingi525 – 5251Copper 2; via tele nitrogenCombined sources
Metal bindingi526 – 5261Copper 3Combined sources
Metal bindingi527 – 5271Copper 1; via tele nitrogenCombined sources
Metal bindingi531 – 5311Copper 3; via pros nitrogenCombined sources

GO - Molecular functioni

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

Keywords - Molecular functioni

OxidoreductaseSAAS annotation

Keywords - Ligandi

CopperCombined sourcesSAAS annotation, Metal-bindingCombined sourcesSAAS annotation

Names & Taxonomyi

Protein namesi
Submitted name:
LaccaseImported
OrganismiBotrytis acladaImported
Taxonomic identifieri139639 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaLeotiomycetesHelotialesSclerotiniaceaeBotrytis

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi39 ↔ 48Combined sources
Glycosylationi76 – 761N-linked (GlcNAc...)Combined sources
Glycosylationi92 – 921N-linked (GlcNAc...)Combined sources
Glycosylationi119 – 1191N-linked (GlcNAc...)Combined sources
Disulfide bondi145 ↔ 561Combined sources
Glycosylationi231 – 2311N-linked (GlcNAc...)Combined sources
Disulfide bondi238 ↔ 246Combined sources
Disulfide bondi334 ↔ 368Combined sources
Glycosylationi342 – 3421N-linked (GlcNAc...)Combined sources
Glycosylationi375 – 3751O-linked (Man...)Combined sources
Glycosylationi407 – 4071N-linked (GlcNAc...)Combined sources
Glycosylationi426 – 4261N-linked (GlcNAc...)Combined sources

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3SQRX-ray1.67A1-580[»]
ModBaseiSearch...
MobiDBiSearch...

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. 1 hit.
PS00080. MULTICOPPER_OXIDASE2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

H8ZRU2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKYFTVFTAL TALFAQASAS AIPAVRSTLT PRQNTTASCA NSATSRSCWG
60 70 80 90 100
EYSIDTNWYD VTPTGVTREY WLSVENSTIT PDGYTRSAMT FNGTVPGPAI
110 120 130 140 150
IADWGDNLII HVTNNLEHNG TSIHWHGIRQ LGSLEYDGVP GVTQCPIAPG
160 170 180 190 200
DTLTYKFQVT QYGTTWYHSH FSLQYGDGLF GPLIINGPAT ADYDEDVGVI
210 220 230 240 250
FLQDWAHESV FEIWDTARLG APPALENTLM NGTNTFDCSA STDPNCVGGG
260 270 280 290 300
KKFELTFVEG TKYRLRLINV GIDSHFEFAI DNHTLTVIAN DLVPIVPYTT
310 320 330 340 350
DTLLIGIGQR YDVIVEANAA ADNYWIRGNW GTTCSTNNEA ANATGILRYD
360 370 380 390 400
SSSIANPTSV GTTPRGTCED EPVASLVPHL ALDVGGYSLV DEQVSSAFTN
410 420 430 440 450
YFTWTINSSS LLLDWSSPTT LKIFNNETIF PTEYNVVALE QTNANEEWVV
460 470 480 490 500
YVIEDLTGFG IWHPIHLHGH DFFIVAQETD VFNSDESPAK FNLVNPPRRD
510 520 530 540 550
VAALPGNGYL AIAFKLDNPG SWLLHCHIAW HASEGLAMQF VESQSSIAVK
560 570 580
MTDTAIFEDT CANWNAYTPT QLFAEDDSGI
Length:580
Mass (Da):63,629
Last modified:May 16, 2012 - v1
Checksum:i32A1C1C8C0BDA0F5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
JN559771 Genomic DNA. Translation: AFC76164.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
JN559771 Genomic DNA. Translation: AFC76164.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3SQRX-ray1.67A1-580[»]
ModBaseiSearch...
MobiDBiSearch...

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.
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. 1 hit.
PS00080. MULTICOPPER_OXIDASE2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "A chloride tolerant laccase from the plant pathogen ascomycete Botrytis aclada expressed at high levels in Pichia pastoris."
    Kittl R., Mueangtoom K., Gonaus C., Khazaneh S.T., Sygmund C., Haltrich D., Ludwig R.
    J. Biotechnol. 157:304-314(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "Effect of the L499M mutation of the ascomycetous Botrytis aclada laccase on redox potential and catalytic properties."
    Osipov E., Polyakov K., Kittl R., Shleev S., Dorovatovsky P., Tikhonova T., Hann S., Ludwig R., Popov V.
    Acta Crystallogr. D 70:2913-2923(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) IN COMPLEX WITH COPPER, ACTIVE SITE, GLYCOSYLATION AT ASN-76; ASN-92; ASN-119; ASN-231; ASN-342; SER-375; ASN-407 AND ASN-426.

Entry informationi

Entry nameiH8ZRU2_9HELO
AccessioniPrimary (citable) accession number: H8ZRU2
Entry historyi
Integrated into UniProtKB/TrEMBL: May 16, 2012
Last sequence update: May 16, 2012
Last modified: March 4, 2015
This is version 17 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.