SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

H8ZRU2

- H8ZRU2_9HELO

UniProt

H8ZRU2 - H8ZRU2_9HELO

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Submitted name:

Laccase

Gene
N/A
Organism
Botrytis aclada
Status
Unreviewed - Annotation score: 2 out of 5 - Experimental evidence at protein leveli

Functioni

Sites

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

GO - Molecular functioni

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

Keywords - Molecular functioni

OxidoreductaseSAAS annotations

Keywords - Ligandi

CopperSAAS annotationsImported, Metal-bindingSAAS annotationsImported

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
Glycosylationi76 – 761N-linked (GlcNAc...)Imported
Glycosylationi92 – 921N-linked (GlcNAc...)Imported
Glycosylationi119 – 1191N-linked (GlcNAc...)Imported
Glycosylationi231 – 2311N-linked (GlcNAc...)Imported
Glycosylationi342 – 3421N-linked (GlcNAc...)Imported
Glycosylationi375 – 3751O-linked (Man...)Imported
Glycosylationi407 – 4071N-linked (GlcNAc...)Imported
Glycosylationi426 – 4261N-linked (GlcNAc...)Imported

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3SQRX-ray1.67A1-580[»]

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

MKYFTVFTAL TALFAQASAS AIPAVRSTLT PRQNTTASCA NSATSRSCWG    50
EYSIDTNWYD VTPTGVTREY WLSVENSTIT PDGYTRSAMT FNGTVPGPAI 100
IADWGDNLII HVTNNLEHNG TSIHWHGIRQ LGSLEYDGVP GVTQCPIAPG 150
DTLTYKFQVT QYGTTWYHSH FSLQYGDGLF GPLIINGPAT ADYDEDVGVI 200
FLQDWAHESV FEIWDTARLG APPALENTLM NGTNTFDCSA STDPNCVGGG 250
KKFELTFVEG TKYRLRLINV GIDSHFEFAI DNHTLTVIAN DLVPIVPYTT 300
DTLLIGIGQR YDVIVEANAA ADNYWIRGNW GTTCSTNNEA ANATGILRYD 350
SSSIANPTSV GTTPRGTCED EPVASLVPHL ALDVGGYSLV DEQVSSAFTN 400
YFTWTINSSS LLLDWSSPTT LKIFNNETIF PTEYNVVALE QTNANEEWVV 450
YVIEDLTGFG IWHPIHLHGH DFFIVAQETD VFNSDESPAK FNLVNPPRRD 500
VAALPGNGYL AIAFKLDNPG SWLLHCHIAW HASEGLAMQF VESQSSIAVK 550
MTDTAIFEDT CANWNAYTPT QLFAEDDSGI 580
Length:580
Mass (Da):63,629
Last modified:May 16, 2012 - v1
Checksum:i32A1C1C8C0BDA0F5
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
JN559771 Genomic DNA. Translation: AFC76164.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
JN559771 Genomic DNA. Translation: AFC76164.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3SQR X-ray 1.67 A 1-580 [» ]
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 2.60.40.420. 3 hits.
InterProi IPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR002355. Cu_oxidase_Cu_BS.
IPR008972. Cupredoxin.
[Graphical view ]
Pfami PF00394. Cu-oxidase. 1 hit.
PF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 1 hit.
[Graphical view ]
SUPFAMi SSF49503. SSF49503. 3 hits.
PROSITEi PS00079. MULTICOPPER_OXIDASE1. 1 hit.
PS00080. MULTICOPPER_OXIDASE2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Structural and kinetic characterization of a chloride resistant laccase from Botrytis aclada."
    Osipov E.M., Polyakov K.M., Tikhonova T.V., Dorovatovsky P.V., Ludwig R., Kittl R., Shleev S.V., Popov V.O.
    Submitted (JUL-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) IN COMPLEX WITH COPPER, GLYCOSYLATION AT ASN-76; ASN-92; ASN-119; ASN-231; ASN-342; SER-375; ASN-407 AND ASN-426.
  2. "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.

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: September 3, 2014
This is version 11 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureImported

External Data

Dasty 3

Similar proteinsi