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P78722

- LAC2_PODAS

UniProt

P78722 - LAC2_PODAS

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Protein

Laccase-2

Gene
LAC2
Organism
Podospora anserina (Pleurage anserina)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

Probably involved in lignin degradation and in the detoxification of lignin-derived products in its natural habitat (herbivorous dung), which is rich in lignin of grasses and straw. Probably involved in melanin synthesis and in perithecia development.

Catalytic activityi

4 benzenediol + O2 = 4 benzosemiquinone + 2 H2O.

Cofactori

Binds 4 copper ions per monomer By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi138 – 1381Copper 1; type 2 By similarity
Metal bindingi140 – 1401Copper 2; type 3 By similarity
Metal bindingi183 – 1831Copper 2; type 3 By similarity
Metal bindingi185 – 1851Copper 3; type 3 By similarity
Metal bindingi476 – 4761Copper 4; type 1 By similarity
Metal bindingi479 – 4791Copper 1; type 2 By similarity
Metal bindingi481 – 4811Copper 3; type 3 By similarity
Metal bindingi548 – 5481Copper 3; type 3 By similarity
Metal bindingi549 – 5491Copper 4; type 1 By similarity
Metal bindingi550 – 5501Copper 2; type 3 By similarity
Metal bindingi554 – 5541Copper 4; type 1 By similarity

GO - Molecular functioni

  1. copper ion binding Source: InterPro
  2. hydroquinone:oxygen oxidoreductase activity Source: UniProtKB-EC

GO - Biological processi

  1. lignin catabolic process Source: UniProtKB-KW
  2. melanin biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Lignin degradation, Melanin biosynthesis

Keywords - Ligandi

Copper, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Laccase-2 (EC:1.10.3.2)
Alternative name(s):
Benzenediol:oxygen oxidoreductase 2
Diphenol oxidase 2
Laccase C
Laccase II
Urishiol oxidase 2
Gene namesi
Name:LAC2
OrganismiPodospora anserina (Pleurage anserina)
Taxonomic identifieri5145 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesLasiosphaeriaceaePodospora

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323 Reviewed predictionAdd
BLAST
Propeptidei24 – 4825 Reviewed predictionPRO_0000002931Add
BLAST
Chaini49 – 605557Laccase-2PRO_0000002932Add
BLAST
Propeptidei606 – 62116 Reviewed predictionPRO_0000002933Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi133 – 1331N-linked (GlcNAc...) Reviewed prediction
Glycosylationi261 – 2611N-linked (GlcNAc...) Reviewed prediction
Glycosylationi276 – 2761N-linked (GlcNAc...) Reviewed prediction
Glycosylationi289 – 2891N-linked (GlcNAc...) Reviewed prediction
Glycosylationi325 – 3251N-linked (GlcNAc...) Reviewed prediction
Glycosylationi334 – 3341N-linked (GlcNAc...) Reviewed prediction
Glycosylationi401 – 4011N-linked (GlcNAc...) Reviewed prediction
Glycosylationi421 – 4211N-linked (GlcNAc...) Reviewed prediction
Glycosylationi441 – 4411N-linked (GlcNAc...) Reviewed prediction

Post-translational modificationi

Proteolytically processed at both its N-terminus and its C-terminus.

Keywords - PTMi

Glycoprotein

Expressioni

Developmental stagei

Low basic levels throughout the growth phase; increases at least 20-fold at the beginning of the autolytic phase and decreases again thereafter.

Inductioni

Under oxidative stress on the mycelium by aromatic xenobiotics (guaiacol, hydroquinone, benzoquinone), and by copper salt at a concentration of 1 mM (growing mycelium).

Interactioni

Subunit structurei

Monomer.

Structurei

3D structure databases

ProteinModelPortaliP78722.
SMRiP78722. Positions 46-605.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini78 – 201124Plastocyanin-like 1Add
BLAST
Domaini210 – 367158Plastocyanin-like 2Add
BLAST
Domaini430 – 566137Plastocyanin-like 3Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Repeat, Signal

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.

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

P78722-1 [UniParc]FASTAAdd to Basket

« Hide

MMKSFFSAAA LLLGLVAPSA VLAAPSLPGV PREVTRDLLR PVEERQSSCH    50
TAANRACWAP GFDINTDYEV STPNTGVTRT YTLTLTEVDN WLGPDGVVKQ 100
KVMLVNGDIF GPTITANWGD WIQVNVINNL RTNGTSIHWH GLHQKGTNMH 150
DGANGVTECP IPPKGGSRIY RFRAQQYGTS WYHSHFSAQY GNGVVGTIVV 200
NGPASVPYDI DLGVFPITDY YHKPADVLVE ETMNGGPPPS DTVLFKGHGK 250
NPQTGAGKFA NVTLTPGKRH RLRIINTSTH DHFQLKLQNH TMTIIAADMV 300
PVQAQTVDSL FLAVGQRYDV TIDANKSVGN YWFNATFGGG LACGASLNPH 350
PAAVFRYQGA PNTLPTNIGT PAADANCMDL NNLTPVVSRS VPTSGFTPRP 400
NNTLPVSLTL GGTPLFVWKV NGSSINVDWD KPIVDYVIAQ NTSYPPQANV 450
ITVNSVNQWT YWLIENDPTG PFSIPHPMHL HGHDFLVVGR SPDQPAGVPQ 500
TRYRFNPATD MALLKSSNPV RRDVAMLPAN GWLLIAFKSD NPGAWLFHCH 550
IAWHVSGGLS VQYLERPNDL RNGFSQADKN QHNNNCNAWR AYWPTNPFPK 600
IDSGLKVKKW VGEHPDWYIK N 621
Length:621
Mass (Da):68,129
Last modified:May 1, 1997 - v1
Checksum:i79F85E2ED25C1CA7
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y08827 Genomic DNA. Translation: CAA70061.1.
PIRiS72493.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y08827 Genomic DNA. Translation: CAA70061.1 .
PIRi S72493.

3D structure databases

ProteinModelPortali P78722.
SMRi P78722. Positions 46-605.
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. "Isolation and characterization of a laccase gene from Podospora anserina."
    Fernandez-Larrea J., Stahl U.
    Mol. Gen. Genet. 252:539-551(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 26003.

Entry informationi

Entry nameiLAC2_PODAS
AccessioniPrimary (citable) accession number: P78722
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 1997
Last modified: June 11, 2014
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Podospora anserina contains at least 3 laccase isozymes named I, II, and III. They differ in their substrate specificity, number of subunits, isoelectronic point and heat stability.

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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