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Reviewed, UniProtKB/Swiss-Prot P78722 (LAC2_PODAN)

Last modified November 24, 2009. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Laccase-2
    EC=1.10.3.2
Alternative name(s):
    Laccase II
    Benzenediol:oxygen oxidoreductase 2
    Urishiol oxidase 2
    Diphenol oxidase 2
    Laccase C
Gene names
Name: LAC2
OrganismPodospora anserina
Taxonomic identifier5145 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Sordariales › Lasiosphaeriaceae › Podospora

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Protein attributes

Sequence length621 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

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 activity

4 benzenediol + O2 = 4 benzosemiquinone + 2 H2O.

Cofactor

Binds 4 copper ions per monomer By similarity.

Subunit structure

Monomer.

Subcellular location

Secreted.

Developmental stage

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

Induction

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

Post-translational modification

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

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.

Sequence similarities

Belongs to the multicopper oxidase family.

Contains 3 plastocyanin-like domains.

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Ontologies

Keywords
   Biological processLignin degradation
Melanin biosynthesis
   Cellular componentSecreted
   DomainRepeat
Signal
   LigandCopper
Metal-binding
   Molecular functionOxidoreductase
   PTMGlycoprotein
Gene Ontology (GO)
   Biological processlignin catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

melanin biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncopper ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

laccase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Propeptide24 – 4825 Potential
PRO_0000002931
Chain49 – 605557Laccase-2
PRO_0000002932
Propeptide606 – 62116 Potential
PRO_0000002933

Regions

Domain78 – 201124Plastocyanin-like 1
Domain210 – 367158Plastocyanin-like 2
Domain430 – 566137Plastocyanin-like 3

Sites

Metal binding1381Copper 1; type 2 By similarity
Metal binding1401Copper 2; type 3 By similarity
Metal binding1831Copper 2; type 3 By similarity
Metal binding1851Copper 3; type 3 By similarity
Metal binding4761Copper 4; type 1 By similarity
Metal binding4791Copper 1; type 2 By similarity
Metal binding4811Copper 3; type 3 By similarity
Metal binding5481Copper 3; type 3 By similarity
Metal binding5491Copper 4; type 1 By similarity
Metal binding5501Copper 2; type 3 By similarity
Metal binding5541Copper 4; type 1 By similarity

Amino acid modifications

Glycosylation1331N-linked (GlcNAc...) Potential
Glycosylation2611N-linked (GlcNAc...) Potential
Glycosylation2761N-linked (GlcNAc...) Potential
Glycosylation2891N-linked (GlcNAc...) Potential
Glycosylation3251N-linked (GlcNAc...) Potential
Glycosylation3341N-linked (GlcNAc...) Potential
Glycosylation4011N-linked (GlcNAc...) Potential
Glycosylation4211N-linked (GlcNAc...) Potential
Glycosylation4411N-linked (GlcNAc...) Potential

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Sequences

Sequence LengthMass (Da)Tools
P78722-1 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 79F85E2ED25C1CA7

FASTA62168,129
        10         20         30         40         50         60 
MMKSFFSAAA LLLGLVAPSA VLAAPSLPGV PREVTRDLLR PVEERQSSCH TAANRACWAP 

        70         80         90        100        110        120 
GFDINTDYEV STPNTGVTRT YTLTLTEVDN WLGPDGVVKQ KVMLVNGDIF GPTITANWGD 

       130        140        150        160        170        180 
WIQVNVINNL RTNGTSIHWH GLHQKGTNMH DGANGVTECP IPPKGGSRIY RFRAQQYGTS 

       190        200        210        220        230        240 
WYHSHFSAQY GNGVVGTIVV NGPASVPYDI DLGVFPITDY YHKPADVLVE ETMNGGPPPS 

       250        260        270        280        290        300 
DTVLFKGHGK NPQTGAGKFA NVTLTPGKRH RLRIINTSTH DHFQLKLQNH TMTIIAADMV 

       310        320        330        340        350        360 
PVQAQTVDSL FLAVGQRYDV TIDANKSVGN YWFNATFGGG LACGASLNPH PAAVFRYQGA 

       370        380        390        400        410        420 
PNTLPTNIGT PAADANCMDL NNLTPVVSRS VPTSGFTPRP NNTLPVSLTL GGTPLFVWKV 

       430        440        450        460        470        480 
NGSSINVDWD KPIVDYVIAQ NTSYPPQANV ITVNSVNQWT YWLIENDPTG PFSIPHPMHL 

       490        500        510        520        530        540 
HGHDFLVVGR SPDQPAGVPQ TRYRFNPATD MALLKSSNPV RRDVAMLPAN GWLLIAFKSD 

       550        560        570        580        590        600 
NPGAWLFHCH IAWHVSGGLS VQYLERPNDL RNGFSQADKN QHNNNCNAWR AYWPTNPFPK 

       610        620 
IDSGLKVKKW VGEHPDWYIK N

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References

[1]"Isolation and characterization of a laccase gene from Podospora anserina."
Fernandez-Larrea J., Stahl U.
Mol. Gen. Genet. 252:539-551(1996) [PubMed: 8914515] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 26003.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Y08827 Genomic DNA. Translation: CAA70061.1.
PIRS72493.

3D structure databases

SMRP78722. Positions 46-605.
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.10.3.2. 142554.

Family and domain databases

InterProIPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR002355. Cu_oxidase_Cu_BS.
IPR008972. Cupredoxin.
[Graphical view]
Gene3DG3DSA:2.60.40.420. Cupredoxin. 3 hits.
PfamPF00394. Cu-oxidase. 1 hit.
PF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 1 hit.
[Graphical view]
PROSITEPS00079. MULTICOPPER_OXIDASE1. 1 hit.
PS00080. MULTICOPPER_OXIDASE2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameLAC2_PODAN
AccessionPrimary (citable) accession number: P78722
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 1997
Last modified: November 24, 2009
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents