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Protein

Laccase-2

Gene

LAC2

Organism
Podospora anserina (Pleurage anserina)
Status
Reviewed-Annotation score: 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

Cu cationBy similarityNote: Binds 4 Cu cations per monomer.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi138Copper 1; type 2By similarity1
Metal bindingi140Copper 2; type 3By similarity1
Metal bindingi183Copper 2; type 3By similarity1
Metal bindingi185Copper 3; type 3By similarity1
Metal bindingi476Copper 4; type 1By similarity1
Metal bindingi479Copper 1; type 2By similarity1
Metal bindingi481Copper 3; type 3By similarity1
Metal bindingi548Copper 3; type 3By similarity1
Metal bindingi549Copper 4; type 1By similarity1
Metal bindingi550Copper 2; type 3By similarity1
Metal bindingi554Copper 4; type 1By similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Lignin degradation, Melanin biosynthesis

Keywords - Ligandi

Copper, Metal-binding

Protein family/group databases

CAZyiAA1. Auxiliary Activities 1.

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

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Sequence analysisAdd BLAST23
PropeptideiPRO_000000293124 – 48Sequence analysisAdd BLAST25
ChainiPRO_000000293249 – 605Laccase-2Add BLAST557
PropeptideiPRO_0000002933606 – 621Sequence analysisAdd BLAST16

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi133N-linked (GlcNAc...)Sequence analysis1
Glycosylationi261N-linked (GlcNAc...)Sequence analysis1
Glycosylationi276N-linked (GlcNAc...)Sequence analysis1
Glycosylationi289N-linked (GlcNAc...)Sequence analysis1
Glycosylationi325N-linked (GlcNAc...)Sequence analysis1
Glycosylationi334N-linked (GlcNAc...)Sequence analysis1
Glycosylationi401N-linked (GlcNAc...)Sequence analysis1
Glycosylationi421N-linked (GlcNAc...)Sequence analysis1
Glycosylationi441N-linked (GlcNAc...)Sequence analysis1

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.

Protein-protein interaction databases

STRINGi515849.XP_001904217.1.

Structurei

3D structure databases

ProteinModelPortaliP78722.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini78 – 201Plastocyanin-like 1Add BLAST124
Domaini210 – 367Plastocyanin-like 2Add BLAST158
Domaini430 – 566Plastocyanin-like 3Add BLAST137

Sequence similaritiesi

Belongs to the multicopper oxidase family.Curated
Contains 3 plastocyanin-like domains.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiKOG1263. Eukaryota.
COG2132. LUCA.

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.
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

        10         20         30         40         50
MMKSFFSAAA LLLGLVAPSA VLAAPSLPGV PREVTRDLLR PVEERQSSCH
60 70 80 90 100
TAANRACWAP GFDINTDYEV STPNTGVTRT YTLTLTEVDN WLGPDGVVKQ
110 120 130 140 150
KVMLVNGDIF GPTITANWGD WIQVNVINNL RTNGTSIHWH GLHQKGTNMH
160 170 180 190 200
DGANGVTECP IPPKGGSRIY RFRAQQYGTS WYHSHFSAQY GNGVVGTIVV
210 220 230 240 250
NGPASVPYDI DLGVFPITDY YHKPADVLVE ETMNGGPPPS DTVLFKGHGK
260 270 280 290 300
NPQTGAGKFA NVTLTPGKRH RLRIINTSTH DHFQLKLQNH TMTIIAADMV
310 320 330 340 350
PVQAQTVDSL FLAVGQRYDV TIDANKSVGN YWFNATFGGG LACGASLNPH
360 370 380 390 400
PAAVFRYQGA PNTLPTNIGT PAADANCMDL NNLTPVVSRS VPTSGFTPRP
410 420 430 440 450
NNTLPVSLTL GGTPLFVWKV NGSSINVDWD KPIVDYVIAQ NTSYPPQANV
460 470 480 490 500
ITVNSVNQWT YWLIENDPTG PFSIPHPMHL HGHDFLVVGR SPDQPAGVPQ
510 520 530 540 550
TRYRFNPATD MALLKSSNPV RRDVAMLPAN GWLLIAFKSD NPGAWLFHCH
560 570 580 590 600
IAWHVSGGLS VQYLERPNDL RNGFSQADKN QHNNNCNAWR AYWPTNPFPK
610 620
IDSGLKVKKW VGEHPDWYIK N
Length:621
Mass (Da):68,129
Last modified:May 1, 1997 - v1
Checksum:i79F85E2ED25C1CA7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y08827 Genomic DNA. Translation: CAA70061.1.
PIRiS72493.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y08827 Genomic DNA. Translation: CAA70061.1.
PIRiS72493.

3D structure databases

ProteinModelPortaliP78722.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi515849.XP_001904217.1.

Protein family/group databases

CAZyiAA1. Auxiliary Activities 1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG1263. Eukaryota.
COG2132. LUCA.

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.
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...

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: October 5, 2016
This is version 94 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

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.