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P17489

- LAC1_EMENI

UniProt

P17489 - LAC1_EMENI

Protein

Laccase-1

Gene

yA

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 3 (26 May 2009)
      Previous versions | rss
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    Functioni

    Required for the conversion of the yellow polyketide pigment synthesized by wA to the conidial green pigment.1 Publication

    Catalytic activityi

    4 benzenediol + O2 = 4 benzosemiquinone + 2 H2O.

    Cofactori

    Binds 4 copper ions per subunit. The copper ions are bound as 3 distinct Cu centers known as type 1 or blue, type 2 or normal, and type 3 or coupled binuclear By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi79 – 791Copper 1; type 2Curated
    Metal bindingi81 – 811Copper 2; type 3Curated
    Metal bindingi123 – 1231Copper 2; type 3Curated
    Metal bindingi125 – 1251Copper 3; type 3Curated
    Metal bindingi508 – 5081Copper 4; type 1Curated
    Metal bindingi511 – 5111Copper 1; type 2Curated
    Metal bindingi513 – 5131Copper 3; type 3Curated
    Metal bindingi585 – 5851Copper 3; type 3Curated
    Metal bindingi586 – 5861Copper 4; type 1Curated
    Metal bindingi587 – 5871Copper 2; type 3Curated
    Metal bindingi591 – 5911Copper 4; type 1Curated
    Metal bindingi596 – 5961Copper 4; type 1Curated

    GO - Molecular functioni

    1. copper ion binding Source: InterPro
    2. hydroquinone:oxygen oxidoreductase activity Source: ASPGD

    GO - Biological processi

    1. conidium formation Source: ASPGD
    2. pigment metabolic process involved in developmental pigmentation Source: ASPGD
    3. sporulation resulting in formation of a cellular spore Source: UniProtKB-KW

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Conidiation, Sporulation

    Keywords - Ligandi

    Copper, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Laccase-1 (EC:1.10.3.2)
    Alternative name(s):
    Benzenediol:oxygen oxidoreductase 1
    Conidial laccase
    Diphenol oxidase 1
    Laccase I
    Urishiol oxidase 1
    Gene namesi
    Name:yA
    ORF Names:AN6635
    OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
    Taxonomic identifieri227321 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000000560: Chromosome I

    Subcellular locationi

    Secreted Curated

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Chaini21 – 609589Laccase-1PRO_0000002927Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi75 – 751N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi257 – 2571N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi268 – 2681N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi403 – 4031N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi443 – 4431N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi486 – 4861N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi531 – 5311N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi546 – 5461N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Expressioni

    Developmental stagei

    Specifically expressed late during asexual development.1 Publication

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini45 – 14197Plastocyanin-like 1Add
    BLAST
    Domaini270 – 372103Plastocyanin-like 2Add
    BLAST
    Domaini463 – 602140Plastocyanin-like 3Add
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiCOG2132.
    HOGENOMiHOG000168741.
    OMAiCHITTHQ.
    OrthoDBiEOG718KNW.

    Family and domain databases

    Gene3Di2.60.40.420. 4 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. 4 hits.
    PROSITEiPS00080. MULTICOPPER_OXIDASE2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P17489-1 [UniParc]FASTAAdd to Basket

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    MYLSTVLFPL LALNLGLSHA RFVRETLELT WEYGSPNGGT PREMVFTNGE    50
    YPGPDLIFDE DDDVEVLVIN NLPFNTTVHW HGLEMRETPE ADGVPGLTQT 100
    PIEPGATFTY RFRAYPAGTF WYHSHYKGLM QDGQVGAMYI RRKPDALRPY 150
    AVITEDPREL AEIQYAEDNP YLMLATDWTY LTSAEYHNIE VESGYNVFCV 200
    DSLLINGRGS VYCPGYQYLE EVSDDGLTAV LEGTHLTEKG CLQPDLHNVQ 250
    GDYGPWNLSA VPTEVVFNCT PSSVEPPVIY VDPEFNGWVS LNFIGGAAQK 300
    AITFSVDNHP MWVYEVDGQF VEPREVEMVG VYSGARYAVM IKLDQTPGDY 350
    AIRIAVNGGD QVMSVYAILS YVNQDWIHRE NVPKAAIGPH TDTVGYMNYG 400
    GGNTSADVRQ LLFTENLPAF GVPPPPPSSE VSTTLRTGMI RVNNSYSWSL 450
    GNNVLYEPEM TSSTPLLFEP DPLAVIAPKY ALTTENNTWV DIVLEITADP 500
    RDLIHPPHPI HKHGNRAYII GNGVGKFRWE NVSAAEAEVP DLFYVNETAA 550
    LRDTFVTDFF DSRLMDGAWI VIRYFVQDKF PSILHCHIAS HQMGGMALAL 600
    LDGVDVWDS 609
    Length:609
    Mass (Da):67,981
    Last modified:May 26, 2009 - v3
    Checksum:i529A20B2DD9AA73E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti225 – 2295DGLTA → TALLS in CAA36787. (PubMed:2192364)Curated
    Sequence conflicti359 – 3591G → A in CAA36787. (PubMed:2192364)Curated
    Sequence conflicti421 – 4211G → A in CAA36787. (PubMed:2192364)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52552 Genomic DNA. Translation: CAA36787.1.
    AACD01000110 Genomic DNA. Translation: EAA58164.1.
    BN001301 Genomic DNA. Translation: CBF71142.1.
    PIRiS10149. KSASL1.
    RefSeqiXP_664239.1. XM_659147.1.

    Genome annotation databases

    EnsemblFungiiCADANIAT00007416; CADANIAP00007416; CADANIAG00007416.
    GeneIDi2870381.
    KEGGiani:AN6635.2.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52552 Genomic DNA. Translation: CAA36787.1 .
    AACD01000110 Genomic DNA. Translation: EAA58164.1 .
    BN001301 Genomic DNA. Translation: CBF71142.1 .
    PIRi S10149. KSASL1.
    RefSeqi XP_664239.1. XM_659147.1.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADANIAT00007416 ; CADANIAP00007416 ; CADANIAG00007416 .
    GeneIDi 2870381.
    KEGGi ani:AN6635.2.

    Phylogenomic databases

    eggNOGi COG2132.
    HOGENOMi HOG000168741.
    OMAi CHITTHQ.
    OrthoDBi EOG718KNW.

    Family and domain databases

    Gene3Di 2.60.40.420. 4 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. 4 hits.
    PROSITEi PS00080. MULTICOPPER_OXIDASE2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence and molecular structure of the Aspergillus nidulans yA (laccase I) gene."
      Aramayo R., Timberlake W.E.
      Nucleic Acids Res. 18:3415-3415(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139 and Winter.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
    3. "The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
      Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G.
      , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
      Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENOME REANNOTATION.
      Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
    4. "Molecular characterization of the Aspergillus nidulans yA locus."
      O'Hara E.B., Timberlake W.E.
      Genetics 121:249-254(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DEVELOPMENTAL STAGE.

    Entry informationi

    Entry nameiLAC1_EMENI
    AccessioniPrimary (citable) accession number: P17489
    Secondary accession number(s): C8V1C0, Q5AYJ5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: May 26, 2009
    Last modified: October 1, 2014
    This is version 106 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3