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Q9HFQ2

- PP2A1_EMENI

UniProt

Q9HFQ2 - PP2A1_EMENI

Protein

Serine/threonine-protein phosphatase PP2A catalytic subunit

Gene

pphA

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 78 (01 Oct 2014)
      Sequence version 2 (01 May 2007)
      Previous versions | rss
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    Functioni

    Involved in hyphal morphogenesis.

    Catalytic activityi

    [a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

    Cofactori

    Binds 2 manganese ions per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi77 – 771Manganese 1By similarity
    Metal bindingi79 – 791Manganese 1By similarity
    Metal bindingi105 – 1051Manganese 1By similarity
    Metal bindingi105 – 1051Manganese 2By similarity
    Metal bindingi137 – 1371Manganese 2By similarity
    Active sitei138 – 1381Proton donorBy similarity
    Metal bindingi187 – 1871Manganese 2By similarity
    Metal bindingi261 – 2611Manganese 2By similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. phosphoprotein phosphatase activity Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Ligandi

    Manganese, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein phosphatase PP2A catalytic subunit (EC:3.1.3.16)
    Short name:
    Protein phosphatase 2a
    Gene namesi
    Name:pphA
    ORF Names:AN6391
    OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
    Taxonomic identifieri227321 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000000560: Chromosome I

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 329329Serine/threonine-protein phosphatase PP2A catalytic subunitPRO_0000058868Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei329 – 3291Leucine methyl esterBy similarity

    Keywords - PTMi

    Methylation

    Proteomic databases

    PRIDEiQ9HFQ2.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9HFQ2.
    SMRiQ9HFQ2. Positions 30-329.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PPP phosphatase family. PP-2A subfamily.Curated

    Phylogenomic databases

    eggNOGiCOG0639.
    HOGENOMiHOG000172696.
    KOiK04382.
    OMAiQVKTLCD.
    OrthoDBiEOG7FFN29.

    Family and domain databases

    Gene3Di3.60.21.10. 1 hit.
    InterProiIPR004843. Calcineurin-like_PHP_apaH.
    IPR029052. Metallo-depent_PP-like.
    IPR006186. Ser/Thr-sp_prot-phosphatase.
    [Graphical view]
    PfamiPF00149. Metallophos. 1 hit.
    [Graphical view]
    PRINTSiPR00114. STPHPHTASE.
    SMARTiSM00156. PP2Ac. 1 hit.
    [Graphical view]
    SUPFAMiSSF56300. SSF56300. 1 hit.
    PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9HFQ2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDNNMEIDAA RSPEPHHLSP TTDPGSIPTL DGWIESLMTC KQLAEEDVRR    50
    LCDRAREVLQ EESNVQPVKC PVTVCGDIHG QFHDLMELFR IGGPNPDTNY 100
    LFMGDYVDRG YYSVETVTLL VCLKIRYPQR ITILRGNHES RQITQVYGFY 150
    DECLRKYGNA NVWKYFTDLF DYLPLTALIE NQIFCLHGGL SPSIDTLDNI 200
    RSLDRIQEVP HEGPMCDLLW SDPDDRCGWG ISPRGAGYTF GQDISEAFNH 250
    NNGLTLVARA HQLVMEGYNW SQDRNVVTIF SAPNYCYRCG NQAAIMEIDE 300
    HLKYTFLQFD PCPRAGEPMV SRRTPDYFL 329
    Length:329
    Mass (Da):37,665
    Last modified:May 1, 2007 - v2
    Checksum:i79308C0B11E95E23
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti133 – 1331I → T in CAC13980. (PubMed:11318104)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ291510 Genomic DNA. Translation: CAC13980.1.
    AACD01000108 Genomic DNA. Translation: EAA58413.1.
    BN001301 Genomic DNA. Translation: CBF69560.1.
    RefSeqiXP_663995.1. XM_658903.1.

    Genome annotation databases

    EnsemblFungiiCADANIAT00006588; CADANIAP00006588; CADANIAG00006588.
    GeneIDi2871291.
    KEGGiani:AN6391.2.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ291510 Genomic DNA. Translation: CAC13980.1 .
    AACD01000108 Genomic DNA. Translation: EAA58413.1 .
    BN001301 Genomic DNA. Translation: CBF69560.1 .
    RefSeqi XP_663995.1. XM_658903.1.

    3D structure databases

    ProteinModelPortali Q9HFQ2.
    SMRi Q9HFQ2. Positions 30-329.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q9HFQ2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADANIAT00006588 ; CADANIAP00006588 ; CADANIAG00006588 .
    GeneIDi 2871291.
    KEGGi ani:AN6391.2.

    Phylogenomic databases

    eggNOGi COG0639.
    HOGENOMi HOG000172696.
    KOi K04382.
    OMAi QVKTLCD.
    OrthoDBi EOG7FFN29.

    Family and domain databases

    Gene3Di 3.60.21.10. 1 hit.
    InterProi IPR004843. Calcineurin-like_PHP_apaH.
    IPR029052. Metallo-depent_PP-like.
    IPR006186. Ser/Thr-sp_prot-phosphatase.
    [Graphical view ]
    Pfami PF00149. Metallophos. 1 hit.
    [Graphical view ]
    PRINTSi PR00114. STPHPHTASE.
    SMARTi SM00156. PP2Ac. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56300. SSF56300. 1 hit.
    PROSITEi PS00125. SER_THR_PHOSPHATASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A type 2A protein phosphatase gene from Aspergillus nidulans is involved in hyphal morphogenesis."
      Kosmidou E., Lunness P., Doonan J.H.
      Curr. Genet. 39:25-34(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    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.

    Entry informationi

    Entry nameiPP2A1_EMENI
    AccessioniPrimary (citable) accession number: Q9HFQ2
    Secondary accession number(s): C8V0P5, Q5AZ89
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 11, 2003
    Last sequence update: May 1, 2007
    Last modified: October 1, 2014
    This is version 78 of the entry and version 2 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