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P48457

- PP2B_EMENI

UniProt

P48457 - PP2B_EMENI

Protein

Serine/threonine-protein phosphatase 2B catalytic subunit

Gene

cnaA

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 3 (16 Nov 2011)
      Previous versions | rss
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    Functioni

    Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin.

    Catalytic activityi

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

    Cofactori

    Binds 1 Fe3+ ion per subunit.By similarity
    Binds 1 zinc ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi112 – 1121IronBy similarity
    Metal bindingi114 – 1141IronBy similarity
    Metal bindingi140 – 1401IronBy similarity
    Metal bindingi140 – 1401ZincBy similarity
    Metal bindingi172 – 1721ZincBy similarity
    Active sitei173 – 1731Proton donorBy similarity
    Metal bindingi221 – 2211ZincBy similarity
    Metal bindingi303 – 3031ZincBy similarity

    GO - Molecular functioni

    1. calcium-dependent protein serine/threonine phosphatase activity Source: ASPGD
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. dephosphorylation Source: GOC
    2. G1/S transition of mitotic cell cycle Source: ASPGD

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Ligandi

    Calmodulin-binding, Iron, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein phosphatase 2B catalytic subunit (EC:3.1.3.16)
    Alternative name(s):
    Calmodulin-dependent calcineurin A subunit
    Gene namesi
    Name:cnaA
    ORF Names:AN8820
    OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
    Taxonomic identifieri227321 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000000560: Chromosome III

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 549549Serine/threonine-protein phosphatase 2B catalytic subunitPRO_0000058834Add
    BLAST

    Interactioni

    Subunit structurei

    Composed of two components (A and B), the A component is the catalytic subunit and the B component confers calcium sensitivity.

    Protein-protein interaction databases

    STRINGi162425.CADANIAP00006237.

    Structurei

    3D structure databases

    ProteinModelPortaliP48457.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0639.
    HOGENOMiHOG000172699.
    KOiK04348.
    OMAiMFWSPED.
    OrthoDBiEOG77M8X9.

    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.

    P48457-1 [UniParc]FASTAAdd to Basket

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    MDRNLARAVA DKQPVPEIDF TLHVMEDGTQ VSTLERVVKE VQAPALNKPS    50
    DDQFWDPEEP TKPNLQFLKQ HFYREGRLTE DQALWIIQAG TQILKSEPNL 100
    LEMDAPITVC GDVHGQYYDL MKLFEVGGDP AETRYLFLGD YVDRGYFSIE 150
    CVLYLWALKI WYPNTLWLLR GNHECRHLTD YFTFKLECKH KYSERIYEAC 200
    IESFCALPLA AVMNKQFLCI HGGLSPELHT LEDIKSIDRF REPPTHGLMC 250
    DILWADPLED FGQEKTGDYF IHNSVRGCSY FFSYPAACAF LEKNNLLSVI 300
    RAHEAQDAGY RMYRKTRTTG FPSVMTIFSA PNYLDVYNNK AAVLKYENNV 350
    MNIRQFNCTP HPYWLPNFMD VFTWSLPFVG EKITDMLIAI LNTCSKEELE 400
    DETPSTISPA EPSPPMPMDT VDTESTEFKR RAIKNKILAI GRLSRVFQVL 450
    REESERVTEL KTAAGGRLPA GTLMLGAEGI KQAITNFEDA RKVDLQNERL 500
    PPSHDEVVRR SEEERRIALD RAQHEADNDT GLATVARRIS MKIPSTTRR 549
    Length:549
    Mass (Da):63,007
    Last modified:November 16, 2011 - v3
    Checksum:iECD795FCBBDF4991
    GO

    Sequence cautioni

    The sequence AAA57873.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence EAA60108.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti386 – 3872ML → IV in AAA57873. (PubMed:8013455)Curated
    Sequence conflicti541 – 5411M → MVRRIR in AAA57873. (PubMed:8013455)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U13919 Genomic DNA. Translation: AAA57873.1. Different initiation.
    AACD01000162 Genomic DNA. Translation: EAA60108.1. Different initiation.
    BN001303 Genomic DNA. Translation: CBF77949.1.
    PIRiS46322.
    RefSeqiXP_682089.1. XM_676997.1.

    Genome annotation databases

    EnsemblFungiiCADANIAT00006237; CADANIAP00006237; CADANIAG00006237.
    GeneIDi2868443.
    KEGGiani:AN8820.2.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U13919 Genomic DNA. Translation: AAA57873.1 . Different initiation.
    AACD01000162 Genomic DNA. Translation: EAA60108.1 . Different initiation.
    BN001303 Genomic DNA. Translation: CBF77949.1 .
    PIRi S46322.
    RefSeqi XP_682089.1. XM_676997.1.

    3D structure databases

    ProteinModelPortali P48457.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 162425.CADANIAP00006237.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADANIAT00006237 ; CADANIAP00006237 ; CADANIAG00006237 .
    GeneIDi 2868443.
    KEGGi ani:AN8820.2.

    Phylogenomic databases

    eggNOGi COG0639.
    HOGENOMi HOG000172699.
    KOi K04348.
    OMAi MFWSPED.
    OrthoDBi EOG77M8X9.

    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. "The calmodulin-dependent protein phosphatase catalytic subunit (calcineurin A) is an essential gene in Aspergillus nidulans."
      Rasmussen C.D., Garen C., Brining S., Kincaid R.L., Means R.L., Means A.R.
      EMBO J. 13:2545-2552(1994) [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 nameiPP2B_EMENI
    AccessioniPrimary (citable) accession number: P48457
    Secondary accession number(s): C8V9L3, Q5ASB0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: November 16, 2011
    Last modified: October 1, 2014
    This is version 85 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