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Q05681

- PP2B_NEUCR

UniProt

Q05681 - PP2B_NEUCR

Protein

Serine/threonine-protein phosphatase 2B catalytic subunit

Gene

cna-1

Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 2 (04 Dec 2007)
      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 bindingi128 – 1281IronBy similarity
    Metal bindingi130 – 1301IronBy similarity
    Metal bindingi156 – 1561IronBy similarity
    Metal bindingi156 – 1561ZincBy similarity
    Metal bindingi188 – 1881ZincBy similarity
    Active sitei189 – 1891Proton donorBy similarity
    Metal bindingi237 – 2371ZincBy similarity
    Metal bindingi319 – 3191ZincBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. adaptation of signaling pathway by response to pheromone involved in conjugation with cellular fusion Source: EnsemblFungi
    2. cellular ion homeostasis Source: EnsemblFungi
    3. fungal-type cell wall organization Source: EnsemblFungi

    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:cna-1
    ORF Names:99H12.070, NCU03804
    OrganismiNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
    Taxonomic identifieri367110 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora
    ProteomesiUP000001805: Chromosome 2, Linkage Group V

    Subcellular locationi

    GO - Cellular componenti

    1. calcineurin complex Source: EnsemblFungi

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 558558Serine/threonine-protein phosphatase 2B catalytic subunitPRO_0000058833Add
    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

    STRINGi5141.NCU03804.1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ05681.
    SMRiQ05681. Positions 46-410.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0639.
    HOGENOMiHOG000172699.
    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.

    Q05681-1 [UniParc]FASTAAdd to Basket

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    MESNNGTGAP GAFHTQQVDN AIRAIQHKRP LPEIDFTIHT MEDGSQVSTM    50
    ERVCKDVQAP AMFKPSDEQF FEDETHTKPD IQFLKQHFYR EGRLTEEQAL 100
    WIIREGTKLL RAEPNLLEMD APITVCGDVH GQYYDLMKLF EVGGDPAETR 150
    YLFLGDYVDR GYFSIECVLY LWALKIHYPK TLWLLRGNHE CRHLTDYFTF 200
    KLECKHKYSE AIYEACMESF CCLPLAAVMN KQFLCIHGGL SPELHTLDDI 250
    RNIDRFREPP TQGLMCDILW ADPLEDFGQE KTTDFFVHNH VRGCSYFFSY 300
    SAACHFLEKN NLLSIIRAHE AQDAGYRMYR KTRTTGFPSV MTIFSAPNYL 350
    DVYNNKAAVL KYENNVMNIR QFNCTPHPYW LPNFMDVFTW SLPFVGEKIT 400
    DMLIAILSTC SEEELREDSA TTSPGSASPA LPSAANQDPD SIEFKRRAIK 450
    NKILAIGRLS RVFQVLREES ERVTELKTVS GGRLPAGTLM LGAEGIKNAI 500
    SSFEDARKVD LQNERLPPSH DEVVKMQDEE RAQALERATR EADNDKKLQT 550
    LSRRLSTS 558
    Length:558
    Mass (Da):63,914
    Last modified:December 4, 2007 - v2
    Checksum:iFDE74D72A000A55E
    GO

    Sequence cautioni

    The sequence AAA33565.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAC18243.1 differs from that shown. Reason: Erroneous gene model prediction.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M73032 mRNA. Translation: AAA33565.1. Different initiation.
    AL451018 Genomic DNA. Translation: CAC18243.1. Sequence problems.
    CM002240 Genomic DNA. Translation: ESA42471.1.
    PIRiA40942.

    Genome annotation databases

    EnsemblFungiiEFNCRT00000003478; EFNCRP00000003478; EFNCRG00000003474.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M73032 mRNA. Translation: AAA33565.1 . Different initiation.
    AL451018 Genomic DNA. Translation: CAC18243.1 . Sequence problems.
    CM002240 Genomic DNA. Translation: ESA42471.1 .
    PIRi A40942.

    3D structure databases

    ProteinModelPortali Q05681.
    SMRi Q05681. Positions 46-410.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5141.NCU03804.1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii EFNCRT00000003478 ; EFNCRP00000003478 ; EFNCRG00000003474 .

    Phylogenomic databases

    eggNOGi COG0639.
    HOGENOMi HOG000172699.
    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. "Calmodulin-dependent protein phosphatase from Neurospora crassa. Molecular cloning and expression of recombinant catalytic subunit."
      Higuchi S., Tamura J., Rathna Giri P., Polli J.W., Kincaid R.L.
      J. Biol. Chem. 266:18104-18112(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "What's in the genome of a filamentous fungus? Analysis of the Neurospora genome sequence."
      Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.
      Nucleic Acids Res. 31:1944-1954(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
    3. "The genome sequence of the filamentous fungus Neurospora crassa."
      Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D.
      , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.
      Nature 422:859-868(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.

    Entry informationi

    Entry nameiPP2B_NEUCR
    AccessioniPrimary (citable) accession number: Q05681
    Secondary accession number(s): Q1K7G7, Q9HEE2, V5INZ9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: December 4, 2007
    Last modified: October 1, 2014
    This is version 87 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