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P30303

- MPIP_EMENI

UniProt

P30303 - MPIP_EMENI

Protein

M-phase inducer phosphatase

Gene

nimT

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 89 (01 Oct 2014)
      Sequence version 2 (01 May 2007)
      Previous versions | rss
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    Functioni

    This protein functions as a dosage-dependent inducer in mitotic control. It is a tyrosine protein phosphatase required for progression of the cell cycle. It may directly dephosphorylate p34(cdc2) and activate the p34(cdc2) kinase activity.

    Catalytic activityi

    Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei421 – 4211By similarity

    GO - Molecular functioni

    1. protein tyrosine phosphatase activity Source: ASPGD

    GO - Biological processi

    1. G2/M transition of mitotic cell cycle Source: ASPGD
    2. mitotic nuclear division Source: UniProtKB-KW
    3. peptidyl-tyrosine dephosphorylation Source: GOC
    4. positive regulation of mitosis Source: ASPGD
    5. regulation of cyclin-dependent protein serine/threonine kinase activity Source: ASPGD

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    M-phase inducer phosphatase (EC:3.1.3.48)
    Gene namesi
    Name:nimT
    ORF Names:AN3941
    OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
    Taxonomic identifieri227321 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000000560: Chromosome II

    Subcellular locationi

    GO - Cellular componenti

    1. intracellular Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 556556M-phase inducer phosphatasePRO_0000198660Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi162425.CADANIAP00004753.

    Structurei

    3D structure databases

    ProteinModelPortaliP30303.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini371 – 474104RhodanesePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the MPI phosphatase family.Curated
    Contains 1 rhodanese domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5105.
    HOGENOMiHOG000215320.
    KOiK02555.
    OMAiQRTCERE.
    OrthoDBiEOG7VMPGR.

    Family and domain databases

    Gene3Di3.40.250.10. 1 hit.
    InterProiIPR000751. MPI_Phosphatase.
    IPR001763. Rhodanese-like_dom.
    [Graphical view]
    PfamiPF00581. Rhodanese. 1 hit.
    [Graphical view]
    PRINTSiPR00716. MPIPHPHTASE.
    SMARTiSM00450. RHOD. 1 hit.
    [Graphical view]
    SUPFAMiSSF52821. SSF52821. 1 hit.
    PROSITEiPS50206. RHODANESE_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P30303-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEHSSPLAAM QPPSVMLGHC FRSDAPTSYH GFSPLPGLGP GGFNFKDLSM    50
    KRSNGDYFGT KVVRGSSPTA SLAADLSQNF HIDQSPQVAT PRRSLFSACL 100
    LGNGNRRGVD DAMTTPPLPS SSPAPAMDIM DMSPLPHKPP FISTPEIELD 150
    SPTLESSPMD TTMMSTDGLV PDSPTVLPKD GKQERRRPTF LRPSLARSKA 200
    QSFQVGMTRP APESQGPPFK FQTNGINKTS SGVAASLEDM FGESPQRERP 250
    MMRINSTSGL NSRLRPPLGS GSHVRGNGSP SAASVRKSAH PNMRPRKQCR 300
    RSLSMYEHPE DVIADSEVSY TSNAPLQSIS DFEETQALQL PHFIPEEQAD 350
    NLPRIDKATL VDIKEGKYDN MFDNIMIIDC RFEYEYDGGH IVGAVNYNDK 400
    ENLAAELFAD PKPRTAIVFH CEYSVHRAPL MAKYIRHRDR AYNVDHYPQL 450
    SYPDMYILEG GYSGFFAEHR SLCYPQNYVE MSAKEHEFAC ERGLGKVKQR 500
    SKLSRAQTFA FGQQSPEMED SPTGRCRNNP GDRKLLASPF NDSPGSRFPG 550
    RRMLSY 556
    Length:556
    Mass (Da):61,626
    Last modified:May 1, 2007 - v2
    Checksum:iF558E77944A0BA59
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti353 – 3531P → G in CAA45885. (PubMed:1534750)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X64601 mRNA. Translation: CAA45885.1.
    AACD01000064 Genomic DNA. Translation: EAA59250.1.
    BN001302 Genomic DNA. Translation: CBF75046.1.
    PIRiS24395.
    RefSeqiXP_661545.1. XM_656453.1.

    Genome annotation databases

    EnsemblFungiiCADANIAT00004753; CADANIAP00004753; CADANIAG00004753.
    GeneIDi2873361.
    KEGGiani:AN3941.2.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X64601 mRNA. Translation: CAA45885.1 .
    AACD01000064 Genomic DNA. Translation: EAA59250.1 .
    BN001302 Genomic DNA. Translation: CBF75046.1 .
    PIRi S24395.
    RefSeqi XP_661545.1. XM_656453.1.

    3D structure databases

    ProteinModelPortali P30303.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 162425.CADANIAP00004753.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADANIAT00004753 ; CADANIAP00004753 ; CADANIAG00004753 .
    GeneIDi 2873361.
    KEGGi ani:AN3941.2.

    Phylogenomic databases

    eggNOGi COG5105.
    HOGENOMi HOG000215320.
    KOi K02555.
    OMAi QRTCERE.
    OrthoDBi EOG7VMPGR.

    Family and domain databases

    Gene3Di 3.40.250.10. 1 hit.
    InterProi IPR000751. MPI_Phosphatase.
    IPR001763. Rhodanese-like_dom.
    [Graphical view ]
    Pfami PF00581. Rhodanese. 1 hit.
    [Graphical view ]
    PRINTSi PR00716. MPIPHPHTASE.
    SMARTi SM00450. RHOD. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52821. SSF52821. 1 hit.
    PROSITEi PS50206. RHODANESE_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "An extra copy of nimEcyclinB elevates pre-MPF levels and partially suppresses mutation of nimTcdc25 in Aspergillus nidulans."
      O'Connell M.J., Osmani A.H., Morris N.R., Osmani S.A.
      EMBO J. 11:2139-2149(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: GB20.
    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 nameiMPIP_EMENI
    AccessioniPrimary (citable) accession number: P30303
    Secondary accession number(s): C8V635, Q5B689
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: May 1, 2007
    Last modified: October 1, 2014
    This is version 89 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