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Q25756

- Q25756_PLAFA

UniProt

Q25756 - Q25756_PLAFA

Protein

Peptidyl-prolyl cis-trans isomerase

Gene
N/A
Organism
Plasmodium falciparum
Status
Unreviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    PPIases accelerate the folding of proteins.UniRule annotation
    PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.UniRule annotation

    Catalytic activityi

    Peptidylproline (omega=180) = peptidylproline (omega=0).SAAS annotation

    GO - Molecular functioni

    1. peptidyl-prolyl cis-trans isomerase activity Source: UniProtKB-KW

    GO - Biological processi

    1. protein folding Source: UniProtKB-KW

    Keywords - Molecular functioni

    Isomerase, RotamaseUniRule annotationSAAS annotation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peptidyl-prolyl cis-trans isomeraseUniRule annotation (EC:5.2.1.8UniRule annotation)
    OrganismiPlasmodium falciparumImported
    Taxonomic identifieri5833 [NCBI]
    Taxonomic lineageiEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiumPlasmodium (Laverania)

    PTM / Processingi

    Proteomic databases

    PRIDEiQ25756.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1QNGX-ray2.10A2-171[»]
    1QNHX-ray2.10A/B2-171[»]
    ProteinModelPortaliQ25756.
    SMRiQ25756. Positions 2-171.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ25756.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the cyclophilin-type PPIase family.UniRule annotation
    Contains 1 PPIase cyclophilin-type domain.UniRule annotation
    Contains PPIase cyclophilin-type domain.SAAS annotation

    Phylogenomic databases

    eggNOGiCOG0652.

    Family and domain databases

    Gene3Di2.40.100.10. 1 hit.
    InterProiIPR029000. Cyclophilin-like_dom.
    IPR024936. Cyclophilin-type_PPIase.
    IPR020892. Cyclophilin-type_PPIase_CS.
    IPR002130. Cyclophilin-type_PPIase_dom.
    [Graphical view]
    PfamiPF00160. Pro_isomerase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001467. Peptidylpro_ismrse. 1 hit.
    PRINTSiPR00153. CSAPPISMRASE.
    SUPFAMiSSF50891. SSF50891. 1 hit.
    PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
    PS50072. CSA_PPIASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q25756-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSKRSKVFFD ISIDNSNAGR IIFELFSDIT PRTCENFRAL CTGEKIGSRG    50
    KNLHYKNSIF HRIIPQFMCQ GGDITNGNGS GGESIYGRSF TDENFNMKHD 100
    QPGLLSMANA GPNTNSSQFF ITLVPCPWLD GKHVVFGKVI EGMNVVREME 150
    KEGAKSGYVK RSVVITDCGE L 171
    Length:171
    Mass (Da):18,953
    Last modified:November 1, 1996 - v1
    Checksum:i0AF10F640A2C1AB4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U33869 mRNA. Translation: AAC41390.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U33869 mRNA. Translation: AAC41390.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1QNG X-ray 2.10 A 2-171 [» ]
    1QNH X-ray 2.10 A/B 2-171 [» ]
    ProteinModelPortali Q25756.
    SMRi Q25756. Positions 2-171.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q25756.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG0652.

    Miscellaneous databases

    EvolutionaryTracei Q25756.

    Family and domain databases

    Gene3Di 2.40.100.10. 1 hit.
    InterProi IPR029000. Cyclophilin-like_dom.
    IPR024936. Cyclophilin-type_PPIase.
    IPR020892. Cyclophilin-type_PPIase_CS.
    IPR002130. Cyclophilin-type_PPIase_dom.
    [Graphical view ]
    Pfami PF00160. Pro_isomerase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001467. Peptidylpro_ismrse. 1 hit.
    PRINTSi PR00153. CSAPPISMRASE.
    SUPFAMi SSF50891. SSF50891. 1 hit.
    PROSITEi PS00170. CSA_PPIASE_1. 1 hit.
    PS50072. CSA_PPIASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Detailed characterization of a cyclophilin from the human malaria parasite Plasmodium falciparum."
      Berriman M., Fairlamb A.H.
      Biochem. J. 334:437-445(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE.
      Strain: FCB1Imported.
    2. "The three-dimensional structure of a Plasmodium falciparum cyclophilin in complex with the potent anti-malarial cyclosporin A."
      Peterson M.R., Hall D.R., Berriman M., Nunes J.A., Leonard G.A., Fairlamb A.H., Hunter W.N.
      J. Mol. Biol. 298:123-133(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 2-171.

    Entry informationi

    Entry nameiQ25756_PLAFA
    AccessioniPrimary (citable) accession number: Q25756
    Entry historyi
    Integrated into UniProtKB/TrEMBL: November 1, 1996
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 83 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Keywords - Technical termi

    3D-structureImported

    External Data

    Dasty 3