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Q4DPB9

- Q4DPB9_TRYCC

UniProt

Q4DPB9 - Q4DPB9_TRYCC

Protein

Peptidyl-prolyl cis-trans isomerase

Gene

Tc00.1047053508577.140

Organism
Trypanosoma cruzi (strain CL Brener)
Status
Unreviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 72 (01 Oct 2014)
      Sequence version 1 (13 Sep 2005)
      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).UniRule annotationSAAS 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)
    Gene namesi
    ORF Names:Tc00.1047053508577.140Imported
    OrganismiTrypanosoma cruzi (strain CL Brener)Imported
    Taxonomic identifieri353153 [NCBI]
    Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosomaSchizotrypanum
    ProteomesiUP000002296: Unassembled WGS sequence

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1XO7X-ray1.61A/B/C/D30-194[»]
    1XQ7X-ray2.07A/B/C30-194[»]
    ProteinModelPortaliQ4DPB9.
    SMRiQ4DPB9. Positions 30-194.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ4DPB9.

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    KOiK03768.

    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.

    Q4DPB9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRYLLLSKVT QLLLLLLLML SAAVSARADP VVTDKVYFDI TIGDEPVGRV    50
    VIGLFGNDVP KTVENFKQLA SGENGFGYKG SIFHRVIRNF MIQGGDFTNF 100
    DGTGGKSIYG TRFDDENLKI KHFVGAVSMA NAGPNSNGSQ FFVTTAPTPW 150
    LDGRHVVFGK VVEGMDVVKK VENTKTGLND KPKKAVKIND CGVL 194
    Length:194
    Mass (Da):21,102
    Last modified:September 13, 2005 - v1
    Checksum:i688E90003CC958D5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAHK01000282 Genomic DNA. Translation: EAN94378.1.
    RefSeqiXP_816229.1. XM_811136.1.

    Genome annotation databases

    GeneIDi3548068.
    KEGGitcr:508577.140.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAHK01000282 Genomic DNA. Translation: EAN94378.1 .
    RefSeqi XP_816229.1. XM_811136.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1XO7 X-ray 1.61 A/B/C/D 30-194 [» ]
    1XQ7 X-ray 2.07 A/B/C 30-194 [» ]
    ProteinModelPortali Q4DPB9.
    SMRi Q4DPB9. Positions 30-194.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 3548068.
    KEGGi tcr:508577.140.

    Phylogenomic databases

    KOi K03768.

    Miscellaneous databases

    EvolutionaryTracei Q4DPB9.

    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. "Crystal structure of cyclophilin from Trypanosoma cruzi."
      Structural Genomics of Pathogenic Protozoa Consortium (SGPP)
      Caruthers J.M., Hol W.G.J.
      Submitted (OCT-2004) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.61 ANGSTROMS) OF 30-194.
    2. "Cyclophilin from Trypanosoma Cruzi Bound to Cyclosporin A."
      (Sgpp), Consortium Structural Genomics of Pathogenic Protozoa
      Caruthers J.M., Hol W.G.J.
      Submitted (OCT-2004) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS) OF 30-194.
    3. "The genome sequence of Trypanosoma cruzi, etiologic agent of Chagas disease."
      El-Sayed N.M.A., Myler P.J., Bartholomeu D.C., Nilsson D., Aggarwal G., Tran A.-N., Ghedin E., Worthey E.A., Delcher A.L., Blandin G., Westenberger S.J., Caler E., Cerqueira G.C., Branche C., Haas B., Anupama A., Arner E., Aslund L.
      , Attipoe P., Bontempi E., Bringaud F., Burton P., Cadag E., Campbell D.A., Carrington M., Crabtree J., Darban H., da Silveira J.F., de Jong P., Edwards K., Englund P.T., Fazelina G., Feldblyum T., Ferella M., Frasch A.C., Gull K., Horn D., Hou L., Huang Y., Kindlund E., Klingbeil M., Kluge S., Koo H., Lacerda D., Levin M.J., Lorenzi H., Louie T., Machado C.R., McCulloch R., McKenna A., Mizuno Y., Mottram J.C., Nelson S., Ochaya S., Osoegawa K., Pai G., Parsons M., Pentony M., Pettersson U., Pop M., Ramirez J.L., Rinta J., Robertson L., Salzberg S.L., Sanchez D.O., Seyler A., Sharma R., Shetty J., Simpson A.J., Sisk E., Tammi M.T., Tarleton R., Teixeira S., Van Aken S., Vogt C., Ward P.N., Wickstead B., Wortman J., White O., Fraser C.M., Stuart K.D., Andersson B.
      Science 309:409-415(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: CL BrenerImported.

    Entry informationi

    Entry nameiQ4DPB9_TRYCC
    AccessioniPrimary (citable) accession number: Q4DPB9
    Entry historyi
    Integrated into UniProtKB/TrEMBL: September 13, 2005
    Last sequence update: September 13, 2005
    Last modified: October 1, 2014
    This is version 72 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Keywords - Technical termi

    3D-structureImported, Complete proteome, Reference proteomeImported

    External Data

    Dasty 3