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Q4QBH1

- Q4QBH1_LEIMA

UniProt

Q4QBH1 - Q4QBH1_LEIMA

Protein

Peptidyl-prolyl cis-trans isomerase

Gene

CYP11

Organism
Leishmania major
Status
Unreviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 79 (01 Oct 2014)
      Sequence version 1 (19 Jul 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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei74 – 741PhosphateImported

    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
    Name:CYP11Imported
    ORF Names:LMJF_23_0050Imported
    OrganismiLeishmania majorImported
    Taxonomic identifieri5664 [NCBI]
    Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmania
    ProteomesiUP000000542: Chromosome 23

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2HQJX-ray2.00A22-199[»]
    ProteinModelPortaliQ4QBH1.
    SMRiQ4QBH1. Positions 22-199.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ4QBH1.

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    HOGENOMiHOG000065980.
    KOiK01802.
    OMAiLGCLSMA.

    Family and domain databases

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

    Sequencei

    Sequence statusi: Complete.

    Q4QBH1-1 [UniParc]FASTAAdd to Basket

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    MSRTSVPPKV GQRPGIGVEK TTNPKVFFDI SIDNKAAGRI VMELYADTVP    50
    KTAENFRALC TGEKGKGRSG KPLHYKSSVF HRVIPNFMIQ GGDFTRGNGT 100
    GGESIYGTTF RDESFSGKAG RHTGLGCLSM ANAGPNTNGS QFFICTAATP 150
    WLDGKHVVFG RVIDGLDVVK KVERLGSSSG KTRSRIVVSD CGEVAADKSK 200
    GQRPPQQQHQ PAKASADMKR AADKKAVAEK LLASSPAAEG QKALSAKKET 250
    PPQVAAPSEA KKRMRAVDEE ETRLARLREK KAKLAALRSS AAGNE 295
    Length:295
    Mass (Da):31,497
    Last modified:July 19, 2005 - v1
    Checksum:i69AAC0FBD9533143
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    FR796419 Genomic DNA. Translation: CAJ03831.1.
    RefSeqiXP_001683327.1. XM_001683275.1.

    Genome annotation databases

    EnsemblProtistsiLmjF.23.0050:mRNA; LmjF.23.0050:pep; LmjF.23.0050.
    GeneIDi5651954.
    KEGGilma:LMJF_23_0050.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    FR796419 Genomic DNA. Translation: CAJ03831.1 .
    RefSeqi XP_001683327.1. XM_001683275.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2HQJ X-ray 2.00 A 22-199 [» ]
    ProteinModelPortali Q4QBH1.
    SMRi Q4QBH1. Positions 22-199.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblProtistsi LmjF.23.0050:mRNA ; LmjF.23.0050:pep ; LmjF.23.0050 .
    GeneIDi 5651954.
    KEGGi lma:LMJF_23_0050.

    Phylogenomic databases

    HOGENOMi HOG000065980.
    KOi K01802.
    OMAi LGCLSMA.

    Miscellaneous databases

    EvolutionaryTracei Q4QBH1.

    Family and domain databases

    Gene3Di 2.40.100.10. 1 hit.
    InterProi IPR029000. Cyclophilin-like_dom.
    IPR020892. Cyclophilin-type_PPIase_CS.
    IPR002130. Cyclophilin-type_PPIase_dom.
    [Graphical view ]
    Pfami PF00160. Pro_isomerase. 1 hit.
    [Graphical view ]
    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. "The genome of the kinetoplastid parasite, Leishmania major."
      Ivens A.C., Peacock C.S., Worthey E.A., Murphy L., Aggarwal G., Berriman M., Sisk E., Rajandream M.A., Adlem E., Aert R., Anupama A., Apostolou Z., Attipoe P., Bason N., Bauser C., Beck A., Beverley S.M., Bianchettin G.
      , Borzym K., Bothe G., Bruschi C.V., Collins M., Cadag E., Ciarloni L., Clayton C., Coulson R.M.R., Cronin A., Cruz A.K., Davies R.M., De Gaudenzi J., Dobson D.E., Duesterhoeft A., Fazelina G., Fosker N., Frasch A.C., Fraser A., Fuchs M., Gabel C., Goble A., Goffeau A., Harris D., Hertz-Fowler C., Hilbert H., Horn D., Huang Y., Klages S., Knights A., Kube M., Larke N., Litvin L., Lord A., Louie T., Marra M., Masuy D., Matthews K., Michaeli S., Mottram J.C., Mueller-Auer S., Munden H., Nelson S., Norbertczak H., Oliver K., O'neil S., Pentony M., Pohl T.M., Price C., Purnelle B., Quail M.A., Rabbinowitsch E., Reinhardt R., Rieger M., Rinta J., Robben J., Robertson L., Ruiz J.C., Rutter S., Saunders D., Schaefer M., Schein J., Schwartz D.C., Seeger K., Seyler A., Sharp S., Shin H., Sivam D., Squares R., Squares S., Tosato V., Vogt C., Volckaert G., Wambutt R., Warren T., Wedler H., Woodward J., Zhou S., Zimmermann W., Smith D.F., Blackwell J.M., Stuart K.D., Barrell B.G., Myler P.J.
      Science 309:436-442(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: MHOM/IL/81/FriedlinImported.
    2. "Cyclophilin from Leishmania major."
      Arakaki T.L., Merritt E.A.
      Submitted (JUL-2006) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 22-199.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: FriedlinImported.

    Entry informationi

    Entry nameiQ4QBH1_LEIMA
    AccessioniPrimary (citable) accession number: Q4QBH1
    Entry historyi
    Integrated into UniProtKB/TrEMBL: July 19, 2005
    Last sequence update: July 19, 2005
    Last modified: October 1, 2014
    This is version 79 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