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Q26548

- PPIE_SCHMA

UniProt

Q26548 - PPIE_SCHMA

Protein

Peptidyl-prolyl cis-trans isomerase E

Gene
N/A
Organism
Schistosoma mansoni (Blood fluke)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 80 (01 Oct 2014)
      Sequence version 2 (01 Jan 1998)
      Previous versions | rss
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    Functioni

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

    Catalytic activityi

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

    Enzyme regulationi

    Binds cyclosporin A (CsA). CsA mediates some of its effects via an inhibitory action on PPIase.

    GO - Molecular functioni

    1. nucleotide binding Source: InterPro
    2. peptide binding Source: UniProtKB-KW
    3. peptidyl-prolyl cis-trans isomerase activity Source: UniProtKB-KW
    4. RNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. protein folding Source: UniProtKB-KW

    Keywords - Molecular functioni

    Isomerase, Rotamase

    Keywords - Ligandi

    Cyclosporin, RNA-binding

    Enzyme and pathway databases

    BRENDAi5.2.1.8. 5608.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peptidyl-prolyl cis-trans isomerase E (EC:5.2.1.8)
    Short name:
    PPIase E
    Alternative name(s):
    Cyclophilin E
    Rotamase E
    OrganismiSchistosoma mansoni (Blood fluke)
    Taxonomic identifieri6183 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaPlatyhelminthesTrematodaDigeneaStrigeididaSchistosomatoideaSchistosomatidaeSchistosoma

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 273273Peptidyl-prolyl cis-trans isomerase EPRO_0000064161Add
    BLAST

    Structurei

    Secondary structure

    1
    273
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi113 – 1208
    Beta strandi123 – 13210
    Turni134 – 1363
    Helixi138 – 14912
    Turni150 – 1523
    Beta strandi160 – 1656
    Turni166 – 1683
    Beta strandi169 – 1724
    Turni175 – 1773
    Beta strandi178 – 1814
    Beta strandi205 – 2084
    Beta strandi220 – 2256
    Helixi228 – 2303
    Turni231 – 2333
    Beta strandi236 – 2427
    Helixi244 – 2496
    Helixi250 – 2534
    Beta strandi264 – 2729

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CK1X-ray1.80A102-273[»]
    2CMTX-ray1.50A102-273[»]
    ProteinModelPortaliQ26548.
    SMRiQ26548. Positions 1-53, 110-273.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ26548.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 4848RRMPROSITE-ProRule annotationAdd
    BLAST
    Domaini115 – 271157PPIase cyclophilin-typePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 PPIase cyclophilin-type domain.PROSITE-ProRule annotation
    Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

    Family and domain databases

    Gene3Di2.40.100.10. 1 hit.
    3.30.70.330. 1 hit.
    InterProiIPR029000. Cyclophilin-like_dom.
    IPR020892. Cyclophilin-type_PPIase_CS.
    IPR002130. Cyclophilin-type_PPIase_dom.
    IPR016304. Cyclophilin-type_PPIase_E.
    IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view]
    PfamiPF00160. Pro_isomerase. 1 hit.
    PF00076. RRM_1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001475. PPI_cyclophilin_E. 1 hit.
    PRINTSiPR00153. CSAPPISMRASE.
    SUPFAMiSSF50891. SSF50891. 1 hit.
    PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
    PS50072. CSA_PPIASE_2. 1 hit.
    PS50102. RRM. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q26548-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPMDYQTEKH RGFAFVEFEE VEDAMSAIDN MNESEIFGRT IRVNVARPVR    50
    IREGWSRPVW SDENWLKKYG SAPLEGRKLD EPDIVNPSDT SENVEDLSDE 100
    EMRTKKQKRN LPRVFFDIRI GNGDAGRIVM ELRSDIVPRT AENFRALCTG 150
    ERGFGYHNCC FHRVIPQFMC QGGDFVKGDG TGGKSIYGRK FDDENFQLRH 200
    EGFGVLSMAN SGPNTNGSQF FICTTKCDWL DGKHVVFGRV VDGQNVVKKM 250
    ESVGSKSGKV KEPVIISRCG ELI 273
    Length:273
    Mass (Da):30,905
    Last modified:January 1, 1998 - v2
    Checksum:iA3CE71D40CB0CDD1
    GO

    Sequence cautioni

    The sequence AAC47317.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti196 – 1961F → I in AAC47317. (PubMed:8898338)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U30265 mRNA. Translation: AAC47543.1.
    U50388 mRNA. Translation: AAC47317.1. Different initiation.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U30265 mRNA. Translation: AAC47543.1 .
    U50388 mRNA. Translation: AAC47317.1 . Different initiation.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CK1 X-ray 1.80 A 102-273 [» ]
    2CMT X-ray 1.50 A 102-273 [» ]
    ProteinModelPortali Q26548.
    SMRi Q26548. Positions 1-53, 110-273.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    BRENDAi 5.2.1.8. 5608.

    Miscellaneous databases

    EvolutionaryTracei Q26548.

    Family and domain databases

    Gene3Di 2.40.100.10. 1 hit.
    3.30.70.330. 1 hit.
    InterProi IPR029000. Cyclophilin-like_dom.
    IPR020892. Cyclophilin-type_PPIase_CS.
    IPR002130. Cyclophilin-type_PPIase_dom.
    IPR016304. Cyclophilin-type_PPIase_E.
    IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view ]
    Pfami PF00160. Pro_isomerase. 1 hit.
    PF00076. RRM_1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001475. PPI_cyclophilin_E. 1 hit.
    PRINTSi PR00153. CSAPPISMRASE.
    SUPFAMi SSF50891. SSF50891. 1 hit.
    PROSITEi PS00170. CSA_PPIASE_1. 1 hit.
    PS50072. CSA_PPIASE_2. 1 hit.
    PS50102. RRM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "RNA trans-splicing in flatworms. Analysis of trans-spliced mRNAs and genes in the human parasite, Schistosoma mansoni."
      Davis R.E., Hardwick C., Tavernier P., Hodgson S., Singh H.
      J. Biol. Chem. 270:21813-21819(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 57-273.

    Entry informationi

    Entry nameiPPIE_SCHMA
    AccessioniPrimary (citable) accession number: Q26548
    Secondary accession number(s): Q26558
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 31, 2004
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 80 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3