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Q5B4R3

- PPIB_EMENI

UniProt

Q5B4R3 - PPIB_EMENI

Protein

Peptidyl-prolyl cis-trans isomerase B

Gene

cpr2

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 66 (01 Oct 2014)
      Sequence version 1 (26 Apr 2005)
      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 By similarity.By similarity

    Catalytic activityi

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

    Enzyme regulationi

    Inhibited by cyclosporin A (CsA).By similarity

    GO - Molecular functioni

    1. peptide binding Source: UniProtKB-KW
    2. peptidyl-prolyl cis-trans isomerase activity Source: ASPGD

    GO - Biological processi

    1. cellular response to farnesol Source: ASPGD
    2. cellular response to heat Source: ASPGD
    3. protein folding Source: UniProtKB-KW
    4. protein peptidyl-prolyl isomerization Source: GOC

    Keywords - Molecular functioni

    Isomerase, Rotamase

    Keywords - Ligandi

    Cyclosporin

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peptidyl-prolyl cis-trans isomerase B (EC:5.2.1.8)
    Short name:
    PPIase B
    Alternative name(s):
    Rotamase B
    Gene namesi
    Name:cpr2
    ORF Names:AN4467
    OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
    Taxonomic identifieri227321 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000000560: Chromosome III

    Subcellular locationi

    Endoplasmic reticulum lumen PROSITE-ProRule annotation

    GO - Cellular componenti

    1. endoplasmic reticulum lumen Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Endoplasmic reticulum

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Sequence AnalysisAdd
    BLAST
    Chaini25 – 214190Peptidyl-prolyl cis-trans isomerase BPRO_0000233047Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi138 – 1381N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PRIDEiQ5B4R3.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5B4R3.
    SMRiQ5B4R3. Positions 29-202.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini37 – 194158PPIase cyclophilin-typePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi211 – 2144Prevents secretion from ER

    Sequence similaritiesi

    Contains 1 PPIase cyclophilin-type domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG0652.
    HOGENOMiHOG000065981.
    KOiK03768.
    OMAiPSVANDK.
    OrthoDBiEOG757D7G.

    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.
    PS00014. ER_TARGET. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q5B4R3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTSLKSLFLS FFLVVALGLA LVNASEPRGP KITNKVYFDI QHGDESLGRI    50
    VLGLYGKTVP ETAENFRALA TGEKGFGYEG SNFHRVIKDF MIQGGDFTRG 100
    DGTGGKSIYG AKFKDENFKL RHTKTGLLSM ANAGKDTNGS QFFITTAVTP 150
    WLDGKHVVFG EVLEGYDIVD KIQNVPKGRN DRPLKDVKIV KSGELEMEAD 200
    VANEGDKKGS HNEL 214
    Length:214
    Mass (Da):23,407
    Last modified:April 26, 2005 - v1
    Checksum:i5A4DCFAEBE529DFA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF107254 Genomic DNA. Translation: AAD17998.1.
    AACD01000077 Genomic DNA. Translation: EAA60232.1.
    BN001303 Genomic DNA. Translation: CBF77459.1.
    RefSeqiXP_662071.1. XM_656979.1.

    Genome annotation databases

    EnsemblFungiiCADANIAT00005984; CADANIAP00005984; CADANIAG00005984.
    GeneIDi2872268.
    KEGGiani:AN4467.2.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF107254 Genomic DNA. Translation: AAD17998.1 .
    AACD01000077 Genomic DNA. Translation: EAA60232.1 .
    BN001303 Genomic DNA. Translation: CBF77459.1 .
    RefSeqi XP_662071.1. XM_656979.1.

    3D structure databases

    ProteinModelPortali Q5B4R3.
    SMRi Q5B4R3. Positions 29-202.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q5B4R3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADANIAT00005984 ; CADANIAP00005984 ; CADANIAG00005984 .
    GeneIDi 2872268.
    KEGGi ani:AN4467.2.

    Phylogenomic databases

    eggNOGi COG0652.
    HOGENOMi HOG000065981.
    KOi K03768.
    OMAi PSVANDK.
    OrthoDBi EOG757D7G.

    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.
    PS00014. ER_TARGET. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and characterization of Aspergillus nidulans cyclophilin B."
      Joseph J.D., Heitman J., Means A.R.
      Fungal Genet. Biol. 27:55-66(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    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 nameiPPIB_EMENI
    AccessioniPrimary (citable) accession number: Q5B4R3
    Secondary accession number(s): C8V8H3, O94190
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 18, 2006
    Last sequence update: April 26, 2005
    Last modified: October 1, 2014
    This is version 66 of the entry and version 1 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