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Q4WHY9

- Q4WHY9_ASPFU

UniProt

Q4WHY9 - Q4WHY9_ASPFU

Protein

Peptidyl-prolyl cis-trans isomerase

Gene

AFUA_2G03720

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Unreviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 75 (01 Oct 2014)
      Sequence version 1 (05 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).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)
    Gene namesi
    ORF Names:AFUA_2G03720Imported
    OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)Imported
    Taxonomic identifieri330879 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000002530: Chromosome 2

    PTM / Processingi

    Proteomic databases

    PRIDEiQ4WHY9.

    Interactioni

    Protein-protein interaction databases

    STRINGi5085.CADAFUAP00003559.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2C3BX-ray1.85A/B1-205[»]
    ProteinModelPortaliQ4WHY9.
    SMRiQ4WHY9. Positions 1-205.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ4WHY9.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni67 – 693Sulfate bindingImported

    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

    HOGENOMiHOG000065981.
    KOiK01802.
    OMAiVFFDVEY.
    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.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q4WHY9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSQVFFDVEY APVGTAETSA RNCAQSGLDA FGLQSILSIL FTDGILLRAV    50
    TAKVGRIVFN LFDKDVPKTA KNFRELCKRP AGEGYRESTF HRIIPNFMIQ 100
    GGDFTRGNGT GGRSIYGDKF ADENFSRKHD KKGILSMANA GPNTNGSQFF 150
    ITTAVTSWLD GKHVVFGEVA DEKSYSVVKE IEALGSSSGS VRSNTRPKIV 200
    NCGEL 205
    Length:205
    Mass (Da):22,290
    Last modified:July 5, 2005 - v1
    Checksum:i28B077F443AA78D8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAHF01000008 Genomic DNA. Translation: EAL87466.1.
    RefSeqiXP_749504.1. XM_744411.1.

    Genome annotation databases

    EnsemblFungiiCADAFUAT00003559; CADAFUAP00003559; CADAFUAG00003559.
    GeneIDi3506781.
    KEGGiafm:AFUA_2G03720.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAHF01000008 Genomic DNA. Translation: EAL87466.1 .
    RefSeqi XP_749504.1. XM_744411.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2C3B X-ray 1.85 A/B 1-205 [» ]
    ProteinModelPortali Q4WHY9.
    SMRi Q4WHY9. Positions 1-205.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5085.CADAFUAP00003559.

    Proteomic databases

    PRIDEi Q4WHY9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADAFUAT00003559 ; CADAFUAP00003559 ; CADAFUAG00003559 .
    GeneIDi 3506781.
    KEGGi afm:AFUA_2G03720.

    Phylogenomic databases

    HOGENOMi HOG000065981.
    KOi K01802.
    OMAi VFFDVEY.
    OrthoDBi EOG757D7G.

    Miscellaneous databases

    EvolutionaryTracei Q4WHY9.

    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. "Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
      Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.
      , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
      Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100Imported.
    2. "The crystal structure of Aspergillus fumigatus cyclophilin reveals 3D domain swapping of a central element."
      Limacher A., Kloer D.P., Fluckiger S., Folkers G., Crameri R., Scapozza L.
      Structure 14:185-195(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).

    Entry informationi

    Entry nameiQ4WHY9_ASPFU
    AccessioniPrimary (citable) accession number: Q4WHY9
    Entry historyi
    Integrated into UniProtKB/TrEMBL: July 5, 2005
    Last sequence update: July 5, 2005
    Last modified: October 1, 2014
    This is version 75 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Caution

    The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.Imported

    Keywords - Technical termi

    3D-structureImported, Complete proteome, Reference proteomeImported

    External Data

    Dasty 3