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Q27450

- CYP1_BRUMA

UniProt

Q27450 - CYP1_BRUMA

Protein

Peptidyl-prolyl cis-trans isomerase 1

Gene

CYP-1

Organism
Brugia malayi (Filarial nematode worm)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      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

    Relatively insensitive to inhibition by cyclosporin A (CsA).

    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, Rotamase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peptidyl-prolyl cis-trans isomerase 1 (EC:5.2.1.8)
    Short name:
    PPIase 1
    Alternative name(s):
    BmCYP-1
    Cyclophilin
    Rotamase 1
    Gene namesi
    Name:CYP-1
    OrganismiBrugia malayi (Filarial nematode worm)
    Taxonomic identifieri6279 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaSpiruridaFilarioideaOnchocercidaeBrugia

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 843843Peptidyl-prolyl cis-trans isomerase 1PRO_0000064215Add
    BLAST

    Proteomic databases

    PRIDEiQ27450.

    Structurei

    Secondary structure

    1
    843
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 53
    Beta strandi7 – 159
    Beta strandi18 – 2710
    Turni29 – 313
    Helixi33 – 4412
    Turni51 – 533
    Beta strandi55 – 573
    Beta strandi63 – 686
    Turni69 – 713
    Beta strandi72 – 754
    Beta strandi79 – 846
    Beta strandi105 – 1117
    Beta strandi113 – 1153
    Beta strandi123 – 1286
    Helixi131 – 1333
    Turni134 – 1363
    Beta strandi139 – 1457
    Helixi147 – 1548
    Beta strandi164 – 1663
    Beta strandi168 – 1769

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A33X-ray2.15A1-177[»]
    1A58X-ray1.95A1-177[»]
    1C5FX-ray2.47A/C/E/G/I/K/M/O1-177[»]
    ProteinModelPortaliQ27450.
    SMRiQ27450. Positions 1-177.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ27450.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini10 – 175166PPIase cyclophilin-typePROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi700 – 70910Poly-Arg
    Compositional biasi713 – 7164Poly-Arg
    Compositional biasi800 – 81516Poly-SerAdd
    BLAST
    Compositional biasi828 – 83710Poly-Ser

    Sequence similaritiesi

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

    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.

    Q27450-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSKKDRRRVF LDVTIDGNLA GRIVMELYND IAPRTCNNFL MLCTGMAGTG    50
    KISGKPLHYK GSTFHRVIKN FMIQGGDFTK GDGTGGESIY GGMFDDEEFV 100
    MKHDEPFVVS MANKGPNTNG SQFFITTTPA PHLNNIHVVF GKVVSGQEVV 150
    TKIEYLKTNS KNRPLADVVI LNCGELVRRK KRQHSSRSNE SVSSSTSTEK 200
    SHKKTKKTKM KEKKRKESDE VEQLEIGTVV PEAELQLSSV KAEDLPDEPD 250
    HQNKYLMRRS KTPENSRKGK KEKQRQSPHR FSRRDIGHRL NRMRRTRTGH 300
    KIKGRGALRF RTPEGSSDHD GSRTPPHWRR EQNRVITLDE LHRLQEKRKA 350
    YELEELENPK NDVVDKAKTG ILLNTSEKIE DKEERYRGKS EKKENRHERS 400
    RHTTRRSPEH VTRHFVKEKN RHKVDEVGNS EDMKQTKRDR RGRADEKEKV 450
    EVNGEKAAAM DELNLDEPTV EVTLDSAEDI RDSDDEAIRI HLLKAKKMAE 500
    EKTKQEAKML EKTGDKEGRD QKTISEAKQK DSAEKDRQHR EHKNDELEKR 550
    AIEKQDKDQI VERDTGSKQR RKSDSKEHRG KTDRKHRSKS IEEDGRRSTS 600
    REKLDDLKRK ETSGQKSQAD SEQTVEAKTN VVDSNSDNSK MSVNGKLKEV 650
    SSTNKENEVS EQKDLKAEST KSEEIKQQVN EVSRKQKGGE KPKEHKRNER 700
    SRSRRRRSRS NGRRRRSSSR RSRSRDRRHK SRSRSRGYVR RFEGWSRSRR 750
    PTRRELYDER MRRERERRRS FDRYSDRRRT RSRSARRDSD RHSRRSRKRS 800
    PSSSSSSSES SSSDSRSTAS SSASSKRSSS SDSSRSSRSR SSN 843
    Length:843
    Mass (Da):97,818
    Last modified:November 1, 1996 - v1
    Checksum:i3C34EC90A32EDBDC
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L37292 mRNA. Translation: AAC37249.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L37292 mRNA. Translation: AAC37249.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A33 X-ray 2.15 A 1-177 [» ]
    1A58 X-ray 1.95 A 1-177 [» ]
    1C5F X-ray 2.47 A/C/E/G/I/K/M/O 1-177 [» ]
    ProteinModelPortali Q27450.
    SMRi Q27450. Positions 1-177.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q27450.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei Q27450.

    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. "Molecular characterization of a cyclosporin A-insensitive cyclophilin from the parasitic nematode Brugia malayi."
      Page A.P., Landry D., Wilson G.G., Carlow C.K.S.
      Biochemistry 34:11545-11550(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The X-ray structure of a divergent cyclophilin from the nematode parasite Brugia malayi."
      Taylor P., Page A.P., Kontopidis G., Husi H., Walkinshaw M.D.
      FEBS Lett. 425:361-366(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1-177.
    3. "Crystal structure of the cyclophilin-like domain from the parasitic nematode Brugia malayi."
      Mikol V., Ma D., Carlow C.K.S.
      Protein Sci. 7:1310-1316(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 1-177.
      Strain: ATCC 75593 / Bmcyp-1.
    4. "Crystal structure of the complex of Brugia malayi cyclophilin and cyclosporin A."
      Ellis P.J., Carlow C.K.S., Ma D., Kuhn P.
      Biochemistry 39:592-598(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.47 ANGSTROMS) OF 1-177 IN COMPLEX WITH CYCLOSPORIN A.

    Entry informationi

    Entry nameiCYP1_BRUMA
    AccessioniPrimary (citable) accession number: Q27450
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 77 of the entry and version 1 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