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Reviewed, UniProtKB/Swiss-Prot Q27450 (CYP1_BRUMA)

Last modified June 16, 2009. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Peptidyl-prolyl cis-trans isomerase 1
      Short name=PPIase 1
    EC=5.2.1.8
Alternative name(s):
    Cyclophilin
    BmCYP-1
Gene names
Name: CYP-1
OrganismBrugia malayi (Filarial nematode worm)
Taxonomic identifier6279 [NCBI]
Taxonomic lineageEukaryotaMetazoaNematodaChromadoreaSpiruridaFilarioideaOnchocercidaeBrugia

Protein attributes

Sequence length843 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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

Catalytic activity

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

Enzyme regulation

Relatively insensitive to inhibition by cyclosporin A (CsA).

Sequence similarities

Contains 1 PPIase cyclophilin-type domain.

Ontologies

Keywords
   Molecular functionIsomerase
Rotamase
   Technical term3D-structure
Gene Ontology (GO)
   Biological processprotein folding

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionpeptidyl-prolyl cis-trans isomerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 843843Peptidyl-prolyl cis-trans isomerase 1
PRO_0000064215

Regions

Domain10 – 175166PPIase cyclophilin-type
Compositional bias700 – 70910Poly-Arg
Compositional bias713 – 7164Poly-Arg
Compositional bias800 – 81516Poly-Ser
Compositional bias828 – 83710Poly-Ser

Secondary structure

................................. 843
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q27450-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 3C34EC90A32EDBDC

FASTA84397,818
        10         20         30         40         50         60 
MSKKDRRRVF LDVTIDGNLA GRIVMELYND IAPRTCNNFL MLCTGMAGTG KISGKPLHYK 

        70         80         90        100        110        120 
GSTFHRVIKN FMIQGGDFTK GDGTGGESIY GGMFDDEEFV MKHDEPFVVS MANKGPNTNG 

       130        140        150        160        170        180 
SQFFITTTPA PHLNNIHVVF GKVVSGQEVV TKIEYLKTNS KNRPLADVVI LNCGELVRRK 

       190        200        210        220        230        240 
KRQHSSRSNE SVSSSTSTEK SHKKTKKTKM KEKKRKESDE VEQLEIGTVV PEAELQLSSV 

       250        260        270        280        290        300 
KAEDLPDEPD HQNKYLMRRS KTPENSRKGK KEKQRQSPHR FSRRDIGHRL NRMRRTRTGH 

       310        320        330        340        350        360 
KIKGRGALRF RTPEGSSDHD GSRTPPHWRR EQNRVITLDE LHRLQEKRKA YELEELENPK 

       370        380        390        400        410        420 
NDVVDKAKTG ILLNTSEKIE DKEERYRGKS EKKENRHERS RHTTRRSPEH VTRHFVKEKN 

       430        440        450        460        470        480 
RHKVDEVGNS EDMKQTKRDR RGRADEKEKV EVNGEKAAAM DELNLDEPTV EVTLDSAEDI 

       490        500        510        520        530        540 
RDSDDEAIRI HLLKAKKMAE EKTKQEAKML EKTGDKEGRD QKTISEAKQK DSAEKDRQHR 

       550        560        570        580        590        600 
EHKNDELEKR AIEKQDKDQI VERDTGSKQR RKSDSKEHRG KTDRKHRSKS IEEDGRRSTS 

       610        620        630        640        650        660 
REKLDDLKRK ETSGQKSQAD SEQTVEAKTN VVDSNSDNSK MSVNGKLKEV SSTNKENEVS 

       670        680        690        700        710        720 
EQKDLKAEST KSEEIKQQVN EVSRKQKGGE KPKEHKRNER SRSRRRRSRS NGRRRRSSSR 

       730        740        750        760        770        780 
RSRSRDRRHK SRSRSRGYVR RFEGWSRSRR PTRRELYDER MRRERERRRS FDRYSDRRRT 

       790        800        810        820        830        840 
RSRSARRDSD RHSRRSRKRS PSSSSSSSES SSSDSRSTAS SSASSKRSSS SDSSRSSRSR 


SSN 

« Hide

References

[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: 7547885] [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: 9559680] [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: 9655334] [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: 10642184] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.47 ANGSTROMS) OF 1-177 IN COMPLEX WITH CYCLOSPORIN A.

Cross-references

Sequence databases

L37292 mRNA. Translation: AAC37249.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1A33X-ray2.15A1-177[»]
1A58X-ray1.95A1-177[»]
1C5FX-ray2.47A/C/E/G/I/K/M/O1-177[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA5.2.1.8. 27.

Family and domain databases

InterProIPR002130. PPIase_cyclophilin.
[Graphical view]
Gene3DG3DSA:2.40.100.10. PPIase_cyclophilin. 1 hit.
PfamPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PRINTSPR00153. CSAPPISMRASE.
PROSITEPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCYP1_BRUMA
AccessionPrimary (citable) accession number: Q27450
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: June 16, 2009
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents