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Q27450

- CYP1_BRUMA

UniProt

Q27450 - CYP1_BRUMA

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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

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
Complete GO annotation...

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.

Miscellaneous databases

EvolutionaryTraceiQ27450.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini10 – 175166PPIase cyclophilin-typeAdd
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

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: July 9, 2014
This is version 76 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

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