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Q25756

- Q25756_PLAFA

UniProt

Q25756 - Q25756_PLAFA

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Protein

Peptidyl-prolyl cis-trans isomerase

Gene
N/A
Organism
Plasmodium falciparum
Status
Unreviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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)
OrganismiPlasmodium falciparumImported
Taxonomic identifieri5833 [NCBI]
Taxonomic lineageiEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiumPlasmodium (Laverania)

PTM / Processingi

Proteomic databases

PRIDEiQ25756.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QNGX-ray2.10A2-171[»]
1QNHX-ray2.10A/B2-171[»]
ProteinModelPortaliQ25756.
SMRiQ25756. Positions 2-171.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ25756.

Family & Domainsi

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

eggNOGiCOG0652.

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.

Q25756 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSKRSKVFFD ISIDNSNAGR IIFELFSDIT PRTCENFRAL CTGEKIGSRG
60 70 80 90 100
KNLHYKNSIF HRIIPQFMCQ GGDITNGNGS GGESIYGRSF TDENFNMKHD
110 120 130 140 150
QPGLLSMANA GPNTNSSQFF ITLVPCPWLD GKHVVFGKVI EGMNVVREME
160 170
KEGAKSGYVK RSVVITDCGE L
Length:171
Mass (Da):18,953
Last modified:November 1, 1996 - v1
Checksum:i0AF10F640A2C1AB4
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U33869 mRNA. Translation: AAC41390.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U33869 mRNA. Translation: AAC41390.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1QNG X-ray 2.10 A 2-171 [» ]
1QNH X-ray 2.10 A/B 2-171 [» ]
ProteinModelPortali Q25756.
SMRi Q25756. Positions 2-171.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q25756.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG0652.

Miscellaneous databases

EvolutionaryTracei Q25756.

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. "Detailed characterization of a cyclophilin from the human malaria parasite Plasmodium falciparum."
    Berriman M., Fairlamb A.H.
    Biochem. J. 334:437-445(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: FCB1Imported.
  2. "The three-dimensional structure of a Plasmodium falciparum cyclophilin in complex with the potent anti-malarial cyclosporin A."
    Peterson M.R., Hall D.R., Berriman M., Nunes J.A., Leonard G.A., Fairlamb A.H., Hunter W.N.
    J. Mol. Biol. 298:123-133(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 2-171.

Entry informationi

Entry nameiQ25756_PLAFA
AccessioniPrimary (citable) accession number: Q25756
Entry historyi
Integrated into UniProtKB/TrEMBL: November 1, 1996
Last sequence update: November 1, 1996
Last modified: October 1, 2014
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureImported

External Data

Dasty 3