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

Catalytic activityi

Peptidylproline (omega=180) = peptidylproline (omega=0).UniRule annotationSAAS annotations

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 annotations

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.

Miscellaneous databases

EvolutionaryTraceiQ25756.

Family & Domainsi

Sequence similaritiesi

Contains PPIase cyclophilin-type domain.SAAS annotations

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.

Q25756-1 [UniParc]FASTAAdd to Basket

« Hide

MSKRSKVFFD ISIDNSNAGR IIFELFSDIT PRTCENFRAL CTGEKIGSRG    50
KNLHYKNSIF HRIIPQFMCQ GGDITNGNGS GGESIYGRSF TDENFNMKHD 100
QPGLLSMANA GPNTNSSQFF ITLVPCPWLD GKHVVFGKVI EGMNVVREME 150
KEGAKSGYVK RSVVITDCGE L 171
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: June 11, 2014
This is version 82 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

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