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Q25756 (Q25756_PLAFA) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Peptidyl-prolyl cis-trans isomerase RuleBase RU000493

EC=5.2.1.8 RuleBase RU000493
OrganismPlasmodium falciparum EMBL AAC41390.1
Taxonomic identifier5833 [NCBI]
Taxonomic lineageEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiumPlasmodium (Laverania)

Protein attributes

Sequence length171 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

PPIases accelerate the folding of proteins By similarity. RuleBase RU000493

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides By similarity. RuleBase RU004223

Catalytic activity

Peptidylproline (omega=180) = peptidylproline (omega=0). RuleBase RU000493 SAAS SAAS002130

Sequence similarities

Belongs to the cyclophilin-type PPIase family.

Contains 1 PPIase cyclophilin-type domain. RuleBase RU003420

Contains PPIase cyclophilin-type domain. SAAS SAAS020892

Ontologies

Keywords
   Molecular functionIsomerase
Rotamase SAAS SAAS002130 RuleBase RU003420
   Technical term3D-structure PDB 1QNG PDB 1QNH
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...

Sequences

Sequence LengthMass (Da)Tools
Q25756 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 0AF10F640A2C1AB4

FASTA17118,953
        10         20         30         40         50         60 
MSKRSKVFFD ISIDNSNAGR IIFELFSDIT PRTCENFRAL CTGEKIGSRG KNLHYKNSIF 

        70         80         90        100        110        120 
HRIIPQFMCQ GGDITNGNGS GGESIYGRSF TDENFNMKHD QPGLLSMANA GPNTNSSQFF 

       130        140        150        160        170 
ITLVPCPWLD GKHVVFGKVI EGMNVVREME KEGAKSGYVK RSVVITDCGE L 

« Hide

References

[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: FCB1 EMBL AAC41390.1.
[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U33869 mRNA. Translation: AAC41390.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QNGX-ray2.10A2-171[»]
1QNHX-ray2.10A/B2-171[»]
ProteinModelPortalQ25756.
SMRQ25756. Positions 2-171.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ25756.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG0652.

Family and domain databases

Gene3D2.40.100.10. 1 hit.
InterProIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PfamPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PIRSFPIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSPR00153. CSAPPISMRASE.
SUPFAMSSF50891. SSF50891. 1 hit.
PROSITEPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ25756.

Entry information

Entry nameQ25756_PLAFA
AccessionPrimary (citable) accession number: Q25756
Entry history
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 statusUnreviewed (UniProtKB/TrEMBL)