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Q27745 (Q27745_PLAFA) Unreviewed, UniProtKB/TrEMBL

Last modified April 3, 2013. Version 67. 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
Gene names
Name:CyP gene EMBL CAA59933.1
OrganismPlasmodium falciparum EMBL CAA59933.1
Taxonomic identifier5833 [NCBI]
Taxonomic lineageEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiumPlasmodium (Laverania)

Protein attributes

Sequence length195 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 SAAS020892

Sequence similarities

Belongs to the cyclophilin-type PPIase family. RuleBase RU004223

Contains 1 PPIase cyclophilin-type domain. SAAS SAAS020892 RuleBase RU003420

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential EMBL CAA59933.1
Chain23 – 195173 Potential EMBL CAA59933.1
PRO_5000146461

Sequences

Sequence LengthMass (Da)Tools
Q27745 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 59569520AC9288B9

FASTA19521,731
        10         20         30         40         50         60 
MNKLVSIILV IFFLFHKYAL CAEEHEITHK TYFDITIDDK PLGRIVFGLY GKVAPKTVEN 

        70         80         90        100        110        120 
FVSICKGTVV DGKMLHYTNS IFHRIIPNFM AQGGDITNFN GTGGLSIYGK KFEDENFKVN 

       130        140        150        160        170        180 
HSKRGLLSMA NAGKNTNGSQ FFILFIPTPW LDGRHVVFGE VVEGLDKLVH IEAVGTDSGE 

       190 
PLKRVLVKES GELPL 

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References

[1]"Molecular and biochemical characterization of a Plasmodium falciparum cyclophilin containing a cleavable signal sequence."
Hirtzlin J., Farber P.M., Franklin R.M., Bell A.
Eur. J. Biochem. 232:765-772(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: K1 EMBL CAA59933.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X85956 mRNA. Translation: CAA59933.1.
PIRS52760. S68357.

3D structure databases

HSSPHSSP built from PDB template 1E3B based on UniProtKB P52011.
ProteinModelPortalQ27745.
SMRQ27745. Positions 24-193.
ModBaseSearch...

Proteomic databases

PRIDEQ27745.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG0652.

Family and domain databases

InterProIPR002130. Cyclophilin-like_PPIase_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
[Graphical view]
PfamPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PIRSFPIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSPR00153. CSAPPISMRASE.
SUPFAMSSF50891. CSA_PPIase. 1 hit.
PROSITEPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ27745_PLAFA
AccessionPrimary (citable) accession number: Q27745
Entry history
Integrated into UniProtKB/TrEMBL: November 1, 1996
Last sequence update: November 1, 1996
Last modified: April 3, 2013
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)