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Q7RSH5 (Q7RSH5_PLAYO) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

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

EC=5.2.1.8 RuleBase RU000493
Gene names
ORF Names:PY00382 EMBL EAA15388.1
OrganismPlasmodium yoelii yoelii [Reference proteome] EMBL EAA15388.1
Taxonomic identifier73239 [NCBI]
Taxonomic lineageEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiumPlasmodium (Vinckeia)

Protein attributes

Sequence length210 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

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data. EMBL EAA15388.1

Ontologies

Sequences

Sequence LengthMass (Da)Tools
Q7RSH5 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 1419CE2A8B60565F

FASTA21023,909
        10         20         30         40         50         60 
MKSNSKDSEN KKVENLVLDD NDENTIIPYY LSNLLTNPSN PVVFMDINLG NNFLGKFKFE 

        70         80         90        100        110        120 
LFQNIVPKTS ENFRQFCTGE YKVNNLPVGY KNTIFHRVIK EFMIQGGDFI NHNGSGSLSI 

       130        140        150        160        170        180 
YGEKFDDENF DIKHDKEGLL SMANSGPNTN GCQFFITTKK CEWLDGKNVV FGRIIDNDSL 

       190        200        210 
LLLKKIENVS VTPYIYKPKI PINVVECGEL 

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence and comparative analysis of the model rodent malaria parasite Plasmodium yoelii yoelii."
Carlton J.M., Angiuoli S.V., Suh B.B., Kooij T.W., Pertea M., Silva J.C., Ermolaeva M.D., Allen J.E., Selengut J.D., Koo H.L., Peterson J.D., Pop M., Kosack D.S., Shumway M.F., Bidwell S.L., Shallom S.J., van Aken S.E., Riedmuller S.B. expand/collapse author list , Feldblyum T.V., Cho J.K., Quackenbush J., Sedegah M., Shoaibi A., Cummings L.M., Florens L., Yates J.R. III, Raine J.D., Sinden R.E., Harris M.A., Cunningham D.A., Preiser P.R., Bergman L.W., Vaidya A.B., van Lin L.H., Janse C.J., Waters A.P., Smith H.O., White O.R., Salzberg S.L., Venter J.C., Fraser C.M., Hoffman S.L., Gardner M.J., Carucci D.J.
Nature 419:512-519(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 17XNL EMBL EAA15388.1.
[2]"Genome-scale protein expression and structural biology of Plasmodium falciparum and related Apicomplexan organisms."
Vedadi M., Lew J., Artz J., Amani M., Zhao Y., Dong A., Wasney G.A., Gao M., Hills T., Brokx S., Qiu W., Sharma S., Diassiti A., Alam Z., Melone M., Mulichak A., Wernimont A., Bray J. expand/collapse author list , Loppnau P., Plotnikova O., Newberry K., Sundararajan E., Houston S., Walker J., Tempel W., Bochkarev A., Kozieradzki I., Edwards A., Arrowsmith C., Roos D., Kain K., Hui R.
Mol. Biochem. Parasitol. 151:100-110(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AABL01000106 Genomic DNA. Translation: EAA15388.1.
RefSeqXP_723823.1. XM_718730.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z81X-ray2.80A1-210[»]
ProteinModelPortalQ7RSH5.
SMRQ7RSH5. Positions 25-210.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING73239.Q7RSH5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3789157.
KEGGpyo:PY00382.

Organism-specific databases

EuPathDBPlasmoDB:PY00382.

Phylogenomic databases

eggNOGCOG0652.
KOK09567.

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

EvolutionaryTraceQ7RSH5.

Entry information

Entry nameQ7RSH5_PLAYO
AccessionPrimary (citable) accession number: Q7RSH5
Entry history
Integrated into UniProtKB/TrEMBL: December 15, 2003
Last sequence update: December 15, 2003
Last modified: July 9, 2014
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)