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Q7RRM6 (Q7RRM6_PLAYO) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 83. 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·Sequence annotation·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:PY00693 EMBL EAA17886.1
OrganismPlasmodium yoelii yoelii [Reference proteome] EMBL EAA17886.1
Taxonomic identifier73239 [NCBI]
Taxonomic lineageEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiumPlasmodium (Vinckeia)

Protein attributes

Sequence length202 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). SAAS SAAS002130

Sequence similarities

Belongs to the cyclophilin-type PPIase family. RuleBase RU004223

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 EAA17886.1

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Binding site631Chloride 1; via amide nitrogen PDB 2B71
Binding site921Chloride 3; via amide nitrogen PDB 2B71
Binding site961Chloride 2 PDB 2B71

Sequences

Sequence LengthMass (Da)Tools
Q7RRM6 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 9C2D43E2364B5AF2

FASTA20222,716
        10         20         30         40         50         60 
MFTLCKGYSD DEEEESNAIN VVSEKTKSLE EKIAYYKMKG HTERGYITIY TNLGDFEVEL 

        70         80         90        100        110        120 
YWYHSPKTCL NFYTLCEMGF YDNTIFHRVI PNFVIQGGDP TGTGKGGKSI YGEYFEDEIN 

       130        140        150        160        170        180 
KELKHTGAGI LSMSNNGPNT NSSQFFITLA PLPHLDGKHT IFARVSKNMT CIENIASVQT 

       190        200 
TATNKPIFDL KILRTSTAVN AD 

« 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 EAA17886.1.
[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 (2.50 ANGSTROMS) OF 7-202 IN COMPLEX WITH CHLORIDE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AABL01000189 Genomic DNA. Translation: EAA17886.1.
RefSeqXP_726321.1. XM_721228.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2B71X-ray2.50A7-202[»]
ProteinModelPortalQ7RRM6.
SMRQ7RRM6. Positions 29-197.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING73239.Q7RRM6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3791661.
KEGGpyo:PY00693.

Organism-specific databases

EuPathDBPlasmoDB:PY00693.

Phylogenomic databases

eggNOGCOG0652.
KOK12733.

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

EvolutionaryTraceQ7RRM6.

Entry information

Entry nameQ7RRM6_PLAYO
AccessionPrimary (citable) accession number: Q7RRM6
Entry history
Integrated into UniProtKB/TrEMBL: December 15, 2003
Last sequence update: December 15, 2003
Last modified: July 9, 2014
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)