Q7RSH5 (Q7RSH5_PLAYO) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Peptidyl-prolyl cis-trans isomerase RuleBase RU000493
EC=5.2.1.8 RuleBase RU000493

Gene names

ORF Names:

PY00382 EMBL EAA15388.1

Organism

Plasmodium yoelii yoelii [Reference proteome] EMBL EAA15388.1

Taxonomic identifier

73239 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Alveolata › Apicomplexa › Aconoidasida › Haemosporida › Plasmodium › Plasmodium (Vinckeia) › Plasmodium yoelii

Protein attributes

Sequence length	210 AA.
Sequence status	Complete.
Protein existence	Evidence 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 SAAS020892
Sequence similarities	Belongs to the cyclophilin-type PPIase family. RuleBase RU004223 Contains 1 PPIase cyclophilin-type domain. RuleBase RU003420 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

Keywords
Molecular function	Isomerase Rotamase SAAS SAAS020892 RuleBase RU003420
Technical term	3D-structure PDB 1Z81 Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein folding Inferred from electronic annotation. Source: UniProtKB-KW protein peptidyl-prolyl isomerization Inferred from electronic annotation. Source: GOC
Molecular_function	peptidyl-prolyl cis-trans isomerase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	Q7RSH5 [UniParc]. Last modified December 15, 2003. Version 1. Checksum: 1419CE2A8B60565F	FASTA	210	23,909
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.

RefSeq

XP_723823.1. XM_718730.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1Z81	X-ray	2.80	A	1-210	[»]

ProteinModelPortal

Q7RSH5.

SMR

Q7RSH5. Positions 25-210.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

3789157.

KEGG

pyo:PY00382.

Organism-specific databases

EuPathDB

PlasmoDB:PY00382.

Phylogenomic databases

eggNOG

COG0652.

KO

K09567.

Family and domain databases

InterPro

IPR002130. Cyclophilin-like_PPIase_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
[Graphical view]

Pfam

PF00160. Pro_isomerase. 1 hit.
[Graphical view]

PIRSF

PIRSF001467. Peptidylpro_ismrse. 1 hit.

PRINTS

PR00153. CSAPPISMRASE.

SUPFAM

SSF50891. CSA_PPIase. 1 hit.

PROSITE

PS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q7RSH5.

Entry information

Entry name

Q7RSH5_PLAYO

Accession

Primary (citable) accession number: Q7RSH5

Entry history

Integrated into UniProtKB/TrEMBL:	December 15, 2003
Last sequence update:	December 15, 2003
Last modified:	May 1, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)