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Q9U9R3 (Q9U9R3_LEIDO) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 78. 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 EMBL AAD46565.1
OrganismLeishmania donovani EMBL AAD46565.1
Taxonomic identifier5661 [NCBI]
Taxonomic lineageEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmania

Protein attributes

Sequence length187 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. RuleBase RU004223

Contains 1 PPIase cyclophilin-type domain.

Contains PPIase cyclophilin-type domain. SAAS SAAS020892

Ontologies

Keywords
   Molecular functionIsomerase
Rotamase SAAS SAAS002130 RuleBase RU003420
   Technical term3D-structure PDB 3EOV PDB 2HAQ PDB 3BT8
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
Q9U9R3 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: A35EC99752114F1D

FASTA18720,429
        10         20         30         40         50         60 
MRFVAVLAVV LCALSFLNVA AEPEVTAKVY FDVMIDSEPL GRITIGLFGK DAPLTTENFR 

        70         80         90        100        110        120 
QLCTGEHGFG YKDSIFHRVI QNFMIQGGDF TNFDGTGGKS IYGEKFADEN LNVKHFVGAL 

       130        140        150        160        170        180 
SMANAGPNTN GSQFFITTAP TPWLDGRHVV FGKVLDGMDV VLRIEKTKTN SHDRPVKPVK 


IVASGEL 

« Hide

References

[1]"Characterization of a cyclophilin homolog that is predominantly expressed in free living Leishmania donovani: implications for cyclosporin resistance."
Dutta M., Delhi P., Sinha K.M., Banerjee R.K., Datta A.K.
Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: D1700 EMBL AAD46565.1.
[2]"Structure of cyclophilin from Leishmania donovani at 1.97 A resolution."
Venugopal V., Sen B., Datta A.K., Banerjee R.
Acta Crystallogr. F 63:60-64(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) OF 22-187.
[3]"Crystal Structure of Mutant Cyclophilin from Leishmania Donovani."
Venugopal V., Sen B., Datta A.K., Banerjee R.
Submitted (DEC-2007) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 22-187.
[4]"Structure of cyclophilin from Leishmania donovani bound to cyclosporin at 2.6 A resolution: correlation between structure and thermodynamic data."
Venugopal V., Datta A.K., Bhattacharyya D., Dasgupta D., Banerjee R.
Acta Crystallogr. D 65:1187-1195(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 22-187.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF158368 Genomic DNA. Translation: AAD46565.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2HAQX-ray1.97A22-187[»]
3BT8X-ray2.70A22-187[»]
3EOVX-ray2.60A/B22-187[»]
ProteinModelPortalQ9U9R3.
SMRQ9U9R3. Positions 22-187.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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

EvolutionaryTraceQ9U9R3.

Entry information

Entry nameQ9U9R3_LEIDO
AccessionPrimary (citable) accession number: Q9U9R3
Entry history
Integrated into UniProtKB/TrEMBL: May 1, 2000
Last sequence update: May 1, 2000
Last modified: June 11, 2014
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)