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Q9U9R3

- Q9U9R3_LEIDO

UniProt

Q9U9R3 - Q9U9R3_LEIDO

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Protein

Peptidyl-prolyl cis-trans isomerase

Gene
CYP
Organism
Leishmania donovani
Status
Unreviewed - Annotation score: 2 out of 5 - Experimental evidence at protein leveli

Functioni

PPIases accelerate the folding of proteins By similarity.UniRule annotation
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides By similarity.UniRule annotation

Catalytic activityi

Peptidylproline (omega=180) = peptidylproline (omega=0).UniRule annotationSAAS annotations

GO - Molecular functioni

  1. peptidyl-prolyl cis-trans isomerase activity Source: UniProtKB-KW

GO - Biological processi

  1. protein folding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, RotamaseUniRule annotationSAAS annotations

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomeraseUniRule annotation (EC:5.2.1.8UniRule annotation)
Gene namesi
Name:CYPImported
OrganismiLeishmania donovaniImported
Taxonomic identifieri5661 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmania

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HAQX-ray1.97A22-187[»]
3BT8X-ray2.70A22-187[»]
3EOVX-ray2.60A/B22-187[»]
ProteinModelPortaliQ9U9R3.
SMRiQ9U9R3. Positions 22-187.

Miscellaneous databases

EvolutionaryTraceiQ9U9R3.

Family & Domainsi

Sequence similaritiesi

Belongs to the cyclophilin-type PPIase family.UniRule annotation
Contains PPIase cyclophilin-type domain.SAAS annotations

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PIRSFiPIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9U9R3-1 [UniParc]FASTAAdd to Basket

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MRFVAVLAVV LCALSFLNVA AEPEVTAKVY FDVMIDSEPL GRITIGLFGK    50
DAPLTTENFR QLCTGEHGFG YKDSIFHRVI QNFMIQGGDF TNFDGTGGKS 100
IYGEKFADEN LNVKHFVGAL SMANAGPNTN GSQFFITTAP TPWLDGRHVV 150
FGKVLDGMDV VLRIEKTKTN SHDRPVKPVK IVASGEL 187
Length:187
Mass (Da):20,429
Last modified:May 1, 2000 - v1
Checksum:iA35EC99752114F1D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF158368 Genomic DNA. Translation: AAD46565.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF158368 Genomic DNA. Translation: AAD46565.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2HAQ X-ray 1.97 A 22-187 [» ]
3BT8 X-ray 2.70 A 22-187 [» ]
3EOV X-ray 2.60 A/B 22-187 [» ]
ProteinModelPortali Q9U9R3.
SMRi Q9U9R3. Positions 22-187.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei Q9U9R3.

Family and domain databases

Gene3Di 2.40.100.10. 1 hit.
InterProi IPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view ]
Pfami PF00160. Pro_isomerase. 1 hit.
[Graphical view ]
PIRSFi PIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSi PR00153. CSAPPISMRASE.
SUPFAMi SSF50891. SSF50891. 1 hit.
PROSITEi PS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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: D1700Imported.
  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.

Entry informationi

Entry nameiQ9U9R3_LEIDO
AccessioniPrimary (citable) accession number: Q9U9R3
Entry historyi
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 statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureImported

External Data

Dasty 3

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