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

Catalytic activityi

Peptidylproline (omega=180) = peptidylproline (omega=0).SAAS annotation

GO - Molecular functioni

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

GO - Biological processi

  1. protein folding Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, RotamaseUniRule annotationSAAS annotation

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:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HAQX-ray1.97A22-187[»]
3BT8X-ray2.70A22-187[»]
3EOVX-ray2.60A/B22-187[»]
ProteinModelPortaliQ9U9R3.
SMRiQ9U9R3. Positions 22-187.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9U9R3.

Family & Domainsi

Sequence similaritiesi

Belongs to the cyclophilin-type PPIase family.UniRule annotation
Contains 1 PPIase cyclophilin-type domain.UniRule annotation
Contains PPIase cyclophilin-type domain.SAAS annotation

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

« Hide

        10         20         30         40         50
MRFVAVLAVV LCALSFLNVA AEPEVTAKVY FDVMIDSEPL GRITIGLFGK
60 70 80 90 100
DAPLTTENFR QLCTGEHGFG YKDSIFHRVI QNFMIQGGDF TNFDGTGGKS
110 120 130 140 150
IYGEKFADEN LNVKHFVGAL SMANAGPNTN GSQFFITTAP TPWLDGRHVV
160 170 180
FGKVLDGMDV VLRIEKTKTN SHDRPVKPVK IVASGEL
Length:187
Mass (Da):20,429
Last modified:May 1, 2000 - v1
Checksum:iA35EC99752114F1D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF158368 Genomic DNA. Translation: AAD46565.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF158368 Genomic DNA. Translation: AAD46565.1 .

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 81 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