Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Peptidyl-prolyl cis-trans isomerase

Gene

Tc00.1047053508577.140

Organism
Trypanosoma cruzi (strain CL Brener)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

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).UniRule annotationSAAS annotation

GO - Molecular functioni

GO - Biological processi

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
ORF Names:Tc00.1047053508577.140Imported
OrganismiTrypanosoma cruzi (strain CL Brener)Imported
Taxonomic identifieri353153 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosomaSchizotrypanum
ProteomesiUP000002296 Componenti: Unassembled WGS sequence

Interactioni

Protein-protein interaction databases

STRINGi353153.XP_816229.1.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XO7X-ray1.61A/B/C/D30-194[»]
1XQ7X-ray2.07A/B/C30-194[»]
ProteinModelPortaliQ4DPB9.
SMRiQ4DPB9. Positions 30-194.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ4DPB9.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

KOiK03768.

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]
PANTHERiPTHR11071. PTHR11071. 1 hit.
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.

Q4DPB9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRYLLLSKVT QLLLLLLLML SAAVSARADP VVTDKVYFDI TIGDEPVGRV
60 70 80 90 100
VIGLFGNDVP KTVENFKQLA SGENGFGYKG SIFHRVIRNF MIQGGDFTNF
110 120 130 140 150
DGTGGKSIYG TRFDDENLKI KHFVGAVSMA NAGPNSNGSQ FFVTTAPTPW
160 170 180 190
LDGRHVVFGK VVEGMDVVKK VENTKTGLND KPKKAVKIND CGVL
Length:194
Mass (Da):21,102
Last modified:September 13, 2005 - v1
Checksum:i688E90003CC958D5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAHK01000282 Genomic DNA. Translation: EAN94378.1.
RefSeqiXP_816229.1. XM_811136.1.

Genome annotation databases

GeneIDi3548068.
KEGGitcr:508577.140.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAHK01000282 Genomic DNA. Translation: EAN94378.1.
RefSeqiXP_816229.1. XM_811136.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XO7X-ray1.61A/B/C/D30-194[»]
1XQ7X-ray2.07A/B/C30-194[»]
ProteinModelPortaliQ4DPB9.
SMRiQ4DPB9. Positions 30-194.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi353153.XP_816229.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi3548068.
KEGGitcr:508577.140.

Phylogenomic databases

KOiK03768.

Miscellaneous databases

EvolutionaryTraceiQ4DPB9.

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]
PANTHERiPTHR11071. PTHR11071. 1 hit.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Crystal structure of cyclophilin from Trypanosoma cruzi."
    Structural Genomics of Pathogenic Protozoa Consortium (SGPP)
    Caruthers J.M., Hol W.G.J.
    Submitted (OCT-2004) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.61 ANGSTROMS) OF 30-194.
  2. "Cyclophilin from Trypanosoma Cruzi Bound to Cyclosporin A."
    (Sgpp), Consortium Structural Genomics of Pathogenic Protozoa
    Caruthers J.M., Hol W.G.J.
    Submitted (OCT-2004) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS) OF 30-194.
  3. "The genome sequence of Trypanosoma cruzi, etiologic agent of Chagas disease."
    El-Sayed N.M., Myler P.J., Bartholomeu D.C., Nilsson D., Aggarwal G., Tran A.N., Ghedin E., Worthey E.A., Delcher A.L., Blandin G., Westenberger S.J., Caler E., Cerqueira G.C., Branche C., Haas B., Anupama A., Arner E., Aslund L.
    , Attipoe P., Bontempi E., Bringaud F., Burton P., Cadag E., Campbell D.A., Carrington M., Crabtree J., Darban H., da Silveira J.F., de Jong P., Edwards K., Englund P.T., Fazelina G., Feldblyum T., Ferella M., Frasch A.C., Gull K., Horn D., Hou L., Huang Y., Kindlund E., Klingbeil M., Kluge S., Koo H., Lacerda D., Levin M.J., Lorenzi H., Louie T., Machado C.R., McCulloch R., McKenna A., Mizuno Y., Mottram J.C., Nelson S., Ochaya S., Osoegawa K., Pai G., Parsons M., Pentony M., Pettersson U., Pop M., Ramirez J.L., Rinta J., Robertson L., Salzberg S.L., Sanchez D.O., Seyler A., Sharma R., Shetty J., Simpson A.J., Sisk E., Tammi M.T., Tarleton R., Teixeira S., Van Aken S., Vogt C., Ward P.N., Wickstead B., Wortman J., White O., Fraser C.M., Stuart K.D., Andersson B.
    Science 309:409-415(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CL BrenerImported.

Entry informationi

Entry nameiQ4DPB9_TRYCC
AccessioniPrimary (citable) accession number: Q4DPB9
Entry historyi
Integrated into UniProtKB/TrEMBL: September 13, 2005
Last sequence update: September 13, 2005
Last modified: June 24, 2015
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.Imported

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.