Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q4DPB9 (Q4DPB9_TRYCC) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Peptidyl-prolyl cis-trans isomerase RuleBase RU000493

EC=5.2.1.8 RuleBase RU000493
Gene names
ORF Names:Tc00.1047053508577.140 EMBL EAN94378.1
OrganismTrypanosoma cruzi (strain CL Brener) [Complete proteome]
Taxonomic identifier353153 [NCBI]
Taxonomic lineageEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosomaSchizotrypanum

Protein attributes

Sequence length194 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). SAAS SAAS002130

Sequence similarities

Belongs to the cyclophilin-type PPIase family. RuleBase RU004223

Contains 1 PPIase cyclophilin-type domain. RuleBase RU003420

Contains PPIase cyclophilin-type domain. SAAS SAAS020892

Ontologies

Keywords
   Molecular functionIsomerase
Rotamase RuleBase RU003420 SAAS SAAS002130
   Technical term3D-structure PDB 1XQ7 PDB 1XO7
Complete proteome
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
Q4DPB9 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 688E90003CC958D5

FASTA19421,102
        10         20         30         40         50         60 
MRYLLLSKVT QLLLLLLLML SAAVSARADP VVTDKVYFDI TIGDEPVGRV VIGLFGNDVP 

        70         80         90        100        110        120 
KTVENFKQLA SGENGFGYKG SIFHRVIRNF MIQGGDFTNF DGTGGKSIYG TRFDDENLKI 

       130        140        150        160        170        180 
KHFVGAVSMA NAGPNSNGSQ FFVTTAPTPW LDGRHVVFGK VVEGMDVVKK VENTKTGLND 

       190 
KPKKAVKIND CGVL 

« Hide

References

« Hide 'large scale' references
[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.A., 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. expand/collapse author list , 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 Brener EMBL EAN94378.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAHK01000282 Genomic DNA. Translation: EAN94378.1.
RefSeqXP_816229.1. XM_811136.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1XO7X-ray1.61A/B/C/D30-194[»]
1XQ7X-ray2.07A/B/C30-194[»]
ProteinModelPortalQ4DPB9.
SMRQ4DPB9. Positions 30-194.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3548068.
KEGGtcr:508577.140.

Phylogenomic databases

KOK03768.

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

EvolutionaryTraceQ4DPB9.

Entry information

Entry nameQ4DPB9_TRYCC
AccessionPrimary (citable) accession number: Q4DPB9
Entry history
Integrated into UniProtKB/TrEMBL: September 13, 2005
Last sequence update: September 13, 2005
Last modified: June 11, 2014
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)