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O96438 (O96438_CRIFA) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 78. Feed History...

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

Names and origin

Protein names

Tryparedoxin I EMBL AAD20445.1
Gene names
Name:TryX EMBL AAC72299.1
Synonyms:txnI EMBL AAD20445.1
OrganismCrithidia fasciculata EMBL AAC72299.1
Taxonomic identifier5656 [NCBI]
Taxonomic lineageEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeCrithidia

Protein attributes

Sequence length146 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

Ontologies

Keywords
   Technical term3D-structure PDB 1O8W PDB 1OKD PDB 1O8X PDB 1O7U PDB 1O85 PDB 1EZK PDB 1EWX PDB 1QK8
Gene Ontology (GO)
None. [Check GOA]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Amino acid modifications

Modified residue21N-actyl X PDB 1EWX

Sequences

Sequence LengthMass (Da)Tools
O96438 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: C9663DE8FD803D43

FASTA14616,481
        10         20         30         40         50         60 
MSGLDKYLPG IEKLRRGDGE VEVKSLAGKL VFFYFSASWC PPCRGFTPQL IEFYDKFHES 

        70         80         90        100        110        120 
KNFEVVFCTW DEEEDGFAGY FAKMPWLAVP FAQSEAVQKL SKHFNVESIP TLIGVDADSG 

       130        140 
DVVTTRARAT LVKDPEGEQF PWKDAP 

« Hide

References

[1]"Sequence, heterologous expression and functional characterization of a novel tryparedoxin from Crithidia fasciculata."
Montemartini M., Kalisz H.M., Kiess M., Nogoceke E., Singh M., Steinert P., Flohe L.
Biol. Chem. 379:1137-1142(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: HS6 EMBL AAD20445.1.
[2]"Cloning, expression and reconstitution of the trypanothione-dependent peroxidase system of Crithidia fasciculata."
Tetaud E., Fairlamb A.H.
Mol. Biochem. Parasitol. 96:111-123(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[3]Guerrero S., Flohe L., Kalisz H.M., Montemartini M., Nogoceke E., Hecht H.-J., Steinert P., Singh M.
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: HS6 EMBL AAD20445.1.
[4]"Sequence, heterologous expression and functional characterization of tryparedoxin1 from Crithidia fasciculata."
Guerrero S.A., Flohe L., Kalisz H.M., Montemartini M., Nogoceke E., Hecht H.J., Steinert P., Singh M.
Eur. J. Biochem. 259:789-794(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: HS6 EMBL AAD20445.1.
[5]"The high resolution crystal structure of recombinant Crithidia fasciculata tryparedoxin-I."
Alphey M.S., Leonard G.A., Gourley D.G., Tetaud E., Fairlamb A.H., Hunter W.N.
J. Biol. Chem. 274:25613-25622(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS).
[6]"Structures of tryparedoxins revealing interaction with trypanothione."
Hofmann B., Budde H., Bruns K., Guerrero S.A., Kalisz H.M., Menge U., Montemartini M., Nogoceke E., Steinert P., Wissing J.B., Flohe L., Hecht H.J.
Biol. Chem. 382:459-471(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 2-146, N-ACTYL X AT SER-2.
[7]"NMR studies of the interaction of tryparedoxin with redox-inactive substrate homologues."
Krumme D., Budde H., Hecht H.J., Menge U., Ohlenschlager O., Ross A., Wissing J., Wray V., Flohe L.
Biochemistry 42:14720-14728(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[8]"Tryparedoxins from Crithidia fasciculata and Trypanosoma brucei: photoreduction of the redox disulfide using synchrotron radiation and evidence for a conformational switch implicated in function."
Alphey M.S., Gabrielsen M., Micossi E., Leonard G.A., McSweeney S.M., Ravelli R.B., Tetaud E., Fairlamb A.H., Bond C.S., Hunter W.N.
J. Biol. Chem. 278:25919-25925(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 1-42 AND 44-146.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF055913 Genomic DNA. Translation: AAC72299.1.
AF084456 Genomic DNA. Translation: AAD20445.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EWXX-ray1.70A2-146[»]
1EZKX-ray1.90A2-146[»]
1O7UX-ray1.50A1-146[»]
1O85X-ray1.50A1-146[»]
1O8WX-ray1.70A1-146[»]
1O8XX-ray1.30A1-42[»]
A44-146[»]
1OKDNMR-A1-146[»]
1QK8X-ray1.40A1-146[»]
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.30.10. 1 hit.
InterProIPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF13905. Thioredoxin_8. 1 hit.
[Graphical view]
SUPFAMSSF52833. SSF52833. 1 hit.
PROSITEPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO96438.

Entry information

Entry nameO96438_CRIFA
AccessionPrimary (citable) accession number: O96438
Entry history
Integrated into UniProtKB/TrEMBL: May 1, 1999
Last sequence update: May 1, 1999
Last modified: July 9, 2014
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)