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Protein
Submitted name:

Tryparedoxin II

Gene

txnII

Organism
Crithidia fasciculata
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Names & Taxonomyi

Protein namesi
Submitted name:
Tryparedoxin IIImported
Gene namesi
Name:txnIIImported
OrganismiCrithidia fasciculataImported
Taxonomic identifieri5656 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeCrithidia

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi56 ↔ 59Combined sources

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FG4X-ray1.90A/B17-165[»]
1I5GX-ray1.40A17-160[»]
1O6JX-ray2.35A/B16-165[»]
1O81X-ray1.50A/B14-165[»]
1OC8X-ray1.50A/B14-165[»]
1OC9X-ray2.35A/B14-165[»]
ProteinModelPortaliO77093.
SMRiO77093. Positions 14-165.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO77093.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini28 – 165138ThioredoxinInterPro annotationAdd
BLAST

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF13905. Thioredoxin_8. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O77093-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYHTLLYDFR DSVPHMSGLK KFFPYSTNVL KGAAADIALP SLAGKTVFFY
60 70 80 90 100
FSASWCPPCR AFTPQLIDFY KAHAEKKNFE VMLISWDESA EDFKDYYAKM
110 120 130 140 150
PWLALPFEDR KGMEFLTTGF DVKSIPTLVG VEADSGNIIT TQARTMVVKD
160
PEAKDFPWPN VEAKK
Length:165
Mass (Da):18,786
Last modified:November 1, 1998 - v1
Checksum:i3DBAC208A32A1F67
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF055986 Genomic DNA. Translation: AAC61984.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF055986 Genomic DNA. Translation: AAC61984.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FG4X-ray1.90A/B17-165[»]
1I5GX-ray1.40A17-160[»]
1O6JX-ray2.35A/B16-165[»]
1O81X-ray1.50A/B14-165[»]
1OC8X-ray1.50A/B14-165[»]
1OC9X-ray2.35A/B14-165[»]
ProteinModelPortaliO77093.
SMRiO77093. Positions 14-165.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiO77093.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF13905. Thioredoxin_8. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Knight M.A., Drinkwater R.D.
    Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: HS6Imported.
  2. Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 17-160, DISULFIDE BONDS.
  3. "De novo phasing of two crystal forms of tryparedoxin II using the anomalous scattering from S atoms: a combination of small signal and medium resolution reveals this to be a general tool for solving protein crystal structures."
    Micossi E., Hunter W.N., Leonard G.A.
    Acta Crystallogr. D 58:21-28(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 14-165, DISULFIDE BONDS.
  4. "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 (1.50 ANGSTROMS) OF 14-165, DISULFIDE BONDS.

Entry informationi

Entry nameiO77093_CRIFA
AccessioniPrimary (citable) accession number: O77093
Entry historyi
Integrated into UniProtKB/TrEMBL: November 1, 1998
Last sequence update: November 1, 1998
Last modified: July 6, 2016
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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 one 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.