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Protein
Submitted name:

Tryparedoxin peroxidase

Gene

TRYP3

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

Functioni

GO - Molecular functioni

  • peroxidase activity Source: UniProtKB-KW
  • peroxiredoxin activity Source: GeneDB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, PeroxidaseImported

Names & Taxonomyi

Protein namesi
Submitted name:
Tryparedoxin peroxidaseImported
Gene namesi
Name:TRYP3Imported
ORF Names:LMJF_15_1080Imported
OrganismiLeishmania majorImported
Taxonomic identifieri5664 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmania
Proteomesi
  • UP000000542 Componenti: Chromosome 15

Interactioni

Protein-protein interaction databases

STRINGi5664.LmjF.15.1080.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3TUEX-ray3.00A/B/C/D/E1-199[»]
4K1FX-ray2.34A/B/C/D/E1-199[»]
ProteinModelPortaliQ4QF76.
SMRiQ4QF76. Positions 6-178.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 165160ThioredoxinInterPro annotationAdd
BLAST

Phylogenomic databases

eggNOGiKOG0852. Eukaryota.
COG0450. LUCA.
HOGENOMiHOG000022343.
InParanoidiQ4QF76.
KOiK11185.
OMAiTHRRWIE.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view]
PIRSFiPIRSF000239. AHPC. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q4QF76-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSCGNAKINS PAPSFEEVAL MPNGSFKKIS LSSYKGKWVV LFFYPLDFTF
60 70 80 90 100
VCPTEVIAFS DSVSRFNELN CEVLACSIDS EYAHLQWTLQ DRKKGGLGTM
110 120 130 140 150
AIPMLADKTK SIARSYGVLE ESQGVAYRGL FIIDPHGMLR QITVNDMPVG
160 170 180 190
RSVEEVLRLL EAFQFVEKHG EVCPANWKKG APTMKPEPNA SVEGYFSKQ
Length:199
Mass (Da):22,128
Last modified:July 19, 2005 - v1
Checksum:iD820E63BC20FB355
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FR796411 Genomic DNA. Translation: CAJ03334.1.
RefSeqiXP_001682022.1. XM_001681970.1.

Genome annotation databases

EnsemblProtistsiLmjF.15.1080:mRNA; LmjF.15.1080:pep; LmjF.15.1080.
GeneIDi5650489.
KEGGilma:LMJF_15_1080.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FR796411 Genomic DNA. Translation: CAJ03334.1.
RefSeqiXP_001682022.1. XM_001681970.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3TUEX-ray3.00A/B/C/D/E1-199[»]
4K1FX-ray2.34A/B/C/D/E1-199[»]
ProteinModelPortaliQ4QF76.
SMRiQ4QF76. Positions 6-178.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5664.LmjF.15.1080.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsiLmjF.15.1080:mRNA; LmjF.15.1080:pep; LmjF.15.1080.
GeneIDi5650489.
KEGGilma:LMJF_15_1080.

Phylogenomic databases

eggNOGiKOG0852. Eukaryota.
COG0450. LUCA.
HOGENOMiHOG000022343.
InParanoidiQ4QF76.
KOiK11185.
OMAiTHRRWIE.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view]
PIRSFiPIRSF000239. AHPC. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome of the kinetoplastid parasite, Leishmania major."
    Ivens A.C., Peacock C.S., Worthey E.A., Murphy L., Aggarwal G., Berriman M., Sisk E., Rajandream M.A., Adlem E., Aert R., Anupama A., Apostolou Z., Attipoe P., Bason N., Bauser C., Beck A., Beverley S.M., Bianchettin G.
    , Borzym K., Bothe G., Bruschi C.V., Collins M., Cadag E., Ciarloni L., Clayton C., Coulson R.M., Cronin A., Cruz A.K., Davies R.M., De Gaudenzi J., Dobson D.E., Duesterhoeft A., Fazelina G., Fosker N., Frasch A.C., Fraser A., Fuchs M., Gabel C., Goble A., Goffeau A., Harris D., Hertz-Fowler C., Hilbert H., Horn D., Huang Y., Klages S., Knights A., Kube M., Larke N., Litvin L., Lord A., Louie T., Marra M., Masuy D., Matthews K., Michaeli S., Mottram J.C., Muller-Auer S., Munden H., Nelson S., Norbertczak H., Oliver K., O'neil S., Pentony M., Pohl T.M., Price C., Purnelle B., Quail M.A., Rabbinowitsch E., Reinhardt R., Rieger M., Rinta J., Robben J., Robertson L., Ruiz J.C., Rutter S., Saunders D., Schafer M., Schein J., Schwartz D.C., Seeger K., Seyler A., Sharp S., Shin H., Sivam D., Squares R., Squares S., Tosato V., Vogt C., Volckaert G., Wambutt R., Warren T., Wedler H., Woodward J., Zhou S., Zimmermann W., Smith D.F., Blackwell J.M., Stuart K.D., Barrell B., Myler P.J.
    Science 309:436-442(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MHOM/IL/81/FriedlinImported.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MHOM/IL/81/FriedlinImported.
  3. "The crystal structures of the tryparedoxin-tryparedoxin peroxidase couple unveil the structural determinants of Leishmania detoxification pathway."
    Fiorillo A., Colotti G., Boffi A., Baiocco P., Ilari A.
    PLoS Negl. Trop. Dis. 6:e1781-e1781(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS).
  4. "Structure-based discovery of the first non-covalent inhibitors of Leishmania major tryparedoxin peroxidase by high throughput docking."
    Brindisi M., Brogi S., Relitti N., Vallone A., Butini S., Gemma S., Novellino E., Colotti G., Angiulli G., Di Chiaro F., Fiorillo A., Ilari A., Campiani G.
    Sci. Rep. 5:9705-9705(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.34 ANGSTROMS).

Entry informationi

Entry nameiQ4QF76_LEIMA
AccessioniPrimary (citable) accession number: Q4QF76
Entry historyi
Integrated into UniProtKB/TrEMBL: July 19, 2005
Last sequence update: July 19, 2005
Last modified: July 6, 2016
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

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.