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Protein

Thioredoxin H-type

Gene

PEC-2

Organism
Brassica campestris (Field mustard)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript leveli

Functioni

Participates in various redox reactions through the reversible oxidation of the active center dithiol to a disulfide. The H form is known to activate a number of cytosolic enzymes (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Thioredoxin H-type
Short name:
Trx-H
Gene namesi
Name:PEC-2
OrganismiBrassica campestris (Field mustard)
Taxonomic identifieri3711 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeBrassiceaeBrassica

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 123123Thioredoxin H-typePRO_0000120054Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi45 ↔ 48Redox-activePROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Interactioni

Protein-protein interaction databases

STRINGi3711.Bra027469.1-P.

Structurei

3D structure databases

ProteinModelPortaliO64432.
SMRiO64432. Positions 10-122.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 119118ThioredoxinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiKOG0907. Eukaryota.
COG0526. LUCA.
KOiK03671.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PANTHERiPTHR10438. PTHR10438. 1 hit.
PfamiPF00085. Thioredoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O64432-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAATAELIPA GEVIACHTVE DWNNKLKAAK ESNKLIVIDF TAVWCPPCRF
60 70 80 90 100
IAPIFVELAK KHLDVVFFKV DVDELATVAK EFDVQAMPTF VYMKGEEKLD
110 120
KVVGAAKEEI EAKLLKHSQV AAA
Length:123
Mass (Da):13,587
Last modified:August 1, 1998 - v1
Checksum:i8E0A18DB446F0172
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB010434 mRNA. Translation: BAA25681.1.
PIRiT14379.
RefSeqiNP_001288844.1. NM_001301915.1.
UniGeneiBra.4621.

Genome annotation databases

GeneIDi103839264.
KEGGibrp:103839264.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB010434 mRNA. Translation: BAA25681.1.
PIRiT14379.
RefSeqiNP_001288844.1. NM_001301915.1.
UniGeneiBra.4621.

3D structure databases

ProteinModelPortaliO64432.
SMRiO64432. Positions 10-122.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3711.Bra027469.1-P.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi103839264.
KEGGibrp:103839264.

Phylogenomic databases

eggNOGiKOG0907. Eukaryota.
COG0526. LUCA.
KOiK03671.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PANTHERiPTHR10438. PTHR10438. 1 hit.
PfamiPF00085. Thioredoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Molecular cloning of a cDNA encoding a pollen extracellular protein as a potential source of a pollen allergen in Brassica rapa."
    Toriyama K., Hanaoka K., Okada T., Watanabe M.
    FEBS Lett. 424:234-238(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Anther.

Entry informationi

Entry nameiTRXH_BRACM
AccessioniPrimary (citable) accession number: O64432
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: August 1, 1998
Last modified: November 11, 2015
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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.