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Protein

Redox-sensing transcriptional repressor Rex

Gene

rex

Organism
Thermus aquaticus
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Modulates transcription in response to changes in cellular NADH/NAD+ redox state.UniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi13 – 5240H-T-H motifUniRule annotationAdd
BLAST
Nucleotide bindingi87 – 926NADUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, NAD

Names & Taxonomyi

Protein namesi
Recommended name:
Redox-sensing transcriptional repressor RexUniRule annotation
Gene namesi
Name:rexUniRule annotation
OrganismiThermus aquaticus
Taxonomic identifieri271 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 211211Redox-sensing transcriptional repressor RexPRO_0000097925Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation1 Publication

Protein-protein interaction databases

DIPiDIP-48428N.

Structurei

Secondary structure

1
211
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 2117Combined sources
Turni22 – 254Combined sources
Helixi31 – 388Combined sources
Helixi42 – 509Combined sources
Helixi64 – 7411Combined sources
Turni75 – 784Combined sources
Beta strandi81 – 877Combined sources
Helixi90 – 956Combined sources
Beta strandi103 – 1119Combined sources
Turni115 – 1195Combined sources
Beta strandi123 – 1286Combined sources
Beta strandi130 – 1323Combined sources
Helixi133 – 1353Combined sources
Turni138 – 1403Combined sources
Beta strandi143 – 1464Combined sources
Helixi150 – 16213Combined sources
Beta strandi166 – 1705Combined sources
Beta strandi172 – 1743Combined sources
Beta strandi182 – 1865Combined sources
Turni189 – 1924Combined sources
Helixi193 – 2019Combined sources
Turni203 – 2053Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XCBX-ray2.90A/B/C/D/E/F/G1-211[»]
ProteinModelPortaliQ9X2V5.
SMRiQ9X2V5. Positions 2-206.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9X2V5.

Family & Domainsi

Sequence similaritiesi

Belongs to the transcriptional regulatory Rex family.UniRule annotation

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.40.50.720. 1 hit.
HAMAPiMF_01131. Rex.
InterProiIPR003781. CoA-bd.
IPR016040. NAD(P)-bd_dom.
IPR009718. Rex_DNA-bd_C_dom.
IPR022876. Tscrpt_rep_Rex.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF02629. CoA_binding. 1 hit.
PF06971. Put_DNA-bind_N. 1 hit.
[Graphical view]
SMARTiSM00881. CoA_binding. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF51735. SSF51735. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9X2V5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVPEAAISR LITYLRILEE LEAQGVHRTS SEQLGELAQV TAFQVRKDLS
60 70 80 90 100
YFGSYGTRGV GYTVPVLKRE LRHILGLNRK WGLCIVGMGR LGSALADYPG
110 120 130 140 150
FGESFELRGF FDVDPEKVGR PVRGGVIEHV DLLPQRVPGR IEIALLTVPR
160 170 180 190 200
EAAQKAADLL VAAGIKGILN FAPVVLEVPK EVAVENVDFL AGLTRLSFAI
210
LNPKWREEMM G
Length:211
Mass (Da):23,222
Last modified:November 1, 1999 - v1
Checksum:iA49C2755DDB1D7EC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF061257 Genomic DNA. Translation: AAD22519.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF061257 Genomic DNA. Translation: AAD22519.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XCBX-ray2.90A/B/C/D/E/F/G1-211[»]
ProteinModelPortaliQ9X2V5.
SMRiQ9X2V5. Positions 2-206.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48428N.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ9X2V5.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.40.50.720. 1 hit.
HAMAPiMF_01131. Rex.
InterProiIPR003781. CoA-bd.
IPR016040. NAD(P)-bd_dom.
IPR009718. Rex_DNA-bd_C_dom.
IPR022876. Tscrpt_rep_Rex.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF02629. CoA_binding. 1 hit.
PF06971. Put_DNA-bind_N. 1 hit.
[Graphical view]
SMARTiSM00881. CoA_binding. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF51735. SSF51735. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Identification, cloning and expression of p25, an AT-rich DNA-binding protein from the extreme thermophile, Thermus aquaticus YT-1."
    Du X., Pene J.J.
    Nucleic Acids Res. 27:1690-1697(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-17, SUBUNIT.
    Strain: YT1.

Entry informationi

Entry nameiREX_THEAQ
AccessioniPrimary (citable) accession number: Q9X2V5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 16, 2004
Last sequence update: November 1, 1999
Last modified: December 9, 2015
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.