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Protein

Arginine repressor

Gene

argR

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Regulates arginine biosynthesis genes.UniRule annotation

Pathwayi: L-arginine biosynthesis

This protein regulates the pathway L-arginine biosynthesis, which is part of Amino-acid biosynthesis.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway L-arginine biosynthesis and in Amino-acid biosynthesis.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

RepressorUniRule annotation

Keywords - Biological processi

Amino-acid biosynthesis, Arginine biosynthesisUniRule annotation, Transcription, Transcription regulationUniRule annotationSAAS annotation

Keywords - Ligandi

DNA-bindingUniRule annotationSAAS annotation

Enzyme and pathway databases

UniPathwayiUPA00068.

Names & Taxonomyi

Protein namesi
Recommended name:
Arginine repressorUniRule annotation
Gene namesi
Name:argRUniRule annotationImported
OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)Imported
Taxonomic identifieri1422 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Subcellular locationi

  • Cytoplasm UniRule annotationSAAS annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

CytoplasmUniRule annotationSAAS annotation

Structurei

3D structure databases

ProteinModelPortaliQ9ZEV1.
SMRiQ9ZEV1. Positions 4-149.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 7070Arg_repressorInterPro annotationAdd
BLAST
Domaini81 – 14464Arg_repressor_CInterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ArgR family.UniRule annotationSAAS annotation

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.30.1360.40. 1 hit.
HAMAPiMF_00173. Arg_repressor.
InterProiIPR001669. Arg_repress.
IPR020899. Arg_repress_C.
IPR024946. Arg_repress_C-like.
IPR020900. Arg_repress_DNA-bd.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF01316. Arg_repressor. 1 hit.
PF02863. Arg_repressor_C. 1 hit.
[Graphical view]
PRINTSiPR01467. ARGREPRESSOR.
ProDomiPD007402. Arg_repress. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF55252. SSF55252. 1 hit.
TIGRFAMsiTIGR01529. argR_whole. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9ZEV1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKGQRHIKI REIIMNHEIE TQDELVDMLK KAGFNVTQAT VSRDIKELQL
60 70 80 90 100
VKVPMANGRY KYSLPSDQRF NPTQKLKRAL MDAFVKLDGS GNLLVLKTLP
110 120 130 140
GNAHAIGVLL DNLDWNEIVG TICGDDTCLI ICRTAEDAEK VSGQLLGML
Length:149
Mass (Da):16,620
Last modified:May 1, 1999 - v1
Checksum:i09D9CD8A20F1FDA7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ010954 Genomic DNA. Translation: CAA09426.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ010954 Genomic DNA. Translation: CAA09426.1.

3D structure databases

ProteinModelPortaliQ9ZEV1.
SMRiQ9ZEV1. Positions 4-149.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00068.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.30.1360.40. 1 hit.
HAMAPiMF_00173. Arg_repressor.
InterProiIPR001669. Arg_repress.
IPR020899. Arg_repress_C.
IPR024946. Arg_repress_C-like.
IPR020900. Arg_repress_DNA-bd.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF01316. Arg_repressor. 1 hit.
PF02863. Arg_repressor_C. 1 hit.
[Graphical view]
PRINTSiPR01467. ARGREPRESSOR.
ProDomiPD007402. Arg_repress. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF55252. SSF55252. 1 hit.
TIGRFAMsiTIGR01529. argR_whole. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Fort C.
    Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: ATCC 31783Imported.
  2. "Mutational analysis of highly thermostable arginine repressor from Bacillus stearothermophilus."
    Miltcheva I., Weigel P., Takahashi M., Cecile F.
    Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: ATCC 31783Imported.

Entry informationi

Entry nameiQ9ZEV1_GEOSE
AccessioniPrimary (citable) accession number: Q9ZEV1
Entry historyi
Integrated into UniProtKB/TrEMBL: May 1, 1999
Last sequence update: May 1, 1999
Last modified: June 8, 2016
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

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.