SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

A8A178

- SYR_ECOHS

UniProt

A8A178 - SYR_ECOHS

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Arginine--tRNA ligase
Gene
argS, EcHS_A1971
Organism
Escherichia coli O9:H4 (strain HS)
Status
Reviewed - Annotation score: 2 out of 5 - Protein inferred from homologyi

Functioni

Catalytic activityi

ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg).UniRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. arginine-tRNA ligase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. arginyl-tRNA aminoacylation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciECOL331112:GHHI-1963-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Arginine--tRNA ligase (EC:6.1.1.19)
Alternative name(s):
Arginyl-tRNA synthetase
Short name:
ArgRS
Gene namesi
Name:argS
Ordered Locus Names:EcHS_A1971
OrganismiEscherichia coli O9:H4 (strain HS)
Taxonomic identifieri331112 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000001123: Chromosome

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 577577Arginine--tRNA ligaseUniRule annotation
PRO_1000057809Add
BLAST

Interactioni

Subunit structurei

Monomer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi331112.EcHS_A1971.

Structurei

3D structure databases

ProteinModelPortaliA8A178.
SMRiA8A178. Positions 1-577.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi122 – 13211"HIGH" regionUniRule annotation
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0018.
HOGENOMiHOG000247212.
KOiK01887.
OMAiMEHMGFG.
OrthoDBiEOG6JB13C.

Family and domain databases

Gene3Di1.10.730.10. 1 hit.
3.30.1360.70. 1 hit.
3.40.50.620. 1 hit.
HAMAPiMF_00123. Arg_tRNA_synth.
InterProiIPR001412. aa-tRNA-synth_I_CS.
IPR001278. Arg-tRNA-ligase.
IPR005148. Arg-tRNA-synth_N.
IPR008909. DALR_anticod-bd.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
[Graphical view]
PANTHERiPTHR11956. PTHR11956. 1 hit.
PfamiPF03485. Arg_tRNA_synt_N. 1 hit.
PF05746. DALR_1. 1 hit.
PF00750. tRNA-synt_1d. 1 hit.
[Graphical view]
PRINTSiPR01038. TRNASYNTHARG.
SMARTiSM01016. Arg_tRNA_synt_N. 1 hit.
SM00836. DALR_1. 1 hit.
[Graphical view]
SUPFAMiSSF47323. SSF47323. 1 hit.
SSF55190. SSF55190. 1 hit.
TIGRFAMsiTIGR00456. argS. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A8A178-1 [UniParc]FASTAAdd to Basket

« Hide

MNIQALLSEK VRQAMIAAGA PADCEPQVRQ SAKVQFGDYQ ANGMMAVAKK    50
LGMAPRQLAE QVLTHLDLNG IASKVEIAGP GFINIFLDPA FLAEHVQQAL 100
ASDRLGVATP EKQTIVVDYS APNVAKEMHV GHLRSTIIGD AAVRTLEFLG 150
HKVIRANHVG DWGTQFGMLI AWLEKQQQEN AGEMELADLE GFYRDAKKHY 200
DEDEEFAERA RNYVVKLQSG DEYFREMWRK LVDITMTQNQ ITYDRLNVTL 250
TRDDVMGESL YNPMLPGIVA DLKAKGLAVE SEGATVVFLD EFKNKEGEPM 300
GVIIQKKDGG YLYTTTDIAC AKYRYETLHA DRVLYYIDSR QHQHLMQAWA 350
IVRKAGYVPE SVPLEHHMFG MMLGKDGKPF KTRAGGTVKL ADLLDEALER 400
ARRLVAEKNP DMPADGLEKL ANAVGIGAVK YADLSKNRTT DYIFDWDNML 450
AFEGNTAPYM QYAYTRVLSV FRKAEIDEEQ LAAAPVIIRE DREAQLAARL 500
LQFEETLTVV AREGTPHVMC AYLYDLAGLF SGFYEHCPIL SAENEEVRNS 550
RLKLAQLTAK TLKLGLDTLG IETVERM 577
Length:577
Mass (Da):64,611
Last modified:October 23, 2007 - v1
Checksum:iB38C0DFA7A3999BB
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000802 Genomic DNA. Translation: ABV06282.1.
RefSeqiYP_001458665.1. NC_009800.1.

Genome annotation databases

EnsemblBacteriaiABV06282; ABV06282; EcHS_A1971.
GeneIDi5592842.
KEGGiecx:EcHS_A1971.
PATRICi18313920. VBIEscCol77814_1931.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000802 Genomic DNA. Translation: ABV06282.1 .
RefSeqi YP_001458665.1. NC_009800.1.

3D structure databases

ProteinModelPortali A8A178.
SMRi A8A178. Positions 1-577.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 331112.EcHS_A1971.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABV06282 ; ABV06282 ; EcHS_A1971 .
GeneIDi 5592842.
KEGGi ecx:EcHS_A1971.
PATRICi 18313920. VBIEscCol77814_1931.

Phylogenomic databases

eggNOGi COG0018.
HOGENOMi HOG000247212.
KOi K01887.
OMAi MEHMGFG.
OrthoDBi EOG6JB13C.

Enzyme and pathway databases

BioCyci ECOL331112:GHHI-1963-MONOMER.

Family and domain databases

Gene3Di 1.10.730.10. 1 hit.
3.30.1360.70. 1 hit.
3.40.50.620. 1 hit.
HAMAPi MF_00123. Arg_tRNA_synth.
InterProi IPR001412. aa-tRNA-synth_I_CS.
IPR001278. Arg-tRNA-ligase.
IPR005148. Arg-tRNA-synth_N.
IPR008909. DALR_anticod-bd.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
[Graphical view ]
PANTHERi PTHR11956. PTHR11956. 1 hit.
Pfami PF03485. Arg_tRNA_synt_N. 1 hit.
PF05746. DALR_1. 1 hit.
PF00750. tRNA-synt_1d. 1 hit.
[Graphical view ]
PRINTSi PR01038. TRNASYNTHARG.
SMARTi SM01016. Arg_tRNA_synt_N. 1 hit.
SM00836. DALR_1. 1 hit.
[Graphical view ]
SUPFAMi SSF47323. SSF47323. 1 hit.
SSF55190. SSF55190. 1 hit.
TIGRFAMsi TIGR00456. argS. 1 hit.
PROSITEi PS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
    Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.
    J. Bacteriol. 190:6881-6893(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HS.

Entry informationi

Entry nameiSYR_ECOHS
AccessioniPrimary (citable) accession number: A8A178
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 23, 2007
Last modified: May 14, 2014
This is version 44 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

Complete proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi