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.

B1LCZ5

- SYR_ECOSM

UniProt

B1LCZ5 - SYR_ECOSM

(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, EcSMS35_1310
Organism
Escherichia coli (strain SMS-3-5 / SECEC)
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

BioCyciECOL439855:GHHB-1308-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:EcSMS35_1310
OrganismiEscherichia coli (strain SMS-3-5 / SECEC)
Taxonomic identifieri439855 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000007011: 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_1000198902Add
BLAST

Interactioni

Subunit structurei

Monomer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi439855.EcSMS35_1310.

Structurei

3D structure databases

ProteinModelPortaliB1LCZ5.
SMRiB1LCZ5. 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.

B1LCZ5-1 [UniParc]FASTAAdd to Basket

« Hide

MNIQALLSEK VRQAMIAAGA PADCEPQVRQ SAKVQFGDYQ ANGMMAVAKK    50
LGMAPRQLAE QVLTHLDLNG IASKVEIAGP GFINIFLDPA FLADHVQQAL 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 DMPADELEKL ANAVGIGAVK YADLSKNRTT DYIFDWDNML 450
AFEGNTAPYM QYAYTRVLSV FRKAEIDEEQ LAAAPVIIRE DREAQLAARL 500
LQFEETLTVV AREGTPHVMC AYLYDLAGLF SGFYEHCPIL SAENEEVRNS 550
RLKLAQLTAK TLKLGLDTLG IETVERM 577
Length:577
Mass (Da):64,669
Last modified:April 29, 2008 - v1
Checksum:iAF6B3588404F372E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000970 Genomic DNA. Translation: ACB19180.1.
RefSeqiYP_001743368.1. NC_010498.1.

Genome annotation databases

EnsemblBacteriaiACB19180; ACB19180; EcSMS35_1310.
GeneIDi6147131.
KEGGiecm:EcSMS35_1310.
PATRICi18431485. VBIEscCol6161_1467.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000970 Genomic DNA. Translation: ACB19180.1 .
RefSeqi YP_001743368.1. NC_010498.1.

3D structure databases

ProteinModelPortali B1LCZ5.
SMRi B1LCZ5. Positions 1-577.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 439855.EcSMS35_1310.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACB19180 ; ACB19180 ; EcSMS35_1310 .
GeneIDi 6147131.
KEGGi ecm:EcSMS35_1310.
PATRICi 18431485. VBIEscCol6161_1467.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci ECOL439855:GHHB-1308-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. "Insights into the environmental resistance gene pool from the genome sequence of the multidrug-resistant environmental isolate Escherichia coli SMS-3-5."
    Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C., Ravel J., Stepanauskas R.
    J. Bacteriol. 190:6779-6794(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SMS-3-5 / SECEC.

Entry informationi

Entry nameiSYR_ECOSM
AccessioniPrimary (citable) accession number: B1LCZ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: April 29, 2008
Last modified: May 14, 2014
This is version 43 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