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Q99W05

- SYR_STAAN

UniProt

Q99W05 - SYR_STAAN

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Protein

Arginine--tRNA ligase

Gene

argS

Organism
Staphylococcus aureus (strain N315)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

GO - Molecular functioni

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

BioCyciSAUR158879:GJCB-599-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Arginine--tRNA ligaseUniRule annotation (EC:6.1.1.19UniRule annotation)
Alternative name(s):
Arginyl-tRNA synthetaseUniRule annotation
Short name:
ArgRSUniRule annotation
Gene namesi
Name:argSUniRule annotation
Ordered Locus Names:SA0564
OrganismiStaphylococcus aureus (strain N315)
Taxonomic identifieri158879 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000000751: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 553553Arginine--tRNA ligasePRO_0000151607Add
BLAST

2D gel databases

SWISS-2DPAGEQ99W05.

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi158879.SA0564.

Structurei

3D structure databases

ProteinModelPortaliQ99W05.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi132 – 1409"HIGH" region

Sequence similaritiesi

Belongs to the class-I aminoacyl-tRNA synthetase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0018.
HOGENOMiHOG000247214.
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.

Q99W05-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNIIDQVKQT LVEEIAASIN KAGLADEIPD IKIEVPKDTK NGDYATNIAM
60 70 80 90 100
VLTKIAKRNP REIAQAIVDN LDTEKAHVKQ IDIAGPGFIN FYLDNQYLTA
110 120 130 140 150
IIPEAIEKGD QFGHVNESKG QNVLLEYVSA NPTGDLHIGH ARNAAVGDAL
160 170 180 190 200
ANILTAAGYN VTREYYINDA GNQITNLARS IETRFFEALG DNSYSMPEDG
210 220 230 240 250
YNGKDIIEIG KDLAEKHPEI KDYSEEARLK EFRKLGVEYE MAKLKNDLAE
260 270 280 290 300
FNTHFDNWFS ETSLYEKGEI LEVLAKMKEL GYTYEADGAT WLRTTDFKDD
310 320 330 340 350
KDRVLIKNDG TYTYFLPDIA YHFDKVKRGN DILIDLFGAD HHGYINRLKA
360 370 380 390 400
SLETFGVDSN RLEIQIMQMV RLMENGKEVK MSKRTGNAIT LREIMDEVGV
410 420 430 440 450
DAARYFLTMR SPDSHFDFDM ELAKEQSQDN PVYYAQYAHA RICSILKQAK
460 470 480 490 500
EQGIEVTAAN DFTTITNEKA IELLKKVADF EPTIESAAEH RSAHRITNYI
510 520 530 540 550
QDLAAHFHKF YNAEKVLTDD IEKTKAHVAM IEAVRITLKN ALAMVGVSAP

ESM
Length:553
Mass (Da):62,365
Last modified:June 1, 2001 - v1
Checksum:i84F0AAAA2212E30C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000018 Genomic DNA. Translation: BAB41796.1.
PIRiA89830.
RefSeqiNP_373818.1. NC_002745.2.

Genome annotation databases

EnsemblBacteriaiBAB41796; BAB41796; BAB41796.
GeneIDi1123370.
KEGGisau:SA0564.
PATRICi19573250. VBIStaAur116463_0595.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000018 Genomic DNA. Translation: BAB41796.1 .
PIRi A89830.
RefSeqi NP_373818.1. NC_002745.2.

3D structure databases

ProteinModelPortali Q99W05.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 158879.SA0564.

2D gel databases

SWISS-2DPAGE Q99W05.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAB41796 ; BAB41796 ; BAB41796 .
GeneIDi 1123370.
KEGGi sau:SA0564.
PATRICi 19573250. VBIStaAur116463_0595.

Phylogenomic databases

eggNOGi COG0018.
HOGENOMi HOG000247214.
KOi K01887.
OMAi MEHMGFG.
OrthoDBi EOG6JB13C.

Enzyme and pathway databases

BioCyci SAUR158879:GJCB-599-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

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: N315.
  2. Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: N315.
  3. "Shotgun proteomic analysis of total and membrane protein extracts of S. aureus strain N315."
    Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.
    Submitted (OCT-2007) to UniProtKB
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: N315.

Entry informationi

Entry nameiSYR_STAAN
AccessioniPrimary (citable) accession number: Q99W05
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: June 1, 2001
Last modified: October 29, 2014
This is version 89 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