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P40329

- SYRC_RAT

UniProt

P40329 - SYRC_RAT

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Protein

Arginine--tRNA ligase, cytoplasmic

Gene

Rars

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Forms part of a macromolecular complex that catalyzes the attachment of specific amino acids to cognate tRNAs during protein synthesis. Modulates the secretion of AIMP1 and may be involved in generation of the inflammatory cytokine EMAP2 from AIMP1 (By similarity).By similarity

Catalytic activityi

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

GO - Molecular functioni

  1. arginine binding Source: RGD
  2. arginine-tRNA ligase activity Source: RGD
  3. ATP binding Source: RGD
  4. tRNA binding Source: RGD

GO - Biological processi

  1. arginyl-tRNA aminoacylation Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Arginine--tRNA ligase, cytoplasmic (EC:6.1.1.19)
Alternative name(s):
Arginyl-tRNA synthetase
Short name:
ArgRS
Gene namesi
Name:Rars
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 10

Organism-specific databases

RGDi1309215. Rars.

Subcellular locationi

GO - Cellular componenti

  1. aminoacyl-tRNA synthetase multienzyme complex Source: RGD
  2. extracellular vesicular exosome Source: Ensembl
  3. mitochondrion Source: Ensembl
  4. nucleus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 660660Arginine--tRNA ligase, cytoplasmicPRO_0000151660Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiP40329.

Expressioni

Gene expression databases

GenevestigatoriP40329.

Interactioni

Subunit structurei

Interacts (via N-terminus) with AIMP1 (via N-terminus); this stimulates its catalytic activity. Interacts with EPRS (via N-terminus). Interacts with LARS2. Monomer; also part of a multisubunit complex that groups tRNA ligases for Arg, Asp, Glu, Gln, Ile, Leu, Lys, Met and Pro (By similarity). Interacts with QARS (By similarity).By similarity

Protein-protein interaction databases

BioGridi252058. 1 interaction.
STRINGi10116.ENSRNOP00000010252.

Structurei

3D structure databases

ProteinModelPortaliP40329.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 7272Could be involved in the assembly of the multisynthetase complexBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi201 – 21212"HIGH" regionBy similarityAdd
BLAST

Domaini

The N-terminus (AA 1-72) has two regions predicted to be alpha-helical that might be involved in the multisynthetase complex assembly.By similarity

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00530000063407.
HOGENOMiHOG000247212.
HOVERGENiHBG029238.
InParanoidiP40329.
KOiK01887.
OMAiKCFDILG.
OrthoDBiEOG764725.
PhylomeDBiP40329.
TreeFamiTF106111.

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.

P40329-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDGLVAQCSA RLLQQEKEIK SLTAEIDRLK NCSYLEASPS LEQLREENLK
60 70 80 90 100
LKYRLNILRR SLQAERKRPT KNMININSRL QELFGCAIKA AYPDLENPPL
110 120 130 140 150
VVTPSQQPKF GDYQCNSAMG ISQMLKAKEQ KVSPREIAEN ITKHLPNNEY
160 170 180 190 200
IDRVEIAGPG FINVHLRKDF VSEQLTNLLV NGVQLPVLGE NEKVIVDFSS
210 220 230 240 250
PNIAKEMHVG HLRSTIIGES MSRLFEFAGY NVLRLNHVGD WGTQFGMLIA
260 270 280 290 300
HLQDKFPDYL TVSPPIGDLQ AFYKESKKRF DTEEEFKKRA YECVVLLQSK
310 320 330 340 350
NPDIMKAWNL ICDVSREEFN KIYDALDITL IERGESFYQD RMKDIVKEFE
360 370 380 390 400
DKGFVQVDDG RKIVFVPGCS VPLTIVKSDG GYTYDTSDLA AIKQRLFEEK
410 420 430 440 450
ANKIIYVVDN GQATHFQTVF AAAQMIGWYD PKVTRVAHVG FGVVLGEDKK
460 470 480 490 500
KFKTRSGETV RLMDLLEEGL RRSMDKLKEK ERDKVLTEEE LKAAQTSVAY
510 520 530 540 550
GCIKYADLSH NRLNDYVFSF DKMLDDRGNT AAYLLYAFTR IRSIARLANI
560 570 580 590 600
DEEMLQRAAR ETKIILDHEK EWKLGRCILR FPEILQKILD DLFLHTLCDY
610 620 630 640 650
IYELATTFTE FYDSCYCVEK DRQTGKVLKV NMWRMLLCEA VAAVMAKGFD
660
ILGIKPVQRM
Length:660
Mass (Da):75,810
Last modified:July 13, 2010 - v2
Checksum:i3C2D718AECDC4655
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC161929 mRNA. Translation: AAI61929.1.
PIRiA35857.
RefSeqiNP_001099247.2. NM_001105777.2.
UniGeneiRn.18711.

Genome annotation databases

EnsembliENSRNOT00000010252; ENSRNOP00000010252; ENSRNOG00000007739.
GeneIDi287191.
KEGGirno:287191.
UCSCiRGD:1309215. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC161929 mRNA. Translation: AAI61929.1 .
PIRi A35857.
RefSeqi NP_001099247.2. NM_001105777.2.
UniGenei Rn.18711.

3D structure databases

ProteinModelPortali P40329.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 252058. 1 interaction.
STRINGi 10116.ENSRNOP00000010252.

Proteomic databases

PRIDEi P40329.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000010252 ; ENSRNOP00000010252 ; ENSRNOG00000007739 .
GeneIDi 287191.
KEGGi rno:287191.
UCSCi RGD:1309215. rat.

Organism-specific databases

CTDi 5917.
RGDi 1309215. Rars.

Phylogenomic databases

GeneTreei ENSGT00530000063407.
HOGENOMi HOG000247212.
HOVERGENi HBG029238.
InParanoidi P40329.
KOi K01887.
OMAi KCFDILG.
OrthoDBi EOG764725.
PhylomeDBi P40329.
TreeFami TF106111.

Miscellaneous databases

NextBioi 625686.

Gene expression databases

Genevestigatori P40329.

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. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Brown Norway/NHsdMcwi.
    Tissue: Liver.
  2. "Existence of two forms of rat liver arginyl-tRNA synthetase suggests channeling of aminoacyl-tRNA for protein synthesis."
    Sivaram P., Deutscher M.P.
    Proc. Natl. Acad. Sci. U.S.A. 87:3665-3669(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 73-92.

Entry informationi

Entry nameiSYRC_RAT
AccessioniPrimary (citable) accession number: P40329
Secondary accession number(s): B1WBX8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: July 13, 2010
Last modified: November 26, 2014
This is version 81 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference 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