SYRC_CAEEL
ID SYRC_CAEEL Reviewed; 713 AA.
AC Q19825;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Probable arginine--tRNA ligase, cytoplasmic;
DE EC=6.1.1.19 {ECO:0000250|UniProtKB:P54136};
DE AltName: Full=Arginyl-tRNA synthetase;
DE Short=ArgRS;
GN Name=rars-1 {ECO:0000312|WormBase:F26F4.10a};
GN Synonyms=rrt-1 {ECO:0000312|WormBase:F26F4.10a};
GN ORFNames=F26F4.10 {ECO:0000312|WormBase:F26F4.10a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Forms part of a macromolecular complex that catalyzes the
CC attachment of specific amino acids to cognate tRNAs during protein
CC synthesis. {ECO:0000250|UniProtKB:P54136}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-
CC tRNA(Arg); Xref=Rhea:RHEA:20301, Rhea:RHEA-COMP:9658, Rhea:RHEA-
CC COMP:9673, ChEBI:CHEBI:30616, ChEBI:CHEBI:32682, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78513, ChEBI:CHEBI:456215;
CC EC=6.1.1.19; Evidence={ECO:0000250|UniProtKB:P54136};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P54136}.
CC Cytoplasm, cytosol {ECO:0000250|UniProtKB:P54136}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FO080682; CCD65757.1; -; Genomic_DNA.
DR PIR; T16176; T16176.
DR RefSeq; NP_001022551.1; NM_001027380.5.
DR AlphaFoldDB; Q19825; -.
DR SMR; Q19825; -.
DR BioGRID; 40893; 10.
DR STRING; 6239.F26F4.10a.1; -.
DR iPTMnet; Q19825; -.
DR EPD; Q19825; -.
DR PaxDb; Q19825; -.
DR PeptideAtlas; Q19825; -.
DR EnsemblMetazoa; F26F4.10a.1; F26F4.10a.1; WBGene00004679.
DR EnsemblMetazoa; F26F4.10a.2; F26F4.10a.2; WBGene00004679.
DR GeneID; 175659; -.
DR KEGG; cel:CELE_F26F4.10; -.
DR UCSC; F26F4.10b.1; c. elegans.
DR CTD; 175659; -.
DR WormBase; F26F4.10a; CE29495; WBGene00004679; rars-1.
DR eggNOG; KOG4426; Eukaryota.
DR InParanoid; Q19825; -.
DR OMA; NKPLHLG; -.
DR OrthoDB; 463402at2759; -.
DR PhylomeDB; Q19825; -.
DR BRENDA; 6.1.1.19; 1045.
DR SignaLink; Q19825; -.
DR PRO; PR:Q19825; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00004679; Expressed in germ line (C elegans) and 4 other tissues.
DR ExpressionAtlas; Q19825; baseline.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0004814; F:arginine-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006420; P:arginyl-tRNA aminoacylation; IBA:GO_Central.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0006412; P:translation; IMP:UniProtKB.
DR CDD; cd00671; ArgRS_core; 1.
DR Gene3D; 3.30.1360.70; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00123; Arg_tRNA_synth; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR001278; Arg-tRNA-ligase.
DR InterPro; IPR005148; Arg-tRNA-synth_N.
DR InterPro; IPR036695; Arg-tRNA-synth_N_sf.
DR InterPro; IPR035684; ArgRS_core.
DR InterPro; IPR008909; DALR_anticod-bd.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR PANTHER; PTHR11956; PTHR11956; 1.
DR Pfam; PF03485; Arg_tRNA_synt_N; 1.
DR Pfam; PF05746; DALR_1; 1.
DR Pfam; PF00750; tRNA-synt_1d; 1.
DR PRINTS; PR01038; TRNASYNTHARG.
DR SMART; SM01016; Arg_tRNA_synt_N; 1.
DR SMART; SM00836; DALR_1; 1.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF55190; SSF55190; 1.
DR TIGRFAMs; TIGR00456; argS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..713
FT /note="Probable arginine--tRNA ligase, cytoplasmic"
FT /id="PRO_0000151661"
FT REGION 74..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..597
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250|UniProtKB:Q05506"
FT MOTIF 252..263
FT /note="'HIGH' region"
FT COMPBIAS 77..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 252..254
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P54136"
FT BINDING 263
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P54136"
FT BINDING 438
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P54136"
FT BINDING 442
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P54136"
FT BINDING 466
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P54136"
SQ SEQUENCE 713 AA; 80896 MW; AC3268576C8D5BC4 CRC64;
MSANKELQQG YSDYSAASDQ AALLNRLITA MQKGELTDEL LEHIPELGDA KKLNDKLKYR
KSILEKSIAE QAAKNKKNGV KATSTSSPSS STSAPAEKKA KKDGKTGGAP PKQAKKVDYV
TVEDYGSSIF GRLQSLFKKA IEDAFPGLDV PLLLAETPNP QFGDYQCNSA MPIAAKLKAN
KINKRPGDVA KEIQAKLPTK IDFVEKIDVM PAGFINIFLN TDYLRRQISL LASEGVKLPK
LTRKRVLVDF SSPNIAKEMH VGHLRSTIIG DSICRLFEAV GFDVLRVNHI GDWGTQFGML
IAHLYDRFPD FLKKLPDISD LQAFYKESKK RFDEDEQFKK RAYEYVVKLQ SHDGDIVKAW
NTICDVSKKY NQIVYNYLDI KIKDVGESFY QDKMIELVKW VKTNKPDMLR EEDGRQIMFP
TGCDIPLTVV KSDGGFTYDT SDLAALKYRM LEEKCDWNIY VVDSGQSLHL ETVYAAGRDF
GWYDESIQRV EHVAFGLVLG DDKKKFKTRS GETVRLLDLL SEGVKRATEK LIEKGRETAM
SEEQLVAARD AVAFGCVKYA DLSHTRTQDY VFSFDRMLED RGNTAVYLLY AYTRIQSIFE
KDEVKNVDLV KYIASTPTLP LDHPGEFKLA KQLLKLSDCV LLVLDSLMLH QMCDYVYQLA
TLFHDFYNEC YVIENKEGEK PFVHMHRLAL CDVTRKVMST CFKILGLREV NKM
