ID   SYRC_CHICK              Reviewed;         661 AA.
AC   Q5ZM11;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   27-MAR-2024, entry version 100.
DE   RecName: Full=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=RARS1; Synonyms=RARS; ORFNames=RCJMB04_3h11;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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   -!- SUBUNIT: Monomer; also part of a multisubunit complex that groups tRNA
CC       ligases for Arg, Asp, Glu, Gln, Ile, Leu, Lys, Met and Pro.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P54136}.
CC       Cytoplasm, cytosol {ECO:0000250|UniProtKB:P54136}.
CC   -!- DOMAIN: The alpha-helical N-terminus (residues 1-72) mediates
CC       interaction with AIMP1 and thereby contributes to the assembly of the
CC       multisynthetase complex. {ECO:0000250|UniProtKB:P54136}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; AJ719573; CAG31232.1; -; mRNA.
DR   RefSeq; NP_001025778.1; NM_001030607.1.
DR   AlphaFoldDB; Q5ZM11; -.
DR   SMR; Q5ZM11; -.
DR   STRING; 9031.ENSGALP00000053061; -.
DR   PaxDb; 9031-ENSGALP00000002862; -.
DR   GeneID; 416168; -.
DR   KEGG; gga:416168; -.
DR   CTD; 416168; -.
DR   VEuPathDB; HostDB:geneid_416168; -.
DR   eggNOG; KOG4426; Eukaryota.
DR   InParanoid; Q5ZM11; -.
DR   PhylomeDB; Q5ZM11; -.
DR   PRO; PR:Q5ZM11; -.
DR   Proteomes; UP000000539; Unassembled WGS sequence.
DR   GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006420; P:arginyl-tRNA aminoacylation; ISS:UniProtKB.
DR   CDD; cd00671; ArgRS_core; 1.
DR   Gene3D; 3.30.1360.70; Arginyl tRNA synthetase N-terminal domain; 1.
DR   Gene3D; 3.40.50.620; HUPs; 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   NCBIfam; TIGR00456; argS; 1.
DR   PANTHER; PTHR11956:SF5; ARGININE--TRNA LIGASE, CYTOPLASMIC-RELATED; 1.
DR   PANTHER; PTHR11956; ARGINYL-TRNA SYNTHETASE; 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; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF55190; Arginyl-tRNA synthetase (ArgRS), N-terminal 'additional' domain; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   2: Evidence at transcript level;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..661
FT                   /note="Arginine--tRNA ligase, cytoplasmic"
FT                   /id="PRO_0000250729"
FT   REGION          1..72
FT                   /note="Could be involved in the assembly of the
FT                   multisynthetase complex"
FT                   /evidence="ECO:0000250"
FT   REGION          530..544
FT                   /note="Interaction with tRNA"
FT                   /evidence="ECO:0000250|UniProtKB:Q05506"
FT   MOTIF           202..213
FT                   /note="'HIGH' region"
FT   BINDING         201..203
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P54136"
FT   BINDING         212
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P54136"
FT   BINDING         385
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P54136"
FT   BINDING         389
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P54136"
FT   BINDING         413
FT                   /ligand="L-arginine"
FT                   /ligand_id="ChEBI:CHEBI:32682"
FT                   /evidence="ECO:0000250|UniProtKB:P54136"
SQ   SEQUENCE   661 AA;  75418 MW;  92D61B5BB5BC030B CRC64;
     MEARVAEAAA RLARQENEIK SLTAEIEHLK NFGCLGISPS LEGLRDENAK LKYRLNFLQK
     SLQEEQSKTV KSMININSRL QEIFGAAIQA AYPELENPPL VVTPSQQPKF GDYQCNSAMG
     ITQILLKTKE QKVSPREIAE KITKHIPANE CIEKVEIAGP GFINVHLRKD FVSKQLSSLL
     VNGVQPPAIG KRKKVILDFS SPNIAKEMHV GHLRSTIIGE SMCRLFEFAG YDVLRLNHLG
     DWGTQFGMLI AHLQDRFPDY LTVSPPIGDL QAFYKESKRR FDTEEEFKKR AYQCVVLLQS
     KDPDFIKAWE LICDVSRKEF QKIYNCLDVT LTERGESFYQ DMMKDIVKEF EDKGFVQVDD
     GRKIVFVPGF SVPLTIMKSD GGYTYDTSDL AALRHRLLEE KGDILIYVVD SGQSVHLQTV
     FAAGQMIGWY DPKVTRITHA AFGVVLGEDK KKFKTRSGDT VRLMDLLEEG LKRAMDKLKD
     KERDKVLTPE ELKAAQMSVA FGCIKYADLS HNRLNDYVFS FDKMLDDRGN TAAYLLYAFT
     RIRAIARLAN IDEGMLRKAA REEVIVLDHE KEWKLGKCIL RFPEILQKIL DDLLLHTLCD
     YLYELATTFT EFYDNCYCVE KDRQSGQIMK VNTWRLLLCE ATATIMAKGF DILGIKPVER
     M
//