SYRC_CHICK
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 03-AUG-2022, entry version 94.
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.ENSGALP00000002862; -.
DR PaxDb; Q5ZM11; -.
DR GeneID; 416168; -.
DR KEGG; gga:416168; -.
DR CTD; 104458; -.
DR VEuPathDB; HostDB:geneid_416168; -.
DR eggNOG; KOG4426; Eukaryota.
DR InParanoid; Q5ZM11; -.
DR OrthoDB; 463402at2759; -.
DR PhylomeDB; Q5ZM11; -.
DR PRO; PR:Q5ZM11; -.
DR Proteomes; UP000000539; Unplaced.
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; -; 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 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
