ID A0A2K6RVV3_RHIRO Unreviewed; 660 AA.
AC A0A2K6RVV3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Arginine--tRNA ligase, cytoplasmic {ECO:0000256|ARBA:ARBA00022171};
DE EC=6.1.1.19 {ECO:0000256|ARBA:ARBA00012837};
DE AltName: Full=Arginyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00033033};
GN Name=RARS1 {ECO:0000313|Ensembl:ENSRROP00000045157.1};
OS Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000045157.1, ECO:0000313|Proteomes:UP000233200};
RN [1] {ECO:0000313|Ensembl:ENSRROP00000045157.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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:0000256|ARBA:ARBA00001766};
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363038}.
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DR RefSeq; XP_010356495.1; XM_010358193.1.
DR AlphaFoldDB; A0A2K6RVV3; -.
DR STRING; 61622.ENSRROP00000045157; -.
DR Ensembl; ENSRROT00000069677.1; ENSRROP00000045157.1; ENSRROG00000045496.1.
DR GeneID; 104658235; -.
DR KEGG; rro:104658235; -.
DR CTD; 5917; -.
DR GeneTree; ENSGT00530000063407; -.
DR OMA; CKSMLAW; -.
DR OrthoDB; 67085at2759; -.
DR Proteomes; UP000233200; Unplaced.
DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:Ensembl.
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 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|RuleBase:RU363038};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363038};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363038};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363038};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363038};
KW Reference proteome {ECO:0000313|Proteomes:UP000233200}.
FT DOMAIN 78..166
FT /note="Arginyl tRNA synthetase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01016"
FT DOMAIN 534..660
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
FT COILED 5..61
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 660 AA; 75363 MW; F58CA5DD60F907D1 CRC64;
MDGLVSECSA RLLQQEEEIK SLTAEIDRLK NCGCLGASPN LEQLQEENLK LKYRLNILQK
SLQAERNKPT KNMININSRL QEVFGHAIKA AYPDLENPPL LVTPSQQPKF GDYQCNSAMG
ISQMLKTKEQ KVNPREIAEN ITKHLPDNEC IEKVEIAGPG FINVHLRKDF VSEQLTSLLV
NGIQLPAVGE NKKVIVDFSS PNIAKEMHVG HLRSTIIGES ISRLFEFAGY DVLRLNHVGD
WGTQFGMLIA HLQDKFPDYL TVSPPIGDLQ AFYKESKKRF DTEEEFKKRA YQCVVLLQGK
NPDITKAWKL ICDVSRQEFN KIYDALDVSL IERGESFYQD RMNDIVKEFE DRGFVQVDDG
RKIVFVPGCS IPLTIVKSDG GYTYDTSDLA AIKQRLFEEK ADMVIYVVDS GQSVHFQTIF
AAAQMIGWYD PKVTRVFHAG FGVVLGEDKK KFKTRSGETV RLMDLMGEGL KRSMDKLKEK
ERDKVLTAEE LNAAQTSIAY GCIKYADLSH NRLNDYIFSF DKMLDDRGNT AAYLLYAFTR
IRSIARLANI DEEMLQKAAR ETKILLDHEK EWKLGRCILR FPEILQKILD DLFLHTLCDY
IYELATTFTE FYDSCYCVEK DRQTGKILKV NMWRMLLCEA VAAVMAKGFD ILGIKPVQRM
//
