SYRC_PONAB
ID SYRC_PONAB Reviewed; 660 AA.
AC Q5RA20; Q5NVH0;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 84.
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;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Forms part of a macromolecular complex that catalyzes the
CC attachment of specific amino acids to cognate tRNAs during protein
CC synthesis. Modulates the secretion of AIMP1 and may be involved in
CC generation of the inflammatory cytokine EMAP2 from AIMP1.
CC {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: Interacts (via N-terminus) with AIMP1 (via N-terminus); this
CC stimulates its catalytic activity. Interacts (via N-terminus) with
CC LARS2 (via C-terminus). Monomer. Part of a multisubunit complex that
CC groups tRNA ligases for Arg (RARS1), Asp (DARS1), Gln (QARS1), Ile
CC (IARS1), Leu (LARS1), Lys (KARS1), Met (MARS1) the bifunctional ligase
CC for Glu and Pro (EPRS1) and the auxiliary subunits AIMP1/p43, AIMP2/p38
CC and EEF1E1/p18. Interacts with QARS1. Part of a complex composed of
CC RARS1, QARS1 and AIMP1. {ECO:0000250|UniProtKB:P54136}.
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; CR859203; CAH91390.1; -; mRNA.
DR EMBL; CR926065; CAI29693.1; -; mRNA.
DR RefSeq; NP_001127107.1; NM_001133635.1.
DR AlphaFoldDB; Q5RA20; -.
DR SMR; Q5RA20; -.
DR STRING; 9601.ENSPPYP00000017935; -.
DR GeneID; 100174147; -.
DR KEGG; pon:100174147; -.
DR CTD; 5917; -.
DR eggNOG; KOG4426; Eukaryota.
DR InParanoid; Q5RA20; -.
DR OrthoDB; 463402at2759; -.
DR Proteomes; UP000001595; 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 Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..660
FT /note="Arginine--tRNA ligase, cytoplasmic"
FT /id="PRO_0000250728"
FT REGION 1..72
FT /note="Could be involved in the assembly of the
FT multisynthetase complex"
FT REGION 529..543
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250|UniProtKB:Q05506"
FT MOTIF 201..212
FT /note="'HIGH' region"
FT BINDING 200..202
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P54136"
FT BINDING 211
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P54136"
FT BINDING 384
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P54136"
FT BINDING 388
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P54136"
FT BINDING 412
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P54136"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P54136"
FT CONFLICT 164
FT /note="I -> V (in Ref. 1; CAI29693)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="V -> A (in Ref. 1; CAI29693)"
FT /evidence="ECO:0000305"
FT CONFLICT 402
FT /note="Missing (in Ref. 1; CAI29693)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 660 AA; 75344 MW; C114CA5ED797D8E8 CRC64;
MDVLVTECSA RLLQQEEEIK SLTAEIDRLK NCGCLGASAN LEQLQEENLK LKYRLNILQK
SLQAERNKPT KNMINVISRL QEVFGHAIKA AYPDLENPPL LVTPSQQAKF GDYQCNSAMG
ISQMLKTKEQ KVNPREIAEN ITKHLPDNEC IEKVEIAGPG FINIHLRKDF VSEQLTSLLV
NGVQLPALGE NKKVIVDFSS PNIAKEMHVG HLRSTIIGES ISRLFEFAGY DVLRLNHIGD
WGTQFGMLIA HLQDKFPDYL TVSPPIGDLQ VFYKESKKRF DTEEEFKKRA YQCVVLLQGK
NPDITKAWKL ICDVSRQELN KIYDALDVSL IERGESFYQD MMNDIVKEFE DRGFVQVDDG
RKIVFVPGCS IPLTILKSDG GYTYDTSDLA AIKQRLFEEK ADMIIYVVDN GQSVHFQTIF
AAAQMIGWYD PKVTRVFHAG FGVVLGEDKK KFKTRSGETV RLMDLLGEGL KRSMDKLKEK
ERDKVLTAEE LNAAQTSIAY GCVKYADLSH NRLNDYIFSF DKMLDDKGNT AAYLLYAFTR
IRSIARLANI DEEMLQKAAR ETKILLDHEK EWKLGRCILR FPEILQKILD DLFLHTLCDY
IYELATTFTE FYDSCYCVEK DRQTGKILKV NMWRMLLCEA VAAVMAKGFD ILGIKPVQRM
