SYRC_XENTR
ID SYRC_XENTR Reviewed; 660 AA.
AC Q6P1S4;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
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 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-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. {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; BC064888; AAH64888.1; -; mRNA.
DR RefSeq; NP_989403.1; NM_204072.1.
DR AlphaFoldDB; Q6P1S4; -.
DR SMR; Q6P1S4; -.
DR STRING; 8364.ENSXETP00000029726; -.
DR PaxDb; Q6P1S4; -.
DR PRIDE; Q6P1S4; -.
DR Ensembl; ENSXETT00000054391; ENSXETP00000054391; ENSXETG00000025551.
DR GeneID; 395040; -.
DR KEGG; xtr:395040; -.
DR CTD; 5917; -.
DR Xenbase; XB-GENE-955966; rars1.
DR eggNOG; KOG4426; Eukaryota.
DR HOGENOM; CLU_006406_5_1_1; -.
DR InParanoid; Q6P1S4; -.
DR OMA; KSAHIGH; -.
DR OrthoDB; 463402at2759; -.
DR PhylomeDB; Q6P1S4; -.
DR TreeFam; TF106111; -.
DR Proteomes; UP000008143; Chromosome 3.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000025551; Expressed in testis and 16 other tissues.
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..660
FT /note="Arginine--tRNA ligase, cytoplasmic"
FT /id="PRO_0000250730"
FT REGION 1..72
FT /note="Could be involved in the assembly of the
FT multisynthetase complex"
FT /evidence="ECO:0000250"
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"
SQ SEQUENCE 660 AA; 75258 MW; 062F300B7910F0B2 CRC64;
MELPVCFYEE RLRQQETEIK SLAAEIERLK NCGFVSETPS LEGLREENAK LKYRLNILRK
SLLEEKKKSS KSMININAQI QEIFGTAIGA AYPELQNAPL AVTPSQQPKF GDYQCNSAMA
ITQMLKAMNQ KVSPREIADK IVKNIPTNEL VEKVDIAGPG FINVHLHKDF TSKQISKLLV
NGVQPPVIWE RKKVVVDFSS PNIAKEMHVG HLRSTVIGDS ICRLFEFVGH DVLRLNHLGD
WGTQFGMLIA HLQDKFPDYL TVSPPIGDLQ SFYKESKKRF DEDEEFKKRA YQCVVQLQNK
TPNFIQAWNL ICDVSRKEFQ KIYDCLDISI IDRGESFYQD RMIGVVKEFE EKGLVQVDEG
RKVVFPPGCS VPLTIVKSDG GFTYDTSDLA ALKQRLQEEK ADMIIYVIDS GQAIHMQNVF
SAGRMIGWYD PKVTRIEHAG FGVVLGEDKK KFKTRSGDTV RLIDLLDEGL KRSMEKLKDK
GRDKVLTAEE LLAAQTSVAF GCIKYADLSH NRMNDYIFSF DKMLDDRGNT AAYLLYAYTR
IRSIARLANI SDEDLHKAAK ETEIILEHEK EWKLSKCILR FPEILQKILD DLLLHTLCDY
LYELATTFTE FYDNCYCVEK DRQTGQIVKV NMSRLLLCDA TAAVMAKGFD ILGIKPVQKM
