ID SYR_PARD8 Reviewed; 597 AA.
AC A6LHY5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=Arginine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00123};
DE EC=6.1.1.19 {ECO:0000255|HAMAP-Rule:MF_00123};
DE AltName: Full=Arginyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00123};
DE Short=ArgRS {ECO:0000255|HAMAP-Rule:MF_00123};
GN Name=argS {ECO:0000255|HAMAP-Rule:MF_00123}; OrderedLocusNames=BDI_3601;
OS Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM
OS 5825 / NCTC 11152).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC Parabacteroides.
OX NCBI_TaxID=435591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152;
RX PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA Knight R.D., Gordon J.I.;
RT "Evolution of symbiotic bacteria in the distal human intestine.";
RL PLoS Biol. 5:1574-1586(2007).
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:0000255|HAMAP-Rule:MF_00123};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00123}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00123}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00123}.
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DR EMBL; CP000140; ABR45299.1; -; Genomic_DNA.
DR RefSeq; WP_012056086.1; NC_009615.1.
DR AlphaFoldDB; A6LHY5; -.
DR SMR; A6LHY5; -.
DR STRING; 435591.BDI_3601; -.
DR PaxDb; 435591-BDI_3601; -.
DR KEGG; pdi:BDI_3601; -.
DR PATRIC; fig|435591.13.peg.3564; -.
DR eggNOG; COG0018; Bacteria.
DR HOGENOM; CLU_006406_6_1_10; -.
DR BioCyc; PDIS435591:G1G5A-3693-MONOMER; -.
DR Proteomes; UP000000566; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
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; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..597
FT /note="Arginine--tRNA ligase"
FT /id="PRO_1000018082"
FT MOTIF 125..135
FT /note="'HIGH' region"
SQ SEQUENCE 597 AA; 67557 MW; 0319967D867C68B7 CRC64;
MVIEQQITGA IIAGIKELYG ADVTASQVQL QKTKKEFKGH LTLVVFPFLR MSKKSPEQTA
QEIGEYLLRN EPAVAEFNVI KGFLNLTVAC SCWIDLLNSI NEQPAYGIIP VTEQSPLVMI
EYSSPNTNKP LHLGHVRNNL LGYSLSKIIK ANGNQIVKTN IVNDRGIHIC KSMLAWQKWG
NGATPESTGK KGDHLIGDFY VLFSNKLKEE THALEAKGLT KEEAEAQSTL MAEAREMLRK
WEAGDKEVRA LWEMMNNWVY AGFNETYKMM GVDFDKIYYE SQTYLEGKGK VMEGLEKGIF
YRREDGSVWA DLTKDGLDEK LLLRADGTSV YMTQDIGTAK LRFDDYPINK MIYVVGNEQN
YHFQVLSILL DKLGFEFGKG LVHFSYGMVE LPEGKMKSRE GTVVDADDLM AEMISTAREI
SQELGKLDEM TPEEAENIAR IVGLGSLKYF ILKVDPRKNM TFNPKESIDF NGNTGPFIQY
TYARIRSVLR KAAEQGIVLP EQLPLTFAIS EKEENLIQMI ADYAEIVKEA GKLYSPACVA
NYIYDLVKEY NQFYHDFSIL REENPELKNF RLVLSANVAK IVKSGMDLLG IEVPERM
//
