ID   SYR_PSEA7               Reviewed;         587 AA.
AC   A6VDH2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 79.
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=PSPA7_5788;
OS   Pseudomonas aeruginosa (strain PA7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=381754;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PA7;
RA   Dodson R.J., Harkins D., Paulsen I.T.;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000744; ABR86159.1; -; Genomic_DNA.
DR   RefSeq; WP_003156914.1; NC_009656.1.
DR   AlphaFoldDB; A6VDH2; -.
DR   SMR; A6VDH2; -.
DR   EnsemblBacteria; ABR86159; ABR86159; PSPA7_5788.
DR   KEGG; pap:PSPA7_5788; -.
DR   HOGENOM; CLU_006406_5_1_6; -.
DR   OMA; NKPLHLG; -.
DR   OrthoDB; 1146366at2; -.
DR   Proteomes; UP000001582; 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   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   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..587
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_1000018090"
FT   MOTIF           127..137
FT                   /note="'HIGH' region"
SQ   SEQUENCE   587 AA;  65353 MW;  A845D5C81688EA97 CRC64;
     MKDTIRQLIQ QALDQLTADG TLPAGLTPDI QVENTKDRSH GDFASNIAMM LAKPAGMKPR
     DLATRLVEAL PAHEQLAKVE IAGPGFLNFF QDHIWLAASL DRALADERLG VRKAGPAQRV
     VIDLSSPNLA KEMHVGHLRS TIIGDAVARV LEFLGDTVIR QNHVGDWGTQ FGMLLAYLEE
     QPVDAQAELH DLEVFYRAAK KRFDESPEFA DRARELVVRL QAGDPDCLRL WTRFNEISLS
     HCQKVYDRLG VKLSMADVKG ESAYNDDLAQ VVADLTAKGL LTEDNGALCV FLEEFRNAEG
     NPLPVIVQKA GGGYLYATTD LAAMRYRHNV LHADRALYFV DQRQALHFQQ VFEVARRAGF
     VPADMELEHM GFGTMNGADG RPFKTRDGGT VKLIDLLEEA ESRAYALVKE RNEQRVERGE
     EPFDEAQLRE IGRVVGIDSV KYADLSKHRT SDYSFNFELM LSFEGNTAPY LLYACTRVAS
     VFRKLGQGRE QLGGRIVLEQ PQELALAAQL AQFGDLLNNV ALKGVPHLLC AYLYELAGLF
     SSFYEHCPIL TAEDPAQKDS RLRLAALTGR TLEQGLELLG LKTLERM