ID   SYR_PSESM               Reviewed;         578 AA.
AC   Q87V03;
DT   31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 114.
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};
GN   OrderedLocusNames=PSPTO_5138;
OS   Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=223283;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-871 / DC3000;
RX   PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA   Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA   Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA   Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA   Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA   Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA   Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA   Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA   Collmer A.;
RT   "The complete genome sequence of the Arabidopsis and tomato pathogen
RT   Pseudomonas syringae pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
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; AE016853; AAO58565.1; -; Genomic_DNA.
DR   RefSeq; NP_794870.1; NC_004578.1.
DR   RefSeq; WP_011105333.1; NC_004578.1.
DR   AlphaFoldDB; Q87V03; -.
DR   SMR; Q87V03; -.
DR   STRING; 223283.PSPTO_5138; -.
DR   GeneID; 1186823; -.
DR   KEGG; pst:PSPTO_5138; -.
DR   PATRIC; fig|223283.9.peg.5258; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_5_1_6; -.
DR   OrthoDB; 9803211at2; -.
DR   PhylomeDB; Q87V03; -.
DR   Proteomes; UP000002515; 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; cd07956; Anticodon_Ia_Arg; 1.
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; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..578
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000151594"
FT   MOTIF           127..137
FT                   /note="'HIGH' region"
SQ   SEQUENCE   578 AA;  63640 MW;  7DA9D2D7377CDB07 CRC64;
     MKDTIRQLIQ QALTRLVTEG VLPEGLTPAI QVENARDKTH GDFASNIAMM LAKPAGMKPR
     DLAEKLIAAL PADEQVSKVE IAGPGFLNFF QNTAALASRL DAALSDPQLS VRKAGAAQRV
     VVDLSAPNLA KEMHVGHLRS TIIGDGVANV LEFLGDTVIR QNHVGDWGTQ FGMLLAYLQE
     KPATSDELSD LENFYRAAKQ RFDESEEFAE RARGLVVKLQ AGDAECLTLW TRFKDISLSH
     CQQTYERLNV KLTPADVMGE SAYNDDLANV VNDLKAAGLL VESNGAQCVF LEEFRTADDT
     PLPVIVQKAG GGYLYATTDL AAIRYRSKVL KADRALYFVD QRQALHFQQV FEVARRAGFV
     HEGMQLEHMG FGTMNGADGR PFKTRDGGTV KLIDLLDEAQ ERAYTLVKEK NPQVAEAELR
     SIAKAVGISA VKYADLSKHR ASDYSFNFDQ MLSFEGNTAP YLLYAYTRVA GVFRKLGTPF
     DASKGHIVLE APQEQELAAR LAQFNETLNN VAEKGTPHVL CAYLYDLAGL FSSFYENCPI
     LGAENPDQQQ SRLRLAALTG RTLKQGLDLL GLETLERM
//