ID   SYR_STRM5               Reviewed;         562 AA.
AC   B4STE2;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   04-NOV-2026, entry version 88.
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=Smal_0280;
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Lysobacterales; Lysobacteraceae; Stenotrophomonas;
OC   Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3;
RX   PubMed=19060168; DOI=10.1128/aem.02239-08;
RA   Taghavi S., Garafola C., Monchy S., Newman L., Hoffman A., Weyens N.,
RA   Barac T., Vangronsveld J., van der Lelie D.;
RT   "Genome survey and characterization of endophytic bacteria exhibiting a
RT   beneficial effect on growth and development of poplar trees.";
RL   Appl. Environ. Microbiol. 75:748-757(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=tRNA(Arg) + L-arginine + ATP = L-arginyl-tRNA(Arg) + AMP +
CC         diphosphate; 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; CP001111; ACF49985.1; -; Genomic_DNA.
DR   RefSeq; WP_012509811.1; NC_011071.1.
DR   AlphaFoldDB; B4STE2; -.
DR   SMR; B4STE2; -.
DR   STRING; 391008.Smal_0280; -.
DR   PaxDb; 391008-Smal_0280; -.
DR   KEGG; smt:Smal_0280; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_0_1_6; -.
DR   OMA; AAAYHKW; -.
DR   OrthoDB; 9803211at2; -.
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   FunFam; 1.10.730.10:FF:000008; Arginine--tRNA ligase; 1.
DR   FunFam; 3.30.1360.70:FF:000003; Arginine--tRNA ligase; 1.
DR   FunFam; 3.40.50.620:FF:000062; Arginine--tRNA ligase; 1.
DR   Gene3D; 3.30.1360.70; Arginyl tRNA synthetase N-terminal domain; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 1.10.730.10; Isoleucyl-tRNA Synthetase, Domain 1; 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; 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.
FT   CHAIN           1..562
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_1000095409"
FT   MOTIF           129..139
FT                   /note="'HIGH' region"
SQ   SEQUENCE   562 AA;  61499 MW;  327AB7E3031584FB CRC64;
     MKNLLRALIS QGIEALRANG TLPADSLPPD FVVERPKTRD HGDFATNAAM LLAKAARSNP
     RALAQALVEA LPRSEDVSKV EIAGPGFINF YLAPAAYQRE AASVIKEGHD YGRNLSGNGR
     TVGVEYVSAN PTGPLHVGHG RAAAIGDCVA RVLDANGWNA KREFYYNDAG VQIENLSLSV
     QARVKGIAPD QDGWPEGGYR GEYIADVARA YMAGASVDLE GTLVVGAKDA KDMQAIRRFA
     VAYLRNEQNL DLAAFGVDFD IYFLESSLYA DGKVAEAVAK LQASGHTYEE GGALWLRSTD
     FGDDKDRVMR KSDGTFTYFV PDVAYHLSKW QRGYERAITE LGADHHGSLA RVRAGLQAME
     VGIPQGWPEY VLHQMVTVMR GGEEVKLSKR AGSYFTLRDL IEEAGRDATR WFLIARKPDS
     QLTFDIDLAR QQSNDNPVFY VQYAHARVCS LLRQAQEKGL VYEQGNGLAN LGRLSDDASL
     LLMNEISRYP EVVEAAGVAL EPHLVAQYLR ELAHAFHTWY HGTPVLVDDS ADRNAKLTLA
     CAARQVLANG LELLGVSAPE KM
//