ID   SYR_SHEB8               Reviewed;         581 AA.
AC   A6WIK3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 74.
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=Shew185_0474;
OS   Shewanella baltica (strain OS185).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=402882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS185;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Brettar I., Rodrigues J., Konstantinidis K., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome of Shewanella baltica OS185.";
RL   Submitted (JUL-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; CP000753; ABS06642.1; -; Genomic_DNA.
DR   RefSeq; WP_006083280.1; NC_009665.1.
DR   AlphaFoldDB; A6WIK3; -.
DR   SMR; A6WIK3; -.
DR   GeneID; 11770825; -.
DR   KEGG; sbm:Shew185_0474; -.
DR   HOGENOM; CLU_006406_5_1_6; -.
DR   OMA; NKPLHLG; -.
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..581
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_1000018113"
FT   MOTIF           126..136
FT                   /note="'HIGH' region"
SQ   SEQUENCE   581 AA;  64892 MW;  E2A1FE71AFAC8C31 CRC64;
     MKSHIQSLLE QTLESFKQQG IVPADFEARI QVDRTKDKSH GDLATNLAMM LTKVAGKNPR
     ELAQLIIDTL PASAYVAKVE IAGPGFINFF INDSALADQL QNAVNDEHLG IKLPTPQTVV
     VDYSSPNLAK EMHVGHLRST IIGDSVVRAL EFLGHKVIRQ NHVGDWGTQF GMLLAYMEEL
     RAKNGEKAQL ELSDLENFYR AAKLRFDESA EFATRARQLV VELQSGDEYC NKLWREFNDI
     SLSHCHEVYA RLGVSLTRAD VHGESAYNAD LEQVVKDLDA QGLLTESNGA KVVFQEAFRN
     KEGEPLPVII QKADGGYLYA TSDLAAMRYR SNVLKADRVL YFVDLRQALH FQQVFSLAKL
     AKFVREDMSL EHLGFGTMNG EDGRPFKTRS GGVVKLVDLL EEANVRALEL VRSKNPDMDE
     VTLTEIARVV GISAVKYADL SKNRTSDYIF SFEQMLSFEG NTAPYLLYAY TRVAGIFKRV
     TDLDLSQAKI VLEHEKEKDL GNKLAQFGEI LSRVVDKGQP HVLCAYLYEL AGAFSSFYEA
     CPVLAADNDA QKNSRLLLAQ LTARTLQKGL NLLGIETLER M