ID   SYR_LEPIN               Reviewed;         586 AA.
AC   Q8F5J3;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 2.
DT   25-MAY-2022, entry version 99.
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=LA_1688;
OS   Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS   56601).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=189518;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=56601;
RX   PubMed=12712204; DOI=10.1038/nature01597;
RA   Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X.,
RA   Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X.,
RA   Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F.,
RA   Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y.,
RA   Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I.,
RA   Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.;
RT   "Unique physiological and pathogenic features of Leptospira interrogans
RT   revealed by whole-genome sequencing.";
RL   Nature 422:888-893(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; AE010300; AAN48887.2; -; Genomic_DNA.
DR   RefSeq; NP_711869.2; NC_004342.2.
DR   RefSeq; WP_000662007.1; NC_004342.2.
DR   AlphaFoldDB; Q8F5J3; -.
DR   SMR; Q8F5J3; -.
DR   STRING; 189518.LA_1688; -.
DR   EnsemblBacteria; AAN48887; AAN48887; LA_1688.
DR   KEGG; lil:LA_1688; -.
DR   PATRIC; fig|189518.3.peg.1681; -.
DR   HOGENOM; CLU_006406_0_1_12; -.
DR   InParanoid; Q8F5J3; -.
DR   Proteomes; UP000001408; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006420; P:arginyl-tRNA aminoacylation; IBA:GO_Central.
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; 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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..586
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000151571"
FT   MOTIF           133..143
FT                   /note="'HIGH' region"
SQ   SEQUENCE   586 AA;  66934 MW;  1E1076F05F07E695 CRC64;
     MKENETLKQI VLKTLEESVN SLISSFPEVE KETFKIKIEY SRDEKFGDYS TSFALENSKL
     LKRNPIQVSK ELVEILQKRT DLFEKVDFTP PGFVNFRIST SFLLNYIETS VLSGNYFPKV
     DLPLKINLEF VSANPTGPLN IVSARAAANG DTMASLLKAI GHNVDKEFYI NDYGNQVFLL
     GVSTLVRIRE LKGEEGTQQE TTDDTPIEII LEKNILPAEG YRGEYIKDIA SSLLKDPKKN
     VTIENLLKQK KYKELAELCA VWTIENNLIW QRKDLDAFGV EFDRYFSERT LHEADKVLSV
     MKDLEKSGKI FQEDGKKVFR STEYGDDKDR VVVRDDGRPT YLLADIAYHK DKIERGYDKI
     YDIWGPDHHG YISRLSGAVQ SLGYKKENFK VIISQQVNLL ESGQKVKMSK RAGSFQTMSD
     LIGFLGKHGK DVGRYFFVMR SLDAPLDFDL DLAKDESDKN PVFYLQYAHA RICSIFKEVG
     DQTSKEATAI LEMSEERKRL LFWIARFPEE IFDSANAMEP HRVTNYLQSF AKAFTSFYLA
     KDNRLKDASK EVRLGLARIC LAAKNVLAEG LKLIGVSAPE RMEKEN