ID   SYR_JANSC               Reviewed;         575 AA.
AC   Q28S88;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   25-MAY-2022, entry version 86.
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=Jann_1507;
OS   Jannaschia sp. (strain CCS1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Jannaschia; unclassified Jannaschia.
OX   NCBI_TaxID=290400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCS1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Chertkov O., Saunders E., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Lykidis A., Moran M.A., Belas R., Ye W.,
RA   Buchan A., Gonzalez J.M., Schell M.A., Richardson P.;
RT   "Complete sequence of chromosome of Jannaschia sp. CCS1.";
RL   Submitted (FEB-2006) 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; CP000264; ABD54424.1; -; Genomic_DNA.
DR   RefSeq; WP_011454631.1; NC_007802.1.
DR   AlphaFoldDB; Q28S88; -.
DR   SMR; Q28S88; -.
DR   STRING; 290400.Jann_1507; -.
DR   EnsemblBacteria; ABD54424; ABD54424; Jann_1507.
DR   KEGG; jan:Jann_1507; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_0_1_5; -.
DR   OMA; NKPLHLG; -.
DR   OrthoDB; 1146366at2; -.
DR   Proteomes; UP000008326; 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; Reference proteome.
FT   CHAIN           1..575
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000242033"
FT   MOTIF           131..141
FT                   /note="'HIGH' region"
SQ   SEQUENCE   575 AA;  62834 MW;  35AD4B1913885F38 CRC64;
     MTLFAEIRDT VLAAIDTLVA DNVLPSGLEM RAVTVEPPRD ASHGDMATNA AMVLAKPAGM
     KPRDIAEALA AKLADDARID TVDVAGPGFL NLRLSGDVWR GVIADALTQG EAYGRSKIGA
     GKRVNVEYVS ANPTGPLHVG HTRGAVFGDA LASLLDVAGY DVTREYYIND GGAQVDVLVR
     SVYLRYLEAH GQDVAFEDGT YPGDYLIDVG QALKDKVGDA FVDKGEQFWL AEIREFATEQ
     MMDLIRKDLA LLGVEMDVFY SEKSLYGTGR IEAAIDDLRG KGLIYEGYLE PPKGKTPEDW
     EPREQTLFKS TEHGDDVDRP VMKSDGSWTY FAPDIAYHFD KVSRGFDELI DVFGADHGGY
     VKRMKAAVSA LSGGDVPLDV KLTQLVKLRR GDEELKMSKR AGTFVTLADV VEMVGADVTR
     FHMLTRKNDA PLDFDVDKVR EQSKDNPVWY VQYAHARIKS VLRKAEEAGM SPDPANLNAV
     NDPAELALAA KIAEYPRLIE IAAKGNEPHR VAFYLFDLAS DFHGLWNKGN AETHLRFFQD
     DDPSATSGKL CLISAVAIVI SNGLGILGVT PVDQM