ID   SYR_AMOA5               Reviewed;         596 AA.
AC   B3ERZ8;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   27-MAR-2024, entry version 83.
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=Aasi_0599;
OS   Amoebophilus asiaticus (strain 5a2).
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Amoebophilaceae;
OC   Candidatus Amoebophilus.
OX   NCBI_TaxID=452471;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5a2;
RX   PubMed=20023027; DOI=10.1128/jb.01379-09;
RA   Schmitz-Esser S., Tischler P., Arnold R., Montanaro J., Wagner M.,
RA   Rattei T., Horn M.;
RT   "The genome of the amoeba symbiont 'Candidatus Amoebophilus asiaticus'
RT   reveals common mechanisms for host cell interaction among amoeba-associated
RT   bacteria.";
RL   J. Bacteriol. 192:1045-1057(2010).
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; CP001102; ACE06000.1; -; Genomic_DNA.
DR   RefSeq; WP_012472766.1; NC_010830.1.
DR   AlphaFoldDB; B3ERZ8; -.
DR   SMR; B3ERZ8; -.
DR   STRING; 452471.Aasi_0599; -.
DR   KEGG; aas:Aasi_0599; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_6_1_10; -.
DR   OrthoDB; 9805987at2; -.
DR   Proteomes; UP000001227; 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   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; 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..596
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_1000095332"
FT   MOTIF           123..133
FT                   /note="'HIGH' region"
SQ   SEQUENCE   596 AA;  67709 MW;  B43FCCE03112DB49 CRC64;
     MNIDLVLREA IQNAFQSVFE LSIPLADVNL QPTRKEFEGT HTLIVFPFTT TCKVSPEVIA
     NKIGDWMQTN TQAIASYNVV KGFLNLSIKD TIWLASFNQM YQNKHFGYLP SNRQKIVVEY
     SSPNTNKPLH LGHLRNNFLG HAVSEILQAA GYEVYKVNLV NDRGIHICKS MVAYQHWGRG
     ETPESRGLKG DQLVGKYYVK FDQVYKEQVA ALTQTLGDAE QAAKQAPLLQ EAQVMLKQWE
     AGNEEVLALW RKMNGWVYDG FDITYQKLGI TFDKVYYESQ TYLLGKEVVA EGLAKGTFYK
     KQDGSVWIDL TQEGLDEKLL LRADGTSVYI TQDLGTADLR YQDFKPNKLV YVVGNEQDYH
     FEVLAKIMAR LGRPYATDLY HLSYGMVDLP TGKMKSREGT VVDADMLIDE MIETAEEHTR
     ELGKIDGFSK EEAKDLYHIL AMGALKYFLL RVDAKKRLLF DPQASIDFQG DTGPFIQYTH
     ARIAAVLRKV QQADIAFNDI VEQENFVLHP LEREVIVELA AFPKKLQESA LAYAPAILAQ
     HVLEIAKAYN RMYAELSILH EQDTKVQLFR IQLSVLVAQV IKTVMHLLGI VVPERM
//