ID   SYR_ACIBC               Reviewed;         596 AA.
AC   B2I0Y7;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 79.
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=ACICU_00163;
OS   Acinetobacter baumannii (strain ACICU).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=405416;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACICU;
RX   PubMed=18411315; DOI=10.1128/aac.01643-07;
RA   Iacono M., Villa L., Fortini D., Bordoni R., Imperi F., Bonnal R.J.,
RA   Sicheritz-Ponten T., De Bellis G., Visca P., Cassone A., Carattoli A.;
RT   "Whole-genome pyrosequencing of an epidemic multidrug-resistant
RT   Acinetobacter baumannii strain belonging to the European clone II group.";
RL   Antimicrob. Agents Chemother. 52:2616-2625(2008).
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; CP000863; ACC55475.1; -; Genomic_DNA.
DR   RefSeq; WP_001090284.1; NZ_CP031380.1.
DR   AlphaFoldDB; B2I0Y7; -.
DR   SMR; B2I0Y7; -.
DR   GeneID; 66398861; -.
DR   KEGG; abc:ACICU_00163; -.
DR   HOGENOM; CLU_006406_0_1_6; -.
DR   Proteomes; UP000008839; 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; 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; 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; PF03485; Arg_tRNA_synt_N; 1.
DR   Pfam; PF05746; DALR_1; 1.
DR   Pfam; PF00750; tRNA-synt_1d; 2.
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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..596
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_1000095326"
FT   MOTIF           128..138
FT                   /note="'HIGH' region"
SQ   SEQUENCE   596 AA;  66306 MW;  CE748F8F74F0A64C CRC64;
     MNTAIQAALD HAVQTLQQEG VLPSDWNNSS NLTRTKDRSH GDFASNIAMI GSKAAGMKPR
     DLAEKILAAL PEVADISKAE IAGPGFINFF LNADQRFAIL DQIQAQKESF GRSQSNAAKK
     IQVEFVSANP TSSLHVGHGR GAAYGMTVAN LLEATGAKVD REYYVNDAGR QMDILATSTY
     LRYLELLGQN LVFPKNAYQG DYVKEIAQGI IDKDGDAYVR EVANVYKDVP EDVQYAEELD
     SEGNKVVLSG DKEKHIDGLI ANSQQLLGEG YRVFHQAALH AILDDIKDDL ADFGVTFNQW
     FSEASLSAKI DEALETLDQR GFLYEKDGNI WFKSTEFGDE KDRVVKRRNG QTTYFASDIA
     YHLNKLQRGY TDLVDIWGSD HHGYISRVKA AIDAMGYDSK KLTVLLVQFV SLWRGGEMVQ
     MSSRSGQFVT LRDLRKEVGN DAARFYYVMR KSEQHIDFDL DLAVSQSKDN AVYYIQYAHA
     RICRMLEKAA STGLQFEVSA ARSHAARLSL DAETEILAKL AAYPDVVLRA ANAYEPHQVG
     NYLKELAALF HGWYNEHKVL SDDAELTQAR LLLSINVQQV LRNGLELLGV SAPEAM
//