SYR_ACIBC
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 25-MAY-2022, entry version 73.
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=ACICU_00163;
OS Acinetobacter baumannii (strain ACICU).
OC Bacteria; Proteobacteria; 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 OMA; NKPLHLG; -.
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; -; 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; 2.
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.
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