SYR_ACIBS
ID SYR_ACIBS Reviewed; 596 AA.
AC B0VNJ1;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, 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}; OrderedLocusNames=ABSDF0155;
OS Acinetobacter baumannii (strain SDF).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=509170;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SDF;
RX PubMed=18350144; DOI=10.1371/journal.pone.0001805;
RA Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E.,
RA Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J.,
RA Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C.,
RA Weissenbach J., Cruveiller S.;
RT "Comparative analysis of Acinetobacters: three genomes for three
RT lifestyles.";
RL PLoS ONE 3:E1805-E1805(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; CU468230; CAO99561.1; -; Genomic_DNA.
DR AlphaFoldDB; B0VNJ1; -.
DR SMR; B0VNJ1; -.
DR EnsemblBacteria; CAO99561; CAO99561; ABSDF0155.
DR KEGG; abm:ABSDF0155; -.
DR HOGENOM; CLU_006406_0_1_6; -.
DR OMA; NKPLHLG; -.
DR Proteomes; UP000001741; 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_1000095327"
FT MOTIF 128..138
FT /note="'HIGH' region"
SQ SEQUENCE 596 AA; 66334 MW; E9830F08837021BD CRC64;
MNTAIQAALD HAVQTLQQEG VLPSDWNNSS NLTRTKDRSH GDFASNIAMI GSKAAGMKPR
DLAEKILAAL PEVADISKAE IAGPGFINFF LNADQRFAIL DQIQAQKESF GRSQSNVAKK
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