SYR_TROWT
ID SYR_TROWT Reviewed; 552 AA.
AC Q83GE9;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 110.
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=TWT_351;
OS Tropheryma whipplei (strain Twist) (Whipple's bacillus).
OC Bacteria; Actinobacteria; Micrococcales; Tropherymataceae; Tropheryma.
OX NCBI_TaxID=203267;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Twist;
RX PubMed=12902375; DOI=10.1101/gr.1474603;
RA Raoult D., Ogata H., Audic S., Robert C., Suhre K., Drancourt M.,
RA Claverie J.-M.;
RT "Tropheryma whipplei twist: a human pathogenic Actinobacteria with a
RT reduced genome.";
RL Genome Res. 13:1800-1809(2003).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE014184; AAO44448.1; -; Genomic_DNA.
DR RefSeq; WP_011102520.1; NC_004572.3.
DR AlphaFoldDB; Q83GE9; -.
DR SMR; Q83GE9; -.
DR STRING; 203267.TWT_351; -.
DR PRIDE; Q83GE9; -.
DR EnsemblBacteria; AAO44448; AAO44448; TWT_351.
DR KEGG; twh:TWT_351; -.
DR eggNOG; COG0018; Bacteria.
DR HOGENOM; CLU_006406_0_1_11; -.
DR OMA; NKPLHLG; -.
DR OrthoDB; 1146366at2; -.
DR Proteomes; UP000002200; 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; 2.
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.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..552
FT /note="Arginine--tRNA ligase"
FT /id="PRO_0000242118"
FT MOTIF 124..134
FT /note="'HIGH' region"
SQ SEQUENCE 552 AA; 62999 MW; A74E3374662C9704 CRC64;
MNVEDLKKSV TNIVHSMYNF DCSEIVSLTR PPKPEYGDWA LSLPLKLASL LKSPAIDIAQ
SIASALLELD GVQDVYVAKP GFINLKLSRE HTTGIISEVL EQGSSFGRNT TQSSKKINLE
FVSGNPTGPL HLAHTRWAAV GDSIARILIN CGADVTREYY INNVGNQIHL FSESVYARAL
SKSLPKDGYP GEYVKDIARR IQCEFPNIID LSYEDAIKIF RKRSWQIQIE EIKKSCIAFR
VNFDVWFSEE SLHEPDRFGK SQIDKALARC KQNGYLFQKN GAFFIRTTEF GDDKDRAVLR
SDTSYTYYAA DCAYYLNKIN RGFSDLVILV GADHHGYVKR FQAMSNIFHV DSENNRKNVQ
VLLGQMVLLK NKRQSKREGN VIGLSEIIQS VGVDPLRFWF CRYPIDTPID LDEQHLKKRS
NDNPVYYVQY AYARTRSLIR SANLLQMEKF GFFPELLVHE TETALVSLLY DYKTVVIDAA
RFLQPHRVVR YLESLAGAYH KWYDKCRIIP RKGILDKSEA ELVNTRLELN RAVGQVLYNA
LDLIGVSAPE RM