SYR_SYMTH
ID SYR_SYMTH Reviewed; 558 AA.
AC Q67TI9;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 107.
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=STH19;
OS Symbiobacterium thermophilum (strain T / IAM 14863).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Symbiobacteriaceae;
OC Symbiobacterium.
OX NCBI_TaxID=292459;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T / IAM 14863;
RX PubMed=15383646; DOI=10.1093/nar/gkh830;
RA Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K.,
RA Ikeda H., Hattori M., Beppu T.;
RT "Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium
RT that depends on microbial commensalism.";
RL Nucleic Acids Res. 32:4937-4944(2004).
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; AP006840; BAD39004.1; -; Genomic_DNA.
DR RefSeq; WP_011194154.1; NC_006177.1.
DR AlphaFoldDB; Q67TI9; -.
DR SMR; Q67TI9; -.
DR STRING; 292459.STH19; -.
DR EnsemblBacteria; BAD39004; BAD39004; STH19.
DR KEGG; sth:STH19; -.
DR eggNOG; COG0018; Bacteria.
DR HOGENOM; CLU_006406_0_1_9; -.
DR OMA; YEFKWER; -.
DR OrthoDB; 1146366at2; -.
DR Proteomes; UP000000417; 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; 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..558
FT /note="Arginine--tRNA ligase"
FT /id="PRO_0000242103"
FT MOTIF 134..144
FT /note="'HIGH' region"
SQ SEQUENCE 558 AA; 63061 MW; BA0FA42459141ED8 CRC64;
MRIVEQIKSE IRQALADAVS RAVAAGALVG PAPEVFLETP KAREHGDFAT NLAMVMARQE
KKAPRVIAQA IVDHLQTEGT WIESAEIAGP GFINLRLRQG WVHQVLPAIQ AEGADYGKSD
HGGKQRILLE YVSANPTGPM VLVQARAGAF GSSLARLLNW AGYECHTEFY VNDAGNQVKI
LARTVDLRAQ ELRGATVEIP EGYYPGEDVI DCARALLEQY PDFLEKPEEE RLAFLERWAP
EYFRSGHERV LRSYGVEFDR WFSERSLREA GAPARLVEWL KERGEAYEKD GAVWMRTTAY
GDDKDRVLVK SDGEYTYFAA DACYHKDKYD RGYATLIDIL GQDHHGYLGR MKAMVECLGH
PRDSLEILFT QMVRLFKDGQ EFRMSKRRGN YVTLEDLLEQ VSVDAARYFF LMRSLDTHMD
FDLDLANLKS SDNPVFYVQY AHARICSILR QAREQGLEVP AASEVDTALL ADESEVELMR
KLAEFPEEII GAADAREVHR IPRYLNELAT LFHQFYSRCR VVSDDVPLSR ARLLLVDCTR
TVLANALGIL GVSAPERM