SYR_THEAC
ID SYR_THEAC Reviewed; 546 AA.
AC Q9HLE7;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 109.
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=Ta0281;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
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 -!- 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; AL445063; CAC11426.1; -; Genomic_DNA.
DR RefSeq; WP_010900710.1; NC_002578.1.
DR AlphaFoldDB; Q9HLE7; -.
DR SMR; Q9HLE7; -.
DR STRING; 273075.Ta0281; -.
DR EnsemblBacteria; CAC11426; CAC11426; CAC11426.
DR GeneID; 1455910; -.
DR KEGG; tac:Ta0281; -.
DR eggNOG; arCOG00487; Archaea.
DR HOGENOM; CLU_006406_6_1_2; -.
DR OMA; NKPLHLG; -.
DR OrthoDB; 7046at2157; -.
DR Proteomes; UP000001024; 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; 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; PF05746; DALR_1; 1.
DR Pfam; PF00750; tRNA-synt_1d; 1.
DR PRINTS; PR01038; TRNASYNTHARG.
DR SMART; SM00836; DALR_1; 1.
DR SUPFAM; SSF47323; SSF47323; 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..546
FT /note="Arginine--tRNA ligase"
FT /id="PRO_0000151658"
FT MOTIF 117..127
FT /note="'HIGH' region"
SQ SEQUENCE 546 AA; 63004 MW; EB72B6D59406E078 CRC64;
MLLFQDLRKD IYEIVSKRFR ISENDVYLDD TGHSDITIRV FRILKSPDGG ENAVMEIVRS
ISEKDYVEKA LSEGGYINVW IKRTYMLREV LESIEKSGTY PDVFQEAERV SVEHTSANPT
GPLHIGRARN SIIGDSIYRI LSRYGYRTVR QYFVNDSGKQ MISLYTAYIK YGGPITIENL
LENYQKIYRE MEKDQSIEKE IEKNIERYEN ADPEVFGTLR KIAGVMLDGI ASTLKRIGIE
FDEFDWESDL LLNGSVRKAI DMLETKEEDS ARYIEISGKK VFLTRKDGTT LYFARDIAYH
LFKAENSEWI IDVLGEDHKD HAKSLNHVLK EMLKLENRVS FMYYSFITLE TGKMSTRRGN
IVTLQDLVDR TYDEALKIVN EKRPDLSEEE RKKIAEVIAS SAVRYSIIRV SAPKPITFRW
EEALNFESNS APFIMYSHAR AASILDKAPE PEQSYGMDMP KEEADLVKAM YVYPYYLKDA
AQDLKPDLIA AYLISLVQKF NDFYGACRVI GTDPLTYARR IRIVKAYKQI LSDAGDLIGI
KMLDQM