SYR_CALS4
ID SYR_CALS4 Reviewed; 562 AA.
AC Q8R786;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Arginine--tRNA ligase;
DE EC=6.1.1.19;
DE AltName: Full=Arginyl-tRNA synthetase;
DE Short=ArgRS;
GN Name=argS; OrderedLocusNames=TTE2533;
OS Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM
OS 11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Caldanaerobacter.
OX NCBI_TaxID=273068;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4;
RX PubMed=11997336; DOI=10.1101/gr.219302;
RA Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., Chen Y.,
RA Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., Tan H., Chen R.,
RA Wang J., Yu J., Yang H.;
RT "A complete sequence of the T. tengcongensis genome.";
RL Genome Res. 12:689-700(2002).
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;
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; AE008691; AAM25662.1; -; Genomic_DNA.
DR RefSeq; WP_011026543.1; NC_003869.1.
DR AlphaFoldDB; Q8R786; -.
DR SMR; Q8R786; -.
DR STRING; 273068.TTE2533; -.
DR PRIDE; Q8R786; -.
DR EnsemblBacteria; AAM25662; AAM25662; TTE2533.
DR KEGG; tte:TTE2533; -.
DR eggNOG; COG0018; Bacteria.
DR HOGENOM; CLU_006406_0_1_9; -.
DR OMA; YEFKWER; -.
DR OrthoDB; 1146366at2; -.
DR Proteomes; UP000000555; 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; IPR001412; aa-tRNA-synth_I_CS.
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.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..562
FT /note="Arginine--tRNA ligase"
FT /id="PRO_0000151629"
FT MOTIF 136..146
FT /note="'HIGH' region"
SQ SEQUENCE 562 AA; 63693 MW; 5F49126E19BDC08B CRC64;
MENIVQKAKE EIKDVVLKAL NEAKKEGLLN FESIQDVEVE EPKEKQHGDL ATNFAMVMAR
EAKMAPRKIA EIIASKMNTS GTFIEKVEVA GPGFINFFLN QNFLIETLKL IHKRGKDYGR
VNLGKGKKVQ VEFVSANPTG PMHMGNARGG AIGDVLASIL DYAGYNVSRE FYINDAGNQI
EKFGYSLEAR YLQLLGIDAE VPEGGYHGED IIDRAKEFLE IHGDKYKDVP SEERRKALIE
YGLKKNIEKM KEDLVLYGIE YDVWFSEQSL YDSGEVYKVI EELTEKGYTY EKDGALWFKM
TLFGAEKDDV LVRSNGVPTY LASDIAYHKN KFVTRGFDWV INVWGADHHG HVAPMKGAMK
ALGIDPNRLD VVLMQLVKLI EGGQVVRMSK RTGKMITLRD LIEEVGKDAA RFFFNMRSPD
SPIEFDLDLA KQQTNENPVF YVQYAHARIC SIIRQLEEMG VKIENIEDVD LGLLKEEEEV
DLIKKLAYFP EEITIAAKTL APHRITRYVI DVASLFHSFY NSHRVKGAEE NLMKARFALI
LAVKTVLKNA LDILKVTAPE RM