SYR_VIBA3
ID SYR_VIBA3 Reviewed; 577 AA.
AC B7VI24;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 25-MAY-2022, entry version 68.
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=VS_2230;
OS Vibrio atlanticus (strain LGP32) (Vibrio splendidus (strain Mel32)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=575788;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LGP32;
RA Mazel D., Le Roux F.;
RT "Vibrio splendidus str. LGP32 complete genome.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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; FM954972; CAV19394.1; -; Genomic_DNA.
DR RefSeq; WP_009847308.1; NC_011753.2.
DR AlphaFoldDB; B7VI24; -.
DR SMR; B7VI24; -.
DR STRING; 575788.VS_2230; -.
DR EnsemblBacteria; CAV19394; CAV19394; VS_2230.
DR KEGG; vsp:VS_2230; -.
DR eggNOG; COG0018; Bacteria.
DR HOGENOM; CLU_006406_5_1_6; -.
DR OMA; NKPLHLG; -.
DR OrthoDB; 1146366at2; -.
DR Proteomes; UP000009100; Chromosome 1.
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..577
FT /note="Arginine--tRNA ligase"
FT /id="PRO_1000198941"
FT MOTIF 122..132
FT /note="'HIGH' region"
SQ SEQUENCE 577 AA; 63843 MW; B9DF4171A2F01BAB CRC64;
MNIQALINDK VSQALEAAGA PAGSPAAVRQ SAKPQFGDYQ ANGIMGVAKR LGTNPREFAQ
KVLDVLNLDG IASKVEIAGP GFLNIFLDET FLAQQADAAL ADSRLGVSAA EAQTIVADYS
APNVAKEMHV GHLRSTIIGD AVVRTLEFLG HKVIRANHIG DWGTQFGMLI ANLERIQAET
GEVSMELSDL EQFYRESKKL YDEDEEFAVK ARGYVVKLQG GDAYCAEMWK KLVDVTMVQN
QRNYDRLNVS LTRDDVMGES MYNHMLSNIV SDLQTQGLAK ESDGAQVVFL DEYKNKDGDP
MGVIVQKRDG GFLYTTTDIA CAKYRFEELG ADRVLYFIDS RQHQHLMQAW TIVRKAGYVP
ESVSLEHHAF GMMLGKDGKP FKTRAGGTVR LADLLDEAEV RATQLIESKN PELAEDEKKT
IANTVAMAAV KYADLSKHRT TDYVFDWENM LAFEGNTAPY MQYAYTRVAS IFAKAGISMD
SLEGEIKITE EKEKALIAKL LQFEEAVQSV AREGQPHIMC SYLFELAGQF SSFYEACPIL
VAEDETVKQS RLKLAALTAK TIKQGLSLLG IETLERM