ID   SYR_DESVV               Reviewed;         551 AA.
AC   A1VEG5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 81.
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=Dvul_1814;
OS   Desulfovibrio vulgaris subsp. vulgaris (strain DP4).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=391774;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DP4;
RX   PubMed=19737303; DOI=10.1111/j.1462-2920.2009.01946.x;
RA   Walker C.B., Stolyar S., Chivian D., Pinel N., Gabster J.A., Dehal P.S.,
RA   He Z., Yang Z.K., Yen H.C., Zhou J., Wall J.D., Hazen T.C., Arkin A.P.,
RA   Stahl D.A.;
RT   "Contribution of mobile genetic elements to Desulfovibrio vulgaris genome
RT   plasticity.";
RL   Environ. Microbiol. 11:2244-2252(2009).
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; CP000527; ABM28831.1; -; Genomic_DNA.
DR   RefSeq; WP_011792484.1; NC_008751.1.
DR   AlphaFoldDB; A1VEG5; -.
DR   SMR; A1VEG5; -.
DR   PRIDE; A1VEG5; -.
DR   EnsemblBacteria; ABM28831; ABM28831; Dvul_1814.
DR   KEGG; dvl:Dvul_1814; -.
DR   HOGENOM; CLU_006406_0_1_7; -.
DR   OMA; NKPLHLG; -.
DR   Proteomes; UP000009173; 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.
FT   CHAIN           1..551
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_1000018021"
FT   MOTIF           125..135
FT                   /note="'HIGH' region"
SQ   SEQUENCE   551 AA;  60537 MW;  820AB17CA4856C10 CRC64;
     MRAKKQLLAA LQDIVKDMGL AWPEKATIDT PKATGFGDLA ANIALVLAKQ AGQNPRELAT
     RIADALRNRD ADITAIDIAG PGFLNVTYSQ DFWRETILRA QEAGSAFGSS DTGAGRKVQV
     EYVSANPTGP LHIGHGRGAA VGDSLARIMR FAGYDVSTEY YINDAGRQMR LLGLSVWVRA
     KELAGRPVTL PEDFYRGDYI KDIARELMEK EPGLLDLDDA AGEDRCFAYA MNSILDGIKQ
     DLADFRVEHQ VWFSERSLVE GGAVEKTFNR LKEAGLAFEQ DGALWFRTTD FGDDKDRVLR
     KSDGTLTYFS SDIAYHDNKY DRGFDLVVDI WGADHHGYIP RMRAAVAALG RKPEAFDVVL
     IQLVNLLRGG ELVAMSTRAG QFETLADVVK ETGADAARFM FLSRKSDSPL DFDLELVKQR
     TMDNPVYYVQ YAHARVCSVL RKAAERGIEM PAQLDGASLA PLSGDDEMEL LRLLDRFEET
     VAGAATALAP HHISHYLMEV AGALHSYYAR QPILNATEQD VIVPRLALLR AVGCVLANGL
     SLLGVSAPES M