ID   SYR_MARSD               Reviewed;         547 AA.
AC   C6BU27;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 76.
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};
GN   OrderedLocusNames=Desal_3690;
OS   Maridesulfovibrio salexigens (strain ATCC 14822 / DSM 2638 / NCIMB 8403 /
OS   VKM B-1763) (Desulfovibrio salexigens).
OC   Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC   Desulfovibrionaceae; Maridesulfovibrio.
OX   NCBI_TaxID=526222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14822 / DSM 2638 / NCIMB 8403 / VKM B-1763;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA   Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I.,
RA   Wall J.D., Arkin A.P., Dehal P., Chivian D., Giles B., Hazen T.C.;
RT   "Complete sequence of Desulfovibrio salexigens DSM 2638.";
RL   Submitted (JUN-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; CP001649; ACS81736.1; -; Genomic_DNA.
DR   RefSeq; WP_015853552.1; NC_012881.1.
DR   AlphaFoldDB; C6BU27; -.
DR   SMR; C6BU27; -.
DR   STRING; 526222.Desal_3690; -.
DR   KEGG; dsa:Desal_3690; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_0_1_7; -.
DR   OrthoDB; 9803211at2; -.
DR   Proteomes; UP000002601; 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; cd07956; Anticodon_Ia_Arg; 1.
DR   CDD; cd00671; ArgRS_core; 1.
DR   Gene3D; 3.30.1360.70; Arginyl tRNA synthetase N-terminal domain; 1.
DR   Gene3D; 3.40.50.620; HUPs; 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   NCBIfam; TIGR00456; argS; 1.
DR   PANTHER; PTHR11956:SF5; ARGININE--TRNA LIGASE, CYTOPLASMIC-RELATED; 1.
DR   PANTHER; PTHR11956; ARGINYL-TRNA SYNTHETASE; 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; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF55190; Arginyl-tRNA synthetase (ArgRS), N-terminal 'additional' domain; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 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..547
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_1000203089"
FT   MOTIF           124..134
FT                   /note="'HIGH' region"
SQ   SEQUENCE   547 AA;  61007 MW;  9F1A9511C3A0603F CRC64;
     MKAKQHLENV LGSILEAKGW EWPEKAVIEP PKDKKFGDMS ANIAMMLSKQ AKMNPRAIAE
     TIQSELDGDK YIEKVDIAGP GFLNFTFSNS FWQDLIPEVL TKGEDYGRSE IGKDTKIQVE
     YVSANPTGPL HIGHGRGAAL GDCLVRILEF TGYDVEAEYY VNDAGRQMLI LGTSIWVRLQ
     QSQGRDIADP EDFYKGEYIK DLAAEVLERN PGILDMSDDE AIAICREYGK DEILEGIKKD
     LAAFDVRHDV WFSEKSLVTA NKVEETFADL KARGMAYEED GALWFKSTEL GDDKDRVLRK
     SNGDLTYFAS DIAYHDDKYK RGFDIVVDIW GADHHGYIPR MQAAVEALGK KGQLDVILVQ
     LVNLLRGGEQ IAMSTRAGKF ETLEDVVNEV GRDASRFMFL SRKSDSHLDF DLELVKQKTM
     DNPVYYVQYA HARICSVMRK AADQGIAVPA IDAAPLSALT NAEELNLMKL MDQFADVAEN
     AGKNMSPHVI SYYLRDLASA LHRFYSMHHI LSADEDVIAA RLVLLQAVAR TLANGLSLLG
     VSAPESM
//