ID   SYR_DESAH               Reviewed;         555 AA.
AC   C0QKZ8;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 74.
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=HRM2_31550;
OS   Desulforapulum autotrophicum (strain ATCC 43914 / DSM 3382 / VKM B-1955 /
OS   HRM2) (Desulfobacterium autotrophicum).
OC   Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC   Desulfobacteraceae; Desulforapulum.
OX   NCBI_TaxID=177437;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43914 / DSM 3382 / VKM B-1955 / HRM2;
RX   PubMed=19187283; DOI=10.1111/j.1462-2920.2008.01825.x;
RA   Strittmatter A.W., Liesegang H., Rabus R., Decker I., Amann J., Andres S.,
RA   Henne A., Fricke W.F., Martinez-Arias R., Bartels D., Goesmann A.,
RA   Krause L., Puehler A., Klenk H.P., Richter M., Schuler M., Gloeckner F.O.,
RA   Meyerdierks A., Gottschalk G., Amann R.;
RT   "Genome sequence of Desulfobacterium autotrophicum HRM2, a marine sulfate
RT   reducer oxidizing organic carbon completely to carbon dioxide.";
RL   Environ. Microbiol. 11:1038-1055(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; CP001087; ACN16238.1; -; Genomic_DNA.
DR   RefSeq; WP_015905000.1; NC_012108.1.
DR   AlphaFoldDB; C0QKZ8; -.
DR   SMR; C0QKZ8; -.
DR   STRING; 177437.HRM2_31550; -.
DR   KEGG; dat:HRM2_31550; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_0_1_7; -.
DR   OrthoDB; 9803211at2; -.
DR   Proteomes; UP000000442; 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; 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..555
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_1000203090"
FT   MOTIF           128..138
FT                   /note="'HIGH' region"
SQ   SEQUENCE   555 AA;  61868 MW;  B951095CC522A032 CRC64;
     MKESIKQLIL GGARRAFDKG LLKSDEFPGM EIEAPRHEAH GDFSTNFAMV SAATQKMAPR
     KIAEAVISCM DSDSVIEKTE IAGPGFINFF LANRAWYPTL DRIVKEDDRF GSSDFGAGKK
     VQVEFVSANP TGPLHVGHAR GAAVGDAVAN ILSFAGFDVQ REYYINDSGR QIRTLGLSVW
     LRLCQQLGRE VEFPTDCYQG DYIKEIAADL HGKMGRELSE KDEAEAVSIC AKFAAQVILS
     GIRADLVAFG VEYDQWFSEE SLYASGRVQK AIEEFKARDV IYEKDGAQWF RTERYGDEKD
     RVVVRNNGIT TYFASDIAYH MEKFDRGFDR VIDVWGADHH GYINRINAAI DASGRQSDQF
     DVILVQLVNL LRNGQPVAMS SRSGEFVTLK DIVDEVGKDA ARFLFLSRSY DSGLDFDLEV
     AKQKTSDNPV YYVQYVHARI AGILMKAVSE KVLNEAEKPG AGNRELLVEP EEINLLKILA
     AFPETVEKSA ATLHPHVIFT YLMGLASAFH GYYNRHKVIT PDRELSRGRI SLVFAVKTVI
     RNGLNLLGVS APERM
//