ID   SYR_ANAD2               Reviewed;         598 AA.
AC   B8JBE2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 69.
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=A2cp1_2431;
OS   Anaeromyxobacter dehalogenans (strain 2CP-1 / ATCC BAA-258).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=455488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-1 / ATCC BAA-258;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA   Beliaev A.S., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-1.";
RL   Submitted (JAN-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; CP001359; ACL65769.1; -; Genomic_DNA.
DR   RefSeq; WP_012633571.1; NC_011891.1.
DR   AlphaFoldDB; B8JBE2; -.
DR   SMR; B8JBE2; -.
DR   EnsemblBacteria; ACL65769; ACL65769; A2cp1_2431.
DR   KEGG; acp:A2cp1_2431; -.
DR   HOGENOM; CLU_006406_0_1_7; -.
DR   OMA; NKPLHLG; -.
DR   Proteomes; UP000007089; 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   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..598
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_1000198870"
FT   REGION          288..309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           131..141
FT                   /note="'HIGH' region"
SQ   SEQUENCE   598 AA;  65535 MW;  AAD9357D559C58B1 CRC64;
     MVRDRVIELF RKALAQGADD GRWPAAGAGF SVEAPRDPKH GDFAVNAAMV LAKQAGRPPR
     ELAQAIVEAV RAADTAGDLA GLEIAGPGFI NVRLSPDLWL RTLARAVAEG PDYGRTAVGQ
     GKKVIVEYVS ANPTGPMHVG HGRNAVVGDG VQGLLRWAGF DVTREYYVND YGAQVQTLAR
     SVHLRYQELH GRTVTMPPKS YPGEYVKDIA AGLKAEYGAR FLDAPEAEWL TLFRDHSVQH
     VLGMIRGDLA AVNISFDRWS SEKALYESGT VDRFLRFLEE KDLVYVGKLP PPKSKKGQPP
     PQPQPDEEGV TAAEDLTLFR SSAYGDEVDR PVKKADGTPT YFCADIAYHW DKRQRADALV
     DVLGADHGGY VPRLEAAMEA LGASRKDLHV VLIQMVSLMR GGESVKMSKR AGTLVSLREV
     VDEVGRDATR FIFLTRRSDA PLDFDVELAK RQTLDNPVFY VQYGHARLAA IFQKAREAGH
     AVPDFDLEAA RTLASPEEQD LIRRIAAFPD MLAAAALAYE PHRVAFYLQE TIAAFHSWYT
     QGKKSGEKVI GPDPVKTAAR LFLCRALKQV LANGLAVLGV SAPDRMESPE TRDIADDV