ID   SYR2_HALH5              Reviewed;         561 AA.
AC   Q9KEL8;
DT   14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 123.
DE   RecName: Full=Arginine--tRNA ligase 2;
DE            EC=6.1.1.19;
DE   AltName: Full=Arginyl-tRNA synthetase 2;
DE            Short=ArgRS 2;
GN   Name=argS2; OrderedLocusNames=BH0834;
OS   Halalkalibacterium halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS   / JCM 9153 / C-125) (Bacillus halodurans).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC   Halalkalibacterium (ex Joshi et al. 2022).
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA   Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT   and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
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;
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; BA000004; BAB04553.1; -; Genomic_DNA.
DR   PIR; B83754; B83754.
DR   RefSeq; WP_010897007.1; NC_002570.2.
DR   AlphaFoldDB; Q9KEL8; -.
DR   SMR; Q9KEL8; -.
DR   STRING; 272558.gene:10726708; -.
DR   KEGG; bha:BH0834; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_6_1_9; -.
DR   OrthoDB; 9805987at2; -.
DR   Proteomes; UP000001258; 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; 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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..561
FT                   /note="Arginine--tRNA ligase 2"
FT                   /id="PRO_0000151529"
FT   MOTIF           117..127
FT                   /note="'HIGH' region"
SQ   SEQUENCE   561 AA;  64133 MW;  C9C544BF1DE1A1FF CRC64;
     MLAQMISEEL ARILSLKEDE VERLLEIPPQ ETLGDLAFPC FTLAKTKRKA PPFIAAELEA
     AFLEHKEVTA KATGGYVNFF FHRETVAGQL FQEMKSNQYW QPNSGDGKRV VIDMSSPNIA
     KPFGIGHLRS TIIGHALYHL LKKTGYDPIR VNHLGDWGTQ FGKQIAAYQR WGGDVDLKQN
     PIASFLELYV RFHEEAEKDE SLEDEGREWF KKLEEGDEEA DRLWTYFVKE SLNEFDRMYN
     RLGVEFDYVL GESFYNDQMA PVVKELQEKG LLTCSEGALV VPLEDADLPP CLIVKSDGTS
     IYATRDLATA IYRHHVQKGE KLLYVVGGEQ TLHFKQVFHV LKKMGYKWAD QCEHITFGLL
     RLDGKKMSTR RGRVVMLEDV LNDVVAHAKA KIKEKHPNHP HLHEVAEAVG VGAVIFGDLK
     QDRRLDVNFR LEDALSFEGE TGPYVQYTYA RIQSILRKGD KLNDSRHMDW QHVTKDEGWS
     LLKVLIQYPN VLIKATEARE PHQLARYVLT VSKKFNQFYH KYVILADDET VRQARLILAE
     RTGEVIADAM AVLGVKTPEE L
//