ID   SYR_STRP2               Reviewed;         563 AA.
AC   Q04I94;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   27-MAR-2024, entry version 95.
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=SPD_1905;
OS   Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=373153;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D39 / NCTC 7466;
RX   PubMed=17041037; DOI=10.1128/jb.01148-06;
RA   Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M.,
RA   Wayne K.J., Tettelin H., Glass J.I., Winkler M.E.;
RT   "Genome sequence of Avery's virulent serotype 2 strain D39 of Streptococcus
RT   pneumoniae and comparison with that of unencapsulated laboratory strain
RT   R6.";
RL   J. Bacteriol. 189:38-51(2007).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000410; ABJ54835.1; -; Genomic_DNA.
DR   RefSeq; WP_001092739.1; NZ_JAMLJR010000012.1.
DR   AlphaFoldDB; Q04I94; -.
DR   SMR; Q04I94; -.
DR   PaxDb; 373153-SPD_1905; -.
DR   KEGG; spd:SPD_1905; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_6_1_9; -.
DR   BioCyc; SPNE373153:G1G6V-2050-MONOMER; -.
DR   Proteomes; UP000001452; 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..563
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_1000018127"
FT   MOTIF           121..131
FT                   /note="'HIGH' region"
SQ   SEQUENCE   563 AA;  63458 MW;  1FBF18752CC04183 CRC64;
     MNTKELIASE LSSIIDSLDQ EAILKLLETP KNSEMGDIAF PAFSLAKVER KAPQMIAAEL
     AEKMNSQAFE KVVATGPYVN FFLDKSAISA QVLQAVTTEK EHYADQNIGK QENVVIDMSS
     PNIAKPFSIG HLRSTVIGDS LSHIFQKIGY QTVKVNHLGD WGKQFGMLIV AYKKWGDEEA
     VKAHPIDELL KLYVRINAEA ENDPSLDEEA REWFRKLENG DEEALALWQW FRDESLVEFN
     RLYNELKVEF DSYNGEAFYN DKMDAVVDIL SEKGLLLESE GAQVVNLEKY GIEHPALIKK
     SDGATLYITR DLAAALYRKN EYQFAKSIYV VGQEQSAHFK QLKAVLQEMG YDWSDDITHV
     PFGLVTKEGK KLSTRKGNVI LLEPTVAEAV SRAKVQIEAK NPELENKDQV AHAVGVGAIK
     FYDLKTDRTN GYDFDLEAMV SFEGETGPYV QYAYARIQSI LRKADFKPET AGNYSLNDTE
     SWEIIKLIQD FPRIINRAAD NFEPSIIAKF AISLAQSFNK YYAHTRILDE SPERDSRLAL
     SYATAVVLKE ALRLLGVEAP EKM
//