ID   SYR_KLEP7               Reviewed;         577 AA.
AC   A6TB43;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 87.
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=KPN78578_23530; ORFNames=KPN_02388;
OS   Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=272620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700721 / MGH 78578;
RG   The Klebsiella pneumonia Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA   Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL   Submitted (SEP-2006) 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; CP000647; ABR77814.1; -; Genomic_DNA.
DR   RefSeq; WP_004151452.1; NC_009648.1.
DR   PDB; 3GDZ; X-ray; 2.20 A; A/B/C/D=1-106.
DR   PDBsum; 3GDZ; -.
DR   AlphaFoldDB; A6TB43; -.
DR   SMR; A6TB43; -.
DR   STRING; 272620.KPN_02388; -.
DR   jPOST; A6TB43; -.
DR   PaxDb; 272620-KPN_02388; -.
DR   DNASU; 5342538; -.
DR   EnsemblBacteria; ABR77814; ABR77814; KPN_02388.
DR   KEGG; kpn:KPN_02388; -.
DR   HOGENOM; CLU_006406_5_1_6; -.
DR   EvolutionaryTrace; A6TB43; -.
DR   Proteomes; UP000000265; 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   1: Evidence at protein level;
KW   3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..577
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_1000018046"
FT   MOTIF           122..132
FT                   /note="'HIGH' region"
FT   HELIX           3..17
FT                   /evidence="ECO:0007829|PDB:3GDZ"
FT   STRAND          28..30
FT                   /evidence="ECO:0007829|PDB:3GDZ"
FT   HELIX           34..36
FT                   /evidence="ECO:0007829|PDB:3GDZ"
FT   STRAND          38..41
FT                   /evidence="ECO:0007829|PDB:3GDZ"
FT   HELIX           44..50
FT                   /evidence="ECO:0007829|PDB:3GDZ"
FT   HELIX           55..65
FT                   /evidence="ECO:0007829|PDB:3GDZ"
FT   TURN            69..71
FT                   /evidence="ECO:0007829|PDB:3GDZ"
FT   STRAND          72..78
FT                   /evidence="ECO:0007829|PDB:3GDZ"
FT   TURN            79..81
FT                   /evidence="ECO:0007829|PDB:3GDZ"
FT   STRAND          82..87
FT                   /evidence="ECO:0007829|PDB:3GDZ"
FT   HELIX           89..100
FT                   /evidence="ECO:0007829|PDB:3GDZ"
SQ   SEQUENCE   577 AA;  64242 MW;  93D42215E0585926 CRC64;
     MNIQALLSEK VSQALIAAGA PADCEPQVRQ SAKVQFGDYQ ANGVMAVAKK LGMAPRQLAE
     QVLSHLDLNG IANKVEIAGP GFINIFLDPA FLADNVNRAL QSERLGVTKP QAQTIVVDYS
     APNVAKEMHV GHLRSTIIGD ASVRTLEFLG HKVIRANHVG DWGTQFGMLI AYLEKQQQEN
     AGEMALADLE GFYREAKKHY DEDEAFAERA RSYVVKLQGG DEYFLQMWRK LVDITMSQNQ
     ITYDRLNVTL TRDDVMGESL YNPMLPGIVA DLKAKGLAVE SEGATVVFLD EYKNKEGEPM
     GVIIQKKDGG YLYTTTDIAC AKYRYETLHA DRVLYYIDSR QHQHLMQAWT IVRKAGYVPD
     SVPLEHHMFG MMLGKDGKPF KTRAGGTVKL ADLLDEALER ARRLVAEKNP DMSADELENL
     AKVVGIGAVK YADLSKNRTT DYVFDWDNML AFEGNTAPYM QYAYTRVLSV FRKAGIDENA
     MIDAPVVIAE DREAQLAARL LQFEETLSVV AREGTPHVMC AYLYDLAGLF SGFYEHCPIL
     SAESEETRNS RLKLALLTAK TLKLGLDTLG IETVERM
//