ID   SYR_PROM1               Reviewed;         607 AA.
AC   A2C016;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 82.
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=NATL1_02621;
OS   Prochlorococcus marinus (strain NATL1A).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167555;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NATL1A;
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(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}.
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DR   EMBL; CP000553; ABM74826.1; -; Genomic_DNA.
DR   RefSeq; WP_011823044.1; NC_008819.1.
DR   AlphaFoldDB; A2C016; -.
DR   SMR; A2C016; -.
DR   STRING; 167555.NATL1_02621; -.
DR   EnsemblBacteria; ABM74826; ABM74826; NATL1_02621.
DR   KEGG; pme:NATL1_02621; -.
DR   eggNOG; COG0018; Bacteria.
DR   HOGENOM; CLU_006406_5_1_3; -.
DR   OMA; NKPLHLG; -.
DR   Proteomes; UP000002592; 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   TIGRFAMs; TIGR00456; argS; 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..607
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_1000018087"
FT   MOTIF           147..157
FT                   /note="'HIGH' region"
SQ   SEQUENCE   607 AA;  68529 MW;  2CAF8267062EDB13 CRC64;
     MLEISARLEE ALNRAFTKVF PQEDRSSKTS SILTGSNLVP ASKPEFGDFQ INCALSLAKE
     INRPPRDIAQ QIAKQLQQDN DFVRICNPPL IAGPGFINLS INSKTLISEI HFRLNDKRLG
     VPLKKFNTDK IEEEKSNNRV IIDFSSPNIA KEMHVGHLRS TIIGDSLARV LEFCGYEVLR
     LNHVGDWGTQ FGMLITHLKE VVPEVLHTKD VVEISDLVNF YRQAKKRFDE DQIFQNKSRS
     EVVNLQAGDK ESLIAWQLLC NQSRKEFQKI YDRLDIKLTE RGESFYNKFL VDVINDLKNK
     KLLINDQGAQ CIFLDGLVGK DGKPQPIIIQ KSDGGFNYAT TDLAAIKYRL TIPPHGDGAC
     RLIYVTDAGQ ASHFSGVFQI AKLANWIPTD CQIEHVPFGL VQGEDGKKLK TRSGETIRLV
     DLLDEAIQRA RDDLKNRLNT ESRSENENFI DKVSTTVGIA SIKYADLSQN RISNYQFSFD
     KMLSLQGNTA PYLLYALVRI AGISRKGGDL NVSSQNIQFN ESQEWDLIRK LLQLDSIIAE
     VEKELLPNRL CGYLFELSQT FNRFYDQVPI LKASEPSRAS RLVLCSITAD TLKLGMSLLG
     IPTLERM