ID   SYR_NEIG1               Reviewed;         572 AA.
AC   Q5F835;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
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=NGO0963;
OS   Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=242231;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700825 / FA 1090;
RA   Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F.,
RA   Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C.,
RA   Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S.,
RA   Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.;
RT   "The complete genome sequence of Neisseria gonorrhoeae.";
RL   Submitted (MAR-2003) 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; AE004969; AAW89652.1; -; Genomic_DNA.
DR   RefSeq; WP_010951154.1; NC_002946.2.
DR   RefSeq; YP_208064.1; NC_002946.2.
DR   AlphaFoldDB; Q5F835; -.
DR   SMR; Q5F835; -.
DR   STRING; 242231.NGO_0963; -.
DR   PRIDE; Q5F835; -.
DR   DNASU; 3282609; -.
DR   EnsemblBacteria; AAW89652; AAW89652; NGO_0963.
DR   KEGG; ngo:NGO_0963; -.
DR   PATRIC; fig|242231.10.peg.1127; -.
DR   HOGENOM; CLU_006406_5_1_4; -.
DR   OMA; NKPLHLG; -.
DR   Proteomes; UP000000535; 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; Reference proteome.
FT   CHAIN           1..572
FT                   /note="Arginine--tRNA ligase"
FT                   /id="PRO_0000242053"
FT   MOTIF           122..132
FT                   /note="'HIGH' region"
SQ   SEQUENCE   572 AA;  62620 MW;  B69F0239F7253087 CRC64;
     MNLHQTVEHE AAAAFAAAGI AGSPVVLQPT KNAEHGDFQI NGVMGAAKKA KQNPRELAQK
     VADALAGNAV IESAEVAGPG FINLRLRHEF LAQNIHAALN DARFGVAKTA QPQTVVIDYS
     SPNLAKEMHV GHLRSSIIGD SISRVLEFTG NTVIRQNHVG DWGTQFGMLV AYLVEQQKDN
     AAFELADLEQ FYRAAKVRFD EDPAFADTAR EYVVKLQGGD ETVLALWKQF VDISLSHAQA
     VYDTLGLKLR PEDVAGESKY NDDLQPVADD LVQKGLAVED DGAKVVFLDE FKNKEGEPAA
     FIVQKQGGGF LYASTDLACL RYRIGRLKAG RLLYVVDHRQ ALHFEQLFTT SRKAGYLPED
     AKAEFIGFGT MMGKDGKPFK TRSGDTVKLV DLLTEAVERA TALVKEKNPE LGADEAAKIG
     KTVGIGAVKY ADLSKNRTSD YVFDWDAMLS FEGNTAPYLQ YAYTRVQSVF RKAGEWDATA
     PTVLTEPLEK QLAAELLKFE NVLQSVADTA YPHYLAAYLY QAATLFSRFY EACPILKAEG
     ASRNSRLQLA KLTGNTLKQG LDLLGIDVLD VM