ID   SYR_NEIMB               Reviewed;         572 AA.
AC   Q9JYM8;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 124.
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=NMB1506;
OS   Neisseria meningitidis serogroup B (strain MC58).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC58;
RX   PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA   Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA   Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA   Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA   Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA   Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA   Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA   Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA   Moxon E.R., Rappuoli R., Venter J.C.;
RT   "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT   MC58.";
RL   Science 287:1809-1815(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; 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; AE002098; AAF41862.1; -; Genomic_DNA.
DR   PIR; F81075; F81075.
DR   RefSeq; NP_274514.1; NC_003112.2.
DR   RefSeq; WP_002225071.1; NC_003112.2.
DR   AlphaFoldDB; Q9JYM8; -.
DR   SMR; Q9JYM8; -.
DR   STRING; 122586.NMB1506; -.
DR   PaxDb; 122586-NMB1506; -.
DR   DNASU; 903953; -.
DR   KEGG; nme:NMB1506; -.
DR   PATRIC; fig|122586.8.peg.1907; -.
DR   HOGENOM; CLU_006406_5_1_4; -.
DR   InParanoid; Q9JYM8; -.
DR   OrthoDB; 9803211at2; -.
DR   Proteomes; UP000000425; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006420; P:arginyl-tRNA aminoacylation; IBA:GO_Central.
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   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_0000151583"
FT   MOTIF           122..132
FT                   /note="'HIGH' region"
SQ   SEQUENCE   572 AA;  62802 MW;  DA53F495CBB69EA7 CRC64;
     MNLHQTVEHE AAAAFAAAGI ADSPIVLQPT KNAEHGDFQI NGVMGAAKKA KQNPRELAQK
     VAEALADNAV IESAEVAGPG FINLRLRPEF LAQNIQTALN DARFGVAKTD KPQTVVIDYS
     SPNLAKEMHV GHLRSSIIGD SISRVLAFMG NTVIRQNHVG DWGTQFGMLV AYLVEQQKDN
     AAFELADLEQ FYRAAKVRFD EDPAFADTAR EYVVKLQGGD ETVLALWKQF VDISLSHAQA
     VYDTLGLKLR PEDVAGESKY NDDLQPVVDD LVQKGLAVED DGAKVVFLDE FKNKEGEPAA
     FIVQKQGGGF LYASTDLACL RYRIGRLKAD RLLYVVDHRQ ALHFEQLFTT SRKAGYLPEN
     VGAAFIGFGT MMGKDGKPFK TRSGDTVKLV DLLTEAVERA TALVKEKNPE LGADEAAKIG
     KTVGIGAVKY ADLSKNRTSD YVFDWDAMLS FEGNTAPYLQ YAYTRVQSVF RKAGEWDANA
     PTVLTEPLEK QLAAELLKFE DVLQSVADTA YPHYLAAYLY QIATLFSRFY EACPILKAEG
     ASRNSRLQLA KLTGDTLKQG LDLLGIDVLD VM
//