ID SYR_NEIMA Reviewed; 572 AA.
AC Q9JTM7; A1ISS4;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 126.
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=NMA1707;
OS Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS Z2491).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122587;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15465 / Z2491;
RX PubMed=10761919; DOI=10.1038/35006655;
RA Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA Barrell B.G.;
RT "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT Z2491.";
RL Nature 404:502-506(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}.
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DR EMBL; AL157959; CAM08836.1; -; Genomic_DNA.
DR PIR; F81866; F81866.
DR RefSeq; WP_002247007.1; NC_003116.1.
DR AlphaFoldDB; Q9JTM7; -.
DR SMR; Q9JTM7; -.
DR EnsemblBacteria; CAM08836; CAM08836; NMA1707.
DR KEGG; nma:NMA1707; -.
DR HOGENOM; CLU_006406_5_1_4; -.
DR Proteomes; UP000000626; 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 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..572
FT /note="Arginine--tRNA ligase"
FT /id="PRO_0000151582"
FT MOTIF 122..132
FT /note="'HIGH' region"
SQ SEQUENCE 572 AA; 62705 MW; A2666E45EEE90173 CRC64;
MNLHQTVERE AAAAFAAAGI ADSPVVLQPT KNAEHGDFQI NGVMGAAKKA KQNPRELAQK
VAEALADNAV IESAEVAGPG FINLRLRPEF LAQNIQTALN DARFGIAKTD KPQTVVIDYS
SPNLAKEMHV GHLRSSIIGD SISRVLAFMG NTVVRQNHVG DWGTQFGMLV AYLVEQQKDN
AAFELADLEQ FYRAAKVRFD EDPAFADTAR EYVVKLQGGD ETVLALWKQF VDISLSHAQA
VYDTLGLKLR PEDVAGESKY NDDLQPVVDD LVQKGLAVED DGAKVVFLDE FKNKEGEPAA
FIVQKQGGGF LYASTDLACL RYRVGTLHAD RLLYVVDHRQ ALHFEQLFTT SRKAGYLPEN
VGAAFVGFGT MMGKDGKPFK TRSGDTVKLV DLLTEAVERA AALVKEKNPE LGADEAAKIG
KTVGIGAVKY ADLSKNRTSN YVFDWDAMLS FEGNTAPYLQ YAYTRVQSVF RKAGEWDATA
PTVLSEPLEK QLAAELLKFE DVLQSVADTA YPHYLAAYLY QIATLFSRFY EACPILKAES
ASRNSRLQLA KLTGDTLKQG LDLLGIDVLD VM
//
