SYR_HELPJ
ID SYR_HELPJ Reviewed; 541 AA.
AC Q9ZMB9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=Arginine--tRNA ligase;
DE EC=6.1.1.19;
DE AltName: Full=Arginyl-tRNA synthetase;
DE Short=ArgRS;
GN Name=argS; OrderedLocusNames=jhp_0302;
OS Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J99 / ATCC 700824;
RX PubMed=9923682; DOI=10.1038/16495;
RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT "Genomic sequence comparison of two unrelated isolates of the human gastric
RT pathogen Helicobacter pylori.";
RL Nature 397:176-180(1999).
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;
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; AE001439; AAD05887.1; -; Genomic_DNA.
DR PIR; H71947; H71947.
DR RefSeq; WP_000557128.1; NZ_CP011330.1.
DR AlphaFoldDB; Q9ZMB9; -.
DR SMR; Q9ZMB9; -.
DR STRING; 85963.jhp_0302; -.
DR EnsemblBacteria; AAD05887; AAD05887; jhp_0302.
DR KEGG; hpj:jhp_0302; -.
DR PATRIC; fig|85963.30.peg.711; -.
DR eggNOG; COG0018; Bacteria.
DR OMA; NKPLHLG; -.
DR Proteomes; UP000000804; 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..541
FT /note="Arginine--tRNA ligase"
FT /id="PRO_0000151566"
FT MOTIF 119..129
FT /note="'HIGH' region"
SQ SEQUENCE 541 AA; 62158 MW; 81524A78BC125281 CRC64;
MHTLIKGVLE EILEAEVIIE YPKDREHGHY ATPIAFNLAK VFKKSPLAIA EELALKIGSH
EKTQGFFDRV VACKGYINFT LSLDFLERFT QKALELKEQF GSQVKSERSQ KIFLEFVSAN
PTGPLHIGHA RGAVFGDSLA KIARFLGHEV LCEYYVNDMG SQIRLLGVSV WLAYKEHVLK
ESVTYPEVFY KGEYIIEIAK KAHNDLEPSL FKENEETIIE VLSDYAKDLM LLEIKGNLDA
LDIHFDSYAS EKEVFKHKDA VFDRLEKANA LYEKDSKTWL KSSLYQDESD RVLIKEDKSY
TYLAGDIVYH DEKFQQNYTK YINIWGADHH GYIARVKASL EFLGYDSSKL EVLLAQMVRL
LKDNEPYKMS KRAGNFILIK DVIDDVGKDA LRFIFLSKRL DTHLEFDVNT LKKQDSSNPI
YYIHYANSRI HTMLEKSPFS KEEILQTPLK NLNAEEKYLL FSALSLPKAV ESSFEEYGLQ
KMCEYAKTLA SEFHRFYNAG KILDTPKAKE LLKICLMVSL SLTNAFKLLG IEIKTKISSK
D