ID E6NQM9_HELPQ Unreviewed; 541 AA.
AC E6NQM9;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Arginine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00123};
DE EC=6.1.1.19 {ECO:0000256|HAMAP-Rule:MF_00123};
DE AltName: Full=Arginyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00123};
DE Short=ArgRS {ECO:0000256|HAMAP-Rule:MF_00123};
GN Name=argS {ECO:0000256|HAMAP-Rule:MF_00123,
GN ECO:0000313|EMBL:BAJ59445.1};
GN OrderedLocusNames=HPF57_0371 {ECO:0000313|EMBL:BAJ59445.1};
OS Helicobacter pylori (strain F57).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=866346 {ECO:0000313|EMBL:BAJ59445.1, ECO:0000313|Proteomes:UP000008082};
RN [1] {ECO:0000313|EMBL:BAJ59445.1, ECO:0000313|Proteomes:UP000008082}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F57 {ECO:0000313|EMBL:BAJ59445.1,
RC ECO:0000313|Proteomes:UP000008082};
RX PubMed=21575176; DOI=10.1186/1471-2180-11-104;
RA Kawai M., Furuta Y., Yahara K., Tsuru T., Oshima K., Handa N.,
RA Takahashi N., Yoshida M., Azuma T., Hattori M., Uchiyama I., Kobayashi I.;
RT "Evolution in an oncogenic bacterial species with extreme genome
RT plasticity: Helicobacter pylori East Asian genomes.";
RL BMC Microbiol. 11:104-104(2011).
RN [2] {ECO:0000313|EMBL:BAJ59445.1, ECO:0000313|Proteomes:UP000008082}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F57 {ECO:0000313|EMBL:BAJ59445.1,
RC ECO:0000313|Proteomes:UP000008082};
RX PubMed=21212362; DOI=10.1073/pnas.1012579108;
RA Furuta Y., Kawai M., Yahara K., Takahashi N., Handa N., Tsuru T.,
RA Oshima K., Yoshida M., Azuma T., Hattori M., Uchiyama I., Kobayashi I.;
RT "Birth and death of genes linked to chromosomal inversion.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:1501-1506(2011).
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:0000256|ARBA:ARBA00001766,
CC ECO:0000256|HAMAP-Rule:MF_00123};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00123}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00123}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00123,
CC ECO:0000256|RuleBase:RU363038}.
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DR EMBL; AP011945; BAJ59445.1; -; Genomic_DNA.
DR RefSeq; WP_000557311.1; NC_017367.1.
DR AlphaFoldDB; E6NQM9; -.
DR KEGG; hex:HPF57_0371; -.
DR PATRIC; fig|866346.4.peg.396; -.
DR HOGENOM; CLU_006406_0_1_7; -.
DR Proteomes; UP000008082; 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; 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 {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00123};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00123};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00123};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00123};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00123};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00123}.
FT DOMAIN 3..81
FT /note="Arginyl tRNA synthetase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01016"
FT DOMAIN 423..537
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
FT MOTIF 119..129
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00123"
SQ SEQUENCE 541 AA; 62210 MW; 228105FEF59D261F CRC64;
MHTLVKGVLE EILEEEVIIE YPKDREHGHY ATPIAFNLAK VFKKSPLVIA EELALKISAH
EKTQGLFDSV VACKGYINFT LSLDFLERST QKALELKEKF GSQPKSEYSQ KIFLEFVSAN
PTGPLHIGHA RGAVFGDSLA KIARFLGHEV LREYYVNDMG SQIRLLGLSV WLAYREHVLK
ESVTYPEVFY KGEYIIEIAK KANNDLEPSL FKENEETIIE VLSGYAKDLM LLEIKDNLDA
LGIHFDSYAS EREVFKHKDT VFERLEKANA LYEKDSKIWL KSSLYQDESD RVLIKEDKSY
TYLAGDIVYH DEKFKQNYTK YINIWGADHH GYIARVKASL EFLGYDSNKL EVLLAQMVRL
LKDNEPYKMS KRAGNFILIK DVIDDVGKDA LRFIFLSKRL DTHLEFDVNT LKKQDSSNPI
YYIHYANSRI HTMLEKSPFS KEEILQTPLT NLNAEEKYLL FSALSLPKII ESSFEEYGLQ
KMCEYAKTLA SEFHRFYNAG KILNTPKAKE LLKICLMVSL SLSNAFKLLG IEIKTKISAK
D
//
