SYR_CAMJJ
ID SYR_CAMJJ Reviewed; 530 AA.
AC A1W0F9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 82.
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=CJJ81176_1190;
OS Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=354242;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=81-176;
RA Fouts D.E., Nelson K.E., Sebastian Y.;
RL Submitted (DEC-2006) 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; CP000538; EAQ72230.1; -; Genomic_DNA.
DR RefSeq; WP_011812766.1; NC_008787.1.
DR AlphaFoldDB; A1W0F9; -.
DR SMR; A1W0F9; -.
DR STRING; 354242.CJJ81176_1190; -.
DR EnsemblBacteria; EAQ72230; EAQ72230; CJJ81176_1190.
DR KEGG; cjj:CJJ81176_1190; -.
DR eggNOG; COG0018; Bacteria.
DR HOGENOM; CLU_006406_0_1_7; -.
DR OMA; NKPLHLG; -.
DR Proteomes; UP000000646; 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..530
FT /note="Arginine--tRNA ligase"
FT /id="PRO_1000018011"
FT MOTIF 113..123
FT /note="'HIGH' region"
SQ SEQUENCE 530 AA; 60244 MW; 0CA2E967B6739912 CRC64;
MKSIIFNEIK KILECDFALE NPKDKNLAHF ATPLAFSLAK ELKKSPMLIA SDLASKFQNH
DCFELVEAVN GYLNFRISKT FLNELANQAL TNPNDFTKGE KKQESFLLEY VSANPTGPLH
IGHARGAVFG DTLTRLARHL GYKFDTEYYV NDAGNQIYLL GLSILLSVKE NILHENVEYP
EQYYKGEYIA DLAKEAFEKF GKEFFSEENI PSLADWAKDK MLVLIKQNLE QVKIKIDSYV
SERSYYDALN ATLESLKEHK GIYEQEGKIW LASSQKGDEK DRVIIREDGR GTYLAADIVY
HKDKMSRGYG KCINIWGADH HGYIPRMKAA MEFLGFDSNN LEIILAQMVS LLKDGEPYKM
SKRAGNFILM SDVVDEIGSD ALRYIFLSKK CDTHLEFDIS DLQKEDSSNP VYYINYAHAR
IHQVFAKAGK KIDDVMKADL QSLNQDGVNL LFEALNLKAV LNDAFEARAL QKIPDYLKNL
AANFHKFYNE NKVVGSANEN DLLKLFSLVA LSIKTAFSLM GIEAKNKMEH