SYR_CAMFF
ID SYR_CAMFF Reviewed; 531 AA.
AC A0RQU0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=CFF8240_1433;
OS Campylobacter fetus subsp. fetus (strain 82-40).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360106;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=82-40;
RA Fouts D.E., Nelson K.E.;
RT "Sequence of Campylobacter fetus subsp. fetus 82-40.";
RL Submitted (NOV-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; CP000487; ABK82408.1; -; Genomic_DNA.
DR RefSeq; WP_002850314.1; NC_008599.1.
DR AlphaFoldDB; A0RQU0; -.
DR SMR; A0RQU0; -.
DR STRING; 360106.CFF8240_1433; -.
DR EnsemblBacteria; ABK82408; ABK82408; CFF8240_1433.
DR GeneID; 61065253; -.
DR KEGG; cff:CFF8240_1433; -.
DR eggNOG; COG0018; Bacteria.
DR HOGENOM; CLU_006406_0_1_7; -.
DR OMA; NKPLHLG; -.
DR OrthoDB; 1146366at2; -.
DR Proteomes; UP000000760; 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..531
FT /note="Arginine--tRNA ligase"
FT /id="PRO_1000018009"
FT MOTIF 113..123
FT /note="'HIGH' region"
SQ SEQUENCE 531 AA; 59844 MW; B359CAF39E5D6B7F CRC64;
MKNSVKSEIY RVLGRDFILE KPKDKNLAHY ATPFAFSLAK EFKKSPAIIA SQLALKFENH
ELFDVFSING YLNFKLKGEF LNSLANNALS LAESFGSKKP QSQKDIFIEY ISANPTGPLH
IGHVRGAVYG DTLARVARYI GLDVFTEYYI NDAGNQIDLL GISISLFARE ALFNENVQYP
DKYYRGEYIE DIAKLALGKF GKDIFYDESR NLELAEFGKD EVLKIIKKDL QDVGIFIESW
ASEKSLYDEL EGTIKKLASS GQMYEKDQTT YIASTMLGDD SDRVVIRSDG RPTYLAGDIV
YHDAKFKKGY KHYINIWGAD HHGYIARIKA AINFLGYDES RLEVILMQMV SLLKEGKPFK
MSKRAGTSVL MSDILSEIGS DALRFIFISK ANTSSLEFDI DELKKEDSSN PIFYINYAHA
RVNQVFAKAS KLPNDVVGAD LSNLDESGKN LLFEALILPE VLEDAVTSRS LHKIPEYLKS
LSASFHKFYN ENRVVGSKNE DELLKLFSVV ALSIKVALNL IGIKAKDKME H