SYR_CAMC1
ID SYR_CAMC1 Reviewed; 527 AA.
AC A7ZF21;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 77.
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=Ccon26_15320; ORFNames=CCC13826_0543;
OS Campylobacter concisus (strain 13826).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13826;
RA Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA Mandrell R.E., On S., Nelson K.E.;
RT "Genome sequence of Campylobacter concisus 13826 isolated from human
RT feces.";
RL Submitted (OCT-2007) 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; CP000792; EAT99295.1; -; Genomic_DNA.
DR RefSeq; WP_012140265.1; NC_009802.2.
DR AlphaFoldDB; A7ZF21; -.
DR SMR; A7ZF21; -.
DR STRING; 360104.CCC13826_0543; -.
DR EnsemblBacteria; EAT99295; EAT99295; CCC13826_0543.
DR KEGG; cco:CCC13826_0543; -.
DR eggNOG; COG0018; Bacteria.
DR HOGENOM; CLU_006406_0_1_7; -.
DR OMA; NKPLHLG; -.
DR OrthoDB; 1146366at2; -.
DR Proteomes; UP000001121; 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..527
FT /note="Arginine--tRNA ligase"
FT /id="PRO_1000018007"
FT MOTIF 111..121
FT /note="'HIGH' region"
SQ SEQUENCE 527 AA; 59455 MW; D59CC46E2C8B1465 CRC64;
MKDKVKAEIS KVLEREFVLE KPKDKNLAHY ATPLFSLAKE LRKSPAMIAS EFADKFSDSK
IVEASAVNGY LNFKLKSEFL DEISKQILLD SENFAKEDAK KDSYLIEYIS ANPTGPLHIG
HVRGAVYGDT LARLGKRLGY AISTEYYIND AGNQIDLLGT SISLAAKEQL FNESVVYPEK
YYRGDYILDI AKLANEKFGK EIFYDESRNL ELAEFGKDIV LEIIKKDLAD VGIFIESWAS
EKALYDGLEP TINKLKRSNQ MYEKEGATYI ASTTLGDDND RVVVRNDGRP TYLAGDIIYH
NAKFEKNFDH YINIWGADHH GYIARLKAAI NFLGYDENRL EVILMQMVSL LKEGKPYKMS
KRAGNAVLMS DIASEIGAEA LRFIFISKAN TSSLEFDVDE LKKEDSSNPI FYINYAHARI
NQIFAKAGKS VSDVINADFE CLDENSKNLL FEALILPEIL EDAFASRQLQ KIPDYLKSLA
ASFHKFYNEN RVVGNENEDS LLKVFAVVAV SIKTAFNIMG ITAKDRM