SYR_ELUMP
ID SYR_ELUMP Reviewed; 532 AA.
AC B2KD56;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 25-MAY-2022, entry version 76.
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}; OrderedLocusNames=Emin_0897;
OS Elusimicrobium minutum (strain Pei191).
OC Bacteria; Elusimicrobia; Elusimicrobia; Elusimicrobiales;
OC Elusimicrobiaceae; Elusimicrobium.
OX NCBI_TaxID=445932;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pei191;
RX PubMed=19270133; DOI=10.1128/aem.02698-08;
RA Herlemann D.P.R., Geissinger O., Ikeda-Ohtsubo W., Kunin V., Sun H.,
RA Lapidus A., Hugenholtz P., Brune A.;
RT "Genomic analysis of 'Elusimicrobium minutum,' the first cultivated
RT representative of the phylum 'Elusimicrobia' (formerly termite group 1).";
RL Appl. Environ. Microbiol. 75:2841-2849(2009).
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; CP001055; ACC98452.1; -; Genomic_DNA.
DR RefSeq; WP_012415067.1; NC_010644.1.
DR AlphaFoldDB; B2KD56; -.
DR SMR; B2KD56; -.
DR STRING; 445932.Emin_0897; -.
DR EnsemblBacteria; ACC98452; ACC98452; Emin_0897.
DR KEGG; emi:Emin_0897; -.
DR HOGENOM; CLU_006406_0_1_0; -.
DR OMA; NKPLHLG; -.
DR OrthoDB; 1146366at2; -.
DR Proteomes; UP000001029; 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; 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.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..532
FT /note="Arginine--tRNA ligase"
FT /id="PRO_1000198900"
FT MOTIF 122..132
FT /note="'HIGH' region"
SQ SEQUENCE 532 AA; 59933 MW; E053EF06446F8DDC CRC64;
MLDNLKKDIE TKLFNAEVFE GAVLPPVDLT PAPPHTGADI SLTWAMSAAK TLKKNPLEIA
KAAVKVISEV TFVASASYAA PGFINIILED SFISSSALDR RLKNRKTAGE NKERVLIEFV
SANPTGPLHV ASGRGASLGD SLVRIFNALG IQCDSEYYVN DSGNQAMLLG VSLKARVNGQ
EPPENGYHGS YLIEMADEIR EMSKDWTEEQ FSIYAIEYLI KTHQRDMQAF NVNFTRWFRE
SELYKESLPA KALDFLKEKG LAYEADGAVW FGTTKDNDDK DRVLVRADGR PTYFLADIAY
HKNKYDRGFT TLVDILGADH HGYVPRMKAA VKALGENEES FVPIIHQLVH LIEGGEKVKM
SKRSGRFITL KELTEEVGAD ACRFLFASRT PDAHMNFDID LAKKRTNENP VFYVQYVHAR
AASIARMAEQ KHLQQAENLV DFKLTPQERT LLIKILWFKH ALKNCVRDMS PHHLTTYLIE
LAGNFHSFYD ACRVVDEDNP QTTAHRLLIC DRVRERIKKG LEFLGVSAPE EM