SYR_LIMRD
ID SYR_LIMRD Reviewed; 562 AA.
AC A5VL03;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=Lreu_1270;
OS Limosilactobacillus reuteri (strain DSM 20016) (Lactobacillus reuteri).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=557436;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20016;
RX PubMed=21379339; DOI=10.1371/journal.pgen.1001314;
RA Frese S.A., Benson A.K., Tannock G.W., Loach D.M., Kim J., Zhang M.,
RA Oh P.L., Heng N.C., Patil P.B., Juge N., Mackenzie D.A., Pearson B.M.,
RA Lapidus A., Dalin E., Tice H., Goltsman E., Land M., Hauser L., Ivanova N.,
RA Kyrpides N.C., Walter J.;
RT "The evolution of host specialization in the vertebrate gut symbiont
RT Lactobacillus reuteri.";
RL PLoS Genet. 7:E1001314-E1001314(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: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; CP000705; ABQ83527.1; -; Genomic_DNA.
DR RefSeq; WP_003668521.1; NZ_AZDD01000018.1.
DR AlphaFoldDB; A5VL03; -.
DR SMR; A5VL03; -.
DR STRING; 557436.Lreu_1270; -.
DR PRIDE; A5VL03; -.
DR EnsemblBacteria; ABQ83527; ABQ83527; Lreu_1270.
DR GeneID; 66471407; -.
DR KEGG; lre:Lreu_1270; -.
DR PATRIC; fig|557436.17.peg.593; -.
DR eggNOG; COG0018; Bacteria.
DR HOGENOM; CLU_006406_6_1_9; -.
DR OMA; NKPLHLG; -.
DR Proteomes; UP000001991; 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..562
FT /note="Arginine--tRNA ligase"
FT /id="PRO_1000057811"
FT MOTIF 121..131
FT /note="'HIGH' region"
SQ SEQUENCE 562 AA; 63879 MW; 2CC1383DE68EEF03 CRC64;
MSDKQQVAAA LAQALPEMDV KEIEAKIERP KDSSNGDYAF PTFFLAKTLH KAPQMIASEL
VEKVDQNGFE KVVVAGPYIN FFLDKAQVGA KILQTILADP EHYGEIDLGH QSNVTIDYSS
PNIAKPMGMG HLRSTMIGEA VARILEKVNY NLIRIDYLGD WGTQFGKLMA AYEMWGDEAE
VKKDPINTLL KYYVRINNEA DEHPEYTEAG RNWFAKLEHG DEEAWRLWHW FREVSLERFQ
RVYKMLDVNF DSFNGEAFSA QKMEEPIQLL RDKDLLKPSR GAEIVDLDEY NLPPLLIIKS
NGTTTYITRD LATALFRKRM YGHAKSLYVV GAEQETYFKQ LRAALKEMGF NWWDQIEHIS
FGLMNLNGKK MSTRKGNVVS LEDVLNDSID LARKQIAEKN PDLENADEVA KEVGVGAVIF
HDLKNYRRNA VNFKLEDVVK FEGETGPYVQ YARARAESIL RKGGIRDFSD VDLTKAGAEA
WELISFLGQY SEAIKRAALN YDPSVIAKYA LELAKKFNQY YAHTRILDKD EAQPARLALT
QAVSDVLKSA LDLLDIKAPD EM