SYR_LEUCK
ID SYR_LEUCK Reviewed; 563 AA.
AC B1MZ82;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 75.
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=LCK_01007;
OS Leuconostoc citreum (strain KM20).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Leuconostoc.
OX NCBI_TaxID=349519;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KM20;
RX PubMed=18281406; DOI=10.1128/jb.01862-07;
RA Kim J.F., Jeong H., Lee J.-S., Choi S.-H., Ha M., Hur C.-G., Kim J.-S.,
RA Lee S., Park H.-S., Park Y.-H., Oh T.K.;
RT "Complete genome sequence of Leuconostoc citreum KM20.";
RL J. Bacteriol. 190:3093-3094(2008).
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; DQ489736; ACA82834.1; -; Genomic_DNA.
DR RefSeq; WP_012305268.1; NC_010471.1.
DR AlphaFoldDB; B1MZ82; -.
DR SMR; B1MZ82; -.
DR STRING; 349519.LCK_01007; -.
DR PRIDE; B1MZ82; -.
DR EnsemblBacteria; ACA82834; ACA82834; LCK_01007.
DR KEGG; lci:LCK_01007; -.
DR eggNOG; COG0018; Bacteria.
DR HOGENOM; CLU_006406_6_1_9; -.
DR OMA; NKPLHLG; -.
DR OrthoDB; 1146366at2; -.
DR Proteomes; UP000002166; 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.
FT CHAIN 1..563
FT /note="Arginine--tRNA ligase"
FT /id="PRO_1000095378"
FT MOTIF 121..131
FT /note="'HIGH' region"
SQ SEQUENCE 563 AA; 62783 MW; 17D5C526A02A5EBC CRC64;
MTDNKSIITS LSQVLPDIPV AEIAAKLESP KSSDLGDVAF PTFTLAKLLR QAPQQIASDI
VNRIDQSNFE KVVATGPYVN FFLDKKMTSQ ATLKTILTQG AAFGDNNDGD GANVTIDMSS
PNIAKPMSMG HLRSTVIGNA LANITAKNGY HPIKINHLGD WGTQFGKLIY AYKTWGTEAE
VKADPIATLL RYYVEFHEKA KIDDSLNDAG RAWFKKLEDG DEEAHQLWTW FRAESLKEFT
EIYDRLEISF DSFNGEAFYN DKMDKVVDML AEKSLLVESQ GAQIVDLSDI NPNLTPAMIK
RTDGATLYMT RDLAAAVYRK ETYNFAKSLY VVGGEQREHF VQMKAVLSLM GFDWADDVEH
IAFGLITFNG KKMSTRKGDV VLLKDVLNDA HDLALKQIQE KNPDLADKAT VAEQVGAGAV
VFHDLMNDRT NNFDFNLEEV VRFEGDTGPY VQYTNARAKS ILRKANTAVS VDELNLDDTA
TWDIITTLNQ FPTIVQRAWQ QREASIIAKY ALSLSRAFNK YYANSKILLP DDQLNARLAL
VKAVTIILSE SLRLLGVKAP EEM