SYR_LISMH
ID SYR_LISMH Reviewed; 556 AA.
AC B8DBE8;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 67.
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=LMHCC_0035;
OS Listeria monocytogenes serotype 4a (strain HCC23).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=552536;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HCC23;
RX PubMed=21602330; DOI=10.1128/jb.05236-11;
RA Steele C.L., Donaldson J.R., Paul D., Banes M.M., Arick T., Bridges S.M.,
RA Lawrence M.L.;
RT "Genome sequence of lineage III Listeria monocytogenes strain HCC23.";
RL J. Bacteriol. 193:3679-3680(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; CP001175; ACK38399.1; -; Genomic_DNA.
DR RefSeq; WP_012580731.1; NC_011660.1.
DR AlphaFoldDB; B8DBE8; -.
DR SMR; B8DBE8; -.
DR KEGG; lmh:LMHCC_0035; -.
DR HOGENOM; CLU_006406_0_1_9; -.
DR OMA; YEFKWER; -.
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..556
FT /note="Arginine--tRNA ligase"
FT /id="PRO_1000198918"
FT MOTIF 132..142
FT /note="'HIGH' region"
SQ SEQUENCE 556 AA; 62750 MW; 2587ECA066A72C1D CRC64;
MNVMQENQIK LIAHIKQAVV QAVGLEEAEV PEILLEVPKD KKHGDYSTNI AMQLARVAKK
APRQIAESIV PELKKDNKLI KEVEIAGPGF INFYLDNAYL TDLVPVILTE DKQYGESDFG
KGEKFQIEFV SANPTGDLHL GHARGAAIGD SLANIMKMAG FDVSREYYIN DAGNQINNLV
LSAEARYFEA LGLDSEFPED GYRGADIISL GKDLAAKYGD KYVHTSEEER RSVFRVDALA
FETGKLRADL EEFRVSFDEW FSETSLYEEN KVLPALERLR ENGYIYEQDG ATWLRTTDFE
DDKDRVLIKS DGSYTYFLPD IAYHLNKLER GFDVLIDIWG ADHHGYIPRM RAAIEALGYS
PNQLEVEIIQ LVHLFEDGVQ VKMSKRTGKS VTMRDLIEEV GLDATRYFFA MRSSDTHMNF
DMSLAKSTSN DNPVYYVQYA HARISSILRS GKEQGLEVTK DADMSLLQTE AEYDLLKVLG
EFADVVAEAA TKRAPHRIVR YLNDLASAFH RFYNSNKVLD MDNLEVTKAR LALIKTAQIT
LRNGLTLLGV SAPEKM