ID A0A2K9P3Z7_9FIRM Unreviewed; 567 AA.
AC A0A2K9P3Z7;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Arginine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00123};
DE EC=6.1.1.19 {ECO:0000256|HAMAP-Rule:MF_00123};
DE AltName: Full=Arginyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00123};
DE Short=ArgRS {ECO:0000256|HAMAP-Rule:MF_00123};
GN Name=argS {ECO:0000256|HAMAP-Rule:MF_00123};
GN ORFNames=B9O19_01836 {ECO:0000313|EMBL:AUO19985.1};
OS Monoglobus pectinilyticus.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Monoglobus.
OX NCBI_TaxID=1981510 {ECO:0000313|EMBL:AUO19985.1, ECO:0000313|Proteomes:UP000235589};
RN [1] {ECO:0000313|EMBL:AUO19985.1, ECO:0000313|Proteomes:UP000235589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=14 {ECO:0000313|EMBL:AUO19985.1,
RC ECO:0000313|Proteomes:UP000235589};
RA Kim C., Rosendale D.I., Kelly W.J., Tannock G.W., Patchett M.L.,
RA Jordens J.Z.;
RT "Monoglobus pectinilyticus 14 draft genome.";
RL Submitted (APR-2017) 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:0000256|ARBA:ARBA00001766,
CC ECO:0000256|HAMAP-Rule:MF_00123};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00123}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00123}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00123,
CC ECO:0000256|RuleBase:RU363038}.
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DR EMBL; CP020991; AUO19985.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K9P3Z7; -.
DR OrthoDB; 9805987at2; -.
DR Proteomes; UP000235589; 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; Arginyl tRNA synthetase N-terminal domain; 1.
DR Gene3D; 3.40.50.620; HUPs; 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 NCBIfam; TIGR00456; argS; 1.
DR PANTHER; PTHR11956:SF5; ARGININE--TRNA LIGASE, CYTOPLASMIC-RELATED; 1.
DR PANTHER; PTHR11956; ARGINYL-TRNA SYNTHETASE; 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; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF55190; Arginyl-tRNA synthetase (ArgRS), N-terminal 'additional' domain; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00123};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00123};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00123};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00123};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00123};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00123}; Reference proteome {ECO:0000313|Proteomes:UP000235589}.
FT DOMAIN 17..102
FT /note="Arginyl tRNA synthetase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01016"
FT DOMAIN 447..567
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
FT MOTIF 139..149
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00123"
SQ SEQUENCE 567 AA; 63577 MW; F0BE2F089997FF77 CRC64;
MSIIDGIKSE IIEKISAGYK EAVSNGSLPE TDENIDISSL AKLEVPKDKS HGDFACNIAM
VLAKQLKTAP RKIADAITSN IDKSGDIKDI EVAGAGFINF YLAPDWLYRT MESIEKEGSD
YGKIDLGKGK KVMVEFVSAN PTGPMHMGNA RGGALGDCLA SVLEYAGYDV TREFYINDAG
NQIEKFGKSL SARYIQQLKG EDAIEFPEDG YQGGDITEHA KEFIKLYGDK YLDCGEDERK
QALIDYALEK NISALKTDLE KYRINYDVWF RESLLHKNGE VTSAIERLRK NGYTYDEDGA
VWLNCEKMGL EKNEVLVRQN GIPTYFAADI AYHINKLETR NFDLAINIWG ADHHGHVARM
KNALSAVGID SGRLEIVLMQ LVRLMQDGEI VRMSKRTGKA ITLNDLLEDV SIDAARFFFN
MRGAGSHLDF DLSLAKEQSN DNPVFYVQYA HARICGILRL LSEEGINVKP YAEIKPELLT
DETELDLLKK LSDLPEEIRI SAESLEPSKM TRYVMDLASA FHTFYNACRV NVEDEDLRDC
RMKLIDCTRQ VIAGVLNMLK ITAPEKM
//
