ID G2SX19_ROSHA Unreviewed; 595 AA.
AC G2SX19;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
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 ECO:0000313|EMBL:AEN96933.1};
GN OrderedLocusNames=RHOM_09110 {ECO:0000313|EMBL:AEN96933.1};
OS Roseburia hominis (strain DSM 16839 / JCM 17582 / NCIMB 14029 / A2-183).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Roseburia.
OX NCBI_TaxID=585394 {ECO:0000313|EMBL:AEN96933.1, ECO:0000313|Proteomes:UP000008178};
RN [1] {ECO:0000313|EMBL:AEN96933.1, ECO:0000313|Proteomes:UP000008178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16839 / JCM 17582 / NCIMB 14029 / A2-183
RC {ECO:0000313|Proteomes:UP000008178};
RX PubMed=26543119; DOI=10.1128/genomeA.01286-15;
RA Travis A.J., Kelly D., Flint H.J., Aminov R.I.;
RT "Complete genome sequence of the human gut symbiont Roseburia hominis.";
RL Genome Announc. 3:E0128615-E0128615(2015).
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; CP003040; AEN96933.1; -; Genomic_DNA.
DR RefSeq; WP_014079971.1; NC_015977.1.
DR AlphaFoldDB; G2SX19; -.
DR STRING; 585394.RHOM_09110; -.
DR GeneID; 77459434; -.
DR KEGG; rho:RHOM_09110; -.
DR eggNOG; COG0018; Bacteria.
DR HOGENOM; CLU_006406_5_1_9; -.
DR OrthoDB; 9805987at2; -.
DR BioCyc; RHOM585394:G1H02-1827-MONOMER; -.
DR Proteomes; UP000008178; 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 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}; Coiled coil {ECO:0000256|SAM:Coils};
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:UP000008178}.
FT DOMAIN 2..87
FT /note="Arginyl tRNA synthetase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01016"
FT DOMAIN 477..595
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
FT COILED 406..440
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 124..134
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00123"
SQ SEQUENCE 595 AA; 67128 MW; 1608ADA98F20F8E0 CRC64;
MKKILDLITG EVTQAFVDCG YDAKYGKVTL SNRPDLCEYQ CNGAMAAAKE YKKAPFMIAD
EVAEKLSGNA MFSMVESVKP GFLNLKLDEA YLADYVAKMQ ADEGRYGCEK TKEPKTIMID
YGGPNVAKPL HVGHLRSAII GESIKRIGRF MGHTVIGDVH LGDWGLQMGL IITELRERKP
DLVYFDENYT GEYPEEAPFT ISELEEIYPT ASGKSKEDAA YKEAAMQATY ELQHGRRGYQ
ALLSHILNVS VTDLKRNYKN LNVSFDLWKG ESDAQPYIPD MVQKMKDDGF AYISDGALVV
DVKEDTDTKE IPPCMILKSD GASLYNTTDL ATIVWRMKDY HPDELIYVVD KRQELYFTQV
FRCARKTGLV KPRTGLKFLG FGTMNGKDGK PFKTREGGVM RLQYLLESVN EEMLKKITEN
QKAKENLEIS EEEAKETAKM IALAAIKYGD LSNQASKDYI FDIDRFTSFE GNTGPYILYT
IVRIKSILNK YHSMGKDESG AVIEAAHSAS EKNLMLALSG FGAMMENAYE ETAPHKICSY
IYELANAFNS FYHETKIMSE ENEQIQKSYI RLLELTKSVL ETCIDLLGFQ APERM
//
