ID SYR_PARC0 Reviewed; 569 AA.
AC A1TJ83;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 99.
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=Aave_0414;
OS Paracidovorax citrulli (strain AAC00-1) (Acidovorax citrulli).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Paracidovorax.
OX NCBI_TaxID=397945;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAC00-1;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT "Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1.";
RL Submitted (DEC-2006) 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: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; CP000512; ABM31021.1; -; Genomic_DNA.
DR RefSeq; WP_011793597.1; NC_008752.1.
DR AlphaFoldDB; A1TJ83; -.
DR SMR; A1TJ83; -.
DR STRING; 397945.Aave_0414; -.
DR KEGG; aav:Aave_0414; -.
DR eggNOG; COG0018; Bacteria.
DR HOGENOM; CLU_006406_0_1_4; -.
DR OrthoDB; 9803211at2; -.
DR Proteomes; UP000002596; 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; cd07956; Anticodon_Ia_Arg; 1.
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; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..569
FT /note="Arginine--tRNA ligase"
FT /id="PRO_1000017982"
FT MOTIF 128..138
FT /note="'HIGH' region"
SQ SEQUENCE 569 AA; 62896 MW; 5A0F4FADD80424F3 CRC64;
MLSVKQELLA ALAGELEKLS PGSAGRAAFE SPKVAAHGDF ACTAAMQLAK PLKLNPRALG
EQLKAALEAT PAFARWVDAI EIAGPGFLNI RLKAAAKQEI VREVLSAGDR FGYQKDNGQR
VLVEFVSANP TGPLHVGHGR QAALGDAICN LFSTQGWSVH REFYYNDAGV QIDTLTKSTQ
LRARGFKPGD ECWPTDPENP ASKTFYNGDY IQDIANDFLA KKTVKADDRE FTANGDVEDY
DNIRQFAVAY LRNEQDKDLQ AFNLHFDQYY LESSLYTSGR VEATVNRLVE KGHTYEQDGA
LWLKSTDYGD DKDRVMRKKD GTYTYFVPDV AYHIAKWERG FAKVVNIQGT DHHGTIARVR
AGLQAADVGI PQGYPDYVLH TMVRVVKGGK EVKIGKRAGS YVTLRDLIEW TSKDAVRFFL
LSRKPDTEYT FDVDLAVAQN NDNPVYYVQY AHARIQSVLR AWAEAGGGDV ASLKDVDLSA
LEGPQAQALM LQLAKYPEML TAAAEGEAPH DVTFYLRDLA ASYHSYYDAE RILVDDEAVK
RARLALVAAT AQVLHNGLKV LGVDAPARM
//
