SYR_BURCM
ID SYR_BURCM Reviewed; 593 AA.
AC Q0BBE9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 86.
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=Bamb_2968;
OS Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia
OS (strain AMMD)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=339670;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-244 / AMMD;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P.,
RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K.,
RA Ramette A., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD.";
RL Submitted (AUG-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; CP000440; ABI88524.1; -; Genomic_DNA.
DR RefSeq; WP_011658056.1; NZ_CP009798.1.
DR AlphaFoldDB; Q0BBE9; -.
DR SMR; Q0BBE9; -.
DR STRING; 339670.Bamb_2968; -.
DR EnsemblBacteria; ABI88524; ABI88524; Bamb_2968.
DR GeneID; 44693632; -.
DR KEGG; bam:Bamb_2968; -.
DR PATRIC; fig|339670.21.peg.1910; -.
DR eggNOG; COG0018; Bacteria.
DR OMA; NKPLHLG; -.
DR Proteomes; UP000000662; Chromosome 1.
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..593
FT /note="Arginine--tRNA ligase"
FT /id="PRO_1000017999"
FT MOTIF 138..148
FT /note="'HIGH' region"
SQ SEQUENCE 593 AA; 64289 MW; 5441A622104ACDCC CRC64;
MLPAHKQTLE ALLADSVTQV AHALKGADAA FVAPAITLER PKVAAHGDVA CNVAMQLAKP
LGTNPRQLAE KIVAALTAQP AAQGLVDAAD IAGPGFINLR LTAAAKQAVI AAVFEQGRAF
GTSDREKGKQ VLLEFVSANP TGPLHVGHGR QAALGDVLAN VIASQGYAVH REFYYNDAGV
QIGNLAISTQ ARARGLKPGD AGWPEAAYNG EYIADIARDY LNRETVAAKD GEPVTGAGDI
DDLDAIRKFA VAYLRHEQDM DLQAFGVKFD QYYLESSLYS EGRVEKTVDA LVKAGMTYEQ
DGALWLRTTD EGDDKDRVMR KSDGTYTYFV PDVAYHVTKW ERGFTQVINI QGSDHHGTIA
RVRAGLQGLH VGIPKGYPDY VLHKMVTVMR DGQEVKLSKR AGSYVTVRDL IEWSGGAAPG
QEAAPDLIDE ATITRGRDAV RFFLISRKAD TEFVFDIDLA LKQNDENPVY YVQYAHARIC
SVLNELKSRY NVDVAQLPGA DLSQLTSAQA VSLMQKLAEY PDMLTHAAKE LAPHAVAFYL
RDLAGEFHSF YNAERVLVDD EAPRNARAAL LAATRQVLEN GLAVLGVSAP AKM