SYR_BURMA
ID SYR_BURMA Reviewed; 594 AA.
AC Q62MY7;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=BMA0084;
OS Burkholderia mallei (strain ATCC 23344).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=243160;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23344;
RX PubMed=15377793; DOI=10.1073/pnas.0403306101;
RA Nierman W.C., DeShazer D., Kim H.S., Tettelin H., Nelson K.E.,
RA Feldblyum T.V., Ulrich R.L., Ronning C.M., Brinkac L.M., Daugherty S.C.,
RA Davidsen T.D., DeBoy R.T., Dimitrov G., Dodson R.J., Durkin A.S.,
RA Gwinn M.L., Haft D.H., Khouri H.M., Kolonay J.F., Madupu R., Mohammoud Y.,
RA Nelson W.C., Radune D., Romero C.M., Sarria S., Selengut J., Shamblin C.,
RA Sullivan S.A., White O., Yu Y., Zafar N., Zhou L., Fraser C.M.;
RT "Structural flexibility in the Burkholderia mallei genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14246-14251(2004).
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; CP000010; AAU48639.1; -; Genomic_DNA.
DR RefSeq; WP_004189649.1; NC_006348.1.
DR RefSeq; YP_101930.1; NC_006348.1.
DR AlphaFoldDB; Q62MY7; -.
DR SMR; Q62MY7; -.
DR STRING; 243160.BMA0084; -.
DR EnsemblBacteria; AAU48639; AAU48639; BMA0084.
DR GeneID; 56594611; -.
DR KEGG; bma:BMA0084; -.
DR PATRIC; fig|243160.12.peg.81; -.
DR eggNOG; COG0018; Bacteria.
DR HOGENOM; CLU_006406_0_1_4; -.
DR OMA; NKPLHLG; -.
DR Proteomes; UP000006693; 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..594
FT /note="Arginine--tRNA ligase"
FT /id="PRO_0000241996"
FT MOTIF 139..149
FT /note="'HIGH' region"
SQ SEQUENCE 594 AA; 64578 MW; D8DC2150D8A83604 CRC64;
MLPAQKHTLE TLLENSVKQV VQASKGDADA AFVLPAIALE RPKVAAHGDV ACNVALQLAK
PLGANPRQLA EQIVAALTAQ PEAAGLVDAA EIAGPGFINL RLTPASKQAV IGAVLAQGRA
FGASERDHDK RVLLEFVSAN PTGPLHVGHG RQAALGDALA NVLASQGYAV HREFYYNDAG
VQIGNLAIST QARARGLKPG DAGWPEAAYN GEYIADIARD YLNGETVAAS DGEPVTGKRD
VEDLEAIRKF AVTYLRREQD MDLKAFGVKF DQYYLESSLY TEGRVEKTVD ALIAAGMTYE
QEGALWLRTT DEGDDKDRVM RKTDGTYTYF VPDVAYHVTK WERGFTKVIN IQGSDHHGTI
ARVRAGLQGL HIGIPKGYPD YVLHKMVTVM RDGQEVKISK RAGSYVTVRD LIEWSGGATP
GSEGSPELLD EATITRGRDA VRFFLISRKA DTEFVFDIDL ALKQNDENPV YYVQYAHARI
CSVINEWKSR YGATDALLPG ADLSPLDSKQ AMALMQKLAE YPDVLAHAAG ELAPHAVAFY
LRELASEFHS FYNAERVLVD EQAPRTARVA LLAATRQVLE NGLAMLGVSA PSKM