SYR_BEII9
ID SYR_BEII9 Reviewed; 590 AA.
AC B2IJG9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 25-MAY-2022, entry version 73.
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=Bind_2710;
OS Beijerinckia indica subsp. indica (strain ATCC 9039 / DSM 1715 / NCIMB
OS 8712).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Beijerinckiaceae; Beijerinckia.
OX NCBI_TaxID=395963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9039 / DSM 1715 / NCIMB 8712;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., LaButti K., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Mikhailova N., Dunfield P.F., Dedysh S.N.,
RA Liesack W., Saw J.H., Alam M., Chen Y., Murrell J.C., Richardson P.;
RT "Complete sequence of chromosome of Beijerinckia indica subsp. indica ATCC
RT 9039.";
RL Submitted (MAR-2008) 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; CP001016; ACB96282.1; -; Genomic_DNA.
DR RefSeq; WP_012385633.1; NC_010581.1.
DR AlphaFoldDB; B2IJG9; -.
DR SMR; B2IJG9; -.
DR STRING; 395963.Bind_2710; -.
DR PRIDE; B2IJG9; -.
DR EnsemblBacteria; ACB96282; ACB96282; Bind_2710.
DR KEGG; bid:Bind_2710; -.
DR eggNOG; COG0018; Bacteria.
DR HOGENOM; CLU_006406_0_1_5; -.
DR OMA; NKPLHLG; -.
DR OrthoDB; 1146366at2; -.
DR Proteomes; UP000001695; 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; -; 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; 2.
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; Reference proteome.
FT CHAIN 1..590
FT /note="Arginine--tRNA ligase"
FT /id="PRO_1000198873"
FT MOTIF 134..144
FT /note="'HIGH' region"
SQ SEQUENCE 590 AA; 64693 MW; 67B73284E33453A1 CRC64;
MNIFTEFHAR IAAILRGIIG SGRLPEDLDL TRFVVEPPRE AAHGDLAANA AMVYAKEAKP
AFANPRQLAV EIAVALAEDG DVAEAEVAGP GFINIRLKPE FFGRLLGAAL EQGSDFGRPA
TAAQEKINVE YVSANPTGPM HVGHGRGAVF GDALANLLAF AGFGVTREYY INDAGAQVDV
LARSAHLRYR EALGETIGAI PEGLYPGDYL KSVGASLAQA HGDTYRGSNG EEWLEIFRLA
AIDGMMAMIR DDLAALNITH EVFFSERSLT RSEDGDQVAA AIAFLRDRGL VYEGRLPPPK
GQAIEDWEDR EQVLFKSTDF GDDVDRPLKK SDGTYTYFAS DIAYHKTKID RGYSVLIDVW
GADHGGYVKR MAAAVKALSE GRVTLDVKLC QLVKLMRGGE PVKMSKRAGD FVTLREVVDE
VGVDAVRFMM LFRKNDAVLE FDLAKVIEQS KDNPVFYVQY AHARVKSVFR QAATLLPDLD
CSLAALKTAD FSLLGDEGEA RLIKIIAQFP RVVEGAALAH EPHRIAFYLH DLASELHAHW
TRGKDQPHLR FIYEERRDLT LARLALVHIM AEVLASGLSL LGVSAPSEMR