SYR_ACIF2
ID SYR_ACIF2 Reviewed; 579 AA.
AC B7J3R6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, 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=AFE_0170;
OS Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768
OS / NCIMB 8455) (Ferrobacillus ferrooxidans (strain ATCC 23270)).
OC Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=243159;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455;
RX PubMed=19077236; DOI=10.1186/1471-2164-9-597;
RA Valdes J., Pedroso I., Quatrini R., Dodson R.J., Tettelin H., Blake R. II,
RA Eisen J.A., Holmes D.S.;
RT "Acidithiobacillus ferrooxidans metabolism: from genome sequence to
RT industrial applications.";
RL BMC Genomics 9:597-597(2008).
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; CP001219; ACK78518.1; -; Genomic_DNA.
DR RefSeq; WP_012535997.1; NC_011761.1.
DR AlphaFoldDB; B7J3R6; -.
DR SMR; B7J3R6; -.
DR STRING; 243159.AFE_0170; -.
DR PaxDb; B7J3R6; -.
DR EnsemblBacteria; ACK78518; ACK78518; AFE_0170.
DR GeneID; 66431230; -.
DR KEGG; afr:AFE_0170; -.
DR eggNOG; COG0018; Bacteria.
DR HOGENOM; CLU_006406_0_1_6; -.
DR OMA; NKPLHLG; -.
DR OrthoDB; 1146366at2; -.
DR Proteomes; UP000001362; 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..579
FT /note="Arginine--tRNA ligase"
FT /id="PRO_1000198863"
FT MOTIF 127..137
FT /note="'HIGH' region"
SQ SEQUENCE 579 AA; 64520 MW; 733F5D6CCB2118DC CRC64;
MKAFVSQALQ GALQQLHAQG RIPGIPATLE LDRPKQVEHG HLASNVALLL AKAVGRKPRD
IADDIVAALP ASDWIARTEI AGPGFINFFL QPAAFHAVIH RVRTEKEHFG ANRNGAGQRL
QMEFVSANPT GPLHVGHGRG AAYGASLANI LRFNGFDIFC EYYVNDAGRQ MDILAASVYL
RYLEADKALP WPFPENGYRG DYVREIAAHL REQVGDRLRH AAVGLPNLPQ MSDGDIAIDT
LIAHLKQSLG EDYRTLHSAG LDEILADIRD DLEGFGVHYE RWYSEGSLMD TGAVDSAVAA
LEKAGHCYTQ EGALWFRATA FDDDKDRVLR RDNGAYTYFA SDVAYHAEKF ARGFTHVIDM
WGADHHGYVP RVKAALRALG LDDQQLEVVL VQFAILYRGT EKISMSTRAG EFVTLRELRE
EVGNDAARFF YVLRRADQHL DFDLELAKKH SEENPVFYIQ YAHARVYSLL RQSVEKGLSL
PPADGVGLEI LQESREIALA DALWRFPEVV ATAARDREPH QIAFYLRELA AAFHTYYNST
RILVEETPLR HARLTLCLAV AQSIANGLRL LGVSAPEQM