SYR_MAGSA
ID SYR_MAGSA Reviewed; 576 AA.
AC Q2W492;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 90.
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=amb2529;
OS Magnetospirillum magneticum (strain AMB-1 / ATCC 700264).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Magnetospirillum.
OX NCBI_TaxID=342108;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=16303747; DOI=10.1093/dnares/dsi002;
RA Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.;
RT "Complete genome sequence of the facultative anaerobic magnetotactic
RT bacterium Magnetospirillum sp. strain AMB-1.";
RL DNA Res. 12:157-166(2005).
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; AP007255; BAE51333.1; -; Genomic_DNA.
DR RefSeq; WP_011384910.1; NC_007626.1.
DR AlphaFoldDB; Q2W492; -.
DR SMR; Q2W492; -.
DR STRING; 342108.amb2529; -.
DR EnsemblBacteria; BAE51333; BAE51333; amb2529.
DR KEGG; mag:amb2529; -.
DR HOGENOM; CLU_006406_0_1_5; -.
DR OMA; NKPLHLG; -.
DR OrthoDB; 1146366at2; -.
DR Proteomes; UP000007058; 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; 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; Reference proteome.
FT CHAIN 1..576
FT /note="Arginine--tRNA ligase"
FT /id="PRO_0000242040"
FT MOTIF 125..135
FT /note="'HIGH' region"
SQ SEQUENCE 576 AA; 62999 MW; 0887C23405677058 CRC64;
MNLFKYFREE IIKSVEAIVP GLDTSKVTAE PPREVSHGDV ATNAAMVLTK AAGMKPRDLA
EKIAEVLRAH PAVTGVEVAG PGFINLRLAD SFWFERLAEV LAAGTAYGQS DLGRGHKVNV
EYVSANPTGP MHIGHARGAV FGDALASLLV KAGYDVTREY YVNDAGSQVD VLARSAFLRY
REALGEEIGE IPEGLYPGEY LKPAGEALAK KHGPALKDKP EEEWLPELRG FAVDAMLDMI
KGDLAGLGVR HDVFVSERGL VEAGKVQDAL DYLTAKGLIY EGVLEPPKGK LPDDWEARPQ
TLFKATEFGD DVDRPLKKSD GSWTYFASDI AYHLDKYRRG FGAMIDVWGA DHGGYVKRMQ
AAVKAVSEGG GDLDVKLCQM VNLLKGGQPY KMSKRAGTFV TLRDLVEAVG KDVVRFIMLT
RKNDAHLDFD LDKVLEQSRD NPVFYVQYAH ARCHSVMRHA AGMWPDAVGP VPGVEVLAHL
TDPAELGLIR LLAGWPRLVE SAAEAHEPHR VAFYLYDLAA AFHGLWNKGK DDTSLRFLIE
DDRELSLARL GLLRAVVGVI ASGLGIFGVA PVEEMR