SYR_GEOKA
ID SYR_GEOKA Reviewed; 557 AA.
AC Q5KUF0;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 93.
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=GK3401;
OS Geobacillus kaustophilus (strain HTA426).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=235909;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTA426;
RX PubMed=15576355; DOI=10.1093/nar/gkh970;
RA Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA Matsui S., Uchiyama I.;
RT "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT Geobacillus kaustophilus.";
RL Nucleic Acids Res. 32:6292-6303(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; BA000043; BAD77686.1; -; Genomic_DNA.
DR RefSeq; WP_011232868.1; NC_006510.1.
DR AlphaFoldDB; Q5KUF0; -.
DR SMR; Q5KUF0; -.
DR STRING; 235909.GK3401; -.
DR EnsemblBacteria; BAD77686; BAD77686; GK3401.
DR KEGG; gka:GK3401; -.
DR eggNOG; COG0018; Bacteria.
DR HOGENOM; CLU_006406_0_1_9; -.
DR OMA; YEFKWER; -.
DR Proteomes; UP000001172; 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..557
FT /note="Arginine--tRNA ligase"
FT /id="PRO_0000242025"
FT MOTIF 132..142
FT /note="'HIGH' region"
SQ SEQUENCE 557 AA; 62698 MW; BBECD71C87879653 CRC64;
MNIVGQIKEK MKEEIRQAAV RAGLASADEL PDVLLEVPRD KAHGDYSTNI AMQLARIAKK
PPRAIAEAIV GQLDRERMSV ARIEIAGPGF INFYMDNRYL TAVVPAILQA GQAYGESNVG
NGEKVQVEFV SANPTGDLHL GHARGAAVGD SLCNILAKAG FDVTREYYIN DAGKQIYNLA
KSVEARYFQA LGVDMPLPED GYYGDDIVEI GKKLAEEYGD RFVEMEEEER LAFFRDYGLR
YELEKIKKDL ADFRVPFDVW YSETSLYESG KIDEALSTLR ERGYIYEQDG ATWFRSTAFG
DDKDRVLIKQ DGTYTYLLPD IAYHQDKLRR GFKKLINIWG ADHHGYIPRM KAAIAALGYD
PEALEVEIIQ MVNLYQNGER VKMSKRTGKA VTMRELMEEV GVDAVRYFFA MRSGDTHLDF
DMDLAVSQSN ENPVYYVQYA HARVSSILRQ AEEQHISYDG DLALHHLVET EKEIELLKVL
GDFPDVVAEA ALKRMPHRVT AYAFDLASAL HSFYNAEKVL DLDNIEKTKA RLALVKAVQI
TLQNALALIG VSAPEQM