SYR_RICAH
ID SYR_RICAH Reviewed; 576 AA.
AC A8GM09;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 25-MAY-2022, entry version 77.
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=A1C_00505;
OS Rickettsia akari (strain Hartford).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=293614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hartford;
RA Madan A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA Sanchez A., Whiting M., Dasch G., Eremeeva M.;
RT "Complete genome sequence of Rickettsia akari.";
RL Submitted (SEP-2007) 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; CP000847; ABV74434.1; -; Genomic_DNA.
DR RefSeq; WP_012013304.1; NC_009881.1.
DR AlphaFoldDB; A8GM09; -.
DR SMR; A8GM09; -.
DR STRING; 293614.A1C_00505; -.
DR EnsemblBacteria; ABV74434; ABV74434; A1C_00505.
DR KEGG; rak:A1C_00505; -.
DR eggNOG; COG0018; Bacteria.
DR HOGENOM; CLU_006406_0_1_5; -.
DR OMA; NKPLHLG; -.
DR Proteomes; UP000006830; 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.
FT CHAIN 1..576
FT /note="Arginine--tRNA ligase"
FT /id="PRO_1000018104"
FT MOTIF 126..136
FT /note="'HIGH' region"
SQ SEQUENCE 576 AA; 65387 MW; 624C29194F64F577 CRC64;
MNIFNKLKQD IIAASRQLYN NQEIANNATI ETPKDNFNGD LSSNIAMIIA AKENISPREV
ALKFKEILIT LPYIASIEIA GPGFINFTIK AETWQIAIKD ILQHEEKFCE IDIDKSRNIN
IEYVSANPTG PMHIGHARGA VYGDVLARIL QKVGYFVTKE YYVNDAGSQI NDLVSTVLLR
YREALGETIT IPDGLYPGEY LIPLGQILAE EYGNKLLMMD EEERFKIVKN FAVEKMLDLN
RKDLADLGIK HDIFFSEQSL HDKCAIEETV KLLTGMGLIY EGILPPPKGK VHDEWDNRVQ
KLFKSTNYGD SQDRPIEKAD GSWSYFASDL AYAKDKIDRG VSHLIYVLGA DHSGYVKRIE
AIVKALGKEQ VKVDVKICQL VNFVENGVPV KMSKRLGSFA SVQDVNHEVG KDIIRFMMLT
RQNDKPLDFD LVKVKEQSRE NPIFYVQYAH VRTISILSKA RELMPESYNN FEACKYDLSL
LSSEEEIAII KLLASWTKTL ETSAKYFEPH RIAFYLINLA SKFHSMWNFG KEHSDYRFII
ESNKELTTAR LALATAIQKV IASGLEVIGV EPMDRM