SYR_RHORT
ID SYR_RHORT Reviewed; 592 AA.
AC Q2RTG6;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 92.
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=Rru_A1779;
OS Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 /
OS NCIMB 8255 / S1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospirillum.
OX NCBI_TaxID=269796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1;
RX PubMed=21886856; DOI=10.4056/sigs.1804360;
RA Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K.,
RA Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C.,
RA Mavromatis K., Richardson P., Rohde M., Goeker M., Klenk H.P., Zhang Y.,
RA Roberts G.P., Reslewic S., Schwartz D.C.;
RT "Complete genome sequence of Rhodospirillum rubrum type strain (S1).";
RL Stand. Genomic Sci. 4:293-302(2011).
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; CP000230; ABC22579.1; -; Genomic_DNA.
DR RefSeq; WP_011389532.1; NC_007643.1.
DR RefSeq; YP_426866.1; NC_007643.1.
DR AlphaFoldDB; Q2RTG6; -.
DR SMR; Q2RTG6; -.
DR STRING; 269796.Rru_A1779; -.
DR EnsemblBacteria; ABC22579; ABC22579; Rru_A1779.
DR KEGG; rru:Rru_A1779; -.
DR PATRIC; fig|269796.9.peg.1857; -.
DR eggNOG; COG0018; Bacteria.
DR HOGENOM; CLU_006406_0_1_5; -.
DR OMA; NKPLHLG; -.
DR OrthoDB; 1146366at2; -.
DR PhylomeDB; Q2RTG6; -.
DR Proteomes; UP000001929; 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..592
FT /note="Arginine--tRNA ligase"
FT /id="PRO_0000242082"
FT MOTIF 131..141
FT /note="'HIGH' region"
SQ SEQUENCE 592 AA; 63983 MW; C82325FE04D7C5A0 CRC64;
MNVFHDIKET VLAQVAALQA EGRLPEGLET GRVAVEPPRE AAHGDMATNA AMVLAKPAGL
APRAVAEMLV EKLVGVDGIV AAETAGPGFI NLRLDPKIWR KTLKTVLTLG TAFGASTMGR
GAAVNVEFVS ANPTGPMHVG HGRGAVFGDA LAALLVKAGW AVTREYYVND AGAQVDSLAR
ALYARYRVAV GDLDEAAFAA MLAAREIEYG GDYLVPVAAD IAQADGTRWT TVAESDWLPA
FRAIGIERML ALIKEDLAAL GVVHDVFTSE QALVRAGRVD EMMTDLESRD LVYVGTLEPP
KGKTPDDWEP RPQTLFRATG FGDEVDRPLK KSDGSWTYFA SDIAYHHDKF KRGFLGMINV
LGADHGGYVK RLKAAVKAVS NGEAELDVKL VQLVKLLDNG EPVKMSKRAG TFITLREVVD
EVGKDVVRFI MLTRKNDAAL DFDYARVTEK TRDNPVFYVQ YAHARACSVA RHAAQTFPGR
DLSAAALAAT ADLDLLDADE EMAMVRLLAG WPRLVESAAE AHEPHRVAFY LGEVAAAFHG
LWNRGNDNAE LRFLLPTDEA RSLARLALVQ AVASVIASGL EIFGVEPVKE MR