SYR_CERS4
ID SYR_CERS4 Reviewed; 580 AA.
AC Q3J281;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 2.
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=RHOS4_15350;
GN ORFNames=RSP_2943;
OS Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=272943;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL Submitted (SEP-2005) 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; CP000143; ABA79103.2; -; Genomic_DNA.
DR RefSeq; WP_017140224.1; NZ_CP030271.1.
DR RefSeq; YP_353004.2; NC_007493.2.
DR AlphaFoldDB; Q3J281; -.
DR SMR; Q3J281; -.
DR STRING; 272943.RSP_2943; -.
DR DNASU; 3720683; -.
DR EnsemblBacteria; ABA79103; ABA79103; RSP_2943.
DR KEGG; rsp:RSP_2943; -.
DR PATRIC; fig|272943.9.peg.1880; -.
DR eggNOG; COG0018; Bacteria.
DR OMA; NKPLHLG; -.
DR Proteomes; UP000002703; Chromosome 1.
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..580
FT /note="Arginine--tRNA ligase"
FT /id="PRO_0000242077"
FT MOTIF 131..141
FT /note="'HIGH' region"
SQ SEQUENCE 580 AA; 63685 MW; 5104EADECB01DE64 CRC64;
MNLFTEIRTL VTAELGAMTE AGDLPAGLDL SAVAVEPPRD PAHGDMSTNA AMVLAKPSGK
PPRTIAEALA TRLAADPRIS SAEVAGPGFL NLRLRPAVWQ GMVATILQAG DTYGRSTIGA
GQKVNVEFVS ANPTGPMHVG HVRGAVVGDA LARLLAYAGW NVTREYYIND GGAQVDVLAR
SAFERYREAH GLEPEIREGL YPGDYLIPVG EALKAKYGDS LLDKGEQHWL TEVREFATEM
MMQMIREDLA ALGVEMDVYS SEKALYGTGK IEAALDRLKE MDLIYEGVLE PPKGKTPEDW
EPREQTLFRS TAHGDDVDRP VKKSDGSWTY FAPDIAYHYD KVTRGFDQLI DIFGADHGGY
VKRMKAAVAA LSAGRVPLDI KLIQLVKLWK NGEPFKMSKR AGTYVTLRDV VEQVGTDVTR
FVMLTRKNDA TLDFDFDKVL EQSKENPVFY VQYANARINS VLRKAREQGM DVSDATLATA
DLDRLDHPAE IALIAKLAEW PRLVEIAART NEPHRVAFYL HELASELHGL WNRGNDEAGL
RFLQDDPVVS QAKIALARAV GVVICAGLGI LGVTPVEEMR
