ID E4UE18_LIBSC Unreviewed; 586 AA. AC E4UE18; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 13-SEP-2023, entry version 65. DE RecName: Full=Arginine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00123}; DE EC=6.1.1.19 {ECO:0000256|HAMAP-Rule:MF_00123}; DE AltName: Full=Arginyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00123}; DE Short=ArgRS {ECO:0000256|HAMAP-Rule:MF_00123}; GN Name=argS {ECO:0000256|HAMAP-Rule:MF_00123}; GN OrderedLocusNames=CKC_05505 {ECO:0000313|EMBL:ADR52846.1}; OS Liberibacter solanacearum (strain CLso-ZC1). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Rhizobiaceae; Liberibacter. OX NCBI_TaxID=658172 {ECO:0000313|EMBL:ADR52846.1, ECO:0000313|Proteomes:UP000007038}; RN [1] {ECO:0000313|Proteomes:UP000007038} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CLso-ZC1 {ECO:0000313|Proteomes:UP000007038}; RA Lin H., Doddapaneni H.V., Lou B., Civerolo E.L., Chen C., Duan Y., Zhou L., RA Glynn J.; RT "Complete genome sequence of Candidatus Liberibacter solanacearum CLso- RT ZC1."; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CLso-ZC1; RA Lin H., Doddapaneni H.V., Lou B., Civerolo E.L., Chen C., Duan Y., Zhou L., RA Glynn J.; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:ADR52846.1, ECO:0000313|Proteomes:UP000007038} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CLso-ZC1 {ECO:0000313|EMBL:ADR52846.1, RC ECO:0000313|Proteomes:UP000007038}; RX PubMed=21552483; DOI=10.1371/journal.pone.0019135; RA Lin H., Lou B., Glynn J.M., Doddapaneni H., Civerolo E.L., Chen C., RA Duan Y., Zhou L., Vahling C.M.; RT "The Complete Genome Sequence of 'Candidatus Liberibacter solanacearum', RT the Bacterium Associated with Potato Zebra Chip Disease."; RL PLoS ONE 6:E19135-E19135(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:0000256|ARBA:ARBA00001766, CC ECO:0000256|HAMAP-Rule:MF_00123}; CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00123}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00123}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00123, CC ECO:0000256|RuleBase:RU363038}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP002371; ADR52846.1; -; Genomic_DNA. DR RefSeq; WP_013462500.1; NC_014774.1. DR AlphaFoldDB; E4UE18; -. DR STRING; 658172.CKC_05505; -. DR KEGG; lso:CKC_05505; -. DR eggNOG; COG0018; Bacteria. DR HOGENOM; CLU_006406_0_1_5; -. DR Proteomes; UP000007038; 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; Arginyl tRNA synthetase N-terminal domain; 1. DR Gene3D; 3.40.50.620; HUPs; 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 NCBIfam; TIGR00456; argS; 1. DR PANTHER; PTHR11956:SF5; ARGININE--TRNA LIGASE, CYTOPLASMIC; 1. DR PANTHER; PTHR11956; ARGINYL-TRNA SYNTHETASE; 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; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1. DR SUPFAM; SSF55190; Arginyl-tRNA synthetase (ArgRS), N-terminal 'additional' domain; 1. DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146, KW ECO:0000256|HAMAP-Rule:MF_00123}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00123}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00123}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00123}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00123}; KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP- KW Rule:MF_00123}. FT DOMAIN 19..93 FT /note="Arginyl tRNA synthetase N-terminal" FT /evidence="ECO:0000259|SMART:SM01016" FT DOMAIN 454..585 FT /note="DALR anticodon binding" FT /evidence="ECO:0000259|SMART:SM00836" FT MOTIF 130..140 FT /note="'HIGH' region" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00123" SQ SEQUENCE 586 AA; 67455 MW; 4F99421FF7CC7CA9 CRC64; MHLFTDFSSR MINYIKDIDF EKNIEKKYLD CIVVERPRNI MHGHLSTNAA MILSRPLSLD PITIAELIIA RIKMDPDVDF VSIGGKGFIN LYLSPSYLSK ILSFIVVSGI EYGRSLIGKG RKVNVEYVSA NPTGPMHVGH CRCAVVGDVL ANLMEFSGYE VTREYYINDA GAQIDTLAHS VFLRYQQVLD NNDFDLPEGF YPGAYLKAIG KELVDKYGSE LLNFYEEKWL PIVRDYAVKA MMEIIKDDLK ALNIRHDVFV SEKNFHRGDH SPIRDIIGDM GRKGYIYEGV LPAPKAKKNK TFDINCEQIL FRSTMVGDDI DRPLFKSDGS YTYFAADLAY FKYKYERGFD QMVYVMGSDH SGYVKRLEAV ASAVAGEKSK VNVLLCELVR LYRDGMPIKM SKRAGDFITL RYVVDEVGCD PVRFMMLWRK NSELLDFDFC KVKEQSKENP VFYVQYAYAR CRSIFRQAKD FFPDIDFDLF PQKALSQDFA WDIAELQLVM HLLEYPRIVE NATIFQEPYR LAFYLHDLAS VFHSHWSHGR ENPRLKFIQE DNRELTIMRL QLVYAVASVI NSGLNIIGVE SPHEMS //