ID SYR_SULAC Reviewed; 618 AA. AC Q4J904; DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot. DT 02-AUG-2005, sequence version 1. DT 27-MAR-2024, entry version 96. 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}; GN OrderedLocusNames=Saci_1396; OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC OS 15157 / NCIMB 11770). OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Sulfolobus. OX NCBI_TaxID=330779; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770; RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005; RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E., RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.; RT "The genome of Sulfolobus acidocaldarius, a model organism of the RT Crenarchaeota."; RL J. Bacteriol. 187:4992-4999(2005). 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 -!- 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}. 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; CP000077; AAY80726.1; -; Genomic_DNA. DR RefSeq; WP_011278228.1; NZ_CP046615.1. DR AlphaFoldDB; Q4J904; -. DR SMR; Q4J904; -. DR STRING; 330779.Saci_1396; -. DR GeneID; 78441741; -. DR KEGG; sai:Saci_1396; -. DR PATRIC; fig|330779.12.peg.1345; -. DR eggNOG; arCOG00487; Archaea. DR HOGENOM; CLU_006406_6_1_2; -. DR Proteomes; UP000001018; 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 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; IPR001278; Arg-tRNA-ligase. 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-RELATED; 1. DR PANTHER; PTHR11956; ARGINYL-TRNA SYNTHETASE; 1. DR Pfam; PF05746; DALR_1; 1. DR Pfam; PF00750; tRNA-synt_1d; 2. DR PRINTS; PR01038; TRNASYNTHARG. 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. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; KW Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1..618 FT /note="Arginine--tRNA ligase" FT /id="PRO_0000151655" FT MOTIF 113..123 FT /note="'HIGH' region" SQ SEQUENCE 618 AA; 71087 MW; 11C9ACB100739ABA CRC64; MNPIRSVKEE FCEIVANGLG ISKDVIFKTL EYPPREELGD ISLPLPSLKL NVRTEVTFSH GKLIKEVRKT GIYVNAFVDE KELFKLLFTE MQDDYGVEKT ENPKRIVVEH TSANPIHPLH IGHLRNSILG DTISRMLKIR GHDVNRRFYV NDAGRQVAIL TLGYILLGEP EPSPKVDHWF GLIYSITNVI IEIRELKEEL KKDLDPDTYK DKINRLDELV ATAQSLRERN PEFFDKLADA INSIPDVESE IQKIIKSYEK GDDPKIKQIV RKIVNLNLDG FRESLDKLEI SFDVYDYESE LLWSGMVDEI LSKAFQIAKD YKGTKALELE DINEKIKEIL NIPKGLKLPP LVLTRSDGTS LYTTRDIAYT VKKFSDFKAD TVINVIAEQQ SIPQMQLRAS LYLLGYERLA QNLVHYSYGM VNLQGMRMSG RLGRFISLDD VIEKVSEVAK KKIEEKSGDI TNLRDIVNSA IRYAILSVAS NKPVTFNINN IVDFEQNSGP YLQYTYARAY NILAKNQDEI KLTDADLSDL IGDKRRLLLL IARFPETFNK AIDELRPEDL IDFLRRTADV FNRWYNFERV LQEPDYRKRI TRLFIVKGIE RVLYNGLNAL GIKPLSKM //