ID SYR_PYRHO Reviewed; 629 AA. AC O59147; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 27-MAR-2024, entry version 140. DE RecName: Full=Arginine--tRNA ligase; DE EC=6.1.1.19; DE AltName: Full=Arginyl-tRNA synthetase; DE Short=ArgRS; GN Name=argS; OrderedLocusNames=PH1478; OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC OS 100139 / OT-3). OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Pyrococcus. OX NCBI_TaxID=70601; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3; RX PubMed=9679194; DOI=10.1093/dnares/5.2.55; RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S., RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K., RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T., RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T., RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.; RT "Complete sequence and gene organization of the genome of a hyper- RT thermophilic archaebacterium, Pyrococcus horikoshii OT3."; RL DNA Res. 5:55-76(1998). 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; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. CC {ECO:0000305}. 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; BA000001; BAA30585.1; -; Genomic_DNA. DR PIR; A71023; A71023. DR RefSeq; WP_010885558.1; NC_000961.1. DR PDB; 2ZUE; X-ray; 2.00 A; A=1-629. DR PDB; 2ZUF; X-ray; 2.30 A; A=1-629. DR PDBsum; 2ZUE; -. DR PDBsum; 2ZUF; -. DR AlphaFoldDB; O59147; -. DR SMR; O59147; -. DR STRING; 70601.gene:9378456; -. DR EnsemblBacteria; BAA30585; BAA30585; BAA30585. DR GeneID; 1443796; -. DR KEGG; pho:PH1478; -. DR eggNOG; arCOG00487; Archaea. DR OrthoDB; 372102at2157; -. DR BRENDA; 6.1.1.19; 5244. DR EvolutionaryTrace; O59147; -. DR Proteomes; UP000000752; 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; cd07956; Anticodon_Ia_Arg; 1. 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-RELATED; 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; 2. 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 1: Evidence at protein level; KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; KW Nucleotide-binding; Protein biosynthesis. FT CHAIN 1..629 FT /note="Arginine--tRNA ligase" FT /id="PRO_0000151653" FT MOTIF 128..138 FT /note="'HIGH' region" FT HELIX 6..20 FT /evidence="ECO:0007829|PDB:2ZUE" FT HELIX 36..38 FT /evidence="ECO:0007829|PDB:2ZUE" FT STRAND 40..43 FT /evidence="ECO:0007829|PDB:2ZUE" FT HELIX 45..53 FT /evidence="ECO:0007829|PDB:2ZUE" FT HELIX 57..68 FT /evidence="ECO:0007829|PDB:2ZUE" FT STRAND 76..82 FT /evidence="ECO:0007829|PDB:2ZUE" FT STRAND 85..90 FT /evidence="ECO:0007829|PDB:2ZUE" FT HELIX 92..106 FT /evidence="ECO:0007829|PDB:2ZUE" FT HELIX 107..109 FT /evidence="ECO:0007829|PDB:2ZUE" FT TURN 115..118 FT /evidence="ECO:0007829|PDB:2ZUE" FT STRAND 120..124 FT /evidence="ECO:0007829|PDB:2ZUE" FT HELIX 136..154 FT /evidence="ECO:0007829|PDB:2ZUE" FT STRAND 158..165 FT /evidence="ECO:0007829|PDB:2ZUE" FT HELIX 170..181 FT /evidence="ECO:0007829|PDB:2ZUE" FT HELIX 183..196 FT /evidence="ECO:0007829|PDB:2ZUE" FT HELIX 203..220 FT /evidence="ECO:0007829|PDB:2ZUE" FT HELIX 222..224 FT /evidence="ECO:0007829|PDB:2ZUE" FT HELIX 225..237 FT /evidence="ECO:0007829|PDB:2ZUE" FT STRAND 238..240 FT /evidence="ECO:0007829|PDB:2ZUE" FT HELIX 243..260 FT /evidence="ECO:0007829|PDB:2ZUE" FT STRAND 265..269 FT /evidence="ECO:0007829|PDB:2ZUE" FT HELIX 270..275 FT /evidence="ECO:0007829|PDB:2ZUE" FT HELIX 278..287 FT /evidence="ECO:0007829|PDB:2ZUE" FT STRAND 296..298 FT /evidence="ECO:0007829|PDB:2ZUE" FT TURN 299..302 FT /evidence="ECO:0007829|PDB:2ZUE" FT STRAND 304..307 FT /evidence="ECO:0007829|PDB:2ZUE" FT TURN 309..311 FT /evidence="ECO:0007829|PDB:2ZUE" FT STRAND 313..316 FT /evidence="ECO:0007829|PDB:2ZUE" FT STRAND 319..323 FT /evidence="ECO:0007829|PDB:2ZUE" FT HELIX 331..342 FT /evidence="ECO:0007829|PDB:2ZUE" FT STRAND 351..354 FT /evidence="ECO:0007829|PDB:2ZUE" FT STRAND 356..358 FT /evidence="ECO:0007829|PDB:2ZUE" FT STRAND 360..362 FT /evidence="ECO:0007829|PDB:2ZUE" FT STRAND 377..384 FT /evidence="ECO:0007829|PDB:2ZUE" FT HELIX 385..387 FT /evidence="ECO:0007829|PDB:2ZUE" FT HELIX 388..400 FT /evidence="ECO:0007829|PDB:2ZUE" FT HELIX 404..408 FT /evidence="ECO:0007829|PDB:2ZUE" FT STRAND 410..415 FT /evidence="ECO:0007829|PDB:2ZUE" FT STRAND 418..420 FT /evidence="ECO:0007829|PDB:2ZUE" FT TURN 427..434 FT /evidence="ECO:0007829|PDB:2ZUE" FT HELIX 437..455 FT /evidence="ECO:0007829|PDB:2ZUE" FT HELIX 461..481 FT /evidence="ECO:0007829|PDB:2ZUE" FT HELIX 493..496 FT /evidence="ECO:0007829|PDB:2ZUE" FT STRAND 500..503 FT /evidence="ECO:0007829|PDB:2ZUE" FT HELIX 504..523 FT /evidence="ECO:0007829|PDB:2ZUE" FT HELIX 530..536 FT /evidence="ECO:0007829|PDB:2ZUE" FT HELIX 544..565 FT /evidence="ECO:0007829|PDB:2ZUE" FT HELIX 570..589 FT /evidence="ECO:0007829|PDB:2ZUE" FT HELIX 599..620 FT /evidence="ECO:0007829|PDB:2ZUE" SQ SEQUENCE 629 AA; 72340 MW; 34CE2D841DBAD48A CRC64; MLMEIRESVK ERIEEIIKEI APQWEGEIEL KETPDPKLGD FGTPIAFKLA KLLKRPPIEI AEKIVEKLKL NLPEGIKDVK AVNGYINVFI DYPHFARILI NDILAKGDRF GSSEIGKGKK VIVEHTSVNP TKPLHMGHAR NAILGDVMAR ILRFLGYEVE VQNYIDDLGI QFAQVYWGYL RLKEEFERIM NELRERGLKD NPIDHALGLL YVEVNRRLED NPELENEIRD IMKKLESGEL YGRKLAEEVV RAQMVTTYKL GVKYDLLVWE SDIVRRKLFE IALELLSKNE NFYIPSDGKY RGAFVMDLRK LFPDMKNPIL VLRRSDGTAT YTGKDIAYHL WKFGKIDVDL LYKEWDSTTW TTAPDGKSMP NKFGNANIVI NVIGAEQKHP QLAIKYALQL LGFEDAAANL YHLAYEHVER PEGKFSGRKG TWVGFTVDEV IQEAVKRARE LIEEKNPALS DEEKAEVAEK VGIGAIRYNL IKYSPDKKII FRWEDVLNFE GESAPYIQYA HARCSSILRK AEEEGIKVDP ETLFKNADFT KLSERERELV IMLSKFPRIV EQAGKDVKPH LIAWFANELA SLFNKFYMDH PVLKAEEGVR EARLLLVMAV EQVLKNALYL MGIEAPERM //