ID SYR_NITOC Reviewed; 585 AA. AC Q3JF27; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 08-NOV-2005, sequence version 1. DT 27-MAR-2024, entry version 98. 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=Noc_0027; OS Nitrosococcus oceani (strain ATCC 19707 / BCRC 17464 / JCM 30415 / NCIMB OS 11848 / C-107). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae; OC Nitrosococcus. OX NCBI_TaxID=323261; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19707 / BCRC 17464 / JCM 30415 / NCIMB 11848 / C-107; RX PubMed=16957257; DOI=10.1128/aem.00463-06; RA Klotz M.G., Arp D.J., Chain P.S.G., El-Sheikh A.F., Hauser L.J., RA Hommes N.G., Larimer F.W., Malfatti S.A., Norton J.M., Poret-Peterson A.T., RA Vergez L.M., Ward B.B.; RT "Complete genome sequence of the marine, chemolithoautotrophic, ammonia- RT oxidizing bacterium Nitrosococcus oceani ATCC 19707."; RL Appl. Environ. Microbiol. 72:6299-6315(2006). 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}. 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; CP000127; ABA56569.1; -; Genomic_DNA. DR RefSeq; WP_002813322.1; NC_007484.1. DR AlphaFoldDB; Q3JF27; -. DR SMR; Q3JF27; -. DR STRING; 323261.Noc_0027; -. DR KEGG; noc:Noc_0027; -. DR eggNOG; COG0018; Bacteria. DR HOGENOM; CLU_006406_0_1_6; -. DR InParanoid; Q3JF27; -. DR Proteomes; UP000006838; 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-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; 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; ATP-binding; Cytoplasm; Ligase; KW Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1..585 FT /note="Arginine--tRNA ligase" FT /id="PRO_0000242056" FT MOTIF 128..138 FT /note="'HIGH' region" SQ SEQUENCE 585 AA; 65983 MW; 4B807D572FD85B94 CRC64; MKEHLWNLIA DALSSLQQEG ILSSWNKDKI QVQRTRDKSH GDFASNISMV LAKEARQKPQ KLADLIVARL PEHPWVKKVD IAGPGFINFT LALPAFQAVV SQVLEQKESF GRCRTGHGKT VHLEFVSANP TGPLHVGHGR GAAYGDALAR LLTAVGYQVH REYYVNDAGR QMDILAVSVW LRYLELCGET LPFPSNGYQG EYVRNIARSL KAGEEDLPHH SATEILAGLP ADAPTGDREK YLDALIQKIK NLLGKNSYQK VFEQALNTIL AGIREDLAKF GVTYDAWFSE RHLTEMGAIE IAIERLKAAG HLYQKAGAWW FYATNFGDEK DRVVIRENGQ PTYFASDIAY HLSKLEQGYH KIIDIWGADH HGYIPRIKAS LQALGADLQQ LDIQLVQFAI LYRGKEKIQM STRSGEFVTL RELCQEVGKD AARFFYVMRG AEQHMDFDLE LAKSQSNENP VYYVQYAHAR ICSVFRQLKT REFVWNSEQG REHLGKLNEA HEVTLLDRLS CYSEVVESAA IQSAPHLLAY YLLDLARDFH TYYNAHTFLV DIPELRDARL ALIAATRQVI KNGLTLLGVS APESM //