ID SYR_PSEA6 Reviewed; 578 AA. AC Q15W53; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 25-JUL-2006, sequence version 1. DT 27-MAR-2024, entry version 118. 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=Patl_1359; OS Pseudoalteromonas atlantica (strain T6c / ATCC BAA-1087). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Paraglaciecola. OX NCBI_TaxID=3042615; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=T6c / ATCC BAA-1087; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Karls A.C., RA Bartlett D., Higgins B.P., Richardson P.; RT "Complete sequence of Pseudoalteromonas atlantica T6c."; RL Submitted (JUN-2006) 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}. 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; CP000388; ABG39885.1; -; Genomic_DNA. DR RefSeq; WP_011574204.1; NC_008228.1. DR AlphaFoldDB; Q15W53; -. DR SMR; Q15W53; -. DR STRING; 342610.Patl_1359; -. DR KEGG; pat:Patl_1359; -. DR eggNOG; COG0018; Bacteria. DR HOGENOM; CLU_006406_5_1_6; -. DR OrthoDB; 9803211at2; -. DR Proteomes; UP000001981; 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; 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. FT CHAIN 1..578 FT /note="Arginine--tRNA ligase" FT /id="PRO_1000018089" FT MOTIF 122..132 FT /note="'HIGH' region" SQ SEQUENCE 578 AA; 64162 MW; 2AFFA4EDD86E2300 CRC64; MNLHTLLLNK FRTALVAIGA PENSPAPLSR ATKVGFGDYQ FNGAMALAKV LKQKPRDIAE KIVEAVELDG IAEKLEVAGP GFINIYLSKE WLAAQLSHAA ADPRLNIESQ PTKTVVVDYS SPNLAKEMHV GHLRTTIIGD AVVKALEFMG HKVIRQNHMG DWGTQFGMLL AHLNDKLESN QVAETALSDL EDFYREAKVR FDEEEGFADR AREYVVKLQG GDSHCLALWQ NFIDVSITHS EEVYHKLNVS LTRDDIMGES AYNHDLANVV SELQAKGLAV ESQGAQVVFL PELADKEGNP AAYIVQKSGG GYLYATTDLA AIRHRNKQLH ADRTLILTDA RQALHFKQTE LVARKAGFIE PEQTYEHCPF GMMLGNDGRP FKTRTGGTVK LVELLDEAVE RAETLLSKRE TDLSSDELKV LANKIGIGAV KYADLSKNRT TDYMFSWDSM LSFEGNTAPY LQYAYTRVMS IFRKAGVDHQ TLNAPISLDA PQEKILAVKQ LQYVEAINQV IAEGTPHVLC TYLYELASLF MSFYEACPML KDGIEQDVRD SRMTLAALTA KTLQSGLSLL GIDTMERM //