ID D7DWT7_NOSA0 Unreviewed; 585 AA. AC D7DWT7; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 27-MAR-2024, entry version 68. 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=Aazo_2060 {ECO:0000313|EMBL:ADI64110.1}; OS Nostoc azollae (strain 0708) (Anabaena azollae (strain 0708)). OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; OC Trichormus. OX NCBI_TaxID=551115 {ECO:0000313|EMBL:ADI64110.1, ECO:0000313|Proteomes:UP000001511}; RN [1] {ECO:0000313|EMBL:ADI64110.1, ECO:0000313|Proteomes:UP000001511} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=0708 {ECO:0000313|EMBL:ADI64110.1, RC ECO:0000313|Proteomes:UP000001511}; RX PubMed=20628610; DOI=10.1371/journal.pone.0011486; RA Ran L., Larsson J., Vigil-Stenman T., Nylander J.A., Ininbergs K., RA Zheng W.W., Lapidus A., Lowry S., Haselkorn R., Bergman B.; RT "Genome erosion in a nitrogen-fixing vertically transmitted endosymbiotic RT multicellular cyanobacterium."; RL PLoS ONE 5:E11486-E11486(2010). 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; CP002059; ADI64110.1; -; Genomic_DNA. DR RefSeq; WP_013191127.1; NC_014248.1. DR AlphaFoldDB; D7DWT7; -. DR STRING; 551115.Aazo_2060; -. DR KEGG; naz:Aazo_2060; -. DR eggNOG; COG0018; Bacteria. DR HOGENOM; CLU_006406_5_1_3; -. DR OrthoDB; 9805987at2; -. DR Proteomes; UP000001511; 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 {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}; Reference proteome {ECO:0000313|Proteomes:UP000001511}. FT DOMAIN 6..90 FT /note="Arginyl tRNA synthetase N-terminal" FT /evidence="ECO:0000259|SMART:SM01016" FT DOMAIN 468..585 FT /note="DALR anticodon binding" FT /evidence="ECO:0000259|SMART:SM00836" FT MOTIF 126..136 FT /note="'HIGH' region" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00123" SQ SEQUENCE 585 AA; 66005 MW; 26518DD0B34C7171 CRC64; MNATQEKLKL KLAQALVAAF GAEYTGVDPI LVTASNPKFG DFQANVALSL SKKLGMQARV IASAIVEKLD VSDICKPPEI AGPGFINLRL QTSYLESQLN AIKTDSRLGV PKTKNSQKEI VDFSSPNIAK EMHVGHLRST IIGDCIARIL EFHGHEVLRL NHVGDWGTQF GMLITYLREV YPEALTTANA LDIGDLVTFY RQAKQRFDAD ETFQETARQE VVRLQAGVED TLHAWKLLCE QSRREFQVIY DLLNVNLIER GESFYNPFLP AVVEDLEKTG LLEENQGAKC VFLDGFTNRE GEPLPLIIQK SDGGYNYATT DLACLRYRIE KDQAKRIIYV TDAGQANHFT QFMQLAKKAN WIPDDVELVH VPFGLVLGDN RKKFKTRSGD TVRLRDLLDE AVSRTRADLE ARLIEEGREE TEEFIKNVAE VVGISAVKYA DLSQNRTSNY VFSYDKMLAL KGNTAPYMLY AYVRTQGISR EGNIDFENLG TDTKILLKED AELTLAKDLL QLDEVISEVE QDLLPNRLCD YLYNLSDKFN KFYENCPVLK SEEPTRTSRL MLCDLTAKTL KLGLDLLGIK VLERM //