ID SYR_ANAVT Reviewed; 588 AA. AC Q3M769; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2005, sequence version 1. DT 16-JUN-2009, entry version 24. DE RecName: Full=Arginyl-tRNA synthetase; DE EC=6.1.1.19; DE AltName: Full=Arginine--tRNA ligase; DE Short=ArgRS; GN Name=argS; OrderedLocusNames=Ava_3561; OS Anabaena variabilis (strain ATCC 29413 / PCC 7937). OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena. OX NCBI_TaxID=240292; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., RA Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.; RT "Complete sequence of Anabaena variabilis ATCC 29413."; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + L-arginine + tRNA(Arg) = AMP + CC diphosphate + L-arginyl-tRNA(Arg). CC -!- SUBUNIT: Monomer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000117; ABA23167.1; -; Genomic_DNA. DR RefSeq; YP_324062.1; -. DR GeneID; 3679585; -. DR GenomeReviews; CP000117_GR; Ava_3561. DR KEGG; ava:Ava_3561; -. DR NMPDR; fig|240292.3.peg.4445; -. DR HOGENOM; Q3M769; -. DR OMA; Q3M769; HMGFGTM. DR BioCyc; AVAR240292:AVA_3561-MON; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:HAMAP. DR GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:HAMAP. DR HAMAP; MF_00123; -; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR001278; Arg-tRNA-synth_Ic. DR InterPro; IPR015945; Arg-tRNA-synth_Ic_core. DR InterPro; IPR005148; Arg-tRNA-synth_Ic_N. DR InterPro; IPR008909; DALR_anticod_bd. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Gene3D; G3DSA:3.30.1360.70; Arg-tRNA-synth_Ic_N; 1. DR Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1. DR PANTHER; PTHR11956; Arg_tRNA-synt_1c; 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 TIGRFAMs; TIGR00456; argS; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Protein biosynthesis. FT CHAIN 1 588 Arginyl-tRNA synthetase. FT /FTId=PRO_0000241974. FT MOTIF 126 136 "HIGH" region. SQ SEQUENCE 588 AA; 65554 MW; 5CB9FB06D47521AD CRC64; MNATQEQLKV KLEQALIAAF GDEYAGVDPI LVTASNPKFG DYQANVALSL SKKLGQPPRA IASAIVEKLD VSEICETPEI AGPGFINLKL KTAYLEAQLN AIQADSRLGV PTAKHPQREI VDFSSPNIAK EMHVGHLRST IIGDSIARIL EFRGHDVLRL NHVGDWGTQF GMLITYLREV SPEALTTANA LDIGDLVSFY RQAKQRFDAD EAFQETARQE VVRLQAGATD TLHAWKLLCE QSRQEFQVIY DLLDVKLTER GESFYNPLLP TVVEGLEASG LLVENQGAKC VFLDGFTNRE GEPLPLIVQK SDGGYNYATT DLAALRYRIQ KDEAKRIVYV TDAGQANHFA QFFQVARKAG WIPNDVELVH VPFGLVLGED GKKFKTRSGD TVRLRDLLDE AVSRAHADLE ERLKAEEREE TPEFIDKVAE VVGISAVKYA DLSQNRTSNY IFSYDKMLDL KGNTAPYMLY AYARIQGISR KGGINFADLG DNAKVILQHD TEFALAKYLL QLGEVISTVE ADLLPNRLCE YLYELSKKFN TFYDRNQGVQ VLSAEEPLRT SRLVLCDLTA RTLKLGLSLL GIQVLERM //