ID SYL1_RHIL3 Reviewed; 838 AA. AC Q1MFI6; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2006, sequence version 1. DT 16-JUN-2009, entry version 28. DE RecName: Full=Leucyl-tRNA synthetase 1; DE EC=6.1.1.4; DE AltName: Full=Leucine--tRNA ligase 1; DE Short=LeuRS 1; GN Name=leuS1; OrderedLocusNames=RL2798; OS Rhizobium leguminosarum bv. viciae (strain 3841). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=216596; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16640791; DOI=10.1186/gb-2006-7-4-r34; RA Young J.P.W., Crossman L.C., Johnston A.W.B., Thomson N.R., RA Ghazoui Z.F., Hull K.H., Wexler M., Curson A.R.J., Todd J.D., RA Poole P.S., Mauchline T.H., East A.K., Quail M.A., Churcher C., RA Arrowsmith C., Cherevach I., Chillingworth T., Clarke K., Cronin A., RA Davis P., Fraser A., Hance Z., Hauser H., Jagels K., Moule S., RA Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M., RA Whitehead S., Parkhill J.; RT "The genome of Rhizobium leguminosarum has recognizable core and RT accessory components."; RL Genome Biol. 7:RESEARCH34.1-RESEARCH34.20(2006). CC -!- CATALYTIC ACTIVITY: ATP + L-leucine + tRNA(Leu) = AMP + CC diphosphate + L-leucyl-tRNA(Leu). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). 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; AM236080; CAK08288.1; -; Genomic_DNA. DR RefSeq; YP_768383.1; -. DR GeneID; 4400999; -. DR GenomeReviews; AM236080_GR; RL2798. DR KEGG; rle:RL2798; -. DR NMPDR; fig|216596.1.peg.2894; -. DR HOGENOM; Q1MFI6; -. DR OMA; Q1MFI6; YYLRFID. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:HAMAP. DR GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:HAMAP. DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:HAMAP. DR HAMAP; MF_00049; -; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR002300; aa-tRNA-synth_Ia. DR InterPro; IPR002302; Leu-tRNA-synth_Ia_bac/mito. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR013155; V/L/I-tRNA-synth_anticodon-bd. DR Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1. DR PANTHER; PTHR11946:SF7; Leu_tRNAsyn_1a; 1. DR Pfam; PF08264; Anticodon_1; 1. DR Pfam; PF00133; tRNA-synt_1; 1. DR PRINTS; PR00985; TRNASYNTHLEU. DR TIGRFAMs; TIGR00396; leuS_bact; 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 1 838 Leucyl-tRNA synthetase 1. FT /FTId=PRO_0000334802. FT MOTIF 40 51 "HIGH" region. FT MOTIF 608 612 "KMSKS" region. FT BINDING 611 611 ATP (By similarity). SQ SEQUENCE 838 AA; 94069 MW; 7C2AC9CEACE16F9F CRC64; MPYDPTKIEP KWQAYWAGHH IFRVEIDPAR PKFYALDMFP YPSGAGLHVG HPLGYTATDI MCRYKRMRGF NVLHPMGWDS FGLPAERHAM RTGVHPDITT KRNIETFRGQ VQRLGFSYDW SREFATTDPA YVRWTQWIFL KLFENGLAYQ AEVAVNWCPA QNAVLADEEV KDGRYVETGD PVIRRRMRQW MLRITAYADR LLQGLDGLDW PENLKAMQRN WIGRSEGAEI RFPLEHGKGV ITVFTTRPET LFGASYILLA PEHPAVAAIV EPEMSEAVAA YIAEAEGLEE TVRADAGREK TGVFTGAYAI NPANGARLPV WVADYVLAGY GTGALMAVPA HDARDYAFAH SHELPIIRVI DSEADIEKGA YEGEGAMVNS GFLSGLGSPE ARSAIVAWLQ ANGTGWPKVM YRLRDWLFSR QRYWGEPIPV LHLADGSVMP LPEECLPLLP PELDDYAPTP DGEPPLARAQ AWVETIVPGT DIPARRETNT MPQWAGSCWY YLRFLDPENT SEPVGREAER YWMPVDLYVG GAEHAVLHLL YARFWHKVLY DIGVVSTEEP FQRLFNQGMI LAHSYRDAAG RYYAPSSVVE EEGRWFAGSV EVQRAVEKMS KSQLNVVNPD DVVHQFGADA LRLYEMFMGP LDAAKPWQTA GVIGVRRFLE RAWRIVCDES DGLSPVVLEA APSPQLLRLR HQTVKTVTAD IEAIRFNTAV SRLMELANAL TAEAARPREV VETFVLLLAP FAPHIAEELW SKLGHGETLT WVSWPTFDPA LIEMETREYV VQINGKVRHR FEAAADLGEA LLAAARSEPS VMALLDGKTV VKEVLVPGRL VNFVVEDL //