ID SYL_ANAVT Reviewed; 872 AA. AC Q3M3A3; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2005, sequence version 1. DT 16-JUN-2009, entry version 35. DE RecName: Full=Leucyl-tRNA synthetase; DE EC=6.1.1.4; DE AltName: Full=Leucine--tRNA ligase; DE Short=LeuRS; GN Name=leuS; OrderedLocusNames=Ava_4936; 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-leucine + tRNA(Leu) = AMP + CC diphosphate + L-leucyl-tRNA(Leu). 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; ABA24533.1; -; Genomic_DNA. DR RefSeq; YP_325428.1; -. DR GeneID; 3679123; -. DR GenomeReviews; CP000117_GR; Ava_4936. DR KEGG; ava:Ava_4936; -. DR NMPDR; fig|240292.3.peg.3656; -. DR HOGENOM; Q3M3A3; -. DR OMA; Q3M3A3; MMFASPP. DR BioCyc; AVAR240292:AVA_4936-MON; -. 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 1 872 Leucyl-tRNA synthetase. FT /FTId=PRO_1000009289. FT MOTIF 42 52 "HIGH" region. FT MOTIF 634 638 "KMSKS" region. FT BINDING 637 637 ATP (By similarity). SQ SEQUENCE 872 AA; 98513 MW; 20AB279E2EC4045C CRC64; MDSRYNPAIL EEKWQKTWVE LGLDKTQTQS NKPKFYALSM FPYPSGSLHM GHVRNYTITD VIARLKRMQG YRVLHPMGWD AFGLPAENAA IDRGVPPANW TYQNITQMRQ QLQRLGLSID WDSEVATCSP DYYKWTQWIF LQFLQAGLAY QKEAAVNWDP IDQTVLANEQ VDNEGRSWRS GAIVERKLLR QWFLKITDYA EELLNDLDKL TGWPERVKLM QANWIGKSVG AYLEFPIVGS TEKIAVYTTR PDTVYGVSYV VLAPEHPLTK QVTSKTQQAV VDTFIQEVTN QSELERTAED KPKRGVATGG KAINPFTGEE VPIWIADYVL YEYGTGAVMG VPAHDVRDFK FAQRYDLPID FVIAAPDDVA GFDLSPTSET EEVTQVVQIE YNQAYTEPGI LINSGAFTGM TSTDAKQAIV KYATEKGFGK ERIQYRLRDW LISRQRYWGA PIPVIHCPNC GIVPVPDKDL PVILPEEVEF TGRGGSPLAQ LESWVNVPCP TCGSPAKRET DTMDTFIDSS WYFLRFTDAR NEAQVFESAK TNDWMPVDQY VGGIEHAILH LLYSRFFTKV LRDRGLLNFD EPFERLLTQG MVQGLTYFNP NKGGKDKWVP SHLVNPNDPR DPQTGEPLQR LYATMSKSKG NGVAPEDVIA KYGVDTARMF ILFKAPPEKD LEWDEADVEG QFRFLNRVWR LVTDYVASGV NPKNKSGELS KSEKDLRRAI HSAIQSVTED LEDEYQFNTA ISELMKLSNA LTDANGKDSR VYAEGIHTLV VLLAPFAPHI AEELWQLLGN SESVHTQTWP AFDPAALVAD EITLVIQVNG KKRADIQVPS QADKAELEKY ARESEVVQRH LEGKEIKKVI VVPGKLVNFV VG //