ID SYL1_SULAC Reviewed; 942 AA. AC Q4JBP0; DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot. DT 02-AUG-2005, sequence version 1. DT 16-JUN-2009, entry version 26. 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=Saci_0373; OS Sulfolobus acidocaldarius. OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Sulfolobus. OX NCBI_TaxID=2285; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33909 / DSM 639 / IFO 15157 / JCM 8929 / NCIB 11770; RX PubMed=15995215; DOI=10.1128/JB.187.14.4992-4999.2005; RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E., RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.; RT "The genome of Sulfolobus acidocaldarius, a model organism of the RT Crenarchaeota."; RL J. Bacteriol. 187:4992-4999(2005). 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; CP000077; AAY79789.1; -; Genomic_DNA. DR RefSeq; YP_255082.1; -. DR GeneID; 3473317; -. DR GenomeReviews; CP000077_GR; Saci_0373. DR KEGG; sai:Saci_0373; -. DR NMPDR; fig|330779.3.peg.1304; -. DR HOGENOM; Q4JBP0; -. DR OMA; Q4JBP0; HGRTYIT. DR BioCyc; SACI330779:SACI_0373-MON; -. DR BRENDA; 6.1.1.4; 434. 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; IPR015413; aa-tRNA-synt_I. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. 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 Pfam; PF08264; Anticodon_1; 1. DR Pfam; PF09334; tRNA-synt_1g; 2. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; FALSE_NEG. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Protein biosynthesis. FT CHAIN 1 942 Leucyl-tRNA synthetase 1. FT /FTId=PRO_0000152142. FT MOTIF 39 49 "HIGH" region. FT MOTIF 624 628 "KMSKS" region. FT BINDING 627 627 ATP (By similarity). SQ SEQUENCE 942 AA; 108215 MW; C62D780A5A6C432F CRC64; MDFLNEIASK WQKVWDSERV YEADVDRTKE KKFITVAFPY TNSPLHIGHG RTYITADIYA RYLRMKGYNV LFPFAFQFTG TPILSIADAV KRGDEEIIST FTNVYQIPIG VISKFSDPSY LSAYFKEDMR NTALTLGLSI DRRREFTTID PAFERFVQWQ YKRLQEIGYI KKEKAPVAYC PVDEFPVGMH DTRGDIEPEI IDLDVIYFQG EKLLFLTATS RPETIFGAVA ILINPDSDYS IVVDNKNGKR LVMSTEAFKK LSFQMSLTEE ERKKGGELIG LNVTNPVTLK KLTVLPSKYV ESKQGTGVVM AVPAHEPLHY LALSELKESF EIVPVIKSED YGDFPAMEVL ETAQTTSAQE LKDYIDTLYR IEFHKGSIRD EVVDLVPDYM KQFVGERIAG KSVREARSSV VELLRNLGVH GNIYEIINGP VYCRCGAEVV VKVFDDQWFI DYSNSTWKSS VLKSLDKIEI LPQDAKREIS KIIFNMKPRP FTRSRGLGVR LPWDDRQIID SLSDSTIYTV FYIVANKVKS YPTSILNERF WDYVVLGRGD SSQLSRELGI PKEQLEELRM EVEYWYPVDS RHSGRDLVQN HIPYYLYHHV GVLGEDKVPK RIVLNGFIRV GGKKMSKSFG NVYPLNKAIR EYGVDTVRLA LTSTSSLSDD IEFSPNIAKS IGEQLKHIHD FIENLIKLQS VNEIRKVDLW ISSLISEYID LIDNCLSNLD LRTAYKTIYY DIYEDLKDYL ELGNGKINSD IIKNVISVWI RLMAPFTPHL AEELWHKLDN SLVVRQRFPS KGELQYDKRA LLEIEYLRYT IDLINSMKSK MSKEPETVII YVNEDNTQRD LIRKAIESLK ERKSLPDFEK EVGDREMARL AYEIAGDLPD KIKNLAEIGI NESEILTSNA QFLLNKLDVK EIYIYNSKDP STPDIKGKKS IALPYKPGII LT //