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SYL_FERNB
ID   SYL_FERNB               Reviewed;         819 AA.
AC   A7HN82;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Leucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00049};
DE            EC=6.1.1.4 {ECO:0000255|HAMAP-Rule:MF_00049};
DE   AltName: Full=Leucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00049};
DE            Short=LeuRS {ECO:0000255|HAMAP-Rule:MF_00049};
GN   Name=leuS {ECO:0000255|HAMAP-Rule:MF_00049}; OrderedLocusNames=Fnod_1522;
OS   Fervidobacterium nodosum (strain ATCC 35602 / DSM 5306 / Rt17-B1).
OC   Bacteria; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC   Fervidobacterium.
OX   NCBI_TaxID=381764;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35602 / DSM 5306 / Rt17-B1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT   "Complete sequence of Fervidobacterium nodosum Rt17-B1.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-
CC         tRNA(Leu); Xref=Rhea:RHEA:11688, Rhea:RHEA-COMP:9613, Rhea:RHEA-
CC         COMP:9622, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57427,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78494, ChEBI:CHEBI:456215; EC=6.1.1.4;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00049};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00049}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00049}.
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DR   EMBL; CP000771; ABS61365.1; -; Genomic_DNA.
DR   RefSeq; WP_011994670.1; NC_009718.1.
DR   AlphaFoldDB; A7HN82; -.
DR   SMR; A7HN82; -.
DR   STRING; 381764.Fnod_1522; -.
DR   PRIDE; A7HN82; -.
DR   EnsemblBacteria; ABS61365; ABS61365; Fnod_1522.
DR   KEGG; fno:Fnod_1522; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_0; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000002415; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.620; -; 2.
DR   HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR002302; Leu-tRNA-ligase.
DR   InterPro; IPR025709; Leu_tRNA-synth_edit.
DR   InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR   InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR   PANTHER; PTHR43740; PTHR43740; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   Pfam; PF13603; tRNA-synt_1_2; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 1.
DR   PRINTS; PR00985; TRNASYNTHLEU.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF50677; SSF50677; 1.
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; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..819
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000071110"
FT   MOTIF           41..51
FT                   /note="'HIGH' region"
FT   MOTIF           578..582
FT                   /note="'KMSKS' region"
FT   BINDING         581
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   819 AA;  94678 MW;  FB35036960663EDB CRC64;
     MKEYKPQEIE SKWQGVWSEK KVFETPQYSD KKKYYALVMF PYPSGTLHVG HVKNYVIGDI
     VARYKRMQGY NVLHPFGYDA FGLPAENAAI AHKIHPKKWT LDNINVIRGQ IKKIGISYDW
     NREVITCTED YYKWTQWVFL KLYEAGLAYK KPGAVNWCPS CQTVLANEQV KDGKCERCGT
     TVTMKYLEQW YFKITDYAEK LLEGLDRLPG WPEHVKTMQR NWIGKSTGAE VDFPVDGMDR
     KIRIFTTRPD TIYGVTFMAI APESPLVMEL VTEDKKKEVE EFLAKVALED RFKRTSVEAK
     KEGVFLGRYA INPLTNEKIP IYVANYILYE YGTGAIMAVP AHDQRDYDFA KTYNLPIKQV
     IKPKDGEWNI NERPYEEEGI MINSGPFDGL ESSKGIEEVT KYIEEKGFGK KSVQYKLRDW
     LISRQRYWGA PIPIVYCEKC GIVPVPEKDL PVRLPENVEF LPTGQSPLTL SEEFKHTTCP
     KCGGPAHREV ETMDTFVDSS WYFLRYVNPK LDDKPFESDD VNYWLPVDQY IGGVEHAVLH
     LLYSRFITKV LHDLGYLKFD EPFENLFTQG MIYKDGWKMS KSKGNVVSPD DMINKYGADT
     LRMYILFMAP PEKDAEWNDA GIDGVNRFIK RLWNNYYKIL DIINSNDTKN ENEFGKEEKN
     LRRKLHAMIK KIKEDIEGGF KFNTAIAGLM EFNNQLSDYL ENTKSPNKKL LREIAEKVVL
     ILSPFAPHMA EEMWHDLGKE TLIVEEKWPE YDPEALKEDE LTIVVQVNGK VRGKITVPAD
     ASEEEIKNRA VENAGKFLEG KTIVNTIYVK GKLVNIVIK
 
 
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