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