SYL_NOCFA
ID SYL_NOCFA Reviewed; 950 AA.
AC Q5YN65;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=NFA_55240;
OS Nocardia farcinica (strain IFM 10152).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia.
OX NCBI_TaxID=247156;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFM 10152;
RX PubMed=15466710; DOI=10.1073/pnas.0406410101;
RA Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K.,
RA Shiba T., Hattori M.;
RT "The complete genomic sequence of Nocardia farcinica IFM 10152.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004).
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; AP006618; BAD60376.1; -; Genomic_DNA.
DR RefSeq; WP_011212058.1; NC_006361.1.
DR AlphaFoldDB; Q5YN65; -.
DR SMR; Q5YN65; -.
DR STRING; 247156.NFA_55240; -.
DR PRIDE; Q5YN65; -.
DR EnsemblBacteria; BAD60376; BAD60376; NFA_55240.
DR GeneID; 61136093; -.
DR KEGG; nfa:NFA_55240; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_11; -.
DR OMA; TFMVLAP; -.
DR BioCyc; NFAR247156:NFA_RS27430-MON; -.
DR Proteomes; UP000006820; 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; -; 3.
DR Gene3D; 3.90.740.10; -; 1.
DR HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
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; 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..950
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000152056"
FT MOTIF 66..77
FT /note="'HIGH' region"
FT MOTIF 721..725
FT /note="'KMSKS' region"
FT BINDING 724
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 950 AA; 105624 MW; 2F6FF32904598B35 CRC64;
MQDTRATESD VPEHRYNAAL AGRIERRWQQ RWLERGTFHA PNPTGPLAGP TATLPADKLF
VQDMFPYPSG AGLHVGHPLG YIATDVFARY HRMRGRNVLH ALGYDAFGLP AEQYAVQTGA
HPRDTTESNI ATMQRQLDRL GLGHDRRRSF ATTDPEYYRW TQWIFLQIYN AWYDLELNRA
RPISELEEQF ASGARPAPDG KDWASMSQAE RAAVIDSYRL VYQTDSMVNW CPGLGTVLSN
EEVTAEGRSE RGNFPVFRKR LWQWMMRITA YADRLVDDLD LLDWPENVKA MQRNWIGRSR
GAQVRFDSPA GQIEVFTTRP DTLFGATYVV LAPEHDLVDA LAAAQWPADT DPRWTGGAAT
PAEAVAQYRK SIAAKSDLER QENKEKTGVF LGVHAVNPVN GARVPIFIAD YVLSGYGTGA
IMAVPGHDQR DWEFATAFGL PIVEVISGGD ITAAAHTGEG ELVNSDYLNG LSVEEAKATV
IGRLEADGHG TGTIQYKLRD WLFARQRYWG EPFPIVYDED GAPHALPESM LPVRLPELDD
FAPVTFDPDD ADSEPSPPLA KATDWVHVEL DLGDGPKKYR RDTNVMPNWA GSSWYQLRYA
DPTNADAFCA KENEQYWLGP RTAEHGPDDP GGVDLYVGGV EHAVLHLLYA RFWQKVLFDL
GYVSSSEPYR RLFNQGYIQA FAYTDPRGAY VPAAEVVERD GAFFWTDATG TEIEVSQEYG
KIGKSLKNAI SPDEVCDQFG ADTFRFYEMS MGPLDTSRPW STKDVVGAHR FLQRVWRLVV
DEETGASRVT EDAPTDETLR FLHRTIAGVD EDFAALRDNT AGAKLIELTN HLTKSYPSGT
PRAAVEPLVL MLAPLAPHVA EELWERLGHS ESLAHGPFPV ADPAWLVEET VEYPIQVNGK
VRSRIQVPAD ADNAAIEAAA LADEKIAALL AGATPRKLIV VPGRLVNIVA
