ID J9G2V5_9ZZZZ Unreviewed; 944 AA.
AC J9G2V5;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=leucine--tRNA ligase {ECO:0000256|ARBA:ARBA00013164};
DE EC=6.1.1.4 {ECO:0000256|ARBA:ARBA00013164};
DE AltName: Full=Leucyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030520};
GN ORFNames=EVA_15764 {ECO:0000313|EMBL:EJW96132.1};
OS gut metagenome.
OC unclassified sequences; metagenomes; organismal metagenomes.
OX NCBI_TaxID=749906 {ECO:0000313|EMBL:EJW96132.1};
RN [1] {ECO:0000313|EMBL:EJW96132.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23251564; DOI=10.1371/journal.pone.0051521;
RA Alcaide M., Messina E., Richter M., Bargiela R., Peplies J., Huws S.A.,
RA Newbold C.J., Golyshin P.N., Simon M.A., Lopez G., Yakimov M.M., Ferrer M.;
RT "Gene sets for utilization of primary and secondary nutrition supplies in
RT the distal gut of endangered iberian lynx.";
RL PLoS ONE 7:E51521-E51521(2012).
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:0000256|ARBA:ARBA00001372};
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJW96132.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AMCI01005442; EJW96132.1; -; Genomic_DNA.
DR AlphaFoldDB; J9G2V5; -.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR Gene3D; 3.40.50.620; HUPs; 3.
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 NCBIfam; TIGR00396; leuS_bact; 1.
DR PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 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; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EJW96132.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 35..163
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 276..437
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 795..908
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 944 AA; 108357 MW; 9D234C8EE1D054E8 CRC64;
MEYNFREIEK KWQKRWVENK TYQVTEDESK QKFYVLNMFP YPSGAGLHVG HPLGYIASDI
YARYKRLQGF NVLNPMGYDA YGLPAEQYAI QTGQHPAITT VNNINRYREQ LDKIGFSFDW
NREIRTCDPE YYHWTQWAFQ KMFGSYYCNE RQQARPISEL VAHFETNGSA NLNVACSEEL
QFTADEWKAM NEKEQQEVLM NYRIAYLGET MVNWCAELGT VLANDEVVDG VSERGGYPVV
QKKMRQWCLR VSAYAQRLLD GLDRIDWTDS LKETQKNWIG RSEGTEVLFK VKDSDLEFTI
FTTRADTMFG VTFMVLAPES ELVAQFTTPE QKAEVDAYLE RTKKRTERER ISDRSVTGVF
SGSYGINPFT GEAVPIWISD YVLAGYGTGA IMAVPAHDSR DYAFAKHFGL EIRPLVEGCD
VSEESFDAKE GIVCNSPREG AAPYCDLNLN GLTIKEAIAA TKKYVKEHQL GRVKVNYRLR
DAIFSRQRYW GEPFPVYYKD GMPYMIDESC LPLELPEVAK FLPTETGEPP LGHATKWAWD
TVNRCVVENE KIDNETIFPL ELNTMPGFAG SSAYYLRYMD PRNHEALVGE KADQYWKNVD
LYVGGTEHAT GHLIYSRFWN KFLFDMGVSC SEEPFQKLVN QGMIQGRSNF VYRIKDTNTF
VSLNLKDQYD VTPLHVDVNI VSNDILDVEA FKAWRPEFQT AEFILEDGKY VCGWAVEKMS
KSMFNVVNPD TIVEKYGADT LRMYEMFLGP VEQSKPWDTN GIDGVHRFIR KFWSLFYSRT
GEYLVKDEPA TKNELKSLHK LIKKVSGDIE QFSYNTSVSA FMICVNELSG LKCNKKEVLE
GLIVLLAPFI PHVCEELWSI LGHDTSVCDA QWPAYNEDYL KEDTINYTIS FNGKARFNME
FAADATSEAI QAAVLADERS QKWVEGKTPK KIIVVPKKIV NIVI
//
