ID W1WF91_9ZZZZ Unreviewed; 806 AA.
AC W1WF91;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=Q604_UNBc4C00029G0027 {ECO:0000313|EMBL:ETJ16857.1};
OS human gut metagenome.
OC unclassified sequences; metagenomes; organismal metagenomes.
OX NCBI_TaxID=408170 {ECO:0000313|EMBL:ETJ16857.1};
RN [1] {ECO:0000313|EMBL:ETJ16857.1}
RP NUCLEOTIDE SEQUENCE.
RA Brown C.T., Sharon I., Thomas B.C., Castelle C.J., Morowitz M.J.,
RA Banfield J.F.;
RT "A Varibaculum cambriense genome reconstructed from a premature infant gut
RT community with otherwise low bacterial novelty that shifts toward anaerobic
RT metabolism during the third week of life.";
RL Submitted (DEC-2013) 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: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:ETJ16857.1}.
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DR EMBL; AZMM01018810; ETJ16857.1; -; Genomic_DNA.
DR AlphaFoldDB; W1WF91; -.
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 CDD; cd00812; LeuRS_core; 1.
DR Gene3D; 3.10.20.590; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 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 NCBIfam; TIGR00396; leuS_bact; 1.
DR PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 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; 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:ETJ16857.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 41..180
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 221..391
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 405..606
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 644..769
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 806 AA; 92068 MW; F188CB53E8227A40 CRC64;
MSVYNFKDVE AKWQHKWEET NQYKTDTRDT SKPLYYTLEM FPYPSGKIHM GHVRNYSIGD
VVARFKKMEG YNVLHPMGWD SFGLPAENAA IKHGIHPAKW TYENIDDMKN QLKLLGLSYD
WERELATSNP DYYKFTQEIF LKFLEAGLAY KKKSFVNWCP SCETVLANEQ VVGGQCERCD
AVVVKKELEQ WYFKTTEFAE ELLNDLDKLE GWPEKVKTMQ RNWIGKSHGA EIVFDIDGSD
DQMIVYTTRP DTVYGTTFMA LAPENPLVKE LVAGTEYEAD VDKFVQKMHT QTEIERTSTD
TEKEGMFIGK YVINPITGRK VPLWIANYIL MDYGTGAIMG VPAHDDRDKE FATKYGIEII
DVIDEDGKMI NSEEFNGMDA TEAQDKITEK LAKEGRGKKT VNYRLRDWLL SRQRYWGVPI
PVVYCEDCGI VPVDKKDLPV LLPTDVEFTG KGESPLTTSK TFINTTCPKC GKHATRDVDT
MDTFVDSSWY FLRYIDNKNQ EAMFDSEVVN KWMPVDQYIG GVEHAIMHLL YARFFVKALK
KVGMVDFDEP FKNLLTQGMV LMDGSKMSKS KGNTVSPLEI IDKYGADTAR LFVLFAAPPE
RDLDWSEQGV EGCFRFLNRV YRLVDELKDI AKSDAKVNVA TKEDKAMRFT IHSTLKKVTD
DLSFKFGFNT AIASLMELIN EMYKYKELDT RNDGIIKEGI ETIVTILAPF TPHVGEELWQ
MIGKEGSIFD ISWPEFDESA LVKDEVEVVV QINGKVRAKL SVGANMTKEE MEKVALENDK
VQASIGDKTV VKVIAIPKKL INIVVK
//