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Database: UniProt
Entry: W1WF91_9ZZZZ
LinkDB: W1WF91_9ZZZZ
Original site: W1WF91_9ZZZZ 
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
//
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