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Database: UniProt
Entry: D1AQ30_SEBTE
LinkDB: D1AQ30_SEBTE
Original site: D1AQ30_SEBTE 
ID   D1AQ30_SEBTE            Unreviewed;       865 AA.
AC   D1AQ30;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   RecName: Full=Leucine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00049};
DE            EC=6.1.1.4 {ECO:0000256|HAMAP-Rule:MF_00049};
DE   AltName: Full=Leucyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00049};
DE            Short=LeuRS {ECO:0000256|HAMAP-Rule:MF_00049};
GN   Name=leuS {ECO:0000256|HAMAP-Rule:MF_00049};
GN   OrderedLocusNames=Sterm_0736 {ECO:0000313|EMBL:ACZ07608.1};
OS   Sebaldella termitidis (strain ATCC 33386 / NCTC 11300).
OC   Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC   Sebaldella.
OX   NCBI_TaxID=526218 {ECO:0000313|EMBL:ACZ07608.1, ECO:0000313|Proteomes:UP000000845};
RN   [1] {ECO:0000313|Proteomes:UP000000845}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33386 / NCTC 11300 {ECO:0000313|Proteomes:UP000000845};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Mikhailova N., Sims D., Meincke L., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.F., Hugenholtz P.,
RA   Woyke T., Wu D., Eisen J.A.;
RT   "The complete chromosome of Sebaldella termitidis ATCC 33386.";
RL   Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACZ07608.1, ECO:0000313|Proteomes:UP000000845}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33386 / NCTC 11300 {ECO:0000313|Proteomes:UP000000845};
RX   PubMed=21304705;
RA   Harmon-Smith M., Celia L., Chertkov O., Lapidus A., Copeland A.,
RA   Glavina Del Rio T., Nolan M., Lucas S., Tice H., Cheng J.F., Han C.,
RA   Detter J.C., Bruce D., Goodwin L., Pitluck S., Pati A., Liolios K.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Chang Y.J., Jeffries C.D., Brettin T., Goker M., Beck B.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P., Chen F.;
RT   "Complete genome sequence of Sebaldella termitidis type strain (NCTC
RT   11300).";
RL   Stand. Genomic Sci. 2:220-227(2010).
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, ECO:0000256|HAMAP-
CC         Rule:MF_00049};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00049}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00049,
CC       ECO:0000256|RuleBase:RU363035}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00049}.
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DR   EMBL; CP001739; ACZ07608.1; -; Genomic_DNA.
DR   RefSeq; WP_012860204.1; NC_013517.1.
DR   AlphaFoldDB; D1AQ30; -.
DR   STRING; 526218.Sterm_0736; -.
DR   KEGG; str:Sterm_0736; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_0; -.
DR   Proteomes; UP000000845; 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   CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR   CDD; cd00812; LeuRS_core; 1.
DR   Gene3D; 2.20.28.290; -; 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; 1.
DR   PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 2.
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   ECO:0000256|HAMAP-Rule:MF_00049};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00049};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00049};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00049};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00049};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00049}; Reference proteome {ECO:0000313|Proteomes:UP000000845}.
FT   DOMAIN          38..175
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          222..407
FT                   /note="Leucyl-tRNA synthetase editing"
FT                   /evidence="ECO:0000259|Pfam:PF13603"
FT   DOMAIN          421..575
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          616..656
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          696..826
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   MOTIF           617..621
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT   BINDING         620
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   865 AA;  99521 MW;  FCE1ED4C15A6F801 CRC64;
     MREYNPKEIE NKWQSKWNKD NIFKSENVSD KENYYILEMF AYPSGNLHVG HLRNYTIGDA
     IARYKKMKGF NVLHPFGWDS FGLPAENAAI ENKAHPGDWT RKNIDNMKRQ LKLMGISHDW
     SRELATYQEN YYKWNQWMFI KMYEKGLVYK KKSYVNWCPE CNTVLANEQV EDGKCWRHSK
     TDVIQKELDQ WYFKITDYSE ELLQSHDDLA GNWPDKVITM QKNWIGKSYG TEIDFVLEDG
     KTKIPAFTTR PDTLYGVTYV VLAPEHPVVE DIILKDNPAL KVKTDAMINE DKIERTAEDK
     EKEGFFTGKY VTNPVNGEKI PLWVGNYVLM DYGTGAVMAV PAHDERDFLF AGKYDLPLRV
     VIEPEGEKLD ISTMKQAYTG EGILVNSDKF DGMKNNDAKT AVSEYLEEIK GGLRTVNYRL
     HDWLLSRQRY WGTPIPALYC EKCGLVMEKI ENLPVKLPMD IEFSGVGNPL ETSEQFKNVT
     CPVCGGTAKR ETDTMDTFVD SSWYYLRFLN PNLDTAPFDK TDADNWTPVD QYIGGVEHAV
     MHLLYARFFH KVLRDMGLLS SNEPFRRLLT QGMVLGPSYY SNEERKFYFE ADVNVDNKTG
     KAYSKKTGEE LAVKVEKMSK SKNNGVDPEV IVKEYGADSA RVFSLFAAPP EKELEWNMNG
     LAGAYRFLNR LFLLIEDTKE FSEAGEIDHG KRNNEDSEIQ KKLHQTVKKV SESMEDNFHF
     NTAIAALMEL LNDMTSYRQK VIDTGKISSE SKKIWREVME KTVLMLSPFA PHIADELWSA
     SGREGYAFLE SWPEYIEELT KESKINLVVQ VNGKLRDTIL ADVNIPKEEL EKIALASEKA
     QKFLEGKEIV KVVVVPNKLV NIVVK
//
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