ID   A0A446B6C4_9PEZI        Unreviewed;      1129 AA.
AC   A0A446B6C4;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 15.
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=TT172_LOCUS417 {ECO:0000313|EMBL:SPQ17998.1};
OS   Thermothielavioides terrestris.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Thermothielavioides.
OX   NCBI_TaxID=2587410 {ECO:0000313|EMBL:SPQ17998.1, ECO:0000313|Proteomes:UP000289323};
RN   [1] {ECO:0000313|EMBL:SPQ17998.1, ECO:0000313|Proteomes:UP000289323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Huttner S., Dainat J.;
RL   Submitted (APR-2018) 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, ECO:0000256|RuleBase:RU363039}.
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DR   EMBL; OUUZ01000001; SPQ17998.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A446B6C4; -.
DR   Proteomes; UP000289323; Unassembled WGS sequence.
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   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR004493; Leu-tRNA-synth_Ia_arc/euk.
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; TIGR00395; leuS_arch; 1.
DR   PANTHER; PTHR45794:SF1; LEUCINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR   PANTHER; PTHR45794; LEUCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 1.
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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|RuleBase:RU363039};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363039};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363039};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU363039};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW   ECO:0000256|RuleBase:RU363039}.
FT   DOMAIN          72..123
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          204..788
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          848..985
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
SQ   SEQUENCE   1129 AA;  126173 MW;  29BA68E1753C295B CRC64;
     MKIENTEKRD TLRAIEQKYQ KLWQEERVFE ADAPSCFDFT AGSHSADGPN SQTRKFFGLS
     SLPVGPWHIR KYVNGVPHLG HAFTVSKMDF AARVARAQRK NTLFPLGFHA TGMPIKACAD
     KLAYEMTLFG ELFSECPAPD ANVDGQQEGP TAPPRPREDV TRFTNVKKGK AALKSAKAKH
     QFQVMLSLGI PREQIHKFAD AGYWLQYFPQ LWQQHLTEFG CGIDWRRSFI TTHVNSYYDS
     FVQWQMRRLR DAGKIRFGKR YTVYSPKDAQ PCLDHDRATG EGVLVQEYVA LKCKVVRWSA
     RASDVLSSCD SIPSDADVFM IAATLRPETM YGQTNLFVSP SLTYGIFRIS AKEFYMTTDR
     AARNLAYQSV FPNWGVIPRV AGVSGSDLLG TLVRAPLSAK GDIYVIPMDS IKESKGTGIV
     ASVPSDSPDD YITTVDLSKK ATLHGVEPEW VCLDVLPIIN TPEHGNMIAP ALVEKLKINS
     PNDERRLLEA QEIAYKTGFY HGTMAYGPFA GKSVQEGKAL VRQQLLDSGD AFTYCEPESP
     VTSRSGDECV AAFLDQWFLT YGVDEEWRND TLEHLRGEDG LGFNCFGSVT KHSLEQSLAW
     MTEWCVTRQY GLGTQLPWDA SQLVEGLSDS TIYMAYYTVA HFLHSDMYGK EAGTGNIRAS
     QMTDNVWDYV FALSDDVGSS DIDKSTLDAM RREFTYWYPL DVRVSGKDLV NNHFVFFLYI
     HQAIWGKQAP QYLPKGIRLN GHLMLNGEKM SKNTGNFLSL DSTIHKFGAD ATRIALADGS
     DGIDDANFEE TTANAAVLKL FELKRWAEAV ICRPRLLGPE ETFEQVRAAE KPDDADTIQR
     TGSMSFWDEL FLNELNSLVR DTVRAYDATH YKAALKAGFY DLASARDTYR AWTAAASSSG
     MHQFCVRRYV GLQALMLAPI APHWADYIWR EVLGKPSTIQ TAPFPSPAPP SRSLTLTWAY
     IKHTLSRLTA ACAAQSKRRA KSRAKNDAHA GDATAEQTLI LRVATAWPPW QTQYLALARR
     HFFSSDAGLD IKALTREIDK SELKRAMPFL QQVKKQLKGG AEPAEVFERQ LGFDEVAVLN
     EMAPLMRRMV AGLKEVRIVK VAGADETSAE PGRPAMEFVG CELDGKQAG
//