ID   A0A0L6WUU9_9AGAR        Unreviewed;      1026 AA.
AC   A0A0L6WUU9;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Putative leucyl-tRNA synthetase, cytoplasmic {ECO:0000313|EMBL:KNZ79345.1};
GN   ORFNames=J132_10542 {ECO:0000313|EMBL:KNZ79345.1};
OS   Termitomyces sp. J132.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Tricholomatineae; Lyophyllaceae;
OC   Termitomyces.
OX   NCBI_TaxID=1306850 {ECO:0000313|EMBL:KNZ79345.1, ECO:0000313|Proteomes:UP000053712};
RN   [1] {ECO:0000313|Proteomes:UP000053712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J132 {ECO:0000313|Proteomes:UP000053712};
RA   Hu H., Poulsen M.;
RT   "The genome of Termitomyces.";
RL   Submitted (JAN-2014) 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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR   EMBL; KQ412415; KNZ79345.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L6WUU9; -.
DR   STRING; 1306850.A0A0L6WUU9; -.
DR   OrthoDB; 5472610at2759; -.
DR   Proteomes; UP000053712; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd07959; Anticodon_Ia_Leu_AEc; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR   InterPro; IPR004493; Leu-tRNA-synth_Ia_arc/euk.
DR   InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR032678; tRNA-synt_1_cat_dom.
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; PF01406; tRNA-synt_1e; 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   4: Predicted;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000313|EMBL:KNZ79345.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053712};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          613..690
FT                   /note="tRNA synthetases class I catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01406"
FT   DOMAIN          738..859
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
SQ   SEQUENCE   1026 AA;  115640 MW;  7132D8BAEBABCD2A CRC64;
     MNGSLHLGHA FTISKIEFAA GYQRMLGKRV LFPHGFHASS DKIIREIELF GPDFERYEEV
     NAKMIAEEVE RDEAEAAAVT DSIIDKSKAK KGKLAAKSTG HTYQFQIMES IGIPRTEIKK
     FADPYYWLTV FPPIAIEDNN AFGARIDWRR SFITTDANPY YDSFVRWQAN KLHQLGKIKF
     GERYTIYSPK DGQPCMDHDR SDGEGIGPQE YTGIKMEVLE WSSAAKYAIE SKVDGRKVFL
     VAATLRPETM YGQTNCYVGI ALKYGVFAVN DKEAFVCTHR AARNMAFQGI STPRGEINQL
     LEITGDKLIG TKIDAPFSLN HEVYVLPMDN VLATKGTGVV TSVPSDSPDD CQTLYDLRKK
     AAFYKIDPSW ASIDPTPVIS TPTYGDMCAP ALLSALKVQS QKDTKQLTEA KEIAYKEGFY
     SGTMLVGEFK GQSVQDAKPK VRQRMIEAGL AFAYAEPEGL VISRSADECV VALMDQWYLD
     YGEECWRNQV ENLLAKMNTY SVETRNHFEK TLAWLNKWAC ARTYGLGSKL PWDPHFLVES
     LSDSTIYMSY YTVAQLLHED SLDGSKPGPL SITPDQMTDE IWEYIFCDGP FPDPSPLARE
     KADALKHEYS YFYPFDIRSS AKDLVPNHLT FCLYNHAAIF PVDKFPLSMR TNGHLMLNGK
     KMSKSLGNFL TLRDGIRKFG ADATRLSLAD AGDGLEDANF EEKTANASIL RVHTLLGWCE
     DIIKDEASLR SGPRNYHDNI FEHEMNELIN VTQGHYEAMT YKDAVKFGFY EFQSARDWYR
     EVTSDVGMHR DLVRYWINAA ALIITPIAPH FAEHIHSTIL KSPTSVQSAL WPTPTQPVDR
     TALEAAVYMR DTIKTIRDAE VSLLKMLQKA KGKKGPGGPV TAFDPKLPKS VRIYVATTFP
     EWQDTCVQAV KDAYDEQTDK VDDAKVKMLL TKRGLIKDKR AMPFVQVFKK RMAQFGAQTA
     FRRALPFSES QVLREILPYL TKSLGLVDAE VLSVEEARQK EGERGYTKSI IDSSEPGTPA
     FEYRNV
//