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Database: UniProt
Entry: A0A2P5F0H3_TREOI
LinkDB: A0A2P5F0H3_TREOI
Original site: A0A2P5F0H3_TREOI 
ID   A0A2P5F0H3_TREOI        Unreviewed;      1001 AA.
AC   A0A2P5F0H3;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
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=TorRG33x02_128430 {ECO:0000313|EMBL:PON91280.1};
OS   Trema orientale (Charcoal tree) (Celtis orientalis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Cannabaceae; Trema.
OX   NCBI_TaxID=63057 {ECO:0000313|EMBL:PON91280.1, ECO:0000313|Proteomes:UP000237000};
RN   [1] {ECO:0000313|Proteomes:UP000237000}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. RG33-2 {ECO:0000313|Proteomes:UP000237000};
RA   Van Velzen R., Holmer R., Bu F., Rutten L., Van Zeijl A., Liu W.,
RA   Santuari L., Cao Q., Sharma T., Shen D., Roswanjaya Y., Wardhani T.,
RA   Kalhor M.S., Jansen J., Van den Hoogen J., Gungor B., Hartog M.,
RA   Hontelez J., Verver J., Yang W.-C., Schijlen E., Repin R., Schilthuizen M.,
RA   Schranz E., Heidstra R., Miyata K., Fedorova E., Kohlen W., Bisseling T.,
RA   Smit S., Geurts R.;
RT   "Parallel loss of symbiosis genes in relatives of nitrogen-fixing non-
RT   legume Parasponia.";
RL   Submitted (JUN-2016) 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:RU363035}.
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:PON91280.1}.
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DR   EMBL; JXTC01000075; PON91280.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P5F0H3; -.
DR   STRING; 63057.A0A2P5F0H3; -.
DR   InParanoid; A0A2P5F0H3; -.
DR   OrthoDB; 2876972at2759; -.
DR   Proteomes; UP000237000; 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   GO; GO:0009791; P:post-embryonic development; IEA:UniProt.
DR   GO; GO:0048608; P:reproductive structure development; IEA:UniProt.
DR   CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR   CDD; cd00812; LeuRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
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; 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   ECO:0000256|RuleBase:RU363035};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363035};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363035};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU363035};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW   ECO:0000256|RuleBase:RU363035};
KW   Reference proteome {ECO:0000313|Proteomes:UP000237000}.
FT   DOMAIN          125..257
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          306..499
FT                   /note="Leucyl-tRNA synthetase editing"
FT                   /evidence="ECO:0000259|Pfam:PF13603"
FT   DOMAIN          755..785
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          841..950
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   REGION          560..589
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1001 AA;  113394 MW;  72C42D6F3D4BEC18 CRC64;
     MNLQNMQART HIQWLAPPPI RFGSVLLPPA QGVHSPKLSN TISSIRNNTL ILRLCNRNSN
     LRTRGLIRSS VAEQEQSQNQ QLGVRRAYPF DEIEPKWQQF WEDNSTFRMP DEIDTSKPKF
     YVLDMFPYPS GAGLHVGHPL GYTATDILAR FKRMKGYNVL HPMGWDAFGL PAEQYAIETG
     THPKITTRKN ISRFRTQLKS LGFSYDWSRE ISTIEPEYYK WTQWIFLQLL KRGLAYQAEV
     PVNWCPALGT VLANEEVVDG VSERGGHPVI RKPMLQWMLR ITEYADRLLE DLDDLDWPES
     VKDMQRNWIG RSEGGEMEFS VLNSEGKERE INIKIYTTRP DTIFGATYLV MAPEHPLLQS
     LMTAEKSKSV QEYIDLASRK SDLERTELQK EKTGVFSGSY ARNPVNGEAI PIWVADYVLG
     SYGTGAIMAV PAHDTRDYEF ASKYDIPIRW VVTPDGEKIG DSGKAFPGEG VVINSSSTFG
     LDINGLSSKE AASKVIEWAE KTGTGKKQVN YKLRDWLFAR QRYWGEPIPV IFLDDTSESI
     PLSETELPLM LPELDDFTPT GTGEPPLSKA ESWVKTKDPL SGKPARRETS TMPQWAGSCW
     YYLRFMDPKN SKELVAKSKE KYWSPVDVYV GGAEHAVLHL LYSRATPLDL FKHNVSNLSK
     GFYSPGYWAY PYKVLYDIGV VSTKEPFKCV INQGIILGEV QYMACKDSDG NLISAESAET
     MGEHNQERIP EENVVKSGDS FVLKDNPNIR LIARAHKMSK SRGNVVNPDD VVSEYGADSL
     RLYEMFMGPL RDSKTWNTSG IEGVHRFLGR TWRLIIGSPL PDGTFQDGTV VTDEEPTQEQ
     LRSLHKCIAK VTEEIEGTRF NTGISAMMEF INVAYKWDKH PRLVIETFVL LLSPYAPHMA
     EELWFRLGHT QSLAYEPFPK ADPSFLKEST IVLPVQINGK TRGTIHVEEK CSEEDAFQLA
     SQDEKLSKYL NGKSIKKRIF VPGKILNVIL DRENAKVGVR G
//
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