ID   E2AGH8_CAMFO            Unreviewed;       811 AA.
AC   E2AGH8;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 68.
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=EAG_12638 {ECO:0000313|EMBL:EFN67462.1};
OS   Camponotus floridanus (Florida carpenter ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Formicinae; Camponotus.
OX   NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN   [1] {ECO:0000313|EMBL:EFN67462.1, ECO:0000313|Proteomes:UP000000311}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
RX   PubMed=20798317; DOI=10.1126/science.1192428;
RA   Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA   Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA   Wang J., Liebig J.;
RT   "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT   saltator.";
RL   Science 329:1068-1071(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};
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363035}.
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DR   EMBL; GL439312; EFN67462.1; -; Genomic_DNA.
DR   AlphaFoldDB; E2AGH8; -.
DR   STRING; 104421.E2AGH8; -.
DR   EnsemblMetazoa; XM_011259394.3; XP_011257696.3; LOC105252137.
DR   InParanoid; E2AGH8; -.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000000311; Unassembled WGS sequence.
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; cd00812; LeuRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR002302; Leu-tRNA-ligase.
DR   InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   NCBIfam; TIGR00396; leuS_bact; 1.
DR   PANTHER; PTHR43740:SF3; 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   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   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:UP000000311}.
FT   DOMAIN          3..174
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          337..514
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          624..728
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
SQ   SEQUENCE   811 AA;  94512 MW;  51AD83DCFC6AE3C2 CRC64;
     MFPYPSGALH MGHVRVYTIS DVLARFYRLK GKNVIHPMGW DAFGLPAENA AIERKIDPAV
     WTSENIKTMH DQLKKLNYSF DWEREFATCD ADYYKWTQDL FLKLFDKGLA YQKKAYVNWD
     PIDQTVLAEE QVDLNQRSWR SGAIVEKKLL KQWFIKTTAF AKSLMEGLDD PNLKDWRDII
     KLQKHWIGDC NGINIDFKMI SEIPDFPETI NLWTDMPEFI EHAKFVAISP QSILHRKEYT
     YDIDVGIKGL NAKIINPFSG DELPIFITDK VIYPPWRDTR LGVPSASMDD LTFSELVGIP
     FTRHSIRNYE QQQQKISEIV QKARKWGIGG YPVSSRLQDW LISRQRYWGT PIPIIHCINC
     GVQPVPRDQL PVTLPKIIHS SSNRGFSIQD VKDWLQTECP KCGGKATREA DTMDTFVDSS
     WYFLRFIDPK NTKEMFAIEK VKEAFPVDLY IGGKEHAVLH LYYARFISHF LHSEGLIPCR
     EPFRQLLVQG VIMGKTYKTK STGKYVTEDE IIKEEDQYKT KSGEVVFMSW EKMSKSKYNG
     VEPFNLLHKY GIDTTRLLIL GDVAPTSTRN WSEDTIPGIK NWQNRIWNSV KQFKSQRDCI
     SLEEFQNEPT DPTYVEHNAY MFDSRNYFLK NVTHNMVKTQ QLSIAISRMQ GLTNSLRKVS
     IECLRKSREY ERALAVQIIM LAPFAPHFAS ELWAIFCSVK HHLIDNNEVS LDKDVLEQKW
     PEIDMDYKLV LNVYINKRQF LKLKIPRHIL DKMTAEMALE YVTLDQHYQK KSDDKNIVEI
     NLQSEKGCDA SLYITMEKQK KDIRNAITDS R
//