ID A0A0M9A1B2_9HYME Unreviewed; 878 AA.
AC A0A0M9A1B2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=WN51_00259 {ECO:0000313|EMBL:KOX74356.1};
OS Melipona quadrifasciata.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Melipona.
OX NCBI_TaxID=166423 {ECO:0000313|EMBL:KOX74356.1, ECO:0000313|Proteomes:UP000053105};
RN [1] {ECO:0000313|EMBL:KOX74356.1, ECO:0000313|Proteomes:UP000053105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0111107301 {ECO:0000313|EMBL:KOX74356.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KOX74356.1};
RA Pan H., Kapheim K.;
RT "The genome of Melipona quadrifasciata.";
RL Submitted (JUL-2015) 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}.
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DR EMBL; KQ435791; KOX74356.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M9A1B2; -.
DR STRING; 166423.A0A0M9A1B2; -.
DR OrthoDB; 2876972at2759; -.
DR Proteomes; UP000053105; 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 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 InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
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 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:UP000053105}.
FT DOMAIN 47..249
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 409..567
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 693..819
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 878 AA; 102519 MW; 45020271F1BB77A5 CRC64;
MKITKSFMSH YMINTFFRNM ICRYVSCGIN QFSNKDITDE IKKSIEKYWK DKVNLHQYDD
TDNTRKRFYV LSMFPYPSGT LHMGHVRVYT ISDTVARFYR MKGYNVLHPI GWDAFGLPAE
NAAFEKKLDP VVWTYDNIKT MRNQLNSLNY SFDWSREFAT CDPEYYKWTQ ELFLKLFDRD
LVYRKESFVN WDPIDETVLA EEQIDTNSCS WRSGAKVEKR LLNQWFIRTI PFAKSLSEGL
NDPTLKEWRD IKTIQQNWIG DCNGTSFELQ LIGNIPNYPK TTNIWTNYPE FIEYAKFIAI
SPKSLLNRSE YCKDVVEGIQ IINAKVVNPF SGNELPIFVT DKITFPNFRD THLGIPSVSM
DDYQFSELIG LKFTRHSIRS YEEQQKKRLE ILSKARKWKI GGYPVGSRLQ DWLISRQRYW
GTPIPIIYCS HCGIQPVPRD KLPVVLPNVA FSSSSKKSIL REMKDWLNTS CPKCGGEAVR
ESDTMDTFVD SSWYYLRYID PQNMKEMFTT NKVKEIFPVD LYIGGKEHAV LHLYYARFIS
HFLHSEGLLP SMEPFKQLLV QGMVLGKTYQ VKKTQKYLKA DEIEENAGEY VEKSTKEPVI
VSWDKMSKSK YNGIDPLVFV EKYGIDTTRL FILADQAPTS DKRCNHDTIP GILNWQSRLW
KTVKTFTDYR NNVTLEELQA QPTDPKFAQD DEYMFDSRNY FLKSVTFNII GSQQLSIAIS
RLQGLTNSIR KVSVECMKKS REYERALAAQ IIMLAPFAPH FASELWSAFS TVKHHLIDKN
EIELDKDVME QKWPEIDINY KMAVEVRING ALCTKIRIPK YETDKLSLEA ALNLIENEPT
VQKRLKKHKI DEFRLLSREG CDPKIFISTK KNIVTVPV
//
