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Database: UniProt
Entry: A0A091GWL7_BUCRH
LinkDB: A0A091GWL7_BUCRH
Original site: A0A091GWL7_BUCRH 
ID   A0A091GWL7_BUCRH        Unreviewed;       904 AA.
AC   A0A091GWL7;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
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=N320_02059 {ECO:0000313|EMBL:KFO86917.1};
OS   Buceros rhinoceros silvestris.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Bucerotiformes; Bucerotidae; Buceros.
OX   NCBI_TaxID=175836 {ECO:0000313|EMBL:KFO86917.1, ECO:0000313|Proteomes:UP000054064};
RN   [1] {ECO:0000313|EMBL:KFO86917.1, ECO:0000313|Proteomes:UP000054064}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N320 {ECO:0000313|EMBL:KFO86917.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-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   -!- 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; KL512536; KFO86917.1; -; Genomic_DNA.
DR   RefSeq; XP_010129860.1; XM_010131558.1.
DR   AlphaFoldDB; A0A091GWL7; -.
DR   GeneID; 104489400; -.
DR   KEGG; brhi:104489400; -.
DR   CTD; 23395; -.
DR   OrthoDB; 2876972at2759; -.
DR   Proteomes; UP000054064; 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; cd07958; Anticodon_Ia_Leu_BEm; 1.
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   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; 3.
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:UP000054064}.
FT   DOMAIN          68..259
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          428..602
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          639..679
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          727..844
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
SQ   SEQUENCE   904 AA;  102943 MW;  AEEA488BEC84CA29 CRC64;
     MQPLCRRAGA CSWCLKRQLR GFLALVKWQR RLVPASARAI YSETGRWEKS YGLETRRRVE
     NWWLPRIKDQ FCSISETDKS RPKFYVLSMF PYPSGKLHMG HVRVYTISDA VARFQKMRGM
     QVINPMGWDA FGLPAENAAV EHGLHPASWT QSNIQHMRKQ FDALGLSFTW EREITTCLPE
     YYRWTQYLFL KLFEAGIVYQ KEALVNWDPV DQTVLANEQV DDNGCSWRSG AKVEQKYLKQ
     WFIKTTAYAK AMLDALSDLP EWYGIKEMQA NWIGDCVGCS LDFSLKVNGE ATGEKLAAYT
     YTPEAIYGAS HVYVVPTHRL LHGSSRLRDV FQRDLVPGKD SLTSVTAVNL LTNQEIPVVI
     SAKATFENFL DTKIGIPSTS AEDAAVAKTL GIPFTEVIET LPNGSERVIN SAEITGMTRQ
     EALKAITQQA KEKRIGGDLT SDKLRDWLIS RQRYWGTPIP VIHCQTCGTV PVPYEDLPVV
     LPNVTTFTGK GASPLETAAE WVNCSCPRCK AAARREVDTM DTFVDSAWYY LRYTDPHNSD
     RPFRSDLADY WMPVDLYIGG KEHAVMHLFY ARFFSHFCHD LKMTKHKEPF HKLLVQGLIK
     NQTFRLTTTG QCLKREEVDL TGAEPVHRKT GEKLQVAWEK MSKSKHNGID PEELVREYGI
     DTLRLYLLFA APPEQDILWE AKTDAVPGVQ RWQTRLWALV TKLIEARTSG TVPSPELLNQ
     KEKAEARKIW EQKNLVISEV TEYFTKDHVF NAAISRLMSL TNVLHQASRP LVLHSAEFED
     ALASLCVMVA PMAPHIASEM WKGLAHMQNK LCTHHHWDVD VLHQSWPKVD AEYLQPSDVV
     EMSVLINNKA LGKVWVPQQA ARSCEEVHEL VLQSELGVKH LQGRTIKKAF LSPRTALINF
     LVQE
//
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