ID R7VU06_COLLI Unreviewed; 826 AA.
AC R7VU06;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
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};
DE Flags: Fragment;
GN ORFNames=A306_12221 {ECO:0000313|EMBL:EMC80165.1};
OS Columba livia (Rock dove).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX NCBI_TaxID=8932 {ECO:0000313|EMBL:EMC80165.1};
RN [1] {ECO:0000313|EMBL:EMC80165.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Blood {ECO:0000313|EMBL:EMC80165.1};
RX PubMed=23371554; DOI=10.1126/science.1230422;
RA Shapiro M.D., Kronenberg Z., Li C., Domyan E.T., Pan H., Campbell M.,
RA Tan H., Huff C.D., Hu H., Vickrey A.I., Nielsen S.C., Stringham S.A.,
RA Hu H., Willerslev E., Gilbert M.T., Yandell M., Zhang G., Wang J.;
RT "Genomic diversity and evolution of the head crest in the rock pigeon.";
RL Science 339:1063-1067(2013).
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; KB375876; EMC80165.1; -; Genomic_DNA.
DR RefSeq; XP_005512220.2; XM_005512163.2.
DR AlphaFoldDB; R7VU06; -.
DR GeneID; 102087119; -.
DR KEGG; clv:102087119; -.
DR CTD; 23395; -.
DR eggNOG; KOG0435; Eukaryota.
DR OrthoDB; 2876972at2759; -.
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; IPR025709; Leu_tRNA-synth_edit.
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 Pfam; PF13603; tRNA-synt_1_2; 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}.
FT DOMAIN 2..181
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 193..352
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 366..524
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 561..601
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 649..766
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EMC80165.1"
SQ SEQUENCE 826 AA; 93688 MW; 63A9C4A852DD8DC6 CRC64;
KSRPKFYVLS MFPYPSGKLH MGHVRVYTIS DAVARFQKMR GMQVINPMGW DAFGLPAENA
AVEHGLHPAS WTQSNIQHMR EQFDALGLSF TWEREIMTCL PEYYKWTQYL FLKLFEAGLV
YQKEALVNWD PVDQTVLANE QVDDNGCSWR SGAKVEQKYL KQWFIKTTAY AKAMFDALSD
LPEWYGIKEM QANWIGDCVG CSLDFLLKVN GQVTGEKLAA YTYTPEAIYG ASHIAILPSH
SLLNGNSSLK EVFQRELIPG KDSLTSVTAV NLLTNQEIPV VISAKNNFEN FLTTKIGIPS
TSAEDAAVAK DLGISFTEVI ETLPNGLEKV INSGEITGMT RQEALKAITQ QAKNKGIGGD
LTSDKLRDWL ISRQRYWGTP IPVIHCQTCG TVPVPYEDLP VVLPNVTTFT GKGASPLESA
PEWVNCPCPR CKAAARREID TMDTFVDSAW YYLRYTDPHN TDRPFNSDVA DYWMPVDLYI
GGKEHAVMHL FYARFFNHFC RDLKMIKHKE PFHKLLVQGL IKNQTFRLTT TGQCLKREEV
DLTGTEPVHL KTGEKLQVAW EKMSKSKHNG IDPEELVKEY GIDTLRLYIL FAAPPEQDIL
WDTKTDAMPG VQRWQTRLWM LVTKLIEART SGTTPNRELL NKKEKAEARK IWEQKNFVIS
EVTECFTKDH LFNAAISRLM SLTNILHQAS RPLILHSAEF EDALATLCIM VAPMAPHIAS
EMWKGLAHMQ NKLCTHHHWD VDVLHQSWPK VDPEYLQPSD VVEMSVLINN KACGKVPVPQ
QAARNFEEVH ELVLQSELGA KHLQGRTIKK AFLSPRTALI NFLVQE
//
