ID A0A2Y9E0T2_TRIMA Unreviewed; 1176 AA.
AC A0A2Y9E0T2;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
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 Name=LOC101349569 {ECO:0000313|RefSeq:XP_004385002.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_004385002.1};
RN [1] {ECO:0000313|RefSeq:XP_004385002.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (SEP-2023) to UniProtKB.
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 RefSeq; XP_004385002.1; XM_004384945.3.
DR AlphaFoldDB; A0A2Y9E0T2; -.
DR STRING; 127582.A0A2Y9E0T2; -.
DR GeneID; 101349569; -.
DR KEGG; tmu:101349569; -.
DR InParanoid; A0A2Y9E0T2; -.
DR OrthoDB; 5472610at2759; -.
DR Proteomes; UP000248480; Unplaced.
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; cd07959; Anticodon_Ia_Leu_AEc; 1.
DR CDD; cd00812; LeuRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR004493; Leu-tRNA-synth_Ia_arc/euk.
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; TIGR00395; leuS_arch; 1.
DR PANTHER; PTHR45794:SF1; LEUCINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR45794; LEUCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 2.
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:UP000248480}.
FT DOMAIN 20..103
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 188..755
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 794..908
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 1176 AA; 134744 MW; DD6A07FCFF125774 CRC64;
MTERKGTAKV DFLKKIEKEI QQKWDAEKVF EVNASDLEKQ SSKSKYFVTF PYPYMNGRLH
LGHTFSLSKC EFAVGYQRLK GKSCLFPFGL HCTGMPIKAC ADKLKREIEL YGCPPEFPDE
EEEEEEINVK TEDIIIKDKA KGKKSKATAK AGSSKYQWGI MRSLGLSDEE IVKFSEAEHW
LDYFPPLAIQ DLKRMGLKVD WRRSFITTDV NPYYDSFVRW QFLTLRERNK IKFGKRYTIY
SPKDGQPCMD HDRQTGEGVG PQEYTLIRLK VLEPYPSKLS GLKGKNIFLV AATLRPETMF
GQTNCWVRPD MKYIGFETVT GDIFICTQRA ARNMAYQGFT KDDGVVPVVK ELMGEEILGA
SLSAPLTSYK VIYVLPMLTI KEDKGTGVVT SVPSDSPDDI AALRDLKKKQ ALRAKYGIRD
DMVLPFEPVP VIEVPGFGSL SAVTICDELK IQSQNDREKL AEAKEKLYLK GFYDGVMLVD
EFKGEKVQDV KKTIQKKMID MGDAFIYMEP EKQVMSRSSD ECVVALCDQW YLDYGEENWK
KQTSQCLKNL ETFCEETRRN FEATLDWLQE HACSRTYGLG TRLPWDEQWL IESLSDSTIY
MAFYTVAHLL QGGNLHGQGE SPLDIRPQQM TKDVWDYIFF KEAPFPKTQI PKEKLDQLKQ
EFEFWYPVDL RVSGKDLVPN HLSYYLYNHV AMWPEQSDKW PTAVRANGHL LLNSEKMSKS
TGNFLTLTQA IDKFSADGMR MALADAGDTV EDANFVEAMA DAGILRLYTW VEWVKEMVAN
WDSLRSGPAS TFNDRVFASE MNAGIIKTDQ NYEKMMFKEA LKTGFFEFQA AKDKYRELAI
EGMHRELVFW FIEVQTLLLT PFCPHLCEHI WTLLGKPGSI MKASWPVAGP VDEALIRSSQ
YLMEVAHDLR LRLKNYMMPA RGKKTDKQPP QRPSHCTIYV AKNYPPWQHT TLSVLRNHFE
ANSGKLPDNK VIASELANLP ELKKYMKKVM PFVAMIKENL EKLGPRVLDL QLEFDEQAVL
MENIVYLTNS LELEHIEVKF ASEAEDKVKE DCCPGKPLNV FRTEPGVLVS LVNPQPSSGH
FSTKIEIRQG DNHDSIIRRL MKMDRGIKDL SRVKLMRFDD PLLGPRQIPV LGKEYSEKTP
ISEHAVFHVD LTSKKIHLTE NGLKADIGDT VIYLVH
//