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Database: UniProt
Entry: A0A2Y9E0T2_TRIMA
LinkDB: A0A2Y9E0T2_TRIMA
Original site: A0A2Y9E0T2_TRIMA 
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
//
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