ID A0A3P8WD11_CYNSE Unreviewed; 1197 AA.
AC A0A3P8WD11;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=LARS1 {ECO:0000313|Ensembl:ENSCSEP00000023511.1};
OS Cynoglossus semilaevis (Tongue sole).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Cynoglossidae;
OC Cynoglossinae; Cynoglossus.
OX NCBI_TaxID=244447 {ECO:0000313|Ensembl:ENSCSEP00000023511.1, ECO:0000313|Proteomes:UP000265120};
RN [1] {ECO:0000313|Ensembl:ENSCSEP00000023511.1, ECO:0000313|Proteomes:UP000265120}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24487278;
RA Chen S., Zhang G., Shao C., Huang Q., Liu G., Zhang P., Song W., An N.,
RA Chalopin D., Volff J.N., Hong Y., Li Q., Sha Z., Zhou H., Xie M., Yu Q.,
RA Liu Y., Xiang H., Wang N., Wu K., Yang C., Zhou Q., Liao X., Yang L.,
RA Hu Q., Zhang J., Meng L., Jin L., Tian Y., Lian J., Yang J., Miao G.,
RA Liu S., Liang Z., Yan F., Li Y., Sun B., Zhang H., Zhang J., Zhu Y., Du M.,
RA Zhao Y., Schartl M., Tang Q., Wang J.;
RT "Whole-genome sequence of a flatfish provides insights into ZW sex
RT chromosome evolution and adaptation to a benthic lifestyle.";
RL Nat. Genet. 46:253-260(2014).
RN [2] {ECO:0000313|Ensembl:ENSCSEP00000023511.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 AlphaFoldDB; A0A3P8WD11; -.
DR STRING; 244447.ENSCSEP00000023511; -.
DR Ensembl; ENSCSET00000023819.1; ENSCSEP00000023511.1; ENSCSEG00000014984.1.
DR GeneTree; ENSGT00390000012163; -.
DR InParanoid; A0A3P8WD11; -.
DR Proteomes; UP000265120; Chromosome 19.
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:UP000265120}.
FT DOMAIN 20..104
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 182..765
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 804..916
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 112..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1197 AA; 136136 MW; 7E7E90D56756F784 CRC64;
MTERKGTAKL DYLRKIEIDV QEKWEKEKAF EHDAPSTVGE SNNKNKYFVT FPYPYMNGRL
HLGHTFSLSK CEFAVGYQAL KGKKCLFPFG LHCTGMPIKA CADKLKREME LYGNPPQFPD
EEEEEKEKEK PKTSDEIIIK DKAKGKKSKA VAKSGTSTFQ WDIMRSLGLT DGEITKFANA
EHWLEYFPPL AVKDLKQMGV KVDWRRSFIT TDVNPFYDSF VRWQFNTLKE RKKIKFGKRY
TIYSPRDGQP CMDHDRQTGE GVGPQEYTLI KMKIVEPYTG KFKSKVFYSS GMKGKSIYLV
AATLRPETMF GQTNCWVRPD MKYVAFETAS GDVFISTSRS ARNMSYQGFT KENGVVPVIM
EILGQDILGC ALSAPLTSYK IIYALPMLTI KEDKGTGVVT SVPSDAPDDI AALRDIKKKQ
ALREKYGIED KMVLPFEPVP IIEIPGYGNL SAPLVCDELK IQSQNDKEKL AEAKEKVYLK
GFYEGIMLVD GFKGQKVQDV KKPIQKMMVE KGEAMIYMEP EKQVMSRSAD ECVVALCDQW
YLDYGDAEWK QQANEALKSL ETFCEETRRN FEATLAWLQE HACSRTYGLG TRLPWDEQWL
IESLSDSTIY MAYYTIAHLL QGGVLNGQEP SPLGIKPEQM TKEVWDFIFF KTSPFPKTDI
PKVNLQKLRR EFEYWYPVDV RVSGKDLVPN HLSYYLYNHV AIWPQDNKKW PQAVRANGHL
LLNSEKMSKS TGNFLTLSQA IDKFSADGMR LALADAGDTV EDANFVETMA DAGILRLYTW
VEWVKEMIAN QNNLRTGPAN TFNDRVFASE MNAGILKTEQ HYDRMMYKEA LKSGFFEFQA
AKDKYRELAI EGMHRDLIFQ FIEKQTLLLA PICPHLCEYT SGLLGKTTSV TKSSWPLAGP
VDEILIRSSQ YLMETAHDLR LRLKAYMLPP KSKKADPKPP AKPSHCTIYV AKSYPPWQHS
ALSLLGKHYK SNKGSLPDNK VIASELGALP ELKKYMKRVM PFVAMIKENL EKNGPRVLDL
ELEFDERAVL MENLVYLTNS LEVLASFIST ICKLEQIDVL FASEADDKVK EDCCPGKPFC
VFRSEPAVCV SLVNPQPCNG LFSTKIDVRQ GDSRDSLIRR LCKVNRLIKD MSKVKLMRYE
DPVGGPRRVP VLGQEELGKL PISSKSVFNI NLEEKKVTLA DNGLSVDIGD TLVYLVQ
//
