ID U3JKN8_FICAL Unreviewed; 1270 AA.
AC U3JKN8;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
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:ENSFALP00000003342.1};
OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000003342.1, ECO:0000313|Proteomes:UP000016665};
RN [1] {ECO:0000313|Ensembl:ENSFALP00000003342.1}
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; U3JKN8; -.
DR STRING; 59894.ENSFALP00000003342; -.
DR Ensembl; ENSFALT00000003355.2; ENSFALP00000003342.1; ENSFALG00000003209.2.
DR eggNOG; KOG0437; Eukaryota.
DR GeneTree; ENSGT00390000012163; -.
DR HOGENOM; CLU_004174_1_0_1; -.
DR OMA; KFIEWQF; -.
DR Proteomes; UP000016665; Unplaced.
DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0005764; C:lysosome; IEA:Ensembl.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004819; F:glutamine-tRNA ligase activity; IEA:Ensembl.
DR GO; GO:0005096; F:GTPase activator activity; IEA:Ensembl.
DR GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0071233; P:cellular response to leucine; IEA:Ensembl.
DR GO; GO:1990253; P:cellular response to leucine starvation; IEA:Ensembl.
DR GO; GO:0006425; P:glutaminyl-tRNA aminoacylation; IEA:Ensembl.
DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:Ensembl.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IEA:Ensembl.
DR GO; GO:0008361; P:regulation of cell size; IEA:Ensembl.
DR CDD; cd07959; Anticodon_Ia_Leu_AEc; 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:UP000016665}.
FT DOMAIN 113..196
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 282..849
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 888..1002
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 75..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1270 AA; 144185 MW; DB1E6EDE652032D3 CRC64;
MNPRRHLGGA LLKGQRAGGR AARMGTGGSF PRPPPRQAAA AIAPSPLPPA LLLSLPFPLS
RARCPPARCL GTARAPPRVP RWHGPRGPVR RGNMAERKGT AKVDFLKKIE REVQQKWDHD
RVFEINAADR RDQRSKGKYF VTFPYPYMNG RLHLGHTFSL SKCEFAVGYQ RLKGKSCLFP
FGLHCTGMPI KACADKLKRE MELYGCPPEF PDEEEEEEEN SGKKEEEIII KDKAKGKKSK
AAAKTGSSKY QWGIMKSLGL SDEEVVSFSE AEHWLDYFPP LAVQDLKSMG LKVDWRRSFI
TTDVNPYYDS FVRWQFLTLK ERNKIKFGKR YTIYSPKDGQ PCMDHDRQTG EGVGPQEYTL
IKMKVLDPYP AKLSGLRGKN IFLVAATLRP ETMFGQTNCW LRPDMKYIGF ETASGDIFIC
TQRAARNMSY QGFTRDSGVL PVVKELMGEE ILGAALSAPL STYKVIYALP MLTIKEDKGT
GVVTSVPSDS PDDFAALRDL KKKQALRVKY GIRDEMVLPF EPVPIIEIPD FGNLCAPFIC
DELKIQSQND REKLAEAKER VYLKGFYEGV MLVSEFKGQK VQDVKKRIQK LMLDKGEAMI
YMEPEKQVMS RSADECVVAL CDQWYLDYGE VSWKKQASEC LQHLETFCEE TRRNFEATLG
WLQEHACSRT YGLGTRLPWD EQWLIESLSD STIYMAYYTV AHLLQGGNLR GQGESPLGIR
AHQMSKEVWD YIFFKTAPFP KTEIPKEKLD KLKEEFEFWY PVDLRVSGKD LVPNHLSYYL
YNHVAMWSEQ REKWPVAVRA NGHLLLNSEK MSKSTGNFLT LTQAVDKFSA DGMRLALADA
GDTVEDANFV EAMADAGILR LYTWVEWVKE MIANRDSLRS GPASTFNDRV FASEMNAGIM
KTDQNYEKMM FKEALKTGFF EFQAAKDKYR ELAIEGMHRD LVFQFIEVQT LLLAPICPHL
CEHIWSLLGK AGSIMGASWP AAGPVDEVLI RSSQYLMEAA HDLRLRLKSY LAPAKGKKST
KEPPQKPSHC TIYVARSYPP WQHSTLSVLR SHFQASGGQL PDNKVIASEL NTLPELKKYM
KKVMPFVAMV KENLEKNGSR VLDLELEFDE RAVLMENIVY LTNSLELDHI EVKFASEAED
KIKEDCCPGK PFSIFRTEPG VPVFLVNPQP CNGHFSTRMD IRQGDSRESI IRRLMKMDRG
IKDLSKVKLM RFDDPVLGPR RVPVLGKEEA GKSPILEQAT FHIDLAQRHV CVTENGLTRD
IGDTIVYLVH
//
