SYLC_PONAB
ID SYLC_PONAB Reviewed; 1176 AA.
AC Q5R614;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Leucine--tRNA ligase, cytoplasmic;
DE EC=6.1.1.4;
DE AltName: Full=Leucyl-tRNA synthetase;
DE Short=LeuRS;
GN Name=LARS1; Synonyms=LARS;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the specific attachment of an amino acid to its
CC cognate tRNA in a two step reaction: the amino acid (AA) is first
CC activated by ATP to form AA-AMP and then transferred to the acceptor
CC end of the tRNA. Exhibits a post-transfer editing activity to hydrolyze
CC mischarged tRNAs. {ECO:0000250|UniProtKB:Q9P2J5}.
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 -!- ACTIVITY REGULATION: 5-fluoro-1,3-dihydro-1-hydroxy-1,2-benzoxaborole
CC inhibits LARS1 by forming a covalent adduct with the 3' adenosine of
CC tRNA(Leu) at the editing site, thus locking the enzyme in an inactive
CC conformation. {ECO:0000250|UniProtKB:Q9P2J5}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; CR860686; CAH92802.1; -; mRNA.
DR AlphaFoldDB; Q5R614; -.
DR SMR; Q5R614; -.
DR STRING; 9601.ENSPPYP00000017795; -.
DR PRIDE; Q5R614; -.
DR eggNOG; KOG0437; Eukaryota.
DR InParanoid; Q5R614; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 Gene3D; 3.40.50.620; -; 1.
DR Gene3D; 3.90.740.10; -; 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 PANTHER; PTHR45794; PTHR45794; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 2.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00395; leuS_arch; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..1176
FT /note="Leucine--tRNA ligase, cytoplasmic"
FT /id="PRO_0000229767"
FT REGION 115..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 53..63
FT /note="'HIGH' region"
FT MOTIF 716..720
FT /note="'KMSKS' region"
FT BINDING 719
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2J5"
FT MOD_RES 720
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2J5"
FT MOD_RES 970
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BMJ2"
FT MOD_RES 1047
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BMJ2"
SQ SEQUENCE 1176 AA; 134562 MW; D9D6C47D90443485 CRC64;
MAERKGTAKV DFLKKIEKEI QQKWDTERVF EVNASSLEKQ TSKGKYFVTF PYPYMNGRLH
LGHTFSLSKC EFAVGYQRLK GKCCLFPFGL HCTGMPIKAC ADKLKREIEL YGCPPDFPDE
EDEEEETNVK TEDTRIKDKA KGKKSKAAAK AGSSKYQWGI MKSLGLSDEE IVKFSEAEHW
LDYFPPLAIQ DLKRLGLKVD WRRSFITTDV NPYYDSFVRW QFLTLRERNK IKFGKRYTIY
SPKDGQPCMD HDRQTGEGVG PQEYTLLKLK VLEPYPSKLS GLKGKNIFLV AATLRPETLF
GQTNCWVRPD MKYIGFETVN GDIFICTQKA ARNMSYQGFT KDNGVVPVVK ELMGEEILGA
SLSAPLTSYK VIYVLPMLTI KEDKGTGVVT SVPSDSPDDI AALRDLKKKQ ALRAKYGIRD
DMVLPFEPVP VIEIPGFGNL SAVTICDELK IQSQNDREKL AEAKEKIYLK GFYEGIMLVD
GFKGQKVQDV KKTIQKKMID AGDALIYMEP EKQVMSRSSD ECVVALCDQW YLDYGEENWK
KQTSQCLKNL ETFCEETRRN FEATLGWLQE HACSRTYGLG THLPWDEQWL IESLSDSTIY
MAFYTVAHLL QGGNLHGQAE SPLGIRPQQM TKEVWDYVFF KEAPFPKTQI AKEKLDQLKQ
EFEFWYPVDL RVSGKDLVPN HLSYYLYNHV AMWPEQSDKW PTAVRANGHL LLNSEKMSKS
TGNFLTLTQA IDKFSADGMR LALADAGDTV EDANFVEAMA DAGILRLYTW VEWVKEMVAN
WDSLRSGPAN TFNDRVFASE LNAGIIKTDQ NYEKMMFKEA LKTGFFEFQA AKDKYRELAV
EGMHRELVFR FIEVQTLLLA PFCPHLCEHI WTLLGKPDSI MNASWPVAGP VDEVLIHSSQ
YLMEVTHDLR LRLKNYMMPA KGKKTDKQPL QKPSHCTIYV AKNYPPWQHT TLSVLRKHFE
ANNRKLPDNK VIASELGSMP ELKKYMKKVM PFVAMIKENL EKMGPRILDL QLEFDEKAVL
MENIVYLTNS LELEHIEVKF ASEAEDKIRE DCCPGKPLNV FRIEPGVSIS LVNPQPSNGH
FSTKIEIRQG DNCDSIIRRL MKMNRGIKDL SKVKLMRFDD PLLGPRRVPV LGKEHTEKTP
ISEHAVFNVD LMSKKIHLTE NGIRVDIGDT IIYLVH
