ID   SYLM_PONAB              Reviewed;         903 AA.
AC   Q5RDP4;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   RecName: Full=Probable leucine--tRNA ligase, mitochondrial;
DE            EC=6.1.1.4;
DE   AltName: Full=Leucyl-tRNA synthetase;
DE            Short=LeuRS;
DE   Flags: Precursor;
GN   Name=LARS2;
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=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; CR857860; CAH90113.1; -; mRNA.
DR   RefSeq; NP_001127239.1; NM_001133767.1.
DR   AlphaFoldDB; Q5RDP4; -.
DR   SMR; Q5RDP4; -.
DR   STRING; 9601.ENSPPYP00000015598; -.
DR   GeneID; 100174294; -.
DR   KEGG; pon:100174294; -.
DR   CTD; 23395; -.
DR   eggNOG; KOG0435; Eukaryota.
DR   InParanoid; Q5RDP4; -.
DR   OrthoDB; 2876972at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005759; C:mitochondrial matrix; 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   CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR   CDD; cd00812; LeuRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR002302; Leu-tRNA-ligase.
DR   InterPro; IPR025709; Leu_tRNA-synth_edit.
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; TIGR00396; leuS_bact; 1.
DR   PANTHER; PTHR43740:SF3; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 3.
DR   Pfam; PF13603; tRNA-synt_1_2; 1.
DR   PRINTS; PR00985; TRNASYNTHLEU.
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   2: Evidence at transcript level;
KW   Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Mitochondrion;
KW   Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..903
FT                   /note="Probable leucine--tRNA ligase, mitochondrial"
FT                   /id="PRO_0000229758"
FT   MOTIF           92..102
FT                   /note="'HIGH' region"
FT   MOTIF           639..643
FT                   /note="'KMSKS' region"
FT   BINDING         642
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         68
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VDC0"
FT   MOD_RES         236
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15031"
FT   MOD_RES         711
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15031"
SQ   SEQUENCE   903 AA;  101941 MW;  0B17DCCE82070CDB CRC64;
     MASVWQRLGF YASLLKRQLN GGPDVIKWER RVIPGCTRSI YSATGKWTKE YTLQTRKDVE
     KWWHQRIKEQ ASKISEADKS KPKFYVLSMF PYPSGKLHMG HVRVYTISDT IARFQKMRGM
     QVINPMGWDA FGLPAENAAV ERNLHPESWT QSNIKHMRKQ LDRLGLCFSW DREITTCLPD
     YYKWTQYLFI KLYEAGLAYQ KEALVNWDPV DQTVLANEQV DEHGCSWRSG AKVEQKYLRQ
     WFIKTTAYAK AMQDALADLP EWYGIKGMQA HWIGDCVGCH LDFTLKVHGQ ATGEKLTAYT
     ATPEAIYGTS HVAISPSHRL LHGHSSLKEA LRMALVPGKD CLTPVMAVNM LTQQEVPVVI
     LAKADLEGSL DSKIGIPSTS SEDTILAQTL GLAYSEVIET LPDGTERLSS SAEFTGMTRQ
     DAFLALTQKA RGKRVGGDVT SDKLKDWLIS RQRYWGTPIP IVHCPVCGPT PVPLEDLPVT
     LPNIASFTGK GGSPLAMASE WVNCSCPRCK GAAKRETDTM DTFVDSAWYY FRYTDPHNPH
     SPFNTAVADY WMPVDLYIGG KEHAVMHLFY ARFFSHFCHD QKMVKHREPF HKLLAQGLIK
     GQTFRLPSGQ YLQREEVDLT GSVPVHAKTK EKLEVTWEKM SKSKHNGVDP EEVVEQYGID
     TIRLYILFAA PPEKDILWDV KTDALPGVLR WQQRLWTLTT RFIEARASGK SPQPQLLSNK
     EKAEARKLWE YKNSVISQVT THFTEDFSLN SAISQLMGLS GALSQASQSV ILHSPEFEDA
     LCALMVMAAP MAPHVTSEIW AGLALVPRKL CAHYTWDVSV LLQAWPAVDP EFLQEPEVVQ
     MAVLINNKAC GKIPVPQQVA RDQDKVHEFV LQSELGVRLL QGRSIKKSFL SPRTALINFP
     VQD
//