ID   SYLM_NEUCR              Reviewed;         994 AA.
AC   P15181; Q7RVC8;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   27-MAR-2024, entry version 168.
DE   RecName: Full=Leucine--tRNA ligase, mitochondrial;
DE            EC=6.1.1.4;
DE   AltName: Full=Leucyl-tRNA synthetase;
DE            Short=LeuRS;
DE   Flags: Precursor;
GN   Name=leu-5; ORFNames=99H12.170, NCU03814;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2574823; DOI=10.1128/mcb.9.11.4631-4644.1989;
RA   Chow C.M., Metzenberg R.L., RajBhandary U.L.;
RT   "Nuclear gene for mitochondrial leucyl-tRNA synthetase of Neurospora
RT   crassa: isolation, sequence, chromosomal mapping, and evidence that the
RT   leu-5 locus specifies structural information.";
RL   Mol. Cell. Biol. 9:4631-4644(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA   Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT   genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; M30472; AAA33599.1; -; Genomic_DNA.
DR   EMBL; AL451018; CAC18253.1; -; Genomic_DNA.
DR   EMBL; CM002240; EAA31967.1; -; Genomic_DNA.
DR   PIR; A33474; SYNCLM.
DR   RefSeq; XP_961203.1; XM_956110.2.
DR   AlphaFoldDB; P15181; -.
DR   SMR; P15181; -.
DR   STRING; 367110.P15181; -.
DR   PaxDb; 5141-EFNCRP00000003503; -.
DR   EnsemblFungi; EAA31967; EAA31967; NCU03814.
DR   GeneID; 3877331; -.
DR   KEGG; ncr:NCU03814; -.
DR   VEuPathDB; FungiDB:NCU03814; -.
DR   HOGENOM; CLU_004427_0_0_1; -.
DR   InParanoid; P15181; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 2876972at2759; -.
DR   Proteomes; UP000001805; Chromosome 2, Linkage Group V.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0006429; P:leucyl-tRNA aminoacylation; IBA:GO_Central.
DR   GO; GO:0032543; P:mitochondrial translation; IBA:GO_Central.
DR   CDD; cd00812; LeuRS_core; 1.
DR   Gene3D; 3.10.20.590; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR   HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
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; IPR015413; Methionyl/Leucyl_tRNA_Synth.
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:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 2.
DR   Pfam; PF13603; tRNA-synt_1_2; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 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   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Mitochondrion;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..52
FT                   /note="Mitochondrion"
FT   CHAIN           53..994
FT                   /note="Leucine--tRNA ligase, mitochondrial"
FT                   /id="PRO_0000035808"
FT   MOTIF           93..103
FT                   /note="'HIGH' region"
FT   MOTIF           697..701
FT                   /note="'KMSKS' region"
FT   BINDING         700
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   994 AA;  109854 MW;  2ADB26302A8465F9 CRC64;
     MPLICARPLG RLVPKLGASL RPVLSSHAAS PRRPVGVALE QHLGTESWKR FYADHKLDLL
     ALDQKWRQKW AESSREKGNK EDEKNKYVLP MFPYPSGHLH LGHLRVYTIA DVIARFQTLQ
     GHKVLLPMGW DAFGLPAENA AIERGINPAT WTKANIAKMK EQLGHMNGSW DWNCELATCD
     PDFYKHTQKI FLALHEKGLA YQAEAEVNYD PVDKTVLANE QVDANGCSWR SGARVEKRKL
     KQWFLKISEF RESLLKDLET LAKNEAWPER VLAMQKNWLG KSKGATVKFP VLAFGQGTPS
     AIEVFTSRPD TLFGVQYIAL AATHPSVQQL AKSDPELQAF LSTLPGLSPD SKVGYLLPHI
     RAVNPLAYHE ETPEDTKVSL PIYVAPYVLG DYGEGAVMGV PGHDLRDHAF WKEHHYDAPV
     RFVLAASEDE STTAMPNEPF TEHGVMNANS GIFKGKSSKE AGEMLVKLLE PAGLAKETEK
     WRLRDWLISR QRYWGTPIPI VHCGSCGTVP VPDEQLPVEL PEVDEHWAGK KTGNPLESQT
     DWINTSCPKC GGEAKRDTDT MDTFVDSSWY YMRFIDAHNK EAPFSPEKAK VLTPVDLYIG
     GVEHAILHLL YSRFIYKFLM TSSFAGKEAE SAEAAESASS EVYEPFKRLI TQGMVHGKTY
     TDPATGRFLK PDEVDLSDPH QPKVVATGAL ANVSYEKMSK SKHNGVDPTT FIAQYGADAT
     RAHILFQAPV SEILDWDESK ITGVTRWLSR VHDLVQKIAC SSTSETPSSA STVKAFFEQQ
     QQQPESVADP AKLDASITIW REVQRTISSV TASYNKVYTL NTVISDLMSL TNVIASPSNY
     DAADPLIRRE AVSALIRMMA PVAPAFAEEC WHVLFPESSS SSLFSGSGSG SGSGSGDEQA
     ARFPVPDGTE GLLKSRKQTC AVQLNGKTKF AVEIGTPPAG LLEKSAEEKL REFIVGEVLK
     TEEGRAKLEG RGVDVSKAKK VIVVRGGKLL NVVM
//