SYLM_NEUCR
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 03-AUG-2022, entry version 162.
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; 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 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:0097157; F:pre-mRNA intronic binding; IEA:EnsemblFungi.
DR GO; GO:0000372; P:Group I intron splicing; IEA:EnsemblFungi.
DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; IBA:GO_Central.
DR GO; GO:0032543; P:mitochondrial translation; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IEA:EnsemblFungi.
DR Gene3D; 3.40.50.620; -; 2.
DR Gene3D; 3.90.740.10; -; 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 PANTHER; PTHR43740; PTHR43740; 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; SSF47323; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00396; leuS_bact; 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
