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SYLC_NEUCR
ID   SYLC_NEUCR              Reviewed;        1123 AA.
AC   P10857; Q7RVI3;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 2.
DT   03-AUG-2022, entry version 161.
DE   RecName: Full=Leucine--tRNA ligase, cytoplasmic;
DE            EC=6.1.1.4;
DE   AltName: Full=Leucyl-tRNA synthetase;
DE            Short=LeuRS;
GN   Name=leu-6; ORFNames=B10K17.030, NCU09463;
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=2532300; DOI=10.1128/mcb.9.11.4645-4652.1989;
RA   Chow C.M., RajBhandary U.L.;
RT   "Regulation of the nuclear genes encoding the cytoplasmic and mitochondrial
RT   leucyl-tRNA synthetases of Neurospora crassa.";
RL   Mol. Cell. Biol. 9:4645-4652(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).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-116.
RX   PubMed=2842224; DOI=10.1093/genetics/119.4.805;
RA   Benarous R., Chow C.M., RajBhandary U.L.;
RT   "Cytoplasmic leucyl-tRNA synthetase of Neurospora crassa is not specified
RT   by the leu-5 locus.";
RL   Genetics 119:805-814(1988).
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: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; M30473; AAA33593.1; -; Genomic_DNA.
DR   EMBL; BX842596; CAE75711.1; -; Genomic_DNA.
DR   EMBL; CM002237; EAA33982.1; -; Genomic_DNA.
DR   EMBL; X13021; CAA31439.1; -; Genomic_DNA.
DR   PIR; A33475; SYNCLC.
DR   RefSeq; XP_963218.1; XM_958125.3.
DR   AlphaFoldDB; P10857; -.
DR   SMR; P10857; -.
DR   STRING; 5141.EFNCRP00000009296; -.
DR   PRIDE; P10857; -.
DR   EnsemblFungi; EAA33982; EAA33982; NCU09463.
DR   GeneID; 3879366; -.
DR   KEGG; ncr:NCU09463; -.
DR   VEuPathDB; FungiDB:NCU09463; -.
DR   HOGENOM; CLU_004174_1_1_1; -.
DR   InParanoid; P10857; -.
DR   OMA; AWNMAFQ; -.
DR   Proteomes; UP000001805; Chromosome 6, Linkage Group II.
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; IBA:GO_Central.
DR   GO; GO:0006429; P:leucyl-tRNA aminoacylation; IBA:GO_Central.
DR   GO; GO:1903432; P:regulation of TORC1 signaling; IEA:EnsemblFungi.
DR   Gene3D; 3.40.50.620; -; 1.
DR   Gene3D; 3.90.740.10; -; 1.
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   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..1123
FT                   /note="Leucine--tRNA ligase, cytoplasmic"
FT                   /id="PRO_0000152153"
FT   MOTIF           84..94
FT                   /note="'HIGH' region"
FT   MOTIF           757..761
FT                   /note="'KMSKS' region"
FT   BINDING         760
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1123 AA;  126399 MW;  78945AFC3D06FFBF CRC64;
     MADTAAVAKG VENLSVSASK TKELKGTEKR DTLIEIEKRY QQKWEQEGVF EVDAPSTAEF
     PLDAITPDEL RQKHPKFFGT IAYPYMNGRL HAGHAFSFSK IEYHTGFARM QGKRALFPQG
     YHCTGLPIKA SADKLVKEIE MFGQEFERYK EDEVVEGAAP AAAAAPKTKE DLTKFNAKKG
     KTVAKTGGAK YQFQILKSLG IPVSEIHKFA DPQYWLHYFP PECKKDLTNF GARIDWRRQF
     VTTDANPYYD AFVRWQMNRL LELNKIKFGK RYTIYSIKDG QPCMDHDRSE GEGVLPQEYT
     ALKLKVTEWA PKAAEALKGK LPEGANVYLC PATLRPETMY GQVCCFVGPA LKYGVFKAAE
     NEYFVITERA AKNMAYQGIF EKEGVIEKAA DIVGSDLIGT LVNAPLSVHK EVYVLPMDTV
     LATKGTGVVT SVPSDSPDDC AMMTELAKKP EFYGIQKEWA EKEIVSVIKT PTSDLLAPYL
     VKKLKINSPK DAKQLLEAKE LAYKEGFYQG IMNYGDFKGE KVETAKPKVR QQLIDAGDAF
     AYSEPENKVV SRSGDECSVA LMDQWYIDYG EDSWRTVLYD YVENKDGKGI NTYYADTQHA
     FKGVIGWLKQ WACARTYGLG SKLPWDPNFL VESLSDSTVY MAYYTVAHWL HRDLFGREKG
     KGNIGADQMI DEVWDYIFCR TELSDHLVTK SGIPKETLDS MRREFQYFYP LDIRVSGKDL
     IPNHLTFWLY NHIALFPREY WPKSVRANGH LQLNGEKMSK STGNFMTLDD VVKKYGADAA
     RVALADAGDG ISDSNFVEDV ADNTILRFYT NKEWIEETLK DESLRTGELN SFQDALFDNE
     MNALVNEARK HYEETSYKLA LKAAHYDFLN ARDMYREACA AAGIPLHKDL VTKYIRLQAL
     VITPIAPHWA DYVWQECLGE PKSIQFARWP EVPAANPALT AARDYVRTTS SAINSAEAAQ
     LKKMAKGRQS DFDPKKPKKL TIFATENFPT WQAKYIDLLS EVWDAATGTQ KIDDKELNGR
     IAKMGEMKKA MPFVQALKKR LKDGEPAEQI LSRKLSFDEK ATLLAMIPGL KRTAGLESVQ
     VVLVEEGSKT GKDLTNGGAE IEVTAPMAEA ALPGQPSFFF TNV
 
 
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