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