ID SYLM_SCHPO Reviewed; 874 AA.
AC Q09828;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 27-MAR-2024, entry version 153.
DE RecName: Full=Putative leucine--tRNA ligase, mitochondrial;
DE EC=6.1.1.4;
DE AltName: Full=Leucyl-tRNA synthetase;
DE Short=LeuRS;
DE Flags: Precursor;
GN ORFNames=SPAC4G8.09;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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; CU329670; CAA91210.1; -; Genomic_DNA.
DR PIR; T38854; S62486.
DR RefSeq; NP_593069.1; NM_001018467.2.
DR AlphaFoldDB; Q09828; -.
DR SMR; Q09828; -.
DR STRING; 284812.Q09828; -.
DR MaxQB; Q09828; -.
DR PaxDb; 4896-SPAC4G8-09-1; -.
DR EnsemblFungi; SPAC4G8.09.1; SPAC4G8.09.1:pep; SPAC4G8.09.
DR GeneID; 2543476; -.
DR KEGG; spo:SPAC4G8.09; -.
DR PomBase; SPAC4G8.09; -.
DR VEuPathDB; FungiDB:SPAC4G8.09; -.
DR eggNOG; KOG0435; Eukaryota.
DR HOGENOM; CLU_004427_2_0_1; -.
DR InParanoid; Q09828; -.
DR OMA; DDVDWAD; -.
DR PhylomeDB; Q09828; -.
DR PRO; PR:Q09828; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005759; C:mitochondrial matrix; IC:PomBase.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0004823; F:leucine-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; ISO:PomBase.
DR GO; GO:0000372; P:Group I intron splicing; ISO:PomBase.
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; 3.40.50.620; HUPs; 2.
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..21
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 22..874
FT /note="Putative leucine--tRNA ligase, mitochondrial"
FT /id="PRO_0000035811"
FT MOTIF 67..77
FT /note="'HIGH' region"
FT MOTIF 628..632
FT /note="'KMSKS' region"
FT BINDING 631
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 874 AA; 100886 MW; 0F9550E7E720AFC6 CRC64;
MLKSVGTNGR KVPKIASLCN FLKFNKNIHS NPDFLAIAEN WKSYWKSHYP FVKNDKGKKK
YILSMFPYPS GLLHIGHVRV YTISDILSRY YRMKGYKVIH PMGWDAFGLP AENAAIENGI
SASSWTYENI KKMKEQTYHM NIYFDWDREI STCNPDYYKW SQYLFLQMFH KGLAYQAEAT
VNWDPVDCTV LANEQVDSHG RSWRSGAIVE KKNLRQWFLK ISDYSDQLLD DLETLPKWPD
KVKKMQRNWI GRTTGFEISF PLLNDKETLT VFTTKPETII DVSFIALSKN HKLVLLESQK
DPSLAEHLRN ESLLDKGYQL PCFAKNPVTG KALPIFYAPY VLDCYGTGAV MGAPIHDRRD
FEFAKRNNII FSKESCIGSY FTNEGKELLN HHDSSNLMDI KQKMLQQKIV SYLEEKKLAK
RVKNYRLKDW LISRQRFWGT PIPMVHCETC GAVPVPESEL PVKLPDLDKI YEKGTSPLSN
LETWMKTTCP KCHGPATRET DTMDTFVDSS WYYFRFLDSK NSELPVGLAS ASSLMPVDIY
IGGVEHSILH LLYSRFFSKF MKDIGLWNGD KYLNEPFTQL ITQGMVHGLT YTTMSDERIL
NPKEVQKIGD EYFLISNPKE KVQLSYQKMS KSKHNGVDPI RTIQKYGSDI IRAYIIFSAP
VEGVLLWNEN AIMGTKRWLT KIWNCVHQLL EREKKMSDAM RQTKLTIVDD HNSRKLESQY
NEFISQCSAH YENVFSLNLV ISDAMKLTNN IADALKNNKV NIGTIKASLE VLVKCIAPII
PCFSSECWLL LGHNSSVYSN WPISKNKKEN MEEPVTIPVQ INGKVRFKIE MPKLNDENEI
LNFVLETNDG KRWLSNKKVL KSFVKQKIIS LVTD
//
