SYLC_SCHPO
ID SYLC_SCHPO Reviewed; 1111 AA.
AC Q10490;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Putative leucine--tRNA ligase, cytoplasmic;
DE EC=6.1.1.4;
DE AltName: Full=Leucyl-tRNA synthetase;
DE Short=LeuRS;
GN Name=lrs1; ORFNames=SPAC26F1.13c;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 739-1110.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
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 {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAA97370.1; -; Genomic_DNA.
DR EMBL; D89170; BAA13832.1; -; mRNA.
DR PIR; T38407; T38407.
DR PIR; T42535; T42535.
DR RefSeq; NP_594882.1; NM_001020311.2.
DR AlphaFoldDB; Q10490; -.
DR SMR; Q10490; -.
DR BioGRID; 279123; 5.
DR STRING; 4896.SPAC26F1.13c.1; -.
DR iPTMnet; Q10490; -.
DR MaxQB; Q10490; -.
DR PaxDb; Q10490; -.
DR PRIDE; Q10490; -.
DR EnsemblFungi; SPAC26F1.13c.1; SPAC26F1.13c.1:pep; SPAC26F1.13c.
DR GeneID; 2542670; -.
DR KEGG; spo:SPAC26F1.13c; -.
DR PomBase; SPAC26F1.13c; lrs1.
DR VEuPathDB; FungiDB:SPAC26F1.13c; -.
DR eggNOG; KOG0437; Eukaryota.
DR HOGENOM; CLU_004174_1_1_1; -.
DR InParanoid; Q10490; -.
DR OMA; AWNMAFQ; -.
DR PhylomeDB; Q10490; -.
DR PRO; PR:Q10490; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
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; ISS:PomBase.
DR GO; GO:0002181; P:cytoplasmic translation; NAS:PomBase.
DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; ISS:PomBase.
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 1: Evidence at protein level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..1111
FT /note="Putative leucine--tRNA ligase, cytoplasmic"
FT /id="PRO_0000152154"
FT MOTIF 74..84
FT /note="'HIGH' region"
FT MOTIF 737..741
FT /note="'KMSKS' region"
FT BINDING 740
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1111 AA; 126452 MW; 88D654634F0415A9 CRC64;
MATTEPSVEQ LETKTAKLKL ENTTKRDTLI ELEKKYQQKW QEEKAFEVDA PLEDVPIDEL
RKKYPKFFGN MPYPYMNGAL HLGHAFTLSK VEFTTAFERL NGKRVLFPMG FHCTGMPICA
SADRLSREIE MFGPSFDVPE EKEEEVEVEV KTPNAREDVT KHSGKKSKAA AKTAAVKYQF
QIMESLGVPR TEIHKFADAK YWLSYFPPLC QRDCTEFGLG IDWRRSFITT DVNPYYDSFV
RWQVNHLHDS GKIKFGERYT VYSIKDGQPC MDHDRKSGEG VGPQEYTGIK MEVLEFPEAA
RKALQSIDLS NKKVCMIAAT LRPETMYGQT NCYVGPNITY GIYESNVPNE LFICTRRAAN
NMAYQKLSKE RGVVSELGTI KGQDLIGALV NAPLSVHKQV YVLPMETVLA TKGTGVVTSV
PSDSPDDFAT LTELRKKAEF YHLNPEWMKY EAVPIIRTPS YGDMCAEFLC KKLKIQSPKD
VKQLAQAKEL AYKECFYQGT MIIGKYSGEK VETAKPKVRK ELIDQGLAFV YNEPEGQVIS
RSGDDCIVAL CDQWFLDYGE ASWKAVTEKA LDRLNTFSPE VRNGFLKTLD WLSQWACARS
YGLGTRLPWD PQFLVESLTD STIYMAYYTI CHLLHSDVYG KVPGALNIKP EQMTPEVWDH
VFRQAPKPKN TSISDEALAR LCREFQYFYP FDIRASGKDL VPNHLTFCLY THTAIFDEKY
WPKGIRANGH LLMNGEKMSK STGNFMTLHE ATKKFGADAT RLALADAGDT VDDANFEEAL
ANSAILRLYT QEAWCKEMME NLDNLRTGPY NFHDKVFENE INQLIESSRE AFSATLFKAA
LKSCFYDLQN ARDWYREVTA DRKMHRDLVC RWIETQVLLL ATFAPHWSEH IWLTTLKKPQ
SIHVSGRFPQ VSSPVNTALS NSLLYIRTLS RVIREAEAAQ LKRQKKGKGM LFDPSKPKRL
TVFVAEKFPE WQAQYVALLQ KYYNESENKF DDKAIISSVD KKEMKRAMPF IQQFKQSVIN
RGEHVSANSI FSRELGFNEL EVLREVKPYL VRNVGIQELR IVLLQKPADK SSAAIGLVES
GSDAGATVEI APNFANTVPG QPTFLFENVS A
