ID   SYIC_SCHPO              Reviewed;        1064 AA.
AC   O13651;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Isoleucine--tRNA ligase, cytoplasmic;
DE            EC=6.1.1.5;
DE   AltName: Full=Isoleucyl-tRNA synthetase;
DE            Short=IleRS;
GN   Name=irs1; ORFNames=pi058, SPBC8D2.06;
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=10620777;
RX   DOI=10.1002/(sici)1097-0061(20000115)16:1<71::aid-yea505>3.0.co;2-5;
RA   Machida M., Yamazaki S., Kunihiro S., Tanaka T., Kushida N., Jinno K.,
RA   Haikawa Y., Yamazaki J., Yamamoto S., Sekine M., Oguchi A., Nagai Y.,
RA   Sakai M., Aoki K., Ogura K., Kudoh Y., Kikuchi H., Zhang M.Q., Yanagida M.;
RT   "A 38 kb segment containing the cdc2 gene from the left arm of fission
RT   yeast chromosome II: sequence analysis and characterization of the genomic
RT   DNA and cDNAs encoded on the segment.";
RL   Yeast 16:71-80(2000).
RN   [2]
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   [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).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-
CC         isoleucyl-tRNA(Ile); Xref=Rhea:RHEA:11060, Rhea:RHEA-COMP:9666,
CC         Rhea:RHEA-COMP:9695, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58045, ChEBI:CHEBI:78442, ChEBI:CHEBI:78528,
CC         ChEBI:CHEBI:456215; EC=6.1.1.5;
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; AB004538; BAA21439.1; -; Genomic_DNA.
DR   EMBL; CU329671; CAA17821.1; -; Genomic_DNA.
DR   PIR; T40751; T40751.
DR   RefSeq; NP_595569.1; NM_001021464.2.
DR   AlphaFoldDB; O13651; -.
DR   SMR; O13651; -.
DR   BioGRID; 277759; 6.
DR   DIP; DIP-59122N; -.
DR   IntAct; O13651; 1.
DR   STRING; 4896.SPBC8D2.06.1; -.
DR   iPTMnet; O13651; -.
DR   SwissPalm; O13651; -.
DR   MaxQB; O13651; -.
DR   PaxDb; O13651; -.
DR   PRIDE; O13651; -.
DR   EnsemblFungi; SPBC8D2.06.1; SPBC8D2.06.1:pep; SPBC8D2.06.
DR   GeneID; 2541245; -.
DR   KEGG; spo:SPBC8D2.06; -.
DR   PomBase; SPBC8D2.06; irs1.
DR   VEuPathDB; FungiDB:SPBC8D2.06; -.
DR   eggNOG; KOG0434; Eukaryota.
DR   HOGENOM; CLU_001493_1_0_1; -.
DR   InParanoid; O13651; -.
DR   OMA; KMMAPFT; -.
DR   PhylomeDB; O13651; -.
DR   PRO; PR:O13651; -.
DR   Proteomes; UP000002485; Chromosome II.
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; ISM:PomBase.
DR   GO; GO:0004822; F:isoleucine-tRNA ligase activity; ISS:PomBase.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0002181; P:cytoplasmic translation; NAS:PomBase.
DR   GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IBA:GO_Central.
DR   CDD; cd07961; Anticodon_Ia_Ile_ABEc; 1.
DR   Gene3D; 3.40.50.620; -; 2.
DR   HAMAP; MF_02003; Ile_tRNA_synth_type2; 1.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR033709; Anticodon_Ile_ABEc.
DR   InterPro; IPR002301; Ile-tRNA-ligase.
DR   InterPro; IPR023586; Ile-tRNA-ligase_type2.
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; PTHR42780; PTHR42780; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   PRINTS; PR00984; TRNASYNTHILE.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF50677; SSF50677; 1.
DR   TIGRFAMs; TIGR00392; ileS; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..1064
FT                   /note="Isoleucine--tRNA ligase, cytoplasmic"
FT                   /id="PRO_0000098603"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           597..601
FT                   /note="'KMSKS' region"
FT   BINDING         600
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1064 AA;  122916 MW;  94AEBA7378BEB665 CRC64;
     MSFNVPKEEE KIVEFWREID AFHTQLKLSQ GRPTYTFFDG PPFATGRPHH GHLLASTIKD
     SVTRYACLKG YHVERRFGWD THGLPVEHEI DKKLGITGSD DVMAMGIDKY NAECRKIVMT
     YASEWRATVE RLGRWIDFDN DYKTLYPSFM ESVWWVFKEL HTKGKVYRGY RVMPYSTACT
     TPLSNFEAQQ NYKEVPDPAI VVAFQSISDP EVSFLAWTTT PWTLPSNLAL AVHPDLQYIK
     ILDKDSNKKY ILMESCLGIL YKNPKKANFE ILERFQGKAL DGQKYEPLFP YFKSTFGERA
     FKLYSADYVE EGSGTGIVHQ APAFGEADYD AAWAAGIIDA DHQPPCPVDE QGLLTSEITD
     FAGQYVKDAD KEIIRSLKAS GHLVKHSQIF HSYPFCWRSD TPLIYRAVPS WFVRVKEITN
     EMVENVMSTH WVPQNIRDKR FANWLKNARD WNISRNRYWG TPIPLWVSDD YEEVVCIGSI
     KELEELSGVS NITDIHRDSI DHITIPSKKG KGTLHRVSEV FDCWFESGSM PYASRHYPFE
     RIEEFKHGFP ADFISEGVDQ TRGWFYTLTV LGTLLFDKAP YKNVIVSGLV MAEDGKKMSK
     RLKNYPEPNL IIEKYGSDAL RLYLINSPVV RAEILKFKED GVREVVTRVL IPWWNSYKFF
     EAQAALYKKV TGKDFVFDDA ATLSSNVMDR WILARCQSLI GFVDEEMKQY RLYTVVPQLL
     GLIEEMTNWY IRFNRRRLKG EDGEIETINA LNVLFEVLFT LVRIMGPFTP FITENIYQHL
     RNYMPIDKNE ISLRSVHFLP FPTYKSELDD ETVLRRVKRM QTIIELARYV REQNNISLKT
     PLKTLIVILT NEEYLEDAKL LERYIAEELN VREVVFTSNE EKYGVVYSVQ ADWPVLGKKL
     RKDMARVKKA LPNVTSEEVK EFQKNKKMVL DGIELVEGDL QIIRSVEVKN EFLKSNTDGI
     CIVLLDIEID AQLQAEGLAR EVINRVQRLR KKSNLQVTDD VRMTYKIKND TIGLESAVDS
     NEALFSKVLR RPIEKETGAD ESNIIASEEQ DVQGATFLLS LLRL