ID   SYIM_SCHPO              Reviewed;         973 AA.
AC   Q9USL3;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Isoleucine--tRNA ligase, mitochondrial;
DE            EC=6.1.1.5;
DE   AltName: Full=Isoleucyl-tRNA synthetase;
DE            Short=IleRS;
GN   Name=ism1; ORFNames=SPCC18B5.08c;
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   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       Mitochondrion matrix {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; CU329672; CAB52155.1; -; Genomic_DNA.
DR   PIR; T41201; T41201.
DR   RefSeq; NP_587938.1; NM_001022929.2.
DR   AlphaFoldDB; Q9USL3; -.
DR   SMR; Q9USL3; -.
DR   STRING; 4896.SPCC18B5.08c.1; -.
DR   MaxQB; Q9USL3; -.
DR   PaxDb; Q9USL3; -.
DR   EnsemblFungi; SPCC18B5.08c.1; SPCC18B5.08c.1:pep; SPCC18B5.08c.
DR   GeneID; 2539323; -.
DR   KEGG; spo:SPCC18B5.08c; -.
DR   PomBase; SPCC18B5.08c; ism1.
DR   VEuPathDB; FungiDB:SPCC18B5.08c; -.
DR   eggNOG; KOG0433; Eukaryota.
DR   HOGENOM; CLU_001493_7_2_1; -.
DR   InParanoid; Q9USL3; -.
DR   OMA; HLGTAWN; -.
DR   PhylomeDB; Q9USL3; -.
DR   PRO; PR:Q9USL3; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005759; C:mitochondrial matrix; IC:PomBase.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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:0006428; P:isoleucyl-tRNA aminoacylation; ISS:PomBase.
DR   GO; GO:0032543; P:mitochondrial translation; IBA:GO_Central.
DR   CDD; cd07960; Anticodon_Ia_Ile_BEm; 1.
DR   Gene3D; 3.40.50.620; -; 2.
DR   Gene3D; 3.90.740.10; -; 1.
DR   HAMAP; MF_02002; Ile_tRNA_synth_type1; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR033708; Anticodon_Ile_BEm.
DR   InterPro; IPR002301; Ile-tRNA-ligase.
DR   InterPro; IPR023585; Ile-tRNA-ligase_type1.
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   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.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Mitochondrion;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..973
FT                   /note="Isoleucine--tRNA ligase, mitochondrial"
FT                   /id="PRO_0000339654"
FT   MOTIF           87..97
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000250"
FT   MOTIF           625..629
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000250"
FT   BINDING         628
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   973 AA;  111255 MW;  7061018D18A6C43B CRC64;
     MKFSYISSLP KGHNHICCKQ AGRFLSSQAD LKKYSESLCL PKTSFPIKPN VKGNNEKYFK
     SITSDLYEWQ KENLNKEDSF VLLDGPPFAN GRLHIGHALN KILKDIINRW QLLKGRSVHY
     VPGWDCHGLP IESKAIKANA ERKSSLEIRK IAKDFANSAV QEQLMMFQRM AVMGDWPSRY
     ITMSDKFEIA ELKVFLSLLQ KDLIFRQNKP VYWSSSSRSA LAESEIEYDD NHVSTSIYFT
     FPVNSFSIDG CEYNNVKALV WTTTPWTIPS NLALSYHPEI NYGLYQHNNS IYLMSDNLVP
     NLDFMQGAKR LASCPSDIIS SFTYENPLLP KQSFPFLQSN YVTNDIGTGI VHVAPGHGME
     DYLLGLENNL RPFSPLDDYG RYTKEALDGS LEGLEVLGDG GKKVISIMKN QNMIVKVSPY
     KHRYPYDWRT HKPLILRATP QWFISLENER KTAIKALDSV KMIPPNSRAR LLGFLNGRPE
     WCISRQRAWG LPIPVLYEKG TKIPLLTVKS VSYIIEKMEV EGVDSWFNDT ENNGHAQWVH
     PDYRNKEYIR GTETLDVWFD SGTSWTTIAP RKNKPLIDLC LEGSDQHRGW FQSLLLTYTA
     YQSKPEAPFS TLFTHGFIFD ERGQKQSKSL GNVTDPEDVI NGKLLKGKKL PYGVDLLRLW
     VASCDSTNDT NLGPNILTQV GESLKKWRLT SRFCLGNLHD WNTSSSVDVG ELRGIDKLAL
     VQLDKFQTEI RELYESYSIN KVVHHLNYFM NSFLSSTYFD AVKDRLYADL PNSVSRRSVQ
     TVLYHSLLTL IWAISPITPL LAQEIWQSLP DSYLNSSYQT PFHAGETHLI SSLRSKVDLL
     DRKFLIKEYL VLQQLKYSIN LLITAARENL TIKNSLEAYV VIKSKSQSLL SFLKNYSSDL
     PFLFNTSKVF INEIPENLKL ASVTQPEVQL DYGVANISLF FSNQQKCLRC WMHTAHEDGL
     CDRCESVLAQ LKR