ID   SYIM_DICDI              Reviewed;        1034 AA.
AC   Q54CE4;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 132.
DE   RecName: Full=Probable isoleucine--tRNA ligase, mitochondrial;
DE            EC=6.1.1.5;
DE   AltName: Full=Isoleucyl-tRNA synthetase;
DE            Short=IleRS;
DE   Flags: Precursor;
GN   Name=mileS; ORFNames=DDB_G0293030;
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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: Mitochondrion matrix {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; AAFI02000199; EAL60867.1; -; Genomic_DNA.
DR   RefSeq; XP_629275.1; XM_629273.1.
DR   AlphaFoldDB; Q54CE4; -.
DR   SMR; Q54CE4; -.
DR   STRING; 44689.Q54CE4; -.
DR   PaxDb; 44689-DDB0231256; -.
DR   EnsemblProtists; EAL60867; EAL60867; DDB_G0293030.
DR   GeneID; 8628997; -.
DR   KEGG; ddi:DDB_G0293030; -.
DR   dictyBase; DDB_G0293030; mileS.
DR   eggNOG; KOG0433; Eukaryota.
DR   HOGENOM; CLU_001493_7_1_1; -.
DR   InParanoid; Q54CE4; -.
DR   OMA; HCWRCKT; -.
DR   PhylomeDB; Q54CE4; -.
DR   PRO; PR:Q54CE4; -.
DR   Proteomes; UP000002195; Chromosome 6.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; ISS:dictyBase.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004822; F:isoleucine-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IBA:GO_Central.
DR   GO; GO:0032543; P:mitochondrial translation; IBA:GO_Central.
DR   CDD; cd07960; Anticodon_Ia_Ile_BEm; 1.
DR   Gene3D; 1.10.730.20; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   Gene3D; 1.10.10.830; Ile-tRNA synthetase CP2 domain-like; 1.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 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   NCBIfam; TIGR00392; ileS; 1.
DR   PANTHER; PTHR42765:SF1; ISOLEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR42765; SOLEUCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   PRINTS; PR00984; TRNASYNTHILE.
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..32
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           33..1034
FT                   /note="Probable isoleucine--tRNA ligase, mitochondrial"
FT                   /id="PRO_0000327970"
FT   MOTIF           94..104
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000250"
FT   MOTIF           655..659
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000250"
FT   BINDING         658
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1034 AA;  118422 MW;  CD81811C34E14FB9 CRC64;
     MISLNNSFFN KRVIVNSFNN YKRSFGTKSQ NEESAIVDSN HSFAHTLNLP KTTFSMKANA
     ATREPTLLKD PYKLYKWQLE NNKGENWVFH DGPPYANGDL HMGHALNKIL KDIVNRYKVL
     KGFKVNYIPG WDCHGLPIEQ QAFKKLKKSS DMKASDIRKI AGDFARKEIE KQSKGFQEMG
     ILGDWENPYK TLDYGYEVEQ IQTFYDMFNK GYIYRGVKPV HWSPSSRTAL ADAELEYNNN
     HTSKSIFVKF NVKSLSNHIL NNLPTTSDIN KAEMVISAII WTTTPWTIPA NQAICVNSEM
     DYILVKPIES EQYRNEMFII SKERLESLTK SFNIGELKVI LEFKGEQLKG TITKHPQYDR
     ESPIITGDHV IEGSGTGLVH TAPGHGVEDF QICQQQYPDL KVLSPVNDLG CFTDEVGEKF
     VGLEVLGDGN EAVINDLETI GSLLHKEDYI HKYPYDWRTK KPIIIRTTLQ WFVGLKNIQK
     TALQSIERVN MVPPSGSNRL SSMIGKRTDW CISRQRVWGC PIPVLYNCKT NEPLINDESI
     NHIKELFGKF GSDCWFEMST QQLLPPSLKD QHENFVKGTD TMDVWFDSGT SWRGVLVERG
     IIDKDTGRAD IYLEGSDQHR GWFQSSLLTS VCVRDIEPYK NVVTHGFLLD ESGIKMSKSI
     GNTIVPSTVI KGGPNKVQNP PYGVDLLRTW VASSDYSKDI SIGPNILIKI LDGIKKIRNT
     LRFMLASNFD FDPTIHAIPY EKLSSLDKYA LHRVFKLQES VTRHYDQFQF QKVHTEIINF
     SIEISSFYFD VIKRHLYAES PNSHSRRSTQ TVLFKMLDVI NIALAPITVH TSEDVFLHQY
     QFKNNGKGLD KNLIENSVFA HGWDQLPSQY ENELISNQFT NIIAIRDVVN RVLQSMRSQG
     IIGRSDETIM ELTVTNEESS PFYDNLFAIN SQLDDIFCVS NVLLKKFNTF EKDVEQQQQQ
     QQQQQQQQPQ QIEPNSKGEF IFNTIISNNS KQLGRIEVLL KISDKFKCPR CWRHTSIEND
     KVCKPCDSVL NSLK
//