SYIM_DICDI
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 03-AUG-2022, entry version 125.
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 (Slime mold).
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.DDB0231256; -.
DR PaxDb; Q54CE4; -.
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; HLGTAWN; -.
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; 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; 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
