ID   A0A0A1U8I9_ENTIV        Unreviewed;      1054 AA.
AC   A0A0A1U8I9;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   08-NOV-2023, entry version 36.
DE   RecName: Full=isoleucine--tRNA ligase {ECO:0000256|ARBA:ARBA00013165};
DE            EC=6.1.1.5 {ECO:0000256|ARBA:ARBA00013165};
DE   AltName: Full=Isoleucyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00032665};
GN   ORFNames=EIN_151770 {ECO:0000313|EMBL:ELP91250.1};
OS   Entamoeba invadens IP1.
OC   Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC   Entamoeba.
OX   NCBI_TaxID=370355 {ECO:0000313|EMBL:ELP91250.1, ECO:0000313|Proteomes:UP000014680};
RN   [1] {ECO:0000313|EMBL:ELP91250.1, ECO:0000313|Proteomes:UP000014680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP1 {ECO:0000313|EMBL:ELP91250.1,
RC   ECO:0000313|Proteomes:UP000014680};
RA   Zafar N., Inman J., Hall N., Lorenzi H., Caler E.;
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
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         Evidence={ECO:0000256|ARBA:ARBA00000114};
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363035}.
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DR   EMBL; KB206474; ELP91250.1; -; Genomic_DNA.
DR   RefSeq; XP_004258021.1; XM_004257973.1.
DR   AlphaFoldDB; A0A0A1U8I9; -.
DR   EnsemblProtists; ELP91250; ELP91250; EIN_151770.
DR   GeneID; 14890338; -.
DR   KEGG; eiv:EIN_151770; -.
DR   VEuPathDB; AmoebaDB:EIN_151770; -.
DR   OrthoDB; 656at2759; -.
DR   Proteomes; UP000014680; Unassembled WGS sequence.
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; IEA:UniProtKB-EC.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd07961; Anticodon_Ia_Ile_ABEc; 1.
DR   CDD; cd00818; IleRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   HAMAP; MF_02003; Ile_tRNA_synth_type2; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
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   NCBIfam; TIGR00392; ileS; 1.
DR   PANTHER; PTHR42780:SF1; ISOLEUCINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR   PANTHER; PTHR42780; SOLEUCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF19302; DUF5915; 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 {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|RuleBase:RU363035};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363035};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363035};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU363035};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW   ECO:0000256|RuleBase:RU363035};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014680}.
FT   DOMAIN          19..636
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          684..834
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
SQ   SEQUENCE   1054 AA;  122824 MW;  A3474F9720D0B1FF CRC64;
     MNTMELPDHI NFPKMEEEIM KYWDDIKVFD QCNELTKDRP KFTFYDGPPF ATGLPHYGHL
     LAGTIKDTVC RYAIQTGHRV DRKFGWDTHG LPIEFEIDKI LGIHTTDEVL KYGIPNYNRE
     CRNIVMRYSE EWKKVVWRTG RWIDMDHAYK TMDISFMESV WWVFKQLYEK QLVYRGLKVM
     PFSTGCCTPL SNFEAGLSYK DVSDPTVTMT FPVVGEENTS FLGWTTTPWT LPSNLALCVN
     ANYDYVKFYD EKTKHNYYML ECRMASLPDA KKAKRTIIAK MKGKDLVGKH YVPLFPYFKD
     LEGCFRVVSD DYVDNTSGTG IVHQAPGFGE DDYRVCLANG VISKGTKLVC PIDFSGNFTD
     EVTDYKGRYI KDCDKDIIDR LKKEGRVFDS RPMVHSYPFC WRSDTPLIYR AIPSWFVNVE
     SFKDKLVENS KQTYWVPENI REGRFQNWLS NARDWAISRN RFWGTPIPIW TDDAFSEFVC
     VGSVQELEEL TGQKITDLHR EYVDDLVIEK NGKKLHRITE VFDCWFESGS MPYGQAHYPF
     ENVEEFKNSF PCDFIAEGID QTRGWFYSLL VLSTALFDKP PFKNLIVNGL VLASDGKKMS
     KRLKNYPDPV EMIDLYGADA LRLSLINSPA VRAETVKFQE KTLKELISSI FLPWFNTMKY
     LQQSFKPGMK IMAIDKIEGI NDMDKWILSS LMSLVKKVRE EMKKFRLYTV VAPLVDLLVT
     LSNWYIKLNR KRFRGESGLT SCSVLYHCLK IMAVLMAPFT PFFSEFCYQK LQNYPLNYEE
     EKFASVHFCQ IPEPTEKYHD AKLEETVEAL KKIIELGRVA RDKKTLPLKQ PLRKLTIIHS
     SKEFLADLMK FKEYILVELN VEDVITTTEQ GQYIALSFAP EKGVIGKKYR KDGKRYCDYF
     EKLGRDEVLK FMETGTIEYD GKTFTDEDLK VHRQFTGDTT IEEPMWEKDV LILLDIVRDK
     ALIEKGICRE VNNRVQKLRK DAGLKVQDNV VVLYSYDDKN HEAIDEAINE QKEFLKTYGV
     ILKQKEDTDK PMFDQNVTLK CVTDSIHLWL VKLN
//