ID   A0A1G4JBB8_9SACH        Unreviewed;      1073 AA.
AC   A0A1G4JBB8;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   13-SEP-2023, entry version 27.
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=LAMI_0D05336G {ECO:0000313|EMBL:SCU87254.1};
OS   Lachancea mirantina.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=1230905 {ECO:0000313|EMBL:SCU87254.1, ECO:0000313|Proteomes:UP000191024};
RN   [1] {ECO:0000313|EMBL:SCU87254.1, ECO:0000313|Proteomes:UP000191024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 11717 {ECO:0000313|EMBL:SCU87254.1};
RA   Devillers H.;
RL   Submitted (MAR-2016) 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; LT598463; SCU87254.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G4JBB8; -.
DR   STRING; 1230905.A0A1G4JBB8; -.
DR   OrthoDB; 656at2759; -.
DR   Proteomes; UP000191024; Chromosome d.
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:UP000191024}.
FT   DOMAIN          16..640
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          693..850
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
SQ   SEQUENCE   1073 AA;  122967 MW;  094910D0C92E9494 CRC64;
     MAEQSGPFSF PKEEEKILEF WNEIDAFHTS LELSKDKPEF SFFDGPPFAT GTPHYGHILA
     STVKDIVPRY ATMNGYHVDR RFGWDTHGLP IEHIIDKKLG IKSKEDVYKL GIDKYNAECK
     AIVMTYAEEW RRTIGRMGRW IDFDNDYKTM YPSFMESTWW GFKQLFEKGQ VYRGHRVMPY
     STGCTTPLSN FEAQQNYKEV NDPAVTIGFK VVGQEKTYLV AWTTTPWTLP SNLALCVNAD
     FEYVKIYDQN RDKYFILVES LIKTLYKKPS NEDFKVVERY SGKDLVGWKY EPLFDYFAKD
     FGEKAFRVIS DNYVTNDSGT GIVHNAPAFG EEDFNVCLKA GIFSEDDDIP NPVDDNGNFT
     SAVSHFAGMY VKAADKEIIK FLTASGNLLL ASQIRHSYPF CWRSDTPLLY RTVPAWFVRV
     KPIIPQFLDS VGKSRWVPHI IKEKRFANWI ANARDWNVSR NRYWGTPIPL WVSEDYEEIV
     CVGSVEELEK LSGVTGITDL HRDSIDNIRI PSKQGKGELK RIEEVFDCWF ESGSMPFASQ
     HYPFENTEKF KDRVPANFIS EGLDQTRGWF YTLGVLGTQI FGTVPYQNVI VTGIILAADG
     KKMSKSLKNY PDPNLILNKY GADALRLYLI NSPVLKAESL RFKEEGVKEV ISKVLLPWLN
     SFKFLEGQIS LLKKTSNVDF SFNPHLKSEN IMDRWIMASL QTLIKDIHSE MQAYKLYAVV
     PQLLSFIDLM TNWYIRLNRR RLKGENGVED CLVALNTLFD ALFNFLSAMA PFTPYLSDNL
     YQKMRDFIPK DVLSQYCKDD RSVHFLLYPT VRQEFFDEAI ERTMSRMQAV IELGRVIREK
     KTISLKTPLK SLVIIHSDPA YLKDVESLKG YIIEELNVRD LIITSDEAAY GVVYQALADW
     PVLGKKLKKD AKKVKDALPS VSSEQVKQYL ETGKIEVAGI PLVKGDLAVS RALPGDKVGE
     GLESRTDQDV LIILDTKIYD DLKTEGLARE LINRIQKLRK KCGLEATDDV SVQYEIVKDT
     IDFDTVVKCH AEMLAKVCRS DITKFDGSRT EGEIADEEQS INDTIFKLKI FKL
//