ID H0H266_SACCK Unreviewed; 996 AA.
AC H0H266;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
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=VIN7_10411 {ECO:0000313|EMBL:EHM99846.1};
OS Saccharomyces cerevisiae x Saccharomyces kudriavzevii (strain VIN7)
OS (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=1095631 {ECO:0000313|EMBL:EHM99846.1, ECO:0000313|Proteomes:UP000009009};
RN [1] {ECO:0000313|EMBL:EHM99846.1, ECO:0000313|Proteomes:UP000009009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VIN7 {ECO:0000313|EMBL:EHM99846.1,
RC ECO:0000313|Proteomes:UP000009009};
RX PubMed=22136070; DOI=10.1111/j.1567-1364.2011.00773.x;
RA Borneman A.R., Desany B.A., Riches D., Affourtit J.P., Forgan A.H.,
RA Pretorius I.S., Egholm M., Chambers P.J.;
RT "The genome sequence of the wine yeast VIN7 reveals an allotriploid hybrid
RT genome with Saccharomyces cerevisiae and Saccharomyces kudriavzevii
RT origins.";
RL FEMS Yeast Res. 12:88-96(2012).
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363035}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHM99846.1}.
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DR EMBL; AGVY01000384; EHM99846.1; -; Genomic_DNA.
DR AlphaFoldDB; H0H266; -.
DR HOGENOM; CLU_001493_7_2_1; -.
DR PhylomeDB; H0H266; -.
DR Proteomes; UP000009009; 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; 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 {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}.
FT DOMAIN 78..706
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 752..910
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 996 AA; 115098 MW; 1A017457E1AA4045 CRC64;
MPRQIRSIIN KRYFAKHAFQ KTLNLPKTKF PNRSNLDTSL RELIPKSSQV VYKEQLDDFF
EDFSKLSTID CKLKFINDKL FILHDGPPYA NGDLHLGHAL NKVLKDIINR YQLSQGKYIF
YKPGWDCHGL PIEIKALKDL SAQQIESISP LKIRSLASKH AQKAIKKQKE TFKQFAILTD
WETPYITMDK HYEIDQLNIF KEMFDRGLIK RQNKPVYWGT ETRTALAEGE LEYNENHKSI
AVYVKFPLEK ESDRDLCRKL GITNNLPIYC LIWTSTPWTL FSNRAICFNQ DFSYSILRIS
DELIVVETDS IDELNLPMGS YKIIKQFQGT HLHGLYYQNR LTNDNVRRPL LNGTHVTSGT
GTGLVHTAPG HGQDDYLIGM QNNLEIYSPV DHEGRYQLNE LPESVRCFMR DEKDASMGKQ
VLDIETANVI LQKLSDLNLL YKSHEYTHSY PYDWRSKKPV IIRATPQWFT DLHDVKNLAL
EGIRRVKFYP ERGYTRLSSF IKSRNEWCIS RQRSWGIPIP SFFKKSEPDA ILMNSETLAH
AIKTIEKKGI NAWFNNENDD MKEWLPEKYH EVAHEYSRSL DTMDVWFDSG SSWSVIKDFY
EKQLKLTKLP YPLYQVCLEG SDQHRGWFQS SLLTKTASSN VSVAPYEEVI THGFTLDENG
LKMSKSVGNT ISPEAIIQGD ECLGLPPLGV DGLRYLIAQS NFTNDIVAGP TVMKHVGEAL
KKIRLTFRYL LGNLQNSTNF NLLPADELRR VDQYTLYKVN ELLDMTRTHY ENYNFSKVLV
ALQYHLNNDL SAFYFDVSKD TLYSDQISSL KREQVQTTLF HILNAYRAIL APILPVMVQE
VWKYVPKGWF QAQEQMSISP MREKWPHFEI NPETNSSFEE SELRIAKQFQ KEFRSLSLEE
GITKTAQSHV TVFTNHSLPF SSSELCDILQ ASAVEISPAD IDHNDLPIIG LGSGTNVQIL
VERSKRHNCP RCWKSNSTEE DTLCDRCEEV VNKNTS
//
