ID A0A061HE04_BLUGR Unreviewed; 1046 AA.
AC A0A061HE04;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 44.
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=BGT96224_3031 {ECO:0000313|EMBL:EPQ62925.1},
GN BGT96224V2_LOCUS5547 {ECO:0000313|EMBL:SUZ12386.1};
OS Blumeria graminis f. sp. tritici 96224.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Blumeria.
OX NCBI_TaxID=1268274 {ECO:0000313|EMBL:SUZ12386.1};
RN [1] {ECO:0000313|Proteomes:UP000053110}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=96224 {ECO:0000313|Proteomes:UP000053110};
RX PubMed=23852167; DOI=10.1038/ng.2704;
RA Wicker T., Oberhaensli S., Parlange F., Buchmann J.P., Shatalina M.,
RA Roffler S., Ben-David R., Dolezel J., Simkova H., Schulze-Lefert P.,
RA Spanu P.D., Bruggmann R., Amselem J., Quesneville H.,
RA Ver Loren van Themaat E., Paape T., Shimizu K.K., Keller B.;
RT "The wheat powdery mildew genome shows the unique evolution of an obligate
RT biotroph.";
RL Nat. Genet. 45:1092-1096(2013).
RN [2] {ECO:0000313|EMBL:EPQ62925.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=96224 {ECO:0000313|EMBL:EPQ62925.1};
RA Oberhaensli S., Wicker T., Keller B.;
RT "The wheat powdery mildew genome reveals unique evolution of an obligate
RT biotroph.";
RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:SUZ12386.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=96224 {ECO:0000313|EMBL:SUZ12386.1};
RA Quirk P.G., Krulwich T.A.;
RL Submitted (JUL-2018) 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; KE375143; EPQ62925.1; -; Genomic_DNA.
DR EMBL; UIGY01000171; SUZ12386.1; -; Genomic_DNA.
DR HOGENOM; CLU_001493_1_0_1; -.
DR OrthoDB; 656at2759; -.
DR Proteomes; UP000053110; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
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:0004823; F:leucine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:EnsemblFungi.
DR CDD; cd07961; Anticodon_Ia_Ile_ABEc; 1.
DR CDD; cd00818; IleRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
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:UP000053110}.
FT DOMAIN 116..608
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 665..820
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 1046 AA; 120864 MW; B7C61C95463D19F3 CRC64;
MSIDFPAEEE RILQQWKNIK AFERQVELSR DRPAYTFYDG PPFATGLPHY GHLLASTIKD
IIPRYWSMKG YYVERRFGWD THGLPIEHEI DKKLGIYGKD AVMKLGLAKY NEECRAITMD
LTFMESEWWI FKQIFDKGAV YQGHRVMPYS TVLTTALSNF EANQNYQDIT DPAVVVSFPL
VGDPNTCLLA WTTTPWTLPS NVALAAHPDF EYVKIFDEIS GKNYILLEKL MGTLYKDPKK
AKFRVIEKIM GNKMVGWKYE PLFDYFYEDF KDCGFMVVNA SYVTDDSGVG IVHQAPAFGE
EDYNVALKNN IITEHRAPPN PIDESGNFTS RVHHFTGQHV KAADKAIIKY LKGTGRMIVD
SQIRHSYPMC PRSDTPLIYR AVPSWFIRIP EIIPQMLKNI ESSHWVPTFV KEKRFSSWIT
NARDWNVSRN RYWGTPIPLW VSDDLEEKVC VGSVQELKEL SGCVEDLTDL HRDKIDHITI
PSKMGKGNLR RIEEVFDCWF ESGSMPYASQ HYPFENKDNF ERTFPGDFIA EGLDQTRGWF
YTLLVLGTHL FGVSPFKNCV VNGIVLAEDG KKMSKRLKNY PDPSIIMNKY GSDALRLYLI
NSPAVKAEPL RFKESGVKDV VAKVLLPLWN SFKFFEGQVL LLKKSEDIDY VFDPSAEINN
SNVMDRWILA SCQSLLQFVD EEMAAYRLYT VVPRLLELID NTTNWYIRFN RKRLKGDLGL
EDTQHALNTL FEVLFTLVKG LAPFTPFITD NIYQRLLPHI PQHLKGVDPR SVHFLEFPTV
RKELFDPQIE RRVSRMQRVI ELSRVSRERR TVGLKIPLKT LIVIHHDLTY LQDIQSLESY
IKEELNIRDL VLSSDEQNYS VQYSVTADWP ILGKKLKKDV QKVKKALPDL SSEEVHQFVL
QKSIVVGGIK LEEGDLVVKR GLKDDESSKN LETNTDDDVL IILDAELYPE LADEGLAREV
INRVQRLRKK AGLQPTDDIK MEYKILQDPD QLGLARTFTE QSKLIEKALR RPVTQYDASK
EIDDLIILEE EQDIQNARFM LRFLQI
//
