ID E6ZYQ0_SPORE Unreviewed; 1087 AA.
AC E6ZYQ0;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 24-JAN-2024, entry version 59.
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=sr13065 {ECO:0000313|EMBL:CBQ72357.1};
OS Sporisorium reilianum (strain SRZ2) (Maize head smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX NCBI_TaxID=999809 {ECO:0000313|EMBL:CBQ72357.1, ECO:0000313|Proteomes:UP000008867};
RN [1] {ECO:0000313|EMBL:CBQ72357.1, ECO:0000313|Proteomes:UP000008867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRZ2 {ECO:0000313|Proteomes:UP000008867};
RX PubMed=21148393; DOI=10.1126/science.1195330;
RA Schirawski J., Mannhaupt G., Muench K., Brefort T., Schipper K.,
RA Doehlemann G., Di Stasio M., Roessel N., Mendoza-Mendoza A., Pester D.,
RA Mueller O., Winterberg B., Meyer E., Ghareeb H., Wollenberg T.,
RA Muensterkoetter M., Wong P., Walter M., Stukenbrock E., Gueldener U.,
RA Kahmann R.;
RT "Pathogenicity determinants in smut fungi revealed by genome comparison.";
RL Science 330:1546-1548(2010).
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; FQ311463; CBQ72357.1; -; Genomic_DNA.
DR AlphaFoldDB; E6ZYQ0; -.
DR EnsemblFungi; CBQ72357; CBQ72357; sr13065.
DR VEuPathDB; FungiDB:sr13065; -.
DR eggNOG; KOG0434; Eukaryota.
DR HOGENOM; CLU_001493_1_0_1; -.
DR OrthoDB; 656at2759; -.
DR Proteomes; UP000008867; Chromosome 4.
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 Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
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}.
FT DOMAIN 29..652
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 706..862
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 1087 AA; 124343 MW; 303F1ABE2F32CAD9 CRC64;
MAETTDSPTV FGEHEVTAAF NFPTEEEKVI RYWRAIDAFK TSLKQSEGRK PFSFYDGPPF
ATGLPHYGHL LAGTVKDIVT RHAHSTGHYV DRRFGWDCHG LPVEHEIDKK LGIKGKEDVM
AMGIDKYNAE CRAIVMTYQK EWKDTVERMG RWIDFDYGYK TMDLNFMESV WWVFKTLHQK
GLVYQGIRVM PYSTACTTPL SNFEAGLDYR EVQDPAVTVS FPLVEDPKTA FLAWTTTPWT
LPSNLGLCVH PDFNYIKIHD DERDMNFIIH EDLLTTLYKD PKKAKFQKLE TFKGKDLVGK
QYEPVFPYFQ ERFQGRAFRV LSDTYVTSDA GTGIVHQAPA FGDDDHRVAI AHGVISRDET
PPNPVDGSGR YTNEVPDYEG VHVKDADKAI QKDLKARGRL IVQATLSHQY PFCWRSGTPL
IYKAIPSWFV RVEPAIEKLV KNNNATRWVP VHVGEGRFGS WIANARDWNI SRNRYWGTPI
PLWASEDMQE IVCVGSVEEL EKLSGVTGIT DLHKDKIDHI TIPSQQGKGQ LKRVEEVFDC
WFESGSMPYA QAHYPFENKD KFEKSFPADF ISEGLDQTRG WFYTLLILAT HLFDTAPWKN
LIVSGLVLAA DGKKMSKSLR NYPDPNLLIN QYGADAIRLY LINSPVVRAE NLRFKEEGVK
EVVASTFLPW LNSFRFFLGS VSLLEKDHGI KFVYQNKAEK SSNVMDRWIL ARCQSLIKLI
SEEMAAYRLY TVVPRLGELI DELTNWYIRF NRRRLKGENG VEDTQAALNS LFETLYTLCR
TLSSFTPFLT ENLYQGLRKF LPPVAADDKE DYRSVHFLSF PEVNESYFDP VIQRQFKALQ
SVVELGRVMR VNSNLAIRVP LKELVVFHTD PEYLHDVESL SDYIKEELNV RDLVLSSDEA
KCGVRFKLFA DWPVLGRKLR KDVGKVRKGL ESVTSDDAKR YRETGKLNVA GVDLVEGDLR
VIRYVETKEI DGTFESNTDG NVVVLLDVQQ RPELVSEGTA REVVNRIQRL RKKAGLVATD
EVDAFYSFEA GLGQALAECI ESQPETFMKA LRRKPLPEAE KRAEAKVILQ EEQEVGEDKF
MLTLAWA
//
