ID K3W2Z0_FUSPC Unreviewed; 1071 AA.
AC K3W2Z0;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
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=FPSE_01294 {ECO:0000313|EMBL:EKJ78485.1};
OS Fusarium pseudograminearum (strain CS3096) (Wheat and barley crown-rot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=1028729 {ECO:0000313|EMBL:EKJ78485.1, ECO:0000313|Proteomes:UP000007978};
RN [1] {ECO:0000313|EMBL:EKJ78485.1, ECO:0000313|Proteomes:UP000007978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CS3096 {ECO:0000313|EMBL:EKJ78485.1,
RC ECO:0000313|Proteomes:UP000007978};
RX PubMed=23028337; DOI=10.1371/journal.ppat.1002952;
RA Gardiner D.M., McDonald M.C., Covarelli L., Solomon P.S., Rusu A.G.,
RA Marshall M., Kazan K., Chakraborty S., McDonald B.A., Manners J.M.;
RT "Comparative pathogenomics reveals horizontally acquired novel virulence
RT genes in fungi infecting cereal hosts.";
RL PLoS Pathog. 8:E1002952-E1002952(2012).
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}.
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:EKJ78485.1}.
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DR EMBL; AFNW01000029; EKJ78485.1; -; Genomic_DNA.
DR RefSeq; XP_009252689.1; XM_009254414.1.
DR AlphaFoldDB; K3W2Z0; -.
DR EnsemblFungi; EKJ78485; EKJ78485; FPSE_01294.
DR GeneID; 20359914; -.
DR KEGG; fpu:FPSE_01294; -.
DR eggNOG; KOG0434; Eukaryota.
DR HOGENOM; CLU_001493_1_1_1; -.
DR OrthoDB; 656at2759; -.
DR Proteomes; UP000007978; Chromosome 3.
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: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 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:UP000007978}.
FT DOMAIN 12..634
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 691..846
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 1071 AA; 123386 MW; C97877F065490638 CRC64;
MSIDFPKEEE VVLQRWREID AFLRQVELSE GRPRYTFYDG PPFATGLPHY GHLLTSTIKD
VIPRYWSMKG FHVERRFGWD THGLPIEHEI DKKLGISGKA AVMELGIAKY NEECRSIVMR
YAKEWRVTVE RLGRWIDFDN DYKTMDPSFM ESEWWVFKQL FDKDQVYQGH RVMPYSTVLT
TALSNFEANQ NYQDVTDPAV VVTFPLVDEP DVNLLAWTTT PWTLPSHLGL AAHPDFEYVK
ILDEKSGKTY ILLEKLLGTL YKDPKKAKFK IVEKILGKDM LGWKYTPPFN YFYDEFKDVA
FKVLNATYVT DDSGVGIVHQ APAFGEDDYN VAVAAGIVTE NRSPPDPVND TGHFTDRVSD
FKGMHVKEAD KHIIKYLKNA GRIANESQLK HSYPMCPRSD TPLIYRAVPS WFIRIPDIIP
DMLKNIKETR WVPSFVKEKR FASWIANARD WNVSRNRYWG TPIPLWVSED LEERVCVGSV
QELRDLSGYE GDLTDLHRDK VDHITIPSKM GKGQLKRIEE VFDCWFESGS MPYASQHYPF
ENVEKFEQSF PGNFIAEGLD QTRGWFYTLT VLGTHLFGKS PFKNCVVNGI VLAEDGKKMS
KRLKNYPDPS IIMSKYGSDA LRLYLINSPV VRAEPLRFKE SGVKEVVQKV LLPLWNSYKF
FEGQVALLKK VENVDFVWDP KLEATNTNVM DRWILASCQS LLAFVNQEME AYRLYTVVPR
LLGLIDNTTN WYIRFNRKRL KGENGLDDTL HALNALFEVL FTLCRGLAPF TPFLTDNIYL
KLLPHIPKEL QGDDSRSVHF LPFPDVRQEL FDEEVERRVG RMQRVIELAR VSRERRTIGL
KQPLKTLVVL HSDSQYLEDV KSLKNYISEE LNVQDLVLSS DESKYNVQYS VTADWPVLGK
KLKKDMARVK KGLPLLTSDQ VKGYLQDKHI DVDGIRLEEG DLVVRRGVKE DDSSKNFETN
TDSEVLTILD TEIHPELVAE GLGREIINRV QRLRKKAGLV PTDDIKMEYR VVADPEDVGL
SGAFKSQTPA FEKALRRPLE EASAETQTEG LIAEEEQEVQ QATFILRLLK L
//
