ID A0A0M9EY07_FUSLA Unreviewed; 1071 AA.
AC A0A0M9EY07;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 13-SEP-2023, entry version 33.
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=FLAG1_05100 {ECO:0000313|EMBL:KPA41992.1};
OS Fusarium langsethiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=179993 {ECO:0000313|EMBL:KPA41992.1, ECO:0000313|Proteomes:UP000037904};
RN [1] {ECO:0000313|EMBL:KPA41992.1, ECO:0000313|Proteomes:UP000037904}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fl201059 {ECO:0000313|EMBL:KPA41992.1,
RC ECO:0000313|Proteomes:UP000037904};
RA Lysoe E., Divon H.H., Terzi V., Orru L., Lamontanara A., Kolseth A.-K.,
RA Frandsen R.J., Nielsen K., Thrane U.;
RT "The draft genome sequence of Fusarium langsethiae, a T-2/HT-2 mycotoxin
RT producer.";
RL Submitted (APR-2015) 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}.
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:KPA41992.1}.
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DR EMBL; JXCE01000078; KPA41992.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M9EY07; -.
DR OrthoDB; 656at2759; -.
DR Proteomes; UP000037904; 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; 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:UP000037904}.
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; 123494 MW; 73D4F6FBD6F61EC1 CRC64;
MSIDFPKEEE AVLQRWREID AFLRQVELSE GRPRYTFYDG PPFATGLPHY GHLLASTIKD
VIPRYWSMKG FHVERRFGWD THGLPIEHEI DKKLGISGKA AVMELGIAKY NEECRSIVMR
YAKEWRQTIE RLGRWIDFDN DYKTMHPNFM ESEWWVFKQL FDKDQVYQGH RVMPYSTVLT
TALSNFEANQ NYQDVTDPAV VVTFPLVDDP EVNLLAWTTT PWTLPSHLGL AAHPDFEYVK
IVDEKTGKTY ILLEKLLGTL YKDPKKAKFK IVEKILGKDM LGWKYTPPFN YFYDEFKDVA
FKVLNATYVT DDSGVGIVHQ APAFGEDDYN VAVAAGIVTE NRSPPDPVND TGHFTDRVSD
FKGMHVKEAD KHIIKYLKNA GRIANESQLK HSYPMCPRSD TPLIYRAVPS WFIRIPDIIP
DMLKNIEETR WVPSFVKEKR FASWIANARD WNVSRNRYWG TPIPLWVSED LEERVCVGSV
QELRELSGYE GDLSDLHRDK VDHITIPSKM GKGQLKRIEE VFDCWFESGS MPYASQHYPF
ENVEKFEQSF PGNFIAEGLD QTRGWFYTLT VLGTHLFGKS PFKNCVVNGI VLAEDGKKMS
KRLKNYPDPS IVMSKYGSDA LRLYLINSPV VRAEPLRFKE SGVKEVVQKV LLPLWNSYKF
FEGQVALLKK VENVDFVWDP KLEATNSNVM DRWILASCQS LLAFVNQEME AYRLYTVVPR
LLGLIDNTTN WYIRFNRKRL KGENGLDDTL HALNALFEVL FTLCRGLAPF TPFLTDNIYL
KLLPHIPKEL QGDDPRSVHF LPFPDVRQEL FDEEVERRVG RMQRVIELAR VSRERRTIGL
KQPLKTLVVL HSDHQYLEDV KSLQNYISEE LNVQDLVLSS DESKYNVQYS VTADWPVLGK
KLKKDMARVK KGLPLLTSDQ VKGYLQDKHI NVDGIRLEEG DLVVRRGVKE EESSKNFETN
TDSEVLTILD TEIHPELVAE GLGREIINRV QRLRKKAGLV PTDDIKMEYR VIADPEDVGL
SGAFKSQTPA FEKALRRPLE EASAETQTEG LIAEEEQEVQ QATFILRLLK L
//
