ID A0A2T4GYP3_FUSCU Unreviewed; 1064 AA.
AC A0A2T4GYP3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 13-SEP-2023, entry version 18.
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=FCULG_00010669 {ECO:0000313|EMBL:PTD08655.1};
OS Fusarium culmorum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=5516 {ECO:0000313|EMBL:PTD08655.1, ECO:0000313|Proteomes:UP000241587};
RN [1] {ECO:0000313|EMBL:PTD08655.1, ECO:0000313|Proteomes:UP000241587}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PV {ECO:0000313|EMBL:PTD08655.1,
RC ECO:0000313|Proteomes:UP000241587};
RA Schmidt R.;
RT "Fusarium culmorum secondary metabolites in fungal-bacterial-plant
RT interactions.";
RL Submitted (FEB-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}.
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:PTD08655.1}.
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DR EMBL; PVEM01000004; PTD08655.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T4GYP3; -.
DR OMA; EIIVIHK; -.
DR Proteomes; UP000241587; 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:UP000241587}.
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 1064 AA; 122606 MW; 65551BE35EE845DF 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
DMLKNIEETR WVPSFVKEKR FASWIANARD WNVSRNRYWG TPIPLWVSED LEERVCVGSV
QELRDLSGYE GDLSDLHRDK 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
KQPLKTLVYL EDVKSLKNYI SEELNVQDLV LSSDESKYNV QYSVTADWPV LGKKLKKDMA
RVKKGLPLLT SDQVKGYLQD KHIDVDGIRL EEGDLVVRRG VKEDDSSKNF ETNTDSEVLT
ILDTEIHPEL VAEGLGREII NRVQRLRKKA GLVPTDDIKM EYRVVADPED VGLSGAFKSQ
TPAFEKALRR PLEEASAETQ TEGLIAEEEQ EVQQATFILR LLKL
//
