ID A0A428QJN4_9HYPO Unreviewed; 1071 AA.
AC A0A428QJN4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 13-SEP-2023, entry version 14.
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=CEP53_003681 {ECO:0000313|EMBL:RSL65486.1};
OS Fusarium sp. AF-6.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium solani species complex.
OX NCBI_TaxID=1325737 {ECO:0000313|EMBL:RSL65486.1, ECO:0000313|Proteomes:UP000287544};
RN [1] {ECO:0000313|EMBL:RSL65486.1, ECO:0000313|Proteomes:UP000287544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL62590 {ECO:0000313|EMBL:RSL65486.1,
RC ECO:0000313|Proteomes:UP000287544};
RA Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA Kasson M.;
RT "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL Submitted (JUN-2017) 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:RSL65486.1}.
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DR EMBL; NKCJ01000056; RSL65486.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A428QJN4; -.
DR STRING; 1325737.A0A428QJN4; -.
DR Proteomes; UP000287544; 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; 2.
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:UP000287544}.
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; 123245 MW; 37FCF4AEFA8E6654 CRC64;
MSIDFPKEEE AIIQRWRDIN AFLRQVELSE GRPRYTFYDG PPFATGLPHY GHLLASTIKD
VIPRYWSMKG FHVERRFGWD THGLPIEHEI DKKLGISGKA AVMELGIAKY NEECRSIVMR
YATEWRHTIE RLGRWIDFDN DYKTMDPRFM ESEWWVFKQL FDKGQVYQGY RVMPYSTVLT
TALSNFEANQ NYQDVTDPAV VVSFPLVDNP EVSLLAWTTT PWTLPSHLGL AANPDFEYIK
ILDEKSGKTY ILLEKLLGTL YKDPKKAKFQ ILERIRGKDM EGWKYLPPFD YYYEDFKDIA
FKVLNAAYVT DDSGVGIVHQ APAFGEDDYN VALAAGIITE KRPPPDPVND TGHFTDRITH
FKGMHVKEAD KHIIKHLKNA GRIANESQIR HSYPMCPRSD TPLIYKAVPS WFIRIPNIIP
DMLKNIEGSH WTPSFVKEKR FASWIANARD WNVSRNRYWG TPIPLWVSDD LEERVCIGSV
EELRELSGYE GDLTDLHRDK VDHITIPSKM GKGQLKRVEE VFDCWFESGS MPYASQHYPF
ENVDKFKESF PGDFIAEGLD QTRGWFYTLL VLGTHLFGCS PFQNCVVNGI VLAEDGKKMS
KRLKNYPDPS IVMSKYGSDA LRLYLINSPV VRAEPLRFKE SGVKEVVQKV LLPLWNSYKF
FDGQVALLKK VENVDYAWDP SMESSNTNVM DRWILASCQS LLQFVNQEMK GYRLYTVVPR
LLGLIDNTTN WYIRFNRKRL KGENGLNDTL HALNALFEVL FTLCRGLAPF TPFLTETIYL
KLLPHIPENL RGADSRSVHF LPFPDVRQEL FDEEVERRVG RMQRVIELAR VSRERRTIGL
KQPLKTLVVI HPDPQYLEDV KSLEGYITEE LNVRDLVLSN DEAKYNVQYS VTADWPVLGK
KLKKDMARVK KGLPSLSSEQ VQGYVRDGHV FVEGIRLEEG DLVVRRGVKE DEASKNFETN
TDSEVLTILD TEIHPELAQE GLGREIINRV QRLRKKAGLV PTDDIRMEYR VLSDPESVGL
SDAFKSQTGA FEKALRRPLD EVAAEAGADG LIAEEEQEVQ QATFLLRLLK L
//
