ID A0A317XAT7_9EURO Unreviewed; 1068 AA.
AC A0A317XAT7;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 13-SEP-2023, entry version 15.
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=BO94DRAFT_531688 {ECO:0000313|EMBL:PWY94752.1};
OS Aspergillus sclerotioniger CBS 115572.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450535 {ECO:0000313|EMBL:PWY94752.1, ECO:0000313|Proteomes:UP000246702};
RN [1] {ECO:0000313|EMBL:PWY94752.1, ECO:0000313|Proteomes:UP000246702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115572 {ECO:0000313|EMBL:PWY94752.1,
RC ECO:0000313|Proteomes:UP000246702};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) 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 -!- 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:PWY94752.1}.
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DR EMBL; MSFK01000004; PWY94752.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317XAT7; -.
DR STRING; 1450535.A0A317XAT7; -.
DR OrthoDB; 656at2759; -.
DR Proteomes; UP000246702; 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 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.
PE 4: Predicted;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000313|EMBL:PWY94752.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000246702}.
FT DOMAIN 12..625
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 682..837
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 1068 AA; 123607 MW; 89460D792EE197E5 CRC64;
MSIDFPHEEE VILQRWREID AFRRQVELSE GRKPYTFYDG PRSRLVFLTM DIIPRYWSMK
GHYVERRFGW DTHGVPIEYE IDKKLGMSGL EAVQKIGIEK YNEECRAIVM RFASEWRQTI
ERLGRWIDFD NDYKTMNVSF MESVWWVFKQ LFDKDLVYRG YRVMPYSTAL NTPLSNFEAQ
QNYKDVQDPA VVVTFPLVED PETSLLAWTT TPWTLPSNIA LAVNPTFEYI KILDEASGKH
YILLESLLRT LYKDPKKAKF KIVDRFKGAT MKDWKYKPLF DYFYEEFKDY GFRVLNAEYV
TAEDGTGIVH QAPAFGEDDY RVGMEGGVIS ESRLPPNPVD EKGCYTAEVK DFEGQHVKAA
DRGIIKHLKA AGRLVVDSQI THSYPFCWRS DTPLIYRAVP AWFVKIGPII PQMLQGIDDS
HWVPSFVKER RFSSWIQNAR DWNISRNRFW GTPLPLWVSD DFKEVVAVGS AEELKQLSGY
EGELTDLHRD KVDNITIPSK QGKGVLRRVS EVFDCWFESG SMPYASQHYP FENKEQFEQS
FPGDFIAEGL DQTRGWFYTL TVLGTHLFGK LPFKNCVVNG IVLAEDGKKM SKRLKNYPDP
SLVMDRYGSD ALRLYLINSP VVRAEPLRFK ESGVKEIVAK VLLPLWNSYK FFEGQAALFK
KTQGFDYTWD PKAEATNTNV MDRWILASCQ SLLKFVNEEM AGYRLYTVVP RLLELIDNTT
NWYIRFNRRR LKGENGVDDT LHALNTLFEV IYTLVRGLAP FTPFLTDTIY LKLLPHIPEA
LRSEDSRSVH FLPFPEVREE LFDEVVERRV SRMQKVIELA RISRERRNIG LKTPLKTLVV
IHQDQQYLDD VKSLQSYILE ELNILDLVLT SDEAKYNVQY SVSADWPTLG KKLKKEVQKV
KKALPSLTSE DVKKFVAEKK MLVDGIELVE GDLVVKRGLK EDSSSANMEP NTDNDALTIL
DANLYPELAE QGLGREIINR LQRLRKKAGL VPTDDVKMEY AVLSDPEDVG IDKAFETQAQ
AIEKVVRRPL DRYELVHGKL PSGDEPEMII QEEQEVQKAT FLLRLLKL
//
