ID A0A0F8V4I0_9EURO Unreviewed; 1077 AA.
AC A0A0F8V4I0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 13-SEP-2023, entry version 32.
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=ARAM_004692 {ECO:0000313|EMBL:KKK26674.1};
OS Aspergillus rambellii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=308745 {ECO:0000313|EMBL:KKK26674.1, ECO:0000313|Proteomes:UP000034291};
RN [1] {ECO:0000313|EMBL:KKK26674.1, ECO:0000313|Proteomes:UP000034291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRRC1468 {ECO:0000313|EMBL:KKK26674.1,
RC ECO:0000313|Proteomes:UP000034291};
RA Moore G.G., Beltz S.B., Mack B.M.;
RT "Draft Genome Sequences of Two Closely-Related Aflatoxigenic Aspergillus
RT Species Obtained from the Cote d'Ivoire.";
RL Submitted (FEB-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:KKK26674.1}.
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DR EMBL; JZBS01000289; KKK26674.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F8V4I0; -.
DR STRING; 308745.A0A0F8V4I0; -.
DR OrthoDB; 656at2759; -.
DR Proteomes; UP000034291; 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:UP000034291}.
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 1077 AA; 124321 MW; 0B36CA57660E5A44 CRC64;
MSIDFPKEEE LVLQRWKEIN AFRRQVELSE GRKPYTFYDG PPFATGLPHY GHLLASTIKD
IIPRYWSMKG HYVERRFGWD THGVPIEYEI DKKLGMSGLE AVQKLGIEKY NDECRAIVMR
FASEWRQTIE RLGRWIDFDN DYKTMNTPFM ESVWWVFKQL FDKGLVYKGY RVMPYSTALN
TPLSNFEAQQ NYKDVQDPAV VVTFPLVDDP ETCLLAWTTT PWTLPSNVAL AVNPGYEYIK
IHDEASGKHY ILLETLLRTL YKDPKKAKFK IVDRFKGSQM KDWKYQPLFN YFYDTFKDHG
YRVLNAEYVT AEDGTGIVHQ APAFGEDDYK TAVDGGVIDE NRQPPNPVDE MGCFTSEVLD
FHGQHVKTAD KAIIKYLKAN GRLIVDSQIT HSYPFCWRSD TPLIYRAVPS WFVKIGPIIP
QMLQGIEESH WVPSFVKDRR FASWIQNARD WNISRNRFWG TPLPLWVSDD FSEVVAVGSV
QELKELSGYE GELTDLHRDK VDHITIPSKK GNGVLRRVSE VFDCWFESGS MPYASQHYPF
ENKDQFEKSF PGDFIAEGLD QTRGWFYTLT VLGTHLFGKL PFKNCVVNGI VLAEDGKKMS
KRLKNYPDPS LVMDRYGSDA LRLYLINSPV VRAEPLRFKE SGVKEIVAKV LLPLWNSYKF
FEGQAALFKK TTDVDYMWDP KAEATNTNVM DRWILASCQS LLKFVNEEMA AYRLYTVVPR
LLELIDNTTN WYIRFNRKRL KGENGVDDTL HALNTLFEVI YTLVRGLAPF TPFLTDNIYQ
RLLPHIPEAL RSEDSRSVHF LPFPEVREEL FDEIVERRVA RMQKVIEMAR ISRERRSLGL
KTPLKTLVVI HQDQQFLDDV KSLETYILEE INVQELVLSS DEAKYNVQYS VTADWPTLGK
KLKKEVQKVK KALPSLSSDD VKKFVTDKKI LVDGIELVEG DLVVKRGLKQ DSSSEAMEPN
ADADVLTILD VHLYPELAHQ GLGREIINRL QRLRKKAGLV PTDDVKMQYV VLSDPDNVGI
REAFETQASV IEKVVRRPLE QCKAAEGKLP NADEEGMIMQ EEQEVQNATF LLRLLKL
//