ID H0ER32_GLAL7 Unreviewed; 1002 AA.
AC H0ER32;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 56.
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=M7I_5147 {ECO:0000313|EMBL:EHK98995.1};
OS Glarea lozoyensis (strain ATCC 74030 / MF5533).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiaceae; Glarea.
OX NCBI_TaxID=1104152 {ECO:0000313|EMBL:EHK98995.1, ECO:0000313|Proteomes:UP000005446};
RN [1] {ECO:0000313|EMBL:EHK98995.1, ECO:0000313|Proteomes:UP000005446}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 74030 / MF5533 {ECO:0000313|Proteomes:UP000005446};
RX PubMed=22302591; DOI=10.1128/EC.05302-11;
RA Youssar L., Gruening B.A., Erxleben A., Guenther S., Huettel W.;
RT "Genome sequence of the fungus Glarea lozoyensis: the first genome sequence
RT of a species from the Helotiaceae family.";
RL Eukaryot. Cell 11:250-250(2012).
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:EHK98995.1}.
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DR EMBL; AGUE01000132; EHK98995.1; -; Genomic_DNA.
DR AlphaFoldDB; H0ER32; -.
DR HOGENOM; CLU_001493_1_1_1; -.
DR InParanoid; H0ER32; -.
DR Proteomes; UP000005446; 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:0004823; F:leucine-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; 3.
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 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; 2.
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:UP000005446}.
FT DOMAIN 12..515
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 517..557
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 614..770
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 1002 AA; 115557 MW; 1DCD66EDFA4C8CE6 CRC64;
MSIDFPKEEE AVLKRWKEIK AFETQVQLSE GRPEYTFYDG PPFATGLPHY GHLLASTIKD
IIPRYWSMKG YHVERRFGWD THGLPIEHEI DKKLGISGKD AVMKLGLAKY NEECRAVVMR
YSSEWRVTID RLGRWIDFDN DYKTMDPQFM ESVWWVFKQV FDKDAVYQGY KVMPFSTALT
TALTAHPDFE YIKIHDEASG KNYILLEKLL GTLYKDPKKA KFKIIQKLKG TDMLGWKYEP
LFDYFYEDFK DYGFRVFNAT YVTDDSGVGI VHQSPAFGEE DYNIAIENGV ITEMRPPPNP
VDEKGCFTER VRDFVGQHVK AADKAIIKYL KGTGRLIVDS QIKHSYPMCP RSDTPLIYRA
VPSWFIRIPE IIPQMLKNIE GSHWVPSFVK EKRFASWIGS ARDWNVSRNR YWGTPIPIWV
SDDFEEKVCV GSVAELKELS GYAGDLTDLH RDKIDHITIP SKQGKGQLKR IEEVFDCWFE
SGSMPYASQH YPFENKEKFE KSFPGDFIAE GLDQTPEDGK KMSKRLKNYP DPSIVMEKYG
SDALRLYLIN SPVVRAEPLR FKEAGVKEVV AKVLLPLWNS FKFFEGQVAL LKKIENVEYC
FDPKAESTNT NVMDKWILAS CQSLLKFVNE EMAAYRLYTV VPRLLDLIDN TTNWYIRFNR
KRLKGELGLD DTKHALNTLF EVLFTLVKGL APFTPFLTDT IYQKLLPHIP KDLQGQDPRS
VHFLSFPDVR EELFNVEIER RVGRMQRVIE LARVSRERRT VGLKTPLKTL IVIHADPVYL
EDIKSLEGYI TEELNIVNLV LSSDEAKYNV QYSVNADWPV LGKKLKKEVQ KVKKALPALT
SDQVHDYVLT KSIDVAGIKL VEGDLVVKRG LKDDDSSKNL ETNTDEDVLT ILDAEVYPEL
AEEAVAREII NRVQRLRKKA GLQPTDDIKM EYKVLSDPDN IGLDKAFVEQ TKTIEKALRR
PIDKHTITEL DGKIPDTKED GIILEEEQEI QNAVFLLRLL KL
//
