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Database: UniProt
Entry: A0A197KEJ5_9FUNG
LinkDB: A0A197KEJ5_9FUNG
Original site: A0A197KEJ5_9FUNG 
ID   A0A197KEJ5_9FUNG        Unreviewed;      1071 AA.
AC   A0A197KEJ5;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   13-SEP-2023, entry version 27.
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=K457DRAFT_132115 {ECO:0000313|EMBL:OAQ36137.1};
OS   Linnemannia elongata AG-77.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC   Mortierellomycetes; Mortierellales; Mortierellaceae; Linnemannia.
OX   NCBI_TaxID=1314771 {ECO:0000313|EMBL:OAQ36137.1, ECO:0000313|Proteomes:UP000078512};
RN   [1] {ECO:0000313|EMBL:OAQ36137.1, ECO:0000313|Proteomes:UP000078512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AG-77 {ECO:0000313|EMBL:OAQ36137.1,
RC   ECO:0000313|Proteomes:UP000078512};
RG   DOE Joint Genome Institute;
RA   Uehling J., Gryganskyi A., Hameed K., Tschaplinski T., Misztal P., Wu S.,
RA   Desiro A., Vande Pol N., Du Z.-Y., Zienkiewicz A., Zienkiewicz K.,
RA   Morin E., Tisserant E., Splivallo R., Hainaut M., Henrissat B., Ohm R.,
RA   Kuo A., Yan J., Lipzen A., Nolan M., Labutti K., Barry K., Goldstein A.,
RA   Labbe J., Schadt C., Tuskan G., Grigoriev I., Martin F., Vilgalys R.,
RA   Bonito G.;
RT   "Genome sequencing reveals origins of a unique bacterial endosymbiosis in
RT   the earliest lineages of terrestrial Fungi.";
RL   Submitted (MAY-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   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363035}.
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DR   EMBL; KV442012; OAQ36137.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A197KEJ5; -.
DR   STRING; 1314771.A0A197KEJ5; -.
DR   OrthoDB; 656at2759; -.
DR   Proteomes; UP000078512; 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   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000078512}.
FT   DOMAIN          16..640
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          694..849
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   COILED          1010..1037
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1071 AA;  123810 MW;  1592A6B297F912C3 CRC64;
     MADGSAQFNF PKEEEKILEF WREIDAFKRS QELNKDKEPF AFFDGPPFAT GLPHYGHLLA
     GTIKDIVTRF AHSTGHSVER RFGWDCHGLP VEYEVDKALG ITGKADVLAM GIDKYNEECR
     SIVMRYAKEW RQTVERAGRW IDFDNDYKTL NVEFMESVWW VFKTLFDKGQ VYRGVRVMPF
     STACSTPVSN FEAQQNYKDV SDPSVVVSFP LLNDPSVAFL AWTTTPWTLP SNLALCVNPT
     HDFIKFLDEA SGNTYIMIEK RLSILYKDPS KAKIKILERM KGADLKGIQY VPLFEYFYKE
     FEATGFRILN DEYVDDSAGT GVVHQAPAFG EDDYRVCINH GVITADGHIP CPVDESGKYF
     DVITDFKGMH VKEADKLIQK HIKGMGRLIV QTQINHSYPF CWRSDTPLIY KAFPSWFVRV
     QPIVDKMLKN NAQSRWVPGF VQEKRFANWI ANARDWNISR SRYWGTPIPI WATEDFSEMH
     CIGSLAELEE LSGCGKLTDI HRHFIDHITF KSPKTGKTMR RVEDVFDCWF ESGSMPYAQQ
     HYPFENKESF SKGFPADFIS EGLDQTRGWF YTLLVLSTHL FDTPPAKNQI VSGLVLASDG
     KKMSKRLKNY PEANIILDAY GADALRLYLI NSPVVRAETL KFKEEGVKDV ITKVFLPWYN
     AYKFFVNQTV LLKKEFNHDF MYNGALKKSD NVMDRWMLAS CQSLIKFVRE EMTNYRLYTV
     VPRLLRLIEE LTNWYVRFNR RRLKGENGLE DATQAMNTLF EVLYTLVRVM SPFTPFLTEN
     MYQTLKNFVP KDPKIVDDRS VHFLDFPEVK EEYFDDDIER AMSRMQAVIE LGRTTRERKT
     ISLKTPLKEL VVIHPDPQYH ADVKSLESYI VDELNVRSLI VTSDEAQYGV KYTIEADFRS
     LGAKLKKDAV KVKNALPKLS EEQIKDFIRN KAITIEGHNL GEEDLTVVRF FESSENSLET
     NSDKDVLILL DVKRYPELEQ EGLAREIINR VQRLRKKAGL EPTDMIHMYY EFTQDLNNAL
     EQVIKEQEET LVRALKRSLE PIATKKEADA VIIEEAQEVN GSTFNLTLVR D
//
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