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Database: UniProt
Entry: A0A168K452_CORDF
LinkDB: A0A168K452_CORDF
Original site: A0A168K452_CORDF 
ID   A0A168K452_CORDF        Unreviewed;       949 AA.
AC   A0A168K452;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, 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=LEL_00752 {ECO:0000313|EMBL:OAA81207.1};
OS   Akanthomyces lecanii RCEF 1005.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces;
OC   Cordyceps confragosa.
OX   NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA81207.1, ECO:0000313|Proteomes:UP000076881};
RN   [1] {ECO:0000313|EMBL:OAA81207.1, ECO:0000313|Proteomes:UP000076881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA81207.1,
RC   ECO:0000313|Proteomes:UP000076881};
RX   PubMed=27071652; DOI=10.1093/gbe/evw082;
RA   Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT   "Divergent and convergent evolution of fungal pathogenicity.";
RL   Genome Biol. Evol. 8:1374-1387(2016).
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:OAA81207.1}.
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DR   EMBL; AZHF01000001; OAA81207.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A168K452; -.
DR   STRING; 1081108.A0A168K452; -.
DR   OrthoDB; 656at2759; -.
DR   Proteomes; UP000076881; 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; cd07960; Anticodon_Ia_Ile_BEm; 1.
DR   Gene3D; 1.10.730.20; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   Gene3D; 1.10.10.830; Ile-tRNA synthetase CP2 domain-like; 1.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR033708; Anticodon_Ile_BEm.
DR   InterPro; IPR002301; Ile-tRNA-ligase.
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; PTHR42765:SF1; ISOLEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR42765; SOLEUCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF08264; Anticodon_1; 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:OAA81207.1}; 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:UP000076881}.
FT   DOMAIN          35..658
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          699..855
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          607..637
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        622..636
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   949 AA;  105795 MW;  5FEBDA0BE6D05583 CRC64;
     MSKSWKSTLR LPRSTFPARP NPKLQRQHLL SCSDEFYSWQ SSRPSEDEPF VLHDGPPYAN
     GPLHTGHSIN KILKDMIVRV QVQNGRHVVY RPGWDCHGLP IEMKALGAAG TKGLSAVQVR
     KQARKLATKT VTEQMKGFRS FAVMSEWDNR WTTMDRAFEI RQLRVFQKMV RHGLIYRKHK
     PVYWSPSSGT ALAEAELEYK DDHQSRSAYI RFPITSDYSE IPELRNFDGP LYAAIWTTTP
     WTLPANKAIG VHNDLLYTVL RVNGYGLLVA SSRIDAVLEF IPEAEVVVDS ITGSKLAGLQ
     YRNKLRGKSA PVQPIIHADF VSADSGTGLV HLAPGHGQDD YEICLAHDIE AFAPIDNEGR
     FTAEAYPDDP EILTSAPSIL DGGSSAVLDL VAEDVIATQD IQHKYPYDWR SKKPVVIRAT
     AQWFADVGSI KDDALNALKN VKFVPESGRV RLESFVKSRS EWCISRQRSW GVPIPALYNS
     SGEAVMTDET IEHIIQVMQE RTSDAWFSDS PDDPAWIPAS LQGEYRRGTD TMDVWFDSGT
     SWAEIEKQVD VYLEGSDQHR GWFQSSLLSY IAAQKADGKA AGGIVAPFRT LITHGFTLDA
     QGKKMSKSLG NTVSPEEVMD GKLLPPAKRK GKDTGQPDAL GPDVLRLWAG SCDFTTDILI
     GPTILQPVHN ALVRYRTILK MLLGSAHESS RQTPLTRLDH IALLQLSTTM EQVWEAYSNY
     EFHKGVGILN RWVSTDLSAF YLEALKDRLY CGDGGGAIEP ILVGMLRMLA PVTPVLVEEA
     WTNRPSWMFE DSLMVHPAKQ LYKSPVIDPK RLTYDAEKLR QDIPKLSAVH EAIKAALEPA
     RLAKEVGSSL QCSVIVTTED AGLLSCLTEY QDELDAIFVV SSVSVNSALP EQPAWHYTAA
     VGGDKAQGEV HVLPPVQAKC SRCWRYQAEE EEGLCERCES EVRKHEQQA
//
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