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Database: UniProt
Entry: A0A094FTK1_9PEZI
LinkDB: A0A094FTK1_9PEZI
Original site: A0A094FTK1_9PEZI 
ID   A0A094FTK1_9PEZI        Unreviewed;      1462 AA.
AC   A0A094FTK1;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 44.
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=V500_04346 {ECO:0000313|EMBL:KFY92048.1};
OS   Pseudogymnoascus sp. VKM F-4518 (FW-2643).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420913 {ECO:0000313|EMBL:KFY92048.1, ECO:0000313|Proteomes:UP000029284};
RN   [1] {ECO:0000313|EMBL:KFY92048.1, ECO:0000313|Proteomes:UP000029284}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4518 (FW-2643) {ECO:0000313|Proteomes:UP000029284};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:KFY92048.1}.
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DR   EMBL; JPKC01001430; KFY92048.1; -; Genomic_DNA.
DR   STRING; 1420913.A0A094FTK1; -.
DR   HOGENOM; CLU_001493_6_0_1; -.
DR   Proteomes; UP000029284; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR   GO; GO:0004822; F:isoleucine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd07960; Anticodon_Ia_Ile_BEm; 1.
DR   CDD; cd00067; GAL4; 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; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR033708; Anticodon_Ile_BEm.
DR   InterPro; IPR021858; Fun_TF.
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   InterPro; IPR001138; Zn2Cys6_DnaBD.
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; PF11951; Fungal_trans_2; 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}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW   ECO:0000256|RuleBase:RU363035};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029284}.
FT   DOMAIN          38..669
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          708..861
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          992..1023
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        996..1018
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1462 AA;  162347 MW;  32573716A92CF222 CRC64;
     MRVPSAKSWS STIRLPKSTF PPRTTPADQA KYLQRCTDDL YAWQAKVRAQ QKPFVLHDGP
     PYANGSLHAG HAVNKILKDL ICRTELQQGR KVQFVPGWDC HGLPIEIKAL EQVRAKSEDG
     EVNLDPIGIR RAARNLARKT VKEQKKGFRE WGIMADWENP WVTMDKDFEL KQLEVFLEMT
     RQGLIFRRYK PVYWSPSSKS ALAEAELEYN ESHESITAYI KFQVVAVPEA LKAQGVDTGR
     LHAVIWTTTP WTLPANKAIA VSPDLEYTVV EVGSEQLLIA KSRLEHVAAK CAFPESFKVI
     VESIKGSELE GLTYVNALHG ENAPIQPLIF ADYVSDASGS GLVHTAPGHG MEDYDVCTKL
     GIEASAPVND AGCFTDEALP HNPSALAGKS VLGGGNEAVL ALLGFQVLGV HKHEHKYPYD
     WRTKLPVIVR ATEQWFADVG SIKDKALKSL DNVKFIPENS RSRLESFIKG RSEWCISRQR
     AWGVPIPALY DESGKAILTQ ESVSHIISVI QERGIDSWWT DAQDDVSWVS PNLRGQGTLK
     RGTDTMDVWF DSGSSWTQTE GPADVYSEGT DQHRGWFQSS LLTHISASGL DSAPFKTLVS
     HGFTIDEHGK KMSKSIGNVI SPAEIMNGTL LPPIKRKGKA TGAPAYDGLG ADALRLWVAS
     SDYTHDIALR QPVFKAINST LLKYRTTLKM LLGSMRESSE KVQLTKLDTI ALYQLQQTQI
     GFAEACRAYN FHKAISILNR WINTDLSSFY LEAIKDRLYC GNGGGVLYPI FMGLMHMLGP
     ITPALVEESW EHRPQWMKDN TSSVHPLQRS TDELRLLTYK FPPSLPTDIS HLMAANAAIK
     TAQEEARAEK LVGSSLQSSV VLTLPKESQD LFQNYADELQ EIFVVSSVEF GSGEDRVAEW
     KFKAEFEVPG GKGTAWVLPP KEAKCPRCWK YVAPAEDELC GRLLSSVATT RCDEVTPHCT
     QCTSTGRECP GPITGVIISD MTSNVRRRAR SKLANRSLGV SHSRSSGRNP SQAGQYEPVP
     NETADDYQNL DVNIIYSDPP DEPTLSLEPV NNNASSIERL GADLDPFESL PVKLHFSTLK
     LLEYCTNCMR NAFVALGPGD PMMDIWLPMI LSDQLLLQCT LYTSAIHMST IFGIDVMESM
     DVVTHKTETL SLLTKRLGDP NHAVNDVSLT AVARYVGQVI LCGNVQETKL HMDGLERMLA
     LTPDLEPSCQ VREMLFWTDL TAAALCHAAP RQLTKRPNIR LYGNPLLQAP RSTIGILCRG
     FQKIIADHEV FRSITDILHD LRCLTAVAHY SDCKVHSEMP IFVSLCFGVD ERLGNLLAME
     GSAMFESCRL AAMVFVEIVL LHNNTPNAVL LAAGMKRTLS RANMEVMLQE QPELLTWILY
     MGNIVAFGTE MAPWFLRSFA QALSFQRLSI FETLEAGAGG NRLTSDERPY HRKTADVLVT
     RISELAVTLI IMSDDNKAEP EK
//
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