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Database: UniProt
Entry: D5GAW0_TUBMM
LinkDB: D5GAW0_TUBMM
Original site: D5GAW0_TUBMM 
ID   D5GAW0_TUBMM            Unreviewed;      1075 AA.
AC   D5GAW0;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   13-SEP-2023, entry version 72.
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=GSTUM_00005330001 {ECO:0000313|EMBL:CAZ81653.1};
OS   Tuber melanosporum (strain Mel28) (Perigord black truffle).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Tuberaceae; Tuber.
OX   NCBI_TaxID=656061 {ECO:0000313|EMBL:CAZ81653.1, ECO:0000313|Proteomes:UP000006911};
RN   [1] {ECO:0000313|EMBL:CAZ81653.1, ECO:0000313|Proteomes:UP000006911}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mel28 {ECO:0000313|EMBL:CAZ81653.1,
RC   ECO:0000313|Proteomes:UP000006911};
RX   PubMed=20348908; DOI=10.1038/nature08867;
RA   Martin F., Kohler A., Murat C., Balestrini R., Coutinho P.M., Jaillon O.,
RA   Montanini B., Morin E., Noel B., Percudani R., Porcel B., Rubini A.,
RA   Amicucci A., Amselem J., Anthouard V., Arcioni S., Artiguenave F.,
RA   Aury J.M., Ballario P., Bolchi A., Brenna A., Brun A., Buee M.,
RA   Cantarel B., Chevalier G., Couloux A., Da Silva C., Denoeud F.,
RA   Duplessis S., Ghignone S., Hilselberger B., Iotti M., Marcais B., Mello A.,
RA   Miranda M., Pacioni G., Quesneville H., Riccioni C., Ruotolo R.,
RA   Splivallo R., Stocchi V., Tisserant E., Viscomi A.R., Zambonelli A.,
RA   Zampieri E., Henrissat B., Lebrun M.H., Paolocci F., Bonfante P.,
RA   Ottonello S., Wincker P.;
RT   "Perigord black truffle genome uncovers evolutionary origins and mechanisms
RT   of symbiosis.";
RL   Nature 464:1033-1038(2010).
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; FN430086; CAZ81653.1; -; Genomic_DNA.
DR   RefSeq; XP_002837462.1; XM_002837416.1.
DR   AlphaFoldDB; D5GAW0; -.
DR   STRING; 656061.D5GAW0; -.
DR   EnsemblFungi; CAZ81653; CAZ81653; GSTUM_00005330001.
DR   GeneID; 9187821; -.
DR   KEGG; tml:GSTUM_00005330001; -.
DR   eggNOG; KOG0434; Eukaryota.
DR   HOGENOM; CLU_001493_1_1_1; -.
DR   InParanoid; D5GAW0; -.
DR   OMA; EIIVIHK; -.
DR   OrthoDB; 656at2759; -.
DR   Proteomes; UP000006911; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
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:EnsemblFungi.
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:UP000006911}.
FT   DOMAIN          10..634
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          689..844
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
SQ   SEQUENCE   1075 AA;  124235 MW;  C3690946125C2F1C CRC64;
     MDFPKEEERI LEFWREIDAF RTSVKLSEGR PPYSFYDGPP FCTGLPHYGH LLASTIKDIV
     PRYWHMKGHY VERRFGWDTH GLPIEHEIDK RLGITSKEDV LKMGMEKYNE ECKAIVMRYS
     TEWRQTIDRL GRWIDFDNDY KSMYPTFMES IWWVCKQLFV KDQVYLGYRV MPYSTACTTP
     LSNFEAQQNY KDVQDPAVVV TFPLLDDPTT ELLAWTTTPW TLPSHTGIAV HPDFEYIKIS
     DRASGRNYIL LESCLKTLYG EKGLKKAKYT ILEKIKGKDM LGWKYEPLFD YFYEQFKDYG
     FKVLNATYVT SDSGTGLVHQ APAFGEEDYS VAMEAGVINE TRPPPNPVNE AGIFTSEVRE
     FAGLHVKAAD KGIIKHLKEK KRLIVDSQIT HSYPFCWRSD TPLIYRAVPA WFVRIPNIIP
     KMLENIEGSH WVPTNVKENR FGNWIQNARD WNISRNRYWG TPIPIWMSDD KEEMVCIGSV
     EELRELSGCG EIPDLHRDKI DHITIPSKKG KGVLRRVEEV FDCWFESGSM PYASSHYPFE
     NKDQFEKAFP ADFIAEGLDQ TRGWFYTLLV LGTHLFGVSP FQNCIVNGIV LAEDGKKMSK
     RLKNYPDPTL VMDKYGSDAL RLYLINSPVV RAMPLRFKEV GVKDVVTKVL LPLWNSYNFF
     EQQSQLLKKL EGVDFIFNPE SGGSKNVMDR WILANCQSYL KFVNQEMKGY RLYTVVGRML
     EMVDNTTNWY IRFNRKRLKG EYGTEDTLHA LNSLFEVLFT LVRGMAPFAP FLTDNIYHRL
     KPHIPDSMLP EDARSVHFLS FPEVREELFD EEVERRFGRM QRVIELARTS RERKAIGLKT
     PLKTLVVIHP DQTYLDDVKS LESYITSELN VRDLVLSADE EKYGVQYKVT ADWPVLGKKL
     KKDLIKVKNA LPSITSAEVK GFVQEKKIVV GGITLIEEDL VVSRGLSGSD TSQDFETNTD
     NDVLTILDTV LHKDLRNEGL AREIVNRVQR LRKKAGLLPT DDIKMEYKVL QDPIGLEEVF
     LEHADTFEKA LRRPLDKATI TQVGEVQPGE NLDKMILEET QEVGEATFML RLLKL
//
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