ID Q0U8S3_PHANO Unreviewed; 1079 AA.
AC Q0U8S3;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 24-JAN-2024, entry version 113.
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=SNOG_11841 {ECO:0000313|EMBL:EAT80885.1};
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614 {ECO:0000313|EMBL:EAT80885.1, ECO:0000313|Proteomes:UP000001055};
RN [1] {ECO:0000313|Proteomes:UP000001055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173
RC {ECO:0000313|Proteomes:UP000001055};
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G., Solomon P.S., Tan K.C., Schoch C.L., Spatafora J.W.,
RA Crous P.W., Kodira C., Birren B.W., Galagan J.E., Torriani S.F.,
RA McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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; CH445344; EAT80885.1; -; Genomic_DNA.
DR RefSeq; XP_001802078.1; XM_001802026.1.
DR AlphaFoldDB; Q0U8S3; -.
DR STRING; 321614.Q0U8S3; -.
DR EnsemblFungi; SNOT_11841; SNOT_11841; SNOG_11841.
DR GeneID; 5978986; -.
DR KEGG; pno:SNOG_11841; -.
DR VEuPathDB; FungiDB:JI435_118410; -.
DR eggNOG; KOG0434; Eukaryota.
DR HOGENOM; CLU_001493_1_0_1; -.
DR InParanoid; Q0U8S3; -.
DR OMA; EIIVIHK; -.
DR OrthoDB; 656at2759; -.
DR Proteomes; UP000001055; 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; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd07961; Anticodon_Ia_Ile_ABEc; 1.
DR CDD; cd00818; IleRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
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:UP000001055}.
FT DOMAIN 12..636
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 691..846
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 1079 AA; 124082 MW; BFE318F61134BE67 CRC64;
MSIDFPKEEE RILARWKEID AFQRQVELSK GKQPYTFYDG PPFATGLPHY GHLLASTIKD
IIPRYWSMKG RYVERRFGWD THGVPIEYEI DKELGMSGRD AVRTLGIAKY NEKCRAIVMR
YAGEWRTTID RLGRWIDFDN DYKTMDTSFM ETEWWVFKRL FDKGAVYRGF KVMPYSTALA
TPLSNFEASQ NYKDVQDPAV VVSFPLVEDP NTLLLAWTTT PWTLPMNTGL CAHPDFEYVK
ILDEATGKHY ILLEALLRTL YKDPKKAKYK VVEKLKGKDL LGWKYEPLFN YLYDEFKDHG
FKVLNDTYVT ADSGVGIVHQ APAYGEDDYR VALAAGVISD TRPPPNPVDD AGCYTSVVKD
FEGQHVKAAD KAIIKHLKGT GRMIVDSQLT HSYPFCWRSD TPLIYRTVPS YFIKIQDIVP
QMLENIAGSH WVPSFVKEKR FANWISNSPD WAVSRNRFWG TPLPLWVSDD GKEMVCVGSV
EELKKLSGYE GELTDIHRDK IDDITIPSQQ GKGVLRRTPE VFDCWFESGS MPYASAHYPF
ENVEQFEKSF PGDFIAEGLD QTRGWFYTLT VLGTHLFGKL PFKNCVVNGI VLAEDGKKMS
KRLKNYPDPS LVMNSYGSDA LRLYLINSPV VRAETLRFKE AGVKEIVSKV LLPLWNSYQF
FEQQATLLKK VADLHFVFDP AAGKTNKNIL DRWILASCQS LLKFVNAEMA AYRLYTVVPR
LLELIDNTTN WYIRFNRRRL KGEYGMEDTK HALNTLFEVL YTLCRGLAPF TPFITDNIYL
RLLPHIPKEL HAEDNRSIHF LPFPEVREEL FDEVVERQVK RMQAVIELGR ICRDRANKGL
KIPLKTLVVI HPDQQYLDDV KSLENYICEE LNIRDLVLSS DEEKYKVQYS ATADFSVLGK
KLKKDAIKVK KALPNLTSQE IKDFLKKGEL LVDGIKVEAE DLMVKRGLAK DDANKDQEFN
TDNDVLIILD VASYPELEQE GLAREVIRRV QDLRKKAGLV PTDDVGMEYR VLSDPENLGL
EQAFENQGPL FEKALRRNVD KHVITEVEGK IPEGKDEKVI VEEEQELHKA TFMLRLVKL
//
