ID   A0A066X8M5_COLSU        Unreviewed;       949 AA.
AC   A0A066X8M5;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 45.
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=CSUB01_02587 {ECO:0000313|EMBL:KDN64024.1};
OS   Colletotrichum sublineola (Sorghum anthracnose fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum graminicola species complex.
OX   NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN64024.1, ECO:0000313|Proteomes:UP000027238};
RN   [1] {ECO:0000313|Proteomes:UP000027238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX   PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA   Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT   "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT   of cultivated sorghum.";
RL   Genome Announc. 2:E0054014-E0054014(2014).
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:KDN64024.1}.
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DR   EMBL; JMSE01001165; KDN64024.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A066X8M5; -.
DR   STRING; 1173701.A0A066X8M5; -.
DR   eggNOG; KOG0433; Eukaryota.
DR   HOGENOM; CLU_001493_7_2_1; -.
DR   OMA; HCWRCKT; -.
DR   OrthoDB; 656at2759; -.
DR   Proteomes; UP000027238; 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; 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; 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.
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:UP000027238}.
FT   DOMAIN          34..663
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          703..793
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
SQ   SEQUENCE   949 AA;  104555 MW;  07598860D172BFD8 CRC64;
     MSKSWASTLR LPKSTFPPRP LSQFRADYLR RSADDFYQWQ LSNESRPEFV LHDGPPYANG
     GLHVGHALNK ILKDMVNRVK VQQGYRIRYR PGWDCHGLPI EMKAVGASGG KDMTATEIRK
     AARQLASATV LEQMDGFRSY GVMADWNARW TTMDPDFEVR QLRLFQQMVR RGLIYRKSKP
     VYWSPSSRTA LAEAELEYNE NHVSTAAYVR YPITTGPSVA GVSGQLYAII WTTTPWTLPA
     NRAIAIHEDL DYAVISVKGN SYLTAVSRLE TVKALFTEEE PQVVVSSIKG SKLQGLKYHN
     RLQGADSAPQ PIIHADFVSA DSGTGLVHIA PGHGFEDYEA CAQLGIDAFA PIDDEGNFTR
     EAFPDAPEKL TEASSILKGG SKAVLALIQD DVLGAAKYKH KYPYDWRTKQ PVVMRSTAQW
     FADVDSIKDD AVNALKDVKF VPASGRNRLE SFVVGRSEWC ISRQRAWGVP IPALYNADGD
     AVVTEESVEH IISVIQQRGI DAWFSDAPDE PAWVAPSLKG QFRRGTDTMD VWFDSGSSWT
     ESNGQAGVYL EGSDQHRGWF QSSLLSYVAA QRAESDGATH VQPKPPFKTL ITHGFTLDQA
     GKKMSKSIGN TITPAQIMDG TLLPPIKVRG KAKVAGAGPT YEALGPDALR LWAASSEYTK
     DVAVGQAVLK SVHTILVKYR TIIKMLTGSM HESARTAPTT ALDHIALVQL KDVMEEVHNA
     FAAHEFYKAF NALNRWVAND LSAFYLEAMK DRLYCGDGGG VLEPIFLGFL RMLSPMTPLL
     VEEAWDHRPE FMKADRALLH PLQTPHDAPI HDRPPSAIGE ASLRKDLPVL MSVSGAVKAA
     LEKGRLAKVL GSSLQSSVVV TTEDRAVAGV LGKYGEELEA MFVVSSVETN AEVPSGSAWR
     YDEVFEVNGA KGTVSVLPPK EHKCPRCWRY VAPKEDALCG RCEDVVSSL
//