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Database: UniProt
Entry: M7ZSS4_TRIUA
LinkDB: M7ZSS4_TRIUA
Original site: M7ZSS4_TRIUA 
ID   M7ZSS4_TRIUA            Unreviewed;      1066 AA.
AC   M7ZSS4;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 57.
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=TRIUR3_08914 {ECO:0000313|EMBL:EMS62671.1};
OS   Triticum urartu (Red wild einkorn) (Crithodium urartu).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4572 {ECO:0000313|EMBL:EMS62671.1};
RN   [1] {ECO:0000313|EMBL:EMS62671.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23535596; DOI=10.1038/nature11997;
RA   Ling H.Q., Zhao S., Liu D., Wang J., Sun H., Zhang C., Fan H., Li D.,
RA   Dong L., Tao Y., Gao C., Wu H., Li Y., Cui Y., Guo X., Zheng S., Wang B.,
RA   Yu K., Liang Q., Yang W., Lou X., Chen J., Feng M., Jian J., Zhang X.,
RA   Luo G., Jiang Y., Liu J., Wang Z., Sha Y., Zhang B., Wu H., Tang D.,
RA   Shen Q., Xue P., Zou S., Wang X., Liu X., Wang F., Yang Y., An X., Dong Z.,
RA   Zhang K., Zhang X., Luo M.C., Dvorak J., Tong Y., Wang J., Yang H., Li Z.,
RA   Wang D., Zhang A., Wang J.;
RT   "Draft genome of the wheat A-genome progenitor Triticum urartu.";
RL   Nature 496:87-90(2013).
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};
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DR   EMBL; KD079244; EMS62671.1; -; Genomic_DNA.
DR   AlphaFoldDB; M7ZSS4; -.
DR   STRING; 4572.M7ZSS4; -.
DR   eggNOG; KOG0434; Eukaryota.
DR   OMA; LLTYWNT; -.
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; cd07961; Anticodon_Ia_Ile_ABEc; 1.
DR   CDD; cd00818; IleRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
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.
PE   4: Predicted;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000313|EMBL:EMS62671.1}; 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}.
FT   DOMAIN          2..584
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          640..712
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
SQ   SEQUENCE   1066 AA;  120621 MW;  790CF076FA599A33 CRC64;
     MRRFGWDCHG LPVEFEIDKL LGITNRQQVL DLGIGKYNET CRGIVTKYVA EWEAVVTRTG
     RWIDFKADYK TMDINFMESV WWVFGQLWDK DLVYKGFKVM PYSTGCKTAL SNFEAGLDYR
     TVPDPAVMVS FPVVGDADNA ALVAWTTTPW TLPSNLALCV NANLVYTKVK DKSNGTVYIV
     AESRLGQLPV KAKASGKKQA PSKGSNAEAV QGGLDTESYE LLAKIPGSSL VGLKYTPLFD
     FFLEFQDTAF RVIADNYVTD DSGTGVVHCA PAFGEDDHRV CLSAGIIEAS GLVVAVDDDG
     HFIEKISQFK GRHVKEADKD IINAVKDKGR LVSKGSIEHS YPYCWRSGTP LIYRAVPSWF
     IKVEKIRDQL LECNKETYWV PDYVKEKRFH NWLEGARDWA VSRSRFWGTP LPVWISQDGE
     EIVVMDSIEK LERLSGVKVN DLHRHHVDDI TIPSSRGPEF GVLKRVEDVF DCWFESGSMP
     YAYIHYPFEN RELFEKNFPG NFVAEGLDQT RGWFYTLMVL STALFGKPAF KNLICNGLVL
     AEDGKKMSKS KQNYPSPMEV IDEYGADALR LYLVNSPVVR AESLRFKRIG VFGVVKDVFL
     PWYNAYRFLV QNAKRLEVEG LTAFSPIDQA SLRKSSNVLD HWIHSATESL VSFVHQEMDA
     YRLYTVVPYL VKYIDNLTNI YVRFNRKRLK GRTGEEDCKI SLSTLYHFFT KICGKRQVNQ
     SRAFIFAVSL PQLGRDIQVR LLALYYAICT FLQIAAMEMV VVHPDSEFLE DITGKLKEYV
     MEEMNVKTVT PCNDPMKYAS LRAEPNFRTF CFLSVLGKRL GKDMGKVSNE VKKMTQEQIL
     AFEQSGEISF LGHCLTLDDI KVVRQFKRPV DVSEKEIDAA GDGDVLVILD LRADQSLIEA
     GVAREVVNRI QKLRKTAQLE PTDLIDVYYE SVDNSNTLEE ILQSQDQYIR DVLGNSLVPK
     AAATSDMVVI CEESHTVHDM SFVIYIARCM PVLAADLLSY ASGNSDHVEA LRVYLLSRSI
     SRLKNEFQTG NGKITVKCIE GYPPIDLQLG KHIFLSAGDF YQANRS
//
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