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Database: UniProt
Entry: Q7RNG8_PLAYO
LinkDB: Q7RNG8_PLAYO
Original site: Q7RNG8_PLAYO 
ID   Q7RNG8_PLAYO            Unreviewed;      1294 AA.
AC   Q7RNG8;
DT   15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2003, sequence version 1.
DT   24-JAN-2024, entry version 123.
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=PY01849 {ECO:0000313|EMBL:EAA21241.1};
OS   Plasmodium yoelii yoelii.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX   NCBI_TaxID=73239 {ECO:0000313|EMBL:EAA21241.1, ECO:0000313|Proteomes:UP000008553};
RN   [1] {ECO:0000313|EMBL:EAA21241.1, ECO:0000313|Proteomes:UP000008553}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17XNL {ECO:0000313|EMBL:EAA21241.1,
RC   ECO:0000313|Proteomes:UP000008553};
RX   PubMed=12368865; DOI=10.1038/nature01099;
RA   Carlton J.M., Angiuoli S.V., Suh B.B., Kooij T.W., Pertea M., Silva J.C.,
RA   Ermolaeva M.D., Allen J.E., Selengut J.D., Koo H.L., Peterson J.D., Pop M.,
RA   Kosack D.S., Shumway M.F., Bidwell S.L., Shallom S.J., van Aken S.E.,
RA   Riedmuller S.B., Feldblyum T.V., Cho J.K., Quackenbush J., Sedegah M.,
RA   Shoaibi A., Cummings L.M., Florens L., Yates J.R., Raine J.D., Sinden R.E.,
RA   Harris M.A., Cunningham D.A., Preiser P.R., Bergman L.W., Vaidya A.B.,
RA   van Lin L.H., Janse C.J., Waters A.P., Smith H.O., White O.R.,
RA   Salzberg S.L., Venter J.C., Fraser C.M., Hoffman S.L., Gardner M.J.,
RA   Carucci D.J.;
RT   "Genome sequence and comparative analysis of the model rodent malaria
RT   parasite Plasmodium yoelii yoelii.";
RL   Nature 419:512-519(2002).
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}.
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:EAA21241.1}.
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DR   EMBL; AABL01000503; EAA21241.1; -; Genomic_DNA.
DR   STRING; 73239.Q7RNG8; -.
DR   PaxDb; 73239-Q7RNG8; -.
DR   EnsemblProtists; EAA21241; EAA21241; EAA21241.
DR   VEuPathDB; PlasmoDB:Py17XNL_001303372; -.
DR   InParanoid; Q7RNG8; -.
DR   OMA; EIIVIHK; -.
DR   Proteomes; UP000008553; 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; cd07961; Anticodon_Ia_Ile_ABEc; 1.
DR   CDD; cd00818; IleRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
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   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:UP000008553}.
FT   DOMAIN          102..828
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          884..1073
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   REGION          992..1021
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1294 AA;  153351 MW;  9E4120FD969CDC08 CRC64;
     MFLKRIKQKV QFIRKFKTLK SEIASVKIEI KKKENNICTV QNIFCEKKKK KIHTIIEKIG
     HEYPRNTHKI NSPKEKKNSE MATKTTFDYV PDNPNIVEEE EKILKYWKNI NAFELSNKLS
     KNRKPYIFYD GPPFATGLPH YGHLLAGIIK DCVTRYFYQS GYSVERRFGW DCHGLPVEYE
     IEKENNINKK EDILKMGIDV YNEKCRSIVL KYSNEWVNTV ERIGRWIDYK NDYKTMDKDF
     MESVWWIFSQ LYKKNYIYKS FKVMPYSCKC NTPISNFELN LNYKDVSDPS IIVGFILLEN
     FPTFPECLEI QKEIDASDSP TKILNEKPQD GKKEEIDFFK KYEKLYEPYF SRVKSNELKT
     SNFDENKKRE DFSESTSDTS NKVTEIIAWT TTPWTLPSNL ALCVNENLIY LRILNKENNR
     IFIFAECRME WVIKELRLKI ENICLLNRFK GKYLNGLKYK PLFNHFYEKF NFKENAYRIL
     CDEFVTNTVG TGIVHCAPTY GEDDFRVCEK NKIINPEKSI FIDPLDSNGY FTNEIKEVEN
     MYIKDADIVI KKILKEQNRL LSNNMIVHSY PFCWRSDTPL IYRAIPAWFV RVNNYTDKLV
     KNNDTTYWIP AHVKEKKFHN WIKDAKDWCI SRNRYWGTPI PIWTDEKMEQ IICIESIKQL
     ETLSGVTNIS DLHRHNIDHI TIDNPRGKNY PKLKRIPEVF DCWFESGSMP YAKVHFPFYC
     SDIANSEIDI SKVSMDQFNQ IFPADFIAEG LDQTRGWFYT LLVISTLLFD KAPYKNLICN
     GLILASDGKK MSKRLKNYPD PIYILNKYGA DSLRLYLINS VAVRAENLKF QEKGVNEIVK
     SFILPFYHSF RFFSQEVIRY ETSYKTTFSF SNKYIYDNNN NIMDQWIFSS IQNLIKSVHY
     EMKQYKLYNV LPKLLNFIEN LTNWYIRLNR DRMRGVIDEI NCLMSLNTIY KTLYLFTLMM
     SPFTPFISEY IYKMLQQVQG FNLVMSSDTH KNVQNGQNVQ NDQNGQNVQN GQNDQNDQND
     QNKSVHFHML PEVDDNYTIR YEIIELIEKM KSVIILGRIL REKRKCPNKR PLKSIKILHR
     ENKFFENFDK IANYIKDELN ILNIEYSTDV SCLTFSVIPN YKKLGTKLGA NLKNIQNKIK
     NMNMEDIKNY EQNKKIIIDN ILLEDDDIII NLKHNLNLEH IEAISENSIT ILMDFTADEQ
     LNNMENAREI CNNIQKMRKK LALSQNSPVQ MHIFIQNETF KNNMIKETEY IHKCLRRNLN
     IINTVDQMEK LQNKFHQETF TVSGQEVIAI FTQN
//
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