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Database: UniProt
Entry: A0A0R3W9N7_TAEAS
LinkDB: A0A0R3W9N7_TAEAS
Original site: A0A0R3W9N7_TAEAS 
ID   A0A0R3W9N7_TAEAS        Unreviewed;      1282 AA.
AC   A0A0R3W9N7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
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=TASK_LOCUS7185 {ECO:0000313|EMBL:VDK37996.1};
OS   Taenia asiatica (Asian tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Cyclophyllidea; Taeniidae; Taenia.
OX   NCBI_TaxID=60517 {ECO:0000313|Proteomes:UP000046400, ECO:0000313|WBParaSite:TASK_0000718401-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:TASK_0000718401-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDK37996.1, ECO:0000313|Proteomes:UP000282613}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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; UYRS01018585; VDK37996.1; -; Genomic_DNA.
DR   STRING; 60517.A0A0R3W9N7; -.
DR   WBParaSite; TASK_0000718401-mRNA-1; TASK_0000718401-mRNA-1; TASK_0000718401.
DR   Proteomes; UP000046400; Unplaced.
DR   Proteomes; UP000282613; 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:UP000282613}.
FT   DOMAIN          19..676
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          732..911
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   REGION          1019..1050
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1282 AA;  144237 MW;  E2208639BA09EF07 CRC64;
     MSRDDLPPSL NFSEEEEKIL QFHNEIEAFK TSCKLSAKRP PFTFYDGPPF ATGLPHYGHI
     LAGTIKDVVT RFAYSEGYHV ERHFGWDCHG LPVEYEVDKL NNINGPQDVE AMGVAAYNAK
     CREIVMRYSL QWRSVVQRIG RWIDFDEDYR TMYPTFMESV WWIFKQLYEK GLVYRGVKVM
     PFSTACSTPL SNFEAGLNYK DVQDPAIVVS FPVEGLDDNI SVELLAWTTT PWTLPSNLAL
     CVNPEKDYVK IKDKSRGRVF IIMECRLEWF YKKAEDYEIL EKMKGEKLVG LKYKPLFDYF
     IKLKESRGAF RVVGDAYVTE ETGTGVVHQA PYFGEDDFRV CLREGIVTKE MAPVCPVDAS
     GRFTAEVVDF AGQYVKDADR LICQHLKHAG RLVHQSTLQH SYPFCWRCVY VFFTFIRSHP
     ASFKSQIQHC DWVTGGLGYR SDTPLLYKAV PTWFVRVECL VERLLVNSAA TYWVPEFIKE
     KRFANWLRDA RDWAISRNRY WGTPIPLWVS EDFEEVVCIG SLDELERLSG HRVTDLHKEF
     VDPITIPSRM GKGELHRISE VFDCWFESGS MPYAQMHYPF ENAERFNSGF PADFVAEGVD
     QTRGWFYTLF VLSTALFDQP PFKNLIVNGI VLASDGQKMS KRQKNYPDPC KIVEQYGADA
     LRLYLVNSPV VRAQSLRFSE SGVRDVLKDV FIPWYNAFRF LMKSGIEPWE RAHGTTFRVR
     PEAWPKSRNL MDRWVLSFTQ SLLSFVRTEL RAYRLYTVVP RLVCFIEQLV NWYIRMNRRR
     LKGEAPTETG VATDAEEDWY GALHTLVKVF FQLIFVMAPF APFFTEFIYQ RLKAKLDFSK
     FPLEGLSDGE SGAVGADLAP ASVHYLVGVS AESRGIDEAL EARVAWMQAA VELGRSIRTR
     HDLPLKAPLR ASVVIHPLAE AREAVTALAS YVTEELNVRN LTVTHDKATY QVRLRARLNP
     VLGARLRARL RPLAAAVAAL PQSSLEAYLT TGEMTVEGEL LSGDDVTVDY VVGDEANTEN
     NNVKAKGSKG KSKENGGAPP PEVADGPKYK AHADGKGMLV LLDVRADTEL EEERVAREII
     NRIQRARKKG NLVPEDAIQV VISTISEVLP RVLASHAALI DATVKQPIVC CTTEDAASTT
     ATAAVQARGE QLGGIVVSDS TTIPPDDLVV TIFHRIAATK DAVGCSTTTA TATSKPQVPG
     VCSSAKSLKV VCPVVKKSID VCLVDAAGKQ LITGVLELLD VVRGAFDWRL AANLRLMHSG
     TELTCDSTVN VLNLAGQELC LV
//
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