ID A0A0S4J4I8_BODSA Unreviewed; 1194 AA.
AC A0A0S4J4I8;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=BSAL_92865 {ECO:0000313|EMBL:CUG86385.1};
OS Bodo saltans (Flagellated protozoan).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Eubodonida; Bodonidae; Bodo.
OX NCBI_TaxID=75058 {ECO:0000313|EMBL:CUG86385.1, ECO:0000313|Proteomes:UP000051952};
RN [1] {ECO:0000313|Proteomes:UP000051952}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lake Konstanz {ECO:0000313|Proteomes:UP000051952};
RG Pathogen Informatics;
RL Submitted (SEP-2015) 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; CYKH01001287; CUG86385.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S4J4I8; -.
DR VEuPathDB; TriTrypDB:BSAL_92865; -.
DR OMA; EIIVIHK; -.
DR OrthoDB; 656at2759; -.
DR Proteomes; UP000051952; 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; 4.
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; 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; 2.
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; 2.
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:UP000051952}.
FT DOMAIN 65..666
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 678..770
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 822..975
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 1194 AA; 136007 MW; CB53FBF734326EBF CRC64;
MLRRGTFWLS SSSSLKSKTT IYQFVRQQPN NSNPFAPTMA AAPAGTGPLK DFPEPLNFAK
MEEEVLAYWK EIKAFETSLK KSEGRKPYTF YDGPPFATGL PHYGHILAGT IKDVVCRYAH
QTGHHVERRF GWDCHGLPIE FEIEKLLGIK SSHDVKAFGI ANYNAECRKI VMRFANEWEE
VVTRVGRWID FKNDYKTMNL SYMESVWWVF KQLWEKKLVY RGFKVMPFST SCTTPLSNFE
ANMNYKDVSD PSAMVSFPLE EDNNTHLIAW TTTPWTLPSN LALCVNPDME YVKVLDAKTS
RHYIFAECRI GEVYKINAKD KDKELPYTSD SGTGVVHCAP GFGEEDNRAC LANKVFEKGT
IVCPVDENGH FTADVTEWAG RYIKDCDNEI LKVIQQNGRL INKAAVVHSY PFCWRSDTPL
IYKAVDSWFV GVESIRDKLL EANAATSWVP DFVKSKRFSN WLEDAKDWNV SRNRYWGTPL
PVWRSDDWEE IICIGSVAEL EELSGVTGIN DIHREFVDTI TIPSKFFFYW EEIICIGSVA
ELEELSGVTG INDIHREFVD TITIPSKRPG MPPLRRVEEV FDCWFESGSM PFGQAHYPFE
NKEKFMDGFP ADFVAEGLDQ TRGWFYTMLV LSTALFGHSS YKNLVVNGLV LAEDGKKMSK
RLKNYLFFFV PACLPSVASR KCLDGFPADF VAEGLDQTRG WFYTMLVLST ALFGHSSYKN
LVVNGLVLAE DGKKMSKRLK NYPEPTIVVD NYGADALRLY LINSPVVRAE PLRFREAGVK
DIVKDVFLPL ANAAKFFITN ANRFISEGGS ISINTTSSNE MDRWILASAQ TLVKCVHNEM
NQYHLYTVVP HVLRFVEELT NWYVRMNRRR IKGTDEDRQD WGNSLSTFLD VLFTVSRVLA
PFTPFIAESL YQRIKPLLPE EVQEDSIHYI MLPEVDASKF DEVLEQSMSR MIKVVDLVRV
LRDRIGIPMK MPVRQVIVVH PNREYLDDVS KMGTYIKHEV NAFDVNFSEE GEYVITKLDG
NMGAIGKRFK KEGMSIKKAL MAMGPEEVRA FIAAEGGVVC DQQLTMEDVK ILRTFREGIE
EFESNTDNDV VVLVDKRSDE ALVNAWRARE FVNRVQQLRK KAKLVITDRV DVFFSSPDAG
LVASILGASE QISQTVKGLW TTEDKMPADA EKIAEEDNDI SEIPIKITFT KPSA
//
