ID A0A3A9AJP4_9FIRM Unreviewed; 1052 AA.
AC A0A3A9AJP4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 18-JUN-2025, entry version 23.
DE RecName: Full=Isoleucine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02003};
DE EC=6.1.1.5 {ECO:0000256|HAMAP-Rule:MF_02003};
DE AltName: Full=Isoleucyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02003};
DE Short=IleRS {ECO:0000256|HAMAP-Rule:MF_02003};
GN Name=ileS {ECO:0000256|HAMAP-Rule:MF_02003};
GN ORFNames=D7V94_08865 {ECO:0000313|EMBL:RKI91790.1};
OS Parablautia intestinalis.
OC Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
OC Lachnospiraceae; Parablautia.
OX NCBI_TaxID=2320100 {ECO:0000313|EMBL:RKI91790.1, ECO:0000313|Proteomes:UP000280696};
RN [1] {ECO:0000313|EMBL:RKI91790.1, ECO:0000313|Proteomes:UP000280696}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0.1xD8-82 {ECO:0000313|EMBL:RKI91790.1,
RC ECO:0000313|Proteomes:UP000280696};
RA Liu C.;
RT "Murine metabolic-syndrome-specific gut microbial biobank.";
RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS
CC can inadvertently accommodate and process structurally similar amino
CC acids such as valine, to avoid such errors it has two additional
CC distinct tRNA(Ile)-dependent editing activities. One activity is
CC designated as 'pretransfer' editing and involves the hydrolysis of
CC activated Val-AMP. The other activity is designated 'posttransfer'
CC editing and involves deacylation of mischarged Val-tRNA(Ile).
CC {ECO:0000256|ARBA:ARBA00025217, ECO:0000256|HAMAP-Rule:MF_02003}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=tRNA(Ile) + L-isoleucine + ATP = L-isoleucyl-tRNA(Ile) + AMP +
CC diphosphate; Xref=Rhea:RHEA:11060, Rhea:RHEA-COMP:9666, Rhea:RHEA-
CC COMP:9695, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58045,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78528, ChEBI:CHEBI:456215; EC=6.1.1.5;
CC Evidence={ECO:0000256|ARBA:ARBA00048359, ECO:0000256|HAMAP-
CC Rule:MF_02003};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|HAMAP-Rule:MF_02003};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245, ECO:0000256|HAMAP-
CC Rule:MF_02003}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_02003}.
CC -!- DOMAIN: IleRS has two distinct active sites: one for aminoacylation and
CC one for editing. The misactivated valine is translocated from the
CC active site to the editing site, which sterically excludes the
CC correctly activated isoleucine. The single editing site contains two
CC valyl binding pockets, one specific for each substrate (Val-AMP or Val-
CC tRNA(Ile)). {ECO:0000256|HAMAP-Rule:MF_02003}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC IleS type 2 subfamily. {ECO:0000256|ARBA:ARBA00007078,
CC ECO:0000256|HAMAP-Rule:MF_02003}.
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:RKI91790.1}.
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DR EMBL; RAYQ01000008; RKI91790.1; -; Genomic_DNA.
DR RefSeq; WP_120469054.1; NZ_RAYQ01000008.1.
DR AlphaFoldDB; A0A3A9AJP4; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000280696; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0002161; F:aminoacyl-tRNA deacylase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004822; F:isoleucine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd07961; Anticodon_Ia_Ile_ABEc; 1.
DR CDD; cd00818; IleRS_core; 1.
DR FunFam; 3.40.50.620:FF:000063; Isoleucine--tRNA ligase; 1.
DR FunFam; 3.40.50.620:FF:000075; Isoleucine--tRNA ligase; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 1.10.730.10; Isoleucyl-tRNA Synthetase, Domain 1; 1.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR HAMAP; MF_02003; Ile_tRNA_synth_type2; 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 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.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_02003};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_02003};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_02003};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02003};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_02003};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_02003};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_02003}; Reference proteome {ECO:0000313|Proteomes:UP000280696};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_02003}.
FT DOMAIN 18..633
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 690..839
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 48..58
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT MOTIF 603..607
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT BINDING 606
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
SQ SEQUENCE 1052 AA; 120093 MW; 1950AE57A3D64A1E CRC64;
MYQKVSTDLN FVEREKKIEK FWKENDIFKK SMENRKGCPT YTFYDGPPTA NGTPHIGHVL
TRVIKDMIPR YRTMKGNMVP RKAGWDTHGL PVELEVEKLL GLDGKEQIEE YGLDPFIRKC
KESVWKYKGM WEDFSGTVGF WADMDDPYVT YHDDFIESEW WALKEIWKKG LLYKGFKIVP
YCPRCGTPLS SHEVAQGYKA VKERSAVVRF KVVGEDAYFL AWTTTPWTLP SNVALCVNPQ
ETYVKIKAAD GYTYYMAQAL LDPVLGKLAG EGESAYEILE TYTGKDLEYK EYEPLFACAG
EAAAKQNKKG HFVTCDNYVT MTDGTGIVHI APAFGEDDAQ VGRKYDLPFV QFVDSKGNMT
QETAYAGKFV KDADPAILMD LDKEGKLFDA PKFEHDYPFC WRCDTPLIYY ARESWFIKMT
AVRDDLVRNN KTVNWIPESI GEGRFGNWLE NIQDWGVSRN RYWGTPLNIW ECEECGYQDA
IGSREELEKL SGNPAARTVE LHRPYIDEIT CTCPKCGKAM KRVPEVIDCW FDSGAMPFAQ
HHYPFENKEL FESQFPAQFI SEAVDQTRGW FYSLMAESTL LFNKSPYENV IVLGHVQDEN
GQKMSKSKGN SVDPFEALAA YGADAVRWYF YINSAPWLPN RFHGKAVMEG QRKFLGTLWN
TYAFFILYAN IDDFDATKYT LEYDKLPVMD KWLLSKLNTA VRETDEHLDN YRIPEAARVL
DNFVDEMSNW YVRRCRERFW AKGMEQDKVN AYMTLYTALV QICKCAAPLI PFMTEEIYQN
LVRSNDKNAP ESIHLCDYPE ANEAMIDKKL EENMEEALHI VVLGRAARNA AGMKNRQPIG
RMYVKAVHSL ESYFMDIIKD ELNVKEVAFK EDVSDLTSYS FKPQLKTVGP KYGKQLGGIR
EYLSAVDGTQ AMKELKADGA LKFEVSGVEI SLGEEDLLID VAQKAGLVTE ADNYVTVVLD
TNLSPDLIEE GFVYEVISKI QTMRKDAGFE VMDHIMVTVN GNAKIAGIVN ANKETICEKV
LAEDILEDAK LASMKEWNVN GEKVTIGVEI KG
//
