ID A0A1F8ECE2_9BACT Unreviewed; 1171 AA.
AC A0A1F8ECE2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=A2649_03175 {ECO:0000313|EMBL:OGM98267.1};
OS Candidatus Yanofskybacteria bacterium RIFCSPHIGHO2_01_FULL_41_26.
OC Bacteria; Candidatus Yanofskybacteria.
OX NCBI_TaxID=1802661 {ECO:0000313|EMBL:OGM98267.1, ECO:0000313|Proteomes:UP000176893};
RN [1] {ECO:0000313|EMBL:OGM98267.1, ECO:0000313|Proteomes:UP000176893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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=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, ECO:0000256|HAMAP-
CC Rule:MF_02003};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02003};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_02003}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {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:OGM98267.1}.
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DR EMBL; MGJB01000017; OGM98267.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8ECE2; -.
DR STRING; 1802661.A2649_03175; -.
DR Proteomes; UP000176893; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0002161; F:aminoacyl-tRNA editing 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; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.620; HUPs; 3.
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; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
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; PF00300; His_Phos_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 2.
DR PRINTS; PR00984; TRNASYNTHILE.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 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|HAMAP-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}; Zinc {ECO:0000256|HAMAP-Rule:MF_02003}.
FT DOMAIN 12..473
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 714..844
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 895..1036
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 43..53
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT MOTIF 810..814
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT BINDING 813
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
SQ SEQUENCE 1171 AA; 136123 MW; A27027BA1026D30B CRC64;
MADSNFVDKE KKILDFWRDN NIFKKSLENR QKAKRFVFFE GPPTANGLPH VGHFLTRIYK
DVFGRYKTMR GYFVLRKAGW DTHGLPVEIE VEKELGFKNK KDIETYGIDK FNKKAKESVW
KYKNEWEQMT KKMGFWLDMN DPYITYKNQY IESLWAIIKK IWDRKLLYLA HRVVPFCTRC
GTPLSSHEVA QGYKTVTDKS VFVKFKVKNS ARSNLVGDLR SNLYVLAWTT TPWTLPGNVA
LAVGKDIGYT AVKVGDEIFI LAESAVGRVL KDTKYEILNT TYKGSDLLGL EYEPLFSVEK
LKSDKSYRIY DADFVSTEDG TGVVHTAVMY GEDDYNLGTK LGLPKFHTVD ERGRFINIGH
GLDRKYVKAK ETEDLILDYL TTNHLLLITF NYEHDYPFCW RCDTPLLYYA KESWFIKMSA
VNKELIENNR KTNWIPEHIK EGRFGQWLKE GKDWAFSRER YWGTPLPIWE CNQPVRTTES
VRSGGCDNKT TIGSVKELEK LSVSPQNTYY IMRHGFSTRN EGGDAIVNTR QENDAYHLTS
EGEKMVEKSI ELLKLEGVDY IFSSPFIRTH ETASIAGKIL HQKVVIDERL HEYRSASGWD
GKPVSRYIAG GGGDRTMDSR QRDAESLNDV RKRMTEFMFE LEAKYKNKNI LIVSHGDPLW
LLNTIAEGLT GDQILNKEGK AQWYPRIAEI KNLNWSKIPR NELGELDLHR PYIDSVVLKC
SKCGSDMKKV PDLIDVWFDS GAMPYAQWHW PFDNKKISKE QFPADFIVEA IDQTRGWFFT
LLAISTLLEK GAPYKNVMVL GHTLDEKGAK MSKSKGNYVP VMEFMDKYGV DVLRWYFLSS
MTIGESKSVI PREIEDKQKG FFSTLDNCLR FYELYGKGEF GSFHDTKGKN LNLLDRWILS
KLNRLLGEVS DGLDKYDPTS AAKTIEKFVA EDLSNWWLRR SRKRKEALGL LRFLLLEIAK
VIAPFIPFMA EDIHMRLHRG RSSGTESVHL HDWPQVNKKQ INKELEKQME EIKNIVTLGL
AQRKEKQIKV RQPLRAVHLG LSNEFPKDLE ILVKEELNVK EIVYDKSQKE LVCLNIELDQ
TLVYEGYARE LMRQIQDMRK EAKYKVDDEI FGQWHSDDKE ISEAIRQWSD EIKKEVLLSE
FRNGPHDEKA YDIEKEFELA PQRKIWIGLR K
//
