ID A0A0G0MM76_9BACT Unreviewed; 692 AA.
AC A0A0G0MM76;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=isoleucine--tRNA ligase {ECO:0000256|ARBA:ARBA00013165};
DE EC=6.1.1.5 {ECO:0000256|ARBA:ARBA00013165};
DE Flags: Fragment;
GN ORFNames=UT31_C0001G0001 {ECO:0000313|EMBL:KKR04218.1};
OS Parcubacteria group bacterium GW2011_GWF2_39_13b.
OC Bacteria.
OX NCBI_TaxID=1618962 {ECO:0000313|EMBL:KKR04218.1, ECO:0000313|Proteomes:UP000034319};
RN [1] {ECO:0000313|EMBL:KKR04218.1, ECO:0000313|Proteomes:UP000034319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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}.
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 -!- 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:KKR04218.1}.
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DR EMBL; LBWH01000001; KKR04218.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0MM76; -.
DR PATRIC; fig|1618962.3.peg.1; -.
DR Proteomes; UP000034319; 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 Gene3D; 3.40.50.620; HUPs; 1.
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; 2.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
PE 4: Predicted;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KKR04218.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 88..315
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 365..549
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KKR04218.1"
SQ SEQUENCE 692 AA; 80295 MW; FA2FBA703A1725CA CRC64;
DGTGIVHLAP AYGEDDLRVG EKENLSVIHT VDQDGIVMSG FDIPGEGKFI KDTDKDIVEN
LKSRNLLFKE ESYEHDYPFC WRCDSPLLYF AKESWFIKMS DLREKLVINN QKINWEPSYI
KDGRFGEFIR EAKDWALSRE RYWGTPLPIW TCEKCGKQTC IGSKKELGVE MEDLHRPFID
EIKLKCACGG EMAREKDVID VWFDSGAMPF AQWGYPEKED SEKELKNHYP ADYISEAIDQ
TRGWFYTLLA IGTLMEECGV AKDGAPYKNV ICLGHVLDKH GKKMSKSKGN VVDPWEMCEK
FGADTLRWYL YTVNSAGDPK KFDIKDVQDK NRRVFGTLYN SLVFFKTYAD KDFLPTDIKS
ENILDKWIVS VFNFLAVEVI DCLEKYDVVS AAREIENFID DLSNWHIRRS RERFQRPACH
ACGKALAGRP KNAEKKNEAA QTLYFILMEL SKLIAPFAPF MAEEIYGELS NYCLSDPPSG
REAKADIRNP STGSGNKYLE SVHLCDYSEP DEKLINKELE EQMKQAREIV AKALALRMEK
KIKIRQPLNE LRFKIYDLRD KELLELIKDE LNVKNVIFDK NIKDEIELDV EITEELKEEG
WAREIARQIQ QMRKEAGFIP SDKIDVRFTI YDLRFKNLME KQDDFIKKET NAKSFEELKG
KEKFDLEKEI NLEGEKIKIG ITKKKRAQRE KG
//
