ID A0A2A4Q219_9BACT Unreviewed; 1154 AA.
AC A0A2A4Q219;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=isoleucine--tRNA ligase {ECO:0000256|ARBA:ARBA00013165};
DE EC=6.1.1.5 {ECO:0000256|ARBA:ARBA00013165};
GN ORFNames=COB87_03045 {ECO:0000313|EMBL:PCH90667.1};
OS Candidatus Wolfebacteria bacterium.
OC Bacteria; Candidatus Wolfebacteria.
OX NCBI_TaxID=2030812 {ECO:0000313|EMBL:PCH90667.1};
RN [1] {ECO:0000313|EMBL:PCH90667.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NORP156 {ECO:0000313|EMBL:PCH90667.1};
RX PubMed=29099490; DOI=.1038/ismej.2017.187;
RA Tully B.J., Wheat C.G., Glazer B.T., Huber J.A.;
RT "A dynamic microbial community with high functional redundancy inhabits the
RT cold, oxic subseafloor aquifer.";
RL ISME J. 12:1-16(2018).
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:PCH90667.1}.
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DR EMBL; NVRX01000009; PCH90667.1; -; Genomic_DNA.
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; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
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.
PE 4: Predicted;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 14..493
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 695..841
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 886..1029
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 1154 AA; 131198 MW; AA664D47BD395015 CRC64;
MSDKSDFAKR EEEVLDFWNK ENIFQKSLSK KSPKGVFTFY DGPPFATGLP HFGHVLASTI
KDAIPRYKTM QGFTVPRRWG WDCHGLPLEA QVEKEFNVST KQEIIDDIGI ENFVERAKKV
VLTYRDDWKK IIPRLGRFVD MENDYRTMDP SYTESVWWVF KTLYNKELIY KGFKVLHLSP
LLGTELSNIE VAQGYKDITD FAVTVKLPIK GEDTSLLVWT TTPWTLPGNT AAAVHSDLTY
VKVKVTGSEK LDGTYILSKE KLSLFEEVEH TVLEEMKGKD LVGKEYEPPF NYYKDKDIEG
KENAWKIYAA DYVTEESGTG AVHIAPAFGA EDLELAQKFG IPIVHHINKS GKFVDEVTDF
KGMDAKPKDD HQATDIEIIK YLAHAGKLFK KEKIKHSYPH SWRTDEPLLN YAMDSWFVNA
PKITKKLVAE NEKVNWVPKE IGSKRFGNWL KGGKEWSISR SRFWGAPLPV WESKEGSRIV
LGGIEDLKKN VKKSGXTYTI MRHGEAQTNA AGMLTHNDSI PSDLTDAGRA KALETAKELQ
GITKIIASPL KRTQQTAKIV AAEIGMSEKD IITEERLREI NFGIFNGKSV KEYHAFFETN
KDLMFARPEG AESWCDVKKR VGEFLYEIEN TYKNETILIV THNSPAFMLA RVMEGHDLKM
CAEVWEKHKN AFVLPGTTRD LPFVPIPHNA EYELDFHRPF IDEIILEKNG EEYTRILDVF
DCWFESGAMP YGQKHFPYEN LDTFNPKGGL FSKPKGYPAQ FIAEGVDQTR GWFYSLIVLG
VGLFGKAPFE NVIVNGMVLG EDGKKLAKKL KNYSDPIEVV DMYGADALRY YMLSSSIVRG
EDLVFTNDGV KEISQKITGR LHNVFSFYSL YESVVEKKKG NTNVLDTWIT SRLHQLIKDT
ERGYDAYELD KATRPLLDFI DDLSTWYVRR SRDRIKNGGE DAAAALYTLH KTLLTLSKVM
APTMPFYAEY LYRNLKEEQD IESVHLCDWP TAGPVDEKVL STMKRVRGVV SDALMMRQKA
GFKVRQPLNA LTLPERVSFS KEYQTIIREE VNVENIVFSG TEMILDTXLT PXLVEKGMVR
DFIRAVQDAR KKADFSPHDK AILTIAGPST FLDAYKEDIM SVAGVEKIQR VQELPGGAEV
EVGDKTLTIL VAHA
//
