ID Q08UA2_STIAD Unreviewed; 1280 AA.
AC Q08UA2;
DT 31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2006, sequence version 1.
DT 24-JAN-2024, entry version 86.
DE RecName: Full=isoleucine--tRNA ligase {ECO:0000256|ARBA:ARBA00013165};
DE EC=6.1.1.5 {ECO:0000256|ARBA:ARBA00013165};
GN Name=ileS {ECO:0000313|EMBL:EAU64053.1};
GN ORFNames=STIAU_5224 {ECO:0000313|EMBL:EAU64053.1};
OS Stigmatella aurantiaca (strain DW4/3-1).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Archangiaceae; Stigmatella.
OX NCBI_TaxID=378806 {ECO:0000313|EMBL:EAU64053.1, ECO:0000313|Proteomes:UP000032702};
RN [1] {ECO:0000313|EMBL:EAU64053.1, ECO:0000313|Proteomes:UP000032702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DW4/3-1 {ECO:0000313|EMBL:EAU64053.1,
RC ECO:0000313|Proteomes:UP000032702};
RA Nierman W.C.;
RL Submitted (APR-2006) 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}.
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:EAU64053.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAMD01000132; EAU64053.1; -; Genomic_DNA.
DR AlphaFoldDB; Q08UA2; -.
DR PATRIC; fig|378806.16.peg.2975; -.
DR Proteomes; UP000032702; 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; 2.
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; 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.
PE 4: Predicted;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000313|EMBL:EAU64053.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EAU64053.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 60..747
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 910..1060
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 1280 AA; 143889 MW; D1E50282C2C31347 CRC64;
MGHVPSALPS GLARPFASHE RAHTGTAGGI THPVMSQPPA PLFATVPNEI DFPADERRTL
AFWKERRIFE QTLQGRDNAP AFIFYEGPPT ANGLPHNGHV LTRVIKDLFP RYKTMRGFRV
PRKAGWDTHG LPVEVEVEKE LRIHGKAEIE RYGVEPFTQR CIESVFRYTN EWERLTERIG
FWVDLPDAYV TYHRTYVESV WWALSELYRK GLLYQGHKVV WWWPQGGTAL SSGEVGMGYR
TVDDPSAYVA FPLKDAPDTG LLIWTTTPWT LPSNMFAAVN PSVDYVTVDA GDRKLIIAAA
LREELIKKLK KDLPVLATQK GSALVGQRYT PPYDVYAQRV GNTELPLKGG GTDAPAWRVI
GADFVTLSSG TGIVHIAPAF GEDDYNAFRQ ERTRFAQPDA LELFCAIRPD GTFSEDFPHL
TGRFVKDADK DIQRELKERG RLVLVEQYRH EYPFCWRADD DPLIQFARPA WYIRTTSVKD
QAIANNRQVN WVPEHIKEGR FGDFLANNVD WALSRERYWG TPLPLWVHSE TGEVEAISSL
QALREKPGNN LAAVEAELKE FLTHKPGATS SEHLIVHKPW IDKVTFEKPG TPGRFVRVPE
VVDVWFDSGC MPFAQWGYPH VAGSQEKFAQ AFPADFISEA IDQTRGWFYS LLMIGTLIFD
EETQRRQGLS PVQGFPLPYK TCIVLGHVSD KEGKKESKSK GNYTPPEIIL DEVRMDFAVL
DDKAAGVPGV AGEALIARED LEGLDIQEGA KVQLFRPDAP GVAVTVTVKV HKKLKRRVVL
LAKKELEALG VAPSARGADV MPVEVPRLAP AERVVLKDPA SRAPGADAFR WFFFAASPTW
SNTRHSLSNV RLLQKDFQVK LRNVYSFFTI YANIDGFSPA TGNAGATEAP WRAIRQSTGW
REPSQRTVLD RWILSEVQLA LRDATRSLDA YQVYEAAQRL VSLVDALSNW YLRRSRERFW
GPGLEQDKLD AYFTLYEALT TITALSAPFI PFFAEEMWGN LVRRPWPTSQ PESVHLGRFP
DVEERLIDEG LSAEMGAVRE LVSLGLKVRT DNRLKVRQPL ARADVVLSRR ELQDRVAVYR
ELIADELNVH EVRFLESGQE TDVVRYKVRP NLRAMGSRLG PKLAPVRKAF DAADSRSLQR
ELTLQGKVVL AVDGEQMTFP AEELEVLVEA NPGYAAAGAG VGVVVLHTEL TEALVDEGLV
RELLARVQAA RKDMALGYTD RIRLWVDGDA RVRKVTEEGR PLISRETLAS ELHVGPEGFT
GQEEEFNLNG LPARLRVERA
//
