ID A0A142X875_9BACT Unreviewed; 1190 AA.
AC A0A142X875;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
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:AMV23175.1};
GN ORFNames=VT84_02105 {ECO:0000313|EMBL:AMV23175.1};
OS Gemmata sp. SH-PL17.
OC Bacteria; Planctomycetota; Planctomycetia; Gemmatales; Gemmataceae;
OC Gemmata.
OX NCBI_TaxID=1630693 {ECO:0000313|EMBL:AMV23175.1, ECO:0000313|Proteomes:UP000076098};
RN [1] {ECO:0000313|EMBL:AMV23175.1, ECO:0000313|Proteomes:UP000076098}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH-PL17 {ECO:0000313|EMBL:AMV23175.1,
RC ECO:0000313|Proteomes:UP000076098};
RA van der Voort M., Raaijmakers J.M.;
RT "Genome minning of novel planctomycete species.";
RL Submitted (APR-2015) 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};
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DR EMBL; CP011271; AMV23175.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A142X875; -.
DR STRING; 1630693.VT84_02105; -.
DR KEGG; ges:VT84_02105; -.
DR PATRIC; fig|1630693.3.peg.448; -.
DR Proteomes; UP000076098; Chromosome.
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 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; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:AMV23175.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000076098}.
FT DOMAIN 19..757
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 809..963
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 1190 AA; 133266 MW; F044E42949D482D0 CRC64;
MPFEKVESAV DFPSLERMIL QFWDDNKIFD KRKALNAGKP KWSFLDGPIT ANNPMGVHHA
WGRTYKDLYN RYFAMAGHEL RYQNGFDCQG LWVEVEVEKS LGLKSKRDIE NLVPGNPEAS
IDKFVQACKD RVNEFARVQT NQSIRLGYWM DWDRTDADWA KTPDERKSYF TMSEENNYTI
WSFLKKCFCK GLIGRGYDVM PWCGRCGVGI SEQEMKEGYK LVEHRACFVK FPLKGREKEN
LLVWTTTPWT LTSNVGAAIN PELTYLKIKL KGEIYYVAKG AFKLNRMEGS GGEGGDDEEE
GGSKKTRPWL KEVPNLVTIE QHFKVKAGKG DSYEIVGEVK GNDLLGWEYV GPFDDLPAQN
HEYGYPEEVA KITKQSGKWP QVTAAHAHRV VSGGKDVTET EGTGIVHTAP GCGAIDYQWG
KENGLPPVAP IGDDGVFVPG FGALTGKNAV DPTTADAVFE QLKANDRLFA TERYVHRYPH
CWRCKTELLY RLVDEWFINM GPKGERVNDE WTYPRDDKGS FRGDIADVVR QVKFLPESIG
GQKRELDWLG NMGDWMISKK RYWGLALPIW VDENDPTQFE VIGSYQELKE RAVEGWAEFE
GHTPHRPWID RVKIRNAKTG NLMSRVPDVG NPWLDAGIVG FSTLKYNTDR AYWDKWYPAD
FITESFPGQF RNWFYALLAL STMMSDGKPP FKTLLGHGNV RDQYGHEMHK TAGNSIEFIA
AADRGGALKD PKGNALPFQA IGADVMRWLY ARQSPAANLN FGPEPAAEVR SRVFFKLWNT
YSMFCNYAIG DGFDPAAPHV PVAERQDIDR WLLSNLQLLV KDARAAYSAY DVMTFALKAE
EFIEGDLSNW YVRRNKDRLH SKNADLDAAG LKDKSAAYQT LYTTLTTLCK LMAPCVPFIT
EVMWKNLRLP TDPESVHLSD FPVAEDALGD AALSEDMRAV QRVISLGLAA RQQAKLNVRQ
PLAELVVSPS PVKDKTGALL GDADKRAVER FRDLILDELN VKSVRLHDPA VGALLTASVQ
LNKKVAGSKF GSKLKEAEET LAKQDQTEFA SRLDRGPVEL VGVSLDKTDF NIAFAASAGW
AGVADRGTQV AISTTITEAL KLEGLARDVV RQVQSARKDA KLDLLDKIAL HLSADAPDLA
KALTEHRQTI TTAVQATQWS DVPLSGADVH TATVKIDGQP LVIALRVVRA
//
