ID E3BG90_9VIBR Unreviewed; 625 AA.
AC E3BG90;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 08-OCT-2025, entry version 60.
DE RecName: Full=isoleucine--tRNA ligase {ECO:0000256|ARBA:ARBA00013165};
DE EC=6.1.1.5 {ECO:0000256|ARBA:ARBA00013165};
DE Flags: Fragment;
GN Name=ileS {ECO:0000313|EMBL:EFP97903.1};
GN ORFNames=VIBC2010_02760 {ECO:0000313|EMBL:EFP97903.1};
OS Vibrio caribbeanicus ATCC BAA-2122.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Vibrionales;
OC Vibrionaceae; Vibrio.
OX NCBI_TaxID=796620 {ECO:0000313|EMBL:EFP97903.1, ECO:0000313|Proteomes:UP000002943};
RN [1] {ECO:0000313|EMBL:EFP97903.1, ECO:0000313|Proteomes:UP000002943}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-2122 {ECO:0000313|EMBL:EFP97903.1,
RC ECO:0000313|Proteomes:UP000002943};
RX PubMed=21930677; DOI=10.1099/ijs.0.032375-0;
RA Hoffmann M., Monday S.R., Allard M.W., Strain E.A., Whittaker P., Naum M.,
RA McCarthy P.J., Lopez J.V., Fischer M., Brown E.W.;
RT "Vibrio caribbeanicus sp. nov., isolated from the marine sponge
RT Scleritoderma cyanea.";
RL Int. J. Syst. Evol. Microbiol. 62:1736-1743(2012).
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=tRNA(Ile) + L-isoleucine + ATP = L-isoleucyl-tRNA(Ile) + AMP +
CC diphosphate; Xref=Rhea:RHEA:11060, Rhea:RHEA-COMP:9666, Rhea:RHEA-
CC COMP:9695, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58045,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78528, ChEBI:CHEBI:456215; EC=6.1.1.5;
CC Evidence={ECO:0000256|ARBA:ARBA00048359};
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC IleS type 1 subfamily. {ECO:0000256|ARBA:ARBA00006887}.
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:EFP97903.1}.
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DR EMBL; AEIU01000037; EFP97903.1; -; Genomic_DNA.
DR RefSeq; WP_009599968.1; NZ_AEIU01000037.1.
DR AlphaFoldDB; E3BG90; -.
DR STRING; 796620.VIBC2010_02760; -.
DR eggNOG; COG0060; Bacteria.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000002943; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0002161; F:aminoacyl-tRNA deacylase 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd07960; Anticodon_Ia_Ile_BEm; 1.
DR FunFam; 1.10.730.20:FF:000001; Isoleucine--tRNA ligase; 1.
DR FunFam; 3.40.50.620:FF:000048; Isoleucine--tRNA ligase; 1.
DR Gene3D; 1.10.730.20; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 1.10.10.830; Ile-tRNA synthetase CP2 domain-like; 1.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR033708; Anticodon_Ile_BEm.
DR InterPro; IPR002301; Ile-tRNA-ligase.
DR InterPro; IPR050081; Ile-tRNA_ligase.
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 InterPro; IPR010663; Znf_FPG/IleRS.
DR PANTHER; PTHR42765:SF1; ISOLEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR42765; SOLEUCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR Pfam; PF06827; zf-FPG_IleRS; 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 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000313|EMBL:EFP97903.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EFP97903.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000002943};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 92..328
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 373..529
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 585..614
FT /note="Zinc finger FPG/IleRS-type"
FT /evidence="ECO:0000259|Pfam:PF06827"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EFP97903.1"
SQ SEQUENCE 625 AA; 69967 MW; B022F5138EF1905C CRC64;
DFTVPAILGD HVTTESGTGV VHTAPGHGQE DFTVGNQYNL EVANPVGSNG VYLPDTELFA
GQHVFKANDA VVETLKEKGA LLHHHAYEHS YPHCWRHKTP IIFRATPQWF VSMDQAGLRA
KALEAIKGVE WMPEWGQSRI EGMIEGRPEW CISRQRTWGV PIALFVHKET AELHPNTLEL
IENVAKLVEQ KGIQAWWDLD TKELLGSDAE QYEKVLDTLD VWFDSGVTHF SVVDARKEYE
GNSADLYLEG SDQHRGWFQS SLISSIAMKD EAPYKQVLTH GFVVDGHGRK MSKSIGNVVA
PKDVTNKLGA DILRLWVAST DYTGEVAVSD EILKRSADAY RRIRNTARFF LANLNGFNPA
TDIVPVEEMV ALDRWAVGRA LSAQNEIVKA YGDYNTHAVT QRLMQFCSIE MGSFYLDVIK
DRQYTAKRGG HAQRSCQTAL YYIVEALVRW MAPIMSFTAD EIWNEMPGER DKFVFTGEWF
DGLFGLAEGE ELNNTFWTDI QSVRSAVNKL LEDARKDKTI GSALQAEVTL YAEDALVKKL
LKLEDELRFV LLTSAASVKA IGEKTETAQQ TDIEGLFVEV SPVGGEKCDR CWHHTSDVGT
IDGHEKICGR CVSNVEGEGE TRKFA
//
