ID I3TH31_TISMK Unreviewed; 387 AA.
AC I3TH31;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Isoleucyl-tRNA synthetase {ECO:0000313|EMBL:AFK52069.1};
GN Name=ileS {ECO:0000313|EMBL:AFK52069.1};
GN OrderedLocusNames=TMO_0230 {ECO:0000313|EMBL:AFK52069.1};
OS Tistrella mobilis (strain KA081020-065).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Geminicoccales;
OC Geminicoccaceae; Tistrella.
OX NCBI_TaxID=1110502 {ECO:0000313|EMBL:AFK52069.1, ECO:0000313|Proteomes:UP000005258};
RN [1] {ECO:0000313|EMBL:AFK52069.1, ECO:0000313|Proteomes:UP000005258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KA081020-065 {ECO:0000313|EMBL:AFK52069.1,
RC ECO:0000313|Proteomes:UP000005258};
RX PubMed=22458477; DOI=10.1021/ja301735a;
RA Xu Y., Kersten R.D., Nam S.J., Lu L., Al-Suwailem A.M., Zheng H.,
RA Fenical W., Dorrestein P.C., Moore B.S., Qian P.Y.;
RT "Bacterial biosynthesis and maturation of the didemnin anti-cancer
RT agents.";
RL J. Am. Chem. Soc. 134:8625-8632(2012).
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; CP003236; AFK52069.1; -; Genomic_DNA.
DR RefSeq; WP_014743749.1; NC_017956.1.
DR AlphaFoldDB; I3TH31; -.
DR STRING; 1110502.TMO_0230; -.
DR KEGG; tmo:TMO_0230; -.
DR PATRIC; fig|1110502.3.peg.237; -.
DR eggNOG; COG0060; Bacteria.
DR HOGENOM; CLU_713589_0_0_5; -.
DR Proteomes; UP000005258; Chromosome.
DR GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro.
DR Gene3D; 1.10.730.20; -; 1.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR Pfam; PF08264; Anticodon_1; 1.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
PE 4: Predicted;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000313|EMBL:AFK52069.1}; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000005258}.
FT DOMAIN 192..330
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 387 AA; 40440 MW; 0381DDDE2FD5E5A7 CRC64;
MTELLLQATA APFSADLTAG DPTFSPEADP AREARLVDAW AEMRLDRRAR SACAGRPRAA
LPEMSALLPA GAGVVEAALC RDMLARARRM AGFDTPPPGG AAHAAGRRLG LLADADAAAG
DAGADWRRWA ARADQDGADL LRARFAAGDT VDASGAIRGI RAALGRLLDH LAVAPAGLLP
PADRLDMPEI LLLARLVEID AELRDDLEAA DLPAMLARLA RFCADELTAG WAGLRAGLLA
GDADAPGRRA VAAVAARSFN HLVAWIAPLL PFLAEEAWLA RWGAGAGSVH ERLWPSVDPL
WATPGTILAN RRLDRLRALV RDVAGGREIT ADATVELDLP ADRRPPFREA ELGALLGVGR
LRLRSLPAGA APAARFAAAG PVLAATA
//
