ID A0A1G2TI08_9BACT Unreviewed; 1068 AA.
AC A0A1G2TI08;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Isoleucine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02003};
DE EC=6.1.1.5 {ECO:0000256|HAMAP-Rule:MF_02003};
DE AltName: Full=Isoleucyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02003};
DE Short=IleRS {ECO:0000256|HAMAP-Rule:MF_02003};
GN Name=ileS {ECO:0000256|HAMAP-Rule:MF_02003};
GN ORFNames=A3D49_00140 {ECO:0000313|EMBL:OHA96299.1};
OS Candidatus Zambryskibacteria bacterium RIFCSPHIGHO2_02_FULL_43_37.
OC Bacteria; Candidatus Zambryskibacteria.
OX NCBI_TaxID=1802749 {ECO:0000313|EMBL:OHA96299.1, ECO:0000313|Proteomes:UP000177279};
RN [1] {ECO:0000313|EMBL:OHA96299.1, ECO:0000313|Proteomes:UP000177279}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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, ECO:0000256|HAMAP-Rule:MF_02003}.
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, ECO:0000256|HAMAP-
CC Rule:MF_02003};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02003};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_02003}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02003}.
CC -!- DOMAIN: IleRS has two distinct active sites: one for aminoacylation and
CC one for editing. The misactivated valine is translocated from the
CC active site to the editing site, which sterically excludes the
CC correctly activated isoleucine. The single editing site contains two
CC valyl binding pockets, one specific for each substrate (Val-AMP or Val-
CC tRNA(Ile)). {ECO:0000256|HAMAP-Rule:MF_02003}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC IleS type 2 subfamily. {ECO:0000256|ARBA:ARBA00007078,
CC ECO:0000256|HAMAP-Rule:MF_02003}.
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:OHA96299.1}.
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; MHVS01000005; OHA96299.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2TI08; -.
DR Proteomes; UP000177279; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004822; F:isoleucine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd07067; HP_PGM_like; 1.
DR CDD; cd00818; IleRS_core; 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 HAMAP; MF_02003; Ile_tRNA_synth_type2; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
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.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_02003};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_02003};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_02003};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02003};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_02003};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_02003};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_02003}; Zinc {ECO:0000256|HAMAP-Rule:MF_02003}.
FT DOMAIN 14..486
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 650..783
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 827..965
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 44..54
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT MOTIF 745..749
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT BINDING 748
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
SQ SEQUENCE 1068 AA; 123142 MW; D44646614CF4ADF5 CRC64;
MTGKSDRAKK EEEILKFWQD NKIFEKSLEK DAPKGEFVFY DGPPFATGLP HYGHILPGTI
KDVIPRYKTM RGFRVPRRWG WDCHGLPIEN LVEKELGLET KKDIEKFGIA EFNERAKASV
LRYESEWKEI IPRTGRWIDM DNPYKSMDAS YTQSVWWSFK NLFDKGLIYQ GFKSMHLCPR
CETTLSNFEV NQGYKDITDI SVTVEFPLID EPNKFILAWT TTPWTLPGNA ALAINPELQY
VETEGEVPGH IYIVAKSRVE KVFGGKYKIL REFSGKELIG KKYKTLFDYY QTEGLVYGAE
FVQAEEGTGI VHIAPAFGEE DYELSLKEKI PFIQHIGTDG RFKPEVRDFA GEPVKPKDDH
QRTDILIIKH LAAKGLLFSK EKIIHSYPHC WRCDTPLLNY ASSSWFVKVA DIKDKLVANN
QKVKWVPEDI RDGRFGKWLE GARDWAISRS RFWGTTLPVW QTADEKKEIV IDSVETLKKH
AKKSGNRYFL MRHAEAIDNA KHVLDPKGDP NNHLTEKGRE EALASARELK GRKIDAIITS
PFLRTRETAE IVRKELGFPE GSVVVDDRLH EYNEPDVDFV RRRAGEFIFE TEKRYAGKNI
LILSHGNPLW VLEKIVSHQP SNDFSSKVIM NTAEVRELEF VPFPHNKNFE LDLHRPYIDE
IVLEKDGEEY RRVPEVFDTW YDSGSVPFAS RAAFDSRPAD FIAEGLDQTR GWFYTMAVLG
TALFNEIPYR QVVVNGLVLA EDGKKMSKRL KNYPELTDVL DKYGADALRY YLMSSQAVRA
EDIAFSEKSL DEVMKKNISR LENVVGFYEL YAKESAPLQD LPQHILDKWI DLKLNNLVRS
ITDGLERYEI DRASRPIADF IDDLSTWYLR RSRTRPEALP KLREILIEFS KLMAPFMPFM
AEDIYQRLKA DGGKESVHLE AWPIPPPAKG EKEGVLDNMS ETRRIVTLAL EARQKANIKV
RQPLARLEIR TDALSPEYLE IIKDELNVKK VEINNALESD VLLDTNLTPE LIEEGKVRDA
IRVVQDWRKE KGLKPGEKAT YPTDDESILK HKEEIEKATN VELSHLHN
//
