ID A0A1H8EAY0_9FIRM Unreviewed; 1040 AA.
AC A0A1H8EAY0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=SAMN05216454_10159 {ECO:0000313|EMBL:SEN16711.1};
OS Peptostreptococcus russellii.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Peptostreptococcus.
OX NCBI_TaxID=215200 {ECO:0000313|EMBL:SEN16711.1, ECO:0000313|Proteomes:UP000199512};
RN [1] {ECO:0000313|EMBL:SEN16711.1, ECO:0000313|Proteomes:UP000199512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Calf135 {ECO:0000313|EMBL:SEN16711.1,
RC ECO:0000313|Proteomes:UP000199512};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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, 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|HAMAP-Rule:MF_02003}.
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DR EMBL; FODF01000001; SEN16711.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8EAY0; -.
DR STRING; 215200.SAMN05216454_10159; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000199512; 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:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd07961; Anticodon_Ia_Ile_ABEc; 1.
DR CDD; cd00818; IleRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR HAMAP; MF_02003; Ile_tRNA_synth_type2; 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 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}; Cytoplasm {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}; Reference proteome {ECO:0000313|Proteomes:UP000199512};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_02003}.
FT DOMAIN 22..629
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 684..830
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 52..62
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT MOTIF 597..601
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT BINDING 600
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
SQ SEQUENCE 1040 AA; 120729 MW; 1E43F5F6F53A2D1B CRC64;
MEKELVFETL YDGSVSEAEV ETLKRWQEDN ILEKVLEKGK NDPTYVFFEG PPTANGNPGI
HHVISRTLKD WVCRYKTMSG YRVPRKAGWD THGLPVELQV EKELGLSDKK AIEDYGIEEF
CERCRNSVFT YEKQWRQMTE RMAYAVDLDN PYITLDNNYI ETLWWILDKF NKEGLLYEGH
KILPYCPRCG TGLASHEVAQ GYKEVKTNTL VAKFKKKGTE NEYFLAWTTT PWTLPSNVAL
TVNPDIEYIK AEKDGEFYYL AKALADKHLG EGEYEVVETM KGKDLEYQEY EQLMPFVDVD
GKAFFITCGD YVTVTDGTGI VHSAPAFGED DYTMGRKYSL PFVQPVDSEG KFTATPWEGK
FVMEEGLDVE IIKWLAKENK LFSKEKIAHN YPHCWRCSTP LVYYANPGWY IEMTKLKDKL
IENNNGVNWF PEFVGQGRFG NWLEELKDWA ISRTRYWGTP LPVWKCECGN KTTVGSRQEL
ADLAIEDVDP ETIELHRPHI DRVHLKCSEC GKPMTRVTEV IDCWFDSGAM PFAQWHFPFE
HQDDFDTLFP ADYIAEGIDQ TRGWFYSLLA VSTFVTGKSP YKNVLVTDLV LDKDGKKMSK
SKGNTINPFE MFDKYGADAL RWYLLYVSPP WTPLRFDEDG LKEIMSKFVG TLKNTYNFFT
LYANTDKLNP RDFFVEYDQR PELDRWILSK FNNLKKEIEE NLEIFEVNKS IRRMTDFLND
DLSNWYIRRS RRRFWETELN EDKKSVYNTT YEILTEYCKL IAPFAPYLSE EMYRKLTGEY
SVHCADYPRC NEALIDEALE EKMDLTKNLV TLGRAARENS KIKVRQPISE VLIDGKYEEL
ISDLVELIKE ELNVKEVKFV KDLSEYMNFT LKPNFKVLGP VLGKNVNKFG KLLSTLDAHE
VVAKVEAGEK VKVDLDGNDF EFGYDDILIN IESKPGFNVA MENNLFVILE TVLTEELIQE
GLAREFVSKV QQMRKSSGFE VLDNINIYYS GDEEIDKAVA AFDEYIKNET LAVKVEKTEA
QDMEIQNLND HETKMKVERV
//
