ID G0GB96_SPITZ Unreviewed; 1048 AA.
AC G0GB96;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 71.
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 OrderedLocusNames=Spith_1644 {ECO:0000313|EMBL:AEJ61905.1};
OS Spirochaeta thermophila (strain ATCC 700085 / DSM 6578 / Z-1203).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC Spirochaeta.
OX NCBI_TaxID=869211 {ECO:0000313|EMBL:AEJ61905.1, ECO:0000313|Proteomes:UP000007254};
RN [1] {ECO:0000313|EMBL:AEJ61905.1, ECO:0000313|Proteomes:UP000007254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700085 / DSM 6578 / Z-1203
RC {ECO:0000313|Proteomes:UP000007254};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikailova N., Pagani I.,
RA Chertkov O., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S.,
RA Merkhoffer B., Schneider S., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Spirochaeta thermophila DSM 6578.";
RL Submitted (JUN-2011) 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; CP002903; AEJ61905.1; -; Genomic_DNA.
DR RefSeq; WP_014625234.1; NC_017583.1.
DR AlphaFoldDB; G0GB96; -.
DR STRING; 869211.Spith_1644; -.
DR KEGG; stq:Spith_1644; -.
DR HOGENOM; CLU_001493_1_1_12; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000007254; Chromosome.
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:UP000007254};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_02003}.
FT DOMAIN 18..637
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 685..833
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 48..58
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT MOTIF 599..603
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
FT BINDING 602
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02003"
SQ SEQUENCE 1048 AA; 121819 MW; F6432990B8DBF654 CRC64;
MYKPVDPKVS FPKMEEDILA FWQEHGIFEK SIARRAGAEE YVFYDGPPFA TGLPHFGHFV
PGTVKDIFPR YKTMRGYKVE RRFGWDCHGL PVEYEMEKEL GISGKRQIEE YGVARFNEAC
RSIVLRYVKE WRQIVTRMGR WVDFDNDYKT MDPDYMETIW WVMKQLWEKG LLYEGYYILP
YCPRCSTVLS NHELNLGGYQ DVHDPAITVR FRVKDDNPKG WKDTYILAWT TTPWTLPSNL
ALALGPDIEY VRVKDGEEYY VLAKERLSTY YRSEDEYEIV ETFTGKDAVG IPYEPLFPYF
ADLADQGAFR TWTGEFVTTE EGTGIVHIAP GFGEDDYHLL KDSGLPVVCP VDAEGRFTGE
VGDYEGLFVK DADKEIIRRL KEEGKLVKRE QYLHAYPHCW RCKSPLIYRA ISSWFVAVEK
IKERMIANNE KIYWMPSHIK HGRFGKWLEN ARDWAISRNR YWGNPLPIWR CEACGHTECI
GSRQELKEKS GVWPEDLHKH FVDKITYPCP SCGGTMRRIP EVLDCWFESG AMPYAQNHYP
FENKEKFERH FPADFVCEGI DQTRGWFYTL LVLSTALFDE PPFLNNITTG LVLAADGKKM
SKSERNYTDP KDVIETFGAD ALRLFLMHSA VVRAEELRYS DEGVREVLKN VLIPLWNAYA
FFVTYANIDG IRPTAPPEDP AHPLDRWILS EAQRLVLTVT EEMDRYDLVR AIDPIVAFID
SLNNWYIRRS RRRFWKSESD ADKREAYATL WTVLMTLVKV AAPIVPFITE EIYRNLRTEE
MPESVHLCDW PEVDERRRDT VLEEKMRIVR RAVSLGRALR SEHNIKTRQP LRTIYLVTRD
EHERRVLMEM EDIVREELNV KQVVYRENED DVVEYRAKPN YPVLGKRLGP LMKKAARRIE
ALSMEEIKGL LDGATLVLDL DGERLELTSE GIVVQRIEKA GLKVLNEGSL TVALDTELSA
ELVREGLVRD FVRVVQNFRK EKGLEVTDRI RLHYQVPDDL AEAIEAFKEY VMNETLAVAL
VPRDDGQGLE RVACGDAECG LVVERVEE
//
