ID B5Y8D5_COPPD Unreviewed; 906 AA.
AC B5Y8D5;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE RecName: Full=Isoleucine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02002};
DE EC=6.1.1.5 {ECO:0000256|HAMAP-Rule:MF_02002};
DE AltName: Full=Isoleucyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02002};
DE Short=IleRS {ECO:0000256|HAMAP-Rule:MF_02002};
GN Name=ileS {ECO:0000256|HAMAP-Rule:MF_02002,
GN ECO:0000313|EMBL:ACI17812.1};
GN OrderedLocusNames=COPRO5265_0684 {ECO:0000313|EMBL:ACI17812.1};
OS Coprothermobacter proteolyticus (strain ATCC 35245 / DSM 5265 / OCM 4 /
OS BT).
OC Bacteria; Coprothermobacterota; Coprothermobacteria; Coprothermobacterales;
OC Coprothermobacteraceae; Coprothermobacter.
OX NCBI_TaxID=309798 {ECO:0000313|EMBL:ACI17812.1, ECO:0000313|Proteomes:UP000001732};
RN [1] {ECO:0000313|Proteomes:UP000001732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35245 / DSM 5265 / OCM 4 / BT
RC {ECO:0000313|Proteomes:UP000001732};
RA Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT "The complete genome sequence of Coprothermobacter proteolyticus strain
RT ATCC 5245 / DSM 5265 / BT.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACI17812.1, ECO:0000313|Proteomes:UP000001732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35245 / DSM 5265 / OCM 4 / BT
RC {ECO:0000313|Proteomes:UP000001732};
RX PubMed=24831154;
RA Alexiev A., Coil D.A., Badger J.H., Enticknap J., Ward N., Robb F.T.,
RA Eisen J.A.;
RT "Complete Genome Sequence of Coprothermobacter proteolyticus DSM 5265.";
RL Genome Announc. 2:e00470-14(2014).
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_02002}.
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_02002};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02002};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_02002};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_02002}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02002}.
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_02002}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC IleS type 1 subfamily. {ECO:0000256|ARBA:ARBA00006887,
CC ECO:0000256|HAMAP-Rule:MF_02002}.
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DR EMBL; CP001145; ACI17812.1; -; Genomic_DNA.
DR RefSeq; WP_012544464.1; NC_011295.1.
DR AlphaFoldDB; B5Y8D5; -.
DR STRING; 309798.COPRO5265_0684; -.
DR KEGG; cpo:COPRO5265_0684; -.
DR eggNOG; COG0060; Bacteria.
DR HOGENOM; CLU_001493_7_0_9; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000001732; 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; cd07960; Anticodon_Ia_Ile_BEm; 1.
DR CDD; cd00818; IleRS_core; 1.
DR Gene3D; 1.10.730.20; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 1.10.10.830; Ile-tRNA synthetase CP2 domain-like; 1.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR HAMAP; MF_02002; Ile_tRNA_synth_type1; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR033708; Anticodon_Ile_BEm.
DR InterPro; IPR002301; Ile-tRNA-ligase.
DR InterPro; IPR023585; Ile-tRNA-ligase_type1.
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 NCBIfam; TIGR00392; ileS; 1.
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.
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_02002};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_02002};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_02002};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02002};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_02002};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_02002};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_02002}; Reference proteome {ECO:0000313|Proteomes:UP000001732};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_02002}.
FT DOMAIN 32..633
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 677..833
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 876..901
FT /note="Zinc finger FPG/IleRS-type"
FT /evidence="ECO:0000259|Pfam:PF06827"
FT MOTIF 62..72
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02002"
FT MOTIF 595..599
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02002"
FT BINDING 554
FT /ligand="L-isoleucyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:178002"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02002"
FT BINDING 598
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02002"
FT BINDING 877
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02002"
FT BINDING 880
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02002"
FT BINDING 897
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02002"
FT BINDING 900
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02002"
SQ SEQUENCE 906 AA; 103732 MW; AB7A32EEAFF54237 CRC64;
MAKENEKYNG TINLPKPLLP MKANLPQTEE TWLKFWEDDN VFEKALEKRK NSPLFILHDG
PPYANGDIHL GTALNKVLKD AVNKYKLLRG FKTPYVPGWD THGLPIEQQV TKQTKINPED
FAVTEWRDKC KDFALSYIDK QMKSFKRLGV LGLWKDYYAT FKPEYEGKEL EILADLVEKG
FVIRKRRPVY WCPHCKTTLA EAEIEYREKV SPSIFVAFPA KGGSYKTIAW TTTPWTLPDN
VALAFHPEES YVFVNTGEDT FVVAEKRLQD VAKELSWFDY EVVASKPGAA FEDERFEHPV
YDDKETVAIL ADFVSMEDGT GIVHIAPGHG EEDYLVWEEK GLDFPMMIDD SGRFTEQAGF
LAGVFYADAN DMVLDLLTRK GKLLHKGMVT HSYPHCWRCH NPVIFRALSQ WFIDVDLYRN
EALEALKEVQ WIPMGSDVRI GDMVKSRPDW CLSRQRIWGV PIPSIKCSHC GRSILDPRVV
RNVAAVVRKE GSNIWYSEPL EAFLPAKMEC PDCGSKDFEK EYDILDVWFD SGVSHYAVLE
QYDGMRWPAD LYLEGYDQHR GWFQTSLLTA VPLKGQAPYK TVLSHGFVLD ESGRAMSKSL
GNVIDPSDVV ANVGADVLRL ALLMSDYTAD IQVGQNIFNQ ASEIYKKIRN TFRFMEGNLF
DFQSSDEVPF AEMKPLDRWI LGRWTDMKRK LSSAFDNYEF YSFVSIFHSF CVKELSSTYL
DAIKSRLYLK KPDSEERRSA QTALKIMATE FPVLIAPILT FTAEEMWQAL LSRGLVTEKS
VYFSDWPDSA FSLTEEESSF WENALRLREK ANEQMEKLRK EKSIGHSLDA SVVVYGSGTE
FLSHSEWAEF LVVSSAQIKN EGKEWDIEVE KALGVKCARC WRVREDVGLD AEYPDICGEC
LDDITG
//
