SYI_THEVO
ID SYI_THEVO Reviewed; 1028 AA.
AC Q97AG7;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Isoleucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02003};
DE EC=6.1.1.5 {ECO:0000255|HAMAP-Rule:MF_02003};
DE AltName: Full=Isoleucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02003};
DE Short=IleRS {ECO:0000255|HAMAP-Rule:MF_02003};
GN Name=ileS {ECO:0000255|HAMAP-Rule:MF_02003}; OrderedLocusNames=TV0843;
GN ORFNames=TVG0867938;
OS Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS 15438 / GSS1).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT Thermoplasma volcanium.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000).
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:0000255|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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_02003};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02003};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02003}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_02003}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC IleS type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_02003}.
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DR EMBL; BA000011; BAB59985.1; -; Genomic_DNA.
DR RefSeq; WP_010917087.1; NC_002689.2.
DR AlphaFoldDB; Q97AG7; -.
DR SMR; Q97AG7; -.
DR STRING; 273116.14325060; -.
DR PRIDE; Q97AG7; -.
DR EnsemblBacteria; BAB59985; BAB59985; BAB59985.
DR GeneID; 1441935; -.
DR KEGG; tvo:TVG0867938; -.
DR eggNOG; arCOG00807; Archaea.
DR HOGENOM; CLU_001493_1_1_2; -.
DR OMA; HLGTAWN; -.
DR OrthoDB; 4914at2157; -.
DR PhylomeDB; Q97AG7; -.
DR Proteomes; UP000001017; 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 Gene3D; 3.40.50.620; -; 2.
DR Gene3D; 3.90.740.10; -; 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; 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 PANTHER; PTHR42780; PTHR42780; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR PRINTS; PR00984; TRNASYNTHILE.
DR SUPFAM; SSF47323; SSF47323; 2.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00392; ileS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis; Zinc.
FT CHAIN 1..1028
FT /note="Isoleucine--tRNA ligase"
FT /id="PRO_0000098596"
FT MOTIF 51..61
FT /note="'HIGH' region"
FT MOTIF 591..595
FT /note="'KMSKS' region"
FT BINDING 594
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ SEQUENCE 1028 AA; 119494 MW; ABBBCD972B46641F CRC64;
MQAQRYRLIE QGNTIMDIDN EILRYWNDHA INEKIFKKEG TKKFVFLEGP PTANGRPHIG
HAMTRTIKDI VLRYNTMTGH KIYRRYGGWD CHGLPVELEA EKYFGFKTKS DIINYGVEKF
NSYCRDSVFR YIDEWKTVDQ IIGFSIDHSG DYITLRNEYI ESEWYVLKYI YENGLLYKDY
TVVPYCPRCE TSLSSHEVAQ GYKDVKDPSV YVRFKEKGSE NTYFVAWTTT PWTLPSNEFL
VVNPDIEYSL IEYNNAKYYV ASSRAQYIFK DFKVLKKMKG FELAGKGYEQ LLPFLDPPAG
ALRVVTGDFV TDIDGSGIVH AAPAFGSDDY QIGKRENVPI LNPVDKNGRF SDERLPWYGK
KVREANEDII VYLKNNGLLI KSEKYEHSYP FCYRCDTPLL YYPLDAWFIR VSSVRDKLVE
NNEKIRWKPD YLKHGRFGNF LDEAKDWNLS RDRFWGTPLP VWRCRNNHVR FIGSRKEIEE
MGATVPQDLH RPYIDEVKFV CPDCGEEMRR EPYVIDTWFD SGSATYAAMH YPFEDNFDPS
SDLPVSFITE AIDQTRGWFY VLHVISTIMF NKNAYDSALS ISFILDEQGR KMSKSKGNSV
FALDYLKQVA PDSLRLFFLY GAPWKSKNLD RKIIDEVSRR VISTLLNVYS FFAYNANIDG
FEFKGILEAK DTLDKWLISK INTFIIESRR AYDDLDFHEV VRLSMDFVDN LSNFYLRLSR
RRFWAEDVTE DKLAAYSTLY TAIMTCSKVL APIVPFVSDY LYLSLHGPYE SIHLDSFPEP
DTSKIDHDLE KRMDQAYSVI ETVRRIRQEI NIKGRQPVKE ILLSGNIDPE IIPVVSQEVN
AKEIRIVSSE QRPLKYTVDL KMETAAPILR SSVNSVREAL KSIDGKAAFD AVQNGGKLRV
LDHELTGEML NISTIPDPDY GYSRDEKNGI DVFVNKRIDR NEYLEGLARE IVRRIQLMRK
EMNLDYTDRI NVWIDPVGDF SDAIDKFESY IKAETQCDSL NVGHTDDLRK WEIGDETIGI
RIEKVVPK
