SYI_SULAC
ID SYI_SULAC Reviewed; 1050 AA.
AC P46215; Q4JB38;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 133.
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=Saci_0599;
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 84-636.
RX PubMed=7708661; DOI=10.1073/pnas.92.7.2441;
RA Brown J.R., Doolittle W.F.;
RT "Root of the universal tree of life based on ancient aminoacyl-tRNA
RT synthetase gene duplications.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:2441-2445(1995).
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; CP000077; AAY79991.1; -; Genomic_DNA.
DR EMBL; L37106; AAC41447.1; -; Genomic_DNA.
DR RefSeq; WP_011277493.1; NC_007181.1.
DR AlphaFoldDB; P46215; -.
DR SMR; P46215; -.
DR STRING; 330779.Saci_0599; -.
DR EnsemblBacteria; AAY79991; AAY79991; Saci_0599.
DR GeneID; 3473519; -.
DR KEGG; sai:Saci_0599; -.
DR PATRIC; fig|330779.12.peg.578; -.
DR eggNOG; arCOG00807; Archaea.
DR HOGENOM; CLU_001493_1_1_2; -.
DR OMA; HLGTAWN; -.
DR Proteomes; UP000001018; 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 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; Reference proteome; Zinc.
FT CHAIN 1..1050
FT /note="Isoleucine--tRNA ligase"
FT /id="PRO_0000098592"
FT MOTIF 45..56
FT /note="'HIGH' region"
FT MOTIF 594..598
FT /note="'KMSKS' region"
FT BINDING 597
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
FT CONFLICT 164..167
FT /note="KAYE -> SIR (in Ref. 2; AAC41447)"
FT /evidence="ECO:0000305"
FT CONFLICT 483
FT /note="S -> G (in Ref. 2; AAC41447)"
FT /evidence="ECO:0000305"
FT CONFLICT 486
FT /note="S -> P (in Ref. 2; AAC41447)"
FT /evidence="ECO:0000305"
FT CONFLICT 504..512
FT /note="VRCEKCGGE -> LDVKNVEGQ (in Ref. 2; AAC41447)"
FT /evidence="ECO:0000305"
FT CONFLICT 614..636
FT /note="RDTLRLWLLRNTTWEDAKFSWKS -> QRYVKIMVTLEIPHGKMSKSHGN
FT (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1050 AA; 122024 MW; A25145ED9D005935 CRC64;
MTSKFDPLKF EEEVLKYWDD NNIYKKLKEI NEKNHKKFLF IDGPPYPSSP IPHIGTVWNK
TIKDCILRYE RLMGYSVKDQ PGYDTHGLPI EVETEKRLGI KSKAEIIEKV GVDNFISKCK
EFAVNNSKSL TQNFRNLGIF MDWENPYFTF NNDYISNSWA VIKKAYERGL LYKGVHVLHW
CSRCETTLAD YEVSEYRDLE DPSIYVKFRV KGEPNRYLVI WTTTPWTLPA NVFVMINKDF
EYADVRVGDE ILVIAKDRVK ELMKEARIKE YKILRVYKGE ELLGLEYEHP LADIVSAQSK
INNHHKVLDG GEAVTLQEGT GLVHSAPGHG DVDFEIGKKY DMPVVMLVND KGEFTQDSGK
YAGKYVRSAS EEIISDLKQR SALLHASKIV HRYPVCWRCK TPLILRAIEQ WFIAVSKLKD
HLMGEIDRVR WIPDWGKTRI GNMVKEVRDW VISRQRFWGT PLPIWVCSNC QNIIVVGGVD
ELSKISINQV PQDLHRPWID SVVVRCEKCG GEARRISDVA DVWFDSGVAF FASLGQDWRK
RWSELGPVDL VLEGHDQLRG WFFSLLRTGV ILMDKAPYEA VLVHGFMLDE QGREMHKSSG
NYVEPSQVVS KYGRDTLRLW LLRNTTWEDA KFSWKSLDMT RRDLNIIWNV YVFANTYMSL
DEFKYSKYSY NDIKDYLKLE DIWLLSRYYR MLKEVIEAMK EYKVHELANK VTAFIIDDIS
RFYLRVTRKR AWNEANDPDK IAMYYVLYHV LKGSLILLST VIPFTAEKIY LDFVQERLES
ISMEKIPEIK EEFINSEIEE AFEVAKEIID AGLNARAKAG IKLRWPLKEV YVFLVSDKDR
RSIEKITDVL SSLLNSKSII IEGIDGYKRF SKIRATPNTG SIGPTFKRLS VKVAEYIQNN
SDKVAQDIVS KGYHEFNVDS ENLRLDISHV NLVEEVEKGY VSARFSKGVV LLKQEMSKEE
EEEGIIRDLI RRIQFMRKQL SLNVNEYILL SIRAPDDKVD LIKKWEQYIK NETRAKELRI
GDVSGDLIQD WDVEEETYTI GVSKADVSVS
