SYI_PYRFU
ID SYI_PYRFU Reviewed; 1066 AA.
AC P46214;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 2.
DT 03-AUG-2022, entry version 135.
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=PF1096;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 87-632.
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; AE009950; AAL81220.1; -; Genomic_DNA.
DR EMBL; L37105; AAC41446.1; -; Genomic_DNA.
DR RefSeq; WP_011012235.1; NZ_CP023154.1.
DR AlphaFoldDB; P46214; -.
DR SMR; P46214; -.
DR STRING; 186497.PF1096; -.
DR EnsemblBacteria; AAL81220; AAL81220; PF1096.
DR GeneID; 41712904; -.
DR KEGG; pfu:PF1096; -.
DR PATRIC; fig|186497.12.peg.1156; -.
DR eggNOG; arCOG00807; Archaea.
DR HOGENOM; CLU_001493_1_1_2; -.
DR OMA; HLGTAWN; -.
DR OrthoDB; 4914at2157; -.
DR PhylomeDB; P46214; -.
DR Proteomes; UP000001013; 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; Reference proteome; Zinc.
FT CHAIN 1..1066
FT /note="Isoleucine--tRNA ligase"
FT /id="PRO_0000098589"
FT MOTIF 49..59
FT /note="'HIGH' region"
FT MOTIF 625..629
FT /note="'KMSKS' region"
FT BINDING 628
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
FT CONFLICT 88
FT /note="M -> T (in Ref. 2; AAC41446)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="I -> V (in Ref. 2; AAC41446)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="R -> W (in Ref. 2; AAC41446)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="H -> L (in Ref. 2; AAC41446)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="R -> G (in Ref. 2; AAC41446)"
FT /evidence="ECO:0000305"
FT CONFLICT 494
FT /note="A -> T (in Ref. 2; AAC41446)"
FT /evidence="ECO:0000305"
FT CONFLICT 501
FT /note="G -> S (in Ref. 2; AAC41446)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1066 AA; 125752 MW; 4704936EBC5D2272 CRC64;
MIKEPEFRDY TPGKLEEKIE QFWKESNIYQ KVKELRKNGP KYYFLDGPPY VSGAIHLGTA
WNKIIKDMII RFRTMQGYNV WRQPGYDMHG LPIEVKVEQA LGLKTKKEIE EKIGVENFIQ
KCKEFALNNL RIMTEQFKML GVWMDWDNPY MTIKNEYIES AWFTLKRAWE KGLLEKDKRV
LHWCPRCETA LAEHEVRGEY KLRKDPSIYV KFPVEGKENE YLLIWTTTPW TLPANLAVSA
HPDYDYVKVR VDLNGREEYW ILAKALVEKV LGDIGVKGEV VEEFKGKELE GLRYVHILMD
EYPRQKEFRE KYEWVHRVIL ADFVTLEEGT GLVHTAPGHG EEDFEVGQKY GLPVYSPVDD
QGKYVEGKWK GVYVKEADPQ IIEHLKEKGY LVKAGEIEHK YPHCWRCKTP LIFRATDQWF
LKVSKVKEKI IKENDEKVTW YPEWVKIRFD NGVRDSGDWV ISRQRYWGIP LPIWQSEDGE
IYVVGSWKEL VELAVAIEVN GERIDLPESY EEKLKVIEEK LGPEDLHRPY VDAFIIKVNG
KEMRRVKDVV DVWFDSGIAS WASLGYPRNK ELFEKLWPAD FIVEGEDQVT KWFYSQQAAS
VIAFDTVPYR AVAMHGYVLD EKGDKMSKSL GNIIRPEEVV EKAGRDTFRF YMLWATNPWE
NLKFSWKGVE QVRRMLNILW NVYVLSATYM SLDNFDPRNV KVEELEFREE DKWILSRVNN
LIKEVENGIE TFYLTKATRA LYNFVVEDLS RWYVRLIRKR LWVEGDDPDK LAAYYTLWKV
FDVLLRLMAP FTPYITEEIY QNIMRPFTGI ESVHMLDWPK PDESAVDEEL EREMEFIRRI
VEAGSAARQK AKIKLRYPVR KIIIETQDDT VKKAVERLNY ILRDQLNAKE VVVGNVEREI
TVKPNFAKVG PEFKGDARLV AKWISEHGLE LYEKGEVDVE IEGKKFHLTR EHIIVEENIP
DFLVAEDFEG GRVYVDKTLT RELLAEGLAR EFVRRIQEMR KRLDLDVNDR IVVTIETTEE
NRELLQENLE YIMRETRAIE VRFEEAKGYV VEWPEVQAKI GIEKIE
