SYI_RICTY
ID SYI_RICTY Reviewed; 1086 AA.
AC Q68WC2;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=RT0606;
OS Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=257363;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-144 / Wilmington;
RX PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA Yu X.-J., Walker D.H., Weinstock G.M.;
RT "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT of other Rickettsiae.";
RL J. Bacteriol. 186:5842-5855(2004).
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; AE017197; AAU04070.1; -; Genomic_DNA.
DR RefSeq; WP_011191050.1; NC_006142.1.
DR AlphaFoldDB; Q68WC2; -.
DR SMR; Q68WC2; -.
DR STRING; 257363.RT0606; -.
DR EnsemblBacteria; AAU04070; AAU04070; RT0606.
DR KEGG; rty:RT0606; -.
DR eggNOG; COG0060; Bacteria.
DR HOGENOM; CLU_001493_1_1_5; -.
DR OMA; KMMAPFT; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000000604; 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; 1.
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..1086
FT /note="Isoleucine--tRNA ligase"
FT /id="PRO_0000098561"
FT MOTIF 53..63
FT /note="'HIGH' region"
FT MOTIF 624..628
FT /note="'KMSKS' region"
FT BINDING 627
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02003"
SQ SEQUENCE 1086 AA; 125447 MW; 02F4A7D6A1934203 CRC64;
MTNTKYYPDV SANVDFAAIE REILKFWQNN NIFQKSIDHR DGESEFIFYD GPPFANGLPH
YGHLLTGFIK DVYARYQTVK GKKVERRFGW DCHGLPAEMQ SEKELGISGR LAITNFGIEK
FNNHCRASVM QYASEWKQYV TRQARWVAFD NAYKTMDKNF MESVLWAFKE LYNKGLLYES
MRVMPYSWAC ETPLSNFETR LDNSYRERTD KAITVSFMLN DITLFNSMIS QKLGMTGGDN
FKEYRILAWT TTPWTLPANL ALAVGSDIDY ALVNKNDVCY IIAASSVAKY AKELGLSGKE
NFEIIKGLKL QGLSYKPLFN YFENHPNSFK IFASNFVVEG EGTGIVHMAP GFGEDDQILC
ESKGIELVCP VDNSGKFTKE IPDLEGVQVF DANDKIIIKL KEQGNWIKTE QYIHNYPHCW
RTDTPLIYKA VPSWYVRVTQ FKDRMVELNQ QINWIPHNVK DNLFGKWLEN ARDWSISRNR
FWGTPLPVWK SDDPKYPRID VYGSIEEIEQ DFGVKINDLH RPFIDELTRT NPDDPTGKSI
MRRIDDVFDC WFESGSMPYG QAHYPFENKK WFVEHFPADF IVEYSSQTRG WFYTLIVLST
ALFDRPPFLN CICHGVILDA TGQKLSKRLN NYADPLELFD RYGSDALRVT MLSSNVVKGQ
ELLIDKDGKM IFDTLRLFIK PIWNAYHFFT IYANADALKG TLNFTSQNVL DIYILSKLKI
AVNKIEESLD NFDTQTAYHA VSEFFEVLNN WYIRRSRARF WKKEKDTDKQ NAYNTLYSCL
ETMTIAMSAL VPMISEAIYQ GLHNTAITQL NCLLLEGKHV VQNPMSGTQD YNTSVHLCNY
PTLSDFEINH ELVSTMDNVL DICSNSLFIR STKNIRVRQP LACITIISKH NNNLKDFEDL
IKDEINVKTV IYRDDLENYA HKKLSLNFAI LGKRLPHKMK AIIDASKKGE WETSTLGLVI
CGEILNSNEY KLVLEPHSHI KGTANFENNS SLLILDLELT SELIEEGYAR DIIRFIQHAR
KEADFSITDK ILIEIISEFD LSKIIENYGD FIKEQTLGEF AKNFMPDYVS KVALENNLIQ
LKVKRL
