SYI_TREPS
ID SYI_TREPS Reviewed; 1091 AA.
AC B2S348;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=TPASS_0452;
OS Treponema pallidum subsp. pallidum (strain SS14).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=455434;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SS14;
RX PubMed=18482458; DOI=10.1186/1471-2180-8-76;
RA Matejkova P., Strouhal M., Smajs D., Norris S.J., Palzkill T.,
RA Petrosino J.F., Sodergren E., Norton J.E., Singh J., Richmond T.A.,
RA Molla M.N., Albert T.J., Weinstock G.M.;
RT "Complete genome sequence of Treponema pallidum ssp. pallidum strain SS14
RT determined with oligonucleotide arrays.";
RL BMC Microbiol. 8:76-76(2008).
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; CP000805; ACD70877.1; -; Genomic_DNA.
DR RefSeq; WP_010881901.1; NC_021508.1.
DR AlphaFoldDB; B2S348; -.
DR SMR; B2S348; -.
DR EnsemblBacteria; ACD70877; ACD70877; TPASS_0452.
DR KEGG; tpp:TPASS_0452; -.
DR PATRIC; fig|455434.6.peg.453; -.
DR OMA; HLGTAWN; -.
DR Proteomes; UP000001202; 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; 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.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis; Zinc.
FT CHAIN 1..1091
FT /note="Isoleucine--tRNA ligase"
FT /id="PRO_1000216260"
FT MOTIF 48..58
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"
SQ SEQUENCE 1091 AA; 124242 MW; 30FCAE18C6F301A2 CRC64;
MYTPVDPKVD FVAQERRILA FWRERRVFEQ SVAQRAQGKS YVFFDGPPFA TGLPHFGHFV
PSTIKDIIPR YQTMRGAYVP RRFGWDCHGL PIEHLIEQEL NLNSKSDVES YGVSAFNAAC
RSSVLRYVKE WQRTLTRLGR WVDFDNDYKT MDVCYMESVW WVVAQLWQRK LLYEGYKILP
YCPRCATALS NHELNLGGYQ DVSDPAITVR FECTSVVPGS PAAREFCAAA SWGSASLPAH
TCFLAWTTTP WTLPCNAALA LGPQILYVLI EANDEHYILA RSRLEFYYPD SSAYRVVWEK
RGEHLAGIRY RPLFSYPVFG QGPDPSVQGD SEEGLFCTRV ADFVSTEDGT GVVHVAPAFG
EDDYEVFKDA GISIQCPLDA ECRFTAEVAD YQGLFVKAAD KAIIARVQKQ GALFRREQIS
HAYPHCWRCA SPLIYRAVHS WFVAVEKIKD KMLAANASIC WQPSHIRDGR FGKWLVCARD
WAISRDRYWG NPLPIWRCVH CGATDCIGSR TQLYERSGML LEDLHKHVVD MVTIPCACGS
VMRRVPEVLD CWFESGAMPY AQQHYPFEHA TDFERYFPAH FISEGLDQTR GWFYTLTILA
VALFERPAFE NCIVTGLVLA SDGKKMSKAL RNYADPNEVM DRYGADALRL FLVRSAVVRA
DDLKYSDEGV KDILKTVIIP LWNSYSFYVT YANIDGIDPP VCAKVDGMGQ AVTRLATHLN
NPLDRWILSL TEKLVQDIAC ALDAYDVSKV ADPIVSYVDQ LNNWYIRRSR RRFWKSINDE
DKRCAYNTLY CVLKRCVLAI APVVPFITES IWQNIRAADD VQSVHLADYP VCTPMVRDDA
LEFKMETVQR VVSMARAIRA QCNLKVRQPL KAMQVITRNP MERSALLEME EDVLDELNVK
ELVFHEKEDE IVEYRAKANF RVLGKELGSK TKRAALSIER LSSAEIQEIL EGTTLYLDVD
GDRLELTEEK ILVQRIERES LKAINEGTLT VALDTTLTED LLLEGAIRDL VRGVQNLRKE
RGFSLVDRIC LRVFSSDQDI VCARKAYDLH RSYIVGETLA AHVQWARVRD GASAVYVKSD
AVLWEVSIDK A
