SYI_UREPA
ID SYI_UREPA Reviewed; 900 AA.
AC Q9PQ79;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Isoleucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02002};
DE EC=6.1.1.5 {ECO:0000255|HAMAP-Rule:MF_02002};
DE AltName: Full=Isoleucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02002};
DE Short=IleRS {ECO:0000255|HAMAP-Rule:MF_02002};
GN Name=ileS {ECO:0000255|HAMAP-Rule:MF_02002}; OrderedLocusNames=UU410;
OS Ureaplasma parvum serovar 3 (strain ATCC 700970).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX NCBI_TaxID=273119;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700970;
RX PubMed=11048724; DOI=10.1038/35037619;
RA Glass J.I., Lefkowitz E.J., Glass J.S., Heiner C.R., Chen E.Y.,
RA Cassell G.H.;
RT "The complete sequence of the mucosal pathogen Ureaplasma urealyticum.";
RL Nature 407:757-762(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_02002}.
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_02002};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02002}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02002}.
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_02002}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC IleS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_02002}.
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DR EMBL; AF222894; AAF30821.1; -; Genomic_DNA.
DR RefSeq; WP_006688542.1; NC_002162.1.
DR AlphaFoldDB; Q9PQ79; -.
DR SMR; Q9PQ79; -.
DR STRING; 273119.UU410; -.
DR PRIDE; Q9PQ79; -.
DR EnsemblBacteria; AAF30821; AAF30821; UU410.
DR GeneID; 29672433; -.
DR KEGG; uur:UU410; -.
DR eggNOG; COG0060; Bacteria.
DR HOGENOM; CLU_001493_7_1_14; -.
DR OMA; HLGTAWN; -.
DR Proteomes; UP000000423; 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:0006428; P:isoleucyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd07960; Anticodon_Ia_Ile_BEm; 1.
DR Gene3D; 3.40.50.620; -; 2.
DR HAMAP; MF_02002; Ile_tRNA_synth_type1; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR033708; Anticodon_Ile_BEm.
DR InterPro; IPR002301; Ile-tRNA-ligase.
DR InterPro; IPR023585; Ile-tRNA-ligase_type1.
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 InterPro; IPR010663; Znf_FPG/IleRS.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR Pfam; PF06827; zf-FPG_IleRS; 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;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..900
FT /note="Isoleucine--tRNA ligase"
FT /id="PRO_0000098496"
FT MOTIF 58..68
FT /note="'HIGH' region"
FT MOTIF 593..597
FT /note="'KMSKS' region"
FT BINDING 552
FT /ligand="L-isoleucyl-5'-AMP"
FT /ligand_id="ChEBI:CHEBI:178002"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT BINDING 596
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
SQ SEQUENCE 900 AA; 105806 MW; FA478902AE347D87 CRC64;
MKDYKSTLNM PTTGFEMRAN LNVKEPKIQQ FWVEHQIYEK LLTKNKDKKP FILHDGPPYA
NGNIHIGHAL NKILKDFVVS YHNMNNYYSP YIPGWDTHGL PIEVALSKKI KLSNLSVNER
REQCKKYALE QVNNQIQQFL RLGMISDFKQ RYLTLDHNYE IDQLKLFTYM LKKGFIYQDF
KPVFWSWSSQ TALAESEIEY ADRQSSAIYV KMKVVDHNDL FTDKPTSLVI WTTTPWTLPA
NLAIAIHPEL VYSLIEYKNE NYIIAKPLVE TFVKKVGFED YKWIKDFKAN TLEKIKYISP
ISKKHAFVIM DEYVSANDGT GLVHNAPAFG LEDYYACKKY GIETVVMIDQ FGKYNALVND
LELENMFYED ANQVILNRLM NEHLLIHHEV ITHSVAHDWR TKKPVMYRAT KQWFVSIEKI
LPNILQTLNN DVKSTSFRGI ERMHEMIVNR KEWCISRQRV WGVPIPMIFD ENHNAIMDHE
LVENIINVLN EKGVNAWFDL DVNAFLTPKY LSMKNKTFYK EKDIMDVWFD SGSSYNILGH
YNLNYPADVY LEGYDQYRGW FNSSLITGTI LNNRAPYKYL VAHGMVLDGE GYKMSKSKGN
VVDPLDVCKI YGADVLRLWI ANSDYQNDTR ISEEILKQNA EIYRRIRNTL FKYSLSILND
FEPSVDFSFN VRQEEQFVLN EFNELHIKVI KAYENFDYQT VVKLFNKFIL DLSSWYFENI
KDDMYCLAIN DPIRKQIQSA VYWILKNSLI DLTPIIPHTT EEAYSFLKDA NKKESIRLED
FYDQSQFQFK KGIAHVKAFF SIKDQIFNEL ENARKNNILK KNNEAFVTIA KNLILDDYLI
NNPKLLAKWF GVAKIEFANN TNVANANFKK CLRCWNHFPD EEMYNDELSM NCYKVINKIK
