(data stored in ACNUC7421 zone)

SWISSPROT: SYI_HISS2

ID   SYI_HISS2               Reviewed;         937 AA.
AC   B0UV12;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   11-DEC-2019, entry version 79.
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=HSM_0054;
OS   Histophilus somni (strain 2336) (Haemophilus somnus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Histophilus.
OX   NCBI_TaxID=228400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2336;
RG   US DOE Joint Genome Institute;
RA   Siddaramappa S., Duncan A.J., Challacombe J.F., Rainey D., Gillaspy A.F.,
RA   Carson M., Gipson J., Gipson M., Bruce D., Detter J.C., Han C.S., Land M.,
RA   Tapia R., Thompson L.S., Orvis J., Zaitshik J., Barnes G., Brettin T.S.,
RA   Dyer D.W., Inzana T.J.;
RT   "Complete sequence of Haemophilus somnus 2336.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02002};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-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}.
DR   EMBL; CP000947; ACA32189.1; -; Genomic_DNA.
DR   RefSeq; WP_012341373.1; NC_010519.1.
DR   PRIDE; B0UV12; -.
DR   EnsemblBacteria; ACA32189; ACA32189; HSM_0054.
DR   GeneID; 31486328; -.
DR   KEGG; hsm:HSM_0054; -.
DR   HOGENOM; HOG000246402; -.
DR   KO; K01870; -.
DR   OMA; PSWYIRT; -.
DR   OrthoDB; 32262at2; -.
DR   BioCyc; HSOM228400:G1GB8-54-MONOMER; -.
DR   Proteomes; UP000008543; 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; cd07960; Anticodon_Ia_Ile_BEm; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   Gene3D; 3.90.740.10; -; 1.
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;
DR   PRODOM; B0UV12.
DR   SWISS-2DPAGE; B0UV12.
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome; Zinc.
FT   CHAIN           1..937
FT                   /note="Isoleucine--tRNA ligase"
FT                   /id="PRO_1000088547"
FT   MOTIF           58..68
FT                   /note="'HIGH' region"
FT   MOTIF           602..606
FT                   /note="'KMSKS' region"
FT   METAL           900
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT   METAL           903
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT   METAL           920
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT   METAL           923
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT   BINDING         561
FT                   /note="Aminoacyl-adenylate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
FT   BINDING         605
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02002"
SQ   SEQUENCE   937 AA;  105956 MW;  260FD415D7822660 CRC64;
     MTDYKNTLNL PETGFPMRGD LAKREPDMLK NWYDKNLYQK VREASKGKKT FILHDGPPYA
     NGTLHLGHAV NKILKDIIMK SKTALGFDTP YVPGWDCHGL PIELKVEGLV GKPNEKISAA
     EFRQACRDYA KEQVEGQKAD FIRMGVLGDW DNPYLTMNFE TEAEIIRTLG KVIQNGHLYK
     GSKPVHWCLD CASSLAEAEV EYEDKVSPSI YVRFAAVSAA EVEEKFNALG KGQGALSAVI
     WTTTPWTLPS NRAIAVNAEL EYQLVQLGDE RVILAAELVQ AVQNALKIEQ LEILGSTTGQ
     DLELVRFHHP FYDFSVPIIL GDHVTVDGGT GLVHTAPDHG QDDFVVSKKY GLEMAGLVAN
     DGKFISSTPF FAGKGVFEAN DLVLEKLKET GALLKLERIK HSYPHCWRHK TPIIFRATPQ
     WFIGMETQDL RIKALSEIKS VRWIPSWGEA RIDKMVANRP DWCISRQRTW GVPMTMFVHN
     ETEELHPRTL ELLEDIAKRV EKAGIQAWWD LDPAELLGED AKTYHKVPDT LDVWFDSGST
     YASVVEQRPE FNGKSTDMYL EGSDQHRGWF MSSLMLSTAT NNKAPYKQVL THGFTVDEKG
     RKMSKSLGNV IVPSEVWNKN GADILRLWVA STDYTGEIAV SHKILNSAGD TYRRIRNTAR
     FLLANLNGFD PKNDLVNPEE MISLDRWAVS CALEAQNEIK EAYDNYQFHT VVQRLMRFCS
     IEMGSFYLDI IKDRQYTTKA DSLARRSCQT ALWHISEALV RWIAPILSFT ADEIWGYLPK
     LDNRAEFVFT EEFYDGLFGL DESDKLDDTY WQQLLKVRAE VNRVLEQARN DKLIGAGLEA
     KVTVYASEEI RPLLEQLGNE LRFVLITSQV VVKPLSKADV AESELTGLAI KVERADGEKC
     PRCWHFSTDI GSNKEHSHIC GRCIENVEGN GEQRQFA
//

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