(data stored in SCRATCH zone)

SWISSPROT: A0LEH3_SYNFM

ID   A0LEH3_SYNFM            Unreviewed;       928 AA.
AC   A0LEH3;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 102.
DE   RecName: Full=Isoleucine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02002};
DE            EC=6.1.1.5 {ECO:0000256|HAMAP-Rule:MF_02002};
DE   AltName: Full=Isoleucyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02002};
DE            Short=IleRS {ECO:0000256|HAMAP-Rule:MF_02002};
GN   Name=ileS {ECO:0000256|HAMAP-Rule:MF_02002};
GN   OrderedLocusNames=Sfum_0122 {ECO:0000313|EMBL:ABK15825.1};
OS   Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC   Syntrophobacteraceae; Syntrophobacter.
OX   NCBI_TaxID=335543 {ECO:0000313|EMBL:ABK15825.1, ECO:0000313|Proteomes:UP000001784};
RN   [1] {ECO:0000313|EMBL:ABK15825.1, ECO:0000313|Proteomes:UP000001784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10017 / MPOB {ECO:0000313|Proteomes:UP000001784};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA   McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J.,
RA   Sieber J., Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT   "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the attachment of isoleucine to tRNA(Ile). As
CC       IleRS can inadvertently accommodate and process structurally
CC       similar amino acids such as valine, to avoid such errors it has
CC       two additional distinct tRNA(Ile)-dependent editing activities.
CC       One activity is designated as 'pretransfer' editing and involves
CC       the hydrolysis of activated Val-AMP. The other activity is
CC       designated 'posttransfer' editing and involves deacylation of
CC       mischarged Val-tRNA(Ile). {ECO:0000256|HAMAP-Rule:MF_02002,
CC       ECO:0000256|SAAS:SAAS00803722}.
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:0000256|HAMAP-
CC         Rule:MF_02002, ECO:0000256|SAAS:SAAS01125826};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_02002};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_02002};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_02002,
CC       ECO:0000256|SAAS:SAAS00803727}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02002,
CC       ECO:0000256|SAAS:SAAS00803728}.
CC   -!- DOMAIN: IleRS has two distinct active sites: one for
CC       aminoacylation and one for editing. The misactivated valine is
CC       translocated from the active site to the editing site, which
CC       sterically excludes the correctly activated isoleucine. The single
CC       editing site contains two valyl binding pockets, one specific for
CC       each substrate (Val-AMP or Val-tRNA(Ile)). {ECO:0000256|HAMAP-
CC       Rule:MF_02002}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. IleS type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_02002,
CC       ECO:0000256|SAAS:SAAS00803716}.
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DR   EMBL; CP000478; ABK15825.1; -; Genomic_DNA.
DR   RefSeq; WP_011696998.1; NC_008554.1.
DR   STRING; 335543.Sfum_0122; -.
DR   EnsemblBacteria; ABK15825; ABK15825; Sfum_0122.
DR   KEGG; sfu:Sfum_0122; -.
DR   eggNOG; ENOG4105C07; Bacteria.
DR   eggNOG; COG0060; LUCA.
DR   HOGENOM; HOG000246402; -.
DR   KO; K01870; -.
DR   OMA; HLGTAWN; -.
DR   OrthoDB; 32262at2; -.
DR   BioCyc; SFUM335543:G1G7I-128-MONOMER; -.
DR   Proteomes; UP000001784; 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; A0LEH3.
DR   SWISS-2DPAGE; A0LEH3.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02002,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00470441,
KW   ECO:0000313|EMBL:ABK15825.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_02002,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00470429};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001784};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02002,
KW   ECO:0000256|SAAS:SAAS00803729};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_02002,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00106025,
KW   ECO:0000313|EMBL:ABK15825.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_02002,
KW   ECO:0000256|SAAS:SAAS00803710};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02002,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00470402};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_02002,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00470368};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001784};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_02002, ECO:0000256|SAAS:SAAS00803712}.
FT   DOMAIN       27    641       tRNA-synt_1. {ECO:0000259|Pfam:PF00133}.
FT   DOMAIN      685    839       Anticodon_1. {ECO:0000259|Pfam:PF08264}.
FT   DOMAIN      895    923       zf-FPG_IleRS. {ECO:0000259|Pfam:PF06827}.
FT   MOTIF        57     67       "HIGH" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_02002}.
FT   MOTIF       602    606       "KMSKS" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_02002}.
FT   METAL       898    898       Zinc. {ECO:0000256|HAMAP-Rule:MF_02002}.
FT   METAL       901    901       Zinc. {ECO:0000256|HAMAP-Rule:MF_02002}.
FT   METAL       918    918       Zinc. {ECO:0000256|HAMAP-Rule:MF_02002}.
FT   METAL       921    921       Zinc. {ECO:0000256|HAMAP-Rule:MF_02002}.
FT   BINDING     561    561       Aminoacyl-adenylate. {ECO:0000256|HAMAP-
FT                                Rule:MF_02002}.
FT   BINDING     605    605       ATP. {ECO:0000256|HAMAP-Rule:MF_02002}.
SQ   SEQUENCE   928 AA;  105366 MW;  9F3BB187ACA16C95 CRC64;
     MDYKATLNLP QTDFPMKANL SRREPEILEK WEAMGLYDML RERSRGRPPY ILHDGPPYAN
     GHIHLGTALN KILKDMIVKS QQMSGKNAVY VPGWDCHGLP IEHQVDKELG KRKQTMSQVE
     IRRHCRKYAE KFIDIQRNEF RRLGVLGEWN NPYLTMSYDY EASIARELGR FFQEGGVIRS
     KKPIYWCTSC KTALAEAEVE YHDHTSPSIY VKFPMSAGGR AKFPELAGKD VAVLIWTTTP
     WTLPANLAIA VHPDFTYVAA DVGREVWILA RGLLESCMES FGIKDYRVLR TFEAGELRGL
     ACSHPFVDRE SVIVTGTHVT LEAGTGCVHT APGHGREDYD MALEYGLDVY SPVDDNGCFT
     DDVPLFAGRF VFDANRAINA KLEETGKLIL EKSITHSYPH CWRCKNPVIF RATEQWFISM
     EKNDLRGRAL QWIDRVDWIP GWGRDRIHNM IANRPDWCIS RQRSWGVPIC VFTCRKCGTV
     LASKELFEKT AALFERNGAD CWFEMTSEEL LPPGATCAGC GGQDFEKEED ILDVWFDSGV
     SHAAVLEARP DLRSPADLYL EGSDQHRGWF HSSLLTAVGT RNAAPYKSVL THGFVVDGQG
     YKMSKSLGNV IAPEEIIRQY GAEVLRLWVS AEDYRDDVRI SPDILKRLSE AYRRIRNTCR
     FLLGNLNDFD PEKDSVPYDR MDELDRFALH QLQEFVRRVR QAYERFEFHR VYHAFHNYCV
     VDLSAFYLDI LKDRLYTSGA AGPARRSAQT AVYRILSALL RLMAPILSFT AEEAWWHLPH
     QSSETVHLEE FPAPDATWAD EALNQRWQKI LTLRSDVTKA LEGARQAKAI GHPLDAKVKL
     ALPPDWIADF AGQEEMLRTV FIVSEVVLAS GEELAGAVEG TEVPGLLIRV EPASGEKCER
     CWMRSETVGQ FSDHPALCGR CRNVVAAH
//

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