(data stored in ACNUC7421 zone)

SWISSPROT: D4ZH24_SHEVD

ID   D4ZH24_SHEVD            Unreviewed;       940 AA.
AC   D4ZH24;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   08-MAY-2019, entry version 70.
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   ECO:0000313|EMBL:BAJ00973.1};
GN   OrderedLocusNames=SVI_1002 {ECO:0000313|EMBL:BAJ00973.1};
OS   Shewanella violacea (strain JCM 10179 / CIP 106290 / LMG 19151 /
OS   DSS12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=637905 {ECO:0000313|EMBL:BAJ00973.1, ECO:0000313|Proteomes:UP000002350};
RN   [1] {ECO:0000313|Proteomes:UP000002350}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10179 / CIP 106290 / LMG 19151 / DSS12
RC   {ECO:0000313|Proteomes:UP000002350};
RX   PubMed=20458400; DOI=10.1039/c000396d;
RA   Aono E., Baba T., Ara T., Nishi T., Nakamichi T., Inamoto E.,
RA   Toyonaga H., Hasegawa M., Takai Y., Okumura Y., Baba M., Tomita M.,
RA   Kato C., Oshima T., Nakasone K., Mori H.;
RT   "Complete genome sequence and comparative analysis of Shewanella
RT   violacea, a psychrophilic and piezophilic bacterium from deep sea
RT   floor sediments.";
RL   Mol. Biosyst. 6:1216-1226(2010).
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; AP011177; BAJ00973.1; -; Genomic_DNA.
DR   RefSeq; WP_013050284.1; NC_014012.1.
DR   STRING; 637905.SVI_1002; -.
DR   EnsemblBacteria; BAJ00973; BAJ00973; SVI_1002.
DR   KEGG; svo:SVI_1002; -.
DR   eggNOG; ENOG4105C07; Bacteria.
DR   eggNOG; COG0060; LUCA.
DR   HOGENOM; HOG000246402; -.
DR   KO; K01870; -.
DR   OMA; HLGTAWN; -.
DR   OrthoDB; 32262at2; -.
DR   BioCyc; SVIO637905:G1GKA-945-MONOMER; -.
DR   Proteomes; UP000002350; 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; D4ZH24.
DR   SWISS-2DPAGE; D4ZH24.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02002,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00470441,
KW   ECO:0000313|EMBL:BAJ00973.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_02002,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00470429};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002350};
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   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:UP000002350};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_02002, ECO:0000256|SAAS:SAAS00803712}.
FT   DOMAIN       28    643       tRNA-synt_1. {ECO:0000259|Pfam:PF00133}.
FT   DOMAIN      688    843       Anticodon_1. {ECO:0000259|Pfam:PF08264}.
FT   DOMAIN      902    928       zf-FPG_IleRS. {ECO:0000259|Pfam:PF06827}.
FT   MOTIF        58     68       "HIGH" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_02002}.
FT   MOTIF       605    609       "KMSKS" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_02002}.
FT   METAL       903    903       Zinc. {ECO:0000256|HAMAP-Rule:MF_02002}.
FT   METAL       906    906       Zinc. {ECO:0000256|HAMAP-Rule:MF_02002}.
FT   METAL       923    923       Zinc. {ECO:0000256|HAMAP-Rule:MF_02002}.
FT   METAL       926    926       Zinc. {ECO:0000256|HAMAP-Rule:MF_02002}.
FT   BINDING     564    564       Aminoacyl-adenylate. {ECO:0000256|HAMAP-
FT                                Rule:MF_02002}.
FT   BINDING     608    608       ATP. {ECO:0000256|HAMAP-Rule:MF_02002}.
SQ   SEQUENCE   940 AA;  105686 MW;  E23CB1C3AB0E3D9D CRC64;
     MSDYKSTLNL PETEFPMRGN LANREPEMLK AWTEDGLYQK IRDSRIGRTP FILHDGPPYA
     NGDIHIGHSV NKILKDIIVK SKTLSGFDAP YIPGWDCHGL PIELKVEQKV GKPGHKVTAA
     EFREKCREYA AKQVDGQRDG FIRLGVFADW YKPYLTMDFG TEANIVRSLS KVIESGHLHK
     GVKPVHWCTD CGSALAEAEV EYEDKKSPAI DVAFVATDKA ALLAKFGALE IEADVSMVIW
     TTTPWTLPAN RALSIAADLD YSLVEFVKDD ATRVVILAEA LVESCMERYG VDSHKVLAQV
     KGQELELLRF DHPFYGFDVP VILGDHVTVD SGTGIVHTAP GHGQDDFIIG LKYGLEVANP
     VGDNGVYKSD TEIFAGQHVF KANANVVTLL EEKGALVKHE SILHSYPHCW RHKTPIIFRA
     TPQWFISMDN KGLRKQALGE IEKTKWIPDW GQSRIEKMVE NRPDWCISRQ RTWGVPITLF
     VHRETEELHP DSISLMERVA NKIEQKGIQA WWDLDTAELL GDEADQYRKV TDTLDVWFDS
     GSSFSSVVAA RPEYQGHGID LYLEGSDQHR GWFMSSLMIS TAMNGKAPYK QVLTHGFTVD
     GKGRKMSKSV GNVIAPQTIT NKLGADILRL WVAGTDYSGE MTVSDEILKR SADSYRRIRN
     TTRFLLANIN GFDPVTDAVA IEDMVALDRW VVRRAAALQE ELLEAYDQYN FHSVTQKLMQ
     FCSVELGSFY LDIIKDRQYT AKGDSHARRS CQSALYLISE AMVRWIAPIL SFTADEIWKL
     LPGERDAYVF TQEWFQGLES VTLESDLSDE FWDNLVSVRG EVNKVIEQAR REKQIGGSLE
     AEITLYADDD LAKILNSLGD ELRFVLLTSK TQVLALSAAP SDAIETELAS LKLGWLKSES
     AKCERCWHHR EDVAQIEAHP TLCTRCVTNI EGEGEVRKFA
//

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