(data stored in ACNUC7421 zone)

HOGENOM: SHEVD_1_PE1002

ID   SHEVD_1_PE1002                       STANDARD;      PRT;   940 AA.
AC   SHEVD_1_PE1002; D4ZH24;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Isoleucyl-tRNA synthetase; EC=6.1.1 5;AltName:
DE   Full=Isoleucine--tRNA ligase; (SHEVD_1.PE1002).
GN   Name=ileS; OrderedLocusNames=SVI_1002;
OS   SHEWANELLA VIOLACEA DSS12.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=637905;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS SHEVD_1.PE1002.
CC       Shewanella violacea DSS12 chromosome, complete genome.
CC       annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:D4ZH24_SHEVD
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) (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + L-isoleucine + tRNA(Ile) = AMP +
CC       diphosphate + L-isoleucyl-tRNA(Ile).
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
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)) (By similarity).
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. IleS type 1 subfamily.
CC   -!- GENE_FAMILY: HOG000246402 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; D4ZH24; -.
DR   EMBL; AP011177; BAJ00973.1; -; Genomic_DNA.
DR   RefSeq; YP_003555751.1; NC_014012.1.
DR   ProteinModelPortal; D4ZH24; -.
DR   GeneID; 8969062; -.
DR   GenomeReviews; AP011177_GR; SVI_1002.
DR   KEGG; svo:SVI_1002; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004822; F:isoleucine-tRNA ligase activity; IEA:HAMAP.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:HAMAP.
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; IPR002301; Ile-tRNA-synt.
DR   InterPro; IPR023585; Ile-tRNA-synt_type1.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_1a_anticodon-bd.
DR   InterPro; IPR013155; V/L/I-tRNA-synth_anticodon-bd.
DR   InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR   InterPro; IPR010663; Znf_DNA_glyclase/IsotRNA_synth.
DR   Gene3D; G3DSA:3.90.740.10; G3DSA:3.90.740.10; 1.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 2.
DR   PANTHER; PTHR11946:SF9; Ile-tRNA-synt_Ia; 1.
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; tRNAsyn_1a_bind; 1.
DR   SUPFAM; SSF50677; ValRS_IleRS_edit; 1.
DR   TIGRFAMs; TIGR00392; IleS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR   HOGENOMDNA; SHEVD_1.PE1002; -.
KW   isoleucyl-tRNA synthetase;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis; Zinc.
SQ   SEQUENCE   940 AA;  UNKNOWN MW;  UNKNOWN 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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