(data stored in ACNUC7421 zone)

HOGENOM: DESAS_1_PE1010

ID   DESAS_1_PE1010                       STANDARD;      PRT;   927 AA.
AC   DESAS_1_PE1010; C8W4A7;
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; (DESAS_1.PE1010).
GN   Name=ileS; OrderedLocusNames=Dtox_1089;
OS   DESULFOTOMACULUM ACETOXIDANS DSM 771.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfotomaculum.
OX   NCBI_TaxID=485916;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS DESAS_1.PE1010.
CC       Desulfotomaculum acetoxidans DSM 771, complete genome.
CC       / IFO 0083) chromosome G, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:C8W4A7_DESAS
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; C8W4A7; -.
DR   EMBL; CP001720; ACV61975.1; -; Genomic_DNA.
DR   RefSeq; YP_003190598.1; NC_013216.1.
DR   ProteinModelPortal; C8W4A7; -.
DR   STRING; C8W4A7; -.
DR   GeneID; 8428028; -.
DR   GenomeReviews; CP001720_GR; Dtox_1089.
DR   KEGG; dae:Dtox_1089; -.
DR   OMA; KQVLTHG; -.
DR   ProtClustDB; PRK05743; -.
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; DESAS_1.PE1010; -.
KW   isoleucyl-tRNA synthetase;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis; Zinc.
SQ   SEQUENCE   927 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MDYGKTINLP QTDFPMRANL PNREPEILKY WTEKNIYRAV QEKNEGKPKF ILHDGPPYAN
     GDIHLGHTLN KILKDIIVKY KSMTGYDAPY VPGWDTHGLP IEQQAIKALG INRHEVDTVV
     FRNKCKEYAL KFVGIQKEEF IRLGVRADWD RSYVTLMPHF EARQIGVFGE MAKRGYIYKG
     LKPVYWCASC ETALAEAEVE YQDKKSPSIY VRFPVADSKG LFPSENTYLV IWTTTPWTIP
     GNVAISLHPE YFYVLVQIGE VKYIVAKELL ASFLELLGAQ GTVLQEFAGA ELERVVCRHP
     LLDRDSLVIL GEHVTLEQGT GCVHTAPGHG QEDFEAAKKY GLPVISPVNG KGVFTDEGGI
     FSGQFYLKAN QSVLDALTER GHLLFQAEID HQYPHCWRCK SSIFFRATEQ WFASIEGFRR
     QALEEIRKVQ WVPAWGEERI YGMVENRGDW CISRQRTWGV PIPIFYCSKC GKALINDRTI
     KHLQGLFKEH GSDVWFARQT ADLLPPDIAC PECSAADFTK ETDIMDVWFD SGSSHLAVLD
     EKTVWPELSW PADLYLEGSD QHRGWFNSSL STSVAVTGRA PYRAVLTHGF LVDEKGRKMS
     KSLGNVVDPL KVIQQLGADI LRLWVSSADY KSDLAVSQNI LKQLSEAYRK IRNTCRFLLS
     NIYDFDPSAD QVAYEKMVEL DRWALLKLHR LIEKVLNAYH DYEFHVVYHA IHNFCTVDMS
     NRYLDIIKDR LYTSPAESPD RRAAQTVLYL ILDALVRLLT PVLAFTSEEI WKHMPRVESR
     PESVQLADMP VVNEAYLDLE LEDKWQRIMA VRNEVIRILE GARQEKVIGN SLEAQVDLYC
     EKELHDFLEP LKDDLAAIFI VSVARLSNAG SEVPVHAVGS EIVSGLHVAV SRAPGGKCER
     CWMYHIAVGN DLEHPSLCPR CAGVLKK
//

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