(data stored in SCRATCH zone)

HOGENOM: EUBR3_1_PE1001

ID   EUBR3_1_PE1001                       STANDARD;      PRT;   1055 AA.
AC   EUBR3_1_PE1001; C4ZGL8;
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; (EUBR3_1.PE1001).
GN   Name=ileS; OrderedLocusNames=EUBREC_1053;
OS   EUBACTERIUM RECTALE ATCC 33656.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae;
OC   Eubacterium.
OX   NCBI_TaxID=515619;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS EUBR3_1.PE1001.
CC       Eubacterium rectale ATCC 33656, complete genome.
CC       pEp5, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:C4ZGL8_EUBR3
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: Zinc (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 2 subfamily.
CC   -!- GENE_FAMILY: HOG000246403 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; C4ZGL8; -.
DR   EMBL; CP001107; ACR74815.1; -; Genomic_DNA.
DR   RefSeq; YP_002936949.1; NC_012781.1.
DR   ProteinModelPortal; C4ZGL8; -.
DR   STRING; C4ZGL8; -.
DR   GeneID; 7965428; -.
DR   GenomeReviews; CP001107_GR; EUBREC_1053.
DR   KEGG; ere:EUBREC_1053; -.
DR   OMA; QFGKWLE; -.
DR   ProtClustDB; PRK06039; -.
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:0008270; F:zinc ion binding; IEA:HAMAP.
DR   GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:HAMAP.
DR   HAMAP; MF_02003; Ile_tRNA_synth_type2; 1; -.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR002301; Ile-tRNA-synt.
DR   InterPro; IPR023586; Ile-tRNA-synt_type2.
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   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   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 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; EUBR3_1.PE1001; -.
KW   isoleucyl-tRNA synthetase;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis; Zinc.
SQ   SEQUENCE   1055 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MYNKVDTNMN FVEREKKTEQ FWRENNIFRK SMENRKEGET YTFYDGPPTA NGKPHIGHVE
     TRTIKDMIPR FQTMKGKYVP RKAGWDTHGL PVEIEVEKLL GLDGKDQIEN YGLEPFIKKC
     KESVWKYKGM WEDFSNTVGF WADMDNPYVT YDDNFIESEW WALKEIWNKG LLYKGFKIVP
     YCPRCGTPLS AQEVAQGYKT VKEKSAVVRF KVVGEDAYFL AWTTTPWTLP SNVALCVNPN
     DTYVKVKAVD GYTYYMAEAL ADKVLSQLLS KEDAEAGKKA YEVLETYKGK DLEYKEYEPL
     YDCAKQVADK QGKKGFFVTC DTYVTMSDGT GIVHIAPAFG EDDANVGRNY DLPFVQFVND
     KGELTAETPF AGMWVKDADP EVLKDLSGRK QLFDAPKFEH EYPHCWRCDK PLIYYARESW
     YIKETAVKDD LIRNNNTVNW IPESIGSGRF GNWLENIQDW AISRNRYWGT PLNIWECECG
     HRECIGSRAE LAEKAGDPKA AEVELHRPYI DAVTIKCPEC GKDMHRVPEV LDCWFDSGAM
     PFAQHHYPFE NKEVFEKQFP AKFISEAVDQ TRGWFHSLMA ESTLLFNKAP YENVIVLGHV
     QDENGQKMSK SKGNAVDPFD ALETYGADAI RWYFYTASAP WIPKKFSGKL VLEGQRKFMG
     TLWNTYAFFV LYANIDNFDA TKYSLEYDKL AVMDKWILSK LNSAVAGVDE CLSNYKIPEA
     AKYLQEFVDD LSNWYVRRSR ERFWAKGMEQ DKINAYMTLY TALVTISKAA APMIPFMTED
     IYRNLVCSID KSAPESIHLC DYPVVDEKLI DKKLEADMDE VLKVVVLGRA CRNEANIKNR
     QPIGKMFVKA PEKLDEFYVD IIADELNVKE VEFTDDVSHY TTYKFKPQLR TVGPKYGKYL
     GQIKAVLAEL DGHKAMEELN STGSLKLDSI SDEVVLSKED LLIEMTQMEG YVTQSDNNIT
     VVLDTNLTPE LIEEGFVREI ISKIQTMRKD AGFEVMDHIA VTYEADEKLS NVFEKFGDEI
     KTEVLAVSIK SGELKGYEKD WKINGEAVKL AVEKQ
//

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