(data stored in SCRATCH zone)

HOGENOM: CHLT1_1_PE100

ID   CHLT1_1_PE100                        STANDARD;      PRT;   896 AA.
AC   CHLT1_1_PE100; D6YPC4;
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=Translation initiation factor IF-2; (CHLT1_1.PE100).
GN   Name=infB; OrderedLocusNames=E11023_00500;
OS   CHLAMYDIA TRACHOMATIS E/11023.
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydia.
OX   NCBI_TaxID=707183;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CHLT1_1.PE100.
CC       Chlamydia trachomatis (serovar E, strain E/11023) chromosome, complete
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:D6YPC4_CHLT1
CC   -!- FUNCTION: One of the essential components for the initiation of
CC       protein synthesis. Protects formylmethionyl-tRNA from spontaneous
CC       hydrolysis and promotes its binding to the 30S ribosomal subunits.
CC       Also involved in the hydrolysis of GTP during the formation of the
CC       70S ribosomal complex (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the IF-2 family.
CC   -!- GENE_FAMILY: HOG000076906 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; D6YPC4; -.
DR   EMBL; CP001890; ADH20554.1; -; Genomic_DNA.
DR   GenomeReviews; CP001890_GR; E11023_00500.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   HAMAP; MF_00100_B; IF_2_B; 1; -.
DR   InterPro; IPR006847; IF2_N.
DR   InterPro; IPR000795; ProtSyn_GTP-bd.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000178; TF_IF2_bacterial-like.
DR   InterPro; IPR015760; TIF_IF2.
DR   InterPro; IPR023115; TIF_IF2_dom3.
DR   InterPro; IPR004161; Transl_elong_EFTu/EF1A_2.
DR   InterPro; IPR009000; Transl_elong_init/rib_B-barrel.
DR   Gene3D; G3DSA:3.40.50.10050; TIF_IF2_dom3; 1.
DR   PANTHER; PTHR23115:SF41; aIF-2; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 2.
DR   Pfam; PF11987; IF-2; 1.
DR   Pfam; PF04760; IF2_N; 1.
DR   SUPFAM; SSF52156; TIF_IF2_dom3; 1.
DR   SUPFAM; SSF50447; Translat_factor; 2.
DR   TIGRFAMs; TIGR00487; IF-2; 1.
DR   TIGRFAMs; TIGR00231; Small_GTP; 1.
DR   PROSITE; PS01176; IF2; 1.
DR   HOGENOMDNA; CHLT1_1.PE100; -.
KW   ADH20554.100024376fold_1320000031;
KW   Translation initiation factor IF-2 ;
KW   Complete proteome; Cytoplasm; GTP-binding; Initiation factor;
KW   Nucleotide-binding; Protein biosynthesis.
SQ   SEQUENCE   896 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MEKAKLTKNL KLKIKNAQLT KAAGLDKLKQ KLAQAGSSDT KNFPASKAQT KEKSSKKTVG
     TPAPAPEVDS GATESTARRI RAKDRSSFAA EPTVTTALPG DASHLTLDAI PAMKAPEITS
     ITQKEQTLVE CTDTSSVQQE EKKESSEETS PETPERVEET PIIRTRTEPK SVVSIKPKFG
     PTGKHINHLL AKTFKAPAKE TKAASTEETT QQQPRQNDAA SYNNKQQPSG TSSRPASFAP
     SYRRESTNNN NNNAKRGSER DRSKRSDESV KAFTGRDRYG LNEGSSEEDK WRKKRVHKTK
     KQAEEHVVQC PARIKIALPI TVKDLAAEMK LKASELIQKL FIHGMTYVVN DVLDSQTVVE
     YIGLEFGCTI EIDSSAKEKL CLLENAVRDE VNATDPEKLI IRSPIVAFMG HVDHGKTTII
     DALRQSNMAA SEAGAITQHT GAFKCTTPVG EITVLDTPGH EAFSAMRARG AEVCDIVVLV
     VAGDEGIKEQ TIEAIEHAKG ANITIVVAIN KCDKPNFNVE TVYRQLAELD LLPEAWGGSI
     ATINTSAKTG EGLQDLLEML ALQAEVLELK ADPSARARGL VIESELHKGL GAVATVLVQN
     GTLHLGEALV FNDCYGKVKT MHDEHNQLLQ SATPSTPVLI TGLSAIPKAG DPFIVVKNEK
     VAKEIISARL AGQQRSAALQ KKRPNFDAVL QNKKTLKLII KADVQGSIEA LAHSILNIRS
     EKVDVEILSS EVGDISESDI RLASASKATV IGFHTSVESH AEPLIKNLNV KVCLFDIIYH
     AVDAIKEIMT GLLDPIAEEK NLGAAEIKAT FKSSQLGTIY GCLVTEGTIV RNQKIRIIRD
     KEVLWKGSLS SLKRLKEDVK EVKKGMECGI LLDNYQQAQV GDILQCYEVI YHPQKL
//

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