(data stored in ACNUC19888 zone)

HOGENOM: AQAEO1_1_PE1

ID   AQAEO1_1_PE1                         STANDARD;      PRT;   699 AA.
AC   AQAEO1_1_PE1; O66428;
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=Elongation factor G; Short=EF-G; (AQAEO1_1.PE1).
GN   Name=fusA; OrderedLocusNames=aq_001;
OS   AQUIFEX AEOLICUS VF5.
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS AQAEO1_1.PE1.
CC       Aquifex aeolicus VF5, complete genome.
CC       1..8590 annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:EFG_AQUAE
CC   -!- FUNCTION: Catalyzes the GTP-dependent ribosomal translocation step
CC       during translation elongation. During this step, the ribosome
CC       changes from the pre-translocational (PRE) to the post-
CC       translocational (POST) state as the newly formed A-site-bound
CC       peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E
CC       sites, respectively. Catalyzes the coordinated movement of the two
CC       tRNA molecules, the mRNA and conformational changes in the
CC       ribosome (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the GTP-binding elongation factor family.
CC       EF-G/EF-2 subfamily.
CC   -!- GENE_FAMILY: HOG000231587 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; O66428; -.
DR   EMBL; AE000657; AAC06402.1; -; Genomic_DNA.
DR   PIR; A70300; A70300.
DR   RefSeq; NP_212986.1; NC_000918.1.
DR   ProteinModelPortal; O66428; -.
DR   SMR; O66428; 5-690.
DR   GeneID; 1192533; -.
DR   GenomeReviews; AE000657_GR; aq_001.
DR   KEGG; aae:aq_001; -.
DR   NMPDR; fig|224324.1.peg.1; -.
DR   OMA; SDNVKDD; -.
DR   PhylomeDB; O66428; -.
DR   ProtClustDB; PRK00007; -.
DR   BioCyc; AAEO224324:AQ_001-MON; -.
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:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR   HAMAP; MF_00054_B; EF-G_EF-2_B; 1; -.
DR   InterPro; IPR009022; Elongation_fac_G/III/V.
DR   InterPro; IPR000795; ProtSyn_GTP-bd.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR004540; Transl_elong_EFG/EF2.
DR   InterPro; IPR000640; Transl_elong_EFG/EF2_C.
DR   InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR   InterPro; IPR004161; Transl_elong_EFTu/EF1A_2.
DR   InterPro; IPR009000; Transl_elong_init/rib_B-barrel.
DR   Gene3D; G3DSA:3.30.230.10; Ribosomal_S5_D2-type_fold; 1.
DR   Gene3D; G3DSA:3.30.70.240; Transl_elong_EFG/EF2_C; 1.
DR   Pfam; PF00679; EFG_C; 1.
DR   Pfam; PF03764; EFG_IV; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SMART; SM00838; EFG_C; 1.
DR   SMART; SM00889; EFG_IV; 1.
DR   SUPFAM; SSF54980; EFG_III_V; 2.
DR   SUPFAM; SSF54211; Ribosomal_S5_D2-typ_fold; 1.
DR   SUPFAM; SSF50447; Translat_factor; 1.
DR   TIGRFAMs; TIGR00484; EF-G; 1.
DR   TIGRFAMs; TIGR00231; Small_GTP; 1.
DR   PROSITE; PS00301; EFACTOR_GTP; 1.
DR   HOGENOMDNA; AQAEO1_1.PE1; -.
KW   elongation factor G;
KW   Complete proteome; Cytoplasm; Elongation factor; GTP-binding;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
SQ   SEQUENCE   699 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MAREVPIEKL RNIGIVAHID AGKTTTTERI LYYTGKTYKI GEVHEGAATM DWMPQEKERG
     ITITVATTAC YWTRNGERYQ INIIDTPGHV DFSVEVVRSM KVLDGIVFIF SAVEGVQPQS
     EANWRWADRF QVPRIAFINK MDRLGADFYR VFKEIEEKLT IKPVAIQIPL GAEDQFEGVI
     DLMEMKAIRW LEETLGAKYE VVDIPPEYQE KAQEWREKMI ETIVETDDEL MEKYLEGQEI
     SIDELRKALR KATIERKLVP VLCGSAFKNK GVQPLLDAVI DYLPSPIDLP PVKGTNPKTG
     EEEVRHPSDD EPFCAYAFKV MSDPYAGQLT YIRVFSGTLK AGSYVYNATK DEKQRAGRLL
     LMHANSREEI QQVSAGEICA VVGLDAATGD TLCDEKHPII LEKLEFPDPV ISMAIEPKTK
     KDQEKLSQVL NKFMKEDPTF RATTDPETGQ ILIHGMGELH LEIMVDRMKR EYGIEVNVGK
     PQVAYKETIR KKAIGEGKFI KQTGGRGQYG HAIIEIEPLP RGAGFEFIDD IHGGVIPKEF
     IPSVEKGVKE AMQNGILAGY PVVDVRVRLF DGSYHEVDSS DIAFQVAGSL AFKDAAKKAD
     PVLLEPIMEV EVETPEKYVG DVIGDLNSRR GKIMGMENKG VITVIKAHVP LAEMFGYATT
     LRSLTQGRGT FIMKFSHYDE VPQQIAEKII GERMAGKSS
//

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