(data stored in SCRATCH zone)

SWISSPROT: C1E231_MICCC

ID   C1E231_MICCC            Unreviewed;       435 AA.
AC   C1E231;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   30-AUG-2017, entry version 44.
DE   RecName: Full=Elongation factor Tu {ECO:0000256|RuleBase:RU004061};
GN   ORFNames=MICPUN_90282 {ECO:0000313|EMBL:ACO62268.1};
OS   Micromonas commoda (strain RCC299 / NOUM17 / CCMP2709) (Picoplanktonic
OS   green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; prasinophytes; Mamiellophyceae;
OC   Mamiellales; Mamiellaceae; Micromonas.
OX   NCBI_TaxID=296587 {ECO:0000313|EMBL:ACO62268.1, ECO:0000313|Proteomes:UP000002009};
RN   [1] {ECO:0000313|EMBL:ACO62268.1, ECO:0000313|Proteomes:UP000002009}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC299 / NOUM17 {ECO:0000313|Proteomes:UP000002009};
RX   PubMed=19359590; DOI=10.1126/science.1167222;
RA   Worden A.Z., Lee J.H., Mock T., Rouze P., Simmons M.P., Aerts A.L.,
RA   Allen A.E., Cuvelier M.L., Derelle E., Everett M.V., Foulon E.,
RA   Grimwood J., Gundlach H., Henrissat B., Napoli C., McDonald S.M.,
RA   Parker M.S., Rombauts S., Salamov A., Von Dassow P., Badger J.H.,
RA   Coutinho P.M., Demir E., Dubchak I., Gentemann C., Eikrem W.,
RA   Gready J.E., John U., Lanier W., Lindquist E.A., Lucas S., Mayer K.F.,
RA   Moreau H., Not F., Otillar R., Panaud O., Pangilinan J., Paulsen I.,
RA   Piegu B., Poliakov A., Robbens S., Schmutz J., Toulza E., Wyss T.,
RA   Zelensky A., Zhou K., Armbrust E.V., Bhattacharya D., Goodenough U.W.,
RA   Van de Peer Y., Grigoriev I.V.;
RT   "Green evolution and dynamic adaptations revealed by genomes of the
RT   marine picoeukaryotes Micromonas.";
RL   Science 324:268-272(2009).
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of
CC       aminoacyl-tRNA to the A-site of ribosomes during protein
CC       biosynthesis. {ECO:0000256|RuleBase:RU000325}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC       subfamily. {ECO:0000256|RuleBase:RU000325}.
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DR   EMBL; CP001324; ACO62268.1; -; Genomic_DNA.
DR   RefSeq; XP_002501010.1; XM_002500964.1.
DR   ProteinModelPortal; C1E231; -.
DR   GeneID; 8241782; -.
DR   KEGG; mis:MICPUN_90282; -.
DR   HOGENOM; HOG000229290; -.
DR   InParanoid; C1E231; -.
DR   KO; K02358; -.
DR   Proteomes; UP000002009; Chromosome 3.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR   CDD; cd03697; EFTU_II; 1.
DR   HAMAP; MF_00118_B; EF_Tu_B; 1.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR033720; EFTU_2.
DR   InterPro; IPR031157; G_TR_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; TF_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel.
DR   InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR   InterPro; IPR004541; Transl_elong_EFTu/EF1A_bac/org.
DR   InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF03143; GTP_EFTU_D3; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF50465; SSF50465; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00485; EF-Tu; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; C1E231.
DR   SWISS-2DPAGE; C1E231.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002009};
KW   Elongation factor {ECO:0000256|RuleBase:RU000325};
KW   GTP-binding {ECO:0000256|RuleBase:RU000325};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU000325};
KW   Protein biosynthesis {ECO:0000256|RuleBase:RU000325};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002009}.
FT   DOMAIN       50    245       Tr-type G (guanine nucleotide-binding).
FT                                {ECO:0000259|PROSITE:PS51722}.
SQ   SEQUENCE   435 AA;  47353 MW;  A43F6BBCE8BB02B9 CRC64;
     MSSSLRRLAT TVARAAAPVY QGTSRAAGWR QTTPALWRTA RAYDVNSRSK EHLNIGTIGH
     VDHGKTTLTA AITKVLAEIG GAEVVAFDQI DKAPEEKARG ITISTSHVEY ETDKRHYAHV
     DCPGHADYVK NMITGAAQMD GGILVVSAAD GPMPQTREHI LLARQVGVPN LAVFLNKVDM
     VDDEELIDLV EMELREMLSF YKFDGDNIPI VRGSALHALK GTDDKLGKEA ILELMKACDA
     FPSPERVLDK PFSMPVEDVF SIQGRGTVAT GRIEQGIVKA GEDVELIGIV PTQKTTVTGV
     EMFKKSLTQG QAGDNCGLLL RGLKRDQVQR GQVLCKPGSI TPHKKFEAEI YVLNKDEGGR
     HTPFFSNYRP QFFMRTADIT GTITLPEGTE MVMPGDNITA VFELITPIAL EKGLRFALRE
     GGRTVGAGIV SKVLD
//

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