ID I7MDQ0_TETTS Unreviewed; 842 AA.
AC I7MDQ0;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=Elongation factor 2 {ECO:0000256|ARBA:ARBA00017891};
GN ORFNames=TTHERM_00706400 {ECO:0000313|EMBL:EAR90725.1};
OS Tetrahymena thermophila (strain SB210).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC Tetrahymena.
OX NCBI_TaxID=312017 {ECO:0000313|EMBL:EAR90725.1, ECO:0000313|Proteomes:UP000009168};
RN [1] {ECO:0000313|Proteomes:UP000009168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB210 {ECO:0000313|Proteomes:UP000009168};
RX PubMed=16933976; DOI=10.1371/journal.pbio.0040286;
RA Eisen J.A., Coyne R.S., Wu M., Wu D., Thiagarajan M., Wortman J.R.,
RA Badger J.H., Ren Q., Amedeo P., Jones K.M., Tallon L.J., Delcher A.L.,
RA Salzberg S.L., Silva J.C., Haas B.J., Majoros W.H., Farzad M.,
RA Carlton J.M., Smith R.K. Jr., Garg J., Pearlman R.E., Karrer K.M., Sun L.,
RA Manning G., Elde N.C., Turkewitz A.P., Asai D.J., Wilkes D.E., Wang Y.,
RA Cai H., Collins K., Stewart B.A., Lee S.R., Wilamowska K., Weinberg Z.,
RA Ruzzo W.L., Wloga D., Gaertig J., Frankel J., Tsao C.-C., Gorovsky M.A.,
RA Keeling P.J., Waller R.F., Patron N.J., Cherry J.M., Stover N.A.,
RA Krieger C.J., del Toro C., Ryder H.F., Williamson S.C., Barbeau R.A.,
RA Hamilton E.P., Orias E.;
RT "Macronuclear genome sequence of the ciliate Tetrahymena thermophila, a
RT model eukaryote.";
RL PLoS Biol. 4:1620-1642(2006).
CC -!- FUNCTION: Catalyzes the GTP-dependent ribosomal translocation step
CC during translation elongation. During this step, the ribosome changes
CC from the pre-translocational (PRE) to the post-translocational (POST)
CC state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound
CC deacylated tRNA move to the P and E sites, respectively. Catalyzes the
CC coordinated movement of the two tRNA molecules, the mRNA and
CC conformational changes in the ribosome.
CC {ECO:0000256|ARBA:ARBA00024731}.
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DR EMBL; GG662794; EAR90725.1; -; Genomic_DNA.
DR RefSeq; XP_001010970.1; XM_001010970.3.
DR AlphaFoldDB; I7MDQ0; -.
DR STRING; 312017.I7MDQ0; -.
DR EnsemblProtists; EAR90725; EAR90725; TTHERM_00706400.
DR GeneID; 7840201; -.
DR KEGG; tet:TTHERM_00706400; -.
DR eggNOG; KOG0469; Eukaryota.
DR HOGENOM; CLU_002794_11_2_1; -.
DR InParanoid; I7MDQ0; -.
DR OrthoDB; 143042at2759; -.
DR Proteomes; UP000009168; Unassembled WGS sequence.
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 CDD; cd01681; aeEF2_snRNP_like_IV; 1.
DR CDD; cd04096; eEF2_snRNP_like_C; 1.
DR CDD; cd01885; EF2; 1.
DR CDD; cd16268; EF2_II; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.240; -; 1.
DR Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR041095; EFG_II.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR42908:SF3; ELONGATION FACTOR-LIKE GTPASE 1; 1.
DR PANTHER; PTHR42908; TRANSLATION ELONGATION FACTOR-RELATED; 1.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF14492; EFG_III; 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; EF-G C-terminal domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW Elongation factor {ECO:0000313|EMBL:EAR90725.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000313|EMBL:EAR90725.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009168}.
FT DOMAIN 17..344
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 842 AA; 94250 MW; DC0ACFEAEC8EFD52 CRC64;
MKTLQIEKIR ELMMNPNQIR NMSVIAHVDH GKTTLTDSLL ARAGIISENN AGKACMMDTD
PKEQEMGITI KSTGVSLYYQ NTVNKQESII NLIDSPGHID FSGEVTAALR VTDGALVVVD
AVEGVAVQTE TVLRQACQER IRPVLVINKL DRLFSELKDD YENIYQRLIK IIAKVNSILE
MHENDSIKNY TLDPSLGNVA FSSGKQCWGF TLKTFARIYS QKFSTKEDIL MNKLWGDNYF
NPQTKSFTQD AHLINNEGKK AQRSFIEFVL APLDKYYSAS SNADIETLSK MVEKLHISTI
LTTAELDRLK QLEVQERIKK SMRAWLPLAD AILEMVQDHL PSPREAMKYR SMYLYEGPAD
DEACTAMKEC NSEGPLMVYI SKMVPTSDLS RFYAFGRVFS GTITQGMKVR VQGPDYKPGT
KEGLFIKTIQ RTFLMMGKQQ EAIESVPAGG TVLILGIDSA LTKTGTLTTS ESAHNIRNMK
YTISPILRVA VSTPNQQDLP RLLEGLKMLQ QYDQLVQVEI DENTGSYVVA GGGELHVQIC
LEKLNDFTHN SIKIVASQPT VSYRETISEK SSQTCLAKTA NKLNRLYGTC DPLDEALGSA
ISDNKINIQE VNSQETINTL VNTYNWERED AKKIWCFGPL EKESTNCIVN LTVGIQGMPA
IQPSIITAFE WCTKEGLLCD EPLRNTRFNI TDAVIHIDPA HHRSNQITPA ARRLFKACQY
VSEPKILEPF YQCDIRIPDD SKGPIYAVLN KRRGIVVGEE YEEALSMIQA HIPVSESFGL
DQALKSATQG KAIPALSFSH WQVVQGNPLD PETKSGKIVT EIRTRKGLTA KIPELNNYLD
KL
//