EF2_CHICK
ID EF2_CHICK Reviewed; 858 AA.
AC Q90705;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Elongation factor 2;
DE Short=EF-2;
GN Name=EEF2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Intestine;
RA Kim C.W., Jung E.J., Ahn H.J., Kim J.C., Kang K.R., Eom M.-O., Kim Y.W.,
RA Kang Y.-S.;
RT "Molecular cloning of chicken elongation factor 2 (EF-2): sequence
RT comparison with mammalian EF-2 and its expression in the early
RT developmental stages of the embryos.";
RL Mol. Cells 3:27-33(1993).
RN [2]
RP PROTEIN SEQUENCE OF 2-22, AND PHOSPHORYLATION.
RX PubMed=1708237; DOI=10.1016/0006-291x(91)91578-z;
RA Kim Y.W., Kim C.W., Kang K.R., Byun S.M., Kang Y.S.;
RT "Elongation factor-2 in chick embryo is phosphorylated on tyrosine as well
RT as serine and threonine.";
RL Biochem. Biophys. Res. Commun. 175:400-406(1991).
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 -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- PTM: Phosphorylation by EF-2 kinase completely inactivates EF-2.
CC {ECO:0000250}.
CC -!- PTM: Diphthamide is 2-[3-carboxyamido-3-(trimethyl-
CC ammonio)propyl]histidine (By similarity).
CC {ECO:0000250|UniProtKB:P05197}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-G/EF-2
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01059}.
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DR EMBL; U46663; AAA87587.1; -; mRNA.
DR RefSeq; NP_990699.1; NM_205368.1.
DR AlphaFoldDB; Q90705; -.
DR SMR; Q90705; -.
DR BioGRID; 676581; 1.
DR STRING; 9031.ENSGALP00000042519; -.
DR PaxDb; Q90705; -.
DR GeneID; 396325; -.
DR KEGG; gga:396325; -.
DR CTD; 1938; -.
DR VEuPathDB; HostDB:geneid_396325; -.
DR eggNOG; KOG0469; Eukaryota.
DR InParanoid; Q90705; -.
DR OrthoDB; 140796at2759; -.
DR PhylomeDB; Q90705; -.
DR PRO; PR:Q90705; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR GO; GO:0006414; P:translational elongation; IBA:GO_Central.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 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; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
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; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
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; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF54980; SSF54980; 2.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Elongation factor; GTP-binding;
KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1708237"
FT CHAIN 2..858
FT /note="Elongation factor 2"
FT /id="PRO_0000091005"
FT DOMAIN 17..362
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT BINDING 26..33
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 104..108
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 158..161
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 57
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 59
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 715
FT /note="Diphthamide"
FT /evidence="ECO:0000250|UniProtKB:P05197"
SQ SEQUENCE 858 AA; 95378 MW; 287F13E49173D754 CRC64;
MVNFTVDQIR AIMDKKANIR NMSVIAHVDH GKSTLTDSLV CKAGIIASAR AGETRFTDTR
KDEQERCITI KSTAISLFYE LSENDLAFIK QSKDGSGFLI NLIDSPGHVD FSSEVTAALR
VTDGALVVVD CVSGVCVQTE TVLRQAIAER IKPVLMMNKM DRALLELQLD PEELYQTFQR
IVENVNVIIS TYGEGESGPM GNIMIDPVLG TVGFGSGLHG WAFTLKQFAE MYVAKFAAKG
DAQMNPTERA KKVEDMMKKL WGDRYFDPAT GKFSKSATGP DGKKLPRTFC QLILDPIFKV
FDAIMTFKKE EAAKLIEKLD IKLDSEDKDK EGKPLLKAVM RRWLPAGDAL LQMITIHLPS
PVTAQKYRCE LLYEGPPDDE AAIGIKNCDP RGSLMMYISK MVPTSDKGRF YAFGRVFSGL
VSTGLKVRIM GPNYTPGKKE DLYLKPIQRT ILMMGRYVEP IEDVPCGNIV GLVGVDQFLV
KTGTITTFEH AHNMRVMKFS VSPVVRVAVE AKNPADLPKL VEGLKRLAKS DPMVQCIIEE
SGEHIIAGAG ELHLEICLKD LEEDHACIPI KKSDPVVSYR ETVSEESNVM CLSKSPNKHN
RLYMKARPFP DGLAEDIDKG EVSARQELKQ RARYLAEKYE WDVTEARKIW CFGPDGTGPN
ILTDITKGVQ YLNEIKDSVV AGFQWATKEG VLCEENMRGV RFDVHDVTLH ADAIHRGGGQ
IIPTARRCLY ACVLTAQPRL MEPIYLVEIQ CPEQVVGGIY GVLNRKRGHV FEESQVAGTP
MFVVKAYLPV NESFGFTADL RSNTGGQAFP QCVFDHWQIL PGDPFDSASR PSQVVAETRK
RKGLKEGIPA LDNFLDKL
