ID EF2_DEBHA Reviewed; 842 AA.
AC Q6BJ25;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 27-MAR-2024, entry version 114.
DE RecName: Full=Elongation factor 2;
DE Short=EF-2;
DE EC=3.6.5.- {ECO:0000250|UniProtKB:P32324};
GN Name=EFT1; OrderedLocusNames=DEHA2G05742g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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. {ECO:0000250|UniProtKB:P32324}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000250|UniProtKB:P32324};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000250|UniProtKB:P32324};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P32324}.
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; CR382139; CAG90255.1; -; Genomic_DNA.
DR RefSeq; XP_461796.1; XM_461796.1.
DR AlphaFoldDB; Q6BJ25; -.
DR SMR; Q6BJ25; -.
DR STRING; 284592.Q6BJ25; -.
DR GeneID; 2904673; -.
DR KEGG; dha:DEHA2G05742g; -.
DR VEuPathDB; FungiDB:DEHA2G05742g; -.
DR eggNOG; KOG0469; Eukaryota.
DR HOGENOM; CLU_002794_11_2_1; -.
DR InParanoid; Q6BJ25; -.
DR OMA; NRHNRFY; -.
DR OrthoDB; 166721at2759; -.
DR Proteomes; UP000000599; Chromosome G.
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 CDD; cd01681; aeEF2_snRNP_like_IV; 1.
DR CDD; cd04096; eEF2_snRNP_like_C; 1.
DR CDD; cd01885; EF2; 1.
DR CDD; cd16261; EF2_snRNP_III; 1.
DR CDD; cd03700; EF2_snRNP_like_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; IPR031157; G_TR_CS.
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:SF10; ELONGATION FACTOR 2; 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; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Elongation factor; GTP-binding; Hydrolase; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..842
FT /note="Elongation factor 2"
FT /id="PRO_0000091017"
FT DOMAIN 17..253
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|UniProtKB:P32324"
FT BINDING 158..161
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32324"
FT BINDING 213..215
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32324"
FT MOD_RES 699
FT /note="Diphthamide"
FT /evidence="ECO:0000250|UniProtKB:P32324"
SQ SEQUENCE 842 AA; 93194 MW; 230ADE6BBFDAC663 CRC64;
MVAFTIEQIR ELMDKVTNVR NMSVIAHVDH GKSTLTDSLV QRAGIISAAK AGEARFTDTR
KDEQERGITI KSTAISLYAS MTDDDCKEIQ QKTVGNSFLI NLIDSPGHVD FSSEVTAALR
VTDGALVVVD CVEGVCVQTE TVLRQALGER IKPVVIINKV DRALLELQVT KEDLYQSFSR
TIESVNVIIS TYVDSSLGDS QVYPDKGTVA FGSGLHGWAF TVRQFATRYS KKFGVDRIKM
MERLWGDSYF NPKTKKWTNK DKDAEGKTLE RAFNMFVLDP IFRLFSSIMN FKKSEIPTLL
EKLEINLKAE EKELEGKALL KVVMRKFLPA ADALLEMIVI HLPSPVTAQA YRAETLYEGP
ADDASCIAIK NCDPTADLMV YISKMVPTSD KGRFYAFGRV FAGTVKSGQK VRIQGPNYQV
GKKDDLFVKA IQRTVLMMGR FVEAIDDCPA GNIVGLVGVD QFLLKSGTIT TNEASHNMKV
MKFSVSPVVQ VAVEVKNAND LPKLVEGLKR LSKSDPCVLT SMSESGEHIV AATGELHLEI
CLSDLQNDHA GIPLKISPPI VSYRETVNAE SSMVALSKSP NKHNRIYVKA QPIDEEVSLD
IEKGVINPRD DFKARARILA DNHGWDVTDA RKIWCFGPDG NGPNLVVDQT KAVQYLNEIK
DSVVAAFQWA TKEGPIFGEN VRSVRVNILD VTLHADAIHR GGGQIIPTMR RVTYASMLLA
EPAIQEPVFL VEIQCPENAI GGIYSVLNKK RGQVISEEQR PGTPLFTVKA YLPVNESFGF
SGELRQSTGG QAFPQLIFDH WANLNGDPTD PTSKVGTIVK EKRERQGMKP DVPGYEEYYD
KL
//
