EF2_KLULA
ID EF2_KLULA Reviewed; 842 AA.
AC Q6CPQ9;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Elongation factor 2;
DE Short=EF-2;
GN Name=EFT1; OrderedLocusNames=KLLA0E02926g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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; CR382125; CAG99167.1; -; Genomic_DNA.
DR RefSeq; XP_454080.1; XM_454080.1.
DR AlphaFoldDB; Q6CPQ9; -.
DR SMR; Q6CPQ9; -.
DR STRING; 28985.XP_454080.1; -.
DR PRIDE; Q6CPQ9; -.
DR EnsemblFungi; CAG99167; CAG99167; KLLA0_E02993g.
DR GeneID; 2893753; -.
DR KEGG; kla:KLLA0_E02993g; -.
DR eggNOG; KOG0469; Eukaryota.
DR HOGENOM; CLU_002794_11_2_1; -.
DR InParanoid; Q6CPQ9; -.
DR OMA; GVMTQTE; -.
DR Proteomes; UP000000598; Chromosome E.
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 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 3: Inferred from homology;
KW Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..842
FT /note="Elongation factor 2"
FT /id="PRO_0000091018"
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"
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 699
FT /note="Diphthamide"
FT /evidence="ECO:0000250"
SQ SEQUENCE 842 AA; 93417 MW; 05159A7087340FC9 CRC64;
MVAFTVDQIR SLMDKVTNVR NMSVIAHVDH GKSTLTDSLV QRAGIISAAK AGEARFTDTR
KDEQERGITI KSTAISLFSE MSDDDVKDIK QKTDGNAFLI NLIDSPGHVD FSSEVTAALR
VTDGALVVVD TVEGVCVQTE TVLRQSLAER IKPVVVINKV DRALLELQVS KEDLYQSFSR
TVESVNVIIS TYADEVLGDV QVYPQRGTVA FGSGLHGWAF TVRQFANRYS KKFGVDREKM
MDRLWGDSYF NPKTKKWTNK ERDADGKPLE RAFNMFVLDP IFRLFAAIMN FKKEEIPVLL
EKLEINLKGD EKELEGKNLL KVVMRKFLPA ADALLEMIIL HLPSPVTAQN YRAEQLYEGP
SDDPACIAIK NCDPKSDLML YVSKMVPTSD KGRFYAFGRV FAGTVKSGQK VRIQGPNFIP
GKKEDLFIKA IQRAVLMMGR FVEPIDDCPA GNIIGLVGID QFLLKTGTLT TFEGAHNMKV
MKFSVSPVVQ VAVEVKNAND LPKLVEGLKR LSKSDPCVLV SMSESGEHIV AGTGELHLEI
CLQDLENDHA GIPLKISPPV VAYRETVEGE SSQTALSKSP NKHNRIYLKA QPIDEEVSLA
IEGGKINPRD DFKARARIMA DEFGWDVTDA RKIWCFGPDG NGPNLVVDQT KAVQYLNEIK
DSVVAAFQWA TKEGPIFGEQ MRSVRVNILD VTLHADAIHR GGGQIIPTMR RATYAGFLLA
EPKIQEPVFL VEIQCPEQAI GGIYSVLNKK RGQVVSEEQR PGTPLFTVKA YLPINESFGF
TGELRQATGG QAFPQMVFDH WATLGTDPLD PSTKAGEIVL AARKRQGMKE EVPGWQEYYD
KL
