EF2_CANAW
ID EF2_CANAW Reviewed; 842 AA.
AC C4YJQ8; O13430; Q9P4S4;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Elongation factor 2;
DE Short=EF-2;
GN Name=EFT2; ORFNames=CAWG_04077;
OS Candida albicans (strain WO-1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294748;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WO-1;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 17-829.
RC STRAIN=WO-1;
RA Shastry M., Ku T., Justice M.C.;
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
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 -!- MISCELLANEOUS: Has antigenic properties. {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; CH672350; EEQ45742.1; -; Genomic_DNA.
DR EMBL; AF107286; AAF81924.1; -; Genomic_DNA.
DR AlphaFoldDB; C4YJQ8; -.
DR SMR; C4YJQ8; -.
DR STRING; 5476.C4YJQ8; -.
DR PRIDE; C4YJQ8; -.
DR EnsemblFungi; EEQ45742; EEQ45742; CAWG_04077.
DR VEuPathDB; FungiDB:CAWG_04077; -.
DR HOGENOM; CLU_002794_11_2_1; -.
DR OMA; GVMTQTE; -.
DR Proteomes; UP000001429; Chromosome 2, Supercontig 1.5.
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.
FT CHAIN 1..842
FT /note="Elongation factor 2"
FT /id="PRO_0000412978"
FT DOMAIN 17..346
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; 93384 MW; 4626DEABA4C22098 CRC64;
MVAFTIEQIR GLMDKVTNVR NMSVIAHVDH GKSTLSDSLV QKAGIISAAK AGDARFMDTR
KDEQERGITI KSTAISLYAS MTDEDVKDIK QKTDGNSFLV NLIDSPGHVD FSSEVTAALR
VTDGALVVVD TVEGVCVQTE TVLRQALGER IKPVVVINKV DRALLELQTT KEDLYQTFAR
TVESVNVIIS TYCDPVLGDV QVYPQKGTVA FASGLHGWAF TVRQFANKYS KKFGVDKEKM
MERLWGDSYF NPKTKKWTNK DKDADGKPLE RAFNMFILDP IFRLFAAIMN FKKDEIPVLL
EKLEIQLKGD EKDLEGKALL KVVMRKFLPA ADALLEMIVL HLPSPVTAQT YRAETLYEGP
SDDPFCTAIR NCDPNADLML YVSKMVPTSD KGRFYAFGRV FAGTVKSGQK VRIQGPNYQV
GKKEDLFLKS IQRTVLMMGR SVEQIDDCPA GNIIGLVGID QFLLKSGTIT TNEAAHNMKV
MKFSVSPVVQ VAVEVKNAND LPKLVEGLKR LSKSDPCVLT YMSESGEHIV AGTGELHLEI
CLQDLENDHA GVPLRISPPV VSYRETVEGE SSMVALSKSP NKHNRIYVKA QPIDEEVSLD
IENGVINPRD DFKARARILA DKHGWDVVDA RKIWCFGPDG NGPNLVVDQT KAVQYLNEIK
DSVVAAFQWA TKEGPIFGEN CRSVRVNILD VTLHADAIHR GGGQIIPTMR RVTYASMLLA
EPAIQEPVFL VEIQCPENAI GGIYSVLNKK RGQVISEEQR PGTPLFTVKA YLPVNESFGF
TGELRQATGG QAFPQLIFDH WQVMSGDVTD ENSKPGAIVK EKRVRAGLKP EVPEYTEYYD
KL
