EF2_ASHGO
ID EF2_ASHGO Reviewed; 842 AA.
AC Q754C8; Q6JEG2;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Elongation factor 2;
DE Short=EF-2;
GN Name=EFT1; OrderedLocusNames=AFR142C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 586-786.
RC STRAIN=ATCC 8717 / IMI 31268;
RA Diezmann S., Cox C.J., Schoenian G., Vilgalys R.J., Mitchell T.G.;
RT "Molecular phylogeny and evolution of Candida and related species within
RT the order saccharomycetales as inferred from multilocus sequence
RT analysis.";
RL Submitted (DEC-2003) 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 -!- 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; AE016819; AAS53513.1; -; Genomic_DNA.
DR EMBL; AY497630; AAT12544.1; -; Genomic_DNA.
DR RefSeq; NP_985689.1; NM_211043.1.
DR AlphaFoldDB; Q754C8; -.
DR SMR; Q754C8; -.
DR STRING; 33169.AAS53513; -.
DR EnsemblFungi; AAS53513; AAS53513; AGOS_AFR142C.
DR GeneID; 4621940; -.
DR KEGG; ago:AGOS_AFR142C; -.
DR eggNOG; KOG0469; Eukaryota.
DR HOGENOM; CLU_002794_11_2_1; -.
DR InParanoid; Q754C8; -.
DR OMA; GVMTQTE; -.
DR Proteomes; UP000000591; Chromosome VI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 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_0000091014"
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; 93546 MW; 3589DE3FE3D1696A CRC64;
MVAFTVDQIR SLMDKVTNVR NMSVIAHVDH GKSTLTDSLV QRAGIISAAK AGEARFTDTR
KDEQERGITI KSTAISLFSE MSEEDVKDIK QKTEGNSFLI NLIDSPGHVD FSSEVTAALR
VTDGALVVVD TVEGVCVQTE TVLRQALGER IKPVVVINKV DRALLELQVS KEDLYQSFSR
TVESVNVIIS TYADEVLGDV QVYPQKGTVA FGSGLHGWAF TIRQFANRYS KKFGVDREKM
MERLWGDSYF NPKTKKWTNK DRDADGKPLE RAFNMFVLDP IFRLFAAIMN FKKDEIPVLL
EKLEIALKSD ERDLEGKALL KVVMRKFLPA ADALLEMIIM HLPSPVTAQN YRAEQLYEGP
SDDPACIAIK NCDPKADLML YVSKMVPTSD KGRFYAFGRV FSGTVKSGQK VRIQGPSFTV
GKKEDLFIKA IQRAVLMMGR FVEPIDDCPA GNIVGLVGID QFLLKTGTLT TFESAHNMKV
MKFSVSPVVQ VAVEVKNAND LPKLVEGLKR LSKSDPCVLT YMSESGEHIV AGTGELHLEI
CLQDLENDHA GIPLKISPPV VAYRETVEGE SSQVALSKSP NKHNRIYLKA QPIDEEVSLA
IEGGKINPRD DFKARARVMA DEYGWDVTDA RKIWCFGPDG NGPNLVVDQT KAVQYLNEIK
DSVVSAFQWA TKEGPIFGEQ MRSVRINLLD VTLHADAIHR GAGQIMPTMR RATYAGFLLA
EPKIQEPVFL VEIQCPEQAV GGIYSVLNRK RGQVVSEEQR PGTPLFTVKA YLPVNESFGF
TGELRQATGG QAFPQMVFDH WATLGTDPLD PTTKAGEIVV EARKRHGLKE NVPGWQEYYD
KL
