EF2_CANGA
ID EF2_CANGA Reviewed; 842 AA.
AC Q6FYA7;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Elongation factor 2;
DE Short=EF-2;
GN Name=EFT1; OrderedLocusNames=CAGL0A03234g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380947; CAG57801.1; -; Genomic_DNA.
DR RefSeq; XP_444908.1; XM_444908.1.
DR AlphaFoldDB; Q6FYA7; -.
DR SMR; Q6FYA7; -.
DR STRING; 5478.XP_444908.1; -.
DR PRIDE; Q6FYA7; -.
DR EnsemblFungi; CAG57801; CAG57801; CAGL0A03234g.
DR GeneID; 2886326; -.
DR KEGG; cgr:CAGL0A03234g; -.
DR CGD; CAL0126687; EFT2.
DR VEuPathDB; FungiDB:CAGL0A03234g; -.
DR eggNOG; KOG0469; Eukaryota.
DR HOGENOM; CLU_002794_11_2_1; -.
DR InParanoid; Q6FYA7; -.
DR OMA; GVMTQTE; -.
DR Proteomes; UP000002428; Chromosome A.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0062040; C:fungal biofilm matrix; IDA:CGD.
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_0000091016"
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; 93329 MW; B7A4D4771E9CE6B8 CRC64;
MVAFTVDQMR SLMDKVTNVR NMSVIAHVDH GKSTLTDSLV QKAGIISAAK AGEARFMDTR
KDEQERGITI KSTAISLYSD LPEEDVKEIP QKSDGNSFLI NLIDSPGHVD FSSEVTAALR
VTDGALVVVD TVEGVCVQTE TVLRQALGER IKPVVCINKV DRALLELQVS KEDLYQSFSR
TVESVNVIIS TYSDEVLGDV QVYPSKGTVA FGSGLHGWAF TIRQFATRYA KKFGVDKQKM
MERLWGDSFF NPKTKKWTNK ETDTDGKPLE RAFNMFVLDP IFRLFAAIMN FKKDEIPTLL
EKLEINLKSD EKDLEGKALL KVVMRKFLPA ADALLEMIVM HLPSPVTAQN YRAEQLYEGP
ADDANCIAIK KCDPTADLML YVSKMVPTSD KGRFYAFGRV FAGTVKSGQK IRIQGPNYVP
GKKDDLFLKA VQRVVLMMGS RVEPIDDCPA GNIVGLVGID QFLLKTGTLT TSETAYNMKV
MKFSVSPVVQ VAVDVKNAND LPKLVEGLKR LSKSDPCVLT QMSESGEHIV AGTGELHLEI
CLQDLENEHA GIPLKISPPV VAYRETVEAE SSQVALSKSP NKHNRIYLKA EPMDEEVSLA
IEQGKINPRD DFKARARVMA DEYGWDVTDA RKIWCFGPDG NGPNLVVDQT KAVQYLNEIK
DSVVSAFQWA TKEGPILGET MRSVRVNILD VTLHADAIHR GAGQIMPTMR RATYAGFLLA
EPKIQEPVFL VEIQCPEQAV GGIYSVLNKK RGQVVSEEQR PGTPLFTVKA YLPVNESFGF
TGELRQATGG QAFPQMVFDH WATLNSDPLD PTSKAGEIVT AARKRHGMKE EVPGWQEYYD
KL
