EF2_PICGU
ID EF2_PICGU Reviewed; 842 AA.
AC A5DI11; Q6JED1; Q6JED3; Q9P4S2;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Elongation factor 2;
DE Short=EF-2;
GN Name=EFT2; ORFNames=PGUG_02912;
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
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 472-579.
RX PubMed=11158355; DOI=10.1099/00221287-147-2-383;
RA Shastry M., Nielsen J., Ku T., Hsu M.-J., Liberator P., Anderson J.,
RA Schmatz D., Justice M.C.;
RT "Species-specific inhibition of fungal protein synthesis by sordarin:
RT identification of a sordarin-specificity region in eukaryotic elongation
RT factor 2.";
RL Microbiology 147:383-390(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 586-786.
RC STRAIN=ATCC 46036 / CBS 2030 / IFO 10106 / NRRL Y-2075, MMRL 1635,
RC MMRL 1636, and MMRL 1759;
RX PubMed=15583292; DOI=10.1128/jcm.42.12.5624-5635.2004;
RA Diezmann S., Cox C.J., Schoenian G., Vilgalys R.J., Mitchell T.G.;
RT "Phylogeny and evolution of medical species of Candida and related taxa: a
RT multigenic analysis.";
RL J. Clin. Microbiol. 42:5624-5635(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 -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation.
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; CH408157; EDK38814.1; -; Genomic_DNA.
DR EMBL; AF107288; AAF81926.1; -; Genomic_DNA.
DR EMBL; AY497642; AAT12555.1; -; Genomic_DNA.
DR EMBL; AY497661; AAT12573.1; -; Genomic_DNA.
DR EMBL; AY497662; AAT12574.1; -; Genomic_DNA.
DR EMBL; AY497663; AAT12575.1; -; Genomic_DNA.
DR RefSeq; XP_001485183.1; XM_001485133.1.
DR AlphaFoldDB; A5DI11; -.
DR SMR; A5DI11; -.
DR STRING; 4929.XP_001485183.1; -.
DR PRIDE; A5DI11; -.
DR EnsemblFungi; EDK38814; EDK38814; PGUG_02912.
DR GeneID; 5126516; -.
DR KEGG; pgu:PGUG_02912; -.
DR VEuPathDB; FungiDB:PGUG_02912; -.
DR eggNOG; KOG0469; Eukaryota.
DR HOGENOM; CLU_002794_11_2_1; -.
DR InParanoid; A5DI11; -.
DR OMA; GVMTQTE; -.
DR OrthoDB; 140796at2759; -.
DR UniPathway; UPA00345; -.
DR Proteomes; UP000001997; Unassembled WGS sequence.
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_0000295030"
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; 93184 MW; B4C99E392F124E6B CRC64;
MVAFTIEQIR DLMDKVANVR NMSVIAHVDH GKSTLTDSLV QRAGIISAGK AGEARFMDTR
KDEQERGITI KSTAISLYAS MDDDDVKEIK QKTDGNSFLI NLIDSPGHVD FSSEVTAALR
VTDGALVVVD TVEGVCVQTE TVLRQALGER IKPVLVVNKV DRALLELQVS KEDLYQTFAR
TVESVNVIIS TYVDPALGDA QVYPDKGTVA FGSGLHGWAF TVRQFALRYS KKFGVDRAKM
MERLWGDSFF NPKTKKWTNK DKDADGKPLE RAFNMFVLDP IFRLFAAIMN FKKDEIPTLL
EKLEINLKNE EKELEGKALL KVVMRKFLPA ADALLEMIVL HLPSPVTAQA YRAETLYEGP
SDDEFCTAIR NCDPKADLML YVSKMVPTSD KGRFYAFGRV FAGTVKAGQK IRIQGPNYTP
GKKEDLFLKS IQRTVLMMGR NTEAIDDCPA GNIVGLVGVD QFLLKSGTIT TNEAAHNMKV
MKFSVSPVVE VAVEVKNAND LPKLVEGLKR LSKSDPCVKT YMSESGEHIV AGTGELHLEI
CLSDLQNDHA GIPLRISDPV VAYRETIQAE SSMVALSKSP NKHNRIYVKA QPIDEEVSLD
IENGIINPRD DFKARARILA DKHGWDVAEA RKIWCFGPDG NGPNLVVDQT KAVQYLNEIK
DSVVAAFQWA TKEGPIFGEN VRSVRVNILD VTLHADAIHR GGGQIIPTMR RVTYASMLLA
EPAIQEPVFL VEIQCPENAI GGIYSVLNKK RGQVVSEEQR PGTPLFTVKA YLPVNESFGF
SGDLRQATGG QAFPQLVFDH WAVLSGDVTD PTSKPGIIAK AKRERQGLKP EVPGYEEYYD
KL
