ID   EF2_CANAL               Reviewed;         842 AA.
AC   Q5A0M4; A0A1D8PGT9; O13430; Q9P4S4;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 2.
DT   27-MAR-2024, entry version 129.
DE   RecName: Full=Elongation factor 2;
DE            Short=EF-2;
DE            EC=3.6.5.- {ECO:0000250|UniProtKB:P32324};
GN   Name=EFT2; OrderedLocusNames=CAALFM_C203100WA;
GN   ORFNames=CaO19.13210, CaO19.5788;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 10261 / CBS 2718 / NBRC 1061;
RA   Capa L., Mendoza A., Serramia M.J., Garcia-Bustos J.F.;
RL   Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN   [5]
RP   PROTEIN SEQUENCE OF 559-564; 581-585 AND 675-682, SUBCELLULAR LOCATION, AND
RP   ANTIGENICITY.
RC   STRAIN=SC5314 / ATCC MYA-2876; TISSUE=Protoplast;
RX   PubMed=15378761; DOI=10.1002/pmic.200400903;
RA   Pitarch A., Abian J., Carrascal M., Sanchez M., Nombela C., Gil C.;
RT   "Proteomics-based identification of novel Candida albicans antigens for
RT   diagnosis of systemic candidiasis in patients with underlying hematological
RT   malignancies.";
RL   Proteomics 4:3084-3106(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. {ECO:0000250|UniProtKB:P32324}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC         Evidence={ECO:0000250|UniProtKB:P32324};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC         Evidence={ECO:0000250|UniProtKB:P32324};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15378761}.
CC   -!- MISCELLANEOUS: Has antigenic properties.
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; Y09664; CAA70857.2; -; Genomic_DNA.
DR   EMBL; CP017624; AOW27347.1; -; Genomic_DNA.
DR   RefSeq; XP_019330758.1; XM_019475213.1.
DR   AlphaFoldDB; Q5A0M4; -.
DR   SMR; Q5A0M4; -.
DR   BioGRID; 1226092; 3.
DR   STRING; 237561.Q5A0M4; -.
DR   MoonProt; Q5A0M4; -.
DR   EnsemblFungi; C2_03100W_A-T; C2_03100W_A-T-p1; C2_03100W_A.
DR   GeneID; 3642998; -.
DR   KEGG; cal:CAALFM_C203100WA; -.
DR   CGD; CAL0000189676; EFT2.
DR   VEuPathDB; FungiDB:C2_03100W_A; -.
DR   eggNOG; KOG0469; Eukaryota.
DR   HOGENOM; CLU_002794_11_2_1; -.
DR   InParanoid; Q5A0M4; -.
DR   OMA; NRHNRFY; -.
DR   OrthoDB; 166721at2759; -.
DR   PRO; PR:Q5A0M4; -.
DR   Proteomes; UP000000559; Chromosome 2.
DR   GO; GO:0009986; C:cell surface; IDA:CGD.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IDA:CGD.
DR   GO; GO:0005886; C:plasma membrane; IDA:CGD.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR   GO; GO:0030445; C:yeast-form cell wall; IDA:CGD.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IDA:CGD.
DR   GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR   GO; GO:0003746; F:translation elongation factor activity; IMP:CGD.
DR   GO; GO:0006414; P:translational elongation; IBA:GO_Central.
DR   CDD; cd01681; aeEF2_snRNP_like_IV; 1.
DR   CDD; cd04096; eEF2_snRNP_like_C; 1.
DR   CDD; cd01885; EF2; 1.
DR   CDD; cd16261; EF2_snRNP_III; 1.
DR   CDD; cd03700; EF2_snRNP_like_II; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.70.240; -; 1.
DR   Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 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_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_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   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR42908:SF10; ELONGATION FACTOR 2; 1.
DR   PANTHER; PTHR42908; TRANSLATION ELONGATION FACTOR-RELATED; 1.
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; SSF54980; EF-G C-terminal domain-like; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Elongation factor; GTP-binding;
KW   Hydrolase; Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..842
FT                   /note="Elongation factor 2"
FT                   /id="PRO_0000091015"
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|UniProtKB:P32324"
FT   BINDING         158..161
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P32324"
FT   BINDING         213..215
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P32324"
FT   MOD_RES         699
FT                   /note="Diphthamide"
FT                   /evidence="ECO:0000250|UniProtKB:P32324"
SQ   SEQUENCE   842 AA;  93354 MW;  5C8C740109A23189 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 HLPSPVTAQA 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
//