EF2_ENCCU
ID EF2_ENCCU Reviewed; 850 AA.
AC Q8SQT7;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Elongation factor 2;
DE Short=EF-2;
DE AltName: Full=Eukaryotic elongation factor 2;
DE Short=eEF2;
DE AltName: Full=Ribosomal translocase;
DE AltName: Full=Translation elongation factor 2;
GN Name=EFT1; OrderedLocusNames=ECU11_1460;
OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=284813;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11719806; DOI=10.1038/35106579;
RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA Vivares C.P.;
RT "Genome sequence and gene compaction of the eukaryote parasite
RT Encephalitozoon cuniculi.";
RL Nature 414:450-453(2001).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND
RP DEVELOPMENTAL STAGE.
RX PubMed=16691553; DOI=10.1002/pmic.200500796;
RA Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.;
RT "Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi
RT (microsporidia): a reference map for proteins expressed in late sporogonial
RT stages.";
RL Proteomics 6:3625-3635(2006).
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 -!- DEVELOPMENTAL STAGE: Expressed in late sporogonial stages.
CC {ECO:0000269|PubMed:16691553}.
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; AL590450; CAD26056.1; -; Genomic_DNA.
DR RefSeq; NP_586452.1; NM_001042285.1.
DR AlphaFoldDB; Q8SQT7; -.
DR SMR; Q8SQT7; -.
DR STRING; 284813.Q8SQT7; -.
DR PRIDE; Q8SQT7; -.
DR GeneID; 860106; -.
DR KEGG; ecu:ECU11_1460; -.
DR VEuPathDB; MicrosporidiaDB:ECU11_1460; -.
DR HOGENOM; CLU_002794_11_2_1; -.
DR InParanoid; Q8SQT7; -.
DR OMA; GVMTQTE; -.
DR OrthoDB; 140796at2759; -.
DR UniPathway; UPA00345; -.
DR Proteomes; UP000000819; Chromosome XI.
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:0019843; F:rRNA binding; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome; RNA-binding; rRNA-binding.
FT CHAIN 1..850
FT /note="Elongation factor 2"
FT /id="PRO_0000383140"
FT DOMAIN 17..351
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 105..109
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 159..162
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 850 AA; 94474 MW; 4ABC406CDCA4B289 CRC64;
MADFHISKVH ELMMNQKNIR NISVIAHVDH GKSTLTDCLV IKAKIVSKDS GGGRYMDSRE
DEQQRGITIK SSAISLHFQV QKDVLEAYTK EGDTNGTEFL INLIDSPGHV DFSSEVTAAL
RVTDGALVVV DCVDGICVQT ETVLGQAMNE RIIPTLVLNK LDRAILELEY PQEKLGEVLR
RRVEGFNAKL STLGYNFKVE SLLPEKNEIS FCSGLQGWGF TLRQFARFYL EKFNMNGFEG
ERKLTNFLWS HKVSCTSDDP FDASIKHIAK PNPARSPFVV YVLNPIYKVK ELCNNGKVEE
IKEYLKFYKV DFKGVVLTGS GKSLFKEVMK TWLPAADCIL EQIALKLPSP LQSQKLRYDY
LYEGPADDEV ANAIKMCDGS DEAPVSMYVS KMIPSNDNRF IAFGRVFSGK IFPGMKIRVQ
EPGYSPGSEE LSNTSLIHNK SVLRTVVMMG RGYKDVPNCP AGNIIGIIGI DDCLKKTGTI
TNREAAHNIR SMKFSVSPVV KVAVSAKRPE DLGKLQEGLN KLAQSDPLCV VERNDKGQNT
IACAGSLHLE ICLKDLQDQY AKVPIIADDP LVTYFEGISC AVSDSKMTKS ANKHNRIYMT
VEPLDQNIVD NLKDVKSDQA KTMATNFREK LDIRDDWIRK IWCYAPEVNP LNLLVDGTKG
ISIINEIKEH VNTGFRAAVN DGPLIGEVMR GLKFELKDAV LHADAIHRGI NQLLQPVKNL
CKGLLLAAGP ILYEPIYEVE ITTPNDYSGA VTTILLSKRG TAEDFKTLPG NDTTMITGTL
PVKESFTFNE DLKSGSRGKA GASMRFSHYS ILPGNLEDPN SLMFKTVEAV RKLKKMNPAP
PTPDSFFDRL
