ID EF2_LACK1 Reviewed; 842 AA.
AC Q875S0;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=Elongation factor 2;
DE Short=EF-2;
GN Name=EFT2;
OS Lachancea kluyveri (strain ATCC 58438 / CBS 3082 / BCRC 21498 / NBRC 1685 /
OS JCM 7257 / NCYC 543 / NRRL Y-12651) (Yeast) (Saccharomyces kluyveri).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=226302;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 58438 / CBS 3082 / BCRC 21498 / NBRC 1685 / JCM 7257 / NCYC 543
RC / NRRL Y-12651;
RX PubMed=12594514; DOI=10.1038/nature01419;
RA Langkjaer R.B., Cliften P.F., Johnston M., Piskur J.;
RT "Yeast genome duplication was followed by asynchronous differentiation of
RT duplicated genes.";
RL Nature 421:848-852(2003).
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; AY144999; AAO32562.1; -; Genomic_DNA.
DR AlphaFoldDB; Q875S0; -.
DR SMR; Q875S0; -.
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 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 3: Inferred from homology;
KW Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW Protein biosynthesis.
FT CHAIN 1..842
FT /note="Elongation factor 2"
FT /id="PRO_0000091022"
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; 93362 MW; 3EC66C0511A19CDB CRC64;
MVAFTVDQIR SLMDKVTNIR NMSVIAHVDH GKSTLTDSLV QRAGIISAAK AGEARFTDTR
KDEQERGITI KSTAISLFSE MSDDDVKDIK QKTEGNSFLI NLIDSPGHVD FSSEVTAALR
VTDGALVVVD TVEGVCVQTE TVLRQALGER IKPVVCVNKV DRALLELQVS KEDLYQSFAR
TVESVNVIIS TYADEVLGDV QVYPSKGTIA FGSGLHGWAF TIRQFANRYS KKFGVDREKM
MERLWGDSYF NPKTKKWTNK ETDTDGKPLE RAFNMFVLDP IFRLFSAIMN FKKDEIPVLL
EKLEINLKGE EKELEGKALL KIVMRKFLPA ADALLEMIIM HLPSPVTAQN YRAEQLYEGP
SDDPACIAIK NCDPKADLML YVSKMVPTSD KGRFYAFGRV FAGTVKSGQK VRIQGPNYIP
GKKDDLFIKA VQRAVLMMGR FVEPIDDCPA GNIVGLVGVD QFLLKTGTLT TFEGAHNMKV
MKFSVSPVVQ VAVEVKNAND LPKLVEGLKR LSKSDPCVLT YMSESGEHIV AGTGELHLEI
CLQDLENDHA GIPLKISPPV VAYRETVEGE SSQVALSKSP NKHNRIYLKA EPIDEEVSLA
IEAGKINPRD DFKARARVMA DDFGWDVTDA RKIWCFGPDG NGPNLVVDQT KAVQYLNEIK
DSVVAAFQWA SKEGPIFGEQ MRSVRVNILD VTLHADAIHR GGGQIIPTMR RATYAGFLLA
EPKIQEPVFL VEIQCPEQAV GGIYSVLNRK RGQVVSEEQR PGTPLFTVKA YLPVNESFGF
TGELRQATGG QAFPQMVFDH WATLGTDPLD PTTKAGEIVT AARKRHGMKE EVPGWQEYYD
KL
//
