EF2_SCHPO
ID EF2_SCHPO Reviewed; 842 AA.
AC O14460; P78802; Q9USG7; Q9USZ9; Q9UT64;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Elongation factor 2;
DE Short=EF-2;
GN Name=eft201; Synonyms=eft2, eft2-1; ORFNames=SPAC513.01c, SPAPYUK71.04c;
GN and
GN Name=eft202; ORFNames=SPCP31B10.07;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (EFT201 AND EFT202).
RC STRAIN=JY333;
RX PubMed=9099890; DOI=10.1016/s0378-1119(96)00764-0;
RA Mita K., Morimyo M., Ito K., Sugaya K., Ebihara K., Hongo E., Higashi T.,
RA Hirayama Y., Nakamura Y.;
RT "Comprehensive cloning of Schizosaccharomyces pombe genes encoding
RT translation elongation factors.";
RL Gene 187:259-266(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (EFT201 AND EFT202).
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 177-842 (EFT202).
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-568 AND THR-574, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA13813.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D83976; BAA23591.1; -; Genomic_DNA.
DR EMBL; D83975; BAA23590.1; -; Genomic_DNA.
DR EMBL; CU329672; CAB58373.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB52147.1; -; Genomic_DNA.
DR EMBL; D89151; BAA13813.1; ALT_FRAME; mRNA.
DR PIR; T41697; T41697.
DR RefSeq; NP_587863.1; NM_001022856.2.
DR RefSeq; XP_001713073.1; XM_001713021.2.
DR AlphaFoldDB; O14460; -.
DR SMR; O14460; -.
DR BioGRID; 276105; 6.
DR BioGRID; 280559; 15.
DR DIP; DIP-57891N; -.
DR IntAct; O14460; 2.
DR MINT; O14460; -.
DR STRING; 4896.SPAC513.01c.1; -.
DR iPTMnet; O14460; -.
DR MaxQB; O14460; -.
DR PaxDb; O14460; -.
DR PRIDE; O14460; -.
DR EnsemblFungi; SPAC513.01c.1; SPAC513.01c.1:pep; SPAC513.01c.
DR EnsemblFungi; SPCP31B10.07.1; SPCP31B10.07.1:pep; SPCP31B10.07.
DR GeneID; 2539544; -.
DR KEGG; spo:SPCP31B10.07; -.
DR PomBase; SPAC513.01c; eft201.
DR PomBase; SPCP31B10.07; eft202.
DR VEuPathDB; FungiDB:SPAC513.01c; -.
DR VEuPathDB; FungiDB:SPCP31B10.07; -.
DR eggNOG; KOG0469; Eukaryota.
DR HOGENOM; CLU_002794_11_1_1; -.
DR InParanoid; O14460; -.
DR OMA; GVMTQTE; -.
DR PhylomeDB; O14460; -.
DR Reactome; R-SPO-156902; Peptide chain elongation.
DR Reactome; R-SPO-5358493; Synthesis of diphthamide-EEF2.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR PRO; PR:O14460; -.
DR Proteomes; UP000002485; Chromosome I.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; ISM:PomBase.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR GO; GO:0003746; F:translation elongation factor activity; ISO:PomBase.
DR GO; GO:0002182; P:cytoplasmic translational elongation; ISO:PomBase.
DR GO; GO:0006414; P:translational elongation; IBA:GO_Central.
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 Phosphoprotein; Protein biosynthesis; Reference proteome.
FT CHAIN 1..842
FT /note="Elongation factor 2"
FT /id="PRO_0000091023"
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 568
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 574
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 699
FT /note="Diphthamide"
FT /evidence="ECO:0000250"
FT CONFLICT 323
FT /note="V -> D (in Ref. 3; BAA13813)"
FT /evidence="ECO:0000305"
FT CONFLICT 464
FT /note="V -> A (in Ref. 3; BAA13813)"
FT /evidence="ECO:0000305"
FT CONFLICT 821..823
FT /note="EAR -> DVG (in Ref. 1; BAA23591/BAA23590)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 842 AA; 93231 MW; A544C5C454BC55C7 CRC64;
MVAFTPEEVR NLMGKPSNVR NMSVIAHVDH GKSTLTDSLV QKAGIISAAK AGDARFMDTR
ADEQERGVTI KSTAISLFAE MTDDDMKDMK EPADGTDFLV NLIDSPGHVD FSSEVTAALR
VTDGALVVVD TIEGVCVQTE TVLRQALGER IRPVVVVNKV DRALLELQIS QEELYQNFAR
VVESVNVVIS TYYDKVLGDC QVFPDKGTVA FASGLHGWAF TVRQFANRYA KKFGIDRNKM
MQRLWGENYF NPKTKKWSKS ATDANGNSNQ RAFNMFILDP IYRIFDAVMN SRKDEVFTLL
SKLEVTIKPD EKELEGKALL KVVMRKFLPA ADALMEMIVL HLPSPKTAQQ YRAETLYEGP
MDDECAVGIR NCDANAPLMI YVSKMVPTSD RGRFYAFGRV FSGTVRSGLK VRIQGPNYVP
GKKDDLFIKA IQRTVLMMGS RIEPIEDCPA GNIIGLVGVD QFLVKSGTLT TSEVAHNMKV
MKFSVSPVVQ VAVEVKNGND LPKLVEGLKR LSKSDPCVLC TTSESGEHIV AGAGELHLEI
CLKDLQEDHA GIPLKISPPV VSYRESVSEP SSMTALSKSP NKHNRIFMTA EPMSEELSVA
IETGHVNPRD DFKVRARIMA DEFGWDVTDA RKIWCFGPDT TGANVVVDQT KAVAYLNEIK
DSVVAAFAWA SKEGPMFEEN LRSCRFNILD VVLHADAIHR GGGQIIPTAR RVVYASTLLA
SPIIQEPVFL VEIQVSENAM GGIYSVLNKK RGHVFSEEQR VGTPLYNIKA YLPVNESFGF
TGELRQATAG QAFPQLVFDH WSPMSGDPLD PTSKPGQIVC EARKRKGLKE NVPDYTEYYD
RL
