ID   EF2_SCHPO               Reviewed;         842 AA.
AC   O14460; Q9USG7; Q9USZ9; Q9UT64;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2001, sequence version 2.
DT   10-AUG-2010, entry version 84.
DE   RecName: Full=Elongation factor 2;
DE            Short=EF-2;
GN   Name=eft1; ORFNames=SPCP31B10.07;
GN   and
GN   Name=eft2; ORFNames=SPAC513.01c, SPAPYUK71.04c;
OS   Schizosaccharomyces pombe (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=4896;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=JY333;
RX   MEDLINE=97254480; PubMed=9099890; DOI=10.1016/S0378-1119(96)00764-0;
RA   Mita K., Morimyo M., Ito K., Sugaya K., Ebihara K., Hongo E.,
RA   Higashi T., 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] (EFT1 AND EFT2).
RC   STRAIN=ATCC 38366 / 972;
RX   MEDLINE=21848401; 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.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-568 AND THR-574, AND
RP   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: This protein promotes the GTP-dependent translocation of
CC       the nascent protein chain from the A-site to the P-site of the
CC       ribosome (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the GTP-binding elongation factor family.
CC       EF-G/EF-2 subfamily.
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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   PIR; T41697; T41697.
DR   RefSeq; NP_587863.1; -.
DR   RefSeq; XP_001713073.1; -.
DR   ProteinModelPortal; O14460; -.
DR   SMR; O14460; 1-842.
DR   MINT; MINT-4672831; -.
DR   STRING; O14460; -.
DR   EnsemblFungi; SPAC513.01c-1; SPAC513.01c-1; SPAC513.01c.
DR   EnsemblFungi; SPCP31B10.07-1; SPCP31B10.07-1; SPCP31B10.07.
DR   GeneID; 2539544; -.
DR   GeneID; 3361483; -.
DR   GenomeReviews; CU329670_GR; eft2.
DR   GenomeReviews; CU329672_GR; eft2.
DR   KEGG; spo:SPAC513.01c; -.
DR   KEGG; spo:SPCP31B10.07; -.
DR   GeneDB_Spombe; SPAC513.01c; -.
DR   GeneDB_Spombe; SPCP31B10.07; -.
DR   eggNOG; fuNOG07681; -.
DR   HOGENOM; HBG737692; -.
DR   OMA; GIQYLNE; -.
DR   OrthoDB; EOG9C898X; -.
DR   PhylomeDB; O14460; -.
DR   BioCyc; SPOM-XXX-01:SPOM-XXX-01-001929-MONOMER; -.
DR   BioCyc; SPOM-XXX-01:SPOM-XXX-01-002211-MONOMER; -.
DR   ArrayExpress; O14460; -.
DR   GO; GO:0005829; C:cytosol; IDA:GeneDB_Spombe.
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; TAS:GeneDB_Spombe.
DR   InterPro; IPR009022; Elongation_fac_G/III/V.
DR   InterPro; IPR000795; ProtSyn_GTP-bd.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   InterPro; IPR000640; Transl_elong_EFG/EF2_C.
DR   InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR   InterPro; IPR004161; Transl_elong_EFTu/EF1A_2.
DR   InterPro; IPR009000; Transl_elong_init/rib_B-barrel.
DR   Gene3D; G3DSA:3.30.230.10; Ribosomal_S5_D2-type_fold; 2.
DR   Pfam; PF00679; EFG_C; 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; EFG_III_V; 2.
DR   SUPFAM; SSF54211; Ribosomal_S5_D2-typ_fold; 1.
DR   SUPFAM; SSF50447; Translat_factor; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS00301; EFACTOR_GTP; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Cytoplasm; Elongation factor; GTP-binding;
KW   Nucleotide-binding; Phosphoprotein; Protein biosynthesis.
FT   CHAIN         1    842       Elongation factor 2.
FT                                /FTId=PRO_0000091023.
FT   NP_BIND      26     33       GTP (By similarity).
FT   NP_BIND     104    108       GTP (By similarity).
FT   NP_BIND     158    161       GTP (By similarity).
FT   MOD_RES     568    568       Phosphoserine; by MAPK sty1.
FT   MOD_RES     574    574       Phosphothreonine.
FT   MOD_RES     699    699       Diphthamide (By similarity).
FT   CONFLICT    821    823       EAR -> DVG (in Ref. 1; BAA23591/
FT                                BAA23590).
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
//
