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
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