EF2_NEUCR
ID EF2_NEUCR Reviewed; 844 AA.
AC Q96X45; Q7RVG5;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 3.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Elongation factor 2;
DE Short=EF-2;
DE AltName: Full=Colonial temperature-sensitive 3;
GN Name=cot-3; ORFNames=NCU07700;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11254137; DOI=10.1007/s004380000379;
RA Propheta O., Vierula J., Toporowski P., Gorovits R., Yarden O.;
RT "The Neurospora crassa colonial temperature-sensitive 3 (cot-3) gene
RT encodes protein elongation factor 2.";
RL Mol. Gen. Genet. 264:894-901(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(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; AF258620; AAK49353.1; -; Genomic_DNA.
DR EMBL; CM002239; EAA33050.2; -; Genomic_DNA.
DR RefSeq; XP_962286.2; XM_957193.3.
DR AlphaFoldDB; Q96X45; -.
DR SMR; Q96X45; -.
DR STRING; 5141.EFNCRP00000007996; -.
DR PRIDE; Q96X45; -.
DR EnsemblFungi; EAA33050; EAA33050; NCU07700.
DR GeneID; 3878434; -.
DR KEGG; ncr:NCU07700; -.
DR VEuPathDB; FungiDB:NCU07700; -.
DR HOGENOM; CLU_002794_11_2_1; -.
DR InParanoid; Q96X45; -.
DR OMA; GVMTQTE; -.
DR Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
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; IBA:GO_Central.
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 3: Inferred from homology;
KW Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW Phosphoprotein; Protein biosynthesis; Reference proteome.
FT CHAIN 1..844
FT /note="Elongation factor 2"
FT /id="PRO_0000091019"
FT DOMAIN 17..255
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 106..110
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 160..163
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 57
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 59
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 700
FT /note="Diphthamide"
FT /evidence="ECO:0000250"
FT VARIANT 278
FT /note="I -> N (in cot-3 mutation; abnormal hypha
FT elongation)"
FT CONFLICT 154
FT /note="K -> E (in Ref. 1; AAK49353)"
FT /evidence="ECO:0000305"
FT CONFLICT 397
FT /note="A -> G (in Ref. 1; AAK49353)"
FT /evidence="ECO:0000305"
FT CONFLICT 419
FT /note="Y -> H (in Ref. 1; AAK49353)"
FT /evidence="ECO:0000305"
FT CONFLICT 424
FT /note="K -> M (in Ref. 1; AAK49353)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 844 AA; 93262 MW; 525D8F0D16D37D03 CRC64;
MVNFTIDEIR ALMDKPTNVR NMSVIAHVDH GKSTLTDSLL AKAGIISSGK AGEARATDTR
ADEQERGITI KSTAISLYGT LPDEEDIKDI VGQKTDGKDF LINLIDSPGH VDFSSEVTAA
LRVTDGALVV VDTVEGVCVQ TETVLRQALG ERIKPVVVIN KVDRALLELQ VSKEDLYQSF
SRTIESVNVI ISTYFDKSLG DVQVYPDRGT VAFGSGLHGW AFTIRQFATR YAKKFGVDRN
KMMERLWGDN YFNPKTKKWT KNGTYEGKEL ERAFNQFILD PIFKIFSAVM NFKKDEVAAL
LEKLNLKLAT DDREKEGKQL LKAVMKAFLP AADCLLEMMI LHLPSPVTAQ AYRAETLYEG
PQDDEAAMAI KTCDPKGPLM LYVSKMVPTS DKGRFYAFGR VFAGTVRSGL KVRIQGPNYT
PGKKEDLFIK AIQRTVLMMG GKVEPIDDMP AGNIVGLVGI DQFLLKSGTL TTSETAHNMK
VMKFSVSPVV QRSVQVKNAQ DLPKLVEGLK RLSKSDPCVL TFSNESGEHV VAGAGELHLE
ICLNDLENDH AGVPLTISDP VVQYRETVAG KSSMTALSKS PNKHNRLYMV AEPLEEDLCL
AIEAGKITPR DDFKARARIL ADDFGWDVTD ARKIWAFGPD TNGANLLVDQ TKAVQYLNEI
KDSVVSGFQW ATREGPIGEE PMRSIRFNIL DVTLHADAIH RGGGQIIPTA RRVLYAATLL
AEPSLLEPVF LVEIQVPEQA MGGVYGVLTR RRGHVFGEEQ RPGTPLFTIK AYLPVMESFG
FNGDLRAATS GQAFPQSVFD HWERLPGGSP LDSTSKVGQI VQEMRKRKGL KVEVPGYENY
YDKL
