ID A7E7R3_SCLS1 Unreviewed; 790 AA.
AC A7E7R3;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=Elongation factor 2 {ECO:0000256|ARBA:ARBA00017891};
GN ORFNames=SS1G_01341 {ECO:0000313|EMBL:EDN96415.1};
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079 {ECO:0000313|EMBL:EDN96415.1, ECO:0000313|Proteomes:UP000001312};
RN [1] {ECO:0000313|Proteomes:UP000001312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000001312};
RX PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH476622; EDN96415.1; -; Genomic_DNA.
DR RefSeq; XP_001597147.1; XM_001597097.1.
DR AlphaFoldDB; A7E7R3; -.
DR SMR; A7E7R3; -.
DR STRING; 665079.A7E7R3; -.
DR EnsemblFungi; EDN96415; EDN96415; SS1G_01341.
DR GeneID; 5494072; -.
DR KEGG; ssl:SS1G_01341; -.
DR eggNOG; KOG0469; Eukaryota.
DR HOGENOM; CLU_002794_11_2_1; -.
DR InParanoid; A7E7R3; -.
DR OMA; NRHNRFY; -.
DR OrthoDB; 166721at2759; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
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 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 Gene3D; 3.30.230.10; -; 2.
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 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; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SMART; SM00838; EFG_C; 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 4: Predicted;
KW Elongation factor {ECO:0000313|EMBL:EDN96415.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000001312}.
FT DOMAIN 17..255
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 790 AA; 87432 MW; 51DD314E57E4E1CC CRC64;
MVNFTVEEVR QLMDKATNVR NMSVIAHVDH GKSTLTDSLL SKAGIISAAK AGDARATDTR
ADEQERGITI KSTAISLYGN LPDDDDLKDI VGQKTDGRDF LINLIDSPGH VDFSSEVTAA
LRVTDGALVV VDTIEGVCVQ TETVLRQALG ERIKPVVIIN KVDRALLELQ VSKEDLYQSF
SRTIESVNVV ISTYFDKTLG DVQVYPGKGT VAFGSGLHGW AFTIRQFAQR YAKKFGVDRN
KMMERLWGDN YFNPYTKKWT TKSSHEGKEL ERAFNQFILD PIFRIFAAVM NFKKDEIPTL
LEKLNIKLSP DDKDKEGKAL LKVIMRTFLP AADALLEMLI LHLPSPVTAQ KYRAETLYEG
PPDDEACIGI RDCDPKAPLM LYVSKMVPTS DKGRFYAFGR VFAGTVRSGL KVRIQGPNYT
PGKKDDLFIK AIQRVVLMMG GKVDPIDDVP AGNILGLVGI DQFLLKSGTL TTSDTAHNLK
VMKFSVSPVV QRSVEVKNAQ DLPKLVEGLK RLSKSDPCVL TFISESGEHV VAGAGELHLE
ICLKDLEEDH AGVPLRISDP VVPYRETVTG KSSMTALSKS PNKHNRLYMI AEPLDEEVSK
EIEAGKIGPR DDFKARARIL ADEHGWDVTR CPFNIMDVTL HADAIHRGSG QVMPTTRRVL
YASTLLAEPG LLEPVFLVEI QVPESAMGGV YGVLTRRRGH VFAEEQRPGT PLFTIKAYLP
VGESFGFNAD LRSHTSGQAF PQSIFDHWQI LPGGSPIDAT SKTGQIVQEL RKRKGLKIEV
PGYENYYDKL
//
