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Database: UniProt
Entry: A0A3R7J5P6_9STRA
LinkDB: A0A3R7J5P6_9STRA
Original site: A0A3R7J5P6_9STRA 
ID   A0A3R7J5P6_9STRA        Unreviewed;      1051 AA.
AC   A0A3R7J5P6;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Elongation factor 2 {ECO:0000256|ARBA:ARBA00017891};
GN   ORFNames=BBI17_009142 {ECO:0000313|EMBL:RLN06496.1}, BBO99_00009130
GN   {ECO:0000313|EMBL:RLN74024.1}, JM16_008988
GN   {ECO:0000313|EMBL:KAG2507364.1}, JM18_009028
GN   {ECO:0000313|EMBL:KAG2509912.1};
OS   Phytophthora kernoviae.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=325452 {ECO:0000313|EMBL:RLN06496.1, ECO:0000313|Proteomes:UP000285883};
RN   [1] {ECO:0000313|EMBL:KAG2507364.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NZFS 2646 {ECO:0000313|EMBL:KAG2507364.1}, and NZFS 3630
RC   {ECO:0000313|EMBL:KAG2509912.1};
RX   PubMed=26981359;
RA   Studholme D.J., McDougal R.L., Sambles C., Hansen E., Hardy G., Grant M.,
RA   Ganley R.J., Williams N.M.;
RT   "Genome sequences of six Phytophthora species associated with forests in
RT   New Zealand.";
RL   Genom Data 7:54-56(2015).
RN   [2] {ECO:0000313|Proteomes:UP000285624, ECO:0000313|Proteomes:UP000285883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Chile2 {ECO:0000313|EMBL:RLN06496.1}, and Chile4
RC   {ECO:0000313|EMBL:RLN74024.1};
RA   Studholme D.J., Sanfuentes E., Panda P., Hill R., Sambles C., Grant M.,
RA   Williams N.M., Mcdougal R.L.;
RT   "Genome sequencing of oomycete isolates from Chile give support for New
RT   Zealand origin for Phytophthora kernoviae and make available the first
RT   Nothophytophthora sp. genome.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:KAG2507364.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NZFS 2646 {ECO:0000313|EMBL:KAG2507364.1}, and NZFS 3630
RC   {ECO:0000313|EMBL:KAG2509912.1};
RA   Studholme D.J.;
RL   Submitted (JUN-2020) to the EMBL/GenBank/DDBJ databases.
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.
CC       {ECO:0000256|ARBA:ARBA00024731}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RLN06496.1}.
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DR   EMBL; JPWV03000615; KAG2507364.1; -; Genomic_DNA.
DR   EMBL; JPWU03000635; KAG2509912.1; -; Genomic_DNA.
DR   EMBL; MAYM02001953; RLN06496.1; -; Genomic_DNA.
DR   EMBL; MBDN02000624; RLN74024.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3R7J5P6; -.
DR   STRING; 325452.A0A3R7J5P6; -.
DR   Proteomes; UP000285624; Unassembled WGS sequence.
DR   Proteomes; UP000285883; Unassembled WGS sequence.
DR   Proteomes; UP000785171; Unassembled WGS sequence.
DR   Proteomes; UP000792063; Unassembled WGS sequence.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   CDD; cd01681; aeEF2_snRNP_like_IV; 1.
DR   CDD; cd04096; eEF2_snRNP_like_C; 1.
DR   CDD; cd01885; EF2; 1.
DR   CDD; cd16268; EF2_II; 1.
DR   CDD; cd16261; EF2_snRNP_III; 1.
DR   Gene3D; 3.30.230.10; -; 1.
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   Gene3D; 3.90.1430.10; Yeast translation eEF2 (G' domain); 1.
DR   InterPro; IPR041095; EFG_II.
DR   InterPro; IPR035647; EFG_III/V.
DR   InterPro; IPR000640; EFG_V-like.
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   InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR42908:SF3; ELONGATION FACTOR-LIKE GTPASE 1; 1.
DR   PANTHER; PTHR42908; TRANSLATION ELONGATION FACTOR-RELATED; 1.
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   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; PS51722; G_TR_2; 1.
PE   4: Predicted;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000285624}.
FT   DOMAIN          18..280
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   1051 AA;  116973 MW;  A3DB81BDE4438F39 CRC64;
     MATRATPELL GSLQHAPERI RNICILAHVD HGKTTLSDSL VSSNGIISER LAGKVRYLDN
     TEEEQIRGIT MKSSAISLVY QPEPITDKES EAPYLINLVD SPGHVDFSFD VSTAVRLCDG
     ALVLIDAVEG VCAQTHAVIR QAWKEGIRPC LVINKMDRLI FELQFSPMEA YQRLNRILEQ
     ANAVLSSMIR MDVLEKYDQE DTSEEKKEVE ESVDGDEVST DKIEITLDDE AISKVTEQLE
     NEMLFSPANG NVIFASATDG WAFGIGYFAS LYAKKLELPV RVMRQALWGE YYYNGKTKKI
     VTKPPTSNSQ TMFCSFILDL VWSAYTTLTK PVGSDADLES LRKLTRQLRV ARLVTDRELK
     QSDRKNAIQA VMRKWLPLST TVLKMVTRVL PSPVTAQVKR AEKLCTISSE QLDKSPQHAR
     VFRSLQACET SEEAPLVIYI CKVISVEANV LSDYHQAGLA ANDEVYVGVG RVYSGVLRAG
     QPLYVLDPKF QGISGEVDVD TVDPSTVKHI TRIDNGLIKT YMIMGRDLLK LDRVPAGNIV
     GIVGLQEHVL KTATLSSTLA CPSLTKMPYQ AKPIVRVAVE PEDPRNFGAL EAGLQRLYRS
     DPTVEVHVQE TGEHVIVALG ELHLERCIKD LKDRFAKVAV QVSEPLVGFR ESIVDGTISS
     FQENIVFKDL LTPDVPKEDQ IDKEASASTD ADPKVALGTT PDGSLTLKLR ALPLPLETAQ
     LLEESAVLLK RIVHSKKTTG DEINIKELVV DAGAEEISAF KKKLEKSLQK SENSFLKTLP
     LDKIWSCGPR RVGPNILINN IPDYCASGRL FPSDSTTEIS VSNSEKAGAI KKMENSIVTG
     FQMTSSAGPL CDEPVWGVAF IIEDVTFHEK ESEENKEEEQ AEVSKYGPLS GQVISIMRTT
     CLMSFVKQSV RLVEAVYECT VQCQAEQLGK LYSVISKRRG DIYSEELSDG TALFTVKAHL
     PVVESFGFAT DLLIQTSGAA SNPQLIFSHW SIIDMDPFFQ PQTEEEREDY GERVYEHNYV
     RRYIEAVRKR KGLSRDEKIV VHAEKQRTLK R
//
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