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Database: UniProt
Entry: Q6JU94_9INSE
LinkDB: Q6JU94_9INSE
Original site: Q6JU94_9INSE 
ID   Q6JU94_9INSE            Unreviewed;       726 AA.
AC   Q6JU94;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   SubName: Full=Elongation factor-2 {ECO:0000313|EMBL:AAR01306.1};
DE   Flags: Fragment;
OS   Nicoletia phytophila.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Zygentoma;
OC   Nicoletiidae; Nicoletia.
OX   NCBI_TaxID=1350298 {ECO:0000313|EMBL:AAR01306.1};
RN   [1] {ECO:0000313|EMBL:AAR01306.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Regier J.C.;
RT   "Elongation factor-2 sequences from Panarthropoda.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC         Evidence={ECO:0000256|ARBA:ARBA00001702};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC         Evidence={ECO:0000256|ARBA:ARBA00001702};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR   EMBL; AY305514; AAR01306.1; -; mRNA.
DR   AlphaFoldDB; Q6JU94; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-KW.
DR   CDD; cd01681; aeEF2_snRNP_like_IV; 1.
DR   CDD; cd01885; EF2; 1.
DR   CDD; cd16261; EF2_snRNP_III; 1.
DR   CDD; cd03700; EF2_snRNP_like_II; 1.
DR   Gene3D; 3.30.230.10; -; 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; 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   InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR42908:SF10; ELONGATION FACTOR 2; 1.
DR   PANTHER; PTHR42908; TRANSLATION ELONGATION FACTOR-RELATED; 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; SM00889; EFG_IV; 1.
DR   SUPFAM; SSF54980; EF-G C-terminal domain-like; 1.
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   2: Evidence at transcript level;
KW   Elongation factor {ECO:0000313|EMBL:AAR01306.1};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000313|EMBL:AAR01306.1}.
FT   DOMAIN          10..341
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAR01306.1"
FT   NON_TER         726
FT                   /evidence="ECO:0000313|EMBL:AAR01306.1"
SQ   SEQUENCE   726 AA;  81605 MW;  84DFD874B2F44A5E CRC64;
     EIRAMMDKKR NIRNMSVIAH VDHGKSTLTD SLVSKAGIIA SAKAGETRFT DTRKDEQERC
     ITIKSTAISM YFELEDKDLA FITNVDQREK GEKGFLINLI DSPGHVDFSS EVTAALRVTD
     GALVVVDCVS GVCVQTETVL RQAIAERIKP VLFMNKMDRA LLELQLEQEE LYQTFQRIVE
     NVNVIIATYS DDTGPMGEVR VDPSKGSVGF GSGLHSWAFT LKQFSEMYAE KFKIDVIKLM
     NRLWGESFFN PKTKKWAKQK EDDNRRSFCM YILDPIYKVF DAIMNYQKEE TALLLQKLNI
     ELKPDDRDKD GKALLKVVMR TWLPAGEALL QMIAIHLPSP VVAQKYRMEM LYEGPHDDEA
     AIGIKNCDPN APLMMYVSKM VPTSDKGRFY AFGRVFSGKV ATGQKARIMG PNYMPGKKED
     LYEKAIQRTI LMMGRYVEAI EDVPSGNTCG LVGVDQFLVK TGTITTFKDA HNMRVMKFSV
     SPVVRVAVEP KSPADLPKLV EGLKRLAKSD PMVQCIIEES GEHIIAGAGE LHLEICLKDL
     EEDHACIPIK KSEPVVSYRE TVSEESDQMC LSKSPNKHNR LFMKAVPMPD GLAEDIDKGD
     VNPRDDFKVR ARYLCDKYDY DITEARKIWC FGPDGTGPNI LIDCTKGVQY LNEIKDSVVA
     GFQWATKEGV LAEENMRGVR FNIYDVTLHA DAIHRGGGQI IPTTRRCLYA CALTAAPRLM
     EPVYLC
//
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