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Database: UniProt
Entry: Q6JSR1_9MYRI
LinkDB: Q6JSR1_9MYRI
Original site: Q6JSR1_9MYRI 
ID   Q6JSR1_9MYRI            Unreviewed;       728 AA.
AC   Q6JSR1;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   SubName: Full=Elongation factor 2 {ECO:0000313|EMBL:AAQ77161.1};
DE   Flags: Fragment;
OS   Geophilus vittatus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Myriapoda; Chilopoda;
OC   Pleurostigmophora; Geophilomorpha; Geophilidae; Geophilus.
OX   NCBI_TaxID=118466 {ECO:0000313|EMBL:AAQ77161.1};
RN   [1] {ECO:0000313|EMBL:AAQ77161.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=15579388; DOI=10.1016/j.ympev.2004.09.005;
RA   Regier J.C., Wilson H.M., Shultz J.W.;
RT   "Phylogenetic analysis of Myriapoda using three nuclear protein-coding
RT   genes.";
RL   Mol. Phylogenet. Evol. 34:147-158(2005).
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; AY310259; AAQ77161.1; -; mRNA.
DR   AlphaFoldDB; Q6JSR1; -.
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:AAQ77161.1};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000313|EMBL:AAQ77161.1}.
FT   DOMAIN          10..343
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAQ77161.1"
FT   NON_TER         728
FT                   /evidence="ECO:0000313|EMBL:AAQ77161.1"
SQ   SEQUENCE   728 AA;  81604 MW;  E113700E0B4B3524 CRC64;
     EIRGLMDRKR NIRNMSVIAH VDHGKSTLTD SLVGKAGIIA AQKAGEMRFT DTRKDEQERC
     ITIKSTAISM YFEVEQKDLQ FITEESQKEK DTKGFLINLI DSPGHVDFSS EVTAALRVTD
     GALVVVDCVS GVCVQTETVL RQAIAERIKP VLFMNKMDRA LLELQLEAED LFQTFQRIVE
     NVNVIIATYG DETGPMGDVK VDPSRGNVGF GSGLHGWAFT LKQFSEMYAE KFKIDIDKLM
     KKLWGDNFYN PKTKKWAKSR DDGGEYKRTF CMFILDPIYR VFEAIMGYKT TEIPKLLEKL
     NITLKGEDKD KDGKALLKIV MRQWLPAGEA LLQMIAIHLP SPVTAQRYRM EMLYEGPHDD
     EAAVAIKTCD PNGPLMMYIS KMVPTSDKGR FYAFGRVFAG TVSTGQKVRI MGPNYTPGKK
     EDLYEKAIQR TILMMGRYTE AIEDVPSGNI CGLVGVDQFL VKTGTISTFK DAHNLRVMKF
     SVSPVVRVAV EPKNPSELPK LVEGLKRLAK SDPMVQCIIE ESGEHIVAGA GELHLEICLK
     DLEEDHACIP IKVSDPVVSY RETVSEESSI MCLAKSPNKH NRLFMKAQPM PEGLAEDIDK
     GDVTARDDFK ARARYLTEKY DYDITEARKI WCFGPDGTGP NILVDCTKGV QYLNEIKDSV
     VAGFQWATKE GVMAEENMRG VRFNIFDVTL HADAIHRGGG QIIPTARRVL YACILTAAPR
     MMEPVYLC
//
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