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Database: UniProt
Entry: E3NX15_CAERE
LinkDB: E3NX15_CAERE
Original site: E3NX15_CAERE 
ID   E3NX15_CAERE            Unreviewed;       651 AA.
AC   E3NX15;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=Tr-type G domain-containing protein {ECO:0000259|PROSITE:PS51722};
GN   ORFNames=CRE_19648 {ECO:0000313|EMBL:EFP08189.1};
OS   Caenorhabditis remanei (Caenorhabditis vulgaris).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN   [1] {ECO:0000313|Proteomes:UP000008281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG   Caenorhabditis remanei Sequencing Consortium;
RA   Wilson R.K.;
RT   "PCAP assembly of the Caenorhabditis remanei genome.";
RL   Submitted (JUL-2007) 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; DS271987; EFP08189.1; -; Genomic_DNA.
DR   RefSeq; XP_003087056.1; XM_003087008.1.
DR   AlphaFoldDB; E3NX15; -.
DR   STRING; 31234.E3NX15; -.
DR   EnsemblMetazoa; CRE19648.1; CRE19648.1; WBGene00076936.
DR   eggNOG; KOG0469; Eukaryota.
DR   HOGENOM; CLU_002794_11_1_1; -.
DR   InParanoid; E3NX15; -.
DR   OMA; ATFANMY; -.
DR   OrthoDB; 166721at2759; -.
DR   Proteomes; UP000008281; Unassembled WGS sequence.
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   CDD; cd01681; aeEF2_snRNP_like_IV; 1.
DR   CDD; cd01885; EF2; 1.
DR   CDD; cd16261; EF2_snRNP_III; 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   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   4: Predicted;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008281}.
FT   DOMAIN          5..317
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   651 AA;  72951 MW;  EEEE66378CD5171E CRC64;
     MDRRRNIRNM SVIAHVDHGK STLTDSLVSK AGIIAQSKAG EARFTDTRKD EQERCITIKS
     TAISLFFELD KKDLDFVQGE HQCETIEVNG KPEKFNGFLI NLIDSPGHVD FSSEVTAALR
     VTDGAMVVVD CVSGVCVQTE TVLRQAIAER IKPILFMNKM DRALLELQLG AEEMYQTFRR
     IVENVNVIIA TYLDDDGPMG PVMVDPSIGN VDKLMKNLWG DRFFNPTTKK WSYTKTDDNS
     KRGFNQFVLE PILMVFDAIM NVKKEKIQEL VKKLSIKLDY DEEDLEGKPL LKAFMRRWLP
     AGDTMLQMIA FHLPSPVAAQ NYRMEMLYEG PHDDDAALAI KNCDPNGPLM MYISKMVPTS
     DKGRFYAFGR VFSGKVATGM KARIQGPNYV PGKKDDLYEK TIQRTIIMMG KYVECIEDIP
     CGNIAGLVGV DQYLVKGGTI TTFKDAHNLR VMKFSVSPVV RVAVEAKNPA DLPKLVEGLK
     RLAKSDPMVQ CTFESSGEHI IAGAGELHLE ICLKDLEEDH ACIPLKISDP VVSYRETVQA
     ESSQICLAKS ANKLNRLHCS AQPMPDGLAD DIEGGVINAR YEFKSRAKTL SEKYNYDVTE
     ARRIWCFGPD GTGPNLLFDV TKGVQYLNDI KDPMMAGFSW ATREVSFVRR L
//
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