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Database: UniProt
Entry: B3RSP1_TRIAD
LinkDB: B3RSP1_TRIAD
Original site: B3RSP1_TRIAD 
ID   B3RSP1_TRIAD            Unreviewed;       828 AA.
AC   B3RSP1;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   RecName: Full=Tr-type G domain-containing protein {ECO:0000259|PROSITE:PS51722};
GN   ORFNames=TRIADDRAFT_37398 {ECO:0000313|EMBL:EDV26551.1};
OS   Trichoplax adhaerens (Trichoplax reptans).
OC   Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC   Trichoplax.
OX   NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV26551.1, ECO:0000313|Proteomes:UP000009022};
RN   [1] {ECO:0000313|EMBL:EDV26551.1, ECO:0000313|Proteomes:UP000009022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV26551.1,
RC   ECO:0000313|Proteomes:UP000009022};
RX   PubMed=18719581; DOI=10.1038/nature07191;
RA   Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA   Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA   Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA   Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA   Rokhsar D.S.;
RT   "The Trichoplax genome and the nature of placozoans.";
RL   Nature 454:955-960(2008).
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; DS985243; EDV26551.1; -; Genomic_DNA.
DR   RefSeq; XP_002110547.1; XM_002110511.1.
DR   AlphaFoldDB; B3RSP1; -.
DR   STRING; 10228.B3RSP1; -.
DR   EnsemblMetazoa; TriadT37398; TriadP37398; TriadG37398.
DR   GeneID; 6751760; -.
DR   KEGG; tad:TRIADDRAFT_37398; -.
DR   CTD; 6751760; -.
DR   eggNOG; KOG0469; Eukaryota.
DR   HOGENOM; CLU_002794_11_2_1; -.
DR   InParanoid; B3RSP1; -.
DR   OMA; NRHNRFY; -.
DR   OrthoDB; 166721at2759; -.
DR   PhylomeDB; B3RSP1; -.
DR   Proteomes; UP000009022; 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   CDD; cd03700; EF2_snRNP_like_II; 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   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   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; PF00679; EFG_C; 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; SM00838; EFG_C; 1.
DR   SMART; SM00889; EFG_IV; 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   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:UP000009022}.
FT   DOMAIN          5..332
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   828 AA;  92349 MW;  177B03856F6F0893 CRC64;
     MDKRQNIRNM SVIAHVDHGK STLTDSLVSK AGIIAGAKAG ETRFTDTRKD EQERCITIKS
     TAISMYYELA EKDLEYVTQE KLGKGFLINL IDSPGHVDFS SEVTAALRVT DGALVVVDCV
     SGVCVQTETV LRQAISERIK PVLFMNKMDR ALLELQLDPE DLYQTFRRIV ENVNVIIATY
     NDENGPMGNI QVDPSKGTVG FGSGLHGWAF TLKQFGEIYA DKFKIEPSKL MGRLWGDNFC
     NPKSRKWNKT GGDGFVRGFT QFILDPIYKI FKSVMNFEKE KYEKMLTQLN IKLSVEDREK
     EGKPLLKAIM RRWLPAGDAL LQMITIHLPS PVTAQKYRME MLYEGPHDDA LALAIKNCDP
     TGHLCMYVSK MVPTSDRGRF YAFGRVFSGT VATGQKVRIM GPNFIPGKKE DLYLKQIQRT
     ILMMGRYIEP IEDVPCGNIV GLVGVDQFLV KTGTITTFEE AHNLKVMKFS VSPVVRVAVE
     AKNPSDLPKL VEGLKRLAKS DPMVQCTIEE SGEHIVAGAG ELHLEICLKD LEEDHACIPI
     KKSDPVVSYR ETVSEESDRT CLSKSPNKHN RLFMRAVPFP EGLAEDIDKG DVTPRGEVKA
     RARLLAEKYE YDVSEARKIW CFGPEGNGPN LLIDVTKGVQ YLNEIKDSVV AGFQWATKEG
     VMCEENVRGV RYNIHDVTLH ADAIHRGGGQ IIPTARRCLY ACSLTAQPRI LEPVYLVEIQ
     CPENAVGGIY GVLNRRRGHV FEESQTPGTP MFAVKAYLPV NESFGFTADL RSNTGGQAFP
     QCVFDHWQIL PGDPSDEASK PGQVVSTTRK RKGLSAGIPS LDKYFDKL
//
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