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Database: UniProt
Entry: E4XT88_OIKDI
LinkDB: E4XT88_OIKDI
Original site: E4XT88_OIKDI 
ID   E4XT88_OIKDI            Unreviewed;       843 AA.
AC   E4XT88;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=Tr-type G domain-containing protein {ECO:0000259|PROSITE:PS51722};
GN   ORFNames=GSOID_T00003020001 {ECO:0000313|EMBL:CBY12950.1};
OS   Oikopleura dioica (Tunicate).
OC   Eukaryota; Metazoa; Chordata; Tunicata; Appendicularia; Copelata;
OC   Oikopleuridae; Oikopleura.
OX   NCBI_TaxID=34765 {ECO:0000313|EMBL:CBY12950.1};
RN   [1] {ECO:0000313|EMBL:CBY12950.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21097902; DOI=10.1126/science.1194167;
RA   Denoeud F., Henriet S., Mungpakdee S., Aury J.M., Da Silva C.,
RA   Brinkmann H., Mikhaleva J., Olsen L.C., Jubin C., Canestro C.,
RA   Bouquet J.M., Danks G., Poulain J., Campsteijn C., Adamski M., Cross I.,
RA   Yadetie F., Muffato M., Louis A., Butcher S., Tsagkogeorga G., Konrad A.,
RA   Singh S., Jensen M.F., Cong E.H., Eikeseth-Otteraa H., Noel B.,
RA   Anthouard V., Porcel B.M., Kachouri-Lafond R., Nishino A., Ugolini M.,
RA   Chourrout P., Nishida H., Aasland R., Huzurbazar S., Westhof E., Delsuc F.,
RA   Lehrach H., Reinhardt R., Weissenbach J., Roy S.W., Artiguenave F.,
RA   Postlethwait J.H., Manak J.R., Thompson E.M., Jaillon O., Du Pasquier L.,
RA   Boudinot P., Liberles D.A., Volff J.N., Philippe H., Lenhard B.,
RA   Roest Crollius H., Wincker P., Chourrout D.;
RT   "Plasticity of animal genome architecture unmasked by rapid evolution of a
RT   pelagic tunicate.";
RL   Science 330:1381-1385(2010).
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; FN653150; CBY12950.1; -; Genomic_DNA.
DR   AlphaFoldDB; E4XT88; -.
DR   InParanoid; E4XT88; -.
DR   Proteomes; UP000001307; 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   GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
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   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:UP000001307}.
FT   DOMAIN          17..347
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   843 AA;  94204 MW;  92A34B38FDC08BF4 CRC64;
     MVNFTIDEIR EIMDKKENIR NMSVIAHVDH GKSTLTDSLV SKAGIIAGSK AGETRFTDTR
     KDEQERCITI KSTAISLFYE LSDVDMSFVK QKTNGNAFLI NLIDSPGHVD FSSEVTAALR
     VTDGALVVVD CVSGVCVQTE TVLRQAIAER IKPVLFMNKM DRALLELQLD PEELYQTFAR
     IVENVNVIIA TYGGADEDGP MGCLYVSPGD GTVGFGSGLH GWAFTLKQFA EMYASKFKID
     LDKMMKNLWG DRFYDAKAKK WVKQMSKTAP KRGFVQWILD PIYKAFRSIM DEKMEEATKI
     MGVCGVTLKG DDKDLRGKPL LKCFMRNWLP AGETLLQMIA IHLPSPLTAQ AYRCEMLYEG
     PQDDELAKAF RTCDADGPLM AYISKMVPTS DKGRFYAFGR VFAGKIATGQ KVRIMGPNFV
     PGQKSDLYCK QIQRTILMMG RYIEAIDDVP CGNLVGLVGV DQYLVKTGAI TTFEGAHNMK
     QMKFSVSPVV RVAVQCKNPA DLPKLVEGLK RLAKSDPMVQ IISEESGEHI IAGAGELHLE
     ICLKDLEEDH ACIPIKKSEP VVSYRETVTE ASNQVCLSKS PNKHNRLYMK ASPMPEGMAD
     EIEDKKITPR DEVKARARYM SEKYEWDVND CRKIWCFGPD QNGANMVIDV TKGVQFLNEI
     KDSVKAGFDW AAKEGVLCDE NMRGIRFDLH DVTLHADAIH RGGGQLIPTA RRCFYACVMT
     AQPRLLEPVY LVEVQCPETA MGGIYSVLNR KRGHVFAEEA VTGTPMFMVR AYLPVNESFG
     FDSDLRAATS GQAFPQCVFD HWQTLDSDPL EENSQANKIV LHTRKRKGLS EMLPPLDRFL
     DKL
//
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