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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//