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Database: UniProt
Entry: D9CJ50_VOLCA
LinkDB: D9CJ50_VOLCA
Original site: D9CJ50_VOLCA 
ID   D9CJ50_VOLCA            Unreviewed;       416 AA.
AC   D9CJ50;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=Elongation factor Tu {ECO:0000256|RuleBase:RU000325};
GN   Name=EFG8m {ECO:0000313|EMBL:ADI46910.1};
OS   Volvox carteri f. nagariensis.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Volvocaceae; Volvox.
OX   NCBI_TaxID=3068 {ECO:0000313|EMBL:ADI46910.1};
RN   [1] {ECO:0000313|EMBL:ADI46910.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Adam {ECO:0000313|EMBL:ADI46910.1};
RX   PubMed=20395508; DOI=10.1126/science.1186222;
RA   Ferris P., Olson B.J., De Hoff P.L., Douglass S., Casero D., Prochnik S.,
RA   Geng S., Rai R., Grimwood J., Schmutz J., Nishii I., Hamaji T., Nozaki H.,
RA   Pellegrini M., Umen J.G.;
RT   "Evolution of an expanded sex-determining locus in Volvox.";
RL   Science 328:351-354(2010).
CC   -!- FUNCTION: Protein transport. Probably involved in vesicular traffic.
CC       {ECO:0000256|ARBA:ARBA00025673}.
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC       tRNA to the A-site of ribosomes during protein biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00003982, ECO:0000256|RuleBase:RU000325}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000256|ARBA:ARBA00004229}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC       subfamily. {ECO:0000256|ARBA:ARBA00007249,
CC       ECO:0000256|RuleBase:RU000325}.
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DR   EMBL; GU784916; ADI46910.1; -; Genomic_DNA.
DR   AlphaFoldDB; D9CJ50; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR   CDD; cd01884; EF_Tu; 1.
DR   CDD; cd03697; EFTU_II; 1.
DR   CDD; cd03707; EFTU_III; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
DR   HAMAP; MF_00118_B; EF_Tu_B; 1.
DR   InterPro; IPR041709; EF-Tu_GTP-bd.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR033720; EFTU_2.
DR   InterPro; IPR031157; G_TR_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR   InterPro; IPR004541; Transl_elong_EFTu/EF1A_bac/org.
DR   InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR   NCBIfam; TIGR00485; EF-Tu; 1.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR43721:SF22; ELONGATION FACTOR TU, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43721; ELONGATION FACTOR TU-RELATED; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF03143; GTP_EFTU_D3; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Elongation factor {ECO:0000256|ARBA:ARBA00022768,
KW   ECO:0000256|RuleBase:RU000325};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU000325};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000325};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT   DOMAIN          29..227
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   416 AA;  45416 MW;  FF73CFCB298517B9 CRC64;
     MSRSELVSSK IHCLSAWRSF CYDINSRAKP HLNVGTIGHV DHGKTTLTAA ITKVLSETNG
     STRAVPYDQI DKAPEEKARG ITISATHVEY QTTNRHYAHV DCPGHADYVK NMITGAAQMD
     GAILVVSAAD GPMPQTREHI LLAKQVGVPR IVVFLNKCDV VEDKELQELV EMEVRELLNF
     YKFPGEEIPV IKGSALCALK GEKSDTLGRN SVLKLMEAVD DYITVPQRAT DKPFQMPVED
     VFSIAGRGTV VTGRVEQGVI KAGDDVEIVG LYETIKSTVT GVEMFKKCLT QGQAGDNVGL
     LIRGIKREDV SRGQVVCKVG SLKTYKRFEA EVYALTKEEG GRHTPFTSKY KPQFFIRTAD
     VSGQIVLPES TAMVMPGDNF RATVELSAPM ALEVGLRFAI RDSGKTVGAG VVTKVI
//
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