ID   EFTU_DICDI              Reviewed;         424 AA.
AC   Q54HB2;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Elongation factor Tu, mitochondrial;
DE   Flags: Precursor;
GN   Name=tufm; ORFNames=DDB_G0289593;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [2]
RP   PROTEIN SEQUENCE OF 86-101; 198-216; 236-254 AND 269-294, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=AX2;
RA   Bienvenut W.V., Ura S., Insall R.H.;
RL   Submitted (JUL-2009) to UniProtKB.
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC       tRNA to the A-site of ribosomes during protein biosynthesis.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AAFI02000146; EAL62650.2; -; Genomic_DNA.
DR   RefSeq; XP_636148.2; XM_631056.2.
DR   AlphaFoldDB; Q54HB2; -.
DR   SMR; Q54HB2; -.
DR   STRING; 44689.DDB0235257; -.
DR   PaxDb; Q54HB2; -.
DR   PRIDE; Q54HB2; -.
DR   EnsemblProtists; EAL62650; EAL62650; DDB_G0289593.
DR   GeneID; 8627215; -.
DR   KEGG; ddi:DDB_G0289593; -.
DR   dictyBase; DDB_G0289593; tufM.
DR   eggNOG; KOG0460; Eukaryota.
DR   HOGENOM; CLU_007265_0_1_1; -.
DR   InParanoid; Q54HB2; -.
DR   OMA; EGDKEWG; -.
DR   PhylomeDB; Q54HB2; -.
DR   PRO; PR:Q54HB2; -.
DR   Proteomes; UP000002195; Chromosome 5.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; ISS:UniProtKB.
DR   GO; GO:0070125; P:mitochondrial translational elongation; IBA:GO_Central.
DR   GO; GO:0006414; P:translational elongation; ISS:UniProtKB.
DR   CDD; cd01884; EF_Tu; 1.
DR   CDD; cd03697; EFTU_II; 1.
DR   Gene3D; 3.40.50.300; -; 1.
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   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; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF50465; SSF50465; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00485; EF-Tu; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Elongation factor; GTP-binding; Mitochondrion;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..424
FT                   /note="Elongation factor Tu, mitochondrial"
FT                   /id="PRO_0000328177"
FT   DOMAIN          36..234
FT                   /note="tr-type G"
FT   REGION          45..52
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          86..90
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          107..110
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          162..165
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          199..201
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         45..52
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         107..111
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         162..165
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   424 AA;  46026 MW;  5FDCB971E615F2F0 CRC64;
     MISRLFASNQ NVKLVRTFKS TSISMAAEKK KFERTKPHVN VGTIGHVDHG KTTLTAAITK
     TLSDRGLANF KSYAQIDKSP EEKARGITIT ASHIEYESAT RHYAHIDCPG HQHYIKNMIT
     GAAQMDGAIL VVSAPDGPQE QTREHIILSR EVGIPALVVF LNKMDNADPD LVEIVEMEVR
     ELLSQYGFNG DETPFVKGAA AVALAETNET ATQYGRKAID ELVEVLDTKI PLPHRAVDKP
     FLMPVEEVFS ISGRGTVATG RIEQGTLKVG EEVAIVGIKP VPKVAVTGIE MFGKLLDFAQ
     AGENVGCLLR GLKREEVLRG EVISKPGTIK ASTKFKAKTY VLTEAEGGRK KGFATGYRPQ
     FFIRTANVTG MIELPPTHAV ILPGDSLEFT VELISPTPLS INGRFAIREG QLTVGAGVIS
     EILN