ID   EFTU_SCHPO              Reviewed;         439 AA.
AC   Q9Y700;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=Elongation factor Tu, mitochondrial;
DE   Flags: Precursor;
GN   Name=tuf1; ORFNames=SPBC9B6.04c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
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; CU329671; CAB42365.1; -; Genomic_DNA.
DR   PIR; T40785; T40785.
DR   RefSeq; NP_595746.1; NM_001021646.2.
DR   AlphaFoldDB; Q9Y700; -.
DR   SMR; Q9Y700; -.
DR   BioGRID; 276743; 5.
DR   STRING; 4896.SPBC9B6.04c.1; -.
DR   MaxQB; Q9Y700; -.
DR   PaxDb; Q9Y700; -.
DR   PRIDE; Q9Y700; -.
DR   EnsemblFungi; SPBC9B6.04c.1; SPBC9B6.04c.1:pep; SPBC9B6.04c.
DR   GeneID; 2540210; -.
DR   KEGG; spo:SPBC9B6.04c; -.
DR   PomBase; SPBC9B6.04c; tuf1.
DR   VEuPathDB; FungiDB:SPBC9B6.04c; -.
DR   eggNOG; KOG0460; Eukaryota.
DR   HOGENOM; CLU_007265_0_0_1; -.
DR   InParanoid; Q9Y700; -.
DR   OMA; EGDKEWG; -.
DR   PhylomeDB; Q9Y700; -.
DR   PRO; PR:Q9Y700; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005759; C:mitochondrial matrix; ISS:PomBase.
DR   GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR   GO; GO:0005525; F:GTP binding; ISS:PomBase.
DR   GO; GO:0003924; F:GTPase activity; ISO:PomBase.
DR   GO; GO:0003746; F:translation elongation factor activity; ISS:PomBase.
DR   GO; GO:0000049; F:tRNA binding; ISS:PomBase.
DR   GO; GO:0070125; P:mitochondrial translational elongation; IGI:PomBase.
DR   GO; GO:0006414; P:translational elongation; IBA:GO_Central.
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   3: Inferred from homology;
KW   Elongation factor; GTP-binding; Mitochondrion; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT   CHAIN           ?..439
FT                   /note="Elongation factor Tu, mitochondrial"
FT                   /id="PRO_0000007464"
FT   DOMAIN          51..246
FT                   /note="tr-type G"
FT   REGION          60..67
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          101..105
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          122..125
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          177..180
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          214..216
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         60..67
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         122..126
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         177..180
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   439 AA;  48282 MW;  8B2CA4F1D693BF75 CRC64;
     MNSAKATSLL FQGFRKNCLR LNRISFASGL INRFTVPART YADEKVFVRK KPHVNIGTIG
     HVDHGKTTLT AAITKCLSDL GQASFMDYSQ IDKAPEEKAR GITISSAHVE YETANRHYAH
     VDCPGHADYI KNMITGAATM DGAIIVVSAT DGQMPQTREH LLLARQVGVK QIVVYINKVD
     MVEPDMIELV EMEMRELLSE YGFDGDNTPI VSGSALCALE GREPEIGLNS ITKLMEAVDS
     YITLPERKTD VPFLMAIEDV FSISGRGTVV TGRVERGTLK KGAEIEIVGY GSHLKTTVTG
     IEMFKKQLDA AVAGDNCGLL LRSIKREQLK RGMIVAQPGT VAPHQKFKAS FYILTKEEGG
     RRTGFVDKYR PQLYSRTSDV TVELTHPDPN DSDKMVMPGD NVEMICTLIH PIVIEKGQRF
     TVREGGSTVG TALVTELLD