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 27-MAR-2024, entry version 152.
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; 284812.Q9Y700; -.
DR MaxQB; Q9Y700; -.
DR PaxDb; 4896-SPBC9B6-04c-1; -.
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; FHNNYRP; -.
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; EXP:PomBase.
DR GO; GO:0000049; F:tRNA binding; ISS:PomBase.
DR GO; GO:0032543; P:mitochondrial translation; EXP:PomBase.
DR GO; GO:0070125; P:mitochondrial translational elongation; IBA:GO_Central.
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; 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
//
