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Database: UniProt/SWISS-PROT
Entry: EFTU_SCHPO
LinkDB: EFTU_SCHPO
Original site: EFTU_SCHPO 
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   28-FEB-2018, entry version 130.
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;
OC   Schizosaccharomycetaceae; 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.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., 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
CC       aminoacyl-tRNA to the A-site of ribosomes during protein
CC       biosynthesis. {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}.
DR   EMBL; CU329671; CAB42365.1; -; Genomic_DNA.
DR   PIR; T40785; T40785.
DR   RefSeq; NP_595746.1; NM_001021646.2.
DR   ProteinModelPortal; Q9Y700; -.
DR   SMR; Q9Y700; -.
DR   BioGrid; 276743; 4.
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   EuPathDB; FungiDB:SPBC9B6.04c; -.
DR   PomBase; SPBC9B6.04c; tuf1.
DR   HOGENOM; HOG000229290; -.
DR   InParanoid; Q9Y700; -.
DR   KO; K02358; -.
DR   OMA; YGHIDCP; -.
DR   OrthoDB; EOG092C2HV8; -.
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   CDD; cd03697; EFTU_II; 1.
DR   HAMAP; MF_00118_B; EF_Tu_B; 1.
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; TF_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   Complete proteome; Elongation factor; GTP-binding; Mitochondrion;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome;
KW   Transit peptide.
FT   TRANSIT       1      ?       Mitochondrion.
FT   CHAIN         ?    439       Elongation factor Tu, mitochondrial.
FT                                /FTId=PRO_0000007464.
FT   DOMAIN       51    246       tr-type G.
FT   NP_BIND      60     67       GTP. {ECO:0000250}.
FT   NP_BIND     122    126       GTP. {ECO:0000250}.
FT   NP_BIND     177    180       GTP. {ECO:0000250}.
FT   REGION       60     67       G1. {ECO:0000250}.
FT   REGION      101    105       G2. {ECO:0000250}.
FT   REGION      122    125       G3. {ECO:0000250}.
FT   REGION      177    180       G4. {ECO:0000250}.
FT   REGION      214    216       G5. {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
//
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