EFTU_PICGU
ID EFTU_PICGU Reviewed; 426 AA.
AC A5DN78; Q0ZIA9;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Elongation factor Tu, mitochondrial;
DE AltName: Full=tufM;
DE Flags: Precursor;
GN Name=TUF1; ORFNames=PGUG_04729;
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 133-371.
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RA Piche Y., Boissinot M., Boudreau D.K., Trepanier H., Boily M.-J.,
RA Picard F.J., Ouellette M., Roy P.H., Bergeron M.G.;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: G-protein that, in its active GTP-bound form, binds to and
CC delivers aminoacyl-tRNA to the A-site of ribosomes during protein
CC biosynthesis. In the presence of a correct codon-anticodon match
CC between the aminoacyl-tRNA and the A-site codon of the ribosome-bound
CC mRNA, the ribosome acts as a GTPase activator and the GTP is
CC hydrolyzed. The inactive GDP-bound form leaves the ribosome and must be
CC recycled before binding another molecule of aminoacyl-tRNA. Required
CC for mitochondrial protein biosynthesis and maintenance of mitochondrial
CC DNA (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation.
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; CH408160; EDK40631.1; -; Genomic_DNA.
DR EMBL; DQ447250; ABE27744.1; -; Genomic_DNA.
DR RefSeq; XP_001482774.1; XM_001482724.1.
DR AlphaFoldDB; A5DN78; -.
DR SMR; A5DN78; -.
DR STRING; 4929.XP_001482774.1; -.
DR EnsemblFungi; EDK40631; EDK40631; PGUG_04729.
DR GeneID; 5124936; -.
DR KEGG; pgu:PGUG_04729; -.
DR VEuPathDB; FungiDB:PGUG_04729; -.
DR eggNOG; KOG0460; Eukaryota.
DR HOGENOM; CLU_007265_0_0_1; -.
DR InParanoid; A5DN78; -.
DR OMA; EGDKEWG; -.
DR OrthoDB; 491836at2759; -.
DR UniPathway; UPA00345; -.
DR Proteomes; UP000001997; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-KW.
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..27
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 28..426
FT /note="Elongation factor Tu, mitochondrial"
FT /id="PRO_0000295031"
FT DOMAIN 34..230
FT /note="tr-type G"
FT REGION 43..50
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 84..88
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 105..108
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 160..163
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 198..200
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 43..50
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 105..109
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 160..163
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 426 AA; 46778 MW; 020E05906F3DD320 CRC64;
MFKNLAGSFR AVSRVAFKTR PSLVRSYAAF DRSKPHVNIG TIGHVDHGKT TLTAAITKVL
SEKGGANFLD YGSIDRAPEE RARGITISTA HVEYQTDKRH YAHVDCPGHA DYIKNMITGA
AQMDGAIIVV AATDGQMPQT REHLLLARQV GVQHLVVFVN KVDTIDDPEM LELVEMEMRE
LLSQYGFDGD NTPVIMGSAL CALESKQPEI GVQAIEKLLD AVDEHIPTPT RDLEQPFLLP
VEDVFSISGR GTVVTGRVER GSLKKGEEIE IVGDFDKPFK TTVTGIEMFK KELDAAMAGD
NAGILLRGVK RDDVKRGMVL AKPSTVTSHK KVLASLYILS KEEGGRHSPF GENYKPQLFI
RTTDVTGTLR FPAGEGVDHS QMVMPGDNVE MEIELVRKTP LEVNQRFNIR EGGKTVGTGL
VTRIIE
