ID   EFTU_CHICK              Reviewed;         352 AA.
AC   P84172;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Elongation factor Tu, mitochondrial;
DE            Short=EF-Tu;
DE   Flags: Precursor; Fragment;
GN   Name=TUFM {ECO:0000250|UniProtKB:P49411};
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-208.
RA   Cogburn L.A., Monsonego-Ornan E.;
RT   "Chicken ESTs from muscle.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 203-352.
RC   TISSUE=Embryo;
RA   Murray F.;
RL   Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000305}
RP   IDENTIFICATION, AND MASS SPECTROMETRY.
RC   TISSUE=Embryo {ECO:0000269|PubMed:16287166};
RX   PubMed=16287166; DOI=10.1002/pmic.200402056;
RA   Agudo D., Gomez-Esquer F., Diaz-Gil G., Martinez-Arribas F., Delcan J.,
RA   Schneider J., Palomar M.A., Linares R.;
RT   "Proteomic analysis of the Gallus gallus embryo at stage-29 of
RT   development.";
RL   Proteomics 5:4946-4957(2005).
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|UniProtKB:P49411}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P49411}.
CC   -!- MASS SPECTROMETRY: Mass=27665; Mass_error=1; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:16287166};
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU01059}.
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DR   EMBL; CD215156; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AL585562; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P84172; -.
DR   SMR; P84172; -.
DR   PRIDE; P84172; -.
DR   VEuPathDB; HostDB:geneid_419244; -.
DR   InParanoid; P84172; -.
DR   PhylomeDB; P84172; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
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   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; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   1: Evidence at protein level;
KW   Elongation factor; GTP-binding; Mitochondrion; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome; Transit peptide.
FT   TRANSIT         <1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000305"
FT   CHAIN           ?..>352
FT                   /note="Elongation factor Tu, mitochondrial"
FT                   /id="PRO_0000223488"
FT   DOMAIN          45..241
FT                   /note="tr-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          54..61
FT                   /note="G1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          95..99
FT                   /note="G2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          116..119
FT                   /note="G3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          171..174
FT                   /note="G4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          209..211
FT                   /note="G5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   BINDING         54..61
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P49411"
FT   BINDING         116..120
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P49411"
FT   BINDING         171..174
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P49411"
FT   NON_TER         1
FT                   /evidence="ECO:0000305"
FT   NON_TER         352
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   352 AA;  38250 MW;  7567B76C8EFD4F0E CRC64;
     GPLRVRTSKM ALPAALLRAA ALRCRLPLAS VGRRHLAAEA FVRDRPHVNV GTIGHVDHGK
     TTLTAAITKV LSESGGARFQ RYEDIDKAPE ERARGITINA AHVEYSTARR HYAHTDCPGH
     ADYVKNMITG TAPLDGCILV VAATDGQMPQ TREHLLLARQ VGVRHVVVYV NKADAVSDAE
     LLPLVELELR ELLAEMGYDA ERTPVVVGSA LCALQDRDPT LGRDSVLQLL EAIDTHIPLP
     HRDVQRPFLL PIEGVHSIPG RGTVVTGTVE RGAVSKGDEC ELRGYGRVLK AVVTGLETFH
     KSLPRAEAGD NVGALLRGLR REDVRRGMVM GQPGALRDHR KLQAQVYVLS AQ