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EFGM_DICDI
ID   EFGM_DICDI              Reviewed;         734 AA.
AC   Q55E94;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Elongation factor G, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03061};
DE            Short=EF-Gmt {ECO:0000255|HAMAP-Rule:MF_03061};
DE   AltName: Full=Elongation factor G 1, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03061};
DE            Short=mEF-G 1 {ECO:0000255|HAMAP-Rule:MF_03061};
DE   AltName: Full=Elongation factor G1 {ECO:0000255|HAMAP-Rule:MF_03061};
DE   Flags: Precursor;
GN   Name=gfm1; ORFNames=DDB_G0270482;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Mitochondrial GTPase that catalyzes the GTP-dependent
CC       ribosomal translocation step during translation elongation. During this
CC       step, the ribosome changes from the pre-translocational (PRE) to the
CC       post-translocational (POST) state as the newly formed A-site-bound
CC       peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E
CC       sites, respectively. Catalyzes the coordinated movement of the two tRNA
CC       molecules, the mRNA and conformational changes in the ribosome.
CC       {ECO:0000255|HAMAP-Rule:MF_03061}.
CC   -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation.
CC       {ECO:0000255|HAMAP-Rule:MF_03061}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03061}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-G/EF-2
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AAFI02000005; EAL72591.1; -; Genomic_DNA.
DR   RefSeq; XP_645887.1; XM_640795.1.
DR   AlphaFoldDB; Q55E94; -.
DR   SMR; Q55E94; -.
DR   STRING; 44689.DDB0234169; -.
DR   PaxDb; Q55E94; -.
DR   EnsemblProtists; EAL72591; EAL72591; DDB_G0270482.
DR   GeneID; 8616829; -.
DR   KEGG; ddi:DDB_G0270482; -.
DR   dictyBase; DDB_G0270482; gfm1.
DR   eggNOG; KOG0465; Eukaryota.
DR   HOGENOM; CLU_002794_4_0_1; -.
DR   InParanoid; Q55E94; -.
DR   OMA; AATTCHW; -.
DR   PhylomeDB; Q55E94; -.
DR   UniPathway; UPA00345; -.
DR   PRO; PR:Q55E94; -.
DR   Proteomes; UP000002195; Chromosome 1.
DR   GO; GO:0005739; C:mitochondrion; ISS:dictyBase.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR   GO; GO:0032543; P:mitochondrial translation; ISS:dictyBase.
DR   GO; GO:0070125; P:mitochondrial translational elongation; IBA:GO_Central.
DR   CDD; cd16262; EFG_III; 1.
DR   CDD; cd01434; EFG_mtEFG1_IV; 1.
DR   CDD; cd04097; mtEFG1_C; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00054_B; EF_G_EF_2_B; 1.
DR   InterPro; IPR045044; EFG1-like.
DR   InterPro; IPR041095; EFG_II.
DR   InterPro; IPR009022; EFG_III.
DR   InterPro; IPR035647; EFG_III/V.
DR   InterPro; IPR035649; EFG_V.
DR   InterPro; IPR000640; EFG_V-like.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR031157; G_TR_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR004540; Transl_elong_EFG/EF2.
DR   InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR   PANTHER; PTHR43636; PTHR43636; 1.
DR   Pfam; PF00679; EFG_C; 1.
DR   Pfam; PF14492; EFG_III; 1.
DR   Pfam; PF03764; EFG_IV; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SMART; SM00838; EFG_C; 1.
DR   SMART; SM00889; EFG_IV; 1.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF54980; SSF54980; 2.
DR   TIGRFAMs; TIGR00484; EF-G; 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..32
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT   CHAIN           33..734
FT                   /note="Elongation factor G, mitochondrial"
FT                   /id="PRO_0000327444"
FT   DOMAIN          38..318
FT                   /note="tr-type G"
FT   BINDING         47..54
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT   BINDING         114..118
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT   BINDING         168..171
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
SQ   SEQUENCE   734 AA;  81931 MW;  08D36609693B0B89 CRC64;
     MTSFLTSRFG GLALRNVMNN KNGINSFGLR CFSTNSVSGL RNIGISAHID SGKTTLTERI
     LYYTGRIKEI HEVRGKDGVG AKMDSMDLER EKGITIQSAA TYCKWGENHI NIIDTPGHVD
     FTIEVERALR VLDGAVLVMC GVSGVQSQTI TVDRQMRRYN VPRVVFINKL DRTGANPWNV
     IEQLRKKLNL NAIALQVPIG KESNLEGVID LVTEKAMIFG EKGTAPIIEE IPSNFVEFVK
     EKKMELVETI ANVDDELGEW MIENDFPNNM PDEKTLTAAI RRTTIARKVV PVMMGSAFKN
     TGVQPLLDGV IKYLPSPNEK KIIALDTSVK DKETEVELES DPKKPFVGLA FKLEEGRFGQ
     LTYMRVYQGT LKRGDTIKNV NLGKTIKVPR LVKMHASEME EVSEVGPGEI CAMFGVDCYS
     GNTFTHQNCS YTMTSMHVPE PVMSLSIQPK SKDGQANFSK ALSKFQKEDP TFRVKSDQES
     GQIIISGMGE LHLEIYVERM KREYNVETVT GKPLVAYRET IQQRGDYNFT HRKQSGGQGQ
     YAKMIGFAEQ SENGMENEFV NDVIGTAIPP TFIEAIKKGF KDCIEKGPLI GHPVVGVKFV
     VSDGNTHSVD SSELAFRIAT AGAFKEAFED GEPTILEPIM KVEISLPQEF QGTVISGVNR
     RKGAIVNTTT QGESLTFECE VPLNNMFGYS TELRSMTQGK GEFSMEYLKH TNVSRELYNQ
     LLEEYKKKRT EENK
 
 
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