ID   EFGM_PONAB              Reviewed;         751 AA.
AC   Q5R9V1; Q5R5I6;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 94.
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 {ECO:0000255|HAMAP-Rule:MF_03061};
GN   Synonyms=EFG1 {ECO:0000255|HAMAP-Rule:MF_03061};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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. Does
CC       not mediate the disassembly of ribosomes from messenger RNA at the
CC       termination of mitochondrial protein biosynthesis. {ECO:0000255|HAMAP-
CC       Rule:MF_03061}.
CC   -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation.
CC       {ECO:0000255|HAMAP-Rule:MF_03061}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
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; CR859281; CAH91459.1; -; mRNA.
DR   EMBL; CR860873; CAH92980.1; -; mRNA.
DR   RefSeq; NP_001126761.1; NM_001133289.1.
DR   AlphaFoldDB; Q5R9V1; -.
DR   SMR; Q5R9V1; -.
DR   STRING; 9601.ENSPPYP00000015927; -.
DR   GeneID; 100173763; -.
DR   KEGG; pon:100173763; -.
DR   CTD; 85476; -.
DR   eggNOG; KOG0465; Eukaryota.
DR   InParanoid; Q5R9V1; -.
DR   OrthoDB; 637899at2759; -.
DR   UniPathway; UPA00345; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR   GO; GO:0003746; F:translation elongation factor activity; ISS:UniProtKB.
DR   GO; GO:0070125; P:mitochondrial translational elongation; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Acetylation; Elongation factor; GTP-binding; Mitochondrion;
KW   Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..36
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT   CHAIN           37..751
FT                   /note="Elongation factor G, mitochondrial"
FT                   /id="PRO_0000007442"
FT   DOMAIN          44..321
FT                   /note="tr-type G"
FT   BINDING         53..60
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT   BINDING         120..124
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT   BINDING         174..177
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT   MOD_RES         91
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96RP9"
FT   MOD_RES         175
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96RP9"
FT   CONFLICT        49
FT                   /note="I -> T (in Ref. 1; CAH92980)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        412
FT                   /note="A -> V (in Ref. 1; CAH92980)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        536
FT                   /note="D -> G (in Ref. 1; CAH92980)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   751 AA;  83295 MW;  80BD6D209EFB9B63 CRC64;
     MRLLGAAAVA ALGRGRAPAS LGWQRKQVNW KACRWSSSGV IPNEKIRNIG ISAHIDSGKT
     TLTERVLYYT GRIAKMHEVK GKDGVGAVMD SMELERQRGI TIQSAATYTM WKDVNINIID
     TPGHVDFTIE VERALRVLDG AVLVLCAVGG VQCQTMTVNR QMKRYNVPFL TFINKLDRMG
     SNPARALQQM RSKLNHNAAF MQIPIGLEGD FKGIIDLIEE RAIYFDGDFG QIVQYGEIPA
     ELRAAAADHR QELIECVANS DEQLGEMFLE EKIPSISDLK LAIRRATLKR SFTPVFLGSA
     LKNKGVQPLL DAVLEYLPNP SEVQNYAILN KEDDSKEKTK ILMNSNRDNS HPFVGLAFKL
     EVGRFGQLTY VRSYQGELKK GDTIYNTRTG KKVRLQRLAR MHADMMEDVE KAYAGDICAL
     FGIDCASGDT FTDKANSGLS MESIHVPDPV ISIAMKPSNK NDLEKFSKGI GRFTREDPTF
     KVHFDTENKE TIISGMGELH LEIYAQRLER EYGCPCITGK PKVAFRETIT APVPFDFTHK
     RQSGGAGQYG KVIGVLEPLD PEDYTKLEFS DETFGSNIPK QFVPAVEKGF LDACEKGPLS
     GHKLSGLRFV LQDGAHHMVD SNEISFIRAG EGALKQALAN ATLCILEPIM AVEVVAPNEF
     QGQVIAGINR RHGVITGQDG VEDYFTLYAD VPLNDMFGYS TELRSCTEGK GEYTMEYGRY
     QPCLPSTQED VINKYLEATG QLPVKKGKAK N