ID   RRF2M_DROSE             Reviewed;         692 AA.
AC   B4HEQ8;
DT   13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Ribosome-releasing factor 2, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03059};
DE            Short=RRF2mt {ECO:0000255|HAMAP-Rule:MF_03059};
DE   AltName: Full=Elongation factor G 2, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03059};
DE            Short=EF-G2mt {ECO:0000255|HAMAP-Rule:MF_03059};
DE            Short=mEF-G 2 {ECO:0000255|HAMAP-Rule:MF_03059};
DE   Flags: Precursor;
GN   Name=mRRF2 {ECO:0000250|UniProtKB:Q9VCX4};
GN   Synonyms=EF-G2 {ECO:0000250|UniProtKB:Q9VCX4}; ORFNames=GM26450;
OS   Drosophila sechellia (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rob3c / Tucson 14021-0248.25;
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
CC   -!- FUNCTION: Mitochondrial GTPase that mediates the disassembly of
CC       ribosomes from messenger RNA at the termination of mitochondrial
CC       protein biosynthesis. Not involved in the GTP-dependent ribosomal
CC       translocation step during translation elongation. {ECO:0000255|HAMAP-
CC       Rule:MF_03059}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03059}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-G/EF-2
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_03059}.
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DR   EMBL; CH480815; EDW43219.1; -; Genomic_DNA.
DR   RefSeq; XP_002032233.1; XM_002032197.1.
DR   AlphaFoldDB; B4HEQ8; -.
DR   SMR; B4HEQ8; -.
DR   STRING; 7238.B4HEQ8; -.
DR   EnsemblMetazoa; FBtr0209435; FBpp0207927; FBgn0181303.
DR   HOGENOM; CLU_002794_4_1_1; -.
DR   OMA; AVCQIPW; -.
DR   PhylomeDB; B4HEQ8; -.
DR   Proteomes; UP000001292; Unassembled WGS sequence.
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:0032543; P:mitochondrial translation; ISS:UniProtKB.
DR   GO; GO:0032790; P:ribosome disassembly; ISS:UniProtKB.
DR   CDD; cd16262; EFG_III; 1.
DR   CDD; cd03713; EFG_mtEFG_C; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_03059; mEF_G_2; 1.
DR   InterPro; IPR030851; EFG2.
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; 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   Pfam; PF00679; EFG_C; 1.
DR   Pfam; PF14492; EFG_III; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SMART; SM00838; EFG_C; 1.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF54980; SSF54980; 2.
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   GTP-binding; Mitochondrion; Nucleotide-binding; Protein biosynthesis;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..29
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT   CHAIN           30..692
FT                   /note="Ribosome-releasing factor 2, mitochondrial"
FT                   /id="PRO_0000385604"
FT   DOMAIN          31..310
FT                   /note="tr-type G"
FT   BINDING         40..47
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT   BINDING         104..108
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT   BINDING         158..161
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
SQ   SEQUENCE   692 AA;  76562 MW;  0BABFB125B00CB95 CRC64;
     MLKYAWQSGP KQRNRWLWHL SNQIWKRSYS SKIRNIGILA HIDAGKTTTT ERMLFYAGKT
     RALGEVHRGN TVTDYLTQER ERGITICSSA VTFPWNDHRI NLLDTPGHID FTMEVEQSLY
     AVDGVVVVLD GTAGVEAQTV TVWSQADKHK LPRLIFVNKM DRPDADFEKC VSDLKDKLET
     QPVCLQYPVK NDDGVLAIND VITLERLSWQ KKDLGRSYRN VKLEPSDDLR VLQEKRNELI
     DQLSGLDDEL ADVVISTESF DNVDNALIER ALRRATAQQK VVPVLLGSAY KNVGIQRLMD
     AVNAYLPAPE ERNQIYDCFG GEIKRGMRLI SARGQAEVVS KLYEPLADEY REVGAVQSGD
     VVICAGLKST VTGDLLTSTE EDDELDESAE LFAIDPQIPD AVYFCSIEPP SVSSQTAMEQ
     ALKQLQREDP SLRVSYDSVT GQTVLGGMGE LHMDIIKSRI LSDYKIDVDL GPLQIAYKET
     IEAPALTTQS VEKEIAGSKQ SVSITLEVVK NQAELFSLDK SPENLPNLNT LRPRILQVLR
     KGSISALERG PRVGGQVVET QIRLHNATIG RGTADSFVMA TAAQCVQKLL STSGTRLLEP
     IMALQIVAPS ERISGIIADL SRRRALINDV LPKGERNKMI LVNAPLAELS GYSSALRTIS
     SGTGSMTMQP CGFSSMNSVD ESLAERRAQG LE