ID   RRF2M_DROYA             Reviewed;         712 AA.
AC   B4PMC6;
DT   13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=GE10317;
OS   Drosophila yakuba (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tai18E2 / Tucson 14021-0261.01;
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; CM000160; EDW98031.1; -; Genomic_DNA.
DR   RefSeq; XP_002098319.2; XM_002098283.2.
DR   AlphaFoldDB; B4PMC6; -.
DR   SMR; B4PMC6; -.
DR   STRING; 7245.FBpp0255327; -.
DR   GeneID; 6537778; -.
DR   KEGG; dya:Dyak_GE10317; -.
DR   eggNOG; KOG0464; Eukaryota.
DR   HOGENOM; CLU_002794_4_1_1; -.
DR   OMA; AVCQIPW; -.
DR   PhylomeDB; B4PMC6; -.
DR   Proteomes; UP000002282; Chromosome 3R.
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   Transit peptide.
FT   TRANSIT         1..29
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT   CHAIN           30..712
FT                   /note="Ribosome-releasing factor 2, mitochondrial"
FT                   /id="PRO_0000385607"
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   712 AA;  79034 MW;  38DFCA7661B844B6 CRC64;
     MLRCAWQNGP RQSNRWLRHL SNQIWKRSYS SKIRNIGILA HIDAGKTTTT ERMLFYAGKT
     RALGEVHRGN TVTDYLTQER ERGITICSSA VTFPWNDHRI NLLDTPGHID FTMEVEQSLF
     AVDGVVVVLD GTAGVEAQTV TVWSQADKHK LPRLIFVNKM DRPDADFDKC VADLKDKLET
     QPVCLQYPVK NEDGVLAIND VITLERLSWH QKDLGRSYKN VKLEPSDDLR QLQEKRSELI
     DQLSGLDDEL ADVVISTESF DKVDNALIER ALRRATTQQK VVPVLLGSAY KNVGIQRLMD
     AVNSYLPAPE ERNQIYDCFG TEVAGKVFKI VHDKQRGPLT LIRILRGEIK RGMRLISARG
     QAEVVSKLYE PLADEYREVS AVQSGDVVIC AGLKSTVTDE EDDELDESDE LFAIDPQIPD
     AVYFCSIEPP SVSSQTAMEQ ALKQLQREDP SLRVSYDSVT GQTVLGGMGE LHMDIIKSRI
     LSEYKIDVDL GPLQIAYKET IESPALTTLS VEKEIAGSKQ SVSITLEVVK NQAEMFSLDK
     SPENLPNLNT LRPRILQVLR KGSISALERG PRVGGQVVET QIRLHNATIG RGTADSFVMA
     TAAQCVQKLL STSGTRLLEP IMALQIVAPS ERISGIMADL SRRRALINDV LPKGERNKMI
     LVNAPLAELS GYSSALRTIS SGTASMTMQP CGFSSMNSVD ESLAERRAQG LE