RRF2M_DROPE
ID RRF2M_DROPE Reviewed; 737 AA.
AC B4GNT0;
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=GL13749;
OS Drosophila persimilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7234;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSH-3 / Tucson 14011-0111.49;
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; CH479186; EDW38813.1; -; Genomic_DNA.
DR RefSeq; XP_002020001.1; XM_002019965.1.
DR AlphaFoldDB; B4GNT0; -.
DR SMR; B4GNT0; -.
DR STRING; 7234.FBpp0177856; -.
DR PRIDE; B4GNT0; -.
DR EnsemblMetazoa; FBtr0179364; FBpp0177856; FBgn0151354.
DR GeneID; 6594882; -.
DR KEGG; dpe:6594882; -.
DR eggNOG; KOG0464; Eukaryota.
DR HOGENOM; CLU_002794_4_1_1; -.
DR OMA; AVCQIPW; -.
DR PhylomeDB; B4GNT0; -.
DR Proteomes; UP000008744; 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..737
FT /note="Ribosome-releasing factor 2, mitochondrial"
FT /id="PRO_0000385602"
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 737 AA; 81417 MW; 50205E9E4EB097D3 CRC64;
MLKYALHSGG MPRNRLLRQL SAYIFRRSYS SNIRNIGILA HIDAGKTTTT ERMLFYSGKT
RSLGEVHRGN TVTDYLTQER ERGITICSSA VTFPWSGNRI NLLDTPGHID FTMEVEQSLY
AVDGVVVVLD GTAGVEAQTV TVWTQADKHK LPRLAFVNKM DRPDADFDKC VNDLRTKLET
QPVCIQYPSK NQDGLLAIND VITLEQLTWQ PKDLGRSYSK TKLEPSDDLR QLQEKRNELI
DQLSGLDDEL ADVVISTESF DNVSNALIER ALRRATCQQK VVPVLLGSAY KNVGIQRLMD
AVNTYLPAPE ERNQIYDCFG NEVAGKVFKI VHDKQRGPLT LVRILRGEIK RGMRLICSRG
QAEVVSKLYE PLADEYREVG AVQSGDVVIC AGLKSTVTGD LLTSSQTALR NAQKRLKQSQ
GTVSADEDEE LDTDELFGID RQIPDAVYFC SIEPPSVSSQ TAMEQALRQL QREDPSLRVS
YDSVTGQTVL GGMGELHMDI IKSRILSEYK IDVDLGPLQI AYKETIESPS LTTLSVEKEI
AGSKQNVSLT LEVVKDHDEL FSLDKSPENL SNLNTLRPRT LQVIRKGSVS ALERGPRVGG
QVVDTQIRLH NAIIGRGTAD SFVMATAAQC VQKLLSTSGT RLLEPIMALQ IVAPSERISG
IMADLSRRRA LINDVLPKGE RNKMILVNAP LAELSGYSSA LRTISSGTAS MTMQPSGFSG
MNAVDESLAE RRVQGLE
