RRF2M_DROVI
ID RRF2M_DROVI Reviewed; 712 AA.
AC B4M416;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=GJ10848;
OS Drosophila virilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7244;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15010-1051.87;
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; CH940652; EDW59377.1; -; Genomic_DNA.
DR RefSeq; XP_002056265.2; XM_002056229.2.
DR AlphaFoldDB; B4M416; -.
DR SMR; B4M416; -.
DR STRING; 7244.FBpp0225265; -.
DR GeneID; 6633042; -.
DR KEGG; dvi:6633042; -.
DR eggNOG; KOG0464; Eukaryota.
DR HOGENOM; CLU_002794_4_1_1; -.
DR InParanoid; B4M416; -.
DR OMA; AVCQIPW; -.
DR PhylomeDB; B4M416; -.
DR Proteomes; UP000008792; 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..28
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT CHAIN 29..712
FT /note="Ribosome-releasing factor 2, mitochondrial"
FT /id="PRO_0000385605"
FT DOMAIN 30..309
FT /note="tr-type G"
FT BINDING 39..46
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT BINDING 103..107
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT BINDING 157..160
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
SQ SEQUENCE 712 AA; 78679 MW; 4D3BFC43067EE6BA CRC64;
MQYSLLSAQL RCSRFLLRQQ APFINRCYSD DIRNIGILAH IDAGKTTTTE RMLYYAGKTR
SLGEVHRGNT VTDYLTQERE RGITICSSAV TFAWNGKRIN LLDTPGHIDF TMEVEQSLYA
VDGVIVVLDG TAGVEAQTVT VWTQADNHRL PRLVFVNKMD RSDAIFDKCI DDLKAKLDAK
PICTQLPAKN VDGQLGIYDV ITLEQLTWQQ NDFGRTYSIN KLESSSEIRE LREKRNELID
QLSGVDDELA EVVISTESFD KVSNELIVQA LRRATCQQKV VPVLLGSAYK NIGIQRVMDA
VNAYLPTPNE RNQIYNCFGG ELKRGMRVLS SRGQAEVISK IYEPLADEYR EVSSVRAGDV
AICAGLKSTV TGDLLTTSHT SLKNAQKRLI QSLDATSPQY DEDEVDVNQE LFSIEPKIPD
AVYFCSIEPP SLSTQTAMEQ ALKQLQREDP SLRVNYDTVT GQTVLGGMGE LHMEIIKSRL
LSEYKIDVDL GPLQIAYKEA IETPAITTLS VEKDIAGSKQ NVNITLQLTN NQTELFSLDK
SPENVQNLNA LRPRVLQVLR KGAIGALERG PRVGGQVVDT QIRLHNVTVG RGTADSFVMA
AAAQCVQKLL SKSGTRLLEP IMAMQIVAPN ERVSGIIADL SRRRALIKDV MPKGDRNKLI
LVNAPLAELS GYSSALRTIS SGTASMTMQP CGFSEMNAAD ETLAVRRAQG LD
