RRF2M_DROER
ID RRF2M_DROER Reviewed; 718 AA.
AC B3P8M3;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-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=GG11151;
OS Drosophila erecta (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7220;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14021-0224.01;
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; CH954182; EDV54118.1; -; Genomic_DNA.
DR RefSeq; XP_001982248.2; XM_001982212.2.
DR AlphaFoldDB; B3P8M3; -.
DR SMR; B3P8M3; -.
DR STRING; 7220.FBpp0129697; -.
DR eggNOG; KOG0464; Eukaryota.
DR HOGENOM; CLU_002794_4_1_1; -.
DR OMA; AVCQIPW; -.
DR PhylomeDB; B3P8M3; -.
DR Proteomes; UP000008711; 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 Transit peptide.
FT TRANSIT 1..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT CHAIN 30..718
FT /note="Ribosome-releasing factor 2, mitochondrial"
FT /id="PRO_0000385599"
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 718 AA; 79695 MW; F456BBF1BDA7B0A0 CRC64;
MLKCAWQNGP RQSNRWLWQL SNQIWKRSYS SKIRNIGILA HIDAGKTTTT ERMLFYAGKT
RALGEVHRGN TVTDYLTQER ERGITICSSA VTFPWNDHRI NLLDTPGHID FTMEVEQSLY
AVDGVVVVLD GTAGVEAQTV TVWSQADKHK LPRLIFVNKM DRPDADFVKC VSDLKDKLET
QPVCLQYPVK NEDGQLAIND VIHLERLSWQ QKDLGRSYKN VKLEPSDDLR QLQEKRNELI
DQLSGLDDEL ADVVISTESF DKVDNALIER ALRRATTQQK VVPVLLGSAY KNVGIQRLMD
AVNSYLPAPE ERNQIYDCFG TEVAGKVFKI VHDKQRGPLT LVRILRGEIK RGMRLISARG
QAEVVSKLYE PLADEYREVS AVQSGDVVIC AGLKSTVTGD LLTSSEEDDE FDESHELFAI
DPQIPDAVYF CSIEPPSVSS QTAMEQALKQ LQREDPSLRV SYDSVTGQTV LGGMGELHMD
IIKSRILSEY KIDVDLGPLQ IAYKEAIESP ALTTLSVEKE IAGSKQSVSI TLEVVKNQAE
LFSLDKSPEN LPNLNTLRPR ILQVLRKGSI SALERGPRVG GQVVETQIRL HNATIGRGTA
DSFVMATASQ CVQKLLSTSG TRLLEPIMAL QIVAPSERIS GIMADLSRRR ALINDVLPKG
ERNKMILVNA PLAELSGYSS ALRTISSGTA SMTMQPCGFS SMNSVDESLA ERRAQGLE
