RRF2M_DROAN
ID RRF2M_DROAN Reviewed; 741 AA.
AC B3M011;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=GF18865;
OS Drosophila ananassae (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7217;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14024-0371.13;
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; CH902617; EDV44201.1; -; Genomic_DNA.
DR RefSeq; XP_001955640.1; XM_001955604.2.
DR AlphaFoldDB; B3M011; -.
DR SMR; B3M011; -.
DR STRING; 7217.FBpp0122057; -.
DR EnsemblMetazoa; FBtr0123565; FBpp0122057; FBgn0095879.
DR GeneID; 6501630; -.
DR KEGG; dan:6501630; -.
DR eggNOG; KOG0464; Eukaryota.
DR HOGENOM; CLU_002794_4_1_1; -.
DR InParanoid; B3M011; -.
DR OMA; AVCQIPW; -.
DR OrthoDB; 637899at2759; -.
DR PhylomeDB; B3M011; -.
DR Proteomes; UP000007801; 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..741
FT /note="Ribosome-releasing factor 2, mitochondrial"
FT /id="PRO_0000385598"
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 741 AA; 82094 MW; 9B816C67E43D228A CRC64;
MLKYEFLHGL QKRSHYLRQL SGQFFSRSYS SKIRNIGILA HIDAGKTTTT ERMLFYAGKT
RTLGEVHRGN TVTDYLTQER ERGITICSSA VTFAWNGHRI NLLDTPGHID FTMEVEQSLY
AVDGVVVVLD GTAGVEAQTV TVWTQADKHK LPRLIFVNKM DRPDADFEKC IADLKEKLEA
HPVCLQYPVK NEDGVLAIND VITLERLTWQ QKDLGQKYIR MKLEPSDELR DLQEKRNELI
DRLSGVDDEL ADVVISTESF DKVDNHLIER ALRRATGQLK VVPVLLGSAY KNVGIQRLMD
AVNSYLPAPE ERNQIYDCFG SEVAGKVFKI VHDKQRGALT LVRILRGEIK KGMRLISARG
QAEVVSKLYE PLADEYREVN AVQSGDVVIC AGLKSTVTGD LLTSSQSTLK NAQKRLKQSL
GTTESVIPEL DDESEESEDM FGLDPQIPDA VYFCSIEPPS ISSQTAMEQA LRQLQREDPS
LRVSYDSVTG QTVLGGMGEL HMDIIKSRIL SEYKIDVDLG PLQIAYKETI ESPALTTLSV
EKEIAGAKQN VSITLELVKD KSEIFSLDKS PENMPNLNTL RPRILQVLKK GAIGALERGP
RVGGQVVDTQ IRLHNATIGR GTADSFVMAT AAQCVQKVLS TSGTRLLEPI MSLQIVAPSE
RISGIMADLS RRRAQINDVL PKGERNKMIL VNAPLAELSG YSSALRTISS GTASMTMQPC
GFSAMNSVDE SQAERRAQGL E
