RRF2M_DROGR
ID RRF2M_DROGR Reviewed; 734 AA.
AC B4JSI3;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-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=GH22468;
OS Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Hawaiian Drosophila.
OX NCBI_TaxID=7222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15287-2541.00;
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; CH916373; EDV94723.1; -; Genomic_DNA.
DR RefSeq; XP_001993987.1; XM_001993951.1.
DR AlphaFoldDB; B4JSI3; -.
DR SMR; B4JSI3; -.
DR STRING; 7222.FBpp0156374; -.
DR EnsemblMetazoa; FBtr0157882; FBpp0156374; FBgn0129926.
DR GeneID; 6567460; -.
DR KEGG; dgr:6567460; -.
DR eggNOG; KOG0464; Eukaryota.
DR HOGENOM; CLU_002794_4_1_1; -.
DR InParanoid; B4JSI3; -.
DR OMA; AVCQIPW; -.
DR OrthoDB; 637899at2759; -.
DR PhylomeDB; B4JSI3; -.
DR Proteomes; UP000001070; 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..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT CHAIN 26..734
FT /note="Ribosome-releasing factor 2, mitochondrial"
FT /id="PRO_0000385600"
FT DOMAIN 27..303
FT /note="tr-type G"
FT BINDING 36..43
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT BINDING 100..104
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT BINDING 154..157
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
SQ SEQUENCE 734 AA; 81007 MW; C6DD5E85E78E869C CRC64;
MLQYCLLRRY RFLLRQHAQV IKRCYSGDIR NIGILAHIDA GKTTTTERML FYAGKTRSLG
EVHRGNTVTD YLAQERERGI TICSSAVTFN WNGKRINLLD TPGHIDFTME VEQSLYAVDG
VIVVLDGTAG VEAQTVTVWT QADKHKLPRL VFVNKMDRPD ANFEKCIVDL TEKLDAKPIC
TQYPTKSADG QLGIFDVITM EQMTWQQNDL GRNYSKVKLE SSTELQEKRN ELIDQLSGLD
DELADVVIST ESFDKVSNEL IGQALRRATC QQKVVPVLLG SAYKNIGIQP LMDAVNAYLP
MPEERNQMYD CFGNDFAGKV FKIVHDKQRG PLTLVRLLRG ELKRGMRLLC SARGQAEVVS
KIYEPLADEY REVGSMQAGD VAICAGLKST VTGDLLTSSH TSLKNAQKRL LQSRGAAMPQ
DEDEVLDDAS HELFSIEPKI PDAVYFCSIE PPSISSQTAM EQALKQLQRE DPSLRVSYDS
VTGQTVLGGM GELHMDIIKS RMLSEYKIDV DLGPLQIAYK ETLGSSAITT LSVDKDIAGS
KQSVSITLQL VSDQRELFSL DKSPENVQHL NALRPRILGV LRKGAVSALE RGPRVGGQVV
DTQIRLHNVT VGRGTADSFV MAAAAQCVQK LLITSGTRLL EPIMAIQIVA PNERISGIMA
DLSRRRALIR DVTSKGDRNK IILVNAPLAE LSGYSSALRT ISSGTASMTM QPCGFSEMNT
ADESLAVRRA QGLD
