RRF2M_DROME
ID RRF2M_DROME Reviewed; 740 AA.
AC Q9VCX4; D3KU70; F1JZV4;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 3.
DT 03-AUG-2022, entry version 169.
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 AltName: Full=Elongation factor G2 {ECO:0000303|PubMed:20132446};
DE AltName: Full=Ribosome-recycling factor 2, mitochondrial {ECO:0000312|FlyBase:FBgn0051159};
DE Flags: Precursor;
GN Name=mRRF2 {ECO:0000312|FlyBase:FBgn0051159};
GN Synonyms=EF-G2 {ECO:0000303|PubMed:20132446};
GN ORFNames=CG31159 {ECO:0000312|FlyBase:FBgn0051159};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=20132446; DOI=10.1111/j.1365-2958.2010.07067.x;
RA Suematsu T., Yokobori S., Morita H., Yoshinari S., Ueda T., Kita K.,
RA Takeuchi N., Watanabe Y.;
RT "A bacterial elongation factor G homologue exclusively functions in
RT ribosome recycling in the spirochaete Borrelia burgdorferi.";
RL Mol. Microbiol. 75:1445-1454(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryo;
RX PubMed=21364917; DOI=10.1371/journal.pone.0016799;
RA Trivigno C., Haerry T.E.;
RT "The Drosophila mitochondrial translation elongation factor G1 contains a
RT nuclear localization signal and inhibits growth and DPP signaling.";
RL PLoS ONE 6:E16799-E16799(2011).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAI79334.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB514521; BAI79334.1; ALT_INIT; mRNA.
DR EMBL; JF309280; ADZ24788.1; -; mRNA.
DR EMBL; AE014297; AAF56031.3; -; Genomic_DNA.
DR RefSeq; NP_732771.2; NM_170028.3.
DR AlphaFoldDB; Q9VCX4; -.
DR SMR; Q9VCX4; -.
DR IntAct; Q9VCX4; 4.
DR STRING; 7227.FBpp0083663; -.
DR PaxDb; Q9VCX4; -.
DR EnsemblMetazoa; FBtr0084270; FBpp0083663; FBgn0051159.
DR GeneID; 42670; -.
DR KEGG; dme:Dmel_CG31159; -.
DR UCSC; CG31159-RA; d. melanogaster.
DR CTD; 42670; -.
DR FlyBase; FBgn0051159; mRRF2.
DR VEuPathDB; VectorBase:FBgn0051159; -.
DR eggNOG; KOG0464; Eukaryota.
DR GeneTree; ENSGT00550000074890; -.
DR HOGENOM; CLU_002794_4_1_1; -.
DR InParanoid; Q9VCX4; -.
DR OMA; AVCQIPW; -.
DR OrthoDB; 637899at2759; -.
DR PhylomeDB; Q9VCX4; -.
DR Reactome; R-DME-5419276; Mitochondrial translation termination.
DR BioGRID-ORCS; 42670; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 42670; -.
DR PRO; PR:Q9VCX4; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0051159; Expressed in egg cell and 19 other tissues.
DR ExpressionAtlas; Q9VCX4; baseline and differential.
DR Genevisible; Q9VCX4; DM.
DR GO; GO:0005739; C:mitochondrion; ISS:FlyBase.
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 2: Evidence at transcript level;
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..740
FT /note="Ribosome-releasing factor 2, mitochondrial"
FT /id="PRO_0000385601"
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"
FT CONFLICT 425
FT /note="A -> T (in Ref. 1; BAI79334)"
FT /evidence="ECO:0000305"
FT CONFLICT 441
FT /note="A -> D (in Ref. 1; BAI79334)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 740 AA; 81961 MW; DFFB8B9C97DE63F7 CRC64;
MLKYAWQSGP KQSNRWLWHL SNQIWKRSYS SKIRNIGILA HIDAGKTTTT ERMLFYAGKT
RALGEVHRGN TVTDYLTQER ERGITICSSA VTFSWNDHRI NLLDTPGHID FTMEVEQSLY
AVDGVVVVLD GTAGVEAQTV TVWSQADKHK LPRLIFVNKM DRPDADFEKC VSDLKDKLET
QPVCLQYPVK NEDGVLAIND VITLERLSWQ QKDLGRSYRN VKLEPSDDLR LLQEKRNELI
DQLSGLDDEL ADVVISTESF DNVDNALIER ALRRATTQQK VVPVLLGSAY KNVGIQRLMD
AVNAYLPAPE ERNQIYDCFG TEVAGKVFKI VHDKQRGPLT LVRILRGEIK RGMRLISARG
QAEVVSKLYE PLADEYREVS AVQSGDVVIC AGLKSTVTGD LLTSSQSALK NAQKRYKQSL
GNTAAKVEED DELDESDELF AIDPQIPDAV YFCSIEPPSV SSQTAMEQAL KQLQREDPSL
RVSYDSVTGQ TVLGGMGELH MDIIKSRILS EYKIDVDLGP LQIAYKETIE APALTTLSVE
KEIAGSKQSV SITLEVVKNQ AELFSLDKSP DNLPNLNTLR PRILQVLRKG SISALERGPR
VGGQVVETQI RLHNATIGRG TADSFVMATA AQCVQKLLST SGTRLLEPIM ALQIVAPSER
ISGIMADLSR RRALINDVLP KGERNKMILV NAPLAELSGY SSALRTISSG TASMTMQPCG
FSSMNSVDES LAERRAQGLE
