RRF2M_DANRE
ID RRF2M_DANRE Reviewed; 762 AA.
AC A0JMI9; A2BHE0; Q4VBG9;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 2.
DT 03-AUG-2022, entry version 104.
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=gfm2; Synonyms=efg2; ORFNames=si:dkey-35i22.3, zgc:153835;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Mitochondrial GTPase that mediates the disassembly of
CC ribosomes from messenger RNA at the termination of mitochondrial
CC protein biosynthesis. Acts in collaboration with mrrf. GTP hydrolysis
CC follows the ribosome disassembly and probably occurs on the ribosome
CC large subunit. 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=CAM16014.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; BX571730; CAM16014.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC095886; AAH95886.1; -; mRNA.
DR EMBL; BC125896; AAI25897.1; -; mRNA.
DR RefSeq; NP_001071013.1; NM_001077545.1.
DR AlphaFoldDB; A0JMI9; -.
DR SMR; A0JMI9; -.
DR STRING; 7955.ENSDARP00000006504; -.
DR PaxDb; A0JMI9; -.
DR PeptideAtlas; A0JMI9; -.
DR PRIDE; A0JMI9; -.
DR Ensembl; ENSDART00000016314; ENSDARP00000006504; ENSDARG00000005561.
DR GeneID; 558184; -.
DR KEGG; dre:558184; -.
DR CTD; 84340; -.
DR ZFIN; ZDB-GENE-060201-3; gfm2.
DR eggNOG; KOG0464; Eukaryota.
DR GeneTree; ENSGT00550000074890; -.
DR HOGENOM; CLU_002794_4_1_1; -.
DR InParanoid; A0JMI9; -.
DR OMA; AVCQIPW; -.
DR OrthoDB; 637899at2759; -.
DR PhylomeDB; A0JMI9; -.
DR TreeFam; TF314848; -.
DR Reactome; R-DRE-5419276; Mitochondrial translation termination.
DR PRO; PR:A0JMI9; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 5.
DR Bgee; ENSDARG00000005561; Expressed in somite and 27 other tissues.
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; IPR004161; EFTu-like_2.
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 InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF14492; EFG_III; 1.
DR Pfam; PF03764; EFG_IV; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SMART; SM00838; EFG_C; 1.
DR SMART; SM00889; EFG_IV; 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..35
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT CHAIN 36..762
FT /note="Ribosome-releasing factor 2, mitochondrial"
FT /id="PRO_0000385595"
FT DOMAIN 54..341
FT /note="tr-type G"
FT BINDING 63..70
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT BINDING 127..131
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT BINDING 181..184
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT CONFLICT 246
FT /note="I -> V (in Ref. 2; AAH95886)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="D -> E (in Ref. 2; AAH95886/AAI25897)"
FT /evidence="ECO:0000305"
FT CONFLICT 456
FT /note="R -> M (in Ref. 2; AAH95886/AAI25897)"
FT /evidence="ECO:0000305"
FT CONFLICT 556
FT /note="A -> V (in Ref. 2; AAI25897)"
FT /evidence="ECO:0000305"
FT CONFLICT 637
FT /note="N -> D (in Ref. 2; AAH95886/AAI25897)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 762 AA; 83643 MW; 4BDFB2427D11278A CRC64;
MLLSLTFPVL RGCTGHLVNR SLQAPRWRVT WKRSYSLLQD EVKSLRTVVN PDISKIRNIG
IMAHIDAGKT TTTERMLYYS GYTRALGDVD DGDTVTDYMA QERERGITIQ SAAVTFDWKD
YRINLIDTPG HVDFTLEVER ALRVLDGAVA VFDASAGVEA QTMTVWRQAE KHQIPCVCFL
NKMDKPAASL RYSLDSIKAK LKANPVLLQI PIGSGKSFTG LVDLITRQKM MWQGNALTND
GRSFEINSLQ PSDDPNVLLA VSEARAALIE QVADLDDDFA ELLLGEYGEN FDAVPAVKLQ
EAVRRVTLAR KGVPVLCGSS LKNKGVQPLL DAITAYLPAP NERNHDLVRW YKNDLCALAF
KVVHDKQRGP LVFVRIYSGS MKAQSSVHNI NRNETEKMSR LLLPFADQQI EIPSLSAGNI
ALTVGLKQTV TGDTIVSSKA SAAAAIRRAQ AEAESRSNSH SAALAGVEVP EPVFFCSIEP
PTMAKQADLE HALNCLQRED PSLKVRIDPD SGQTVLCGMG ELHIEIIHDR IKREYKIETH
LGPLQVAYRE TILQSATAKD LLDRILGEKR HVVSVELTVH PLKENSSASC DITFEEDVKA
MLPADVREAV ENGVQSAYLQ GPVLGFPVQG VQTVIQNVRL ESGTSAAMVS ACVSRCMLKA
LKQAGGQVLE PVMALEVTVG EEHLSSVLAD LSQRRGTICD IQSRQDNKIL LADVPLAEMM
GYSTVLRTLT SGNATFSLEL SSYEPMNSQD QNILLNKMAG LT
