RRF2M_RAT
ID RRF2M_RAT Reviewed; 779 AA.
AC Q5BJP6;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 2.
DT 03-AUG-2022, entry version 113.
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};
GN Name=Gfm2; Synonyms=Efg2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 38-779.
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 -!- MISCELLANEOUS: This protein may be expected to contain an N-terminal
CC transit peptide but none has been predicted. {ECO:0000255|HAMAP-
CC 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 ---------------------------------------------------------------------------
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; CH473955; EDM10129.1; -; Genomic_DNA.
DR EMBL; BC091392; AAH91392.1; -; mRNA.
DR AlphaFoldDB; Q5BJP6; -.
DR SMR; Q5BJP6; -.
DR STRING; 10116.ENSRNOP00000043087; -.
DR PaxDb; Q5BJP6; -.
DR PRIDE; Q5BJP6; -.
DR UCSC; RGD:1309854; rat.
DR RGD; 1309854; Gfm2.
DR eggNOG; KOG0464; Eukaryota.
DR InParanoid; Q5BJP6; -.
DR PhylomeDB; Q5BJP6; -.
DR Reactome; R-RNO-5419276; Mitochondrial translation termination.
DR PRO; PR:Q5BJP6; -.
DR Proteomes; UP000002494; Unplaced.
DR Proteomes; UP000234681; Chromosome 2.
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.
FT CHAIN 1..779
FT /note="Ribosome-releasing factor 2, mitochondrial"
FT /id="PRO_0000385594"
FT DOMAIN 68..353
FT /note="tr-type G"
FT BINDING 77..84
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT BINDING 141..145
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT BINDING 195..198
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT CONFLICT 616
FT /note="M -> L (in Ref. 2; AAH91392)"
FT /evidence="ECO:0000305"
FT CONFLICT 628
FT /note="I -> V (in Ref. 2; AAH91392)"
FT /evidence="ECO:0000305"
FT CONFLICT 778
FT /note="V -> M (in Ref. 2; AAH91392)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 779 AA; 85914 MW; D19A8B83F751F2B0 CRC64;
MFTNWRIFAV NRQKTFSVHI HTTCYCKIKA NLKRSKTQVP LTRSYSSPPG IVGNEVKSLH
SIINPPVAKI RNIGIMAHID AGKTTTTERI LYYSGYTRSL GDVDDGDTVT DFMAQERERG
ITIQSAAVTL DWKGYRVNLI DTPGHVDFTL EVERCLRVLD GAVAVFDASA GVEAQTLTVW
RQADKHKIPR ICFLNKMDKT GASFNYAVES IREKLKAKPL ILQLPIGEAR TFQGVVDVVN
REKLIWNSDS DDGKDFERKP LSEASDPTLL KETVEARNSL IEQVADLDDE FADLVLGEFS
EDFDLVPAEK LQAAIHRVTL AQAAVPVLCG SALKNKGVQP LLDAVTTYLP SPEEREHGFL
QWYKGDLCAL AFKVLHDKQR GPLVFLRIYS GTLTPQSAVH NVNRNCTERM SRLLLPFADQ
HVEIPSLTAG NIALTVGLKQ TATGDTIVSS KSSALAAARR AGKGERKPGR ISEAESVLLA
GVEIPEPVFF CTIEPPSAAK QPDLDHALEH LQREDPSLKV KLDPDSGQTV LCGMGELHIE
IIHDRIKREY GLETYLGPLQ VAYRETILNS VRATDTLDRV LGDKRHFARA ELEVRPAEEP
CGVATIEYAD SVGEDMLQAP REDIENAIHS ACLQGPLLGS PIQDVAVTLH SLMIHPGTST
TMVTACISRC VQKALKKADK QVLEPLMSLE VTVSREYLSP VLADLAQRRG NIQEIQTRQD
NKVVLGFVPL AEIMGYSTVL RTLTSGSATF ALELSTYQAM SPQDQRTLLS QRSGLARVL
