ID RRF2M_EREGS Reviewed; 835 AA.
AC Q754I9;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 24-JAN-2024, entry version 136.
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=MEF2 {ECO:0000255|HAMAP-Rule:MF_03059}; OrderedLocusNames=AFR085W;
OS Eremothecium gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL
OS Y-1056) (Yeast) (Ashbya gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016819; AAS53456.1; -; Genomic_DNA.
DR RefSeq; NP_985632.1; NM_210986.1.
DR AlphaFoldDB; Q754I9; -.
DR SMR; Q754I9; -.
DR STRING; 284811.Q754I9; -.
DR EnsemblFungi; AAS53456; AAS53456; AGOS_AFR085W.
DR GeneID; 4621875; -.
DR KEGG; ago:AGOS_AFR085W; -.
DR eggNOG; KOG0465; Eukaryota.
DR HOGENOM; CLU_002794_4_1_1; -.
DR InParanoid; Q754I9; -.
DR OMA; GPQFTFP; -.
DR OrthoDB; 148165at2759; -.
DR Proteomes; UP000000591; Chromosome VI.
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; IBA:GO_Central.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IEA:EnsemblFungi.
DR GO; GO:0032543; P:mitochondrial translation; IBA:GO_Central.
DR GO; GO:0051881; P:regulation of mitochondrial membrane potential; IEA:EnsemblFungi.
DR GO; GO:0032790; P:ribosome disassembly; IBA:GO_Central.
DR CDD; cd01886; EF-G; 1.
DR CDD; cd16262; EFG_III; 1.
DR CDD; cd03713; EFG_mtEFG_C; 1.
DR Gene3D; 3.30.70.240; -; 1.
DR Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 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; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43261:SF1; RIBOSOME-RELEASING FACTOR 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43261; TRANSLATION ELONGATION FACTOR G-RELATED; 1.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF14492; EFG_III; 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 SUPFAM; SSF54980; EF-G C-terminal domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 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..50
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT CHAIN 51..835
FT /note="Ribosome-releasing factor 2, mitochondrial"
FT /id="PRO_0000385608"
FT DOMAIN 57..343
FT /note="tr-type G"
FT BINDING 66..73
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT BINDING 131..135
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT BINDING 183..186
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
SQ SEQUENCE 835 AA; 92559 MW; B55C5B55E24560C4 CRC64;
MPWCNTRLRT CGASPKIFLR RVRCPVLLHN WTIGRVSSVS KMILRFLRSY SKRVDITRVR
NIGIIAHIDA GKTTTTERML YYSGKIKRIG DVDHGDTITD FLPQERSRGI TIQSAAISFN
WRDNYTVNLI DTPGHADFTF EVIRSLRVLD GCVTILDAVA GVEAQTEKVW KQAAEIPKVC
FINKMDRVGA GYSRAVKELI VKLKTRVLLL NTPLFAARDS SADPVFVGVL DAVNGQLLEW
DPEDPDKISA KAVDKECAHY EELVSAREAL VETLSEVDEK LVEYFLGEAD GDYMKVPVEV
LNESIRRATL SQYAVPVLCG ASFKNIGVQP LLDAVVDYLP SPAEARLPEL SNKDLPVQHH
LKNGLLVNKN ANLCLALAFK VTTDPIRGAM VFIRVYSGVL NSGHTVYNSS TGVKFKLGKL
IKMHANVAED IKSLHPGDIG VLAGANVADH VRTGDTIVAH CTSKDGIRSF KKAELALRIH
PIDIPPPVFS AAVEPRTLGN KKAMDESLTQ LTREDPSLVI VRDEETGQTV MNGMGELHLE
IAADRLLNEF KAPVRVGKVA VSYKETINTA TETKHSETDD GYSFELEVRQ YNEEDKVLFS
NGWYPLGSDN NYLVIDPNPR FNEDNWPFPL KYEAFVNSII SCCIVALQRG GKTAGFPLHS
CVIHVKRWRL PLDCAAAASI LLTVRPLIIS ALTSLPTSAF SILEPIMNVE VTVQQQDLGS
VVQDLTGARK ANILSIDDEH HWADAAVTDK DVHLFHDIAE KQYLPPDSTV FQAKLNKEGQ
TGKIVKAHVP LKEMVSYMNK LRMLTKGRGS FHMSYLGMER ASSDRVDGIL EDADL
//
