RRF2M_YEAS1
ID RRF2M_YEAS1 Reviewed; 819 AA.
AC B3LQ11;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
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}; ORFNames=SCRG_03569;
OS Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=285006;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM11-1a;
RG The Broad Institute Genome Sequencing Platform;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Cuomo C.,
RA Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K.,
RA LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA O'Leary S., Kodira C.D., Zeng Q., Yandava C., Alvarado L., Pratt S.,
RA Kruglyak L.;
RT "Annotation of the Saccharomyces cerevisiae RM11-1a genome.";
RL Submitted (MAR-2005) 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. 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 ---------------------------------------------------------------------------
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; CH408050; EDV12664.1; -; Genomic_DNA.
DR AlphaFoldDB; B3LQ11; -.
DR SMR; B3LQ11; -.
DR EnsemblFungi; EDV12664; EDV12664; SCRG_03569.
DR HOGENOM; CLU_002794_4_1_1; -.
DR Proteomes; UP000008335; 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; IEA:UniProtKB-UniRule.
DR GO; GO:0032543; P:mitochondrial translation; IEA:UniProtKB-UniRule.
DR GO; GO:0032790; P:ribosome disassembly; IEA:UniProtKB-UniRule.
DR CDD; cd16262; EFG_III; 1.
DR CDD; cd03713; EFG_mtEFG_C; 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; 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 Pfam; PF03144; GTP_EFTU_D2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SMART; SM00838; EFG_C; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52540; SSF52540; 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 Transit peptide.
FT TRANSIT 1..30
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT CHAIN 31..819
FT /note="Ribosome-releasing factor 2, mitochondrial"
FT /id="PRO_0000385624"
FT DOMAIN 39..327
FT /note="tr-type G"
FT BINDING 48..55
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT BINDING 113..117
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT BINDING 165..168
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
SQ SEQUENCE 819 AA; 91283 MW; DDACCD85FC6F6798 CRC64;
MWKWNVRRWA GARVNISKNR LSVINVGSRY LSTARSPLSK VRNIGIIAHI DAGKTTTTER
MLYYAGISKH IGDVDTGDTI TDFLEQERSR GITIQSAAIS FPWRNTFAIN LIDTPGHIDF
TFEVIRALKV IDSCVVILDA VAGVEAQTEK VWKQSKSKPK ICFINKMDRM GASFNHTVND
LINKFMRGTT TKPVLVNIPY YRKQPTSNDY VFQGVIDVVN GKRLTWNPEN PDEIIVDELD
GTSLEQCNRC RESMIETLTE YDEDLVQHFL EEAEGDYSKV SAQFLNASIR KLTMKNMIVP
VLCGASFKNI GVQPLLDAIV NYLPSPIEAE LPELNDKTVP MKYDPKVGCL VNNNKNLCIA
LAFKVITDPI RGKQIFIRIY SGTLNSGNTV YNSTTGEKFK LGKLLIPHAG TSQPVNILTA
GQIGLLTGST VENNISTGDT LITHSSKKDG LKSLDKKKEL TLKINSIFIP PPVFGVSIEP
RTLSNKKSME EALNTLITED PSLSISQNDE TGQTVLNGMG ELHLEIAKDR LVNDLKADVE
FGQLMVSYKE TINSETNIET YESDDGYRFS LSLLPNSDAL PNCLAYPLGV NENFLIMEKN
GNWDKEWKYQ VSFESILNSI IASCIVGLQR GGKIANFPLY ACSIKINSDW SVPPDIETPQ
EILKITRNLI FKALNDLKPE KYNLLEPIMN LDLTIPQSDV GTVLQDLTGA RKAQILSIED
ESSVSNSGAS TCNSPENSNR IYIPSDAVTT LHATKDKKNT QETSSNVKKI IKAKVPLREI
TTYTNKLRSL SQGRGEFNIE YSDMEKVTND RLQSILHDL