RRF2M_DEBHA
ID RRF2M_DEBHA Reviewed; 860 AA.
AC B5RUN4;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=MEF2 {ECO:0000255|HAMAP-Rule:MF_03059};
GN OrderedLocusNames=DEHA2F24662g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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 -!- 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}.
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DR EMBL; CR382138; CAR66412.1; -; Genomic_DNA.
DR RefSeq; XP_002770895.1; XM_002770849.1.
DR AlphaFoldDB; B5RUN4; -.
DR SMR; B5RUN4; -.
DR STRING; 4959.XP_002770895.1; -.
DR EnsemblFungi; CAR66412; CAR66412; DEHA2F24662g.
DR GeneID; 8999064; -.
DR KEGG; dha:DEHA2F24662g; -.
DR VEuPathDB; FungiDB:DEHA2F24662g; -.
DR eggNOG; KOG0465; Eukaryota.
DR HOGENOM; CLU_002794_4_1_1; -.
DR InParanoid; B5RUN4; -.
DR OMA; AVCQIPW; -.
DR OrthoDB; 637899at2759; -.
DR Proteomes; UP000000599; Chromosome F.
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 Reference proteome.
FT CHAIN 1..860
FT /note="Ribosome-releasing factor 2, mitochondrial"
FT /id="PRO_0000385614"
FT DOMAIN 45..337
FT /note="tr-type G"
FT BINDING 54..61
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT BINDING 118..122
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT BINDING 172..175
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
SQ SEQUENCE 860 AA; 95795 MW; 26952D63D27EA84B CRC64;
MTNTGPIVRR VFRYASVLDT ICYKRGIHSS RALLSESRLN SVPPDRTRNI GIIAHIDAGK
TTTTERMLFY SGKTRRIGNV DEGDTVTDYL PSERERGITI QSAAITIPWN KNKINIIDTP
GHADFTFEVT RSLRVLDSCV TILDAVAGVE AQTEKVWKQA QALGIPKIAY VNKMDRDGAG
FSRTVKEIIQ KLQTRVVLCN IPYWETPVND VPIFKGVLDV LNKKLLKWNS DSNANGTDIS
VTDLEKEMDK YPELYEMVSK SRESMVETLG EFDETIIDSF LENDEDYMKI PVAVLNSAIK
RGTLANYVTP VFCGSSFRNI GVQPLMDAVV NFLPSPLETK VPDISSNAPK ALAKMKGKNR
KKKVTSEPTD VPLSMDPKHG LVINKNPNLT TALAFKVITH PTRGVMTFFR VYSGKLTSNT
TIMNTRTGKK LNLRKLLLMH GDEPEVVPSI SAGNIGVISG TDDDIVTGDT IVSHGPVNKP
FNDLESSLKM LPIEIPPPLF NSSIEPLTAG DTRHLNSCIQ ILLREDPSLK VSVDEDLGQI
ILSGMGELHL EIIKERLVTD MKANARLRDV AVSYKETLGK PNYKSVTQST GDNGCVSIEI
SMDSFEGLAE ESSFADEDGA IVLEHENNIV ILEPSATPEY MQTAIDERRW KSDHSLEDLQ
ESLVHGCITA LQLGGPVFGF ALHSTVIRIK NWHFPVDSKD YNSSSLLDIS RRAVTKNIKD
LGESEKDLFS LLEPIMQTKV YINSDSLGEV VHDLTHRCQA TITSIDDESE NMDALNWANE
ESERVYVPPD YTMKNTNNLQ VELRNKKVIV AETPLREMIG YLSRLRSITQ GRGVFDMSYL
GMKRVIKSRL ASISNEFNFM