RRF2M_YARLI
ID RRF2M_YARLI Reviewed; 802 AA.
AC Q6CBI0;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 124.
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=YALI0C18557g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
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; CR382129; CAG82302.1; -; Genomic_DNA.
DR RefSeq; XP_501982.1; XM_501982.1.
DR AlphaFoldDB; Q6CBI0; -.
DR SMR; Q6CBI0; -.
DR STRING; 4952.CAG82302; -.
DR EnsemblFungi; CAG82302; CAG82302; YALI0_C18557g.
DR GeneID; 2909984; -.
DR KEGG; yli:YALI0C18557g; -.
DR VEuPathDB; FungiDB:YALI0_C18557g; -.
DR HOGENOM; CLU_002794_4_1_1; -.
DR InParanoid; Q6CBI0; -.
DR OMA; AVCQIPW; -.
DR Proteomes; UP000001300; Chromosome C.
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; 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; 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 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..802
FT /note="Ribosome-releasing factor 2, mitochondrial"
FT /id="PRO_0000385623"
FT DOMAIN 13..297
FT /note="tr-type G"
FT BINDING 22..29
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT BINDING 86..90
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT BINDING 140..143
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
SQ SEQUENCE 802 AA; 88188 MW; B148F6721613C60E CRC64;
MASRHYSAKN TTKKIRNIGI IAHIDAGKTT TTERILYLSG TIKHLGNVDE GDTTMDFLPA
ERERGITIAS AATSFNWNNH TVNLIDTPGH ADFTFEVIRS IRVLDGAVCI LDGVAGVEAQ
TEKVWKQASE MGIPKIAFVN KMDRAGAGFG RTVKEIVSKL RTRVALLTVP VFSKSSDQVF
EGVVDILNGC VITWTTGGDG KQTVVVPVSE ASAEVQEEYQ KARTALVETL TELDEELVEK
FLESEDYMQI TTEDIKRALR TATINNDIVP VLCGASFRNI GVQPLMDAVV DFLPSPAERP
PTDALIAKSY TGGKKSKVIP ERAITLDDSM KNLCCALCFK VVQDPQKGTL VYVRVYKGEL
KQNSVLYNTT SGTKDRVSRL LKVHADTTSE VTSITEGNIG VILGSQGLAT GDTIVCHSIK
KDGVMKLPPD NRLIQLKPIA VPPPVFFVRI DPASIGDTRP MNEALELLLR EDPSLNVSFD
DETNQTTLSG MGELHLEIAQ NRLIEDFKAN IVIGPIIISY KETLNEPTKS ITKTVEPEPG
AVSTVRLRLE PITEMDEACE NENVIDHEQN TVSFPYELSD ADLESVGEGN QRISFERDTK
ELTPEIMEEC FRVGSIPPLV SCGPVCRLPL RSVRVVIEAW HIAQHINNTA SLKTATRLAI
MEALSTANAT LMEPIMNVYV SVNEADIGLV VKDLSGSRNG QIVSIMDPSQ LNEGDIHSEE
YVAMATNTYV PADYTMYLSK HQDQTRTQQS VVHARVPLRE MVGYLKTLRS MTQGRGSFTM
EVDQYEAVTP DKIQPIVDSI FA
