RRF2M_LODEL
ID RRF2M_LODEL Reviewed; 826 AA.
AC A5DTX8;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=LELG_00814;
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC YB-4239;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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; CH981524; EDK42636.1; -; Genomic_DNA.
DR RefSeq; XP_001528294.1; XM_001528244.1.
DR AlphaFoldDB; A5DTX8; -.
DR SMR; A5DTX8; -.
DR STRING; 379508.A5DTX8; -.
DR EnsemblFungi; EDK42636; EDK42636; LELG_00814.
DR GeneID; 5234768; -.
DR KEGG; lel:LELG_00814; -.
DR VEuPathDB; FungiDB:LELG_00814; -.
DR eggNOG; KOG0465; Eukaryota.
DR HOGENOM; CLU_002794_4_1_1; -.
DR InParanoid; A5DTX8; -.
DR OMA; AVCQIPW; -.
DR OrthoDB; 637899at2759; -.
DR Proteomes; UP000001996; 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 Reference proteome; Transit peptide.
FT TRANSIT 1..44
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT CHAIN 45..826
FT /note="Ribosome-releasing factor 2, mitochondrial"
FT /id="PRO_0000385617"
FT DOMAIN 53..340
FT /note="tr-type G"
FT BINDING 62..69
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT BINDING 126..130
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT BINDING 180..183
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
SQ SEQUENCE 826 AA; 92269 MW; 9459300F16EBC88C CRC64;
MIVRNLLGKN RLCCLQPKLL LSTLSQRPQL QLSLQLLCRA TRLYATVNDI ALPKTRNIGI
IAHIDAGKTT TTERMIYYSG KSKRIGNVDE GDTVTDYLQA ERERGITIQL AAITIPWNNH
KINIIDTPGH ADFTFEVIRS LRVLDGAVTI LDAVAGVEAQ TEKVWKQASA LKLPRMIYVN
KMDRPGAGFS RTVKEVIQKL ETRVVLCNTP FFENQELNPE FRGVIDVIHG KLLKWKEADE
FGKEIDVEDI DETKPELYDV YCKAREYMVE TLGEYDESII DAFLENDENY LKISPELLNR
AIRKATIDNY LVPVFCGASF RNIGVQPLMD GITNYLPSPL ETPVPDIKSK KKQEISAKMA
NNGLIINNDP KLTVGLVFKV MNHATRGPMA FVRIYSGKLV ANSMVVNSRT GAKHSVRKLL
IMHGDQPEEV KFIGAGNIGV ISGFEDEFHT GDTVISHATS KKAVGTMEST IKLMPIDIPP
PLFNSSIEPF TAGDEAHMKK CIDILIREDP SLKVHTEEDM GQTILSGMGE LHLEIVRDRL
INDMKVKANL RDIAVAYKES YIGKTPTNGL FETESIQVKL SIEHVDDCKS FEDVDGAIIF
EDQNNVIIVP ESLASETVQS ATEGRRWKCP SSYEELHEAV VNGCSMALQT GGPHLGLSLH
STLVKVEFWN APVEVNEELI PPLMNAAREA VQSVKASENK FGFLEPLMNV RVFVDSADMG
EVSHDLSQRC QALIHSVEDE SLLNLETANW AKDEAERAYL PPDYTMSKTA LADNYKTRKV
IHAETPLKEM IGYLSKLRSL TGGKATFDMS FLGMRRVTQS RLNQIF
