RRF2M_CANDC
ID RRF2M_CANDC Reviewed; 807 AA.
AC B9W892;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=CD36_06540;
OS Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS NRRL Y-17841) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=573826;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841;
RX PubMed=19745113; DOI=10.1101/gr.097501.109;
RA Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT Candida albicans.";
RL Genome Res. 19:2231-2244(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}.
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; FM992688; CAX44946.1; -; Genomic_DNA.
DR RefSeq; XP_002417313.1; XM_002417268.1.
DR AlphaFoldDB; B9W892; -.
DR SMR; B9W892; -.
DR STRING; 42374.XP_002417313.1; -.
DR EnsemblFungi; CAX44946; CAX44946; CD36_06540.
DR GeneID; 8045535; -.
DR KEGG; cdu:CD36_06540; -.
DR CGD; CAL0000170034; Cd36_06540.
DR eggNOG; KOG0465; Eukaryota.
DR HOGENOM; CLU_002794_4_1_1; -.
DR OrthoDB; 637899at2759; -.
DR Proteomes; UP000002605; Chromosome 1.
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..18
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT CHAIN 19..807
FT /note="Ribosome-releasing factor 2, mitochondrial"
FT /id="PRO_0000385612"
FT DOMAIN 27..315
FT /note="tr-type G"
FT BINDING 36..43
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT BINDING 100..104
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT BINDING 154..157
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
SQ SEQUENCE 807 AA; 90458 MW; 0C50ED829B98E8DC CRC64;
MFCRKYAFQT WKQFSRFYSA VNNIRASKTR NIGIIAHIDA GKTTTTERMI YYSGKIKRIG
NVDEGDTVTD YLPSERERGI TIQSAAITLP WNQHKINIID TPGHADFTFE VIRSLRVLDG
AVTILDAVAG VEAQTEKVWK QASSLNLPKI VYVNKMDRPG AGFSRTVQEV IQKLETRVVL
CNLPYFETNK ESDLEFKGVI DVIHQKLLKW NEMDANGNEI SVVDIDKTTP ELLQILEKSR
ESMVETLGEY DERIIDSFLE HDENYLKIPP ILLDQVIRKA TIDNYLTPVF CGASFRNIGV
QPLMDGITKY LPSPLETSLP EITKNGKEVP KKADDEKGLV VANDNNLTLA LAFKVMTHST
RGPMTFVRVY SGKLNAASNL INTRTGKKLL IRKLLVMHGD SPEEVKSISA GNIGVIPGYE
TDFQTGDTLV SSAVAKRNFT AKDSAYRLLP IDIPPPLFNA AIEPHTAGDE AYMKQCVETL
IREDPSLKVH LDEEMGQVVL SGMGELHLDI VRERLVNDMK AKVNLKDVVV SYKESYVGKK
EKEAVITDEE IEVVVTLSHT EDARDYIGQE GALVIEGDNN VILLSQTALS EHVQATIDER
RWKCENNLEE LKEAILNGCL TALQMGGPIL GFPLHSTLVT VKRWNAPVEQ AQEQALNLMN
ASRQAVQSLK NEEKDFSILE PIMSIKVYVD SNDLGEVSHD LTQRCKAMIV EIQDQSTQNL
ETAAWAKDEA TKVYVPPDYT IKKNVSKFDD IANKKIIVAE TPLREMIGYL SKLRALTQGR
ATFDMTLIGM RRAVGNRVDS IVEEYKF
