RRF2M_PICGU
ID RRF2M_PICGU Reviewed; 837 AA.
AC A5DB27;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 88.
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=PGUG_00482;
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
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; CH408155; EDK36384.2; -; Genomic_DNA.
DR RefSeq; XP_001487105.1; XM_001487055.1.
DR AlphaFoldDB; A5DB27; -.
DR SMR; A5DB27; -.
DR STRING; 4929.XP_001487105.1; -.
DR EnsemblFungi; EDK36384; EDK36384; PGUG_00482.
DR GeneID; 5129600; -.
DR KEGG; pgu:PGUG_00482; -.
DR VEuPathDB; FungiDB:PGUG_00482; -.
DR eggNOG; KOG0465; Eukaryota.
DR HOGENOM; CLU_002794_4_1_1; -.
DR InParanoid; A5DB27; -.
DR OMA; AVCQIPW; -.
DR OrthoDB; 637899at2759; -.
DR Proteomes; UP000001997; 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..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT CHAIN 30..837
FT /note="Ribosome-releasing factor 2, mitochondrial"
FT /id="PRO_0000385619"
FT DOMAIN 40..331
FT /note="tr-type G"
FT REGION 338..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 49..56
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 167..170
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
SQ SEQUENCE 837 AA; 92327 MW; 827F8EC7752AA82D CRC64;
MFSINARTKV PIWVPFIARK GFSMSTRQLA EPKLNQVSSL NTRNIGIIAH IDAGKTTTTE
RMLFYSGKTT TMGDVDQGDT VTDYLPSERS RGITIQSAAI TIPWNNNKIN IIDTPGHADF
TFEVIRSLRV LDGCVTILDA VAGVEAQTEK VWKQAQALKI PRIAFVNKMD RPGAGFSRTV
KEVVQKLQTK VVLCNIPYFE MSKDDAVFVG VIDILHNKIL KWNIDEDPNG RDITVIDLQE
AKESHQEAYM EALKCRESMV ETLGGIEETV VDAFLECDED YMKIPSSILK SAIRKACISN
QVTPVFCGSA FRKIAVQPLL DGVVDYLPSP LQTPVPEITA STSKVSKKQK QKKNSKVSSV
PIEMNPKKGL IVNKNPQLTV ALAFKVMTHA TRGVMTFFRV YSGSLTSNTT VVNTRTGKKL
HLNKVLLMHG DTPEPVSQIS SGNIGVITGT ENDVITGDTL VSHGPVKRNF TDLETSIKLL
PIEIPPPLFN SSIEPLTAGD ARYMNECINT LIREDPSLNV NVDEELGQTI LSGMGELHLE
IVRDRLINDM KAKIRLRNVA VSFKETVSKP SLEVVKASKN DGLVKVEVSL EAIDGPAEES
THADENGSVL LETDNNVVKL PPEAAASHIN ESLSERRWKS EHSLEELNDI ILQGITTGLQ
LGGPILGLPL HSVVVRVIHW DFPVEGKEVS ASMLLDASRQ VVREALSKLP ESSFCILEPI
MSTRVYVDSG SMGEVVHDLS HRCSAHITSI EDESENMDSN AWANEEAENL YLPQDYTMKS
GKNAVNFTNK KVVVAETPLR DMVGYLSKLR SITQGRGVFD MTYLGMRRAI RPVLLDS
