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RRF2M_CANGA
ID   RRF2M_CANGA             Reviewed;         807 AA.
AC   Q6FLG2;
DT   13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 125.
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=CAGL0L03652g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380958; CAG61902.1; -; Genomic_DNA.
DR   RefSeq; XP_448932.1; XM_448932.1.
DR   AlphaFoldDB; Q6FLG2; -.
DR   SMR; Q6FLG2; -.
DR   STRING; 5478.XP_448932.1; -.
DR   EnsemblFungi; CAG61902; CAG61902; CAGL0L03652g.
DR   GeneID; 2890538; -.
DR   KEGG; cgr:CAGL0L03652g; -.
DR   CGD; CAL0135510; CAGL0L03652g.
DR   VEuPathDB; FungiDB:CAGL0L03652g; -.
DR   eggNOG; KOG0465; Eukaryota.
DR   HOGENOM; CLU_002794_4_1_1; -.
DR   InParanoid; Q6FLG2; -.
DR   OMA; AVCQIPW; -.
DR   Proteomes; UP000002428; Chromosome L.
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:0000002; P:mitochondrial genome maintenance; IEA:EnsemblFungi.
DR   GO; GO:0032543; P:mitochondrial translation; IEA:UniProtKB-UniRule.
DR   GO; GO:0051881; P:regulation of mitochondrial membrane potential; IEA:EnsemblFungi.
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..807
FT                   /note="Ribosome-releasing factor 2, mitochondrial"
FT                   /id="PRO_0000385613"
FT   DOMAIN          21..319
FT                   /note="tr-type G"
FT   BINDING         30..37
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT   BINDING         101..105
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT   BINDING         153..156
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
SQ   SEQUENCE   807 AA;  89628 MW;  D18376630441EA0A CRC64;
     MLRFVCGRFQ SGIRRYATTI DRFRNIGIIA HIDAGKTTTT ERMLYCAGKI KRIGDVDSGD
     TVTDFLPQER DRGITIQSAA ISFQWHDSSR DNSPRVINLI DTPGHADFIF EVIRSLKVLD
     GAVLILDGVA GVEAQTEKLW RYSRNIPKIC FVNKMDRVGA GFSKTLKELT YKTDRRCVVV
     NFPYFEQTNQ SEDPVFCGVI DVINMKLLKW DTKANSPDAV TVVDLLELND SDNAKVEAIK
     SRESMVEILG ELDDVFVQEF FDGPSEGNSL KVSAQVLNKS IRKLTIANEL TPVLAGASFK
     NVGIQPLLDG IIQYLPSPLE ARLPEVNPKD IPVVHDPKVG ALINKQNNLC VALAFKVTHD
     QIRGLMVFVR IYSGVLNSGN TVMNTTTGEK FRIGKLVIMQ ADQAQEVKSL SPGQIGVLTG
     ATITNKVATG DTIISHSIKK DGIRSFGEKE SQLKVNAIQI PPPVFSVIVE PKSLGNKKLI
     EDALKEITME DPSLHVIIDE ETGQTVLNGM GQLHLEIAKF RLVNEMKVPV DFGKIAVSYK
     ETLELPTEVV TFKDERGFHF SLSVESFEKD TINIEERSGA SCFSVDNDEN YLIIEGFQDR
     LQKSNWAYQI PIRNFVTTIL SSAMASLQSA GKVGHLPLYS CAVRLKKDWD FPLDLQSPAE
     LLSITRSLIT EALQTVDVSN YTLLEPVMDA HISVPQNDIG TVMQDLCSAR TATISSLDDE
     NVSSSDKLME LESQSKHLYY PTDSTLGTAK IQDDKLKTIH AICPLKEMVT YSSKLRSLTK
     GRGELHMDYK GMSKVSQERI PDILQEL
 
 
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