RRF2M_CANAL
ID RRF2M_CANAL Reviewed; 807 AA.
AC Q5AAV3; A0A1D8PDY3; Q5AB43;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 2.
DT 03-AUG-2022, entry version 126.
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};
GN OrderedLocusNames=CAALFM_C107000WA; ORFNames=CaO19.13589, CaO19.6208;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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 -!- SEQUENCE CAUTION:
CC Sequence=AOW26352.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP017623; AOW26352.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_718798.2; XM_713705.2.
DR AlphaFoldDB; Q5AAV3; -.
DR SMR; Q5AAV3; -.
DR STRING; 237561.Q5AAV3; -.
DR PRIDE; Q5AAV3; -.
DR GeneID; 3639564; -.
DR KEGG; cal:CAALFM_C107000WA; -.
DR CGD; CAL0000188276; MEF2.
DR eggNOG; KOG0465; Eukaryota.
DR HOGENOM; CLU_002794_4_1_1; -.
DR InParanoid; Q5AAV3; -.
DR OrthoDB; 637899at2759; -.
DR PRO; PR:Q5AAV3; -.
DR Proteomes; UP000000559; 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; IBA:GO_Central.
DR GO; GO:0032543; P:mitochondrial translation; IBA:GO_Central.
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; 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..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_0000385611"
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; 90224 MW; 0DDA477EF4CDAF0F CRC64;
MFCRKYVFQT WKQLSRSYST VNSIGAAKTR NIGIIAHIDA GKTTTTERMI YYSGRTKRIG
NVDEGDTVTD YLPSERERGI TIQSAAITLP WNQHKINIID TPGHADFTFE VIRSLRVLDG
AVTILDAVAG VEAQTEKVWK QASALNLPKV VYVNKMDRPG AGFSRTVQEV IQKLETRVVL
CNLPYFETNK ESDLEFKGVI DVIHQKLLKW NETDANGNEI SVVNIDETTP DLLQILEKSR
ESMVETLGEY DERIIDSFLE HDENYLKIPP MLLDQVIRKA TIDNYLTPVF CGASFRNIGV
QPLMDGITKY LPSPLETSLP QITKNGKDVT KKVDGEKGLV VANDNNLTLA LAFKVMTHST
RGPMTFVRVY SGKLNAASNL INTRTGKKLL IRKLLVMHGD SPEEVKSISA GNIGVIPGYE
TDFQTGDTLV SSAVAKRNFT AKDSAYRLLP IDIPPPLFNA AIEPHTAGDE AYMKQCVETL
IREDPSLKVH LDKEMGQVVL SGMGELHLDI VRERLVNDMK AKVNLKDVVV SYKESFVGKR
EKEAVITNEE IEVAVTLSHI EDARDYVGQE GALVIEEDNN VILLSETASS EHVRATIDER
RWKCENNLEE LKEAILNGCL TALQMGGPIL GFPLHSTLVT VNRWNVPVEV AQEQALNLMN
ASRQAVQSLK DEKKDFSILE PIMSTKVYVD SNDLGEVSHD LTQRCKAMIV EIQDQSTQNL
ETAAWAKDEA AKVYVPPDYT IKKNVSKFDD IANKKIIVAE TPLREMIGYL SKLRALTRGR
ATFDMTLIGM RRAVGNRVDS IVEEYKF