RRF2M_VANPO
ID RRF2M_VANPO Reviewed; 799 AA.
AC A7TQJ9;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
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}; ORFNames=Kpol_463p13;
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC Y-8283 / UCD 57-17;
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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; DS480459; EDO15463.1; -; Genomic_DNA.
DR RefSeq; XP_001643321.1; XM_001643271.1.
DR AlphaFoldDB; A7TQJ9; -.
DR SMR; A7TQJ9; -.
DR STRING; 436907.A7TQJ9; -.
DR EnsemblFungi; EDO15463; EDO15463; Kpol_463p13.
DR GeneID; 5543532; -.
DR KEGG; vpo:Kpol_463p13; -.
DR eggNOG; KOG0465; Eukaryota.
DR HOGENOM; CLU_002794_4_1_1; -.
DR InParanoid; A7TQJ9; -.
DR OMA; AVCQIPW; -.
DR OrthoDB; 637899at2759; -.
DR Proteomes; UP000000267; 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.
FT CHAIN 1..799
FT /note="Ribosome-releasing factor 2, mitochondrial"
FT /id="PRO_0000385622"
FT DOMAIN 19..306
FT /note="tr-type G"
FT BINDING 28..35
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT BINDING 93..97
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT BINDING 145..148
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
SQ SEQUENCE 799 AA; 89184 MW; EC5286D506D2F96A CRC64;
MFGFGIRQLR GYASKTDLSK IRNIGIIAHI DAGKTTTTER MLYYSGKTNR IGNVDQGDTV
TDYLPQERSR GITIQSAAIS FNWQNDHRIN LIDTPGHVDF TFEVIKSLKV LDGCVTILDA
VAGVEAQTEK VWKQSYGIPK ICYINKMDRV GSGYSRTVKE LMIKMNQRVV LANMPLFKLD
PVTNEQVFEG VLDVVNMKAL RWDSTDVNKV DIADIDKFDS SLLDELTKAR EAMVETLSEF
DENLVEHFLE DAEGDYLKVS PTILNSSIRK STLSQDITPI LCGSSFRNIG VQPLLDAVVN
YLPSPLEAKF PELNEDIPIS YDKRKGLLFD NNSEICVAFA FKVITDEIRG QLVFVRVYSG
TLKNGHSVYN STNGKTFKIN KPVIMHANKT EDVQSLSAGE IGVLTGSTVF GRIETGDTLI
SHSMVKDGLK SIERKGNLNL KINPIIIPPP VFSVYIEPKT LGNRKAMEAA LKILVTEDPS
LHVSQDEETS QTLLSGMGEL HLEIARDKLL NDLKAEVGIG KLMISYKETI NSTTNPVIYQ
DDIGYKFTIQ IEPLEGEEVR VDKDTATEAW YPLGVDNNYL IFEKSNKPGL GAVWKHQIPY
DVVINTIKSS CLASFQRGGK IGGYALHSCA VRIKGDFEVP YDATSSNEIL NITRKLIIKS
LQALHESSYS LLEPIMDVEI VVNQKFMGEV IQDLTGHHKA NILSIEDEHG LDYNNERSTL
NFKDIVDSQY LPPDITLNLA KLDNGGDRCK VIKAEAPLKE MVSYSNKLRS LTEGRGMVYM
NYHGMKKVTP ERLDDVLQG
