ID A0A2T6ZBC8_TUBBO Unreviewed; 852 AA.
AC A0A2T6ZBC8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Ribosome-releasing factor 2, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03059};
DE Short=RRF2mt {ECO:0000256|HAMAP-Rule:MF_03059};
DE AltName: Full=Elongation factor G 2, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03059};
DE Short=EF-G2mt {ECO:0000256|HAMAP-Rule:MF_03059};
DE Short=mEF-G 2 {ECO:0000256|HAMAP-Rule:MF_03059};
GN Name=MEF2 {ECO:0000256|HAMAP-Rule:MF_03059};
GN ORFNames=B9Z19DRAFT_1136717 {ECO:0000313|EMBL:PUU72783.1};
OS Tuber borchii (White truffle).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Tuberaceae; Tuber.
OX NCBI_TaxID=42251 {ECO:0000313|EMBL:PUU72783.1, ECO:0000313|Proteomes:UP000244722};
RN [1] {ECO:0000313|EMBL:PUU72783.1, ECO:0000313|Proteomes:UP000244722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tbo3840 {ECO:0000313|EMBL:PUU72783.1,
RC ECO:0000313|Proteomes:UP000244722};
RG DOE Joint Genome Institute;
RA Murat C., Kuo A., Barry K.W., Clum A., Dockter R.B., Fauchery L., Iotti M.,
RA Kohler A., Labutti K., Lindquist E.A., Lipzen A., Ohm R.A., Wang M.,
RA Grigoriev I.V., Zambonelli A., Martin F.M.;
RT "Draft genome sequence of Tuber borchii Vittad., a whitish edible
RT truffle.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-
CC Rule:MF_03059}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|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:0000256|HAMAP-Rule:MF_03059}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PUU72783.1}.
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DR EMBL; NESQ01000466; PUU72783.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T6ZBC8; -.
DR STRING; 42251.A0A2T6ZBC8; -.
DR Proteomes; UP000244722; 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; cd01886; EF-G; 1.
DR CDD; cd16262; EFG_III; 1.
DR CDD; cd03713; EFG_mtEFG_C; 1.
DR CDD; cd04092; mtEFG2_II_like; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.240; -; 1.
DR Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 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; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43261:SF1; RIBOSOME-RELEASING FACTOR 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43261; TRANSLATION ELONGATION FACTOR G-RELATED; 1.
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; SSF54980; EF-G C-terminal domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_03059}; Hydrolase {ECO:0000313|EMBL:PUU72783.1};
KW Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03059};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03059}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_03059};
KW Reference proteome {ECO:0000313|Proteomes:UP000244722}.
FT DOMAIN 55..353
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 64..71
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03059"
FT BINDING 135..139
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03059"
FT BINDING 189..192
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03059"
SQ SEQUENCE 852 AA; 92908 MW; F884135C323DFB89 CRC64;
MLLPARTASA IYWRYLPLPK TTPSLGRTIL SLQNSPKRFY ATPSATGANA PVDLAQTRNI
GIIAHIDAGK TTTTERMLYY SGFTRRIGEV DEGSTVMDYL PAERSRGITI TSAAITFNWT
PSTPGSQSYT INLIDTPGHA DFTFEVERSI RVLDGAVTIL DGVAGVEAQT EKVWRQAEKY
GIPRLIFVNK LDRVGAKFGP TVKEIASKLN AWPAVLQLPI YEQDTKGDDI FRGVVDIVEK
RVFIWGLEGD GQKIDMYDYT WLKGNRPDLY SEALTARAAL VELLSEHDEE LVEVFLDIGD
HHAISPGAIK KSLRKQTLRG SSEVVPVLCG ASFRNIGVQP LLDAVIDYLP SPLDKPETEI
SYNHGKARGV LNASEDRLCA LAFKVINDPK RGAMVFVRVY SGTLVRAHHL YNTTLGVKER
VHRLLKMYAD DAIDIQSIPA GHIGVIIGLK NARTGDTLIS DHQHHFGKGN KHHQKASDSF
GTVQLRPIEV PPPVFFASIE PNSLSEQKPL EDALSMLLRE DPSLHINIDE DSGQMLISGM
GELHLEIARD RLVGELKAKA EMGRILISYR ETIPSTSGYE LRTAFEKEIA GKLSKAGCHV
SVIGLDEPPI LDPGTPDETV VDGNLISADI IAPNHTLTMD EAEVEHTKLP KSIDTEELKG
SLISGAIAAL GRGPYLGFPV RNSSIKITID PSKDYFGTES TLAAYSSAAR LAVTMALKEA
IASNEEGILM EPMMNVIVTV DEKDLGKVVG DLSSARGGHV LELGGGDEGG VERLDTSKVY
APGQAGKVDD NDGGVRGKRS VVATVPLKEM VGYLKHLRSM TTGRGTFVMN LLGWERMTRL
RAVDVLKDIR GG
//
