RRF2M_DROWI
ID RRF2M_DROWI Reviewed; 741 AA.
AC B4NAU8;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=EF-G2; ORFNames=GK11305;
OS Drosophila willistoni (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7260;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14030-0811.24;
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(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 -!- 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; CH964232; EDW80912.1; -; Genomic_DNA.
DR RefSeq; XP_002069926.1; XM_002069890.2.
DR AlphaFoldDB; B4NAU8; -.
DR SMR; B4NAU8; -.
DR STRING; 7260.FBpp0240448; -.
DR PRIDE; B4NAU8; -.
DR EnsemblMetazoa; FBtr0241956; FBpp0240448; FBgn0213316.
DR GeneID; 6648107; -.
DR KEGG; dwi:6648107; -.
DR eggNOG; KOG0464; Eukaryota.
DR HOGENOM; CLU_002794_4_1_1; -.
DR InParanoid; B4NAU8; -.
DR OMA; AVCQIPW; -.
DR OrthoDB; 637899at2759; -.
DR PhylomeDB; B4NAU8; -.
DR Proteomes; UP000007798; 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; ISS:UniProtKB.
DR GO; GO:0032543; P:mitochondrial translation; ISS:UniProtKB.
DR GO; GO:0032790; P:ribosome disassembly; ISS:UniProtKB.
DR CDD; cd16262; EFG_III; 1.
DR CDD; cd03713; EFG_mtEFG_C; 1.
DR Gene3D; 3.30.230.10; -; 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; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_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 Pfam; PF00679; EFG_C; 1.
DR Pfam; PF14492; EFG_III; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SMART; SM00838; EFG_C; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 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..741
FT /note="Ribosome-releasing factor 2, mitochondrial"
FT /id="PRO_0000385606"
FT DOMAIN 31..310
FT /note="tr-type G"
FT REGION 408..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 40..47
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT BINDING 104..108
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT BINDING 158..161
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
SQ SEQUENCE 741 AA; 82287 MW; 88C286239A685C71 CRC64;
MLRYVYFNGF GMRQGLLKRC SSHILRRSYS SDIRNIGILA HIDAGKTTTT ERMLFYAGKT
RSLGEVHRGN TVTDYLTQER ERGITICSSA VTFPWNGKRI NLLDTPGHID FTMEVEQSLH
AVDGVIVVLD ATAGVEAQTM TVWSQADKHR LPRLVFVNKM DRPDADFNKC VEDLKSKLET
FPVCIQYPAK SNEGQLGIYD VITLEQLNWQ QKDLGRSYSK LKLEPSDGLR QLQDKRNELI
DQLSGLDDEL ADVVISTESF DKVSNELVNK ALRRVICQQK AVPVLLGSAY KNIGIQCLMD
AVNHYLPAPE ERNEIYNCFG NELAGKVFKI VHDKQRGPLT LVRVMRGELK RGMRLTCSSG
QAEVISKLYE PLADEYREVS VVSSGDVALC AGLKSTVTGD LLTSSQSSLK NAEKRFKQQR
HSDGMSEEED DDEDHHLDGL FDLAPQIPDA VYFCSIEPPS ISSQTAMEQA LRQLQREDPS
LRVSYDSITG QTVLGGMGEL HMDIIKSRIL SEYKIDVDLG PLQIAYKETI EAPSLTTLSV
EKEIAGTKQN VSITLELVKN QSEIFSLDKS PENLQNLNKL RPRIVQVLRK GSISALERGP
RVGGQVVDTQ IRLHNAIIGR GTADAFIMAT AAQCVQKLLS ENGTRLLEPI MALQIVAPSE
RVSSIMADLS RRRAIINDVL PKGDRNKLIL INAPLAELPG YASTLRTISS GTASMTMQPC
GFSNMNSSDE SLAIRRAQGL E
