ID A0A0D9RSG1_CHLSB Unreviewed; 777 AA.
AC A0A0D9RSG1;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=GFM2 {ECO:0000256|HAMAP-Rule:MF_03059,
GN ECO:0000313|Ensembl:ENSCSAP00000011550.1};
GN Synonyms=EFG2 {ECO:0000256|HAMAP-Rule:MF_03059};
OS Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000011550.1, ECO:0000313|Proteomes:UP000029965};
RN [1] {ECO:0000313|Ensembl:ENSCSAP00000011550.1, ECO:0000313|Proteomes:UP000029965}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCSAP00000011550.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Mitochondrial GTPase that mediates the disassembly of
CC ribosomes from messenger RNA at the termination of mitochondrial
CC protein biosynthesis. Acts in collaboration with MRRF. GTP hydrolysis
CC follows the ribosome disassembly and probably occurs on the ribosome
CC large subunit. 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}.
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DR EMBL; AQIB01086739; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_007973509.1; XM_007975318.1.
DR RefSeq; XP_007973519.1; XM_007975328.1.
DR RefSeq; XP_007973529.1; XM_007975338.1.
DR AlphaFoldDB; A0A0D9RSG1; -.
DR STRING; 60711.ENSCSAP00000011550; -.
DR Ensembl; ENSCSAT00000013555.1; ENSCSAP00000011550.1; ENSCSAG00000015464.1.
DR GeneID; 103223136; -.
DR KEGG; csab:103223136; -.
DR CTD; 84340; -.
DR eggNOG; KOG0464; Eukaryota.
DR GeneTree; ENSGT00550000074890; -.
DR OMA; GPQFTFP; -.
DR OrthoDB; 148165at2759; -.
DR BioGRID-ORCS; 103223136; 7 hits in 15 CRISPR screens.
DR Proteomes; UP000029965; Chromosome 4.
DR Bgee; ENSCSAG00000015464; Expressed in pituitary gland and 7 other cell types or tissues.
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 CDD; cd01693; mtEFG2_like_IV; 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; IPR020568; Ribosomal_Su5_D2-typ_SF.
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 InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
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; PF03764; EFG_IV; 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 SMART; SM00889; EFG_IV; 1.
DR SUPFAM; SSF54980; EF-G C-terminal domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 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:0000256|ARBA:ARBA00022801};
KW Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03059};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03059};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_03059}; Reference proteome {ECO:0000313|Proteomes:UP000029965}.
FT DOMAIN 68..353
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 77..84
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03059"
FT BINDING 141..145
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03059"
FT BINDING 195..198
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03059"
SQ SEQUENCE 777 AA; 85955 MW; 6AAB84BF2F73BF86 CRC64;
MLSNLRICAV SHQTIPSVHI NNICCYKVRA SLKRLKPHVP LGRNYSSLPG LIGNDIKSLH
SIINPPIAKI RNIGIMAHID AGKTTTTERI LYYSGYTRSL GDVDDGDTVT DFMAQERERG
ITIQSAAVTF DWKGYRVNLI DTPGHVDFTL EVERCLRVLD GAVAIFDASA GVEAQTLTVW
RQADKHNIPR ICFLNKMDKT GASFKYAVES IREKLKAKPL LLQLPIGEAK TFKGVVDVVT
KEKLLWNSNS NDGKDFERKP LLEMSDPELL KETTEARNAL IEQVADLDDE FADLVLEEFS
ENFDLLPAEK LQTAIHRVTL AQTAVPVLCG SALKNKGIQP LLDAVTVYLP SPVERNYEFL
QWYKDDLCAL AFKVLHDKQR GPLVFMRIYS GTIKPQLAIH NVNGNCTERI SRLLLPFADQ
HVEIPSLTAG NIALTVGLKH TATGDTIVSS KSSALAAARR AEREGEKKHR QNNEAERVLL
AGVEIPEPVF FCTIEPPSVS KQPDLEHALK CLQREDPSLK VRLDPDSGQT VLCGMGELHI
EIIHDRIKRE YGLETYLGPL QVAYRETILN SVRATDTLDR TLGDKRHLVT VEVEARPIET
SSVTPVIEYA ESISEGLLNV SQEAIESGIH SACLQGPLLG SPVQDVAITL HSLTIHPGTS
TTMISACVSR CVQKALKKAD KQVLEPLMNL EVTVARDYLS PVLADLAQRR GNIQEIQTRQ
DNKVVIGFVP LADIMGYSTV LRTLTSGSAT FALELSTYQA MNSQDQNTLL NRRSGLT
//
