ID A0A2K5K991_COLAP Unreviewed; 777 AA.
AC A0A2K5K991;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
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 Synonyms=EFG2 {ECO:0000256|HAMAP-Rule:MF_03059};
OS Colobus angolensis palliatus (Peters' Angolan colobus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Colobus.
OX NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000037657.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000037657.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 RefSeq; XP_011814639.1; XM_011959249.1.
DR RefSeq; XP_011814640.1; XM_011959250.1.
DR AlphaFoldDB; A0A2K5K991; -.
DR STRING; 336983.ENSCANP00000037657; -.
DR Ensembl; ENSCANT00000060910.1; ENSCANP00000037657.1; ENSCANG00000042500.1.
DR GeneID; 105524128; -.
DR KEGG; cang:105524128; -.
DR CTD; 84340; -.
DR OrthoDB; 148165at2759; -.
DR Proteomes; UP000233080; Unplaced.
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:UP000233080}.
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; 86019 MW; B2427B6E8645097B CRC64;
MLSILRIFAV SHQTIPSVHI NNICCYKVRA SLKRLKPHVP LGRNYSSLPG LIGNDIKSLH
SIINPPIAKI RNIGIMAHID AGKTTTTERI LYYSGYTRSL GDVDDGDTVT DFMAQERERG
ITIQSAAVTF DWKGYRVNLI DTPGHVDFTL EVERCLRVLD GAVAIFDASA GVEAQTLTVW
RQADKHNIPR ICFLNKMDKT GASFKYAVES IREKLKAKPL LLQLPIGEAK TFKGVVDVVT
KEKLLWNSNS NDGKDFERKL LLEMSDPALL KETTEARNAL IEQVADLDDE FADLVLEEFS
ENFDLLPAEK LQTAIHRVTL AQTAVPVLCG SALKNKGIQP LLDAVTMYLP SPEERNYEFL
QWYKDDLCAL AFKVLHDKQR GPLVFMRIYS GTIKPQLAIH NVNGNCTERI SRLLLPFADQ
HVEIPSLTAG NIALTVGLKH TATGDTIVSS KSSALAAARR AEREGEKKHR QNKEAERVLL
AGVEIPEPVF FCTIEPPSVS KQPDLEHALK CLQREDPSLK VRLDPDSGQT VLCGMGELHI
EIIHDRIKRE YGLETYLGPL QVAYRETILN SVRATDTLDR TLGDKRHLVT VEVEARPIET
SSVTPVIEYA ESISEGLLKV SQEAIESGIH SACLQGPLLG SPVQDVAITL HSLTIHPGTS
TTMISACVSR CVQKALKKAD KQVLEPLMSL EVTVARDYLS PVLADLAQRR GNIQEIQTRQ
DNKVVIGFVP LADIMGYSTV LRTLTSGSAT FALELSTYQA MNSQDQNTLL NRRSGLT
//
