RRF2M_PONAB
ID RRF2M_PONAB Reviewed; 777 AA.
AC Q5R600;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=GFM2 {ECO:0000255|HAMAP-Rule:MF_03059};
GN Synonyms=EFG2 {ECO:0000255|HAMAP-Rule:MF_03059};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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. 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: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; CR860700; CAH92816.1; -; mRNA.
DR RefSeq; NP_001126644.1; NM_001133172.1.
DR AlphaFoldDB; Q5R600; -.
DR SMR; Q5R600; -.
DR STRING; 9601.ENSPPYP00000017390; -.
DR GeneID; 100173642; -.
DR KEGG; pon:100173642; -.
DR CTD; 84340; -.
DR eggNOG; KOG0464; Eukaryota.
DR InParanoid; Q5R600; -.
DR OrthoDB; 637899at2759; -.
DR Proteomes; UP000001595; 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; 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; IPR004161; EFTu-like_2.
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 InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
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; 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 2: Evidence at transcript level;
KW GTP-binding; Mitochondrion; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..777
FT /note="Ribosome-releasing factor 2, mitochondrial"
FT /id="PRO_0000385593"
FT DOMAIN 68..353
FT /note="tr-type G"
FT BINDING 77..84
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT BINDING 141..145
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT BINDING 195..198
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
SQ SEQUENCE 777 AA; 86038 MW; B0051D3ACFFFDE25 CRC64;
MLTNLRIFAM SHQTIPSVCI NNICCYKIRA SLKRLKPHVP LGRNCSSLPG LIGNDIKSLH
SIINPPIAKI RNIGIMAHID AGKTTTTERI LYYSGYTRSL GDVDDGDTVT DFMAQERERG
ITIQSAAVTF DWKGYRVNLI DTPGHVDFTL EVERCLRVLD GAVAVFDASA GVEAQTLTVW
RQADKHNIPR ICFLNKMDKT GASFKYAVES IREKLKAKPL LLQLPIGEAK TFKGVVDVVT
KEKLLWNCNS NDGKDFERKP LLEMNDPELL KETTEARNAL IEQVADLDDE FADLVLEEFS
ENFDLLPAEK LQTAIHRVTL AQTAVPVLCG SALKNKGIQP LLDAVTMYLP SPEECNCEFL
QWYKDDLCAL AFKVLHDKQR GPLVFMRIYS GTIKPQLAIH NINGNCTERI SRLLLPFADQ
HVEIPSLTAG NIALTVGLKH TATGDTIVSS KSSALAAARR AEREGEKKHR QNSEAERLVL
AGVEIPEPVF FCTIEPPSVS KQPDLEHALK CLQREDPSLK VRLDPDSGQT VLCGMGELHI
EIIHDRIKRE YGLEAYLGPL QVAYRETILN SVRATDTLDR TLGDKRHLVT VEVEARPTET
TSVMPVIEYA ESIHEGLLKV SQEAIENGIY SACLQGPLLG SPIQDVAITL HSLTIHPGTS
TTMISACVSR CVQKALKKAD KQVLEPLMNL EVTVARDYLS PVLADLAQRR GNIQEIQTRQ
DNKVVIGFVP LAEIMGYSTV LRTLTSGSAT FALELSTNQA MNPQDQNTLL NRRSGLT
