RRF2M_BOVIN
ID RRF2M_BOVIN Reviewed; 777 AA.
AC A6QNM2;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 99.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Heart ventricle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) 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; BC148895; AAI48896.1; -; mRNA.
DR RefSeq; NP_001095579.1; NM_001102109.2.
DR AlphaFoldDB; A6QNM2; -.
DR SMR; A6QNM2; -.
DR STRING; 9913.ENSBTAP00000048999; -.
DR PaxDb; A6QNM2; -.
DR PRIDE; A6QNM2; -.
DR Ensembl; ENSBTAT00000054796; ENSBTAP00000048999; ENSBTAG00000015519.
DR GeneID; 527467; -.
DR KEGG; bta:527467; -.
DR CTD; 84340; -.
DR VEuPathDB; HostDB:ENSBTAG00000015519; -.
DR VGNC; VGNC:29328; GFM2.
DR eggNOG; KOG0464; Eukaryota.
DR GeneTree; ENSGT00550000074890; -.
DR HOGENOM; CLU_002794_4_1_1; -.
DR InParanoid; A6QNM2; -.
DR OMA; AVCQIPW; -.
DR OrthoDB; 637899at2759; -.
DR TreeFam; TF314848; -.
DR Proteomes; UP000009136; Chromosome 20.
DR ExpressionAtlas; A6QNM2; baseline and differential.
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_0000385592"
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; 86031 MW; E7DAC55186E6A0C2 CRC64;
MSNLRIFAVN QKKISSLHYF NNMCSSKIRA SLKRLKLHVL LGRNYSSLPG LIGNDIKSLH
SIINPPIAKI RNIGIMAHID AGKTTTTERI LYYSGYTRSL GDVDDGDTVT DFMAQERERG
ITIQSAAVTF DWKGYRINLI DTPGHVDFTL EVERCLRVLD GAVAVFDASA GVEAQTLTVW
RQADKHKVPR ICFLNKMDKI GASFNYAVES IREKLKAKPL LLQLPIGEGK AFKGVVDVVR
TEKLLWNPNS DDGKDFERKP LLEMSDPKLL KETTEARNAL IEQVADLDDE FADLVLGEFS
ENFDLLPAEK LQTAIHRVTL AQTAVPVLCG SALKNKGVQP LLDAITMYLP SPEERNYEFL
QWYKGDLCAL AFKVLHDKQR GPLVFMRIYS GMLKPQTAIH NINGNCTERV SRLLLPFADQ
HIEIPLLTAG NIALTVGLKH TATGDTIVSS RSSALAASRR AKREGEKKQK ENNEAERLLL
AGVEIPEPVF FCTIEPPSMA KQPDLDHALK CLQREDPSLK VKLDPDSGQT VLCGMGELHI
EIIHDRIKRE YGLETYLGPL QVAYREAILN SIRATDTLDR TLGDKRHLVT VELEAKPVET
SSLLPVIEYA ASVAGDLSQA SREAFENGVH SACLQGPLLG SPVQDVAVTL HSLVIHPGTS
TTMISACVSR CLQKALKKAD KQILEPLMNL EVTVSREYLS PVLADLAQRR GNIQEIQSRQ
DNKVVIGYVP LAEIMGYSTV LRTLTSGSAT FALELSNYQA MNPQDQSTLL SQRHGLS
