GenomeNet

Database: UniProt
Entry: A0A1G4JIV6_9SACH
LinkDB: A0A1G4JIV6_9SACH
Original site: A0A1G4JIV6_9SACH 
ID   A0A1G4JIV6_9SACH        Unreviewed;       815 AA.
AC   A0A1G4JIV6;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
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=MEF2 {ECO:0000256|HAMAP-Rule:MF_03059};
GN   ORFNames=LANO_0D08636G {ECO:0000313|EMBL:SCU90408.1};
OS   Lachancea nothofagi CBS 11611.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=1266666 {ECO:0000313|EMBL:SCU90408.1};
RN   [1] {ECO:0000313|EMBL:SCU90408.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Ploux O.;
RL   Submitted (MAR-2016) 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. 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LT598448; SCU90408.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G4JIV6; -.
DR   OrthoDB; 148165at2759; -.
DR   Proteomes; UP000189911; Chromosome d.
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   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; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
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; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SMART; SM00838; EFG_C; 1.
DR   SUPFAM; SSF54980; EF-G C-terminal domain-like; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128, ECO:0000256|HAMAP-
KW   Rule:MF_03059};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_03059}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_03059}.
FT   DOMAIN          41..327
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   BINDING         50..57
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03059"
FT   BINDING         115..119
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03059"
FT   BINDING         167..170
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03059"
SQ   SEQUENCE   815 AA;  90003 MW;  7E5DEF853706BBAB CRC64;
     MNLKVSASKA FGADTLSTMF KMRMLRLEIG RRSFSSKTDV SALRNIGIIA HIDAGKTTTT
     ERMLYFSGKT KRIGNVDEGD TITDFLPQER SRGITIQSAA ISFSWQNKFR INLIDTPGHA
     DFTFEVIRSL KVLDGCVTIL DAVAGVEAQT EKVWKQAKGI PKICFINKMD RAGAGFSRTT
     KELIAKLNTR VLLLNVPVFA NTSGPGEPVF EGVLDVVNKK VLRWTPQDPE RVSVEDIICN
     SYYWNDLVKL RECLVETLSE FDEELVEYFL DTANGDYMIV PPELINKSVK KSLLANYAVP
     VLCGASFRNI GVQPLLDAVV NYLPSPLEAK LPEFNTNVPV EVNKKEGSVI NNNKNLCVAQ
     AFKVITDPIR GIMVYVRVYS GCLNSGFTVY NSTTGAKFKI GKLVIMHANV AEEVKQLKCG
     EIGVLTGSTV SENVRTGDTI ITHSMKKDGL KSLNRVKELG LKINPIETPP PVFSVAVEPR
     TLGNKKLMEE SIATIIREDP SLHVNVDEET GQTLLSGMGQ LHLEIAKDRL LNELKAEVEV
     GKVMVSFKET LNACTKQSVL QTEDGYRFSI SVEPLDVAMA AKSSDEDWHY LSTDNNYLIL
     EKSPACAGNW PYQISYEQIV NAVISSSIVA LQKSGKIANF PLHSCAVRIK NDWSIPLDAT
     SVSQTLALSR GLIFEALREL PDTAFAVLEP IMHINVTVKQ SDMGHVLQDL TGARKANILS
     IDDEHDLTSG ENADIQYQRL AEDQFLPMDA TLGLANISSG ATVNKTIRAL VPLKEIVSYM
     SKLRSLTKGR GSYTMNYHGM EKVTSDRLPS ILEEF
//
DBGET integrated database retrieval system