ID A0A1L0BSG8_9ASCO Unreviewed; 849 AA.
AC A0A1L0BSG8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, 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=MEF2 {ECO:0000256|HAMAP-Rule:MF_03059};
GN ORFNames=SAMEA4029010_CIC11G00000005571 {ECO:0000313|EMBL:SGZ54203.1};
OS [Candida] intermedia.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC Candida/Metschnikowiaceae.
OX NCBI_TaxID=45354 {ECO:0000313|EMBL:SGZ54203.1, ECO:0000313|Proteomes:UP000182334};
RN [1] {ECO:0000313|EMBL:SGZ54203.1, ECO:0000313|Proteomes:UP000182334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 141442 {ECO:0000313|EMBL:SGZ54203.1,
RC ECO:0000313|Proteomes:UP000182334};
RA de Groot N.N.;
RL Submitted (OCT-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}.
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DR EMBL; LT635759; SGZ54203.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L0BSG8; -.
DR STRING; 45354.A0A1L0BSG8; -.
DR OrthoDB; 148165at2759; -.
DR Proteomes; UP000182334; Chromosome iv.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000182334}.
FT DOMAIN 40..331
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 49..56
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03059"
FT BINDING 113..117
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 849 AA; 93423 MW; F099C05F36608AE8 CRC64;
MFKPATRKPV VGCILRVVFK NNLHGSLVLN EPKLNSVPID KTRNIGIIAH IDAGKTTTTE
RMLFYSGKTQ RIGNVDEGDT VTDYLPSERE RGITIQLAAI SIPWNNHKIN IIDTPGHADF
TFEVTRSLRV LDGAVTILDA VAGVEAQTEK VWKQAGSLGI PRIAYVNKMD RPGAGFSRTV
KEIVSKLQTR AVCVNLPYFK QTGNSDPVFT GVLDVIYGKL LVWDPMTDSS GKSVRAIDLD
PQNPDLAPLF DVVAKSRESM VETLGEFDEK VIESFFEHED YMKVPSAILQ EAIRNATINN
QVTPVLCGSS FRNIGVQPLM DAVVSYLPSP LQTSLPEITS SSSKRVGKKK KRSTVSESIE
VPVEMDKNKG LIINKNGNLT VGLAFKVTTH PARGVMTFFR VYSGKLASNS TVMNTRTGKK
IHLRKLMLMH GDAPEEVLTI SAGNIGVVAG TDDDIVTGDT FVSQGVTHSK SFNETEKNLT
LLPIVIPPPL FNSGIEPATA GDERYMNECI KTLLREDPSL QVHMDEDLGQ TVLSGMGELH
LEIIRDRLVN DMKAKVRLRD VAVSYKETVS KPDGSIVTVT SAENPDVSVS VTLDSFEGEA
GESAFAEEDG AVLLDLDNNI IILDSNATPE HMIKAVEERR WKAEQSLEEL QDTLIQGCAT
GLHIGGPMFG LPLHSCVIRI TKWNFPVEDK SVAPAALLDV GRRAITKAVG ALDEKPGENF
CVLEPLMNTS VYVDSDVLGE VVHDLNNRCQ ATILSIDDEA SDSLDTQSWA QDEAEKIFLP
DDYTMKNMDR EIKNKKTVVA ETPLKEMIGY LSRLRSITQG RGMFDMQYQG MRRAVKARLS
SIKNEFTFL
//
