ID A0A0M8P814_9EURO Unreviewed; 873 AA.
AC A0A0M8P814;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=ACN38_g6473 {ECO:0000313|EMBL:KOS42621.1};
OS Penicillium nordicum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=229535 {ECO:0000313|EMBL:KOS42621.1, ECO:0000313|Proteomes:UP000037696};
RN [1] {ECO:0000313|EMBL:KOS42621.1, ECO:0000313|Proteomes:UP000037696}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOMC 185683 {ECO:0000313|EMBL:KOS42621.1,
RC ECO:0000313|Proteomes:UP000037696};
RA Nguyen H.D., Seifert K.A.;
RT "Genome sequencing of Penicillium nordicum.";
RL Submitted (AUG-2015) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KOS42621.1}.
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DR EMBL; LHQQ01000101; KOS42621.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8P814; -.
DR STRING; 229535.A0A0M8P814; -.
DR OrthoDB; 148165at2759; -.
DR Proteomes; UP000037696; Unassembled WGS sequence.
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 Gene3D; 3.30.230.10; -; 2.
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 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; 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};
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};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_03059}; Reference proteome {ECO:0000313|Proteomes:UP000037696};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 11..324
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 20..27
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03059"
FT BINDING 108..112
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03059"
FT BINDING 162..165
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03059"
SQ SEQUENCE 873 AA; 94215 MW; 8EB07E559D2E282C CRC64;
MTSACHDEAL DRTRNIGIIA HIDAGKTTTT ERMLFYSGFT RRIGDVDEGS TVTDFLPAER
ARGITIQSAA ITFHWPPGEV TGASAPQAGA QSEPTPRSAY PHTINLIDTP GHADFTFEVM
RSLRILDGAV CILDGVAGVE AQTEKVWNQA SAYRIPRVIY VNKLDRDGAA FGRTVREVST
RLSVYPAVCQ IPWFDGGNGP FIGVADAIHL QGLRWKEGED GRTVKVADLK QLEAEEPALA
AELRRARIAL IELLSEHDED IVEKFFECEE DHLAVSSADI IESLRRCVLD QTSRIIPLFA
GASFRNMGVQ PLLDSIVNLL PSPPEAPDPE VSIGGVKGGL RGLLSGDLIV EQSEKASAPS
KGKQPKKKHL ALQTSSKDAI SKLQSCALAF KVVNDAKRGV LVYVRVYSGS LDRNSLLFNT
NLQLSERAPR LLKMYANDAV EVDSIPAGHI GVVVGLKQTR TGDTLVSYAG NKATPPEPLT
SLQLRPIAVP PPVFFTSVEP HSLSEEKRMK ESLALLLRED PSLHVNIDEE SGQTLLSGMG
ELHLEIARDR LINDLKAKAT MGRIEIGYRE SALGTSSSIT KIFDKEIAGR KGKAGCTAVA
EPLDEDLESP EVDQDTLLVE TYDGNRIIVR APGLQVDRSS RSEEETSPFL PPGMDLVAFR
TALQNGAVAA LARGPQFTFP MHNTRVTLTI NPSVDLFGNE TTTSALSSAA RQATAAALQN
VQFGAGTVMM EPVMNVIISI DEASLGSVVH DISSSRGGHI ISLDEEVPLS GTDASSTSAS
ALEDEALPPI DHSRVYAPPD PFETPSVGVQ IPVAATRPRT IIAKVPLKEM VGYLKHLRSL
TAGRGTFVMS VDRFEKMSGQ RQKAVLAELR GGF
//
