ID Q0CAG2_ASPTN Unreviewed; 857 AA.
AC Q0CAG2;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 08-NOV-2023, entry version 86.
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=ATEG_09322 {ECO:0000313|EMBL:EAU30459.1};
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663 {ECO:0000313|EMBL:EAU30459.1, ECO:0000313|Proteomes:UP000007963};
RN [1] {ECO:0000313|Proteomes:UP000007963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156 {ECO:0000313|Proteomes:UP000007963};
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) 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; CH476607; EAU30459.1; -; Genomic_DNA.
DR RefSeq; XP_001217944.1; XM_001217943.1.
DR AlphaFoldDB; Q0CAG2; -.
DR STRING; 341663.Q0CAG2; -.
DR EnsemblFungi; EAU30459; EAU30459; ATEG_09322.
DR GeneID; 4353599; -.
DR VEuPathDB; FungiDB:ATEG_09322; -.
DR eggNOG; KOG0465; Eukaryota.
DR HOGENOM; CLU_002794_4_1_1; -.
DR OMA; GPQFTFP; -.
DR OrthoDB; 148165at2759; -.
DR Proteomes; UP000007963; 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:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IEA:EnsemblFungi.
DR GO; GO:0032543; P:mitochondrial translation; IEA:UniProtKB-UniRule.
DR GO; GO:0051881; P:regulation of mitochondrial membrane potential; IEA:EnsemblFungi.
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; 3.30.70.240; -; 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; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
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 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 Elongation factor {ECO:0000313|EMBL:EAU30459.1};
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:UP000007963};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 1..311
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 10..17
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03059"
FT BINDING 95..99
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03059"
FT BINDING 149..152
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03059"
SQ SEQUENCE 857 AA; 92304 MW; 8DE390B138E88979 CRC64;
MEDLNIGIIA HIDAGKTTTT ERMLYYSGFT RRLGDVDEGS TVTDFLPAER ARGITIQSAA
ITFHWPPENA AEANASPHDA QSPRSAVPHT VNLIDTPGHA DFTFEVMRSL RILDGAVCIL
DGVAGVEAQT EQVWHQASSY SIPRVVYVNK LDRDGAAFGR TVREVASRLS GWPAVCQIPW
FEGGNGRFIG VADAINLQGL RWDDGDGKSV KMFDLQQLDA EDGQLAQELR RARVALVELL
SEHDETMIER FFDCDEDHLA VPPLDILESL RRCLHQQTGR KIIPVFAGAS FRNIGVQPLL
DAVVNLLPSP LETADPEVSI GGVKGGLRRL LSGDLLVEQS EQAATKGKPK KKSAAIHAES
RTAIEKLQGC ALAFKVVNDA KRGVLVYVRV YSGSLDRNSV LFNTNLNVSE RAPRLLKMYA
NDAVEVDSIP EGHIGVVAGL KHTRTGDTLV TYAGNKATPP EPLNTLQLRP ITVPPPVFFA
SVEPHSLSEE KRLQDSLAML LREDPSLHVT VDEDSGQTLL SGMGELHLEI ARDRLLNDLK
AKASMGRIEI GYRECPLAAS GPVTQIFDKE IAGRKGKAGC TATVEPFDPD SSPAVDESSA
LSVEISDGNQ IVILAPGLDV EISKRGVEES PLLPATLDVP TLRSALHNGC LAALARGPQF
TFPLHNTRVI LTFDPAAHLF GNETTPSALS AAARLATSSA LRTLVSSAPA SATALMEPVM
NVVITVDEAS LGAVVHDISS SRGGHIVSLD EEIPLPATDL VASPEPTEDL PPIDPAKVYA
PPDPFQSASL GVDLPASTNR PRTITAKVPL KEMVGYLKHL RSLSAGRGTF VMSVDRFEKM
SAPRQKAVLS DLRGEYM
//
