RRF2M_ASPFN
ID RRF2M_ASPFN Reviewed; 909 AA.
AC B8NDZ1;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 83.
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};
DE Flags: Precursor;
GN Name=mef2; ORFNames=AFLA_057220;
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC 167;
RX PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
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:0000255|HAMAP-
CC Rule:MF_03059}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|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:0000255|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; EQ963477; EED51459.1; -; Genomic_DNA.
DR RefSeq; XP_002378466.1; XM_002378425.1.
DR AlphaFoldDB; B8NDZ1; -.
DR SMR; B8NDZ1; -.
DR STRING; 5059.CADAFLAP00006331; -.
DR EnsemblFungi; EED51459; EED51459; AFLA_057220.
DR VEuPathDB; FungiDB:AFLA_057220; -.
DR eggNOG; KOG0465; Eukaryota.
DR HOGENOM; CLU_002794_4_1_1; -.
DR OMA; AVCQIPW; -.
DR Proteomes; UP000001875; 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: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; 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; 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 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; 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 3: Inferred from homology;
KW GTP-binding; Mitochondrion; Nucleotide-binding; Protein biosynthesis;
KW Transit peptide.
FT TRANSIT 1..15
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT CHAIN 16..909
FT /note="Ribosome-releasing factor 2, mitochondrial"
FT /id="PRO_0000385609"
FT DOMAIN 57..367
FT /note="tr-type G"
FT REGION 121..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 66..73
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT BINDING 151..155
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT BINDING 205..208
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
SQ SEQUENCE 909 AA; 98329 MW; 68E75E2275B7BF80 CRC64;
MVAAPLLRAH QAARLQSVST SRLGLNPHVI KSAGRLQLLR GSSFSTATSK WQAGVLDRTR
NIGIIAHIDA GKTTTTERML YYSGFTRRIG DVDEGSTVTD FLPAERARGI TIQSAAITFH
WPPQTAGDGN TTPQEPQTPR SASSHTVNLI DTPGHADFTF EVMRSLRILD GAVCILDGVA
GVEAQTEQVW HQASTYRIPR IVYVNKLDRD GAAFGRTVRE VASRLGGWPA VCQIPWFEGG
NGRFTGIADA INLQGLRWEE GDGKSVKMFN LEQLASEEPQ LAQELKRARV ALVELLSEHD
EAMVEKFFDC EEDHLAVPPN DILESLRRCL LEEQGRKIIP IFAGASFRNI GVQPLLDAVT
NLLPSPPETP EPEVSIGGVK GGLRRLLSGD LLVEQGEKAA SAKGKHKKKS AIQAESRNAI
EKLQGCALAF KVVNDPKRGV LVYVRVYSGS LDRNSILYNT NLNVSERAPR LLKMYANDAV
EVDSIPEGHI GVVAGLKHTR TGDTLVTYSG NKATPPEPLN TLQLRPITVP PPVFFASVEP
HSLSEEKRLQ ESLAMLLRED PSLHVTVDED SGQTLLSGMG ELHLEIARDR LLNDLKAKAS
MGRIEIGYRE CPLGASGPIT KIFDKEIAGR KGKAGCTATV EPFDPEETTT EPDPSTLSIQ
TTDGNQIIIQ APGLEVEVNK KGIEESPLLP PGLDVHALRT ALQNGCLAAL ARGPQFTFPM
HGTRVTLTFN PAEHLFGNES TPSALSAAAR LATSSALRDL PSGAGTSLME PVMNVIISVD
EASLGAVVHD ISSSRGGHII SLDEETPLQT TGITSNPTDD LLPPIDPNKV YAPPDPFQSS
TVGIDLPSSA NRPRTITAKV PLKEMVGYLK HLRSLSAGRG TFVMSVDRFE KMSAPRQKAV
LAELRGDFF
