RRF2M_TALSN
ID RRF2M_TALSN Reviewed; 931 AA.
AC B8MR69;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 2.
DT 03-AUG-2022, entry version 71.
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};
GN Name=mef2; ORFNames=TSTA_054740;
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006;
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(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 -!- MISCELLANEOUS: This protein may be expected to contain an N-terminal
CC transit peptide but none has been predicted. {ECO:0000255|HAMAP-
CC 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 -!- SEQUENCE CAUTION:
CC Sequence=EED12964.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; EQ962659; EED12964.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_002487075.1; XM_002487030.1.
DR AlphaFoldDB; B8MR69; -.
DR SMR; B8MR69; -.
DR STRING; 441959.B8MR69; -.
DR PRIDE; B8MR69; -.
DR EnsemblFungi; EED12964; EED12964; TSTA_054740.
DR GeneID; 8100481; -.
DR eggNOG; KOG0465; Eukaryota.
DR HOGENOM; CLU_002794_4_1_1; -.
DR InParanoid; B8MR69; -.
DR OrthoDB; 637899at2759; -.
DR Proteomes; UP000001745; 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; 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 Reference proteome.
FT CHAIN 1..931
FT /note="Ribosome-releasing factor 2, mitochondrial"
FT /id="PRO_0000385621"
FT DOMAIN 63..379
FT /note="tr-type G"
FT BINDING 72..79
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT BINDING 162..166
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT BINDING 216..219
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
SQ SEQUENCE 931 AA; 100817 MW; 120A682F290E28F7 CRC64;
MVSAPLLGWA AIRPIPVSRL KTCKYASNSL QSYNGIVASY LRLHYYRSLS SSAVLAEAIV
HLEKTRNIGI IAHIDAGKTT TTERMLYYSG FTRRIGDVDD GSTVTDFLPA ERARGITIQS
AAITFHWPPL TGDGTSSSPS LEDLEAQNLP RSRASHTVNL IDTPGHADFT FEVLRSLRIL
DGAVCILDGV AGVEAQTEKV WHQASVYQIP RIVYVNKLDR DGAAFGRTVR EVGSRLQGWP
AVCQIPWFEG SNGRFTGIAD VVSLQGLLWK EGGDGKSVKV FDLNGLENED KSLAEELKRA
RVALVELLSE HDEDMVESFF EHEEDHLTVP SITILKSLRK CLLGPETQKI IPVFAGSSFR
NMGVQPLLDA VNNLLPGPSE SHDPEISLGS DKTSLGNLLS GELALQQDPK TASIEKSKQK
KKAVVTRTSV DIKSLTANLE SCALAFKVVS DAKRGVLVYV RVYSGSLNRN CHLYNTNLHV
TERAPRLFKM YANDAVEVDS IPAGHIGVVV GLKYARTGDT LISCTGSKSV PPEPLNTLQL
RPIDVPPPVF FASIEPHSLS EEKNMQEALA LLLREDPSLH VTIDEDSGQT LLSGMGELHL
EIARDRLVND FKAKASMGRI EIGYRECVLD QSNPVTKIFD REVAGRKGKA GCTAVVEPYG
QELESDGNDT SGSDDIIFTE TVDGNKIIIS APGVNITTDK KGKEESTSLP PQLDLNSFRT
SLYNGALSAL ARGPQFAFPM HNTKVTLTCN AAEHLFGSES SASALSAAAR LATQGALRNL
TTTAASTGTG MMEPVMNVII SVDEASLGAV VHDISSARGG HIVSLDEEMP ISTSLSQSPE
SQDQPVAVDI NKIYAPPDPF ETPSVAGGLP IQAPANQPRT ITAKVPLKEM VGYLKHLRSL
SAGRGTFVMH VDRFERMSAQ RQKAVLAELN R
