RRF2M_TALMQ
ID RRF2M_TALMQ Reviewed; 927 AA.
AC B6Q1T9;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=PMAA_037280;
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333;
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 -!- 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; DS995899; EEA28942.1; -; Genomic_DNA.
DR RefSeq; XP_002145457.1; XM_002145421.1.
DR AlphaFoldDB; B6Q1T9; -.
DR SMR; B6Q1T9; -.
DR STRING; 441960.B6Q1T9; -.
DR PRIDE; B6Q1T9; -.
DR EnsemblFungi; EEA28942; EEA28942; PMAA_037280.
DR GeneID; 7023174; -.
DR KEGG; tmf:PMAA_037280; -.
DR VEuPathDB; FungiDB:PMAA_037280; -.
DR HOGENOM; CLU_002794_4_1_1; -.
DR OrthoDB; 637899at2759; -.
DR PhylomeDB; B6Q1T9; -.
DR Proteomes; UP000001294; 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; Transit peptide.
FT TRANSIT 1..57
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT CHAIN 58..927
FT /note="Ribosome-releasing factor 2, mitochondrial"
FT /id="PRO_0000385618"
FT DOMAIN 64..379
FT /note="tr-type G"
FT BINDING 73..80
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT BINDING 163..167
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT BINDING 217..220
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
SQ SEQUENCE 927 AA; 100113 MW; 8D54503B2D72A592 CRC64;
MVTAPLLGWV AVRPIPRLSK LNTCKYVSSS LQSYKRSVGS CLGKQQSRDF SYSATLTDAG
INLEKTRNIG IIAHIDAGKT TTTERMLYYS GFTRRIGDVD DGSTVTDFLP AERARGITIQ
SAAITFHWPP LAADGTSSGP SLEELESQNL PRSRASHTVN LIDTPGHADF TFEVLRSLRI
LDGAVCILDG VAGVEAQTEK VWHQASVYQI PRVVYVNKLD RDGAAFGRTV REVGSRLQGW
PAVCQIPWFE GGNGRFTGIA DVISLQGLLW KEGGDGKSVK VFDLAGLENE DKRLAEELKH
ARVALVELLS EHDEDMVESF FEHEDHLKVP PMTILKSLRK CLLGPEAQKI IPVFAGSSFR
NMGVQPLLDA VNNLLPGPSE SVDPEISLGN SKGSLGNLLS GELTLQQEPK TANIAKPKQK
KKTAVAPTSV DTKHLAANLE SCALAFKVVS DAKRGVLVYV RVYSGTLNKG CQLYNTNLHV
TERAPRLFKM YANDAVEVDS IPAGHIGVVS GLKYARTGDT LISCTGSKMT PPEPLNTLQL
RPIDVPPPVF FASIEPHSLS EEKNMQEALA LLLREDPSLH VTVDEDSGQT LLSGMGELHL
EIARDRLVND FKAKATMGRI EIGYRECVLG QSNPVTKIFD REVAGRKGKA GCTAVVEPYD
PESGEPSSGG EDIIFAEIVE GNRIIISAPG INISTDKRGK EESSSLPSQF DVNSFRTSLY
NGALSALARG PQFAFPMHNT KVTLTCNVVE HLFGSDSSAS ALSAAARLAT QGALRDLATG
QNSGTGIMEP VMNVIISIDE ASLGAVVHDI SSARGGHIIS LDEEMPISTS IGGNDSPESE
QVVIDVNKIY APPDPFETPS VAGGLPIQAS ANQTRTITAK VPLKEMVGYL KHLRSLSAGR
GTFVMHVDRF ERMSAQRQKA VLAELHR
