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Database: UniProt
Entry: B6Q1T9
LinkDB: B6Q1T9
Original site: B6Q1T9 
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   24-JAN-2024, entry version 81.
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}.
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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   VEuPathDB; FungiDB:PMAA_037280; -.
DR   HOGENOM; CLU_002794_4_1_1; -.
DR   OrthoDB; 148165at2759; -.
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; cd01886; EF-G; 1.
DR   CDD; cd16262; EFG_III; 1.
DR   CDD; cd03713; EFG_mtEFG_C; 1.
DR   Gene3D; 3.30.230.10; -; 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; 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; 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
//
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