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Database: UniProt
Entry: A0A139IE04_9PEZI
LinkDB: A0A139IE04_9PEZI
Original site: A0A139IE04_9PEZI 
ID   A0A139IE04_9PEZI        Unreviewed;       857 AA.
AC   A0A139IE04;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
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=AC579_7607 {ECO:0000313|EMBL:KXT12846.1};
OS   Pseudocercospora musae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=113226 {ECO:0000313|EMBL:KXT12846.1, ECO:0000313|Proteomes:UP000073492};
RN   [1] {ECO:0000313|EMBL:KXT12846.1, ECO:0000313|Proteomes:UP000073492}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 116634 {ECO:0000313|EMBL:KXT12846.1,
RC   ECO:0000313|Proteomes:UP000073492};
RA   Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT   "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT   link between parallel evolutionary changes in Pseudocercospora fijiensis
RT   and Pseudocercospora eumusae and increased virulence on the banana host.";
RL   Submitted (JUL-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXT12846.1}.
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DR   EMBL; LFZO01000138; KXT12846.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139IE04; -.
DR   STRING; 113226.A0A139IE04; -.
DR   Proteomes; UP000073492; 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 {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_03059}; Mitochondrion {ECO:0000256|HAMAP-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:UP000073492}.
FT   DOMAIN          24..331
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          89..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         33..40
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03059"
FT   BINDING         116..120
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03059"
FT   BINDING         170..173
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03059"
SQ   SEQUENCE   857 AA;  92538 MW;  3AF9E53C3A06F90A CRC64;
     MQTGAFIRHA TRTFASSTRK PAFARTRNIG IIAHIDAGKT TTTERMLYYT GFTRRLGDVD
     EGSTVTDFLP AERARGITIQ SAAISFSWPP SAGDKDHPST PGTPTSSIPH NINLIDTPGH
     ADFTFEVLRS LRVLDGAVCI LDGVAGVEAQ TEKVWAQAGA YAIPKILLVN KLDRDGAAFA
     RTVKEVGARL GAWPAVCGIP WWNSEGRLQG VGDVVGLRGL KYPEGGDGKD IKTFDMQQLE
     AQDPALAAEL KKARIALIER LSEHDDEMVE KYLEADEDHL EITPNDTIDS LRRCVLQHPQ
     QVAPLYAGAS FRNIGVQPLL DAIVDLLPSP EERPDPEVSL GSDSTTKGAL SAFLSGKLVA
     KAAPAELKRG KAKPSMALQS LETCALAFKV VADAKRGVLV YVRVYSGSLN RNTSLWNTNL
     QITERAQRLL KMYANDAVEI DSISAGQIGV IPGLKFARTG DTLISYRGAN PKTGPPSPVN
     TLQLRPIEVP PPVFFVSVEP NSLAEERHIK ESLELLLRED PSLHVSVDEE SGQTHLSGMG
     ELHLEIARDR LVQDLKAKAR IGNIEIGYRE AVTGASTNVT EVFDRDIGGK SAKAACMANV
     ESLDDYAEPR DKHTHLFCLH DNNRLIVTTP TLRKDGSSVD EEKPSLPDSI PMQTLLQSLQ
     TGVSAAMARG PMHGYPLHST EINITFDPSQ HLFSNTTPAA LSSAARLAVQ LALKQSAESS
     PTVMMEPVML VTISVNEDSL GSVVHDISSA RGGSVVSLGA EDDSDSSQQD IDVKKIYTPP
     DPFAGSSSGF ADASLSGGSG IRQIVARVPL KEMVGYLKHL RSLTAGRGTF TMVVDNFERL
     SAPRQRAVLN EMRGEYA
//
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