ID A0A0J8R252_COCIT Unreviewed; 826 AA.
AC A0A0J8R252;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=CISG_07660 {ECO:0000313|EMBL:KMU79229.1};
OS Coccidioides immitis RMSCC 3703.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=454286 {ECO:0000313|EMBL:KMU79229.1, ECO:0000313|Proteomes:UP000054559};
RN [1] {ECO:0000313|Proteomes:UP000054559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RMSCC 3703 {ECO:0000313|Proteomes:UP000054559};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
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}.
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DR EMBL; DS268172; KMU79229.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J8R252; -.
DR STRING; 454286.A0A0J8R252; -.
DR Proteomes; UP000054559; 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:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
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 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; 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; PF14492; EFG_III; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF54980; EF-G C-terminal domain-like; 1.
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 Elongation factor {ECO:0000313|EMBL:KMU79229.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_03059};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128, ECO:0000256|HAMAP-
KW Rule:MF_03059};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03059}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_03059};
KW Reference proteome {ECO:0000313|Proteomes:UP000054559};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 18..329
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 784..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 27..34
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03059"
FT BINDING 113..117
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03059"
FT BINDING 167..170
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03059"
SQ SEQUENCE 826 AA; 89220 MW; 519229872E00145F CRC64;
MVRGYSTSPN PNAIEDLNLT RNIGIIAHID AGKTTTTERM LYYSGFTRRL GDVDDGSTVT
DFLPAERARG ITIQSAAITF HWPPVNQSTA SSEDAKAKGL PRSVLPHTIN LIDTPGHADF
TFEVLRSLRI LDGAVCILDG VAGVEAQTEQ VWHQASTYSI PRIAYVNKLD REGAAFGRTV
KEIGSRLGAW PAVCQIPWFE GGDGKFRGVG DIISLQGLYW EAGGDGKQII ASGLKDLEQQ
DGQFAQEMKN ARIALVELLS EHDDTMVECF LEHDEDHLAV KPIEIWESLR RCLLRDGSRV
IPTFAGASFR NIGVQPLLDA VVNLLPSPTE RPDPEVSIGS VKTGLQNLLA GKVSLESTNN
PTKHKHKKKH ASLHSDTTTA LQKLECCALA FKVVSDARKG VLVYARVYSG TLNRNALLFN
TNLDISERAP RIFKMYANEA VEVQSIPAGH IGVIAGLKFA RTGDTLLSFT GNKQSAPEPL
NTLQLRPIDV PPPVFFTSVE PYSLSEEKNM QDSLALLLRE DPSLHVSVDE DSGQTLLSGM
GELHLEIASD RLVKDFKAKV STGHIEIGYR ECISEASSST TRIFDKEIAG RKGKAGCAAV
VQPLYEGQEN EHTEDPSILF SKEKDGNRIT IKAPGLISTE KTKLPGDLLP HHLSLPVIQS
SIYNGCLAGL TRGPKYSFPV HSVDVTLTFD ITEHLFGSDT TPSALSAAAR LATQSALKEV
STNASLMEPV MNVSISVQES SLGAVVHDIS SSRGGHIVSL DDDTSSSAEA TPDLPQIDVS
KIYAPRDPFG PSSPDAGLSN ATANQSRTIT AKVPLKEMVG VLEASA
//
