ID   A0A0E0QTU2_ORYRU        Unreviewed;       732 AA.
AC   A0A0E0QTU2;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Translation initiation factor IF-2, mitochondrial {ECO:0000256|ARBA:ARBA00044200};
OS   Oryza rufipogon (Brownbeard rice) (Asian wild rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4529 {ECO:0000313|EnsemblPlants:ORUFI09G17680.4, ECO:0000313|Proteomes:UP000008022};
RN   [1] {ECO:0000313|Proteomes:UP000008022}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. W1943 {ECO:0000313|Proteomes:UP000008022};
RA   Zhao Q.;
RL   Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:ORUFI09G17680.4}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- FUNCTION: One of the essential components for the initiation of protein
CC       synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis
CC       and promotes its binding to the 30S ribosomal subunits. Also involved
CC       in the hydrolysis of GTP during the formation of the 70S ribosomal
CC       complex. {ECO:0000256|ARBA:ARBA00025162}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC       {ECO:0000256|ARBA:ARBA00007733}.
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DR   AlphaFoldDB; A0A0E0QTU2; -.
DR   EnsemblPlants; ORUFI09G17680.4; ORUFI09G17680.4; ORUFI09G17680.
DR   Gramene; ORUFI09G17680.4; ORUFI09G17680.4; ORUFI09G17680.
DR   HOGENOM; CLU_006301_5_2_1; -.
DR   Proteomes; UP000008022; Unassembled WGS sequence.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   CDD; cd01887; IF2_eIF5B; 1.
DR   CDD; cd03702; IF2_mtIF2_II; 1.
DR   CDD; cd03692; mtIF2_IVc; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
DR   Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 1.
DR   HAMAP; MF_00100_B; IF_2_B; 1.
DR   InterPro; IPR044145; IF2_II.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR000178; TF_IF2_bacterial-like.
DR   InterPro; IPR015760; TIF_IF2.
DR   InterPro; IPR023115; TIF_IF2_dom3.
DR   InterPro; IPR036925; TIF_IF2_dom3_sf.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   NCBIfam; TIGR00487; IF-2; 1.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR43381:SF20; TRANSLATION INITIATION FACTOR IF-2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF11987; IF-2; 1.
DR   SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50447; Translation proteins; 2.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Initiation factor {ECO:0000256|ARBA:ARBA00022540};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008022}.
FT   DOMAIN          195..365
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   732 AA;  78984 MW;  80D5849D710306B9 CRC64;
     MAWRMLRRKD FHTGLVNLAS RVDHGGAKNF SSGTFGKLAD FVLSDTHTPI VKGAANCTAY
     KHCTIRNFHA GVYMLAWSRK REEVAGLKAP KKEKRVKRET RTQPPVEAPY VAPKQKIAIK
     SSPDKTVDIF DGMTLLDLSK RTGASIGALQ DILTDLGEKV ESEFDAISID LAELVAMELG
     VNIRRMHTGE GTLEPRPAVV TIMGHVDHGK TSLLDSLRQT SVAAKEAGGI TQHIGAFVVE
     MPSGASITFL DTPGHAAFSA MRARGAAVTD IVVLVVAADD GVMPQTLEAM SHAKAANVPI
     VVAVNKCDKS GADPERVRIQ LGSEGLLLED MGGDVQVVEI SAVTKLGLDK LEEALLLQAE
     IMDLKARIDG PAQAFVVEAR VDRGRGPLAT AIVKAGTLVS GQHIVVGAEW GRIRSLRDTA
     GKITESAKPA MPVEIEGLRG LPMAGDDVVV VDSEERARML SQGRKKKQEK DRLRKIDEDM
     TEEAEIGEET PERVEMPIIV KADVQGSVQA VTDALRSLNS PQVFVNIVHV GVGPISQHDI
     DLAQACRAYI VGFNIRTPPS AITLAATQAN IKILLHKVIY HLLEEMGREI VEKAPGTPET
     QVSGEAEVLN IFELKGRSKS KGPDIKIAGC RITDGHLSKT GTMRLLRSGD VVFEGPCASL
     KREKQDAETV DKGNDCGLVI QDCNDFQVGD IVQCLEQVIR KPKFISTQSG AICDSFLLID
     LVLIVKRPGS KN
//