ID   IF2_DEIGD               Reviewed;         601 AA.
AC   Q1IZ02;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Dgeo_1236;
OS   Deinococcus geothermalis (strain DSM 11300 / AG-3a).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=319795;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11300 / AG-3a;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Daly M.J.,
RA   Fredrickson J.K., Makarova K.S., Gaidamakova E.K., Zhai M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Deinococcus geothermalis DSM 11300.";
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
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:0000255|HAMAP-Rule:MF_00100}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00100}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00100}.
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DR   EMBL; CP000359; ABF45532.1; -; Genomic_DNA.
DR   RefSeq; WP_011530369.1; NC_008025.1.
DR   AlphaFoldDB; Q1IZ02; -.
DR   SMR; Q1IZ02; -.
DR   STRING; 319795.Dgeo_1236; -.
DR   EnsemblBacteria; ABF45532; ABF45532; Dgeo_1236.
DR   KEGG; dge:Dgeo_1236; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_5_2_0; -.
DR   OMA; NRDNRTG; -.
DR   OrthoDB; 347113at2; -.
DR   Proteomes; UP000002431; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR   CDD; cd03702; IF2_mtIF2_II; 1.
DR   Gene3D; 3.40.50.10050; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00100_B; IF_2_B; 1.
DR   InterPro; IPR044145; IF2_II.
DR   InterPro; IPR006847; IF2_N.
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   PANTHER; PTHR43381; PTHR43381; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF11987; IF-2; 1.
DR   Pfam; PF04760; IF2_N; 1.
DR   SUPFAM; SSF50447; SSF50447; 2.
DR   SUPFAM; SSF52156; SSF52156; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00487; IF-2; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
DR   PROSITE; PS01176; IF2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..601
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000008236"
FT   DOMAIN          104..273
FT                   /note="tr-type G"
FT   REGION          54..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          113..120
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          138..142
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          159..162
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          213..216
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          249..251
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        62..86
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         113..120
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         159..163
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         213..216
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   601 AA;  64583 MW;  F5925523467F0E26 CRC64;
     MSKVRIYTLA KDLGVDNAKM LEILDGLGVA YKSVSSTIEE DTVELIKQIL EEEGHTASAE
     PAPAQASGSP ASPAQTEAQE APQPTATATA EREPAAPPAR ELPHRAPVVT IMGHVDHGKT
     SLLDYIRKTK VAAKEAGGIT QHVGAFEAKT SKGKIVFIDT PGHEAFTTIR ARGANVADIA
     VIVIAADDSL MPQTREAIAH AQAAKVPMIV AINKVDLPQA DPEKVKTDLT QLNLVPEEYG
     GDLIVVPVSA KTGEGVEDLL EYISLTAELE DLRADPQGEF SGVIIESRVD RQAGVLATVM
     VQEGTLHVGD FLVVGENYGK VKAMTDSNGG RIKEAGPSTP VQVLGFSEAP SSGEKVVSVK
     NEHAARELVA QRVETRREAE NARVQRKKTL EEMMGPLGET RTVNLILRAD TQGSLEAIQG
     ILARKETEDV KLNVMLAGIG SPTEGDVLLA STADATILCF NVTASGSVKK AAEQRDIELK
     SFRIIYELID EVDRLIKGNV EPVFEERPLG RAEVRMVIRH PKSGNIAGSY VTDGLLRRNA
     KARVLRGKQV VYEGTIVGLK RFKDDVREVQ AGYECGVNLD WNDVQEGDII EASELVEVAQ
     A