ID   IF2_DEIDV               Reviewed;         607 AA.
AC   C1CUQ9;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Deide_10370;
OS   Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=546414;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17065 / CIP 109153 / LMG 22923 / VCD115;
RX   PubMed=19370165; DOI=10.1371/journal.pgen.1000434;
RA   de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B.,
RA   Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M.,
RA   Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.;
RT   "Alliance of proteomics and genomics to unravel the specificities of Sahara
RT   bacterium Deinococcus deserti.";
RL   PLoS Genet. 5:E1000434-E1000434(2009).
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; CP001114; ACO45926.1; -; Genomic_DNA.
DR   RefSeq; WP_012693049.1; NC_012526.1.
DR   AlphaFoldDB; C1CUQ9; -.
DR   SMR; C1CUQ9; -.
DR   STRING; 546414.Deide_10370; -.
DR   PaxDb; C1CUQ9; -.
DR   PRIDE; C1CUQ9; -.
DR   EnsemblBacteria; ACO45926; ACO45926; Deide_10370.
DR   KEGG; ddr:Deide_10370; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_5_2_0; -.
DR   OMA; NRDNRTG; -.
DR   OrthoDB; 347113at2; -.
DR   Proteomes; UP000002208; 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..607
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000202768"
FT   DOMAIN          108..281
FT                   /note="tr-type G"
FT   REGION          54..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          117..124
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          142..146
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          163..166
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          217..220
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          253..255
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         117..124
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         163..167
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         217..220
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   607 AA;  65074 MW;  AC11C3D5AAD844E5 CRC64;
     MSKVRIYTLA KDLGVENARM LEILDGLGVA YKSVSSTIEE ETVDLIKQIL EEESAPQAQD
     STPVAETPAA AQPAAPQAAS SQPAAAQAAQ AVAEPVAAPE PAVNEIPHRA PVVTIMGHVD
     HGKTSLLDYI RKTRVAAKEA GGITQHVGAF EAKTSKGKIV FIDTPGHEAF TTIRARGANV
     ADIAIIVIAA DDSLMPQTRE AIAHAQAAKV PMIVAINKVD LPQADPERVK TDLTQLNLVP
     EEYGGDLIVV PVSAKTGEGV EDLLEYISLT AELEDLRADP KGPFSGVIIE GKVDRQAGVL
     ATVMVQEGTL HVGDFLVVGE NYGKIKAMTD SAGGRIKEAG PSTPVQVLGF SEVPASGEKV
     QSAKNEHAAR DVIAARADVR RDQENARDRR KTQRTLEDIM GPIGEVRTVN LVLRADTQGS
     VEALQGILAR KEGEDVKINV MLAGIGAPTE GDVLLASTAE ATILCFSVTP SGSVTKMAEN
     KGVDIKSYRI IYELIDEVDR LIKGNVEPVF EERYLGRAEV RMVIRHPKSG NIAGSYVTDG
     MFRRNAKAKV TRGKQTVYEG TIVGLKRFKD DVREVQTGYE CGINLDWNDV MEGDIIEASE
     MVEVEQA