ID   A0A0G0RKP1_9BACT        Unreviewed;       477 AA.
AC   A0A0G0RKP1;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000256|ARBA:ARBA00020675, ECO:0000256|RuleBase:RU000644};
GN   ORFNames=UT84_C0011G0002 {ECO:0000313|EMBL:KKR50456.1};
OS   Candidatus Curtissbacteria bacterium GW2011_GWA1_40_16.
OC   Bacteria; Candidatus Curtissbacteria.
OX   NCBI_TaxID=1618405 {ECO:0000313|EMBL:KKR50456.1, ECO:0000313|Proteomes:UP000034531};
RN   [1] {ECO:0000313|EMBL:KKR50456.1, ECO:0000313|Proteomes:UP000034531}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
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|RuleBase:RU000644}.
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, ECO:0000256|RuleBase:RU000644}.
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:KKR50456.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LBYI01000011; KKR50456.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0RKP1; -.
DR   PATRIC; fig|1618405.3.peg.517; -.
DR   Proteomes; UP000034531; 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   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   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:SF5; TR-TYPE G DOMAIN-CONTAINING PROTEIN; 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   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Initiation factor {ECO:0000256|ARBA:ARBA00022540,
KW   ECO:0000256|RuleBase:RU000644};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW   ECO:0000256|RuleBase:RU000644}.
FT   DOMAIN          9..177
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   477 AA;  51463 MW;  AF97E117F4E8A2F8 CRC64;
     MTNTKLENSR PPIVTLMGHV DHGKTTLLDA IRKTNVVAGE HGGITQHIGA YQIVFNGNPI
     TFIDTPGHAA FEKMRSRGAE AADIVILVVA ANDGVKPQTT EAIKHIKKAQ TPIIVAITKT
     DLPNINIEKV KKGLQDHDVV IESYGGQVPV VEVAATKGQG INDLLEVIEL LWQISPQPNL
     PNDPIEAVVV ESYMDKNRGA VVSVIPQKGT LKIGNKIQID GEPITIRALI SDTGENIKEA
     PPGKPCEILG FKKAVDVGTI IRDTTVTREI HSQKSASLSE IIAKSQEVKD KFKIIVKADV
     LGSLEAILAN LPQNVLVVSS GVGEVQASDI NFAKLAHAPI LAFNVKTSPS VKQQAEREGV
     MVRPYQIIYE LISDIEDVST GFEAAKQEKK VKSQAQIVAI FNIEGKKVAG SKVTKGKLKI
     NDDVIIRSPG EQPKESKISS IKKYKKDVES VVAGQDCGIC FSNDLDFKEG DIIESLG
//