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Database: UniProt
Entry: A0A1F7HIK0_9BACT
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ID   A0A1F7HIK0_9BACT        Unreviewed;       482 AA.
AC   A0A1F7HIK0;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000256|ARBA:ARBA00020675, ECO:0000256|RuleBase:RU000644};
GN   ORFNames=A3F29_02345 {ECO:0000313|EMBL:OGK30915.1};
OS   Candidatus Roizmanbacteria bacterium RIFCSPHIGHO2_12_FULL_33_9.
OC   Bacteria; Candidatus Roizmanbacteria.
OX   NCBI_TaxID=1802045 {ECO:0000313|EMBL:OGK30915.1, ECO:0000313|Proteomes:UP000177199};
RN   [1] {ECO:0000313|EMBL:OGK30915.1, ECO:0000313|Proteomes:UP000177199}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OGK30915.1}.
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DR   EMBL; MFZV01000039; OGK30915.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F7HIK0; -.
DR   Proteomes; UP000177199; 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:SF4; EUKARYOTIC TRANSLATION INITIATION FACTOR 5B; 1.
DR   PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF11987; IF-2; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
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:ARBA00023134};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW   ECO:0000256|RuleBase:RU000644}.
FT   DOMAIN          3..177
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   482 AA;  53344 MW;  79AB999B75C819FD CRC64;
     MKNRPPIVAI LGHVDHGKTT LLDFIRKSKL AEKEHGKITQ SIGAYEIKTG IKGYNTDRIT
     FIDTPGHEAF SKLRSRGANV ADFAILLIDA KDSVMPQTEE SISHIKNAGI PFIIVLNKID
     LKDARPEKVK TDLLKYDVMV EDKGGKVPTV NISAKEGKGI SELLEAILLI SSEMNLKYDD
     KTQPIAYIIE TKKDRRGNVV SSIIKQGELK VGDTVYSSGQ KTKIRSLFND MNKSVRSVLP
     SSPFELLGFN ELPQVGSEIR TSDQKLTEKV ADTISQKRTL KIEELLEKNK GKKLNVILKA
     DSKGSLEAIN DALAKKGNIE IVMQGIGTVQ KSDVFLATSS KSIILAFNID IESEAQDVAK
     NEKIIIKNFN IIYELLDELE EVSDLMTQKD MIEKDLKGES VVLASFMIHD KLVYGVKVTK
     GKINLGDNIQ IVRNNNLIAK TKLSSLQIRS KAVKEVKKGQ ESGIMIIPSV DIKVGDVLKY
     SL
//
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