ID A0A1G1VTX0_9BACT Unreviewed; 478 AA.
AC A0A1G1VTX0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000256|ARBA:ARBA00020675, ECO:0000256|RuleBase:RU000644};
GN ORFNames=A2786_05285 {ECO:0000313|EMBL:OGY18873.1};
OS Candidatus Chisholmbacteria bacterium RIFCSPHIGHO2_01_FULL_52_32.
OC Bacteria; Candidatus Chisholmbacteria.
OX NCBI_TaxID=1797591 {ECO:0000313|EMBL:OGY18873.1, ECO:0000313|Proteomes:UP000179233};
RN [1] {ECO:0000313|EMBL:OGY18873.1, ECO:0000313|Proteomes:UP000179233}
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:OGY18873.1}.
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DR EMBL; MHCJ01000003; OGY18873.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1VTX0; -.
DR Proteomes; UP000179233; 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 1..162
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 256..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 478 AA; 52111 MW; A8D4B5818551D04A CRC64;
MGHVDHGKTT LLDAIRKTNV VASEHGGITQ SIGAYQIQYK GRRITFIDTP GHAAFSKMRA
HGAQVTDIVV LVIAANDGVK PQTREALQHI RAAKVPFLVA VSKIDLPEAN VERVKGQLAE
EDVVVESYGG KIPLVEVSAK TGERIGDLLE MILLVSDLED LRADPQGELD VVVIETRQDR
RKGPLATLLV KNGTLKVGSK MTLGDQTITI KALTDADGKP VETAGPATPV EVLGWKKLPG
VGQTIRGEEK KLEIVKTEKE QPKQALTNKE AKEDETAEGE EQKEKQTVNV ILKTDIAGTL
EAITTNLSEE VEIVGSGIGE VNESDVLLAS ATEAKIYAFN TEVTPSAKKL AEAEKVTIKT
FNIIYKLFED LEKQVLKMLE PTIDEEIVGE AVIIAQFEIH GEHIAGCKVK TGEIKKISPI
HLKRGEERVS DAKIKSLHRG KEEIESAKQG TECGIILKPQ VDFKLGDVII SYRKIEET
//
